BMI1

Summary

BMI1 (BMI1 proto-oncogene, polycomb ring finger, HGNC:1066) is a protein-coding gene on chromosome 10p12.2, encoding Polycomb complex protein BMI-1 (P35226). Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development.

This gene encodes a ring finger protein that is major component of the polycomb group complex 1 (PRC1). This complex functions through chromatin remodeling as an essential epigenetic repressor of multiple regulatory genes involved in embryonic development and self-renewal in somatic stem cells. This protein also plays a central role in DNA damage repair. This gene is an oncogene and aberrant expression is associated with numerous cancers and is associated with resistance to certain chemotherapies. A pseudogene of this gene is found on chromosome X. Read-through transcription also exists between this gene and the upstream COMM domain containing 3 (COMMD3) gene.

Source: NCBI Gene 648 — RefSeq curated summary.

At a glance

• GWAS associations: 1
• Clinical variants (ClinVar): 9 total
• Druggable target: yes
• MANE Select transcript: NM_005180

Identifiers

Gene identifiers

Field	Value
HGNC ID	HGNC:1066
Approved symbol	BMI1
Name	BMI1 proto-oncogene, polycomb ring finger
Location	10p12.2
Locus type	gene with protein product
Status	Approved
Aliases	RNF51
Ensembl gene	ENSG00000168283
Ensembl biotype	protein_coding
OMIM	164831
Entrez	648

Gene structure

Transcript identifiers

Ensembl transcripts: 22 — 16 protein_coding, 6 retained_intron

ENST00000376663, ENST00000416820, ENST00000442508, ENST00000443519, ENST00000456675, ENST00000490311, ENST00000496174, ENST00000602358, ENST00000602523, ENST00000602524, ENST00000895844, ENST00000895845, ENST00000895846, ENST00000895847, ENST00000895848, ENST00000895849, ENST00000922171, ENST00000922172, ENST00000922173, ENST00000963380, ENST00000963381, ENST00000963382

RefSeq mRNA: 5 — MANE Select: NM_005180 NM_001428309, NM_001428310, NM_001428311, NM_001428312, NM_005180

CCDS: CCDS7138

Canonical transcript exons

ENST00000376663 — 10 exons

Exon	Start	End
ENSE00001251863	22321099	22321696
ENSE00001916123	22329213	22331484
ENSE00003459313	22326431	22326561
ENSE00003504644	22328600	22328698
ENSE00003515184	22326890	22326986
ENSE00003518293	22327595	22327650
ENSE00003554393	22328134	22328179
ENSE00003596686	22329048	22329128
ENSE00003644277	22327742	22327792
ENSE00003686223	22327950	22328058

Expression profiles

Bgee: expression breadth ubiquitous, 293 present calls, max score 98.62.

FANTOM5 (CAGE): breadth ubiquitous, TPM avg 19.9562 / max 390.4914, expressed in 1791 samples.

FANTOM5 promoters (13 alternative TSS)

Promoter ID	TPM avg	Samples expressed
104237	7.5790	1680
104239	3.6909	1238
104248	3.2667	1343
104246	1.2263	737
104241	1.0123	679
104244	0.8798	426
104240	0.8788	481
104242	0.4307	197
104243	0.2997	125
104249	0.2417	84

Top tissues by expression

295 total, by Bgee expression score (0-100, higher = more expressed):

Tissue	Anatomy ID	Expression score	Quality
germinal epithelium of ovary	UBERON:0001304	98.62	gold quality
choroid plexus epithelium	UBERON:0003911	98.32	gold quality
endothelial cell	CL:0000115	97.95	gold quality
cranial nerve II	UBERON:0000941	97.29	gold quality
Brodmann (1909) area 23	UBERON:0013554	97.26	gold quality
visceral pleura	UBERON:0002401	97.25	gold quality
corpus callosum	UBERON:0002336	97.08	gold quality
pigmented layer of retina	UBERON:0001782	96.93	gold quality
tibia	UBERON:0000979	96.80	gold quality
parietal pleura	UBERON:0002400	96.79	gold quality
superficial temporal artery	UBERON:0001614	96.66	gold quality
pleura	UBERON:0000977	96.51	gold quality
epithelium of nasopharynx	UBERON:0001951	96.47	gold quality
corpus epididymis	UBERON:0004359	96.42	gold quality
cauda epididymis	UBERON:0004360	96.40	gold quality
biceps brachii	UBERON:0001507	96.38	gold quality
cortical plate	UBERON:0005343	96.32	gold quality
calcaneal tendon	UBERON:0003701	96.29	gold quality
caput epididymis	UBERON:0004358	96.20	gold quality
islet of Langerhans	UBERON:0000006	96.18	gold quality
primordial germ cell in gonad	CL:0000670 ∩ UBERON:0000991	96.10	gold quality
skeletal muscle tissue of biceps brachii	UBERON:0004502	96.07	gold quality
mucosa of paranasal sinus	UBERON:0005030	95.97	gold quality
blood vessel layer	UBERON:0004797	95.95	gold quality
skeletal muscle tissue of rectus abdominis	UBERON:0004511	95.85	gold quality
bronchial epithelial cell	CL:0002328	95.76	gold quality
endometrium	UBERON:0001295	95.70	gold quality
palpebral conjunctiva	UBERON:0001812	95.70	gold quality
endometrium epithelium	UBERON:0004811	95.69	gold quality
ganglionic eminence	UBERON:0004023	95.56	gold quality

Single-cell (SCXA)

Detected in 2 experiment(s), a significant marker in 1.

Experiment	Marker?	Max mean expression
E-ANND-3	yes	6.98
E-MTAB-7303	no	285.37

Regulation

Is transcription factor: yes

Downstream targets (CollecTRI)

4 targets.

Target	Regulation
BMI1	Activation
CDKN2A	Unknown
PTEN	Repression
TERT	Repression

Upstream regulators (CollecTRI, top): BCL6, BCOR, BMI1, CEBPA, E2F1, EGR1, ESR1, EZH2, FOXC1, FOXM1, GLI1, ID1, KDM5B, KMT2A, MBD2, MYC, MYCN, NANOG, SALL4, SOX9, SP1, SUZ12, TWIST1, YBX1, ZEB1, ZNF277

miRNA regulators (miRDB)

129 targeting BMI1, top 30 by miRDB confidence (max_score; target_count = how many genes the miRNA targets in total — lower means more specific):

miRNA	Max score	Avg score	miRNA target_count
HSA-MIR-3646	100.00	73.56	5283
HSA-MIR-340-5P	100.00	72.50	4437
HSA-MIR-548C-3P	99.99	74.01	7587
HSA-MIR-4282	99.99	75.36	6408
HSA-MIR-196A-1-3P	99.99	72.15	2772
HSA-MIR-548N	99.98	71.94	4170
HSA-MIR-27A-3P	99.98	72.13	2955
HSA-MIR-27B-3P	99.98	72.13	2955
HSA-MIR-9985	99.98	72.11	2939
HSA-MIR-5688	99.96	73.23	4504
HSA-MIR-551B-5P	99.96	71.28	3493
HSA-MIR-495-3P	99.96	72.81	4197
HSA-MIR-559	99.95	72.28	3609
HSA-LET-7C-3P	99.95	73.42	2862
HSA-MIR-548AB	99.95	71.31	3488
HSA-MIR-128-3P	99.95	71.17	2484
HSA-MIR-216A-3P	99.95	71.19	2505
HSA-MIR-3910	99.95	71.13	2227
HSA-MIR-548A-5P	99.94	71.27	3482
HSA-MIR-548AD-5P	99.94	71.23	3502
HSA-MIR-548AE-5P	99.94	71.23	3502
HSA-MIR-548AK	99.94	71.24	3488
HSA-MIR-548AM-5P	99.94	71.24	3488
HSA-MIR-548AP-5P	99.94	71.14	3489
HSA-MIR-548AQ-5P	99.94	71.34	3426
HSA-MIR-548AR-5P	99.94	71.28	3515
HSA-MIR-548AS-5P	99.94	71.22	3482
HSA-MIR-548AU-5P	99.94	71.24	3488
HSA-MIR-548AY-5P	99.94	71.23	3502
HSA-MIR-548B-5P	99.94	71.23	3502

Literature-anchored findings (GeneRIF, showing 40)

• The Bmi-1 oncogene induces telomerase activity and immortalizes human mammary epithelial cells. (PMID:12183433)
• Bmi-1 extends the replicative life span of human fibroblasts by suppressing the p16-dependent senescence pathway (PMID:12482990)
• BMI-1 binds the MLL repression domain. Recruitment of BMI-1 to the MLL protein may be able to modulate its function. (PMID:12829790)
• E2a-Pbx1 and Bmi-1 are likely to play a role in the pathogenesis of human lymphoid leukemias through downregulation of the INK4A-ARF gene (PMID:14536079)
• modulation of Bmi-1 protein might be involved in human colorectal carcinogenesis by repressing the INK4a/ARF proteins (PMID:14732230)
• BMI-1 is transiently localized with the centromeric region in interphase. (PMID:15009096)
• BMI1 overexpression is an alternative or additive mechanism in the pathogenesis of medulloblastomas (PMID:15029199)
• Activation or overexpression of MAPKAP kinase 3pK resulted in phosphorylation of Bmi1 and other PcG members and their dissociation from chromatin (PMID:15563468)
• Altered expression is associated with therapy failure and death in patients with multiple types of cancer. (PMID:15931389)
• a subgroup of M0 patients has a high expression level of polycomb group gene BMI-1, which may contribute to leukemogenesis (PMID:16105758)
• CALM-AF10+ T-ALL associatd with elevated expression of subset of HOXA genes and some of there transcriptional and functional regulators, as well as specific overexpression of oncogene BMI1 (PMID:16107895)
• EZH2 is essential for BMI1 recruitment to the polycomb bodies. (PMID:16314526)
• Critical for the short-term survival of cancer cells, and inhibition has minimal effect on the survival of normal cells. (PMID:16501599)
• p16(INK4a) expression was regulated by the Polycomb group repressor Bmi-1, which is shown as a direct transcriptional target of c-Myc. (PMID:16537449)
• Bmi-1-Ring1B complex stabilizes the interaction of the ubiquitin ligase complex. (PMID:16714294)
• Bmi1 is required for H2A ubiquitylation; H2A ubiquitylation regulates Bmi1-mediated gene expression (PMID:16751658)
• BMI-1 is expressed in gastrointestinal stem cells and may have a role protein in cellular differentiation and stem cell maintenance (PMID:16874656)
• bmi1 expression caused by oxidative stress may be involved in the pathogenesis of cellular senescence of biliary epithelial cells in primary biliary cirrhosis. (PMID:16936260)
• Advanced cell- & animal imaging, expression profiling, stable siRNA-gene targeting, and TMAs of experimental and clinical samples indicate that activation of the BMI1 oncogene-associated PcG pathway plays an essential role in metastatic prostate cancer. (PMID:16963837)
• Bmi-1 regulates the differentiation and clonogenic self-renewal of I-type neuroblastoma cells (PMID:16982619)
• PcG protein BMI1 is associated with adverse pathological features and clinical PSA recurrence of prostate cancer. (PMID:17134822)
• The oncogenic role of Bmi-1 in human primary breast carcinomas is not determined by its capacity to inhibit INK4a/ARF proteins(p16INK4a, p14ARF, or h-TERT) or to induce telomerase activity. (PMID:17145810)
• Bmi1 overexpression was correlated with the malignant grades of human digestive precancerous tissues, which suggests that advanced Bmi1 dysregulation might predict malignant progression. (PMID:17145814)
• ERK5 probably mediates HOXB9 expression by repressing BMI1 in Hodgkin lymphoma cell lines (PMID:17148583)
• Bmi-1 and LMP1 down-regulate the ataxia telangiectasia-mutated (ATM) tumor suppressor and conclude that Bmi-1 contributes to LMP1-induced oncogenesis in Hodgkin lymphoma (PMID:17148591)
• Our data suggest that Mel-18 regulates Bmi-1 expression during senescence via down-regulation of c-Myc. (PMID:17151361)
• Our results provide new information on the roles of Bmi-1 and HPV-16 E6 in the multi-step process of oral epithelial carcinogenesis. (PMID:17161394)
• The Bmi-1 may act through p16(INK4A)-independent pathways to regulate cellular proliferation during oral cancer progression. (PMID:17179983)
• many human cell types undergo senescence by activation of the p16(INK4a)/Rb pathway, and that introduction of Bmi-1 can inhibit p16(INK4a) expression and extend the life span of human epithelial cells (PMID:17233832)
• The intensive expression of Bmi-1 in breast cancer is related to tumor progression. (PMID:17298744)
• Study shows that the ability of the oncogene BMI1 to repress the INK4A-ARF locus requires its direct association and is dependent on the continued presence of the EZH2-containing Polycomb-Repressive Complex 2 complex. (PMID:17344414)
• In a cohort of 64 CML patients, the level of BMI1 at diagnosis correlated with time to transformation to blast crisis, and the combination of low BMI1 and high proteinase-3 expression was associated with an improved overall survival (PMID:17360938)
• These results suggest that Bmi-1 and Mel-18 may have overlapping functions in cancer cell growth. (PMID:17452456)
• Bmi-1 seems to play a secondary role in chronic myeloid leukemia transformation (PMID:17454639)
• Mel-18 and Bmi-1 may regulate the Akt pathway in breast cancer cells, and that Mel-18 functions as a tumor suppressor by repressing the expression of Bmi-1 and consequently down-regulating Akt activity. (PMID:17545584)
• BMI1 is a target gene for SALL4 in leukemic cells. (PMID:17557835)
• BMI-1 mediated repression of p16(ink4a) may contribute to an increased aggressive behavior of stem cell-like melanoma cells. (PMID:17597110)
• Bmi-1 may promote maintenance of suprabasal keratinocyte survival to prevent premature death during differentiation. (PMID:17625597)
• Bmi-1 mRNA expression is correlated to differentiation and metastasis of gastric carcinoma and may facilitate its prognostic evaluation. (PMID:17666329)
• Elevated Bmi-1 is associated with breast cancer (PMID:17711569)

Cross-species orthologs

6 orthologs

Organism	Symbol	Gene ID
danio_rerio	bmi1a	ENSDARG00000006010
danio_rerio	bmi1b	ENSDARG00000013076
mus_musculus	Bmi1	ENSMUSG00000026739
rattus_norvegicus	Bmi1	ENSRNOG00000016585
drosophila_melanogaster	Psc	FBGN0005624
drosophila_melanogaster	Su(z)2	FBGN0265623

Paralogs (7): PCGF1 (ENSG00000115289), RNF2 (ENSG00000121481), PCGF6 (ENSG00000156374), PCGF5 (ENSG00000180628), PCGF3 (ENSG00000185619), RING1 (ENSG00000204227), PCGF2 (ENSG00000277258)

Protein

Protein identifiers

Polycomb complex protein BMI-1 — P35226 (reviewed: P35226)

Alternative names: Polycomb group RING finger protein 4, RING finger protein 51

All UniProt accessions (4): P35226, Q5T8Z2, Q5T8Z4, Q5T8Z6

UniProt curated annotations — full annotation on UniProt →

Function. Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A ‘Lys-119’, rendering chromatin heritably changed in its expressibility. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. In the PRC1-like complex, regulates the E3 ubiquitin-protein ligase activity of RNF2/RING2.

Subunit / interactions. Component of a PRC1-like complex. Identified in a PRC1-like HPRC-H complex with CBX2, CBX4, CBX8, PHC1, PHC2, PHC3 RING1 and RNF2. Interacts with RNF2/RING2. Interacts with RING1. Part of a complex that contains RNF2, UB2D3 and BMI1, where RNF2 and BMI1 form a tight heterodimer, and UB2D3 interacts only with RNF2. The complex composed of RNF2, UB2D3 and BMI1 binds nucleosomes, and has activity only with nucleosomal histone H2A. Interacts with CBX7 and CBX8. Interacts with SPOP. Part of a complex consisting of BMI1, CUL3 and SPOP. Interacts with E4F1. Interacts with PHC2. Interacts with zinc finger protein ZNF277. May be part of a complex including at least ZNF277, BMI1 and RNF2/RING2.

Subcellular location. Nucleus. Cytoplasm.

Post-translational modifications. Monoubiquitinated. May be polyubiquitinated; which does not lead to proteasomal degradation.

Induction. Down-regulated by oxidative stress.

Miscellaneous. The hPRC-H complex purification reported by PubMed:12167701 probably presents a mixture of different PRC1-like complexes.

RefSeq proteins (5): NP_001415238, NP_001415239, NP_001415240, NP_001415241, NP_005171* (*=MANE)

Domains & families (InterPro)

ID	Name	Type
IPR001841	Znf_RING	Domain
IPR013083	Znf_RING/FYVE/PHD	Homologous_superfamily
IPR017907	Znf_RING_CS	Conserved_site
IPR032443	RAWUL	Domain

Pfam: PF13923, PF16207

UniProt features (43 total): strand 10, helix 10, mutagenesis site 7, turn 4, region of interest 3, compositionally biased region 3, sequence conflict 2, chain 1, zinc finger region 1, short sequence motif 1, sequence variant 1

Structure

Experimental structures (PDB)

13 structures.

PDB	Method	Resolution (Å)
6WI7	X-RAY DIFFRACTION	1.7
2H0D	X-RAY DIFFRACTION	2.5
5FR6	X-RAY DIFFRACTION	2.51
3RPG	X-RAY DIFFRACTION	2.65
9DBY	ELECTRON MICROSCOPY	2.8
8PP7	ELECTRON MICROSCOPY	2.91
9DGG	ELECTRON MICROSCOPY	2.98
8GRM	ELECTRON MICROSCOPY	3.05
6WI8	X-RAY DIFFRACTION	3.09
9DDE	ELECTRON MICROSCOPY	3.2
4R8P	X-RAY DIFFRACTION	3.28
2NA1	SOLUTION NMR
7ND1	SOLUTION NMR

Predicted structure (AlphaFold)

Model	pLDDT	Fraction very-high
AF-P35226-F1	78.09	0.55

Functional residue map

Curated UniProt residues grouped by drug-discovery relevance — catalytic, ligand-binding, modification, and mutation-validated positions. Source: UniProtKB sequence features.

Mutagenesis-validated functional residues (7):

Position	Phenotype
62	strongly decreases histone h2a ubiquitination; when associated with a-64.
64	mildly decreases histone h2a ubiquitination. strongly decreases histone h2a ubiquitination; when associated with a-62.
73	increases stimulation of rnf2 ubiquitin ligase activity; when associated with e-77.
77	increases stimulation of rnf2 ubiquitin ligase activity; when associated with n-73.
165	decreases affinity for phc2. abolishes interaction with phc2; when associated with e-174.
170	strongly decreases affinity for phc2.
174	strongly decreases affinity for phc2. abolishes interaction with phc2; when associated with e-165.

Function

Pathways and Gene Ontology

Reactome pathways

25 pathways

ID	Pathway
R-HSA-2559580	Oxidative Stress Induced Senescence
R-HSA-3108214	SUMOylation of DNA damage response and repair proteins
R-HSA-3899300	SUMOylation of transcription cofactors
R-HSA-4551638	SUMOylation of chromatin organization proteins
R-HSA-4570464	SUMOylation of RNA binding proteins
R-HSA-4655427	SUMOylation of DNA methylation proteins
R-HSA-8939243	RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known
R-HSA-8943724	Regulation of PTEN gene transcription
R-HSA-8953750	Transcriptional Regulation by E2F6
R-HSA-9976102	Differentiation of naive CD4+ T cells to T helper 2 cells (Th2 cells)
R-HSA-1257604	PIP3 activates AKT signaling
R-HSA-162582	Signal Transduction
R-HSA-212436	Generic Transcription Pathway
R-HSA-2262752	Cellular responses to stress
R-HSA-2559583	Cellular Senescence
R-HSA-2990846	SUMOylation
R-HSA-3108232	SUMO E3 ligases SUMOylate target proteins
R-HSA-392499	Metabolism of proteins
R-HSA-597592	Post-translational protein modification
R-HSA-6807070	PTEN Regulation
R-HSA-73857	RNA Polymerase II Transcription
R-HSA-74160	Gene expression (Transcription)
R-HSA-8878171	Transcriptional regulation by RUNX1
R-HSA-8953897	Cellular responses to stimuli
R-HSA-9006925	Intracellular signaling by second messengers

MSigDB gene sets: 437 (showing top): GSE45365_NK_CELL_VS_BCELL_DN, GOBP_REGULATION_OF_CELL_ACTIVATION, RNGTGGGC_UNKNOWN, FXR_IR1_Q6, GOBP_REGULATION_OF_LEUKOCYTE_PROLIFERATION, GOBP_EMBRYO_DEVELOPMENT_ENDING_IN_BIRTH_OR_EGG_HATCHING, GOBP_EPITHELIUM_DEVELOPMENT, ZHAN_LATE_DIFFERENTIATION_GENES_UP, GOBP_SKELETAL_SYSTEM_DEVELOPMENT, GGGNRMNNYCAT_UNKNOWN, GOBP_RESPONSE_TO_PEPTIDE, GOBP_CELLULAR_RESPONSE_TO_LIPID, GOBP_B_CELL_ACTIVATION, GOBP_RESPONSE_TO_CORTICOSTEROID, GOBP_EMBRYONIC_SKELETAL_SYSTEM_DEVELOPMENT

GO Biological Process (26): negative regulation of transcription by RNA polymerase II (GO:0000122), in utero embryonic development (GO:0001701), chromatin remodeling (GO:0006338), DNA methylation-dependent constitutive heterochromatin formation (GO:0006346), humoral immune response (GO:0006959), segment specification (GO:0007379), brain development (GO:0007420), regulation of gene expression (GO:0010468), rostrocaudal neural tube patterning (GO:0021903), hemopoiesis (GO:0030097), positive regulation of B cell proliferation (GO:0030890), positive regulation of immature T cell proliferation in thymus (GO:0033092), negative regulation of gene expression, epigenetic (GO:0045814), somatic stem cell division (GO:0048103), positive regulation of fibroblast proliferation (GO:0048146), embryonic skeletal system morphogenesis (GO:0048704), positive regulation of ubiquitin-protein transferase activity (GO:0051443), cellular response to interleukin-1 (GO:0071347), cellular response to dexamethasone stimulus (GO:0071549), regulation of kidney development (GO:0090183), apoptotic signaling pathway (GO:0097190), regulation of adaxial/abaxial pattern formation (GO:2000011), negative regulation of apoptotic signaling pathway (GO:2001234), skeletal system development (GO:0001501), chromatin organization (GO:0006325), embryonic skeletal system development (GO:0048706)

GO Molecular Function (7): zinc ion binding (GO:0008270), RING-like zinc finger domain binding (GO:0071535), ubiquitin-protein transferase activator activity (GO:0097027), promoter-specific chromatin binding (GO:1990841), chromatin binding (GO:0003682), protein binding (GO:0005515), metal ion binding (GO:0046872)

GO Cellular Component (9): ubiquitin ligase complex (GO:0000151), heterochromatin (GO:0000792), nucleus (GO:0005634), nucleoplasm (GO:0005654), cytosol (GO:0005829), nuclear body (GO:0016604), PcG protein complex (GO:0031519), PRC1 complex (GO:0035102), cytoplasm (GO:0005737)

Reactome top-level categories

Rollup of top-14 pathways:

Category	Pathways
SUMO E3 ligases SUMOylate target proteins	5
Cellular Senescence	1
Transcriptional regulation by RUNX1	1
PTEN Regulation	1
Generic Transcription Pathway	1
Differentiation of T cells	1
Intracellular signaling by second messengers	1
RNA Polymerase II Transcription	1
Cellular responses to stimuli	1
Cellular responses to stress	1
Post-translational protein modification	1
SUMOylation	1
Metabolism of proteins	1
PIP3 activates AKT signaling	1

GO top-level categories

Rollup of top GO terms by namespace:

Category	Terms
cellular anatomical structure	3
ubiquitin-protein transferase activity	2
binding	2
regulation of transcription by RNA polymerase II	1
transcription by RNA polymerase II	1
negative regulation of DNA-templated transcription	1
chordate embryonic development	1
chromatin organization	1
constitutive heterochromatin formation	1
immune response	1
pattern specification process	1
segmentation	1
central nervous system development	1
animal organ development	1
head development	1
gene expression	1
regulation of macromolecule biosynthetic process	1
anterior/posterior pattern specification	1
neural tube patterning	1
cell development	1
regulation of B cell proliferation	1
B cell proliferation	1
positive regulation of lymphocyte proliferation	1
positive regulation of B cell activation	1
immature T cell proliferation in thymus	1
regulation of immature T cell proliferation in thymus	1
positive regulation of immature T cell proliferation	1
negative regulation of gene expression	1
epigenetic regulation of gene expression	1
stem cell division	1
positive regulation of cell population proliferation	1
fibroblast proliferation	1
regulation of fibroblast proliferation	1
embryonic organ morphogenesis	1
skeletal system morphogenesis	1
embryonic skeletal system development	1
positive regulation of protein ubiquitination	1
positive regulation of catalytic activity	1
regulation of ubiquitin-protein transferase activity	1
response to interleukin-1	1

Protein interactions and networks

STRING

4511 interactions, top by confidence (×1000):

Protein A	Protein B	Partner UniProt	Score
BMI1	RNF2	Q99496	999
BMI1	RING1	Q06587	999
BMI1	PHC1	P78364	997
BMI1	CBX2	Q14781	995
BMI1	CBX7	O95931	992
BMI1	CBX4	O00257	991
BMI1	CBX1	P23197	991
BMI1	PCGF2	P35227	987
BMI1	EZH2	Q15910	985
BMI1	CBX8	Q9HC52	977
BMI1	SLC25A3	Q00325	970
BMI1	SUZ12	Q15022	970
BMI1	PHC2	Q8IXK0	964
BMI1	TTK	P33981	964
BMI1	RYBP	Q8N488	964

IntAct

205 interactions, top by confidence:

A	B	Type	Score
BMI1	CBX8	psi-mi:“MI:0915”(physical association)	0.970
CBX8	BMI1	psi-mi:“MI:2364”(proximity)	0.970
CBX8	BMI1	psi-mi:“MI:0407”(direct interaction)	0.970
CBX8	BMI1	psi-mi:“MI:0914”(association)	0.970
CBX8	BMI1	psi-mi:“MI:0915”(physical association)	0.970
BMI1	CBX8	psi-mi:“MI:0403”(colocalization)	0.970
RING1	BMI1	psi-mi:“MI:0915”(physical association)	0.960
BMI1	RING1	psi-mi:“MI:0915”(physical association)	0.960
RNF2	BMI1	psi-mi:“MI:0915”(physical association)	0.960
BMI1	RNF2	psi-mi:“MI:0915”(physical association)	0.960
RING1	BMI1	psi-mi:“MI:0914”(association)	0.960
BMI1	RING1	psi-mi:“MI:0914”(association)	0.960

BioGRID (1045): RNF2 (Co-purification), RNF2 (Reconstituted Complex), PHC2 (Two-hybrid), RING1 (Two-hybrid), NDEL1 (Two-hybrid), BMI1 (Co-crystal Structure), BMI1 (Protein-peptide), BMI1 (Affinity Capture-MS), BMI1 (Affinity Capture-MS), YLPM1 (Affinity Capture-MS), ILF3 (Affinity Capture-MS), TAF15 (Affinity Capture-MS), TDRD1 (Affinity Capture-MS), UPF1 (Affinity Capture-MS), ADAR (Affinity Capture-MS)

ESM2 similar proteins: A0JN86, A2AHJ4, A2APV2, A2AQW0, A9JRL3, B3DK16, O08874, O35099, P0CF52, P19447, P23798, P25916, P32866, P35226, P35227, P49135, Q07139, Q1JPS1, Q1RMT1, Q21029, Q28H21, Q2YDF9, Q32KX7, Q3UK78, Q4QR06, Q5R8L2, Q5RA62, Q5SDR3, Q5ZKK7, Q640D5, Q6DD21, Q6DLV9, Q6GN16, Q6RI45, Q6ZN16, Q7T3E6, Q7Z569, Q7ZYZ7, Q86SE9, Q8BPM2

Diamond homologs: A0JN86, B3DK16, P23798, P25916, P35226, P35227, Q07G17, Q0WX00, Q14527, Q1JPS1, Q28H21, Q2KJ29, Q2YDF9, Q32KX7, Q3KNV8, Q3UK78, Q4QR06, Q5R8L2, Q5SDR3, Q5XI70, Q640D5, Q6CJM4, Q6DLV9, Q7T3E6, Q7ZYZ7, Q86SE9, Q8BTQ0, Q8JIR0, Q8R023, Q91648, Q94AY3, Q99NA9, Q9BSM1, Q9BYE7, Q9FKW0, Q9LS86, Q9M9Y4, Q9TST0, O60106, Q19336

SIGNOR signaling

19 interactions.

A	Effect	B	Mechanism
BMI1	“down-regulates quantity by repression”	CDKN2A	“transcriptional regulation”
BMI1	“down-regulates quantity by repression”	PTEN	“transcriptional regulation”
BMI1	“up-regulates quantity by expression”	BMI1	“transcriptional regulation”
AKT	“up-regulates activity”	BMI1	phosphorylation
NDN	down-regulates	BMI1
BMI1	down-regulates	NDN
UBAP2L	“up-regulates activity”	BMI1	binding
BMI1	“form complex”	“Polycomb repressive complex 1”	binding
Ub:E2	“up-regulates activity”	BMI1	ubiquitination
SPOP	“up-regulates activity”	BMI1	binding
“Cullin 3-RBX1-Skp1”	“up-regulates activity”	BMI1	ubiquitination
CSNK2A1	“down-regulates quantity by destabilization”	BMI1	phosphorylation
BMI1	“up-regulates activity”	H2AX	ubiquitination
AKT2	“up-regulates activity”	BMI1	phosphorylation
AKT3	“up-regulates activity”	BMI1	phosphorylation
Membrane_blebbing	“up-regulates activity”	BMI1	phosphorylation
AKT1	“up-regulates activity”	BMI1	phosphorylation

Enriched among interaction partners

Reactome pathways and GO biological processes over-represented among this gene’s 101 IntAct physical interaction partners (hypergeometric vs the genome-wide background, BH-FDR, gene-set size 15–500, ranked by fold). A functional readout of the neighbourhood — distinct from this gene’s own memberships above, and biased toward well-studied / hub proteins, so read it as themes rather than proof.

Reactome pathways:

Pathway	Partners	Fold	FDR
SUMOylation of DNA methylation proteins	11	113.7×	3e-19
RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known	15	69.3×	3e-22
Transcriptional Regulation by E2F6	11	49.5×	2e-14
SUMOylation of transcription cofactors	11	41.1×	1e-13
SUMOylation of RNA binding proteins	11	40.3×	1e-13
Regulation of PTEN gene transcription	14	38.4×	6e-17
SUMOylation of chromatin organization proteins	12	29.3×	3e-13
SUMOylation of DNA damage response and repair proteins	11	24.8×	3e-11

GO biological processes:

GO term	Partners	Fold	FDR
negative regulation of proteasomal ubiquitin-dependent protein catabolic process	6	27.7×	2e-05
heterochromatin formation	5	14.7×	2e-03

Disease & clinical

Clinical variants and AI predictions

ClinVar

9 variants total. Per-class counts are floors (≥ shown; pagination cap):

Classification	Count (floor)
Pathogenic	0
Likely pathogenic	0
Uncertain significance	7
Likely benign	1
Benign	1

Top pathogenic / likely-pathogenic (0)

SpliceAI

1162 predictions. Top by Δscore:

Variant	Effect	Δscore
10:22326426:TGCA:T	acceptor_loss	1.0000
10:22326427:GCAG:G	acceptor_loss	1.0000
10:22326428:CA:C	acceptor_loss	1.0000
10:22326429:A:AC	acceptor_loss	1.0000
10:22326429:A:AG	acceptor_gain	1.0000
10:22326429:AG:A	acceptor_gain	1.0000
10:22326430:G:GA	acceptor_gain	1.0000
10:22326430:GG:G	acceptor_gain	1.0000
10:22326430:GGA:G	acceptor_gain	1.0000
10:22326430:GGAT:G	acceptor_gain	1.0000
10:22326430:GGATT:G	acceptor_gain	1.0000
10:22326557:TTCCT:T	donor_gain	1.0000
10:22326558:TCCT:T	donor_gain	1.0000
10:22326558:TCCTG:T	donor_loss	1.0000
10:22326559:CCT:C	donor_gain	1.0000
10:22326559:CCTGT:C	donor_loss	1.0000
10:22326560:CT:C	donor_gain	1.0000
10:22326560:CTGT:C	donor_loss	1.0000
10:22326561:TG:T	donor_loss	1.0000
10:22326562:G:GG	donor_gain	1.0000
10:22326562:GTAA:G	donor_loss	1.0000
10:22326563:T:A	donor_loss	1.0000
10:22326563:T:G	donor_loss	1.0000
10:22326564:AA:A	donor_loss	1.0000
10:22326888:A:AG	acceptor_gain	1.0000
10:22326889:G:GA	acceptor_gain	1.0000
10:22326889:GT:G	acceptor_gain	1.0000
10:22326889:GTCT:G	acceptor_gain	1.0000
10:22327651:G:GG	donor_gain	1.0000
10:22327738:TCAGA:T	acceptor_loss	1.0000

AlphaMissense

2165 scored. Top likely-pathogenic:

Variant	Protein change	am_pathogenicity
10:22326484:T:A	L12Q	1.000
10:22326484:T:C	L12P	1.000
10:22326488:T:A	N13K	1.000
10:22326488:T:G	N13K	1.000
10:22326496:T:A	L16Q	1.000
10:22326496:T:C	L16P	1.000
10:22326501:T:A	C18S	1.000
10:22326501:T:C	C18R	1.000
10:22326502:G:A	C18Y	1.000
10:22326502:G:C	C18S	1.000
10:22326502:G:T	C18F	1.000
10:22326503:T:G	C18W	1.000
10:22326510:T:A	C21S	1.000
10:22326510:T:C	C21R	1.000
10:22326511:G:A	C21Y	1.000
10:22326511:G:C	C21S	1.000
10:22326511:G:T	C21F	1.000
10:22326512:T:G	C21W	1.000
10:22326516:G:A	G23R	1.000
10:22326516:G:C	G23R	1.000
10:22326516:G:T	G23W	1.000
10:22326517:G:A	G23E	1.000
10:22326517:G:T	G23V	1.000
10:22326519:T:C	Y24H	1.000
10:22326523:T:C	F25S	1.000
10:22326526:T:A	I26N	1.000
10:22326529:A:T	D27V	1.000
10:22326532:C:A	A28D	1.000
10:22326532:C:T	A28V	1.000
10:22326538:C:T	T30I	1.000

dbSNP variants (sampled 300 via entrez): RS1000104172 (10:22331976 A>C,T), RS1000814650 (10:22319566 T>A,C), RS1001065063 (10:22326251 C>T), RS1001221720 (10:22323605 T>G), RS1001531663 (10:22321631 A>C,G), RS1001754277 (10:22330801 A>G), RS1002227937 (10:22322303 G>A,C,T), RS1002408957 (10:22321976 G>A), RS1002484452 (10:22321485 C>G,T), RS1002748376 (10:22325623 T>C,G), RS1002895331 (10:22325120 C>T), RS1003022707 (10:22319636 A>G), RS1003075558 (10:22324363 A>G), RS1003409145 (10:22322993 C>T), RS1003482800 (10:22331834 T>G)

Disease associations

OMIM: gene MIM:164831 | disease phenotypes:

GenCC curated gene-disease

Mondo (1): breast ductal adenocarcinoma (MONDO:0005590)

Orphanet (0):

HPO phenotypes

0 total (0 of 0 shown, HPO-id order):

GWAS associations

1 associations (top):

Study	Trait	p-value
GCST004093_34	Prostate-specific antigen levels	1.000000e-14

MeSH disease descriptors (1)

Descriptor	Name	Tree numbers
D018270	Carcinoma, Ductal, Breast	C04.557.470.200.025.232.500; C04.557.470.615.132.500; C04.588.180.390; C17.800.090.500.390

Drugs & pharmacology

Drug and pharmacology data

Is drug target: yes

ChEMBL targets (3): CHEMBL4295749 (SINGLE PROTEIN), CHEMBL6066042 (PROTEIN-PROTEIN INTERACTION), CHEMBL6193762 (PROTEIN-PROTEIN INTERACTION)

PharmGKB: 1 entry (VIP=true, CPIC=false)

ChEMBL bioactivities

25 potent at pChembl≥5 of 25 total, top 25 by pChembl (potency: 10 = 0.1 nM, 6 = 1 µM).

pChembl	Type	Value	Unit	Molecule
9.00	IC50	1	nM	CHEMBL5270667
9.00	IC50	1	nM	CHEMBL5275887
9.00	IC50	1	nM	CHEMBL5272249
9.00	IC50	1	nM	CHEMBL5271126
9.00	IC50	1	nM	CHEMBL5269901
9.00	IC50	1	nM	CHEMBL5282393
9.00	IC50	1	nM	CHEMBL5281109
9.00	IC50	1	nM	CHEMBL5288239
9.00	IC50	1	nM	CHEMBL5287305
9.00	IC50	1	nM	CHEMBL5270834
9.00	IC50	1	nM	CHEMBL5274905
9.00	IC50	1	nM	CHEMBL5285217
9.00	IC50	1	nM	CHEMBL5278557
9.00	IC50	1	nM	CHEMBL5282609
9.00	IC50	1	nM	CHEMBL5289952
9.00	IC50	1	nM	CHEMBL5268696
9.00	IC50	1	nM	CHEMBL5273906
9.00	IC50	1	nM	CHEMBL5280041
9.00	IC50	1	nM	CHEMBL5276953
9.00	IC50	1	nM	CHEMBL5266175
9.00	IC50	1	nM	CHEMBL5270622
9.00	IC50	1	nM	CHEMBL5272817
9.00	IC50	1	nM	CHEMBL5272260
9.00	IC50	1	nM	CHEMBL5282796
9.00	IC50	1	nM	CHEMBL5278972

PubChem BioAssay actives

50 with measured affinity, of 81 total; 25 most potent distinct compounds. Largely complementary to BindingDB; screening values are coarse (µM, 4 dp), so sub-nM hits tie at the floor.

Compound	Assay	Type	Value	Unit
5-(2-methylbenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
3-(2-ethylbenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
N-[4-(difluoromethoxy)phenyl]-5-(6-fluoro-2-methylbenzimidazol-1-yl)-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
3-(2-cyclopropylbenzimidazol-1-yl)-N-[4-(difluoromethoxy)phenyl]-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
5-(2-ethylbenzimidazol-1-yl)-N-(4-methoxyphenyl)-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
3-(2-cyclopropyl-6-fluorobenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
N-[4-(difluoromethoxy)phenyl]-3-(2-ethylbenzimidazol-1-yl)-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
5-(2-cyclopropylbenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
3-(2-ethyl-6-fluorobenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
5-(2-ethylbenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
5-(2-ethylbenzimidazol-1-yl)-N-(4-methylphenyl)-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
N-(4-methoxyphenyl)-5-(2-methylbenzimidazol-1-yl)-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
3-(2-cyclopropylbenzimidazol-1-yl)-N-(4-methoxyphenyl)-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
5-(2-methylbenzimidazol-1-yl)-N-(4-methylphenyl)-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
5-(6-fluoro-2-methylbenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
N-[4-(difluoromethoxy)phenyl]-5-(2-ethylbenzimidazol-1-yl)-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
3-(2-ethylbenzimidazol-1-yl)-N-(4-methoxyphenyl)-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
5-(2-cyclopropyl-6-fluorobenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
N-[4-(difluoromethoxy)phenyl]-5-(2-methylbenzimidazol-1-yl)-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
N-[4-(difluoromethoxy)phenyl]-5-(2-ethyl-6-fluorobenzimidazol-1-yl)-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
N-[4-(difluoromethoxy)phenyl]-3-(2-methylbenzimidazol-1-yl)-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
3-(2-cyclopropylbenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
3-(2-methylbenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-5-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
5-(2-ethyl-6-fluorobenzimidazol-1-yl)-N-[4-(trifluoromethyl)phenyl]-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM
5-(2-cyclopropylbenzimidazol-1-yl)-N-[4-(difluoromethoxy)phenyl]-1,2,4-triazin-3-amine	1958785: Inhibition of BMI1 (unknown origin) by ELISA assay	ic50	0.0010	uM

CTD chemical–gene interactions

59 total (human), top 30 by PubMed support.

Chemical	Actions (top 5)	PubMed papers
Cisplatin	increases expression, decreases reaction, increases phosphorylation, increases abundance, decreases response to substance (+4 more)	5
sodium arsenite	increases reaction, decreases reaction, increases expression, affects reaction, affects expression (+2 more)	4
Smoke	decreases reaction, increases expression, decreases expression	3
bisphenol A	increases expression, affects cotreatment, decreases expression	2
trichostatin A	affects cotreatment, increases expression, affects expression	2
Acetaminophen	decreases expression	2
Silicon Dioxide	decreases expression, increases expression, decreases acetylation, decreases reaction, affects expression (+2 more)	2
Tretinoin	increases expression	2
Valproic Acid	decreases methylation, increases expression	2
FR900359	increases phosphorylation	1
napabucasin	decreases expression	1
triphenyl phosphate	affects expression	1
cobaltous chloride	decreases expression	1
nickel sulfate	decreases expression	1
S-(1,2-dichlorovinyl)cysteine	affects response to substance, increases expression	1
diallyl trisulfide	affects expression	1
3-deazaneplanocin	increases expression, decreases reaction	1
casticin	decreases expression, increases reaction, decreases reaction	1
di-n-butylphosphoric acid	affects expression	1
benzyloxycarbonylleucyl-leucyl-leucine aldehyde	increases expression	1
abrine	increases expression	1
imetelstat	decreases expression	1
protoapigenone	decreases expression	1
bisphenol S	affects cotreatment, decreases expression	1
jinfukang	decreases expression, increases reaction	1
ibrutinib	decreases expression	1
(+)-JQ1 compound	decreases expression	1
2-pyridine-3-yl-methylene-indan-1,3-dione	decreases expression	1
Rosiglitazone	decreases expression	1
Temozolomide	decreases expression	1

ChEMBL screening assays

25 unique, capped per target: 25 binding

Representative assays (with source publication via chembl_document):

Assay ID	Type	Description	Source paper
CHEMBL4270360	Binding	Inhibition of Bmi1 in human HCT116 cells assessed as reduction in H2A-K119Ub level after 8 hrs by Western blot analysis	Synthesis of Cyanoenone-Modified Diterpenoid Analogs as Novel Bmi-1-Mediated Antitumor Agents. — ACS Med Chem Lett

Cellosaurus cell lines

43 cell lines: 19 telomerase immortalized cell line, 14 finite cell line, 4 transformed cell line, 4 cancer cell line, 2 embryonic stem cell

First 10 cell lines (id-ordered, not curated):

Cellosaurus	Name	Category	Sex
CVCL_3222	UBE6T-15	Telomerase immortalized cell line	Female
CVCL_3223	UBE6T-6	Telomerase immortalized cell line	Female
CVCL_3224	UBE6T-7	Telomerase immortalized cell line	Female
CVCL_4W37	HAdpc-25-Bmi-1-TERT	Telomerase immortalized cell line	Female
CVCL_4W38	HAdpc-26-E6-Bmi-1-TERT	Transformed cell line	Female
CVCL_6F31	HAdpc-24-Bmi-1	Finite cell line	Female
CVCL_6F33	UBE6T-8	Telomerase immortalized cell line	Female
CVCL_6F37	BCPb8	Telomerase immortalized cell line	Sex unspecified
CVCL_6F38	UBT-10	Telomerase immortalized cell line	Female
CVCL_A0I7	SEES3-1V human BMI1, clone1	Embryonic stem cell	Male

Clinical trials (associated diseases)

11 trials via MONDO — disease-level, not drug-specific.

Trial	Phase	Status	Title
NCT03414970	PHASE3	ACTIVE_NOT_RECRUITING	Hypofractionated Radiation Therapy After Mastectomy in Preventing Recurrence in Patients With Stage IIa-IIIa Breast Cancer
NCT00461344	PHASE2	TERMINATED	Docetaxel + Doxorubicin as Neoadjuvant Chemotherapy in Patients With Breast Cancer
NCT07499999	PHASE2	NOT_YET_RECRUITING	Randomized Double-Blind Phase II Trial of Baby Exemestane Versus Baby Tamoxifen in Post-Menopausal Women at High Risk for Breast Cancer
NCT00637364	PHASE1/PHASE2	SUSPENDED	High Intensity Focused Ultrasound Tumor Treatment for Pancreatic Cancer Pain
NCT02779855	PHASE1/PHASE2	COMPLETED	Talimogene Laherparepvec in Combination With Neoadjuvant Chemotherapy in Triple Negative Breast Cancer
NCT01753908	EARLY_PHASE1	COMPLETED	Broccoli Sprout Extract in Treating Patients With Breast Cancer
NCT01796041	EARLY_PHASE1	COMPLETED	Intraoperative Imaging of Breast Cancer With Indocyanine Green
NCT01208974	Not specified	ACTIVE_NOT_RECRUITING	Nipple-Areola Complex (NAC) Irradiation After Nipple-Sparing Mastectomy and Reconstruction
NCT01875198	Not specified	TERMINATED	Oncologic Impact of Splenectomy-omitting Radical Pancreatectomy in Well-selected Left-sided Pancreatic Cancer
NCT03543397	Not specified	UNKNOWN	MRI in Ductal Carcinoma in Situ (DCIS)
NCT03834532	Not specified	COMPLETED	Living Well After Breast Surgery