O75150 (BRE1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
E3 ubiquitin-protein ligase BRE1B
Short name=BRE1-B
EC=6.3.2.-

Alternative name(s):
95 kDa retinoblastoma-associated protein
Short name=RBP95
RING finger protein 40

Gene names

Name:	RNF40
Synonyms:	BRE1B, KIAA0661

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1001 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Component of the RNF20/40 E3 ubiquitin-protein ligase complex that mediates monoubiquitination of 'Lys-120' of histone H2B (H2BK120ub1). H2BK120ub1 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation (H3K4me and H3K79me, respectively). It thereby plays a central role in histone code and gene regulation. The RNF20/40 complex forms a H2B ubiquitin ligase complex in cooperation with the E2 enzyme UBE2A or UBE2B; reports about the cooperation with UBE2E1/UBCH are contradictory. Required for transcriptional activation of Hox genes. Ref.7 Ref.8
Pathway	Protein modification; protein ubiquitination.
Subunit structure	Component of the RNF20/40 complex (also known as BRE1 complex) probably composed of 2 copies of RNF20/BRE1A and 2 copies of RNF40/BRE1B. Interacts with UBE2E1/UBCH6. Interacts with RB1 and WAC. Ref.1 Ref.7 Ref.8 Ref.10
Subcellular location	Nucleus Ref.1.
Tissue specificity	Ubiquitously expressed. Expressed at higher level in testis, heart and pancreas, while it is only weakly expressed in lung, skeletal muscle and small intestine. Ref.1
Sequence similarities	Belongs to the BRE1 family. Contains 1 RING-type zinc finger.
Sequence caution	The sequence BAA31636.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened. The sequence CAE45869.1 differs from that shown. Reason: Aberrant splicing.

Ontologies

Keywords
Biological process	Ubl conjugation pathway
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Chromatin regulator Ligase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	histone H2B ubiquitination Inferred from direct assay Ref.7. Source: UniProtKB histone monoubiquitination Inferred from direct assay Ref.7. Source: UniProtKB ubiquitin-dependent protein catabolic process Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	HULC complex Inferred from direct assay Ref.8. Source: UniProtKB cytoplasm Inferred from direct assay. Source: HPA neuron projection Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay Ref.1Ref.7. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA
Molecular_function	ubiquitin-protein ligase activity Inferred from electronic annotation. Source: Compara zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
RB1	P06400	3	EBI-744408,EBI-491274
RNF20	Q5VTR2	10	EBI-744408,EBI-2372238

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75150-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 3 (identifier: O75150-3)

The sequence of this isoform differs from the canonical sequence as follows:
     822-838: DAQLLTVQKLEEKERAL → WPPPACRLELERWGSWP
     839-1001: Missing.

Note: No experimental confirmation available.

Isoform 4 (identifier: O75150-4)

The sequence of this isoform differs from the canonical sequence as follows:
     332-431: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1001	1001	E3 ubiquitin-protein ligase BRE1B		PRO_0000055839
Regions
	Zinc finger	948 – 987	40	RING-type
	Coiled coil	44 – 91	48	Potential
	Coiled coil	189 – 377	189	Potential
	Coiled coil	437 – 525	89	Potential
	Coiled coil	627 – 946	320	Potential
Natural variations
	Alternative sequence	332 – 431	100	Missing in isoform 4.		VSP_016681
	Alternative sequence	822 – 838	17	DAQLL…KERAL → WPPPACRLELERWGSWP in isoform 3.		VSP_016682
	Alternative sequence	839 – 1001	163	Missing in isoform 3.		VSP_016683
	Natural variant	463	1	R → H. Corresponds to variant rs11556801 [ dbSNP | Ensembl ].		VAR_055021
	Natural variant	615	1	Q → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Corresponds to variant rs7195142 [ dbSNP | Ensembl ].		VAR_055022
Experimental info
	Mutagenesis	109	1	L → S: Abolishes interaction with RB1. Ref.1
	Mutagenesis	111	1	C → M: Abolishes interaction with RB1. Ref.1
	Mutagenesis	113	1	E → Q: Abolishes interaction with RB1. Ref.1
	Sequence conflict	56	1	N → D in BAB55092. Ref.3
	Sequence conflict	96	1	R → L in AAG13723. Ref.1
	Sequence conflict	108	1	L → P in BAB55092. Ref.3
	Sequence conflict	172	1	S → G in BAB55092. Ref.3
	Sequence conflict	387	1	E → K in CAH10518. Ref.4
	Sequence conflict	562	1	K → E in CAE45869. Ref.4
	Sequence conflict	600	1	S → F in CAE45869. Ref.4
	Sequence conflict	714	1	D → N in BAB55092. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 30, 2010. Version 4. Checksum: 82D7CD183EDD5EFC	FASTA	1,001	113,650
	10 20 30 40 50 60 MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK VLQFKNKKLA 70 80 90 100 110 120 ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ LDETVEALLR CHESQGELSS 130 140 150 160 170 180 APEAPGTQEG PTCDGTPLPE PGTSELRDPL LMQLRPPLSE PALAFVVALG ASSSEEVELE 190 200 210 220 230 240 LQGRMEFSKA AVSRVVEASD RLQRRVEELC QRVYSRGDSE PLSEAAQAHT RELGRENRRL 250 260 270 280 290 300 QDLATQLQEK HHRISLEYSE LQDKVTSAET KVLEMETTVE DLQWDIEKLR KREQKLNKHL 310 320 330 340 350 360 AEALEQLNSG YYVSGSSSGF QGGQITLSMQ KFEMLNAELE ENQELANSRM AELEKLQAEL 370 380 390 400 410 420 QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN ESLQVKTQLD EARGLLLATK 430 440 450 460 470 480 NSHLRHIEHM ESDELGLQKK LRTEVIQLED TLAQVRKEYE MLRIEFEQNL AANEQAGPIN 490 500 510 520 530 540 REMRHLISSL QNHNHQLKGD AQRYKRKLRE VQAEIGKLRA QASGSAHSTP NLGHPEDSGV 550 560 570 580 590 600 SAPAPGKEEG GPGPVSTPDN RKEMAPVPGT TTTTTSVKKE ELVPSEEDFQ GITPGAQGPS 610 620 630 640 650 660 SRGREPEARP KRELQEREGP SLGPPPVASA LSRADREKAK VEETKRKESE LLKGLRAELK 670 680 690 700 710 720 KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV DELRSRIREL EERDRRESKK 730 740 750 760 770 780 IADEDALRRI RQAEEQIEHL QRKLGATKQE EEALLSEMDV TGQAFEDMQE QNGRLLQQLR 790 800 810 820 830 840 EKDDANFKLM SERIKANQIH KLLREEKDEL GEQVLGLKSQ VDAQLLTVQK LEEKERALQG 850 860 870 880 890 900 SLGGVEKELT LRSQALELNK RKAVEAAQLA EDLKVQLEHV QTRLREIQPC LAESRAAREK 910 920 930 940 950 960 ESFNLKRAQE DISRLRRKLE KQRKVEVYAD ADEILQEEIK EYKARLTCPC CNTRKKDAVL 970 980 990 1000 TKCFHVFCFE CVRGRYEARQ RKCPKCNAAF GAHDFHRIYI S
	Isoform 3 [UniParc]. Checksum: 87B68E08B358A730	FASTA	838	94,796
	10 20 30 40 50 60 MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK VLQFKNKKLA 70 80 90 100 110 120 ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ LDETVEALLR CHESQGELSS 130 140 150 160 170 180 APEAPGTQEG PTCDGTPLPE PGTSELRDPL LMQLRPPLSE PALAFVVALG ASSSEEVELE 190 200 210 220 230 240 LQGRMEFSKA AVSRVVEASD RLQRRVEELC QRVYSRGDSE PLSEAAQAHT RELGRENRRL 250 260 270 280 290 300 QDLATQLQEK HHRISLEYSE LQDKVTSAET KVLEMETTVE DLQWDIEKLR KREQKLNKHL 310 320 330 340 350 360 AEALEQLNSG YYVSGSSSGF QGGQITLSMQ KFEMLNAELE ENQELANSRM AELEKLQAEL 370 380 390 400 410 420 QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN ESLQVKTQLD EARGLLLATK 430 440 450 460 470 480 NSHLRHIEHM ESDELGLQKK LRTEVIQLED TLAQVRKEYE MLRIEFEQNL AANEQAGPIN 490 500 510 520 530 540 REMRHLISSL QNHNHQLKGD AQRYKRKLRE VQAEIGKLRA QASGSAHSTP NLGHPEDSGV 550 560 570 580 590 600 SAPAPGKEEG GPGPVSTPDN RKEMAPVPGT TTTTTSVKKE ELVPSEEDFQ GITPGAQGPS 610 620 630 640 650 660 SRGREPEARP KRELQEREGP SLGPPPVASA LSRADREKAK VEETKRKESE LLKGLRAELK 670 680 690 700 710 720 KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV DELRSRIREL EERDRRESKK 730 740 750 760 770 780 IADEDALRRI RQAEEQIEHL QRKLGATKQE EEALLSEMDV TGQAFEDMQE QNGRLLQQLR 790 800 810 820 830 EKDDANFKLM SERIKANQIH KLLREEKDEL GEQVLGLKSQ VWPPPACRLE LERWGSWP
	Isoform 4 [UniParc]. Checksum: 445DD31CF7511205	FASTA	901	102,046
	10 20 30 40 50 60 MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK VLQFKNKKLA 70 80 90 100 110 120 ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ LDETVEALLR CHESQGELSS 130 140 150 160 170 180 APEAPGTQEG PTCDGTPLPE PGTSELRDPL LMQLRPPLSE PALAFVVALG ASSSEEVELE 190 200 210 220 230 240 LQGRMEFSKA AVSRVVEASD RLQRRVEELC QRVYSRGDSE PLSEAAQAHT RELGRENRRL 250 260 270 280 290 300 QDLATQLQEK HHRISLEYSE LQDKVTSAET KVLEMETTVE DLQWDIEKLR KREQKLNKHL 310 320 330 340 350 360 AEALEQLNSG YYVSGSSSGF QGGQITLSMQ KSDELGLQKK LRTEVIQLED TLAQVRKEYE 370 380 390 400 410 420 MLRIEFEQNL AANEQAGPIN REMRHLISSL QNHNHQLKGD AQRYKRKLRE VQAEIGKLRA 430 440 450 460 470 480 QASGSAHSTP NLGHPEDSGV SAPAPGKEEG GPGPVSTPDN RKEMAPVPGT TTTTTSVKKE 490 500 510 520 530 540 ELVPSEEDFQ GITPGAQGPS SRGREPEARP KRELQEREGP SLGPPPVASA LSRADREKAK 550 560 570 580 590 600 VEETKRKESE LLKGLRAELK KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV 610 620 630 640 650 660 DELRSRIREL EERDRRESKK IADEDALRRI RQAEEQIEHL QRKLGATKQE EEALLSEMDV 670 680 690 700 710 720 TGQAFEDMQE QNGRLLQQLR EKDDANFKLM SERIKANQIH KLLREEKDEL GEQVLGLKSQ 730 740 750 760 770 780 VDAQLLTVQK LEEKERALQG SLGGVEKELT LRSQALELNK RKAVEAAQLA EDLKVQLEHV 790 800 810 820 830 840 QTRLREIQPC LAESRAAREK ESFNLKRAQE DISRLRRKLE KQRKVEVYAD ADEILQEEIK 850 860 870 880 890 900 EYKARLTCPC CNTRKKDAVL TKCFHVFCFE CVRGRYEARQ RKCPKCNAAF GAHDFHRIYI S

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"RBP95, a novel leucine zipper protein, binds to the retinoblastoma protein." Wen H., Ao S. Biochem. Biophys. Res. Commun. 275:141-148(2000) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, SUBUNIT, INTERACTION WITH RB1, MUTAGENESIS OF LEU-109; CYS-111 AND GLU-113, VARIANT ARG-615. Tissue: Fetal brain.
[2]	"Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro." Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O. DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-615. Tissue: Brain.
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), VARIANT ARG-615. Tissue: Teratocarcinoma.
[4]	"The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-615. Tissue: Cervix and Rectum tumor.
[5]	"The sequence and analysis of duplication-rich human chromosome 16." Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J. , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A. Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-615. Tissue: Brain, Mammary gland, Skin and Uterus.
[7]	"Monoubiquitination of human histone H2B: the factors involved and their roles in HOX gene regulation." Zhu B., Zheng Y., Pham A.-D., Mandal S.S., Erdjument-Bromage H., Tempst P., Reinberg D. Mol. Cell 20:601-611(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH RNF20 AND UBE2E1.
[8]	"RAD6-mediated transcription-coupled H2B ubiquitylation directly stimulates H3K4 methylation in human cells." Kim J., Guermah M., McGinty R.K., Lee J.S., Tang Z., Milne T.A., Shilatifard A., Muir T.W., Roeder R.G. Cell 137:459-471(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[9]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]	"WAC, a functional partner of RNF20/40, regulates histone H2B ubiquitination and gene transcription." Zhang F., Yu X. Mol. Cell 41:384-397(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH WAC.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF122819 mRNA. Translation: AAG13723.1. AB014561 mRNA. Translation: BAA31636.2. Different initiation. AK027406 mRNA. Translation: BAB55092.1. BX640763 mRNA. Translation: CAE45869.1. Sequence problems. CR627431 mRNA. Translation: CAH10518.1. AC106886 Genomic DNA. No translation available. BC004527 mRNA. Translation: AAH04527.2. BC006133 mRNA. Translation: AAH06133.1. BC011769 mRNA. Translation: AAH11769.1. BC018647 mRNA. Translation: AAH18647.1. BC030802 mRNA. Translation: AAH30802.2.
IPI	IPI00162563. IPI00290648. IPI00377273.
PIR	JC7363.
RefSeq	NP_001193962.1. NM_001207033.1. NP_001193963.1. NM_001207034.1. NP_055586.1. NM_014771.3.
UniGene	Hs.65238.
3D structure databases
ProteinModelPortal	O75150.
SMR	O75150. Positions 938-998.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75150. 11 interactions.
MINT	MINT-1466706.
STRING	9606.ENSP00000325677.
PTM databases
PhosphoSite	O75150.
Proteomic databases
PaxDb	O75150.
PRIDE	O75150.
Protocols and materials databases
DNASU	9810.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000324685; ENSP00000325677; ENSG00000103549. ENST00000357890; ENSP00000350563; ENSG00000103549.
GeneID	9810.
KEGG	hsa:9810.
UCSC	uc002dzq.3. human. uc010cab.3. human.
Organism-specific databases
CTD	9810.
GeneCards	GC16P030773.
HGNC	HGNC:16867. RNF40.
HPA	HPA041330.
MIM	607700. gene.
neXtProt	NX_O75150.
PharmGKB	PA34440.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG263074.
HOVERGEN	HBG080312.
InParanoid	O75150.
KO	K10696.
OMA	CHESQGE.
OrthoDB	EOG4933HD.
PhylomeDB	O75150.
Enzyme and pathway databases
UniPathway	UPA00143.
Gene expression databases
ArrayExpress	O75150.
Bgee	O75150.
CleanEx	HS_RNF40.
Genevestigator	O75150.
GermOnline	ENSG00000103549. Homo sapiens.
Family and domain databases
Gene3D	3.30.40.10. 1 hit.
InterPro	IPR001841. Znf_RING. IPR013083. Znf_RING/FYVE/PHD. IPR017907. Znf_RING_CS. [Graphical view]
SMART	SM00184. RING. 1 hit. [Graphical view]
PROSITE	PS00518. ZF_RING_1. 1 hit. PS50089. ZF_RING_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9810.
NextBio	36932.
SOURCE	Search...

Entry information

Entry name

BRE1B_HUMAN

Accession

Primary (citable) accession number: O75150
Secondary accession number(s): Q6AHZ6 , Q6N005, Q7L3T6, Q8N615, Q96T18, Q9BSV9, Q9HC82

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	November 30, 2010
Last modified:	May 1, 2013
This is version 106 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.