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O75150 (BRE1B_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 114. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1001 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10011001E3 ubiquitin-protein ligase BRE1B
PRO_0000055839

Regions

Zinc finger948 – 98740RING-type
Coiled coil44 – 9148 Potential
Coiled coil189 – 377189 Potential
Coiled coil437 – 52589 Potential
Coiled coil627 – 946320 Potential

Amino acid modifications

Modified residue201N6-acetyllysine By similarity
Modified residue5171N6-acetyllysine By similarity

Natural variations

Alternative sequence332 – 431100Missing in isoform 4.
VSP_016681
Alternative sequence822 – 83817DAQLL…KERAL → WPPPACRLELERWGSWP in isoform 3.
VSP_016682
Alternative sequence839 – 1001163Missing in isoform 3.
VSP_016683
Natural variant4631R → H.
Corresponds to variant rs11556801 [ dbSNP | Ensembl ].
VAR_055021
Natural variant6151Q → R. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6
Corresponds to variant rs7195142 [ dbSNP | Ensembl ].
VAR_055022

Experimental info

Mutagenesis1091L → S: Abolishes interaction with RB1. Ref.1
Mutagenesis1111C → M: Abolishes interaction with RB1. Ref.1
Mutagenesis1131E → Q: Abolishes interaction with RB1. Ref.1
Sequence conflict561N → D in BAB55092. Ref.3
Sequence conflict961R → L in AAG13723. Ref.1
Sequence conflict1081L → P in BAB55092. Ref.3
Sequence conflict1721S → G in BAB55092. Ref.3
Sequence conflict3871E → K in CAH10518. Ref.4
Sequence conflict5621K → E in CAE45869. Ref.4
Sequence conflict6001S → F in CAE45869. Ref.4
Sequence conflict7141D → N in BAB55092. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 30, 2010. Version 4.
Checksum: 82D7CD183EDD5EFC

FASTA1,001113,650
        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 

« Hide

Isoform 3 [UniParc].

Checksum: 87B68E08B358A730
Show »

FASTA83894,796
Isoform 4 [UniParc].

Checksum: 445DD31CF7511205
Show »

FASTA901102,046

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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.
PIRJC7363.
RefSeqNP_001193962.1. NM_001207033.1.
NP_001193963.1. NM_001207034.1.
NP_001273501.1. NM_001286572.1.
NP_055586.1. NM_014771.3.
UniGeneHs.65238.

3D structure databases

ProteinModelPortalO75150.
SMRO75150. Positions 931-1000.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115149. 38 interactions.
IntActO75150. 13 interactions.
MINTMINT-1466706.
STRING9606.ENSP00000325677.

PTM databases

PhosphoSiteO75150.

Proteomic databases

PaxDbO75150.
PRIDEO75150.

Protocols and materials databases

DNASU9810.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324685; ENSP00000325677; ENSG00000103549. [O75150-1]
ENST00000357890; ENSP00000350563; ENSG00000103549. [O75150-4]
GeneID9810.
KEGGhsa:9810.
UCSCuc002dzq.3. human. [O75150-1]
uc010cab.3. human. [O75150-4]

Organism-specific databases

CTD9810.
GeneCardsGC16P030775.
HGNCHGNC:16867. RNF40.
HPAHPA041330.
MIM607700. gene.
neXtProtNX_O75150.
PharmGKBPA34440.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG263074.
HOVERGENHBG080312.
InParanoidO75150.
KOK10696.
OMACHESQGE.
OrthoDBEOG7DVD99.
PhylomeDBO75150.
TreeFamTF323183.

Enzyme and pathway databases

UniPathwayUPA00143.

Gene expression databases

ArrayExpressO75150.
BgeeO75150.
CleanExHS_RNF40.
GenevestigatorO75150.

Family and domain databases

Gene3D3.30.40.10. 1 hit.
InterProIPR018957. Znf_C3HC4_RING-type.
IPR001841. Znf_RING.
IPR013083. Znf_RING/FYVE/PHD.
IPR017907. Znf_RING_CS.
[Graphical view]
PfamPF00097. zf-C3HC4. 1 hit.
[Graphical view]
SMARTSM00184. RING. 1 hit.
[Graphical view]
PROSITEPS00518. ZF_RING_1. 1 hit.
PS50089. ZF_RING_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRNF40.
GenomeRNAi9810.
NextBio36932.
PROO75150.
SOURCESearch...

Entry information

Entry nameBRE1B_HUMAN
AccessionPrimary (citable) accession number: O75150
Secondary accession number(s): Q6AHZ6 expand/collapse secondary AC list , Q6N005, Q7L3T6, Q8N615, Q96T18, Q9BSV9, Q9HC82
Entry history
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 114 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM