CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-001123
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase BRE1B 
Protein Synonyms/Alias
 BRE1-B; 95 kDa retinoblastoma-associated protein; RBP95; RING finger protein 40 
Gene Name
 RNF40 
Gene Synonyms/Alias
 BRE1B; KIAA0661 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20GGSGPPEKKLSREEKacetylation[1]
50STEEMDLKVLQFKNKubiquitination[2, 3]
189QGRMEFSKAAVSRVVubiquitination[2, 3]
264EYSELQDKVTSAETKubiquitination[2]
420RGLLLATKNSHLRHIubiquitination[3]
439SDELGLQKKLRTEVIubiquitination[2]
457DTLAQVRKEYEMLRIubiquitination[3]
788EKDDANFKLMSERIKubiquitination[4]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473
Functional Description
 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. 
Sequence Annotation
 ZN_FING 948 987 RING-type.  
Keyword
 Alternative splicing; Chromatin regulator; Coiled coil; Complete proteome; Ligase; Metal-binding; Nucleus; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1001 AA 
Protein Sequence
MSGPGNKRAA GDGGSGPPEK KLSREEKTTT TLIEPIRLGG ISSTEEMDLK VLQFKNKKLA 60
ERLEQRQACE DELRERIEKL EKRQATDDAT LLIVNRYWAQ LDETVEALLR CHESQGELSS 120
APEAPGTQEG PTCDGTPLPE PGTSELRDPL LMQLRPPLSE PALAFVVALG ASSSEEVELE 180
LQGRMEFSKA AVSRVVEASD RLQRRVEELC QRVYSRGDSE PLSEAAQAHT RELGRENRRL 240
QDLATQLQEK HHRISLEYSE LQDKVTSAET KVLEMETTVE DLQWDIEKLR KREQKLNKHL 300
AEALEQLNSG YYVSGSSSGF QGGQITLSMQ KFEMLNAELE ENQELANSRM AELEKLQAEL 360
QGAVRTNERL KVALRSLPEE VVRETGEYRM LQAQFSLLYN ESLQVKTQLD EARGLLLATK 420
NSHLRHIEHM ESDELGLQKK LRTEVIQLED TLAQVRKEYE MLRIEFEQNL AANEQAGPIN 480
REMRHLISSL QNHNHQLKGD AQRYKRKLRE VQAEIGKLRA QASGSAHSTP NLGHPEDSGV 540
SAPAPGKEEG GPGPVSTPDN RKEMAPVPGT TTTTTSVKKE ELVPSEEDFQ GITPGAQGPS 600
SRGREPEARP KRELQEREGP SLGPPPVASA LSRADREKAK VEETKRKESE LLKGLRAELK 660
KAQESQKEMK LLLDMYKSAP KEQRDKVQLM AAERKAKAEV DELRSRIREL EERDRRESKK 720
IADEDALRRI RQAEEQIEHL QRKLGATKQE EEALLSEMDV TGQAFEDMQE QNGRLLQQLR 780
EKDDANFKLM SERIKANQIH KLLREEKDEL GEQVLGLKSQ VDAQLLTVQK LEEKERALQG 840
SLGGVEKELT LRSQALELNK RKAVEAAQLA EDLKVQLEHV QTRLREIQPC LAESRAAREK 900
ESFNLKRAQE DISRLRRKLE KQRKVEVYAD ADEILQEEIK EYKARLTCPC CNTRKKDAVL 960
TKCFHVFCFE CVRGRYEARQ RKCPKCNAAF GAHDFHRIYI S 1001 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0033503; C:HULC complex; IDA:UniProtKB.
 GO:0043005; C:neuron projection; ISS:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005886; C:plasma membrane; IDA:HPA.
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:Compara.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0033523; P:histone H2B ubiquitination; IDA:UniProtKB.
 GO:0010390; P:histone monoubiquitination; IDA:UniProtKB.
 GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:UniProtKB. 
Interpro
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
  
SMART
 SM00184; RING 
PROSITE
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS