| Tag | Content |
|---|
| CPLM ID | CPLM-015826 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | E3 ubiquitin-protein ligase UHRF2 |
Protein Synonyms/Alias | NIRF; Np95-like ring finger protein; Nuclear protein 97; Nuclear zinc finger protein Np97; Ubiquitin-like PHD and RING finger domain-containing protein 2; Ubiquitin-like-containing PHD and RING finger domains protein 2 |
Gene Name | Uhrf2 |
Gene Synonyms/Alias | Nirf |
Created Date | July 27, 2013 |
Organism | Mus musculus (Mouse) |
NCBI Taxa ID | 10090 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 438 | MACVGRTKECTIVPS | acetylation | [1] | | 549 | CDAPLDDKIGAESRN | ubiquitination | [2] |
|
Reference | [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways. Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y. Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [ PMID: 22826441] [2] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues. Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C. Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [ PMID: 22790023] |
Functional Description | E3 SUMO-, but not ubiquitin-, protein ligase for ZNF131 (By similarity). E3 ubiquitin-protein ligase that is an intermolecular hub protein in the cell cycle network. Ubiquitinates cyclins, CCND1 and CCNE1, in an apparently phosphorylation-independent manner and induces G1 arrest. Also ubiquitinates PCNP leading to its degradation by the proteasome. Through cooperative DNA and histone binding, may contribute to a tighter epigenetic control of gene expression in differentiated cells. |
Sequence Annotation | DOMAIN 1 78 Ubiquitin-like.
DOMAIN 449 613 YDG.
ZN_FING 340 396 PHD-type.
ZN_FING 734 773 RING-type.
REGION 118 312 Required for interaction with histone H3.
REGION 195 289 Interaction with PCNP (By similarity).
REGION 415 645 Methyl-CpG binding and interaction with
MOD_RES 668 668 Phosphoserine.
DISULFID 705 705 Interchain (By similarity). |
Keyword | Alternative splicing; Cell cycle; Complete proteome; Disulfide bond; DNA-binding; Ligase; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 803 AA |
Protein Sequence | MWIQVRTIDG SQTRTIEDVS RKATIEELRE RVWALFDVRP ECQRLFYRGK QLENGYTLFD 60
YDVGLNDIIQ LLVRPDSSLP STSKQNDAQV KPSSHNPPKV KKTARGGSSS QPSTSARTCL 120
IDPGFGLYKV NELVDARDVG LGAWFEAHIH SVTRASDGHS RGKTPLKNGS SYKRTNGNVN 180
HNSKENTNKL DNVPSTSNSD SVAADEDVIY HIEYDEYPES GILEMNVKDL RPRARTILKW 240
NELNVGDVVM VNYNVENPGK RGFWYDAEIT TLKTISRTKK EVRVKVFLGG SEGTLNDCRV 300
MSVDEIFKIE KPGAHPISFA DGKFLRKNDP ECDLCGGDPD KTCHMCSCHK CGEKRDPNMQ 360
LLCDECNMAY HIYCLSPPLD KVPEEEYWYC PSCKTDSSEV VKAGERLKLS KKKAKMPSAS 420
TESRRDWGRG MACVGRTKEC TIVPSNHYGP IPGIPVGSTW RFRVQVSEAG VHRPHVGGIH 480
GRSNDGAYSL VLAGGFEDEV DRGDEFTYTG SGGKNLAGNK RIGAPSADQT LTNMNRALAL 540
NCDAPLDDKI GAESRNWRAG KPVRVIRSFK GRKISKYAPE EGNRYDGIYK VVKYWPEISS 600
SHGFLVWRYL LRRDDVEPAP WTSEGIERSR RLCLRLQYPA GYPSEKEGKK TKGQSKKQGS 660
EATKRPASDD ECPGDSKVLK ASDSTDAVEA FQLTPQQQRL IREDCQNQKL WDEVLASLVE 720
GPNFLKKLEQ SFMCVCCQEL VYQPVTTECF HNVCKDCLQR SFKAQVFSCP ACRHDLGQNY 780
VMVLNETLQT LLDLFFPGYS KGR 803 |
Gene Ontology | GO:0005720; C:nuclear heterochromatin; IDA:UniProtKB. GO:0003677; F:DNA binding; IEA:UniProtKB-KW. GO:0042393; F:histone binding; IDA:UniProtKB. GO:0004842; F:ubiquitin-protein ligase activity; ISS:HGNC. GO:0008270; F:zinc ion binding; IEA:InterPro. GO:0007049; P:cell cycle; IEA:UniProtKB-KW. GO:0030154; P:cell differentiation; ISS:HGNC. GO:0008283; P:cell proliferation; ISS:HGNC. GO:0071158; P:positive regulation of cell cycle arrest; ISS:UniProtKB. GO:0051865; P:protein autoubiquitination; ISS:HGNC. GO:0006511; P:ubiquitin-dependent protein catabolic process; ISS:HGNC. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |