CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016593
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative E3 ubiquitin-protein ligase UBR7 
Protein Synonyms/Alias
 N-recognin-7 
Gene Name
 Ubr7 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
384NDLKTELKDYLKRFAubiquitination[1]
Reference
 [1] 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 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). 
Sequence Annotation
 ZN_FING 44 116 UBR-type.
 ZN_FING 132 188 PHD-type; atypical.  
Keyword
 Complete proteome; Ligase; Metal-binding; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 425 AA 
Protein Sequence
MAGAESPTEC QAELEPVVSL VDVLEEDEEL ENEACAVLGG SDSEKCSYSQ GSVGRQALYA 60
CSTCTPEGEE PAGICLACSY ECHGSHKLFE LYTKRNFRCD CGNSKFKNLE CKLFPDKSKV 120
NSCNKYNDNF FGLYCVCKRP YPDPEDEVPD EMIQCVVCED WFHGRHLGAI PPESGDFQEM 180
VCQACMRRCS FLWAYAAQLA VTRISAEDDG LLPNATGMGD EDVSKPENGA PQDNGLKEDA 240
PEHGRDSVNE VKAEQKNEPC SSSSSESDLQ TVFKKENIKT EPQSSCRLQE LQAKQFVKKD 300
AATYWPLNWR SKLCTCQDCM KMYGELDVLF LTDECDTVLA YENKGKNDQA TDRRDPLMDT 360
LSSMNRVQQV ELICEYNDLK TELKDYLKRF ADEGTVVKRE DIQQFFEEFQ SKKRRRVDGL 420
QYYCS 425 
Gene Ontology
 GO:0004842; F:ubiquitin-protein ligase activity; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR011011; Znf_FYVE_PHD.
 IPR003126; Znf_N-recognin.
 IPR001965; Znf_PHD.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF02207; zf-UBR 
SMART
 SM00249; PHD 
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS51157; ZF_UBR 
PRINTS