CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-014162
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase MARCH7 
Protein Synonyms/Alias
 Membrane-associated RING finger protein 7; Membrane-associated RING-CH protein VII; MARCH-VII 
Gene Name
 March7 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Rattus norvegicus (Rat) 
NCBI Taxa ID
 10116 
Lysine Modification
Position
Peptide
Type
References
4****MESKPSRIPRRacetylation[1]
611TCELCKEKLQLNLEDubiquitination[2]
Reference
 [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns.
 Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV.
 Cell Rep. 2012 Aug 30;2(2):419-31. [PMID: 22902405]
 [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 ubiquitin-protein ligase which may specifically enhance the E2 activity of HIP2. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates. 
Sequence Annotation
 ZN_FING 545 615 RING-CH-type.
 MOD_RES 687 687 Phosphothreonine (By similarity).
 MOD_RES 688 688 Phosphoserine (By similarity).  
Keyword
 Complete proteome; Ligase; Metal-binding; Phosphoprotein; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 692 AA 
Protein Sequence
MESKPSRIPR RISVQPSGSL SARMVSGNRG TSLNDSYHSR DSSFRLDSEY QSASASASAS 60
PYQSTWYSES EITQGARSRS QNQQRDHDSK RPKLSCTNCT STSAGRNIGS GLNTLSDSSW 120
RPGQVPRSSS MVLGSFGTDL MRERRDLERR RDSSISSLMD YSHRSGDFTA PAYVQERVPS 180
SYSQGARPKE NAANTLQLNS STNHQLPSEH QTVPSSRDSS RSSFRSHFSP RQSESFRNSS 240
HPAFSYLSSR NETPTISSSE RAGSSQRPFQ ESSDNEGRRT TRRLLSRIAS SMSSTFFSRR 300
SSQDSLNTRS LSSENYISPR TLTSQSRNNG ASSSEVNDGR ASEASQGFRF LRRRWGLSSL 360
SQNHSSEPDA ENFNQESEGR NTGPWLSSSL RNRCTPLFSR RRREGRDESS RISPSDVPPR 420
SHLFRRESNE VVHLEAQGDS LGAAASRPQA SGASGNASAS GSTPDLPQGG RNTGIAGILP 480
GSLFRFAVPP ALGSNLTDNV TITVDIIPSG WSSADGKSEK AKSAPSRDPE KLQKIKESLL 540
LEDSDEEEEG DLCRICQMAA ASSSNLLIEP CKCTGSLQYV HQECMKKWLQ AKINSGSSLE 600
AVTTCELCKE KLQLNLEDFD IHELHRAHAN EQAEYEFISS GLYLVVLLHL CEQSFSDMMG 660
NTIEPSTRVR FINLARTLQA HMEDLETSED EF 692 
Gene Ontology
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway. 
Interpro
 IPR011016; Znf_RING-CH.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF12906; RINGv 
SMART
 SM00744; RINGv 
PROSITE
 PS51292; ZF_RING_CH 
PRINTS