CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021536
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase MARCH7 
Protein Synonyms/Alias
 Axotrophin; Membrane-associated RING finger protein 7; Membrane-associated RING-CH protein VII; MARCH-VII; RING finger protein 177 
Gene Name
 MARCH7 
Gene Synonyms/Alias
 AXOT; RNF177 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
4****MESKPSRIPRRubiquitination[1]
93DHDSKRPKLSCTNCTubiquitination[1]
536PERLQKIKESLLLEDubiquitination[1]
586VHQDCMKKWLQAKINubiquitination[1]
591MKKWLQAKINSGSSLubiquitination[1]
608VTTCELCKEKLELNLubiquitination[1, 2]
610TCELCKEKLELNLEDubiquitination[1]
Reference
 [1] 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]
 [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] 
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 544 614 RING-CH-type.
 MOD_RES 686 686 Phosphothreonine.
 MOD_RES 687 687 Phosphoserine.
 MOD_RES 691 691 Phosphoserine.  
Keyword
 Complete proteome; Ligase; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 704 AA 
Protein Sequence
MESKPSRIPR RISVQPSSSL SARMMSGSRG SSLNDTYHSR DSSFRLDSEY QSTSASASAS 60
PFQSAWYSES EITQGARSRS QNQQRDHDSK RPKLSCTNCT TSAGRNVGNG LNTLSDSSWR 120
HSQVPRSSSM VLGSFGTDLM RERRDLERRT DSSISNLMDY SHRSGDFTTS SYVQDRVPSY 180
SQGARPKENS MSTLQLNTSS TNHQLPSEHQ TILSSRDSRN SLRSNFSSRE SESSRSNTQP 240
GFSYSSSRDE APIISNSERV VSSQRPFQES SDNEGRRTTR RLLSRIASSM SSTFFSRRSS 300
QDSLNTRSLN SENSYVSPRI LTASQSRSNV PSASEVPDNR ASEASQGFRF LRRRWGLSSL 360
SHNHSSESDS ENFNQESEGR NTGPWLSSSL RNRCTPLFSR RRREGRDESS RIPTSDTSSR 420
SHIFRRESNE VVHLEAQNDP LGAAANRPQA SAASSSATTG GSTSDSAQGG RNTGISGILP 480
GSLFRFAVPP ALGSNLTDNV MITVDIIPSG WNSADGKSDK TKSAPSRDPE RLQKIKESLL 540
LEDSEEEEGD LCRICQMAAA SSSNLLIEPC KCTGSLQYVH QDCMKKWLQA KINSGSSLEA 600
VTTCELCKEK LELNLEDFDI HELHRAHANE QAEYEFISSG LYLVVLLHLC EQSFSDMMGN 660
TNEPSTRVRF INLARTLQAH MEDLETSEDD SEEDGDHNRT FDIA 704 
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