CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-032136
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase MARCH7 
Protein Synonyms/Alias
 cDNA FLJ52435, highly similar to Homo sapiens membrane-associated ring finger (C3HC4) 7 (MARCH7), mRNA 
Gene Name
 MARCH7 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
55DHDSKRPKLSCTNCTubiquitination[1]
498PERLQKIKESLLLEDubiquitination[1]
548VHQDCMKKWLQAKINubiquitination[1]
553MKKWLQAKINSGSSLubiquitination[1]
570VTTCELCKEKLELNLubiquitination[1, 2, 3]
572TCELCKEKLELNLEDubiquitination[1, 4]
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]
 [3] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 666 AA 
Protein Sequence
MIGNYDHLMS LVTSTSASAS ASPFQSAWYS ESEITQGARS RSQNQQRDHD SKRPKLSCTN 60
CTTSAGRNVG NGLNTLSDSS WRHSQVPRSS SMVLGSFGTD LMRERRDLER RTDSSISNLM 120
DYSHRSGDFT TSSYVQDRVP SYSQGARPKE NSMSTLQLNT SSTNHQLPSE HQTILSSRDS 180
RNSLRSNFSS RESESSRSNT QPGFSYSSSR DEAPIISNSE RVVSSQRPFQ ESSDNEGRRT 240
TRRLLSRIAS SMSSTFFSRR SSQDSLNTRS LNSENSYVSP RILTASQSRS NVPSASEVPD 300
NRASEASQGF RFLRRRWGLS SLSHNHSSES DSENFNQESE GRNTGPWLSS SLRNRCTPLF 360
SRRRREGRDE SSRIPTSDTS SRSHIFRRES NEVVHLEAQN DPLGAAANRP QASAASSSAT 420
TGGSTSDSAQ GGRNTGISGI LPGSLFRFAV PPALGSNLTD NVMITVDIIP SGWNSADGKS 480
DKTKSAPSRD PERLQKIKES LLLEDSEEEE GDLCRICQMA AASSSNLLIE PCKCTGSLQY 540
VHQDCMKKWL QAKINSGSSL EAVTTCELCK EKLELNLEDF DIHELHRAHA NEQAEYEFIS 600
SGLYLVVLLH LCEQSFSDMM GNTNEPSTRV RFINLARTLQ AHMEDLETSE DDSEEDGDHN 660
RTFDIA 666 
Gene Ontology
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR011016; Znf_RING-CH.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF12906; RINGv 
SMART
 SM00744; RINGv 
PROSITE
 PS51292; ZF_RING_CH 
PRINTS