CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020239
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tripartite motif-containing protein 62 
Protein Synonyms/Alias
  
Gene Name
 TRIM62 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67PALAPSLKLANIVERubiquitination[1, 2, 3]
100CQAHDKVKLFCLTDRubiquitination[3]
161TEALQLLKRQLAETKubiquitination[1]
194RLLRERQKAMLEELEubiquitination[3]
214TLTDIEQKVQRYSQQubiquitination[1, 3]
224RYSQQLRKVQEGAQIubiquitination[3]
258LSERLKGKIHETNLTubiquitination[1]
273YEDFPTSKYTGPLQYubiquitination[3]
375AHEAASRKGSIQIQPubiquitination[3]
463GQSHANGKNVQPLRIubiquitination[3]
Reference
 [1] 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]
 [2] 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]
 [3] 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
Functional Description
  
Sequence Annotation
 DOMAIN 277 475 B30.2/SPRY.
 ZN_FING 11 54 RING-type.
 ZN_FING 88 128 B box-type.  
Keyword
 Coiled coil; Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 475 AA 
Protein Sequence
MACSLKDELL CSICLSIYQD PVSLGCEHYF CRRCITEHWV RQEAQGARDC PECRRTFAEP 60
ALAPSLKLAN IVERYSSFPL DAILNARRAA RPCQAHDKVK LFCLTDRALL CFFCDEPALH 120
EQHQVTGIDD AFDELQRELK DQLQALQDSE REHTEALQLL KRQLAETKSS TKSLRTTIGE 180
AFERLHRLLR ERQKAMLEEL EADTARTLTD IEQKVQRYSQ QLRKVQEGAQ ILQERLAETD 240
RHTFLAGVAS LSERLKGKIH ETNLTYEDFP TSKYTGPLQY TIWKSLFQDI HPVPAALTLD 300
PGTAHQRLIL SDDCTIVAYG NLHPQPLQDS PKRFDVEVSV LGSEAFSSGV HYWEVVVAEK 360
TQWVIGLAHE AASRKGSIQI QPSRGFYCIV MHDGNQYSAC TEPWTRLNVR DKLDKVGVFL 420
DYDQGLLIFY NADDMSWLYT FREKFPGKLC SYFSPGQSHA NGKNVQPLRI NTVRI 475 
Gene Ontology
 GO:0005622; C:intracellular; IEA:InterPro.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR003879; Butyrophylin.
 IPR008985; ConA-like_lec_gl_sf.
 IPR006574; PRY.
 IPR003877; SPRY_rcpt.
 IPR000315; Znf_B-box.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00622; SPRY
 PF00643; zf-B_box 
SMART
 SM00589; PRY
 SM00184; RING 
PROSITE
 PS50188; B302_SPRY
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR01407; BUTYPHLNCDUF.