CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015321
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tripartite motif-containing protein 65 
Protein Synonyms/Alias
  
Gene Name
 TRIM65 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
206LRSIEVAKTQALAQAubiquitination[1, 2, 3, 4]
325TVCPLRRKLWQNYRNubiquitination[1, 4]
Reference
 [1] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] 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 313 506 B30.2/SPRY.
 ZN_FING 12 51 RING-type.
 ZN_FING 90 137 B box-type.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 Acetylation; Coiled coil; Complete proteome; Metal-binding; Polymorphism; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 517 AA 
Protein Sequence
MAAQLLEEKL TCAICLGLYQ DPVTLPCGHN FCGACIRDWW DRCGKACPEC REPFPDGAEL 60
RRNVALSGVL EVVRAGPARD PGPDPGPGPD PAARCPRHGR PLELFCRTEG RCVCSVCTVR 120
ECRLHERALL DAERLKREAQ LRASLEVTQQ QATQAEGQLL ELRKQSSQIQ NSACILASWV 180
SGKFSSLLQA LEIQHTTALR SIEVAKTQAL AQARDEEQRL RVHLEAVARH GCRIRELLEQ 240
VDEQTFLQES QLLQPPGPLG PLTPLQWDED QQLGDLKQLL SRLCGLLLEE GSHPGAPAKP 300
VDLAPVEAPG PLAPVPSTVC PLRRKLWQNY RNLTFDPVSA NRHFYLSRQD QQVKHCRQSR 360
GPGGPGSFEL WQVQCAQSFQ AGHHYWEVRA SDHSVTLGVS YPQLPRCRLG PHTDNIGRGP 420
CSWGLCVQED SLQAWHNGEA QRLPGVSGRL LGMDLDLASG CLTFYSLEPQ TQPLYTFHAL 480
FNQPLTPVFW LLEGRTLTLC HQPGAVFPLG PQEEVLS 517 
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.
 IPR003877; SPRY_rcpt.
 IPR000315; Znf_B-box.
 IPR018957; Znf_C3HC4_RING-type.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00622; SPRY
 PF00643; zf-B_box
 PF00097; zf-C3HC4 
SMART
 SM00184; RING 
PROSITE
 PS50188; B302_SPRY
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR01407; BUTYPHLNCDUF.