CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-020373
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Tripartite motif-containing protein 34 
Protein Synonyms/Alias
 Interferon-responsive finger protein 1; RING finger protein 21 
Gene Name
 TRIM34 
Gene Synonyms/Alias
 IFP1; RNF21 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
44ACITVSNKEAVTSMGubiquitination[1]
82ANIVERLKEVKLSPDubiquitination[1]
103LCDHHGEKLLLFCKEubiquitination[1]
109EKLLLFCKEDRKVICubiquitination[1]
173REEKTSWKYQVQTERubiquitination[1, 2]
215EEKKTLDKFAEAEDEubiquitination[1]
227EDELVQQKQLVRELIubiquitination[1, 3]
358WEVDVSKKTAWILGVubiquitination[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] 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]
 [3] 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
  
Sequence Annotation
 DOMAIN 283 488 B30.2/SPRY.
 ZN_FING 15 60 RING-type.
 ZN_FING 92 134 B box-type.  
Keyword
 3D-structure; Alternative splicing; Coiled coil; Complete proteome; Metal-binding; Polymorphism; Reference proteome; Repeat; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 488 AA 
Protein Sequence
MASKILLNVQ EEVTCPICLE LLTEPLSLDC GHSLCRACIT VSNKEAVTSM GGKSSCPVCG 60
ISYSFEHLQA NQHLANIVER LKEVKLSPDN GKKRDLCDHH GEKLLLFCKE DRKVICWLCE 120
RSQEHRGHHT VLTEEVFKEC QEKLQAVLKR LKKEEEEAEK LEADIREEKT SWKYQVQTER 180
QRIQTEFDQL RSILNNEEQR ELQRLEEEEK KTLDKFAEAE DELVQQKQLV RELISDVECR 240
SQWSTMELLQ DMSGIMKWSE IWRLKKPKMV SKKLKTVFHA PDLSRMLQMF RELTAVRCYW 300
VDVTLNSVNL NLNLVLSEDQ RQVISVPIWP FQCYNYGVLG SQYFSSGKHY WEVDVSKKTA 360
WILGVYCRTY SRHMKYVVRR CANRQNLYTK YRPLFGYWVI GLQNKCKYGV FEESLSSDPE 420
VLTLSMAVPP CRVGVFLDYE AGIVSFFNVT SHGSLIYKFS KCCFSQPVYP YFNPWNCPAP 480
MTLCPPSS 488 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0070206; P:protein trimerization; IDA:UniProtKB. 
Interpro
 IPR001870; B30.2/SPRY.
 IPR003879; Butyrophylin.
 IPR008985; ConA-like_lec_gl_sf.
 IPR018355; SPla/RYanodine_receptor_subgr.
 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
 SM00336; BBOX
 SM00184; RING
 SM00449; SPRY 
PROSITE
 PS50188; B302_SPRY
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR01407; BUTYPHLNCDUF.