CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016866
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TRIM32 
Protein Synonyms/Alias
 Tripartite motif-containing protein 32 
Gene Name
 Trim32 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
205EELARSRKFFTGSLAubiquitination[1]
361IQQCLFLKKMGAKGSubiquitination[1]
407FNRKGFLKEIRRSPSubiquitination[1]
473CHRSQLSKPWGITALubiquitination[1]
508DRGAGVVKYSCLCSAubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) (By similarity). Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF-alpha. 
Sequence Annotation
 REPEAT 360 403 NHL 1.
 REPEAT 417 460 NHL 2.
 REPEAT 461 501 NHL 3.
 REPEAT 564 607 NHL 4.
 REPEAT 608 648 NHL 5.
 ZN_FING 21 66 RING-type.
 ZN_FING 96 139 B box-type; atypical.  
Keyword
 Coiled coil; Complete proteome; Cytoplasm; Ligase; Metal-binding; Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 655 AA 
Protein Sequence
MAAAAAASHL NLDALREVLE CPICMESFTE EQLRPKLLHC GHTICRQCLE KLLASSINGV 60
RCPFCSKITR ITSLTQLTDN LTVLKIIDTA GLSEAVGLLM CRGCGRRLPR QFCRSCGVVL 120
CEPCREADHQ PPGHCTLPVK EAAEERRRDF GEKLTRLREL TGELQRRKAA LEGVSRDLQA 180
RYKAVLQEYG HEERRIQEEL ARSRKFFTGS LAEVEKSNSQ VVEEQSYLLN IAEVQAVSRC 240
DYFLAKIKQA DVALLEETAD EEEPELTASL PRELTLQDVE LLKVGHVGPL QIGQAVKKPR 300
TVNMEDSWAG EEGAASSASA SVTFREMDMS PEEVAPSPRA SPAKQRSSEA ASGIQQCLFL 360
KKMGAKGSTP GMFNLPVSLY VTSQSEVLVA DRGNYRIQVF NRKGFLKEIR RSPSGIDSFV 420
LSFLGADLPN LTPLSVAMNC HGLIGVTDSY DNSLKVYTMD GHCVACHRSQ LSKPWGITAL 480
PSGQFVVTDV EGGKLWCFTV DRGAGVVKYS CLCSAVRPKF VTCDAEGTVY FTQGLGLNVE 540
NRQNEHHLEG GFSIGSVGPD GQLGRQISHF FSENEDFRCI AGMCVDARGD LIVADSSRKE 600
ILHFPKGGGY SVLIREGLTC PVGIALTPKG QLLVLDCWDH CVKIYSYHLR RYSTP 655 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:BHF-UCL.
 GO:0005634; C:nucleus; IDA:MGI.
 GO:0043621; F:protein self-association; ISS:BHF-UCL.
 GO:0003723; F:RNA binding; IDA:BHF-UCL.
 GO:0043130; F:ubiquitin binding; ISS:BHF-UCL.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:BHF-UCL.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0045444; P:fat cell differentiation; IEP:BHF-UCL.
 GO:0043066; P:negative regulation of apoptotic process; ISS:BHF-UCL.
 GO:0048147; P:negative regulation of fibroblast proliferation; IEP:BHF-UCL.
 GO:0045787; P:positive regulation of cell cycle; ISS:BHF-UCL.
 GO:0030307; P:positive regulation of cell growth; ISS:BHF-UCL.
 GO:0030335; P:positive regulation of cell migration; ISS:BHF-UCL.
 GO:0050769; P:positive regulation of neurogenesis; IDA:BHF-UCL.
 GO:0045666; P:positive regulation of neuron differentiation; IDA:BHF-UCL.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
 GO:0045732; P:positive regulation of protein catabolic process; IDA:BHF-UCL.
 GO:0045862; P:positive regulation of proteolysis; ISS:BHF-UCL.
 GO:0000209; P:protein polyubiquitination; ISS:BHF-UCL.
 GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; ISS:BHF-UCL.
 GO:0034612; P:response to tumor necrosis factor; IDA:BHF-UCL.
 GO:0009411; P:response to UV; IDA:BHF-UCL. 
Interpro
 IPR011042; 6-blade_b-propeller_TolB-like.
 IPR001258; NHL_repeat.
 IPR013017; NHL_repeat_subgr.
 IPR027370; zf-RING_LisH.
 IPR000315; Znf_B-box.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF01436; NHL
 PF13445; zf-RING_LisH 
SMART
 SM00336; BBOX
 SM00184; RING 
PROSITE
 PS51125; NHL
 PS50119; ZF_BBOX
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS