CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-011980
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TRIM32 
Protein Synonyms/Alias
 72 kDa Tat-interacting protein; Tripartite motif-containing protein 32; Zinc finger protein HT2A 
Gene Name
 TRIM32 
Gene Synonyms/Alias
 HT2A 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
50ICRQCLEKLLASSINubiquitination[1, 2]
66VRCPFCSKITRITSLubiquitination[1]
139GHCTLPVKEAAEERRubiquitination[1, 2]
152RRRDFGEKLTRLRELubiquitination[1]
175AALEGVSKDLQARYKubiquitination[1, 2, 3, 4, 5, 6, 7]
182KDLQARYKAVLQEYGubiquitination[1, 2, 4, 6]
204DELARSRKFFTGSLAubiquitination[1, 2, 3, 4, 5, 6, 7]
215GSLAEVEKSNSQVVEubiquitination[4, 6, 8]
245RCDYFLAKIKQADVAubiquitination[1]
247DYFLAKIKQADVALLubiquitination[1, 4, 6]
282LQDVELLKVGHVGPLubiquitination[2, 4, 6, 8]
296LQIGQAVKKPRTVNVubiquitination[1]
297QIGQAVKKPRTVNVEubiquitination[1]
359IQQCLFLKKMGAKGSubiquitination[1, 8]
360QQCLFLKKMGAKGSTubiquitination[1]
401RIQVFTRKGFLKEIRubiquitination[1]
405FTRKGFLKEIRRSPSubiquitination[1, 2, 3, 6, 7, 8]
471CHRSQLSKPWGITALubiquitination[1, 3, 4, 6, 7]
506DRGSGVVKYSCLCSAubiquitination[1]
604KEILHFPKGGGYSVLubiquitination[2]
627VGIALTPKGQLLVLDubiquitination[1, 2, 8]
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] 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]
 [3] 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]
 [4] 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]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [6] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [8] 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] 
Functional Description
 Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo. 
Sequence Annotation
 REPEAT 358 401 NHL 1.
 REPEAT 415 458 NHL 2.
 REPEAT 459 499 NHL 3.
 REPEAT 562 605 NHL 4.
 REPEAT 606 646 NHL 5.
 ZN_FING 20 65 RING-type.
 ZN_FING 103 133 B box-type.
 MOD_RES 2 2 N-acetylalanine.  
Keyword
 3D-structure; Acetylation; Bardet-Biedl syndrome; Ciliopathy; Coiled coil; Complete proteome; Cytoplasm; Direct protein sequencing; Disease mutation; Ligase; Limb-girdle muscular dystrophy; Mental retardation; Metal-binding; Obesity; Polymorphism; Reference proteome; Repeat; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 653 AA 
Protein Sequence
MAAAAASHLN LDALREVLEC PICMESFTEE QLRPKLLHCG HTICRQCLEK LLASSINGVR 60
CPFCSKITRI TSLTQLTDNL TVLKIIDTAG LSEAVGLLMC RSCGRRLPRQ FCRSCGLVLC 120
EPCREADHQP PGHCTLPVKE AAEERRRDFG EKLTRLRELM GELQRRKAAL EGVSKDLQAR 180
YKAVLQEYGH EERRVQDELA RSRKFFTGSL AEVEKSNSQV VEEQSYLLNI AEVQAVSRCD 240
YFLAKIKQAD VALLEETADE EEPELTASLP RELTLQDVEL LKVGHVGPLQ IGQAVKKPRT 300
VNVEDSWAME ATASAASTSV TFREMDMSPE EVVASPRASP AKQRGPEAAS NIQQCLFLKK 360
MGAKGSTPGM FNLPVSLYVT SQGEVLVADR GNYRIQVFTR KGFLKEIRRS PSGIDSFVLS 420
FLGADLPNLT PLSVAMNCQG LIGVTDSYDN SLKVYTLDGH CVACHRSQLS KPWGITALPS 480
GQFVVTDVEG GKLWCFTVDR GSGVVKYSCL CSAVRPKFVT CDAEGTVYFT QGLGLNLENR 540
QNEHHLEGGF SIGSVGPDGQ LGRQISHFFS ENEDFRCIAG MCVDARGDLI VADSSRKEIL 600
HFPKGGGYSV LIREGLTCPV GIALTPKGQL LVLDCWDHCI KIYSYHLRRY STP 653 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:UniProtKB.
 GO:0005634; C:nucleus; ISS:BHF-UCL.
 GO:0005863; C:striated muscle myosin thick filament; IEA:Compara.
 GO:0017022; F:myosin binding; ISS:BHF-UCL.
 GO:0043621; F:protein self-association; IDA:UniProtKB.
 GO:0003723; F:RNA binding; ISS:BHF-UCL.
 GO:0030957; F:Tat protein binding; TAS:BHF-UCL.
 GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
 GO:0031369; F:translation initiation factor binding; ISS:BHF-UCL.
 GO:0043130; F:ubiquitin binding; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0045444; P:fat cell differentiation; ISS:BHF-UCL.
 GO:0045087; P:innate immune response; TAS:BHF-UCL.
 GO:0043066; P:negative regulation of apoptotic process; IDA:BHF-UCL.
 GO:0048147; P:negative regulation of fibroblast proliferation; ISS:BHF-UCL.
 GO:0045787; P:positive regulation of cell cycle; IDA:BHF-UCL.
 GO:0030307; P:positive regulation of cell growth; IDA:BHF-UCL.
 GO:0030335; P:positive regulation of cell migration; IDA:BHF-UCL.
 GO:0050769; P:positive regulation of neurogenesis; ISS:BHF-UCL.
 GO:0045666; P:positive regulation of neuron differentiation; ISS:BHF-UCL.
 GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; ISS:BHF-UCL.
 GO:0045732; P:positive regulation of protein catabolic process; ISS:BHF-UCL.
 GO:0045862; P:positive regulation of proteolysis; IDA:BHF-UCL.
 GO:0000209; P:protein polyubiquitination; IDA:BHF-UCL.
 GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
 GO:0034612; P:response to tumor necrosis factor; ISS:BHF-UCL.
 GO:0009411; P:response to UV; ISS: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