CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-042426
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 E3 ubiquitin-protein ligase TRIM33 
Protein Synonyms/Alias
  
Gene Name
 TRIM33 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
42DCQLLEHKEHRYQFLubiquitination[1]
57EEAFQNQKGAIENLLubiquitination[2]
66AIENLLAKLLEKKNYubiquitination[1]
71LAKLLEKKNYVHFAAubiquitination[1]
113LINEINKKGKSLLQQubiquitination[1]
115NEINKKGKSLLQQLEubiquitination[1]
126QQLENVTKERQMKLLubiquitination[1]
131VTKERQMKLLQQQNDubiquitination[1, 3]
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] 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] 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] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 888 AA 
Protein Sequence
XSVGASGQRP VFCPVHKQEQ LKLFCETCDR LTCRDCQLLE HKEHRYQFLE EAFQNQKGAI 60
ENLLAKLLEK KNYVHFAATQ VQNRIKEVNE TNKRVEQEIK VAIFTLINEI NKKGKSLLQQ 120
LENVTKERQM KLLQQQNDIT GLSRQVKHVM NFTNWAIASG SSTALLYSKR LITFQLRHIL 180
KARCDPVPAA NGAIRFHCDP TFWAKNVVNL GNLVIESKPA PGYTPNVVVG QVPPGTNHIS 240
KTPGQINLAQ LRLQHMQQQV YAQKHQQLQQ MRMQQPPAPV PTTTTTTQQH PRQAAPQMLQ 300
QQPPRLISVQ TMQRGNMNCG AFQAHQMRLA QNAARIPGIP RHSGPQYSMM QPHLQRQHSN 360
PGHAGPFPVV SVHNTTINPT SPTTATMANA NRGPTSPSVT AIELIPSVTN PENLPSLPDI 420
PPIQANVVPM MHSWYEFGAR EKTQDQNVLE DAGSSSLDNL LSRYISGSHL PPQPTSTMNP 480
SPGPSALSPG SSGLSNSHTP VRPPSTSSTG SRGSCGSSGR TAEKTSLSFK SDQVKVKQEP 540
GTEDEICSFS GGVKQEKTED GRRSACMLSS PESSLTPPLS TNLHLESELD ALASLENHVK 600
IEPADMNESC KQSGLSSLVN GKSPIRSLMH RSARIGGDGN NKDDDPNEDW CAVCQNGGDL 660
LCCEKCPKVF HLTCHVPTLL SFPSGDWICT FCRDIGKPEV EYDCDNLQHS KKGKTAQGLS 720
PVDQRKCERL LLYLYCHELS IEFQEPVPAS IPNYYKIIKK PMDLSTVKKK LQKKHSQHYQ 780
IPDDFVADVR LIFKNCERFN EMMKVVQVYA DTQEINLKAD SEVAQAGKAV ALYFEDKLTE 840
IYSDRTFAPL PEFEQEEDDG EVTEDSDEDF IQPRRKRLKS DERPVHIK 888 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0008270; F:zinc ion binding; IEA:InterPro. 
Interpro
 IPR003649; Bbox_C.
 IPR001487; Bromodomain.
 IPR019786; Zinc_finger_PHD-type_CS.
 IPR000315; Znf_B-box.
 IPR011011; Znf_FYVE_PHD.
 IPR001965; Znf_PHD.
 IPR019787; Znf_PHD-finger.
 IPR013083; Znf_RING/FYVE/PHD. 
Pfam
 PF00439; Bromodomain
 PF00628; PHD
 PF00643; zf-B_box 
SMART
 SM00502; BBC
 SM00336; BBOX
 SM00297; BROMO
 SM00249; PHD 
PROSITE
 PS50014; BROMODOMAIN_2
 PS50119; ZF_BBOX
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS