CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023281
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 E3 ubiquitin-protein ligase TRIM33 
Protein Synonyms/Alias
 Ectodermin homolog; RET-fused gene 7 protein; Protein Rfg7; Transcription intermediary factor 1-gamma; TIF1-gamma; Tripartite motif-containing protein 33 
Gene Name
 TRIM33 
Gene Synonyms/Alias
 KIAA1113; RFG7; TIF1G 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
252HQRVKFTKDHLIRKKacetylation[1]
305DCQLLEHKEHRYQFLubiquitination[2]
329AIENLLAKLLEKKNYubiquitination[2]
334LAKLLEKKNYVHFAAubiquitination[2]
376LINEINKKGKSLLQQubiquitination[2]
378NEINKKGKSLLQQLEubiquitination[2]
389QQLENVTKERQMKLLubiquitination[2]
394VTKERQMKLLQQQNDubiquitination[2, 3, 4]
763SSGRTAEKTSLSFKSacetylation[1]
769EKTSLSFKSDQVKVKacetylation[1]
776KSDQVKVKQEPGTEDsumoylation[5]
951DNLQHSKKGKTAQGLacetylation[1]
951DNLQHSKKGKTAQGLubiquitination[2]
953LQHSKKGKTAQGLSPacetylation[1]
1033ADVRLIFKNCERFNEubiquitination[2]
1057DTQEINLKADSEVAQubiquitination[6]
Reference
 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] 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]
 [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] 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]
 [5] Site-specific identification of SUMO-2 targets in cells reveals an inverted SUMOylation motif and a hydrophobic cluster SUMOylation motif.
 Matic I, Schimmel J, Hendriks IA, van Santen MA, van de Rijke F, van Dam H, Gnad F, Mann M, Vertegaal AC.
 Mol Cell. 2010 Aug 27;39(4):641-52. [PMID: 20797634]
 [6] 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
 Acts as an E3 ubiquitin-protein ligase. Promotes SMAD4 ubiquitination, nuclear exclusion and degradation via the ubiquitin proteasome pathway. According to PubMed:16751102, does not promote a decrease in the level of endogenous SMAD4. May act as a transcriptional repressor. Inhibits the transcriptional response to TGF-beta/BMP signaling cascade. Plays a role in the control of cell proliferation. Its association with SMAD2 and SMAD3 stimulates erythroid differentiation of hematopoietic stem/progenitor (By similarity). Monoubiquitinates SMAD4 and acts as an inhibitor of SMAD4-dependent TGF-beta/BMP signaling cascade (Monoubiquitination of SMAD4 hampers its ability to form a stable complex with activated SMAD2/3 resulting in inhibition of TGF- beta/BMP signaling cascade). 
Sequence Annotation
 DOMAIN 974 1046 Bromo.
 ZN_FING 125 154 RING-type.
 ZN_FING 212 259 B box-type 1.
 ZN_FING 271 312 B box-type 2.
 ZN_FING 887 934 PHD-type.
 REGION 1 147 Necessary for E3 ubiquitin-protein ligase
 REGION 299 401 Necessary for oligomerization.
 MOD_RES 763 763 N6-acetyllysine.
 MOD_RES 769 769 N6-acetyllysine.
 MOD_RES 862 862 Phosphoserine.
 MOD_RES 953 953 N6-acetyllysine.
 MOD_RES 1102 1102 Phosphothreonine.
 MOD_RES 1105 1105 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Bromodomain; Chromosomal rearrangement; Coiled coil; Complete proteome; DNA-binding; Ligase; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1127 AA 
Protein Sequence
MAENKGGGEA ESGGGGSGSA PVTAGAAGPA AQEAEPPLTA VLVEEEEEEG GRAGAEGGAA 60
GPDDGGVAAA SSGSAQAASS PAASVGTGVA GGAVSTPAPA PASAPAPGPS AGPPPGPPAS 120
LLDTCAVCQQ SLQSRREAEP KLLPCLHSFC LRCLPEPERQ LSVPIPGGSN GDIQQVGVIR 180
CPVCRQECRQ IDLVDNYFVK DTSEAPSSSD EKSEQVCTSC EDNASAVGFC VECGEWLCKT 240
CIEAHQRVKF TKDHLIRKKE DVSESVGASG QRPVFCPVHK QEQLKLFCET CDRLTCRDCQ 300
LLEHKEHRYQ FLEEAFQNQK GAIENLLAKL LEKKNYVHFA ATQVQNRIKE VNETNKRVEQ 360
EIKVAIFTLI NEINKKGKSL LQQLENVTKE RQMKLLQQQN DITGLSRQVK HVMNFTNWAI 420
ASGSSTALLY SKRLITFQLR HILKARCDPV PAANGAIRFH CDPTFWAKNV VNLGNLVIES 480
KPAPGYTPNV VVGQVPPGTN HISKTPGQIN LAQLRLQHMQ QQVYAQKHQQ LQQMRMQQPP 540
APVPTTTTTT QQHPRQAAPQ MLQQQPPRLI SVQTMQRGNM NCGAFQAHQM RLAQNAARIP 600
GIPRHSGPQY SMMQPHLQRQ HSNPGHAGPF PVVSVHNTTI NPTSPTTATM ANANRGPTSP 660
SVTAIELIPS VTNPENLPSL PDIPPIQLED AGSSSLDNLL SRYISGSHLP PQPTSTMNPS 720
PGPSALSPGS SGLSNSHTPV RPPSTSSTGS RGSCGSSGRT AEKTSLSFKS DQVKVKQEPG 780
TEDEICSFSG GVKQEKTEDG RRSACMLSSP ESSLTPPLST NLHLESELDA LASLENHVKI 840
EPADMNESCK QSGLSSLVNG KSPIRSLMHR SARIGGDGNN KDDDPNEDWC AVCQNGGDLL 900
CCEKCPKVFH LTCHVPTLLS FPSGDWICTF CRDIGKPEVE YDCDNLQHSK KGKTAQGLSP 960
VDQRKCERLL LYLYCHELSI EFQEPVPASI PNYYKIIKKP MDLSTVKKKL QKKHSQHYQI 1020
PDDFVADVRL IFKNCERFNE MMKVVQVYAD TQEINLKADS EVAQAGKAVA LYFEDKLTEI 1080
YSDRTFAPLP EFEQEEDDGE VTEDSDEDFI QPRRKRLKSD ERPVHIK 1127 
Gene Ontology
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0004842; F:ubiquitin-protein ligase activity; TAS:Reactome.
 GO:0008270; F:zinc ion binding; NAS:UniProtKB.
 GO:0030514; P:negative regulation of BMP signaling pathway; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:Reactome.
 GO:0017015; P:regulation of transforming growth factor beta receptor signaling pathway; IDA:UniProtKB.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
 GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:Reactome. 
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.
 IPR001841; Znf_RING.
 IPR013083; Znf_RING/FYVE/PHD.
 IPR017907; Znf_RING_CS. 
Pfam
 PF00439; Bromodomain
 PF00628; PHD
 PF00643; zf-B_box
 PF13639; zf-RING_2 
SMART
 SM00502; BBC
 SM00336; BBOX
 SM00297; BROMO
 SM00249; PHD
 SM00184; RING 
PROSITE
 PS00633; BROMODOMAIN_1
 PS50014; BROMODOMAIN_2
 PS50119; ZF_BBOX
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2
 PS00518; ZF_RING_1
 PS50089; ZF_RING_2 
PRINTS
 PR00503; BROMODOMAIN.