CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-038718
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
776SSGRTAEKSAHSFKSacetylation[1, 2, 3]
782EKSAHSFKSDQVKVKacetylation[1, 3]
789KSDQVKVKQEPGTEEacetylation[1]
806CSFSGAVKQEKTEDGacetylation[1, 3]
964DNMQHSKKGKTAQGLacetylation[1, 3]
966MQHSKKGKTAQGLSPacetylation[1, 3, 4]
Reference
 [1] Quantitative acetylome analysis reveals the roles of SIRT1 in regulating diverse substrates and cellular pathways.
 Chen Y, Zhao W, Yang JS, Cheng Z, Luo H, Lu Z, Tan M, Gu W, Zhao Y.
 Mol Cell Proteomics. 2012 Oct;11(10):1048-62. [PMID: 22826441]
 [2] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [3] SIRT5-Mediated Lysine Desuccinylation Impacts Diverse Metabolic Pathways.
 Park J, Chen Y, Tishkoff DX, Peng C, Tan M, Dai L, Xie Z, Zhang Y, Zwaans BM, Skinner ME, Lombard DB, Zhao Y.
 Mol Cell. 2013 Jun 27;50(6):919-30. [PMID: 23806337]
 [4] Quantitative assessment of the impact of the gut microbiota on lysine epsilon-acetylation of host proteins using gnotobiotic mice.
 Simon GM, Cheng J, Gordon JI.
 Proc Natl Acad Sci U S A. 2012 Jul 10;109(28):11133-8. [PMID: 22733758
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Metal-binding; Reference proteome; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1123 AA 
Protein Sequence
MAENKGGGEA ESGGGGSGSA PVTAGAAGPT AQEAEPPLAA VLVEEEEEEG GRAGAEGGAA 60
GPDDGGVAAA SSSSAPAASV PAASVGSAVP GGAASTPAPA AAPAPAPAPA PAPAPAPAPA 120
PGSSSGPPLG PPASLLDTCA VCQQSLQSRR EAEPKLLPCL HSFCLRCLPE PERQLSVPIP 180
GGSNGDVQQV GVIRCPVCRQ ECRQIDLVDN YFVKDTSEAP SSSDEKSEQV CTSCEDNASA 240
VGFCVECGEW LCKTCIEAHQ RVKFTKDHLI RKKEDVSESV GTSGQRPVFC PVHKQEQLKL 300
FCETCDRLTC RDCQLLEHKE HRYQFLEEAF QNQKGAIENL LAKLLEKKNY VHFAATQVQN 360
RIKEVNETNK RVEQEIKVAI FTLINEINKK GKSLLQQLEN VTKERQMKLL QQQNDITGLS 420
RQVKHVMNFT NWAIASGSST ALLYSKRLIT FQLRHILKAR CDPVPAANGA IRFHCDPTFW 480
AKNVVNLGNL VIESKPAPGY TPNVVVGQVP PGTNHISKTP GQINLAQLRL QHMQQQVYAQ 540
KHQQLQQMRL QQPPAPIPTT TATTQQHPRQ AAPQMLQQQP PRLISVQTMQ RGNMNCGAFQ 600
AHQMRLAQNA ARIPGIPRHS APQYSMMQPH LQRQHSNPGH AGPFPVVSAH NPINPTSPTT 660
ATMANANRGP TSPSVTAIEL IPSVTNPENL PSLPDIPPIQ LEDAGSSSLD NLLSRYISGS 720
HLPPQPTSTM NPSPGPSALS PGSSGLSNSH TPVRPPSTSS TGSRGSCGSS GRTAEKSAHS 780
FKSDQVKVKQ EPGTEEEICS FSGAVKQEKT EDGRRSACML SSPESSLTPP LSTNLHLESE 840
LDTLTGLENH VKTEPTDISE SCKQSGLSNL VNGKSPIRNL MHRSARIGGD GNSKDDDPNE 900
DWCAVCQNGG DLLCCEKCPK VFHLTCHVPT LLSFPSGDWI CTFCRDIGKP EVEYDCDNMQ 960
HSKKGKTAQG LSPVDQRKCE RLLLYLYCHE LSIEFQEPVP VSIPNYYKII KKPMDLSTVK 1020
KKLQKKHSQH YQIPDDFVAD VRLIFKNCER FNEGDSEVAK AGKAVALYFE DKLSEIYSDR 1080
TFTPLPEFEQ DEDDGEVTED SDEDFIQPRR KRLKSDERPV HIK 1123 
Gene Ontology
 GO:0005634; C:nucleus; IDA:MGI.
 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.
 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
 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.