CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010410
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 General transcription factor II-I 
Protein Synonyms/Alias
 GTFII-I; TFII-I; Bruton tyrosine kinase-associated protein 135; BAP-135; BTK-associated protein 135; SRF-Phox1-interacting protein; SPIN; Williams-Beuren syndrome chromosomal region 6 protein 
Gene Name
 GTF2I 
Gene Synonyms/Alias
 BAP135; WBSCR6 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
70RAFVNTRKDFQKDFVubiquitination[1]
74NTRKDFQKDFVKYCVubiquitination[1, 2, 3, 4]
78DFQKDFVKYCVEEEEubiquitination[1]
140VVPVPYEKMLRDQSAubiquitination[1, 2, 4]
160LPEGVAFKHPENYDLubiquitination[2, 4]
219GGSCGPIKVKTEPTEmethylation[5]
219GGSCGPIKVKTEPTEubiquitination[1, 6]
221SCGPIKVKTEPTEDSsumoylation[7]
240EMAAVTVKEESEDPDsumoylation[7]
353VREFNFEKWNARITDubiquitination[1, 2, 3, 4, 6, 8, 9]
363ARITDLRKQVEELFEubiquitination[1]
380YAQAIKAKGPVTIPYubiquitination[1]
450REDLQLDKPASGVKEacetylation[6, 10, 11]
456DKPASGVKEEWYARIsumoylation[7]
456DKPASGVKEEWYARIubiquitination[1, 9]
476MVDQLFCKKFAEALGubiquitination[8]
488ALGSTEAKAVPYQKFubiquitination[1, 8]
494AKAVPYQKFEAHPNDubiquitination[1, 2, 4, 6]
526YGIPRLEKIIQVGNRubiquitination[1]
539NRIKFVIKRPELLTHubiquitination[2, 4]
561PRTNTPVKEDWNVRIacetylation[6]
561PRTNTPVKEDWNVRIubiquitination[1, 2, 4]
573VRITKLRKQVEEIFNubiquitination[1]
660LPPGMASKINTKALQubiquitination[1]
664MASKINTKALQSPKRubiquitination[1]
715NGSNVPFKPRGREFSubiquitination[1, 3, 6]
736KITDLKQKVENLFNEubiquitination[1]
744VENLFNEKCGEALGLubiquitination[1]
752CGEALGLKQAVKVPFubiquitination[1, 3, 8, 9]
879VNDLFSRKFGEAIGMubiquitination[1, 2, 4]
891IGMGFPVKVPYRKITubiquitination[1]
991TDGSSQIKQEPDPTWsumoylation[7, 12]
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] 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]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] 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]
 [5] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077]
 [6] 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]
 [7] Broad spectrum identification of cellular small ubiquitin-related modifier (SUMO) substrate proteins.
 Zhao Y, Kwon SW, Anselmo A, Kaur K, White MA.
 J Biol Chem. 2004 May 14;279(20):20999-1002. [PMID: 15016812]
 [8] 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]
 [9] 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]
 [10] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [11] 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]
 [12] 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] 
Functional Description
 Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C- FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. 
Sequence Annotation
 REPEAT 103 197 GTF2I-like 1.
 REPEAT 352 446 GTF2I-like 2.
 REPEAT 457 551 GTF2I-like 3.
 REPEAT 562 656 GTF2I-like 4.
 REPEAT 724 818 GTF2I-like 5.
 REPEAT 859 953 GTF2I-like 6.
 MOTIF 320 327 Nuclear localization signal (Potential).
 MOD_RES 2 2 N-acetylalanine.
 MOD_RES 103 103 Phosphoserine.
 MOD_RES 207 207 Phosphoserine.
 MOD_RES 210 210 Phosphoserine.
 MOD_RES 248 248 Phosphotyrosine; by BTK.
 MOD_RES 318 318 Phosphotyrosine; by BTK (Probable).
 MOD_RES 398 398 Phosphotyrosine; by BTK.
 MOD_RES 412 412 Phosphoserine; by PKG/PRKG1.
 MOD_RES 503 503 Phosphotyrosine; by BTK.
 MOD_RES 558 558 Phosphothreonine.
 MOD_RES 668 668 Phosphoserine.
 MOD_RES 784 784 Phosphoserine; by PKG/PRKG1.
 MOD_RES 823 823 Phosphoserine.  
Keyword
 3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Transcription; Transcription regulation; Ubl conjugation; Williams-Beuren syndrome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 998 AA 
Protein Sequence
MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE 60
RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF 120
CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI 180
SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK 240
EESEDPDYYQ YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDSTQHVP 300
SETSEDPEVE VTIEDDDYSP PSKRPKANEL PQPPVPEPAN AGKRKVREFN FEKWNARITD 360
LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE GLPEGIPFRR PSTYGIPRLE 420
RILLAKERIR FVIKKHELLN STREDLQLDK PASGVKEEWY ARITKLRKMV DQLFCKKFAE 480
ALGSTEAKAV PYQKFEAHPN DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR 540
PELLTHSTTE VTQPRTNTPV KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF 600
ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK FVVKKPELVI SYLPPGMASK 660
INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNNNPQTSA VRTPTQTNGS NVPFKPRGRE 720
FSFEAWNAKI TDLKQKVENL FNEKCGEALG LKQAVKVPFA LFESFPEDFY VEGLPEGVPF 780
RRPSTFGIPR LEKILRNKAK IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG 840
VEDLNIIQVT IPDDDNERLS KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN 900
PGCVVVDGMP PGVSFKAPSY LEISSMRRIL DSAEFIKFTV IRPFPGLVIN NQLVDQSESE 960
GPVIQESAEP SQLEVPATEE IKETDGSSQI KQEPDPTW 998 
Gene Ontology
 GO:0042995; C:cell projection; IEA:Compara.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
 GO:0043025; C:neuronal cell body; IEA:Compara.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; NAS:ProtInc.
 GO:0009790; P:embryo development; IEA:Compara.
 GO:0016525; P:negative regulation of angiogenesis; IDA:MGI.
 GO:0051481; P:reduction of cytosolic calcium ion concentration; IEA:Compara.
 GO:0007165; P:signal transduction; TAS:ProtInc.
 GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:ProtInc. 
Interpro
 IPR004212; GTF2I.
 IPR016659; TF_II-I. 
Pfam
 PF02946; GTF2I 
SMART
  
PROSITE
 PS51139; GTF2I 
PRINTS