CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015732
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Transcription elongation factor SPT6 
Protein Synonyms/Alias
 hSPT6; Tat-cotransactivator 2 protein; Tat-CT2 protein 
Gene Name
 SUPT6H 
Gene Synonyms/Alias
 KIAA0162; SPT6H 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
306QLRSIPVKGAEDDELubiquitination[1]
360PSTIQKIKEALGFMRubiquitination[2]
402RVWQWDEKWTQLRIRubiquitination[2, 3, 4]
516EQRGPELKQASRRDMubiquitination[1]
538GLDGLAKKFGLTPEQubiquitination[3, 4]
615QTFQERAKLNITPTKubiquitination[2]
638AHYAYSFKYLKNKPVubiquitination[2]
738NKLLAEAKEYVIKACubiquitination[2, 5]
743EAKEYVIKACSRKLYacetylation[6]
777FMDENQGKGIRVLGIubiquitination[2]
816LRLPHFTKRRTAWREubiquitination[2]
844KKFLLNKKPHVVTVAubiquitination[7]
1002RKGTHLLKILKQNNTubiquitination[3, 4]
1100LENPERLKDLDLDAFubiquitination[1, 3, 4, 8]
1243VTGFIPTKFLSDKVVubiquitination[2, 3, 4]
1248PTKFLSDKVVKRPEEubiquitination[2]
1341SFHNINFKQAEKMMEubiquitination[3, 4]
1471ACKELPGKFLLGYQPubiquitination[2, 3, 4]
1512NGLFRWFKDHYQDPVubiquitination[3, 4]
1676HAAIDWGKMAEQWLQacetylation[5, 6]
1676HAAIDWGKMAEQWLQubiquitination[9]
1685AEQWLQEKEAERRKQubiquitination[9]
Reference
 [1] 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]
 [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] 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] 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]
 [6] 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]
 [7] A data set of human endogenous protein ubiquitination sites.
 Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
 Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
 [8] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [9] 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] 
Functional Description
 Acts to stimulate transcriptional elongation by RNA polymerase II. 
Sequence Annotation
 DOMAIN 1213 1282 S1 motif.
 DOMAIN 1325 1431 SH2.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 7 7 Phosphoserine.
 MOD_RES 12 12 Phosphoserine.
 MOD_RES 73 73 Phosphoserine.
 MOD_RES 75 75 Phosphoserine.
 MOD_RES 78 78 Phosphoserine.
 MOD_RES 125 125 Phosphoserine.
 MOD_RES 267 267 Phosphoserine.
 MOD_RES 743 743 N6-acetyllysine.
 MOD_RES 1523 1523 Phosphothreonine.
 MOD_RES 1532 1532 Phosphothreonine.
 MOD_RES 1535 1535 Phosphoserine.
 MOD_RES 1539 1539 Phosphothreonine.
 MOD_RES 1676 1676 N6-acetyllysine.
 MOD_RES 1697 1697 Phosphothreonine.
 MOD_RES 1701 1701 Phosphoserine.
 MOD_RES 1703 1703 Phosphoserine.
 MOD_RES 1718 1718 Phosphothreonine.  
Keyword
 Acetylation; Alternative splicing; Complete proteome; Host-virus interaction; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1726 AA 
Protein Sequence
MSDFVESEAE ESEEEYNDEG EVVPRVTKKF VEEEDDDEEE EEENLDDQDE QGNLKGFIND 60
DDDEDEGEED EGSDSGDSED DVGHKKRKRT SFDDRLEDDD FDLIEENLGV KVKRGQKYRR 120
VKKMSDDEDD DEEEYGKEEH EKEAIAEEIF QDGEGEEGQE AMEAPMAPPE EEEEDDEESD 180
IDDFIVDDDG QPLKKPKWRK KLPGYTDAAL QEAQEIFGVD FDYDEFEKYN EYDEELEEEY 240
EYEDDEAEGE IRVRPKKTTK KRVSRRSIFE MYEPSELESS HLTDQDNEIR ATDLPERFQL 300
RSIPVKGAED DELEEEADWI YRNAFATPTI SLQESCDYLD RGQPASSFSR KGPSTIQKIK 360
EALGFMRNQH FEVPFIAFYR KEYVEPELHI NDLWRVWQWD EKWTQLRIRK ENLTRLFEKM 420
QAYQYEQISA DPDKPLADGI RALDTTDMER LKDVQSMDEL KDVYNHFLLY YGRDIPKMQN 480
AAKASRKKLK RVREEGDEEG EGDEAEDEEQ RGPELKQASR RDMYTICQSA GLDGLAKKFG 540
LTPEQFGENL RDSYQRHETE QFPAEPLELA KDYVCSQFPT PEAVLEGARY MVALQIAREP 600
LVRQVLRQTF QERAKLNITP TKKGRKDVDE AHYAYSFKYL KNKPVKELRD DQFLKICLAE 660
DEGLLTTDIS IDLKGVEGYG NDQTYFEEIK QFYYRDEFSH QVQEWNRQRT MAIERALQQF 720
LYVQMAKELK NKLLAEAKEY VIKACSRKLY NWLRVAPYRP DQQVEEDDDF MDENQGKGIR 780
VLGIAFSSAR DHPVFCALVN GEGEVTDFLR LPHFTKRRTA WREEEREKKA QDIETLKKFL 840
LNKKPHVVTV AGENRDAQML IEDVKRIVHE LDQGQQLSSI GVELVDNELA ILYMNSKKSE 900
AEFRDYPPVL RQAVSLARRI QDPLIEFAQV CSSDEDILCL KFHPLQEHVV KEELLNALYC 960
EFINRVNEVG VDVNRAIAHP YSQALIQYVC GLGPRKGTHL LKILKQNNTR LESRTQLVTM 1020
CHMGPKVFMN CAGFLKIDTA SLGDSTDSYI EVLDGSRVHP ETYEWARKMA VDALEYDESA 1080
EDANPAGALE EILENPERLK DLDLDAFAEE LERQGYGDKH ITLYDIRAEL SCRYKDLRTA 1140
YRSPNTEEIF NMLTKETPET FYIGKLIICN VTGIAHRRPQ GESYDQAIRN DETGLWQCPF 1200
CQQDNFPELS EVWNHFDSGS CPGQAIGVKT RLDNGVTGFI PTKFLSDKVV KRPEERVKVG 1260
MTVHCRIMKI DIEKFSADLT CRTSDLMDRN NEWKLPKDTY YDFDAEAADH KQEEDMKRKQ 1320
QRTTYIKRVI AHPSFHNINF KQAEKMMETM DQGDVIIRPS SKGENHLTVT WKVSDGIYQH 1380
VDVREEGKEN AFSLGATLWI NSEEFEDLDE IVARYVQPMA SFARDLLNHK YYQDCSGGDR 1440
KKLEELLIKT KKEKPTFIPY FICACKELPG KFLLGYQPRG KPRIEYVTVT PEGFRYRGQI 1500
FPTVNGLFRW FKDHYQDPVP GITPSSSSRT RTPASINATP ANINLADLTR AVNALPQNMT 1560
SQMFSAIAAV TGQGQNPNAT PAQWASSQYG YGGSGGGSSA YHVFPTPAQQ PVATPLMTPS 1620
YSYTTPSQPI TTPQYHQLQA STTPQSAQAQ PQPSSSSRQR QQQPKSNSHA AIDWGKMAEQ 1680
WLQEKEAERR KQKQRLTPRP SPSPMIESTP MSIAGDATPL LDEMDR 1726 
Gene Ontology
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
 GO:0003723; F:RNA binding; IEA:InterPro.
 GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
 GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
 GO:0032784; P:regulation of DNA-dependent transcription, elongation; IEA:InterPro.
 GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IEA:InterPro.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW. 
Interpro
 IPR012340; NA-bd_OB-fold.
 IPR003029; Rbsml_prot_S1_RNA-bd_dom.
 IPR022967; RNA-binding_domain_S1.
 IPR000980; SH2.
 IPR023323; Tex-like_dom.
 IPR023097; Tex_RuvX-like_dom.
 IPR017072; TF_Spt6.
 IPR006641; YqgF/RNaseH-like_dom. 
Pfam
 PF00575; S1
 PF00017; SH2 
SMART
 SM00316; S1
 SM00252; SH2
 SM00732; YqgFc 
PROSITE
 PS50126; S1
 PS50001; SH2 
PRINTS