SPT6H_MOUSE - dbPTM
SPT6H_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPT6H_MOUSE
UniProt AC Q62383
Protein Name Transcription elongation factor SPT6
Gene Name Supt6h
Organism Mus musculus (Mouse).
Sequence Length 1726
Subcellular Localization Nucleus .
Protein Description Transcription elongation factor which binds histone H3 and plays a key role in the regulation of transcription elongation and mRNA processing. Enhances the transcription elongation by RNA polymerase II (RNAPII) and is also required for the efficient activation of transcriptional elongation by the HIV-1 nuclear transcriptional activator, Tat. Besides chaperoning histones in transcription, acts to transport and splice mRNA by forming a complex with IWS1 and the C-terminal domain (CTD) of the RNAPII subunit RPB1 (POLR2A). The SUPT6H:IWS1:CTD complex recruits mRNA export factors (ALYREF/THOC4, EXOSC10) as well as histone modifying enzymes (such as SETD2), to ensure proper mRNA splicing, efficient mRNA export and elongation-coupled H3K36 methylation, a signature chromatin mark of active transcription. SUPT6H via its association with SETD1A, regulates both class-switch recombination and somatic hypermutation through formation of H3K4me3 epigenetic marks on activation-induced cytidine deaminase (AICDA) target loci. Promotes the activation of the myogenic gene program by entailing erasure of the repressive H3K27me3 epigenetic mark through stabilization of the chromatin interaction of the H3K27 demethylase KDM6A..
Protein Sequence MSDFVESEAEESEEEYNHEGEVVPRVTKKFVEEEDDDEEEEEENLDDQDERGNLKDFINDDDDEEEGEEDEGSDSGDSEDDVGHKKRKRPSFDDRLEDDDFDLIEENLGVKVKRGQKYRRVKKMSDDDEDDEEEYGKEEHEKEAIAGEIFQDEEGEEGQEAVEAPMAPPDEEEEDDEESDIDDFIVDDDGQPLKKPKWRKKLPGYTDAALQEAQEIFGVDFDYDEFEKYNEYDEELEEDYEYEDDETEGEIRVRPKKTTKKRVSRRSIFEMYEPSELESSHLTDQDNEIRATDLPERFQLRSIPVKAAEDDELEEEADWIYRNAFATPTISLQDSCDYLDRGQPTSSFSRKGPSTVQKIKEALGFMRNQHFEVPFIAFYRKEYVEPELHINDLWRVWQWDEKWTQLRIRKENLTRLFEKMQAYQYEQISADPDKPLADGIRALDTTDMERLKDVQSMDELKDVYNHFLLYYGRDIPKMQNAAKASRKKLKRIKEDGDEEGEGEEAEDEEQRGPELKQASRRDMYTICQSAGLDGLAKKFGLTPEQFGENLRDSYQRHETEQFPAEPLELAKDYVCSQFPTPEAVLEGARYMVALQIAREPLVRQVLRQTFQERAKLNITPTKKGRKDVDEAHYAYSFKYLKNKPVKELRDDQFLKIGLAEDEGLLTIDISIDMKGVEGYGNDQTYFEEIKQFYYRDEFSHQVQEWNRQRTMAIERALQQFLYVQMAKELKNKLLAEARESVVKACSRKLYNWLRVAPYRPDQQVEEDDDFMDENQGKGIRVLGIAFSSARDHPVFCALVNGEGEVTDFLRLPHFTKRRTAWREEEREKKAQDIETLKKFLVNKKPHVVTIAGENRDAQMLTEDVKRIVHELDQGQQLSSIGVELVDNELAILYMNSKKSEAEFRDYPPVLRQAVSLARRIQDPLIEFAQVCSSDEDILCLKFHPLQEHVVKEELLNALYCEFINRVNEVGVDVNRAIAHPYSQALIQYVCGLGPRKGTHLLKILKQNNTRLESRTQLVTMCHMGPKVFMNCAGFLKIDTASLGDSTDSYIEVLDGSRVHPETYEWARKMAVDALEYDESAEDANPAGALEEILENPERLKDLDLDAFAEELERQGYGDKHITLYDIRAELSCRYKDLRTAYRSPNTEEIFNMLTKETPETFYIGKLIICNVTGIAHRRPQGESYDQAIRNDETGLWQCPFCQQDNFPELSEVWNHFDSGSCPGQAIGVKTRLDNGVTGFIPTKFLSDKVVKRPEERVKVGMTVHCRIMKIDIEKFSADLTCRTSDLMDRNNEWKLPKDTYYDFDAEAADHKQEEDMKRKQQRTTYIKRVIAHPSFHNINFKQAEKMMETMDQGDVIIRPSSKGENHLTVTWKVSAGIYQHVDVREEGKENAFSLGATLWINSEEFEDLDEIVARYVQPMASFARDLLNHKYYQDCSGGDRKKLEELLIKTKKEKPTFIPYFICACKELPGKFLLGYQPRGKPRIEYVTVTPEGFRYRGQIFPTVNGLFRWFKDHYQDPVPGITPSSSNRTRTPASINATPANINLADLTRAVNALPQNMTSQMFSAIAAVTGQGQNPNATPAQWASSQYGYGGSGGGSSAYHVFPTPAQQPVATPLMTPSYSYTTPSQPITTPQYHQLQASTTPQSTQAQPQPSSSSRQRQQQPKSNSHAAIDWGKMAEQWLQEKEAERRKQKQRLTPRPSPSPMIESTPMSIAGDATPLLDEMDR
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Acetylation------MSDFVESEA
------CCCCCCCCH		51.57-
2Phosphorylation------MSDFVESEA
------CCCCCCCCH		51.5723684622
7Phosphorylation-MSDFVESEAEESEE
-CCCCCCCCHHHCHH		36.4824723360
12PhosphorylationVESEAEESEEEYNHE
CCCCHHHCHHHHCCC		41.6427742792
16PhosphorylationAEESEEEYNHEGEVV
HHHCHHHHCCCCCCC		25.7125619855
73PhosphorylationEGEEDEGSDSGDSED
CCCCCCCCCCCCCCC		26.9325521595
75PhosphorylationEEDEGSDSGDSEDDV
CCCCCCCCCCCCCCC		46.3125521595
78PhosphorylationEGSDSGDSEDDVGHK
CCCCCCCCCCCCCCC		46.5825521595
91PhosphorylationHKKRKRPSFDDRLED
CCCCCCCCCCCCCCC		45.3925521595
125PhosphorylationYRRVKKMSDDDEDDE
EEEEECCCCCCCCCH		46.9325521595
135PhosphorylationDEDDEEEYGKEEHEK
CCCCHHHHCHHHHHH		36.4625619855
179PhosphorylationEEEDDEESDIDDFIV
CCCCCCCCCCCCEEE		37.5129514104
267PhosphorylationKKRVSRRSIFEMYEP
CCCCCHHHHHHHCCC		30.4426525534
283PhosphorylationELESSHLTDQDNEIR
HHHHCCCCCCCCCCC		26.6226525534
292PhosphorylationQDNEIRATDLPERFQ
CCCCCCCCCCCHHHC		28.37-
321PhosphorylationEEEADWIYRNAFATP
HHHHHHHHHCCCCCC		8.1218563927
423PhosphorylationLFEKMQAYQYEQISA
HHHHHHHHHHHHCCC		8.5025168779
425PhosphorylationEKMQAYQYEQISADP
HHHHHHHHHHCCCCC		9.3425168779
429PhosphorylationAYQYEQISADPDKPL
HHHHHHCCCCCCCCC		26.7221183079
445PhosphorylationDGIRALDTTDMERLK
CCCCCCCCCCHHHHH		26.0821183079
446PhosphorylationGIRALDTTDMERLKD
CCCCCCCCCHHHHHC		32.7721183079
538UbiquitinationGLDGLAKKFGLTPEQ
CCHHHHHHHCCCHHH		38.7722790023
619PhosphorylationERAKLNITPTKKGRK
HHHCCCCCCCCCCCC		24.6727600695
621PhosphorylationAKLNITPTKKGRKDV
HCCCCCCCCCCCCCC		36.4228066266
666PhosphorylationAEDEGLLTIDISIDM
ECCCCCEEEEEEEEC		22.96-
670PhosphorylationGLLTIDISIDMKGVE
CCEEEEEEEECCCCC		14.59-
743AcetylationEARESVVKACSRKLY
HHHHHHHHHHHHHHH		41.33-
777UbiquitinationFMDENQGKGIRVLGI
CCCCCCCCCEEEEEE		41.2122790023
844UbiquitinationKKFLVNKKPHVVTIA
HHHHHCCCCCEEEEC		34.8422790023
915PhosphorylationPVLRQAVSLARRIQD
HHHHHHHHHHHHHCC		21.2324453211
1039PhosphorylationAGFLKIDTASLGDST
CCEEEEEHHCCCCCC		22.9430635358
1041PhosphorylationFLKIDTASLGDSTDS
EEEEEHHCCCCCCCC		34.6730635358
1045PhosphorylationDTASLGDSTDSYIEV
EHHCCCCCCCCCEEE		32.1130635358
1046PhosphorylationTASLGDSTDSYIEVL
HHCCCCCCCCCEEEC		33.4330635358
1048PhosphorylationSLGDSTDSYIEVLDG
CCCCCCCCCEEECCC		28.2630635358
1049PhosphorylationLGDSTDSYIEVLDGS
CCCCCCCCEEECCCC		12.1530635358
1056PhosphorylationYIEVLDGSRVHPETY
CEEECCCCCCCHHHH		30.6930635358
1100UbiquitinationLENPERLKDLDLDAF
HHCHHHHHCCCHHHH		63.5722790023
1122PhosphorylationGYGDKHITLYDIRAE
CCCCCCEEEEEHHHH		20.98-
1124PhosphorylationGDKHITLYDIRAELS
CCCCEEEEEHHHHHH		10.73-
1134PhosphorylationRAELSCRYKDLRTAY
HHHHHHCHHHHHHHH		17.12-
1139PhosphorylationCRYKDLRTAYRSPNT
HCHHHHHHHHCCCCH		35.02-
1184PhosphorylationRRPQGESYDQAIRND
CCCCCCCHHHHHHCC		14.0523567750
1276PhosphorylationKIDIEKFSADLTCRT
ECCHHHHCCCCEEEH		31.76-
1280PhosphorylationEKFSADLTCRTSDLM
HHHCCCCEEEHHHHC		10.65-
1450PhosphorylationLEELLIKTKKEKPTF
HHHHHHHHCCCCCCC		40.1125177544
1515PhosphorylationFRWFKDHYQDPVPGI
HHHHHHHCCCCCCCC		25.4125619855
1523PhosphorylationQDPVPGITPSSSNRT
CCCCCCCCCCCCCCC		24.0425521595
1525PhosphorylationPVPGITPSSSNRTRT
CCCCCCCCCCCCCCC		37.4425619855
1526PhosphorylationVPGITPSSSNRTRTP
CCCCCCCCCCCCCCC		32.6025619855
1527PhosphorylationPGITPSSSNRTRTPA
CCCCCCCCCCCCCCC		34.3725619855
1530PhosphorylationTPSSSNRTRTPASIN
CCCCCCCCCCCCCCC		43.0525521595
1532PhosphorylationSSSNRTRTPASINAT
CCCCCCCCCCCCCCC		23.6925521595
1535PhosphorylationNRTRTPASINATPAN
CCCCCCCCCCCCCCC		19.9925521595
1539PhosphorylationTPASINATPANINLA
CCCCCCCCCCCCCHH		20.6027087446
1668PhosphorylationQQQPKSNSHAAIDWG
HHCCCCCCCCHHHHH		22.9227600695
1676AcetylationHAAIDWGKMAEQWLQ
CCHHHHHHHHHHHHH		30.5922826441
1697PhosphorylationRKQKQRLTPRPSPSP
HHHHHCCCCCCCCCC		21.3126643407
1701PhosphorylationQRLTPRPSPSPMIES
HCCCCCCCCCCCEEC		39.0126643407
1703PhosphorylationLTPRPSPSPMIESTP
CCCCCCCCCCEECCC		31.2926643407
1708PhosphorylationSPSPMIESTPMSIAG
CCCCCEECCCCCCCC		27.2126643407
1709PhosphorylationPSPMIESTPMSIAGD
CCCCEECCCCCCCCC		15.3826643407
1712PhosphorylationMIESTPMSIAGDATP
CEECCCCCCCCCCCH		15.5326643407
1718PhosphorylationMSIAGDATPLLDEMD
CCCCCCCCHHCCCCC		21.1421082442
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of SPT6H_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPT6H_MOUSE !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of SPT6H_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB1_HUMANPOLR2Aphysical
17234882
SSPN_HUMANSSPNphysical
17234882
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPT6H_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Solid tumor proteome and phosphoproteome analysis by high resolutionmass spectrometry.";
Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J.,Faessler R., Mann M.;
J. Proteome Res. 7:5314-5326(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.

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