SPT6H_HUMAN - dbPTM
SPT6H_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SPT6H_HUMAN
UniProt AC Q7KZ85
Protein Name Transcription elongation factor SPT6
Gene Name SUPT6H
Organism Homo sapiens (Human).
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 MSDFVESEAEESEEEYNDEGEVVPRVTKKFVEEEDDDEEEEEENLDDQDEQGNLKGFINDDDDEDEGEEDEGSDSGDSEDDVGHKKRKRTSFDDRLEDDDFDLIEENLGVKVKRGQKYRRVKKMSDDEDDDEEEYGKEEHEKEAIAEEIFQDGEGEEGQEAMEAPMAPPEEEEEDDEESDIDDFIVDDDGQPLKKPKWRKKLPGYTDAALQEAQEIFGVDFDYDEFEKYNEYDEELEEEYEYEDDEAEGEIRVRPKKTTKKRVSRRSIFEMYEPSELESSHLTDQDNEIRATDLPERFQLRSIPVKGAEDDELEEEADWIYRNAFATPTISLQESCDYLDRGQPASSFSRKGPSTIQKIKEALGFMRNQHFEVPFIAFYRKEYVEPELHINDLWRVWQWDEKWTQLRIRKENLTRLFEKMQAYQYEQISADPDKPLADGIRALDTTDMERLKDVQSMDELKDVYNHFLLYYGRDIPKMQNAAKASRKKLKRVREEGDEEGEGDEAEDEEQRGPELKQASRRDMYTICQSAGLDGLAKKFGLTPEQFGENLRDSYQRHETEQFPAEPLELAKDYVCSQFPTPEAVLEGARYMVALQIAREPLVRQVLRQTFQERAKLNITPTKKGRKDVDEAHYAYSFKYLKNKPVKELRDDQFLKICLAEDEGLLTTDISIDLKGVEGYGNDQTYFEEIKQFYYRDEFSHQVQEWNRQRTMAIERALQQFLYVQMAKELKNKLLAEAKEYVIKACSRKLYNWLRVAPYRPDQQVEEDDDFMDENQGKGIRVLGIAFSSARDHPVFCALVNGEGEVTDFLRLPHFTKRRTAWREEEREKKAQDIETLKKFLLNKKPHVVTVAGENRDAQMLIEDVKRIVHELDQGQQLSSIGVELVDNELAILYMNSKKSEAEFRDYPPVLRQAVSLARRIQDPLIEFAQVCSSDEDILCLKFHPLQEHVVKEELLNALYCEFINRVNEVGVDVNRAIAHPYSQALIQYVCGLGPRKGTHLLKILKQNNTRLESRTQLVTMCHMGPKVFMNCAGFLKIDTASLGDSTDSYIEVLDGSRVHPETYEWARKMAVDALEYDESAEDANPAGALEEILENPERLKDLDLDAFAEELERQGYGDKHITLYDIRAELSCRYKDLRTAYRSPNTEEIFNMLTKETPETFYIGKLIICNVTGIAHRRPQGESYDQAIRNDETGLWQCPFCQQDNFPELSEVWNHFDSGSCPGQAIGVKTRLDNGVTGFIPTKFLSDKVVKRPEERVKVGMTVHCRIMKIDIEKFSADLTCRTSDLMDRNNEWKLPKDTYYDFDAEAADHKQEEDMKRKQQRTTYIKRVIAHPSFHNINFKQAEKMMETMDQGDVIIRPSSKGENHLTVTWKVSDGIYQHVDVREEGKENAFSLGATLWINSEEFEDLDEIVARYVQPMASFARDLLNHKYYQDCSGGDRKKLEELLIKTKKEKPTFIPYFICACKELPGKFLLGYQPRGKPRIEYVTVTPEGFRYRGQIFPTVNGLFRWFKDHYQDPVPGITPSSSSRTRTPASINATPANINLADLTRAVNALPQNMTSQMFSAIAAVTGQGQNPNATPAQWASSQYGYGGSGGGSSAYHVFPTPAQQPVATPLMTPSYSYTTPSQPITTPQYHQLQASTTPQSAQAQPQPSSSSRQRQQQPKSNSHAAIDWGKMAEQWLQEKEAERRKQKQRLTPRPSPSPMIESTPMSIAGDATPLLDEMDR
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
51.5721406692
2Phosphorylation------MSDFVESEA
------CCCCCCCCH
51.5722617229
7Phosphorylation-MSDFVESEAEESEE
-CCCCCCCCHHHCHH
36.4828355574
12PhosphorylationVESEAEESEEEYNDE
CCCCHHHCHHHHCCC
41.6428355574
16PhosphorylationAEESEEEYNDEGEVV
HHHCHHHHCCCCCCC
31.0624300666
17 (in isoform 2)Phosphorylation-44.1025159151
20 (in isoform 2)Phosphorylation-35.5425159151
21 (in isoform 2)Phosphorylation-37.9925159151
27PhosphorylationGEVVPRVTKKFVEEE
CCCCCCHHHHHHCCC
29.7823090842
29AcetylationVVPRVTKKFVEEEDD
CCCCHHHHHHCCCCC
45.3226051181
29UbiquitinationVVPRVTKKFVEEEDD
CCCCHHHHHHCCCCC
45.3229967540
62 (in isoform 2)Ubiquitination-65.1521890473
73PhosphorylationEGEEDEGSDSGDSED
CCCCCCCCCCCCCCC
26.9323927012
75PhosphorylationEEDEGSDSGDSEDDV
CCCCCCCCCCCCCCC
46.3123927012
78PhosphorylationEGSDSGDSEDDVGHK
CCCCCCCCCCCCCCC
46.5823927012
90PhosphorylationGHKKRKRTSFDDRLE
CCCCCCCCCHHHHCC
36.4630266825
91PhosphorylationHKKRKRTSFDDRLED
CCCCCCCCHHHHCCC
30.6130266825
95MethylationKRTSFDDRLEDDDFD
CCCCHHHHCCCCCCC
41.65115917629
125O-linked_GlycosylationYRRVKKMSDDEDDDE
EEEEECCCCCCCCCH
51.2830059200
125PhosphorylationYRRVKKMSDDEDDDE
EEEEECCCCCCCCCH
51.2822167270
135PhosphorylationEDDDEEEYGKEEHEK
CCCCHHHHCHHHHHH
36.4623403867
160 (in isoform 2)Ubiquitination-61.9221890473
179PhosphorylationEEEDDEESDIDDFIV
HCCCCCCCCCCCEEE
37.5118669648
267PhosphorylationKKRVSRRSIFEMYEP
CCCCCHHHHHHHCCC
30.4425159151
272PhosphorylationRRSIFEMYEPSELES
HHHHHHHCCCHHHHH
19.9329978859
275PhosphorylationIFEMYEPSELESSHL
HHHHCCCHHHHHCCC
42.7628348404
279PhosphorylationYEPSELESSHLTDQD
CCCHHHHHCCCCCCC
35.3629496963
279UbiquitinationYEPSELESSHLTDQD
CCCHHHHHCCCCCCC
35.3621890473
280PhosphorylationEPSELESSHLTDQDN
CCHHHHHCCCCCCCC
17.0927251275
283PhosphorylationELESSHLTDQDNEIR
HHHHCCCCCCCCCCC
26.6230576142
290 (in isoform 2)Ubiquitination-25.8421890473
292PhosphorylationQDNEIRATDLPERFQ
CCCCCCCCCCCHHHE
28.3722817900
306UbiquitinationQLRSIPVKGAEDDEL
EEECCCCCCCCCCHH
47.2332015554
327PhosphorylationIYRNAFATPTISLQE
HHHCCCCCCCEEHHH
17.9528348404
329PhosphorylationRNAFATPTISLQESC
HCCCCCCCEEHHHHC
20.8828348404
331PhosphorylationAFATPTISLQESCDY
CCCCCCEEHHHHCCC
26.8628348404
331 (in isoform 2)Ubiquitination-26.8621890473
347PhosphorylationDRGQPASSFSRKGPS
CCCCCCHHHCCCCHH
29.3717081983
351UbiquitinationPASSFSRKGPSTIQK
CCHHHCCCCHHHHHH
74.1729967540
354PhosphorylationSFSRKGPSTIQKIKE
HHCCCCHHHHHHHHH
46.9718669648
354UbiquitinationSFSRKGPSTIQKIKE
HHCCCCHHHHHHHHH
46.9724816145
358UbiquitinationKGPSTIQKIKEALGF
CCHHHHHHHHHHHCH
52.4729967540
360UbiquitinationPSTIQKIKEALGFMR
HHHHHHHHHHHCHHH
43.93-
393UbiquitinationPELHINDLWRVWQWD
CCEEHHHHHHHHHCC
2.4522817900
402UbiquitinationRVWQWDEKWTQLRIR
HHHHCCHHHHHHHHH
53.7421890473
402AcetylationRVWQWDEKWTQLRIR
HHHHCCHHHHHHHHH
53.7488961
402UbiquitinationRVWQWDEKWTQLRIR
HHHHCCHHHHHHHHH
53.7421890473
402 (in isoform 1)Ubiquitination-53.7421890473
402 (in isoform 3)Ubiquitination-53.7421890473
414UbiquitinationRIRKENLTRLFEKMQ
HHHHHHHHHHHHHHH
36.5922817900
415UbiquitinationIRKENLTRLFEKMQA
HHHHHHHHHHHHHHH
40.3121890473
419UbiquitinationNLTRLFEKMQAYQYE
HHHHHHHHHHHHHHH
29.0429967540
434UbiquitinationQISADPDKPLADGIR
HCCCCCCCCCCCCCC
47.5229967540
452UbiquitinationTTDMERLKDVQSMDE
CCCHHHHHCCCCHHH
63.1729967540
456PhosphorylationERLKDVQSMDELKDV
HHHHCCCCHHHHHHH
28.22-
464PhosphorylationMDELKDVYNHFLLYY
HHHHHHHHHHHHHHH
17.04-
470PhosphorylationVYNHFLLYYGRDIPK
HHHHHHHHHCCCHHH
13.16-
477UbiquitinationYYGRDIPKMQNAAKA
HHCCCHHHHHHHHHH
54.1524816145
499UbiquitinationVREEGDEEGEGDEAE
HHHCCCCCCCCCHHH
68.2524816145
511MethylationEAEDEEQRGPELKQA
HHHCHHHHCHHHHHH
66.95115917625
516UbiquitinationEQRGPELKQASRRDM
HHHCHHHHHHHHHHH
42.0021906983
516 (in isoform 1)Ubiquitination-42.0021890473
516 (in isoform 3)Ubiquitination-42.0021890473
537UbiquitinationAGLDGLAKKFGLTPE
CCCHHHHHHHCCCHH
54.3922817900
538UbiquitinationGLDGLAKKFGLTPEQ
CCHHHHHHHCCCHHH
38.7721890473
538UbiquitinationGLDGLAKKFGLTPEQ
CCHHHHHHHCCCHHH
38.7722817900
538 (in isoform 1)Ubiquitination-38.7721890473
538 (in isoform 3)Ubiquitination-38.7721890473
590PhosphorylationAVLEGARYMVALQIA
HHHHHHHHHHHHHHH
8.7320068231
615UbiquitinationQTFQERAKLNITPTK
HHHHHHHCCCCCCCC
48.57-
619PhosphorylationERAKLNITPTKKGRK
HHHCCCCCCCCCCCC
24.6725159151
621PhosphorylationAKLNITPTKKGRKDV
HCCCCCCCCCCCCCC
36.4220068231
622UbiquitinationKLNITPTKKGRKDVD
CCCCCCCCCCCCCCC
55.2024816145
633PhosphorylationKDVDEAHYAYSFKYL
CCCCHHHHHHHHHHH
17.8128152594
635PhosphorylationVDEAHYAYSFKYLKN
CCHHHHHHHHHHHCC
13.8928152594
636PhosphorylationDEAHYAYSFKYLKNK
CHHHHHHHHHHHCCC
13.6924719451
638UbiquitinationAHYAYSFKYLKNKPV
HHHHHHHHHHCCCCH
43.67-
670PhosphorylationGLLTTDISIDLKGVE
CCEEEEEEEECCCCC
16.9224961811
685PhosphorylationGYGNDQTYFEEIKQF
CCCCCHHHHHHHHHH
11.89-
721UbiquitinationERALQQFLYVQMAKE
HHHHHHHHHHHHHHH
3.3920972266
722PhosphorylationRALQQFLYVQMAKEL
HHHHHHHHHHHHHHH
7.0229888752
732UbiquitinationMAKELKNKLLAEAKE
HHHHHHHHHHHHHHH
43.2029967540
7382-HydroxyisobutyrylationNKLLAEAKEYVIKAC
HHHHHHHHHHHHHHH
40.87-
738UbiquitinationNKLLAEAKEYVIKAC
HHHHHHHHHHHHHHH
40.8729967540
740PhosphorylationLLAEAKEYVIKACSR
HHHHHHHHHHHHHHH
13.5321712546
743AcetylationEAKEYVIKACSRKLY
HHHHHHHHHHHHHHH
33.0419608861
746PhosphorylationEYVIKACSRKLYNWL
HHHHHHHHHHHHHHH
36.9921712546
777UbiquitinationFMDENQGKGIRVLGI
CCCCCCCCCEEEEEE
41.21-
816UbiquitinationLRLPHFTKRRTAWRE
HCCCHHHCCCHHHHH
38.65-
835PhosphorylationKKAQDIETLKKFLLN
HHHHHHHHHHHHHHC
44.1820068231
843UbiquitinationLKKFLLNKKPHVVTV
HHHHHHCCCCCEEEE
68.5929967540
844UbiquitinationKKFLLNKKPHVVTVA
HHHHHCCCCCEEEEC
39.0022053931
859SulfoxidationGENRDAQMLIEDVKR
CCCCCHHHHHHHHHH
4.3421406390
879UbiquitinationDQGQQLSSIGVELVD
HCCCCHHHHCEEEEC
31.7721890473
882UbiquitinationQQLSSIGVELVDNEL
CCHHHHCEEEECCCE
4.9822817900
915PhosphorylationPVLRQAVSLARRIQD
HHHHHHHHHHHHHCC
21.2324719451
977UbiquitinationGVDVNRAIAHPYSQA
CCCHHHHHCCCCHHH
3.0621890473
1002UbiquitinationRKGTHLLKILKQNNT
CCCHHHHHHHHHCCC
52.9621890473
1002AcetylationRKGTHLLKILKQNNT
CCCHHHHHHHHHCCC
52.9626051181
1002UbiquitinationRKGTHLLKILKQNNT
CCCHHHHHHHHHCCC
52.9622817900
1002 (in isoform 1)Ubiquitination-52.9621890473
1005UbiquitinationTHLLKILKQNNTRLE
HHHHHHHHHCCCCCC
55.2222817900
1039PhosphorylationAGFLKIDTASLGDST
CCEEEEEHHCCCCCC
22.9420873877
1041PhosphorylationFLKIDTASLGDSTDS
EEEEEHHCCCCCCCC
34.6720873877
1045PhosphorylationDTASLGDSTDSYIEV
EHHCCCCCCCCCEEE
32.1125627689
1046PhosphorylationTASLGDSTDSYIEVL
HHCCCCCCCCCEEEC
33.4325627689
1048PhosphorylationSLGDSTDSYIEVLDG
CCCCCCCCCEEECCC
28.2630576142
1049PhosphorylationLGDSTDSYIEVLDGS
CCCCCCCCEEECCCC
12.1520873877
1062PhosphorylationGSRVHPETYEWARKM
CCCCCHHHHHHHHHH
31.0618452278
1063PhosphorylationSRVHPETYEWARKMA
CCCCHHHHHHHHHHH
14.0718452278
1076PhosphorylationMAVDALEYDESAEDA
HHHHHHCCCCCCCCC
26.3427642862
1079PhosphorylationDALEYDESAEDANPA
HHHCCCCCCCCCCCC
33.7818452278
1100UbiquitinationLENPERLKDLDLDAF
HHCHHHHHCCCHHHH
63.5721890473
1100UbiquitinationLENPERLKDLDLDAF
HHCHHHHHCCCHHHH
63.5722053931
1100 (in isoform 1)Ubiquitination-63.5721890473
1120UbiquitinationRQGYGDKHITLYDIR
HCCCCCCCEEEEEHH
24.0121890473
1122PhosphorylationGYGDKHITLYDIRAE
CCCCCCEEEEEHHHH
20.9824719451
1124PhosphorylationGDKHITLYDIRAELS
CCCCEEEEEHHHHHH
10.7324719451
1125UbiquitinationDKHITLYDIRAELSC
CCCEEEEEHHHHHHH
27.3222817900
1134PhosphorylationRAELSCRYKDLRTAY
HHHHHHCHHHHHHHH
17.1224719451
1139PhosphorylationCRYKDLRTAYRSPNT
HCHHHHHHHHCCCCH
35.0224719451
1141PhosphorylationYKDLRTAYRSPNTEE
HHHHHHHHCCCCHHH
15.8322210691
1154PhosphorylationEEIFNMLTKETPETF
HHHHHHHHCCCCCCE
18.9622210691
1172PhosphorylationKLIICNVTGIAHRRP
EEEEEECCCCCCCCC
14.63-
1183PhosphorylationHRRPQGESYDQAIRN
CCCCCCCCHHHHHHC
40.6128555341
1218UbiquitinationEVWNHFDSGSCPGQA
HHHHHCCCCCCCCCE
31.4921890473
1222UbiquitinationHFDSGSCPGQAIGVK
HCCCCCCCCCEEEEE
39.3622817900
1243UbiquitinationVTGFIPTKFLSDKVV
CCCCCCCHHHCCCCC
38.6621890473
1243AcetylationVTGFIPTKFLSDKVV
CCCCCCCHHHCCCCC
38.6625953088
1243UbiquitinationVTGFIPTKFLSDKVV
CCCCCCCHHHCCCCC
38.6621890473
1243 (in isoform 1)Ubiquitination-38.6621890473
1248AcetylationPTKFLSDKVVKRPEE
CCHHHCCCCCCCHHH
45.6225953088
1248UbiquitinationPTKFLSDKVVKRPEE
CCHHHCCCCCCCHHH
45.6222817900
12692-HydroxyisobutyrylationTVHCRIMKIDIEKFS
EEEEEEEECCHHHHC
34.55-
1269AcetylationTVHCRIMKIDIEKFS
EEEEEEEECCHHHHC
34.5525953088
1274AcetylationIMKIDIEKFSADLTC
EEECCHHHHCCCCEE
44.9826051181
1274UbiquitinationIMKIDIEKFSADLTC
EEECCHHHHCCCCEE
44.9829967540
1276PhosphorylationKIDIEKFSADLTCRT
ECCHHHHCCCCEEEH
31.7623403867
1280PhosphorylationEKFSADLTCRTSDLM
HHHCCCCEEEHHHHC
10.6523879269
1283PhosphorylationSADLTCRTSDLMDRN
CCCCEEEHHHHCCCC
28.8323879269
1284PhosphorylationADLTCRTSDLMDRNN
CCCEEEHHHHCCCCC
14.9223879269
1289MethylationRTSDLMDRNNEWKLP
EHHHHCCCCCCCCCC
33.63115917621
1294UbiquitinationMDRNNEWKLPKDTYY
CCCCCCCCCCCCCCC
49.0529967540
1297UbiquitinationNNEWKLPKDTYYDFD
CCCCCCCCCCCCCCC
73.4729967540
1341UbiquitinationSFHNINFKQAEKMME
HHCCCCHHHHHHHHH
44.0721890473
1341UbiquitinationSFHNINFKQAEKMME
HHCCCCHHHHHHHHH
44.0722817900
1341 (in isoform 1)Ubiquitination-44.0721890473
1343UbiquitinationHNINFKQAEKMMETM
CCCCHHHHHHHHHHC
20.9722817900
1345UbiquitinationINFKQAEKMMETMDQ
CCHHHHHHHHHHCCC
46.7122817900
1348UbiquitinationKQAEKMMETMDQGDV
HHHHHHHHHCCCCCE
37.1721890473
1378PhosphorylationWKVSDGIYQHVDVRE
EEEECCEEEEEECCH
9.71-
1389UbiquitinationDVREEGKENAFSLGA
ECCHHCCCCCEECCC
65.7321890473
1415PhosphorylationLDEIVARYVQPMASF
HHHHHHHHHHHHHHH
8.1626330541
1421PhosphorylationRYVQPMASFARDLLN
HHHHHHHHHHHHHHC
17.1226330541
1430AcetylationARDLLNHKYYQDCSG
HHHHHCCCCCCCCCC
44.5826051181
1450PhosphorylationLEELLIKTKKEKPTF
HHHHHHHHCCCCCCC
40.1126074081
1454AcetylationLIKTKKEKPTFIPYF
HHHHCCCCCCCCCEE
59.2325953088
1456PhosphorylationKTKKEKPTFIPYFIC
HHCCCCCCCCCEEEE
45.3126074081
1460PhosphorylationEKPTFIPYFICACKE
CCCCCCCEEEEECCC
10.7626074081
1466AcetylationPYFICACKELPGKFL
CEEEEECCCCCCCEE
43.7026051181
1466UbiquitinationPYFICACKELPGKFL
CEEEEECCCCCCCEE
43.7022817900
1471UbiquitinationACKELPGKFLLGYQP
ECCCCCCCEEECCCC
30.7921890473
1471AcetylationACKELPGKFLLGYQP
ECCCCCCCEEECCCC
30.7925953088
1471UbiquitinationACKELPGKFLLGYQP
ECCCCCCCEEECCCC
30.7922817900
1471 (in isoform 1)Ubiquitination-30.7921890473
1486PhosphorylationRGKPRIEYVTVTPEG
CCCCCEEEEEECCCC
10.0728152594
1488PhosphorylationKPRIEYVTVTPEGFR
CCCEEEEEECCCCEE
20.1228152594
1512UbiquitinationNGLFRWFKDHYQDPV
HHHHHHHHHHCCCCC
36.3121890473
1512UbiquitinationNGLFRWFKDHYQDPV
HHHHHHHHHHCCCCC
36.3122817900
1512 (in isoform 1)Ubiquitination-36.3121890473
1515PhosphorylationFRWFKDHYQDPVPGI
HHHHHHHCCCCCCCC
25.4123403867
1523O-linked_GlycosylationQDPVPGITPSSSSRT
CCCCCCCCCCCCCCC
24.0430059200
1523PhosphorylationQDPVPGITPSSSSRT
CCCCCCCCCCCCCCC
24.0429255136
1525O-linked_GlycosylationPVPGITPSSSSRTRT
CCCCCCCCCCCCCCC
33.9130059200
1525PhosphorylationPVPGITPSSSSRTRT
CCCCCCCCCCCCCCC
33.9123401153
1526O-linked_GlycosylationVPGITPSSSSRTRTP
CCCCCCCCCCCCCCC
33.2730059200
1526PhosphorylationVPGITPSSSSRTRTP
CCCCCCCCCCCCCCC
33.2730266825
1527O-linked_GlycosylationPGITPSSSSRTRTPA
CCCCCCCCCCCCCCC
28.3330059200
1527PhosphorylationPGITPSSSSRTRTPA
CCCCCCCCCCCCCCC
28.3330266825
1528O-linked_GlycosylationGITPSSSSRTRTPAS
CCCCCCCCCCCCCCC
39.3530059200
1528PhosphorylationGITPSSSSRTRTPAS
CCCCCCCCCCCCCCC
39.3530266825
1530PhosphorylationTPSSSSRTRTPASIN
CCCCCCCCCCCCCCC
40.6223927012
1532O-linked_GlycosylationSSSSRTRTPASINAT
CCCCCCCCCCCCCCC
23.6930059200
1532PhosphorylationSSSSRTRTPASINAT
CCCCCCCCCCCCCCC
23.6929255136
1535O-linked_GlycosylationSRTRTPASINATPAN
CCCCCCCCCCCCCCC
19.9930059200
1535PhosphorylationSRTRTPASINATPAN
CCCCCCCCCCCCCCC
19.9929255136
1539PhosphorylationTPASINATPANINLA
CCCCCCCCCCCCCHH
20.6023927012
1549PhosphorylationNINLADLTRAVNALP
CCCHHHHHHHHHHCC
19.6823403867
1553UbiquitinationADLTRAVNALPQNMT
HHHHHHHHHCCCCHH
34.4722505724
1562UbiquitinationLPQNMTSQMFSAIAA
CCCCHHHHHHHHHHH
27.9822505724
1580PhosphorylationQGQNPNATPAQWASS
CCCCCCCCHHHHHCC
26.2926074081
1614PhosphorylationPAQQPVATPLMTPSY
CCCCCCCCCCCCCCC
19.7226074081
1618PhosphorylationPVATPLMTPSYSYTT
CCCCCCCCCCCCCCC
19.4326074081
1620PhosphorylationATPLMTPSYSYTTPS
CCCCCCCCCCCCCCC
19.9726074081
1621PhosphorylationTPLMTPSYSYTTPSQ
CCCCCCCCCCCCCCC
13.6026074081
1622PhosphorylationPLMTPSYSYTTPSQP
CCCCCCCCCCCCCCC
21.9726074081
1623PhosphorylationLMTPSYSYTTPSQPI
CCCCCCCCCCCCCCC
13.3426074081
1641PhosphorylationQYHQLQASTTPQSAQ
CCEEECCCCCCCHHC
21.61-
1666PhosphorylationQRQQQPKSNSHAAID
HHHHCCCCCCCCHHH
50.6925159151
1668PhosphorylationQQQPKSNSHAAIDWG
HHCCCCCCCCHHHHH
22.9228555341
1676AcetylationHAAIDWGKMAEQWLQ
CCHHHHHHHHHHHHH
30.5919608861
1676UbiquitinationHAAIDWGKMAEQWLQ
CCHHHHHHHHHHHHH
30.5929967540
1685UbiquitinationAEQWLQEKEAERRKQ
HHHHHHHHHHHHHHH
49.6222505724
1697PhosphorylationRKQKQRLTPRPSPSP
HHHHHCCCCCCCCCC
21.3123927012
1701PhosphorylationQRLTPRPSPSPMIES
HCCCCCCCCCCCEEC
39.0125159151
1703PhosphorylationLTPRPSPSPMIESTP
CCCCCCCCCCEECCC
31.2925159151
1708PhosphorylationSPSPMIESTPMSIAG
CCCCCEECCCCCCCC
27.2126503892
1709PhosphorylationPSPMIESTPMSIAGD
CCCCEECCCCCCCCC
15.3826503892
1712PhosphorylationMIESTPMSIAGDATP
CEECCCCCCCCCCCH
15.5323927012
1718PhosphorylationMSIAGDATPLLDEMD
CCCCCCCCHHCCCCC
21.1423927012

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
1523TPhosphorylationKinaseCDK2P24941
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SPT6H_HUMAN !!

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_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RPB1_HUMANPOLR2Aphysical
17234882
PAAF1_HUMANPAAF1physical
22316138
APC7_HUMANANAPC7physical
26344197
NUCL_HUMANNCLphysical
26344197
SPT4H_HUMANSUPT4H1physical
26344197
SPT5H_HUMANSUPT5Hphysical
26344197
BRE1B_HUMANRNF40physical
24441044

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SPT6H_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-743 AND LYS-1676, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-75; SER-78;THR-1532; SER-1535; THR-1539; THR-1697; SER-1701; SER-1703 ANDTHR-1718, AND MASS SPECTROMETRY.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7; SER-12; THR-1697 ANDTHR-1718, AND MASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-75; SER-78;SER-179; SER-267; THR-1523; SER-1526; THR-1532; SER-1535; THR-1539;SER-1701; SER-1703 AND THR-1718, AND MASS SPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1532; SER-1535;THR-1539; SER-1701 AND THR-1718, AND MASS SPECTROMETRY.
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-73; SER-75; SER-78 ANDSER-125, AND MASS SPECTROMETRY.

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