SOX6_HUMAN - dbPTM
SOX6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SOX6_HUMAN
UniProt AC P35712
Protein Name Transcription factor SOX-6
Gene Name SOX6
Organism Homo sapiens (Human).
Sequence Length 828
Subcellular Localization Nucleus .
Protein Description Transcriptional activator. Binds specifically to the DNA sequence 5'-AACAAT-3'. Plays a key role in several developmental processes, including neurogenesis and skeleton formation..
Protein Sequence MSSKQATSPFACAADGEDAMTQDLTSREKEEGSDQHVASHLPLHPIMHNKPHSEELPTLVSTIQQDADWDSVLSSQQRMESENNKLCSLYSFRNTSTSPHKPDEGSRDREIMTSVTFGTPERRKGSLADVVDTLKQKKLEEMTRTEQEDSSCMEKLLSKDWKEKMERLNTSELLGEIKGTPESLAEKERQLSTMITQLISLREQLLAAHDEQKKLAASQIEKQRQQMDLARQQQEQIARQQQQLLQQQHKINLLQQQIQVQGHMPPLMIPIFPHDQRTLAAAAAAQQGFLFPPGITYKPGDNYPVQFIPSTMAAAAASGLSPLQLQKGHVSHPQINQRLKGLSDRFGRNLDTFEHGGGHSYNHKQIEQLYAAQLASMQVSPGAKMPSTPQPPNTAGTVSPTGIKNEKRGTSPVTQVKDEAAAQPLNLSSRPKTAEPVKSPTSPTQNLFPASKTSPVNLPNKSSIPSPIGGSLGRGSSLDILSSLNSPALFGDQDTVMKAIQEARKMREQIQREQQQQQPHGVDGKLSSINNMGLNSCRNEKERTRFENLGPQLTGKSNEDGKLGPGVIDLTRPEDAEGSKAMNGSAAKLQQYYCWPTGGATVAEARVYRDARGRASSEPHIKRPMNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKSMSNQEKQPYYEEQARLSKIHLEKYPNYKYKPRPKRTCIVDGKKLRIGEYKQLMRSRRQEMRQFFTVGQQPQIPITTGTGVVYPGAITMATTTPSPQMTSDCSSTSASPEPSLPVIQSTYGMKTDGGSLAGNEMINGEDEMEMYDDYEDDPKSDYSSENEAPEAVSAN
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
7Phosphorylation-MSSKQATSPFACAA
-CCCCCCCCCCCCCC		34.1427251275
8PhosphorylationMSSKQATSPFACAAD
CCCCCCCCCCCCCCC		22.4929116813
21PhosphorylationADGEDAMTQDLTSRE
CCCCCHHHCCCHHHH		22.2027251275
25PhosphorylationDAMTQDLTSREKEEG
CHHHCCCHHHHHHCC		33.74-
95PhosphorylationSLYSFRNTSTSPHKP
EEEEEECCCCCCCCC		29.1728348404
96PhosphorylationLYSFRNTSTSPHKPD
EEEEECCCCCCCCCC		30.3629116813
97PhosphorylationYSFRNTSTSPHKPDE
EEEECCCCCCCCCCC		44.2129116813
98PhosphorylationSFRNTSTSPHKPDEG
EEECCCCCCCCCCCC		25.4429116813
106PhosphorylationPHKPDEGSRDREIMT
CCCCCCCCCCCHHHH		29.03-
109PhosphorylationPDEGSRDREIMTSVT
CCCCCCCCHHHHEEE		33.9427251275
111PhosphorylationEGSRDREIMTSVTFG
CCCCCCHHHHEEECC		3.67-
113PhosphorylationSRDREIMTSVTFGTP
CCCCHHHHEEECCCC		26.2129255136
114PhosphorylationRDREIMTSVTFGTPE
CCCHHHHEEECCCCC		11.2029255136
116PhosphorylationREIMTSVTFGTPERR
CHHHHEEECCCCCCC		19.0029255136
119PhosphorylationMTSVTFGTPERRKGS
HHEEECCCCCCCCCC		20.1329255136
126PhosphorylationTPERRKGSLADVVDT
CCCCCCCCHHHHHHH		24.3429255136
132PhosphorylationGSLADVVDTLKQKKL
CCHHHHHHHHHHHHH		46.2824719451
133PhosphorylationSLADVVDTLKQKKLE
CHHHHHHHHHHHHHH		25.0123312004
139PhosphorylationDTLKQKKLEEMTRTE
HHHHHHHHHHHHCHH		9.6824719451
159UbiquitinationCMEKLLSKDWKEKME
HHHHHHCHHHHHHHH		68.52-
170PhosphorylationEKMERLNTSELLGEI
HHHHHCCHHHHHHHH		28.3325850435
171PhosphorylationKMERLNTSELLGEIK
HHHHCCHHHHHHHHC		25.7725850435
184PhosphorylationIKGTPESLAEKERQL
HCCCHHHHHHHHHHH		7.32-
193PhosphorylationEKERQLSTMITQLIS
HHHHHHHHHHHHHHH		22.6124043423
196PhosphorylationRQLSTMITQLISLRE
HHHHHHHHHHHHHHH		13.3924043423
200PhosphorylationTMITQLISLREQLLA
HHHHHHHHHHHHHHH		29.9324043423
340UbiquitinationPQINQRLKGLSDRFG
HHHHHHHHHHHHHHC		61.0529967540
353UbiquitinationFGRNLDTFEHGGGHS
HCCCCCCCCCCCCCC		6.96-
376PhosphorylationLYAAQLASMQVSPGA
HHHHHHHHCCCCCCC		20.5228348404
380PhosphorylationQLASMQVSPGAKMPS
HHHHCCCCCCCCCCC		10.7525850435
387PhosphorylationSPGAKMPSTPQPPNT
CCCCCCCCCCCCCCC		49.5829255136
388PhosphorylationPGAKMPSTPQPPNTA
CCCCCCCCCCCCCCC		21.7729255136
393PhosphorylationPSTPQPPNTAGTVSP
CCCCCCCCCCCCCCC		49.6027251275
394PhosphorylationSTPQPPNTAGTVSPT
CCCCCCCCCCCCCCC		32.0329255136
397PhosphorylationQPPNTAGTVSPTGIK
CCCCCCCCCCCCCCC		18.4929255136
398PhosphorylationPPNTAGTVSPTGIKN
CCCCCCCCCCCCCCC		6.7133259812
399PhosphorylationPNTAGTVSPTGIKNE
CCCCCCCCCCCCCCC		19.3129255136
401PhosphorylationTAGTVSPTGIKNEKR
CCCCCCCCCCCCCCC		43.9929255136
404SumoylationTVSPTGIKNEKRGTS
CCCCCCCCCCCCCCC		61.47-
404SumoylationTVSPTGIKNEKRGTS
CCCCCCCCCCCCCCC		61.47-
410PhosphorylationIKNEKRGTSPVTQVK
CCCCCCCCCCCCCCC		33.6129255136
411PhosphorylationKNEKRGTSPVTQVKD
CCCCCCCCCCCCCCH		21.8729255136
412PhosphorylationNEKRGTSPVTQVKDE
CCCCCCCCCCCCCHH		32.7727251275
414PhosphorylationKRGTSPVTQVKDEAA
CCCCCCCCCCCHHHH		30.9129255136
417SumoylationTSPVTQVKDEAAAQP
CCCCCCCCHHHHCCC		39.78-
417SumoylationTSPVTQVKDEAAAQP
CCCCCCCCHHHHCCC		39.78-
423PhosphorylationVKDEAAAQPLNLSSR
CCHHHHCCCCCCCCC		37.9827251275
424PhosphorylationKDEAAAQPLNLSSRP
CHHHHCCCCCCCCCC		20.6324719451
430SumoylationQPLNLSSRPKTAEPV
CCCCCCCCCCCCCCC		33.10-
433PhosphorylationNLSSRPKTAEPVKSP
CCCCCCCCCCCCCCC		38.6523090842
439PhosphorylationKTAEPVKSPTSPTQN
CCCCCCCCCCCCCCC		33.3728348404
441PhosphorylationAEPVKSPTSPTQNLF
CCCCCCCCCCCCCCC		55.2029507054
442PhosphorylationEPVKSPTSPTQNLFP
CCCCCCCCCCCCCCC		29.3628355574
444PhosphorylationVKSPTSPTQNLFPAS
CCCCCCCCCCCCCCC		29.8329507054
451PhosphorylationTQNLFPASKTSPVNL
CCCCCCCCCCCCCCC		36.3823090842
452PhosphorylationQNLFPASKTSPVNLP
CCCCCCCCCCCCCCC		55.94-
453PhosphorylationNLFPASKTSPVNLPN
CCCCCCCCCCCCCCC		35.4528857561
454PhosphorylationLFPASKTSPVNLPNK
CCCCCCCCCCCCCCC		30.5019413330
455PhosphorylationFPASKTSPVNLPNKS
CCCCCCCCCCCCCCC		25.0127251275
457PhosphorylationASKTSPVNLPNKSSI
CCCCCCCCCCCCCCC		53.8424719451
462PhosphorylationPVNLPNKSSIPSPIG
CCCCCCCCCCCCCCC		39.8928555341
466PhosphorylationPNKSSIPSPIGGSLG
CCCCCCCCCCCCCCC		27.7229507054
467PhosphorylationNKSSIPSPIGGSLGR
CCCCCCCCCCCCCCC		24.7219413330
471PhosphorylationIPSPIGGSLGRGSSL
CCCCCCCCCCCCCHH		23.5725072903
474MethylationPIGGSLGRGSSLDIL
CCCCCCCCCCHHHHH		47.30115917557
476PhosphorylationGGSLGRGSSLDILSS
CCCCCCCCHHHHHHH		26.7728348404
477PhosphorylationGSLGRGSSLDILSSL
CCCCCCCHHHHHHHC		32.6529507054
479PhosphorylationLGRGSSLDILSSLNS
CCCCCHHHHHHHCCC		41.5524719451
486PhosphorylationDILSSLNSPALFGDQ
HHHHHCCCCHHHCCH		19.49-
487MethylationILSSLNSPALFGDQD
HHHHCCCCHHHCCHH		31.73-
616PhosphorylationRDARGRASSEPHIKR
HHCCCCCCCCCCCCC		33.6024702127
617PhosphorylationDARGRASSEPHIKRP
HCCCCCCCCCCCCCC		54.9124702127
671PhosphorylationNQEKQPYYEEQARLS
CCCCCCHHHHHHHHH		21.48-
678PhosphorylationYEEQARLSKIHLEKY
HHHHHHHHHHHHHHC		24.8227251275
691PhosphorylationKYPNYKYKPRPKRTC
HCCCCCCCCCCCCEE		30.33-
697PhosphorylationYKPRPKRTCIVDGKK
CCCCCCCEEEECCCE		16.83-
716PhosphorylationEYKQLMRSRRQEMRQ
HHHHHHHHHHHHHHH		20.18-
759PhosphorylationTTPSPQMTSDCSSTS
CCCCCCCCCCCCCCC		19.03-
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
-KUbiquitinationE3 ubiquitin ligaseTRIP12Q14669
PMID:23663701
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SOX6_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 SOX6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CTBP2_HUMANCTBP2physical
11504872
CENPK_HUMANCENPKphysical
10996314
CTNB1_HUMANCTNNB1physical
17412698
HDAC1_HUMANHDAC1physical
17412698
TRIPC_HUMANTRIP12physical
23663701
ZN184_HUMANZNF184physical
21988832
TAF4_HUMANTAF4physical
23884650
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 SOX6_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-454, AND MASSSPECTROMETRY.
Sumoylation
ReferencePubMed
"Repression of SOX6 transcriptional activity by SUMO modification.";
Fernandez-Lloris R., Osses N., Jaffray E., Shen L.N., Vaughan O.A.,Girwood D., Bartrons R., Rosa J.L., Hay R.T., Ventura F.;
FEBS Lett. 580:1215-1221(2006).
Cited for: SUMOYLATION AT LYS-404 AND LYS-417, MUTAGENESIS OF LYS-404 ANDLYS-417, AND SUBCELLULAR LOCATION.

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