STAT6_HUMAN - dbPTM
STAT6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAT6_HUMAN
UniProt AC P42226
Protein Name Signal transducer and activator of transcription 6
Gene Name STAT6
Organism Homo sapiens (Human).
Sequence Length 847
Subcellular Localization Cytoplasm. Nucleus. Translocated into the nucleus in response to phosphorylation.
Protein Description Carries out a dual signal transduction and activation of transcription. Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling..
Protein Sequence MSLWGLVSKMPPEKVQRLYVDFPQHLRHLLGDWLESQPWEFLVGSDAFCCNLASALLSDTVQHLQASVGEQGEGSTILQHISTLESIYQRDPLKLVATFRQILQGEKKAVMEQFRHLPMPFHWKQEELKFKTGLRRLQHRVGEIHLLREALQKGAEAGQVSLHSLIETPANGTGPSEALAMLLQETTGELEAAKALVLKRIQIWKRQQQLAGNGAPFEESLAPLQERCESLVDIYSQLQQEVGAAGGELEPKTRASLTGRLDEVLRTLVTSCFLVEKQPPQVLKTQTKFQAGVRFLLGLRFLGAPAKPPLVRADMVTEKQARELSVPQGPGAGAESTGEIINNTVPLENSIPGNCCSALFKNLLLKKIKRCERKGTESVTEEKCAVLFSASFTLGPGKLPIQLQALSLPLVVIVHGNQDNNAKATILWDNAFSEMDRVPFVVAERVPWEKMCETLNLKFMAEVGTNRGLLPEHFLFLAQKIFNDNSLSMEAFQHRSVSWSQFNKEILLGRGFTFWQWFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHVIRGQDGSPQIENIQPFSAKDLSIRSLGDRIRDLAQLKNLYPKKPKDEAFRSHYKPEQMGKDGRGYVPATIKMTVERDQPLPTPELQMPTMVPSYDLGMAPDSSMSMQLGPDMVPQVYPPHSHSIPPYQGLSPEESVNVLSAFQEPHLQMPPSLGQMSLPFDQPHPQGLLPCQPQEHAVSSPDPLLCSDVTMVEDSCLSQPVTAFPQGTWIGEDIFPPLLPPTEQDLTKLLLEGQGESGGGSLGAQPLLQPSHYGQSGISMSHMDLRANPSW
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
2Phosphorylation------MSLWGLVSK
------CCCCHHHCC		32.5920068231
2Acetylation------MSLWGLVSK
------CCCCHHHCC		32.5922223895
8PhosphorylationMSLWGLVSKMPPEKV
CCCCHHHCCCCHHHH		28.4220068231
9UbiquitinationSLWGLVSKMPPEKVQ
CCCHHHCCCCHHHHH		48.20-
19PhosphorylationPEKVQRLYVDFPQHL
HHHHHHHHCCCHHHH		10.5227642862
27MethylationVDFPQHLRHLLGDWL
CCCHHHHHHHHHHHH		19.11-
107UbiquitinationRQILQGEKKAVMEQF
HHHHHHCHHHHHHHH		53.51-
108UbiquitinationQILQGEKKAVMEQFR
HHHHHCHHHHHHHHH		41.74-
124UbiquitinationLPMPFHWKQEELKFK
CCCCCCCCHHHHHHH		38.98-
129UbiquitinationHWKQEELKFKTGLRR
CCCHHHHHHHHHHHH		48.36-
230PhosphorylationPLQERCESLVDIYSQ
HHHHHHHHHHHHHHH		37.0028348404
252UbiquitinationAGGELEPKTRASLTG
CCCCCCCCHHHHHHH		41.07-
277UbiquitinationTSCFLVEKQPPQVLK
HHHHHHCCCCCCHHC		61.70-
284UbiquitinationKQPPQVLKTQTKFQA
CCCCCHHCCCCCHHH		39.47-
288UbiquitinationQVLKTQTKFQAGVRF
CHHCCCCCHHHHHHH		26.17-
288MalonylationQVLKTQTKFQAGVRF
CHHCCCCCHHHHHHH		26.1726320211
288AcetylationQVLKTQTKFQAGVRF
CHHCCCCCHHHHHHH		26.1725953088
307UbiquitinationRFLGAPAKPPLVRAD
HHCCCCCCCCCEECC		46.22-
319AcetylationRADMVTEKQARELSV
ECCCCCHHHHHHCCC		39.6325953088
319UbiquitinationRADMVTEKQARELSV
ECCCCCHHHHHHCCC		39.63-
361UbiquitinationNCCSALFKNLLLKKI
CHHHHHHHHHHHHHH		47.76-
366UbiquitinationLFKNLLLKKIKRCER
HHHHHHHHHHHHHHH		53.04-
367UbiquitinationFKNLLLKKIKRCERK
HHHHHHHHHHHHHHC		54.12-
407PhosphorylationPIQLQALSLPLVVIV
CHHEEECCCCEEEEE		30.8422000020
421 (in isoform 2)Ubiquitination-51.6221906983
450UbiquitinationAERVPWEKMCETLNL
EECCCHHHHHHHCCC		45.01-
496PhosphorylationMEAFQHRSVSWSQFN
HHHHHCCCCCHHHHC		20.5523403867
498PhosphorylationAFQHRSVSWSQFNKE
HHHCCCCCHHHHCHH		23.4323403867
500PhosphorylationQHRSVSWSQFNKEIL
HCCCCCHHHHCHHHH		19.8623403867
504UbiquitinationVSWSQFNKEILLGRG
CCHHHHCHHHHHCCC		47.63-
525PhosphorylationFDGVLDLTKRCLRSY
HHHHHHHHHHHHHHH		18.99-
595 (in isoform 1)Ubiquitination-58.9921906983
595UbiquitinationNIQPFSAKDLSIRSL
CCCCCCHHHCCHHHH		58.992190698
598PhosphorylationPFSAKDLSIRSLGDR
CCCHHHCCHHHHHHH		26.5324719451
613UbiquitinationIRDLAQLKNLYPKKP
HHHHHHHHHHCCCCC		32.59-
621UbiquitinationNLYPKKPKDEAFRSH
HHCCCCCCCHHHHHH		76.66-
630UbiquitinationEAFRSHYKPEQMGKD
HHHHHHCCHHHCCCC		36.33-
634SulfoxidationSHYKPEQMGKDGRGY
HHCCHHHCCCCCCCC		7.4030846556
636UbiquitinationYKPEQMGKDGRGYVP
CCHHHCCCCCCCCCC		52.22-
641PhosphorylationMGKDGRGYVPATIKM
CCCCCCCCCCEEEEE		11.2522322096
645PhosphorylationGRGYVPATIKMTVER
CCCCCCEEEEEEEEC		18.3022817900
647UbiquitinationGYVPATIKMTVERDQ
CCCCEEEEEEEECCC		24.94-
647AcetylationGYVPATIKMTVERDQ
CCCCEEEEEEEECCC		24.9425953088
707PhosphorylationIPPYQGLSPEESVNV
CCCCCCCCHHHHHHH		36.7721123173
755PhosphorylationQPQEHAVSSPDPLLC
CCCCCCCCCCCCCCC		36.6226074081
756PhosphorylationPQEHAVSSPDPLLCS
CCCCCCCCCCCCCCC		27.0726074081
763PhosphorylationSPDPLLCSDVTMVED
CCCCCCCCCCEEEEC		34.7826074081
813PhosphorylationLLEGQGESGGGSLGA
HHCCCCCCCCCCCCC		49.9528857561
817PhosphorylationQGESGGGSLGAQPLL
CCCCCCCCCCCCCCC		27.2328555341
827PhosphorylationAQPLLQPSHYGQSGI
CCCCCCCCCCCCCCC		19.1724247654
832PhosphorylationQPSHYGQSGISMSHM
CCCCCCCCCCCCCCC		33.4628857561
837PhosphorylationGQSGISMSHMDLRAN
CCCCCCCCCCCCCCC		14.6328857561
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
407SPhosphorylationKinaseTBK1Q9UHD2
PSP
641YPhosphorylationKinaseJAK-FAMILY-GPS
641YPhosphorylationKinaseJAK-Uniprot
641YPhosphorylationKinaseJAK_GROUP-PhosphoELM
707SPhosphorylationKinaseMAPK8P45983
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAT6_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 STAT6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NCOA1_HUMANNCOA1physical
11574547
NCOA1_HUMANNCOA1genetic
11574547
CBP_HUMANCREBBPphysical
11574547
EP300_HUMANEP300genetic
10454341
CBP_HUMANCREBBPgenetic
10454341
EP300_HUMANEP300physical
10454341
NCOA1_HUMANNCOA1physical
12138096
NFKB1_HUMANNFKB1physical
9584180
SND1_HUMANSND1physical
12234934
ANXA2_HUMANANXA2physical
20121258
TIF1A_HUMANTRIM24physical
20211142
DAZP2_HUMANDAZAP2physical
20211142
CEBPZ_HUMANCEBPZphysical
20211142
WWP1_HUMANWWP1physical
20211142
RNF12_HUMANRLIMphysical
20211142
ANKZ1_HUMANANKZF1physical
20211142
ZN407_HUMANZNF407physical
20211142
ZBTB2_HUMANZBTB2physical
20211142
ZNF92_HUMANZNF92physical
20211142
NCOA1_HUMANNCOA1physical
15695802
NCOA3_HUMANNCOA3physical
15145939
NCOA1_HUMANNCOA1physical
14757047
NCOA2_HUMANNCOA2physical
14757047
JUN_HUMANJUNphysical
21357535
SFPQ_HUMANSFPQphysical
21106524
FCER2_HUMANFCER2physical
21081493
STAT2_HUMANSTAT2physical
10490982
PTN2_HUMANPTPN2physical
17210636
IL4RA_HUMANIL4Rphysical
9392697
LITAF_HUMANLITAFphysical
15793005
API5_HUMANAPI5physical
22863883
EHD1_HUMANEHD1physical
22863883
PDE12_HUMANPDE12physical
22863883
PGTB1_HUMANPGGT1Bphysical
22863883
PPARG_HUMANPPARGphysical
21093321
EP300_HUMANEP300physical
23461825
KDM3A_HUMANKDM3Aphysical
26344197
FCL_HUMANTSTA3physical
26344197
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 STAT6_HUMAN

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Related Literatures of Post-Translational Modification

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