STAT6_MOUSE - dbPTM
STAT6_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID STAT6_MOUSE
UniProt AC P52633
Protein Name Signal transducer and transcription activator 6
Gene Name Stat6
Organism Mus musculus (Mouse).
Sequence Length 837
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 MSLWGLISKMSPEKLQRLYVDFPQRLRHLLADWLESQPWEFLVGSDAFCYNMASALLSATVQRLQATAGEQGKGNSILPHISTLESIYQRDPLKLVATIRQILQGEKKAVIEEFRHLPGPFHRKQEELKFTTALGRLQHRVRETRLLRESLQQGAKTGQVSLQNLIDPPVNGPGPSEDLATMLQGTVGDLEATQALVLKRIQIWKRQQQLAGNGTPFEESLAGLQERCESLVEIYSQLQQEIGAASGELEPKTRASLISRLDEVLRTLVTSSFLVEKQPPQVLKTQTKFQAGVRFLLGLQFLGTSAKPPMVRADMVTEKQARELSLAQGPGTGVESTGEIMNNTVPLENSIPSNCCSALFKNLLLKKIKRCERKGTESVTEEKCAVLFSTSFTLGPNKLLIQLQALSLPLVVIVHGNQDNNAKATILWDNAFSEMDRVPFVVAERVPWEKMCETLNLKFMAEVGTSRGLLPEHFLFLAQKIFNDNSLSVEAFQHRCVSWSQFNKEILLGRGFTFWQWFDGVLDLTKRCLRSYWSDRLIIGFISKQYVTSLLLNEPDGTFLLRFSDSEIGGITIAHVIRGQDGSSQIENIQPFSAKDLSIRSLGDRIRDLAQLKNLYPKKPKDEAFRSHYKPEQMGKDGRGYVSTTIKMTVERDQPLPTPEPQMPAMVPPYDLGMAPDASMQLSSDMGYPPQSIHSFQSLEESMSVLPSFQEPHLQMPPNMSQITMPFDQPHPQGLLQCQSQEHAVSSPEPMLCSDVTMVEDSCLTQPVGGFPQGTWVSEDMYPPLMPPTEQDLTKLLLENQGEAGGSLGSQPLLQPSPYGQSGISLSHLDLRTNPSW
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------MSLWGLISK
------CCHHHHHHH
32.59-
8PhosphorylationMSLWGLISKMSPEKL
CCHHHHHHHCCHHHH
27.6126643407
11PhosphorylationWGLISKMSPEKLQRL
HHHHHHCCHHHHHHH
33.3726643407
27MethylationVDFPQRLRHLLADWL
CCHHHHHHHHHHHHH
22.168516401
94UbiquitinationIYQRDPLKLVATIRQ
HHHCCHHHHHHHHHH
46.4322790023
129AcetylationHRKQEELKFTTALGR
CCCHHHHHHHHHHHH
43.906566289
277UbiquitinationTSSFLVEKQPPQVLK
HHHHHCCCCCCCCCC
61.7022790023
376PhosphorylationKRCERKGTESVTEEK
HHHHHCCCCCCCHHH
28.2828576409
558PhosphorylationLLNEPDGTFLLRFSD
HHCCCCCEEEEEEEC
20.6322871156
595UbiquitinationNIQPFSAKDLSIRSL
CCCCCCHHHCCHHHH
58.9922790023
619AcetylationLKNLYPKKPKDEAFR
HHHHCCCCCCCHHHH
53.4419850915
621AcetylationNLYPKKPKDEAFRSH
HHCCCCCCCHHHHHH
76.6619850925
641PhosphorylationMGKDGRGYVSTTIKM
CCCCCCCEEEEEEEE
7.0012244176
643PhosphorylationKDGRGYVSTTIKMTV
CCCCCEEEEEEEEEE
16.0225367039
807PhosphorylationNQGEAGGSLGSQPLL
HCCCCCCCCCCCCCC
28.7423984901
810PhosphorylationEAGGSLGSQPLLQPS
CCCCCCCCCCCCCCC
33.6423984901
817PhosphorylationSQPLLQPSPYGQSGI
CCCCCCCCCCCCCCC
20.1423984901
819PhosphorylationPLLQPSPYGQSGISL
CCCCCCCCCCCCCCC
31.9423984901
822PhosphorylationQPSPYGQSGISLSHL
CCCCCCCCCCCCHHC
33.4623984901
825PhosphorylationPYGQSGISLSHLDLR
CCCCCCCCCHHCCCC
27.6123984901
827PhosphorylationGQSGISLSHLDLRTN
CCCCCCCHHCCCCCC
18.4023984901

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
641YPhosphorylationKinaseJAK-Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of STAT6_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 STAT6_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
STAT6_MOUSEStat6physical
20211142
PAR14_MOUSEParp14physical
16537510
LITAF_MOUSELitafphysical
15793005
RN128_MOUSERnf128physical
25145352

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of STAT6_MOUSE

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Related Literatures of Post-Translational Modification

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