JUN_RAT - dbPTM
JUN_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID JUN_RAT
UniProt AC P17325
Protein Name Transcription factor AP-1
Gene Name Jun
Organism Rattus norvegicus (Rat).
Sequence Length 334
Subcellular Localization Nucleus .
Protein Description Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3'. Promotes activity of NR5A1 when phosphorylated by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation. Involved in activated KRAS-mediated transcriptional activation of USP28 in colorectal cancer (CRC) cells. Binds to the USP28 promoter in colorectal cancer (CRC) cells..
Protein Sequence MTAKMETTFYDDALNASFLQSESGAYGYSNPKILKQSMTLNLADPVGNLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVSGAGMVAPAVASVAGAGGGGGYSASLHSEPPVYANLSNFNPGALSSGGGAPSYGATGLAFPSQPQQQQQPPQPPHHLPQQIPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF
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------MTAKMETTF
------CCCCCCCEE
34.68-
8PhosphorylationMTAKMETTFYDDALN
CCCCCCCEEHHHHHC
13.5926022182
26PhosphorylationLQSESGAYGYSNPKI
HCCCCCCCCCCCHHH
21.8126022182
28PhosphorylationSESGAYGYSNPKILK
CCCCCCCCCCHHHHH
7.8126022182
56AcetylationLKPHLRAKNSDLLTS
CCHHHHHCCCCCCCC
51.02-
58PhosphorylationPHLRAKNSDLLTSPD
HHHHHCCCCCCCCCC
29.0028689409
62PhosphorylationAKNSDLLTSPDVGLL
HCCCCCCCCCCCCHH
45.5727097102
63PhosphorylationKNSDLLTSPDVGLLK
CCCCCCCCCCCCHHH
21.0516831194
73PhosphorylationVGLLKLASPELERLI
CCHHHHCCHHHHHEE
29.371749429
83PhosphorylationLERLIIQSSNGHITT
HHHEEEECCCCCEEC
18.5028689409
84PhosphorylationERLIIQSSNGHITTT
HHEEEECCCCCEECC
30.3828689409
89PhosphorylationQSSNGHITTTPTPTQ
ECCCCCEECCCCCCE
20.9528689409
90PhosphorylationSSNGHITTTPTPTQF
CCCCCEECCCCCCEE
30.1228689409
91PhosphorylationSNGHITTTPTPTQFL
CCCCEECCCCCCEEE
19.2628689409
93PhosphorylationGHITTTPTPTQFLCP
CCEECCCCCCEEECC
36.5528689409
95PhosphorylationITTTPTPTQFLCPKN
EECCCCCCEEECCCC
34.1428689409
234PhosphorylationALKEEPQTVPEMPGE
HHHHCCCCCCCCCCC
49.0628689409
242PhosphorylationVPEMPGETPPLSPID
CCCCCCCCCCCCCCC
35.8021630457
246PhosphorylationPGETPPLSPIDMESQ
CCCCCCCCCCCHHHH
26.111651323
252PhosphorylationLSPIDMESQERIKAE
CCCCCHHHHHHHHHH
30.6122668510
274AcetylationIAASKCRKRKLERIA
HHHHHHHHHHHHHHH
64.45-
289PhosphorylationRLEEKVKTLKAQNSE
HHHHHHHHHHHHCHH
36.16-

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
2TPhosphorylationKinasePAK2Q64303
Uniprot
8TPhosphorylationKinasePAK2Q64303
Uniprot
63SPhosphorylationKinaseCDK1P06493
PSP
63SPhosphorylationKinaseCSNK2A1P19139
GPS
63SPhosphorylationKinasePLK3Q9R011
Uniprot
63SPhosphorylationKinaseMAPK8P49185
Uniprot
73SPhosphorylationKinaseCDK1P06493
PSP
73SPhosphorylationKinasePLK3Q9R011
Uniprot
73SPhosphorylationKinaseJNK1P49185
PSP
73SPhosphorylationKinaseCSNK2A1P19139
GPS
89TPhosphorylationKinasePAK2Q64303
Uniprot
93TPhosphorylationKinasePAK2Q64303
Uniprot
242TPhosphorylationKinaseGSK3-BETAP18266
Uniprot
246SPhosphorylationKinaseMAPK3P21708
GPS
246SPhosphorylationKinaseMAPK1P28482
GPS
246SPhosphorylationKinaseGSK3-BETAP18266
Uniprot
246SPhosphorylationKinaseCDK1P06493
PSP
246SPhosphorylationKinaseDYRK2-Uniprot
252SPhosphorylationKinaseGSK3-BETAP18266
Uniprot
289TPhosphorylationKinasePAK2Q64303
Uniprot
-KUbiquitinationE3 ubiquitin ligaseMap3k1Q62925
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
242TPhosphorylation

-
242TPhosphorylation

-
246SPhosphorylation

-
246SPhosphorylation

-
252SPhosphorylation

-
271KAcetylation

-

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 JUN_RAT !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

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

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Related Literatures of Post-Translational Modification

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