FRAT1_HUMAN - dbPTM
FRAT1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID FRAT1_HUMAN
UniProt AC Q92837
Protein Name Proto-oncogene FRAT1
Gene Name FRAT1
Organism Homo sapiens (Human).
Sequence Length 279
Subcellular Localization Cytoplasm.
Protein Description Positively regulates the Wnt signaling pathway by stabilizing beta-catenin through the association with GSK-3. May play a role in tumor progression and collaborate with PIM1 and MYC in lymphomagenesis..
Protein Sequence MPCRREEEEEAGEEAEGEEEEEDSFLLLQQSVALGSSGEVDRLVAQIGETLQLDAAQHSPASPCGPPGAPLRAPGPLAAAVPADKARSPAVPLLLPPALAETVGPAPPGVLRCALGDRGRVRGRAAPYCVAELATGPSALSPLPPQADLDGPPGAGKQGIPQPLSGPCRRGWLRGAAASRRLQQRRGSQPETRTGDDDPHRLLQQLVLSGNLIKEAVRRLHSRRLQLRAKLPQRPLLGPLSAPVHEPPSPRSPRAACSDPGASGRAQLRTGDGVLVPGS
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
88PhosphorylationVPADKARSPAVPLLL
CCCCHHCCCCCCCCC
23.2828450419
128PhosphorylationVRGRAAPYCVAELAT
CCCCCCCCEEEHHHC
8.5322210691
135PhosphorylationYCVAELATGPSALSP
CEEEHHHCCCCCCCC
63.3522210691
138PhosphorylationAELATGPSALSPLPP
EHHHCCCCCCCCCCC
43.0922210691
179PhosphorylationWLRGAAASRRLQQRR
HHHHHHHHHHHHHHC
17.1330206219
188PhosphorylationRLQQRRGSQPETRTG
HHHHHCCCCCCCCCC
40.5322817900
214UbiquitinationVLSGNLIKEAVRRLH
HHCCHHHHHHHHHHH
42.67-
241PhosphorylationRPLLGPLSAPVHEPP
CCCCCCCCCCCCCCC
33.3927080861
249PhosphorylationAPVHEPPSPRSPRAA
CCCCCCCCCCCCCHH
43.6024719451
252PhosphorylationHEPPSPRSPRAACSD
CCCCCCCCCCHHCCC
23.32-
258PhosphorylationRSPRAACSDPGASGR
CCCCHHCCCCCCCCC
41.9628348404
279PhosphorylationDGVLVPGS-------
CCCCCCCC-------
30.8623403867

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
188SPhosphorylationKinaseGSK3BP49841
PSP
188SPhosphorylationKinasePRKACAP17612
GPS
188SPhosphorylationKinasePRKCAP17252
GPS

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of FRAT1_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 FRAT1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DVL1_HUMANDVL1physical
10428961
GASP2_HUMANGPRASP2physical
21988832
LAMC3_HUMANLAMC3physical
21988832
K1C18_HUMANKRT18physical
21988832
GRN_HUMANGRNphysical
21988832
PLS1_HUMANPLSCR1physical
21988832
PSA3_HUMANPSMA3physical
21988832
LTBP4_HUMANLTBP4physical
21988832
KCNK5_HUMANKCNK5physical
21988832
LMAN2_HUMANLMAN2physical
21988832
TDRD7_HUMANTDRD7physical
21988832
RABE2_HUMANRABEP2physical
21988832
GSK3A_HUMANGSK3Aphysical
26496610
GSK3B_HUMANGSK3Bphysical
26496610
RASK_HUMANKRASphysical
26496610
PIAS1_HUMANPIAS1physical
26496610

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 FRAT1_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-88, AND MASSSPECTROMETRY.

TOP