PTEN_MOUSE - dbPTM
PTEN_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID PTEN_MOUSE
UniProt AC O08586
Protein Name Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
Gene Name Pten
Organism Mus musculus (Mouse).
Sequence Length 403
Subcellular Localization Cytoplasm . Nucleus . Nucleus, PML body . Monoubiquitinated form is nuclear (By similarity). Nonubiquitinated form is cytoplasmic (By similarity). Colocalized with PML and USP7 in PML nuclear bodies (By similarity). XIAP/BIRC4 promotes its nuclear lo
Protein Description In motile cells, suppresses the formation of lateral pseudopods and thereby promotes cell polarization and directed movement (By similarity). Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1,3,4,5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3,4,5)P3 > PtdIns(3,4)P2 > PtdIns3P > Ins(1,3,4,5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. Plays a role as a key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue. The nuclear monoubiquitinated form possesses greater apoptotic potential, whereas the cytoplasmic nonubiquitinated form induces less tumor suppressive ability..
Protein Sequence MTAIIKEIVSRNKRRYQEDGFDLDLTYIYPNIIAMGFPAERLEGVYRNNIDDVVRFLDSKHKNHYKIYNLCAERHYDTAKFNCRVAQYPFEDHNPPQLELIKPFCEDLDQWLSEDDNHVAAIHCKAGKGRTGVMICAYLLHRGKFLKAQEALDFYGEVRTRDKKGVTIPSQRRYVYYYSYLLKNHLDYRPVALLFHKMMFETIPMFSGGTCNPQFVVCQLKVKIYSSNSGPTRREDKFMYFEFPQPLPVCGDIKVEFFHKQNKMLKKDKMFHFWVNTFFIPGPEETSEKVENGSLCDQEIDSICSIERADNDKEYLVLTLTKNDLDKANKDKANRYFSPNFKVKLYFTKTVEEPSNPEASSSTSVTPDVSDNEPDHYRYSDTTDSDPENEPFDEDQHSQITKV
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------MTAIIKEIV
------CCHHHHHHH		26.94-
6Acetylation--MTAIIKEIVSRNK
--CCHHHHHHHHHCC		34.9622826441
46PhosphorylationAERLEGVYRNNIDDV
HHHCCCHHHCCHHHH		20.62-
66UbiquitinationSKHKNHYKIYNLCAE
HCCCCHHHHHHHHHH		31.0322790023
80UbiquitinationERHYDTAKFNCRVAQ
HHCCCCCCCCCEEEC		38.9222790023
170PhosphorylationKKGVTIPSQRRYVYY
CCCCCCCCCCHHHHH		32.2530482847
174PhosphorylationTIPSQRRYVYYYSYL
CCCCCCHHHHHHHHH		8.5922817900
176PhosphorylationPSQRRYVYYYSYLLK
CCCCHHHHHHHHHHH		6.4325293948
177PhosphorylationSQRRYVYYYSYLLKN
CCCHHHHHHHHHHHC		3.9525293948
178PhosphorylationQRRYVYYYSYLLKNH
CCHHHHHHHHHHHCC		3.5225293948
179PhosphorylationRRYVYYYSYLLKNHL
CHHHHHHHHHHHCCC		7.9925293948
180PhosphorylationRYVYYYSYLLKNHLD
HHHHHHHHHHHCCCC		10.4225293948
294PhosphorylationSEKVENGSLCDQEID
CCCCCCCCCCHHHHH		37.0925521595
302PhosphorylationLCDQEIDSICSIERA
CCHHHHHCCEEEEEC		31.0222324799
305PhosphorylationQEIDSICSIERADND
HHHHCCEEEEECCCC		26.3022324799
336PhosphorylationNKDKANRYFSPNFKV
CHHHCCCCCCCCEEE		14.28-
338PhosphorylationDKANRYFSPNFKVKL
HHCCCCCCCCEEEEE		15.2525338131
344MalonylationFSPNFKVKLYFTKTV
CCCCEEEEEEEEEEC		37.7526320211
361PhosphorylationPSNPEASSSTSVTPD
CCCCCCCCCCCCCCC		44.6925338131
362PhosphorylationSNPEASSSTSVTPDV
CCCCCCCCCCCCCCC		23.3925195567
363PhosphorylationNPEASSSTSVTPDVS
CCCCCCCCCCCCCCC		29.2125293948
364PhosphorylationPEASSSTSVTPDVSD
CCCCCCCCCCCCCCC		26.4125293948
366PhosphorylationASSSTSVTPDVSDNE
CCCCCCCCCCCCCCC		17.3425521595
370PhosphorylationTSVTPDVSDNEPDHY
CCCCCCCCCCCCCCC		41.9425521595
377PhosphorylationSDNEPDHYRYSDTTD
CCCCCCCCCCCCCCC		20.7325293948
379PhosphorylationNEPDHYRYSDTTDSD
CCCCCCCCCCCCCCC		12.0625619855
380PhosphorylationEPDHYRYSDTTDSDP
CCCCCCCCCCCCCCC		21.3425619855
382PhosphorylationDHYRYSDTTDSDPEN
CCCCCCCCCCCCCCC		26.9425619855
383PhosphorylationHYRYSDTTDSDPENE
CCCCCCCCCCCCCCC		38.2025521595
385PhosphorylationRYSDTTDSDPENEPF
CCCCCCCCCCCCCCC		53.6325521595
398PhosphorylationPFDEDQHSQITKV--
CCCHHHHHCCCCC--		20.0425619855
401PhosphorylationEDQHSQITKV-----
HHHHHCCCCC-----		20.3725293948
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
336YPhosphorylationKinaseFRKQ922K9
Uniprot
366TPhosphorylationKinaseGSK3BQ9WV60
PSP
366TPhosphorylationKinasePLK3Q60806
Uniprot
370SPhosphorylationKinaseCSNK2A1Q60737
GPS
370SPhosphorylationKinasePLK3Q60806
Uniprot
370SPhosphorylationKinaseCK2-FAMILY-GPS
370SPhosphorylationKinaseCK2-Uniprot
380SPhosphorylationKinaseROCK1P70335
Uniprot
382TPhosphorylationKinaseROCK1P70335
Uniprot
383TPhosphorylationKinaseROCK1P70335
Uniprot
398SPhosphorylationKinaseATMQ62388
PSP
-KUbiquitinationE3 ubiquitin ligaseNedd4P46935
PMID:22199232
-KUbiquitinationE3 ubiquitin ligaseXiapQ60989
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
13Kubiquitylation

19473982
289Kubiquitylation

19473982
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 PTEN_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
XIAP_MOUSEXiapphysical
19473982
FBXW7_MOUSEFbxw7genetic
22513362
NFIP1_MOUSENdfip1physical
23012657
P53_MOUSETrp53physical
18332125
IF4B_HUMANEIF4Bphysical
26496610
MTRR_HUMANMTRRphysical
26496610
RAD51_HUMANRAD51physical
26496610
LRP8_HUMANLRP8physical
26496610
BRAP_HUMANBRAPphysical
26496610
MPZL1_HUMANMPZL1physical
26496610
DCA13_HUMANDCAF13physical
26496610
ITSN2_HUMANITSN2physical
26496610
CC186_HUMANCCDC186physical
26496610
SERC1_HUMANSERINC1physical
26496610
NCK5L_HUMANNCKAP5Lphysical
26496610
BRAF_MOUSEBrafgenetic
27184621
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of PTEN_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Regulation of PTEN stability and activity by Plk3.";
Xu D., Yao Y., Jiang X., Lu L., Dai W.;
J. Biol. Chem. 285:39935-39942(2010).
Cited for: PHOSPHORYLATION AT THR-366 AND SER-370.
"ROCK1 functions as a suppressor of inflammatory cell migration byregulating PTEN phosphorylation and stability.";
Vemula S., Shi J., Hanneman P., Wei L., Kapur R.;
Blood 115:1785-1796(2010).
Cited for: PHOSPHORYLATION AT SER-380; THR-382 AND THR-383, AND INTERACTION WITHROCK1.
"Large-scale phosphorylation analysis of mouse liver.";
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-370 AND SER-385, ANDMASS SPECTROMETRY.

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