PTEN S170N [cytosol]

Stable Identifier
R-HSA-2318408
Type
Protein [EntityWithAccessionedSequence]
Species
Homo sapiens
Compartment
Synonyms
PTEN Ser170Asn
Locations in the PathwayBrowser
General
PTEN missense mutation that results in the substitution of serine at position 170 with asparagine affects the phosphatase domain of PTEN. Serine residue S170 is involved in the formation of intedomain hydrogen bonds between the phosphatase domain and the membrane-binding C2 domain (Lee et al. 1999).PTEN S170N (Ser170Asn) mutant shows markedly decreased phosphoinositide phosphatase activity (Han et al. 2000).
Literature References
PubMed ID Title Journal Year
10866302 Functional evaluation of PTEN missense mutations using in vitro phosphoinositide phosphatase assay

Han, SY, Kato, H, Kato, S, Suzuki, T, Shibata, H, Ishii, S, Shiiba, K, Matsuno, S, Kanamaru, R, Ishioka, C

Cancer Res 2000
10555148 Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association

Lee, JO, Yang, H, Georgescu, MM, Di Cristofano, A, Maehama, T, Shi, Y, Dixon, JE, Pandolfi, P, Pavletich, NP

Cell 1999
Participates
Other forms of this molecule
Modified Residues
Name
L-serine 170 replaced with L-asparagine
Coordinate
170
PsiMod
A protein modification that effectively removes or replaces an L-serine.
A protein modification that effectively converts a source amino acid residue to an L-asparagine.
Disease
Name Identifier Synonyms
endometrial cancer DOID:1380 primary malignant neoplasm of endometrium, neoplasm of endometrium (disorder), endometrial neoplasm, malignant endometrial neoplasm, endometrial Ca, malignant neoplasm of endometrium, tumor of Endometrium
cancer DOID:162 malignant tumor, malignant neoplasm, primary cancer
glioblastoma DOID:3068 GBM, adult glioblastoma multiforme, grade IV adult Astrocytic tumor, primary glioblastoma multiforme, spongioblastoma multiforme
Interactors (49)
Accession #Entities Entities Confidence Score Evidence (IntAct)
 UniProt:O14745 NHRF1      0.826 9
 UniProt:Q5TCQ9 MAGI3      0.747 9
 UniProt:Q15599 NHRF2      0.733 6
 UniProt:P60484 PTEN  20 0.713 19
 UniProt:O60307 MAST3      0.698 4
 UniProt:P09619 PDGFRB  3 0.675 3
 UniProt:P42685 FRK  4 0.639 7
 UniProt:Q06830 PRDX1  4 0.632 7
 UniProt:P30260 CDC27  2 0.616 7
 UniProt:Q9HD26 GOPC  3 0.611 4
 UniProt:Q86UL8 MAGI2  1 0.611 7
 UniProt:Q96L92 SNX27      0.611 4
 UniProt:Q13424 SNTA1  1 0.611 4
 UniProt:Q6P0Q8 MAST2      0.611 4
 UniProt:Q9NZN5-2 ARHGEF12      0.611 4
 UniProt:Q92743 HTRA1  1 0.611 4
 UniProt:Q9H5P4 PDZD7      0.611 4
 UniProt:A4D2P6 GRD2I      0.611 6
 UniProt:Q9Y2H9 MAST1      0.611 4
 UniProt:Q9NY99 SNTG2  1 0.611 3
 UniProt:Q13884 SNTB1  1 0.611 5
 UniProt:Q14160 SCRIB  1 0.611 5
 UniProt:O43791 SPOP  3 0.611 4
 UniProt:P35226 BMI1  3 0.61 7
 UniProt:Q9R1L5 MAST1      0.593 3
 UniProt:Q60592 MAST2      0.593 4
 UniProt:P46934 NEDD4  1 0.591 4
 UniProt:O88382 MAGI2      0.581 3
 UniProt:Q96QZ7 MAGI1      0.544 8
 UniProt:O75970 MPDZ      0.544 7
 UniProt:Q12923 PTPN13  2 0.544 3
 UniProt:Q07157 TJP1  6 0.544 5
 UniProt:Q15700 DLG2  2 0.544 3
 UniProt:Q8NI35 PATJ  1 0.544 10
 UniProt:P62136 PPP1CA  2 0.524 2
 UniProt:Q9JHL1 NHRF2      0.524 2
 UniProt:P21860 ERBB3      0.519 2
 UniProt:Q9NRD5 PICK1  2 0.508 2
 UniProt:Q9JK71 MAGI3      0.508 3
 UniProt:Q9P0U4 CXXC1  1 0.508 2
 UniProt:Q9ULX6 AKAP8L  1 0.499 2
 UniProt:Q93009 USP7  2 0.499 2
 UniProt:Q03135 CAV1  5 0.499 2
 UniProt:P08238 HSP90AB1  6 0.483 2
 UniProt:Q9UER7 DAXX  13 0.483 2
 UniProt:Q16643 DBN1  1 0.471 5
 UniProt:Q9UJX3 ANAPC7  2 0.462 2
 UniProt:Q9UJX5 ANAPC4  2 0.462 2
 UniProt:Q9UJX4 ANAPC5  2 0.462 2
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