EzCatDB: M00169
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DB codeM00169
RLCP classification1.15.36030.52 : Hydrolysis
CATH domainDomain 1-.-.-.-
Domain 2-.-.-.-
Domain 3-.-.-.-
Domain 42.30.42.10 : Pdz3 Domain
Domain 5-.-.-.-
Domain 62.30.42.10 : Pdz3 Domain
Domain 7-.-.-.-
Domain 82.30.42.10 : Pdz3 Domain
Domain 9-.-.-.-
Domain 102.30.42.10 : Pdz3 Domain
Domain 112.30.42.10 : Pdz3 Domain
Domain 12-.-.-.-
Domain 133.90.190.10 : Protein-Tyrosine Phosphatase; Chain ACatalytic domain
E.C.3.1.3.48

CATH domainRelated DB codes (homologues)
2.30.42.10 : Pdz3 DomainT00411
3.90.190.10 : Protein-Tyrosine Phosphatase; Chain AS00458,D00154,M00149,T00221

Enzyme Name
UniProtKBKEGG

Q12923
Protein nameTyrosine-protein phosphatase non-receptor type 13protein-tyrosine-phosphatase
phosphotyrosine phosphatase
phosphoprotein phosphatase (phosphotyrosine)
phosphotyrosine histone phosphatase
protein phosphotyrosine phosphatase
tyrosylprotein phosphatase
phosphotyrosine protein phosphatase
phosphotyrosylprotein phosphatase
tyrosine O-phosphate phosphatase
PPT-phosphatase
PTPase
[phosphotyrosine]protein phosphatase
PTP-phosphatase
SynonymsEC 3.1.3.48
Protein-tyrosine phosphatase 1E
PTP-E1
hPTPE1
PTP-BAS
Protein-tyrosine phosphatase PTPL1
Fas-associated protein-tyrosine phosphatase 1
FAP-1
RefSeqNP_006255.1 (Protein)
NM_006264.2 (DNA/RNA sequence)
NP_542414.1 (Protein)
NM_080683.2 (DNA/RNA sequence)
NP_542415.1 (Protein)
NM_080684.2 (DNA/RNA sequence)
NP_542416.1 (Protein)
NM_080685.2 (DNA/RNA sequence)
PfamPF09380 (FERM_C)
PF00373 (FERM_M)
PF09379 (FERM_N)
PF00595 (PDZ)
PF00102 (Y_phosphatase)
[Graphical view]


UniProtKB:Accession NumberQ12923
Entry namePTN13_HUMAN
ActivityProtein tyrosine phosphate + H(2)O = protein tyrosine + phosphate.
SubunitInteracts with TRIP6 and TNFRSF6 (Fas receptor) through its second PDZ domain. Interacts with the C-terminal SVP motif of NGFR through its third PDZ domain. Interacts with the LIM domain of PDLIM4 through its second and fourth PDZ domains. Binds PLEKHA1 and PLEKHA2 through its first PDZ domain. Interacts with BRD7 and ARHGAP29.
Subcellular locationCytoplasm, cytoskeleton (By similarity).
Cofactor

Compound table: links to PDB-related databases & PoSSuM

SubstratesProducts
KEGG-idC01167C00001C00585C00009
CompoundProtein tyrosine phosphateH2OProtein tyrosineOrthophosphate
Typearomatic ring (only carbon atom),peptide/protein,phosphate group/phosphate ionH2Oaromatic ring (only carbon atom),peptide/proteinphosphate group/phosphate ion
ChEBI
15377

26078
PubChem
962
22247451

22486802
1004
            
1d5gAUnbound UnboundUnbound
1q7xAUnbound UnboundUnbound
3pdzAUnbound UnboundUnbound
1wchAUnbound UnboundBound:PO4 3478

Active-site residues
resource
Swissprot;Q12923 & literature [13]
pdbCatalytic residuesMain-chain involved in catalysis
          
1d5gA 
 
1q7xA 
 
3pdzA 
 
1wchAASP 2378;CYS 2408;ARG 2414;SER 2415
SER 2409;ALA 2410;ILE 2412;GLY 2413;ARG 2414


references
[1]
PubMed ID7528537
JournalBiochemistry
Year1994
Volume33
Pages15483-93
AuthorsPei D, Lorenz U, Klingmuller U, Neel BG, Walsh CT
TitleIntramolecular regulation of protein tyrosine phosphatase SH-PTP1: a new function for Src homology 2 domains.
[2]
PubMed ID9417985
JournalJ Struct Biol
Year1997
Volume120
Pages201-3
AuthorsLiang X, Meng W, Niu T, Zhao Z, Zhou GW
TitleExpression, purification, and crystallization of the catalytic domain of protein tyrosine phosphatase SHP-1.
[3]
PubMed ID9835052
JournalJ Biomol NMR
Year1998
Volume12
Pages455-6
AuthorsEkiel I, Banville D, Shen SH, Slon-Usakiewicz JJ, Koshy A, Gehring K
TitleMain-chain signal assignment for the PDZ2 domain from human protein tyrosine phosphatase hPTP1E and its complex with a C-terminal peptide from the Fas receptor.
[4]
PubMed ID9632781
JournalMol Cell Biol
Year1998
Volume18
Pages3966-73
AuthorsHadari YR, Kouhara H, Lax I, Schlessinger J
TitleBinding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation.
[5]
CommentsSTRUCTURE BY NMR OF 1361-1456 UNCOMPLEXED AND IN COMPLEX WITH THE C-TERMINUS OF TNFRSF6.
Medline ID20170882
PubMed ID10704206
JournalBiochemistry
Year2000
Volume39
Pages2572-80
AuthorsKozlov G, Gehring K, Ekiel I
TitleSolution structure of the PDZ2 domain from human phosphatase hPTP1E and its interactions with C-terminal peptides from the Fas receptor.
Related PDB3pdz
Related UniProtKBQ12923
[6]
PubMed ID11500950
JournalJ Cell Biochem
Year2001
Volume83
Pages14-20
AuthorsYang J, Cheng Z, Niu T, Liang X, Zhao ZJ, Zhou GW
TitleProtein tyrosine phosphatase SHP-1 specifically recognizes C-terminal residues of its substrates via helix alpha0.
[7]
CommentsSTRUCTURE BY NMR OF 1361-1456 IN COMPLEX WITH THE C-TERMINUS OF THE GUANINE NUCLEOTIDE EXCHANGE FACTOR RA-GEF-2.
Medline ID22090786
PubMed ID12095257
JournalJ Mol Biol
Year2002
Volume320
Pages813-20
AuthorsKozlov G, Banville D, Gehring K, Ekiel I
TitleSolution structure of the PDZ2 domain from cytosolic human phosphatase hPTP1E complexed with a peptide reveals contribution of the beta2-beta3 loop to PDZ domain-ligand interactions.
Related PDB1d5g
Related UniProtKBQ12923
[8]
PubMed ID11884147
JournalJ Mol Biol
Year2002
Volume316
Pages1101-10
AuthorsWalma T, Spronk CA, Tessari M, Aelen J, Schepens J, Hendriks W, Vuister GW
TitleStructure, dynamics and binding characteristics of the second PDZ domain of PTP-BL.
[9]
PubMed ID12870871
JournalBiochem Cell Biol
Year2003
Volume81
Pages71-80
AuthorsPapp R, Ekiel I, English AM
TitleESI-MS and FTIR studies of the interaction between the second PDZ domain of hPTP1E and target peptides.
[10]
PubMed ID14653806
JournalEur J Biochem
Year2003
Volume270
Pages4789-98
AuthorsErdmann KS
TitleThe protein tyrosine phosphatase PTP-Basophil/Basophil-like. Interacting proteins and molecular functions.
[11]
CommentsNMR Structure
PubMed ID14596806
JournalJ Mol Biol
Year2003
Volume334
Pages143-55
AuthorsKachel N, Erdmann KS, Kremer W, Wolff P, Gronwald W, Heumann R, Kalbitzer HR
TitleStructure determination and ligand interactions of the PDZ2b domain of PTP-Bas (hPTP1E): splicing-induced modulation of ligand specificity.
Related PDB1q7x
[12]
PubMed ID14725761
JournalStructure (Camb)
Year2004
Volume12
Pages11-20
AuthorsWalma T, Aelen J, Nabuurs SB, Oostendorp M, van den Berk L, Hendriks W, Vuister GW
TitleA closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL.
[13]
PubMed ID15611135
JournalJ Biol Chem
Year2005
Volume280
Pages8180-7
AuthorsVilla F, Deak M, Bloomberg GB, Alessi DR, van Aalten DM
TitleCrystal structure of the PTPL1/FAP-1 human tyrosine phosphatase mutated in colorectal cancer: evidence for a second phosphotyrosine substrate recognition pocket.
Related PDB1wch

comments
This enzyme is composed of the N-terminal kinase non-noncatalytic domain (KIND), FERM domain, five PDZ domains, and the C-terminal catalytic domain (see [10]). The FERM domain is usually involved in localizing itself to the plasma membrane.
The structures of 1d5g, 1q7x, 3pdz (from PDB) correspond to the second PDZ domain, whilst 1wch corresponds to the catalytic domain.
As the catalytic domain is homologous to other phosphatase domains (S00458, D00154, M00149 in EzCatDB) and the catalytic residues are conserved, the mechanism must be similar to those of the counterparts.

createdupdated
2004-03-192009-02-26


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Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
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