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Tyrosine-protein phosphatase non-receptor type 13 (EC 3.1.3.48) (Fas-associated protein-tyrosine phosphatase 1) (FAP-1) (PTP-BAS) (Protein-tyrosine phosphatase 1E) (PTP-E1) (hPTPE1) (Protein-tyrosine phosphatase PTPL1)

 PTN13_HUMAN             Reviewed;        2485 AA.
Q12923; B2RTR0; Q15159; Q15263; Q15264; Q15265; Q15674; Q16826;
Q8IWH7; Q9NYN9; Q9UDA8;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
18-JUL-2018, entry version 201.
RecName: Full=Tyrosine-protein phosphatase non-receptor type 13;
EC=3.1.3.48 {ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:19307596};
AltName: Full=Fas-associated protein-tyrosine phosphatase 1;
Short=FAP-1;
AltName: Full=PTP-BAS;
AltName: Full=Protein-tyrosine phosphatase 1E;
Short=PTP-E1;
Short=hPTPE1;
AltName: Full=Protein-tyrosine phosphatase PTPL1;
Name=PTPN13; Synonyms=PNP1, PTP1E, PTPL1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Mammary carcinoma;
PubMed=8071359;
Banville D., Ahmad S., Stocco R., Shen S.-H.;
"A novel protein-tyrosine phosphatase with homology to both the
cytoskeletal proteins of the band 4.1 family and junction-associated
guanylate kinases.";
J. Biol. Chem. 269:22320-22327(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND ALTERNATIVE
SPLICING.
TISSUE=Leukemia;
PubMed=8287977; DOI=10.1016/0014-5793(94)80273-4;
Maekawa K., Imagawa N., Nagamatsu M., Harada S.;
"Molecular cloning of a novel protein-tyrosine phosphatase containing
a membrane-binding domain and GLGF repeats.";
FEBS Lett. 337:200-206(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Fibroblast;
PubMed=7929060;
Saras J., Claesson-Welsh L., Heldin C.-H., Gonez L.J.;
"Cloning and characterization of PTPL1, a protein tyrosine phosphatase
with similarities to cytoskeletal-associated proteins.";
J. Biol. Chem. 269:24082-24089(1994).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1323-1922 (ISOFORM 1).
TISSUE=Brain, and Eye;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 1216-2485 (ISOFORMS 1/2/3).
TISSUE=Pancreas;
Wang H.-Y.;
Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 1279-1883 (ISOFORM 4).
TISSUE=Brain;
PubMed=7536343; DOI=10.1126/science.7536343;
Sato T., Irie S., Kitada S., Reed J.C.;
"FAP-1: a protein tyrosine phosphatase that associates with Fas.";
Science 268:411-415(1995).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1323-1821 (ISOFORMS 1/2/3), AND
INTERACTION WITH NGFR.
PubMed=10544233; DOI=10.1016/S0014-5793(99)01324-1;
Irie S., Hachiya T., Rabizadeh S., Maruyama W., Mukai J., Li Y.,
Reed J.C., Bredesen D.E., Sato T.A.;
"Functional interaction of Fas-associated phosphatase-1 (FAP-1) with
p75(NTR) and their effect on NF-kappaB activation.";
FEBS Lett. 460:191-198(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 2298-2414.
TISSUE=Leukemia;
PubMed=8483328;
Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.;
"Identification of novel protein-tyrosine phosphatases in a human
leukemia cell line, F-36P.";
Leukemia 7:742-746(1993).
[9]
INTERACTION WITH ARHGAP29.
PubMed=9305890; DOI=10.1074/jbc.272.39.24333;
Saras J., Franzen P., Aspenstroem P., Hellman U., Gonez L.J.,
Heldin C.-H.;
"A novel GTPase-activating protein for Rho interacts with a PDZ domain
of the protein-tyrosine phosphatase PTPL1.";
J. Biol. Chem. 272:24333-24338(1997).
[10]
INTERACTION WITH TRIP6.
PubMed=10400701; DOI=10.1074/jbc.274.29.20679;
Murthy K.K., Clark K., Fortin Y., Shen S.-H., Banville D.;
"ZRP-1, a zyxin-related protein, interacts with the second PDZ domain
of the cytosolic protein tyrosine phosphatase hPTP1E.";
J. Biol. Chem. 274:20679-20687(1999).
[11]
INTERACTION TRIP6, AND SUBCELLULAR LOCATION.
PubMed=10826496; DOI=10.1078/S0171-9335(04)70031-X;
Cuppen E., van Ham M., Wansink D.G., de Leeuw A., Wieringa B.,
Hendriks W.;
"The zyxin-related protein TRIP6 interacts with PDZ motifs in the
adaptor protein RIL and the protein tyrosine phosphatase PTP-BL.";
Eur. J. Cell Biol. 79:283-293(2000).
[12]
INTERACTION WITH PKN2, AND SUBCELLULAR LOCATION.
PubMed=11356191; DOI=10.1016/S0014-5793(01)02401-2;
Gross C., Heumann R., Erdmann K.S.;
"The protein kinase C-related kinase PRK2 interacts with the protein
tyrosine phosphatase PTP-BL via a novel PDZ domain binding motif.";
FEBS Lett. 496:101-104(2001).
[13]
INTERACTION WITH PLEKHA1 AND PLEKHA2.
PubMed=14516276; DOI=10.1042/BJ20031154;
Kimber W.A., Deak M., Prescott A.R., Alessi D.R.;
"Interaction of the protein tyrosine phosphatase PTPL1 with the
PtdIns(3,4)P2-binding adaptor protein TAPP1.";
Biochem. J. 376:525-535(2003).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
CATALYTIC ACTIVITY, AND INTERACTION WITH PDLIM4.
PubMed=19307596; DOI=10.1083/jcb.200810155;
Zhang Y., Tu Y., Zhao J., Chen K., Wu C.;
"Reversion-induced LIM interaction with Src reveals a novel Src
inactivation cycle.";
J. Cell Biol. 184:785-792(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1029 AND SER-1033, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-890; SER-908
AND SER-1085, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[19]
FUNCTION, AND INTERACTION WITH FBXL2 AND PIK3R2.
PubMed=23604317; DOI=10.1038/ncb2731;
Kuchay S., Duan S., Schenkein E., Peschiaroli A., Saraf A.,
Florens L., Washburn M.P., Pagano M.;
"FBXL2- and PTPL1-mediated degradation of p110-free p85beta regulatory
subunit controls the PI(3)K signalling cascade.";
Nat. Cell Biol. 15:472-480(2013).
[20]
INTERACTION WITH SDCCAG3.
PubMed=23108400; DOI=10.1038/onc.2012.485;
Hagemann N., Ackermann N., Christmann J., Brier S., Yu F.,
Erdmann K.S.;
"The serologically defined colon cancer antigen-3 interacts with the
protein tyrosine phosphatase PTPN13 and is involved in the regulation
of cytokinesis.";
Oncogene 32:4602-4613(2013).
[21]
STRUCTURE BY NMR OF 1361-1456 UNCOMPLEXED AND IN COMPLEX WITH THE
C-TERMINUS OF TNFRSF6.
PubMed=10704206; DOI=10.1021/bi991913c;
Kozlov G., Gehring K., Ekiel I.;
"Solution structure of the PDZ2 domain from human phosphatase hPTP1E
and its interactions with C-terminal peptides from the Fas receptor.";
Biochemistry 39:2572-2580(2000).
[22]
STRUCTURE BY NMR OF 1361-1456 IN COMPLEX WITH THE C-TERMINUS OF THE
GUANINE NUCLEOTIDE EXCHANGE FACTOR RA-GEF-2.
PubMed=12095257; DOI=10.1016/S0022-2836(02)00544-2;
Kozlov G., Banville D., Gehring K., Ekiel I.;
"Solution 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.";
J. Mol. Biol. 320:813-820(2002).
[23]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 2163-2477, FUNCTION,
CATALYTIC ACTIVITY, MUTAGENESIS OF ASP-2154; ARG-2205; GLN-2221;
MET-2307; CYS-2408; ARG-2444; HIS-2448; GLY-2449 AND GLU-2474, AND
CHARACTERIZATION OF VARIANT VAL-2458.
PubMed=15611135; DOI=10.1074/jbc.M412211200;
Villa F., Deak M., Bloomberg G.B., Alessi D.R., van Aalten D.M.;
"Crystal structure of the PTPL1/FAP-1 human tyrosine phosphatase
mutated in colorectal cancer: evidence for a second phosphotyrosine
substrate recognition pocket.";
J. Biol. Chem. 280:8180-8187(2005).
[24]
VARIANTS PRO-1419 AND MET-1522.
PubMed=12436199; DOI=10.1007/s100380200094;
Yoshida S., Harada H., Nagai H., Fukino K., Teramoto A., Emi M.;
"Head-to-head juxtaposition of Fas-associated phosphatase-1 (FAP-1)
and c-Jun NH2-terminal kinase 3 (JNK3) genes: genomic structure and
seven polymorphisms of the FAP-1 gene.";
J. Hum. Genet. 47:614-619(2002).
-!- FUNCTION: Tyrosine phosphatase which regulates negatively FAS-
induced apoptosis and NGFR-mediated pro-apoptotic signaling
(PubMed:15611135). May regulate phosphoinositide 3-kinase (PI3K)
signaling through dephosphorylation of PIK3R2 (PubMed:23604317).
{ECO:0000269|PubMed:15611135, ECO:0000269|PubMed:23604317}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000269|PubMed:15611135,
ECO:0000269|PubMed:19307596}.
-!- SUBUNIT: Interacts (via the first PDZ domain) with PLEKHA1 and
PLEKHA2 (PubMed:14516276). Interacts (via the second PDZ domain)
with TNFRSF6 (Fas receptor) (via C-terminus) (PubMed:10704206).
Interacts (via the second PDZ domain) with TRIP6 (via the third
LIM domain and C-terminus) (PubMed:10826496, PubMed:10400701).
Interacts (via the third PDZ domain) with NGFR (via C-terminal SVP
motif) and PKN2 (via C-terminus) (PubMed:10544233,
PubMed:11356191). Interacts (via the second or fourth PDZ domains)
with PDLIM4 (via C-terminus only or via combined C-terminus and
LIM domain, but not LIM domain only). Found in a complex with
PDLIM4 and TRIP6 (By similarity). Interacts with PDLIM4; this
interaction results in dephosphorylation of SRC 'Tyr-419' by this
protein leading to its inactivation (PubMed:19307596). Interacts
with BRD7 (By similarity). Interacts with RAPGEF6
(PubMed:12095257). Interacts with ARHGAP29 (PubMed:9305890).
Interacts with PIK3R2; dephosphorylates PIK3R2 (PubMed:23604317).
Interacts with FBXL2 (PubMed:23604317). Interacts with SDCCAG3
(PubMed:23108400). {ECO:0000250|UniProtKB:Q64512,
ECO:0000269|PubMed:10400701, ECO:0000269|PubMed:10544233,
ECO:0000269|PubMed:10704206, ECO:0000269|PubMed:10826496,
ECO:0000269|PubMed:11356191, ECO:0000269|PubMed:12095257,
ECO:0000269|PubMed:14516276, ECO:0000269|PubMed:19307596,
ECO:0000269|PubMed:23108400, ECO:0000269|PubMed:23604317,
ECO:0000269|PubMed:9305890}.
-!- INTERACTION:
P25445:FAS; NbExp=3; IntAct=EBI-355227, EBI-494743;
Q9BUL8:PDCD10; NbExp=3; IntAct=EBI-355227, EBI-740195;
Q16513:PKN2; NbExp=4; IntAct=EBI-355227, EBI-2511350;
Q9HB21:PLEKHA1; NbExp=6; IntAct=EBI-355227, EBI-2652984;
Q9HB19:PLEKHA2; NbExp=2; IntAct=EBI-355227, EBI-4401947;
Q8TEU7:RAPGEF6; NbExp=4; IntAct=EBI-355227, EBI-2693017;
Q13501:SQSTM1; NbExp=2; IntAct=EBI-355227, EBI-307104;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:11356191}. Nucleus
{ECO:0000269|PubMed:10826496, ECO:0000269|PubMed:11356191}. Cell
projection, lamellipodium {ECO:0000269|PubMed:11356191}.
Note=Colocalizes with F-actin (PubMed:10826496). Colocalizes with
PKN2 in lamellipodia-like structure, regions of large actin
turnover (PubMed:11356191). {ECO:0000269|PubMed:10826496,
ECO:0000269|PubMed:11356191}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q12923-1; Sequence=Displayed;
Name=2;
IsoId=Q12923-2; Sequence=VSP_000496;
Name=3;
IsoId=Q12923-3; Sequence=VSP_000497;
Name=4;
IsoId=Q12923-4; Sequence=VSP_007921;
Note=May be due to a competing donor splice site.;
-!- TISSUE SPECIFICITY: Present in most tissues with the exception of
the liver and skeletal muscle. Most abundant in lung, kidney and
fetal brain.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Non-receptor class subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH39610.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/PTPN13ID41912ch4q21.html";
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EMBL; U12128; AAB60339.1; -; mRNA.
EMBL; D21209; BAA04750.1; -; mRNA.
EMBL; D21210; BAA04751.1; -; mRNA.
EMBL; D21211; BAA04752.1; -; mRNA.
EMBL; X80289; CAA56563.1; -; mRNA.
EMBL; BC039610; AAH39610.1; ALT_SEQ; mRNA.
EMBL; BC140777; AAI40778.1; -; mRNA.
EMBL; X79676; CAA56124.1; -; mRNA.
EMBL; L34583; AAC41755.1; -; mRNA.
EMBL; AF233323; AAF63474.1; -; mRNA.
CCDS; CCDS47093.1; -. [Q12923-4]
CCDS; CCDS47094.1; -. [Q12923-1]
CCDS; CCDS47095.1; -. [Q12923-3]
CCDS; CCDS47096.1; -. [Q12923-2]
PIR; A54971; A54971.
PIR; I67629; I67629.
PIR; I67630; I67630.
RefSeq; NP_006255.1; NM_006264.2. [Q12923-3]
RefSeq; NP_542414.1; NM_080683.2. [Q12923-1]
RefSeq; NP_542415.1; NM_080684.2. [Q12923-2]
RefSeq; NP_542416.1; NM_080685.2. [Q12923-4]
UniGene; Hs.436142; -.
PDB; 1D5G; NMR; -; A=1361-1456.
PDB; 1Q7X; NMR; -; A=1358-1459.
PDB; 1WCH; X-ray; 1.85 A; A=2163-2477.
PDB; 2M0Z; NMR; -; A=1361-1456.
PDB; 2M10; NMR; -; A=1361-1456.
PDB; 3LNX; X-ray; 1.64 A; A/B/C/D/E/F=1361-1456.
PDB; 3LNY; X-ray; 1.30 A; A=1361-1456.
PDB; 3PDZ; NMR; -; A=1361-1456.
PDB; 5GLJ; X-ray; 1.60 A; A/B/C/D=1086-1178.
PDBsum; 1D5G; -.
PDBsum; 1Q7X; -.
PDBsum; 1WCH; -.
PDBsum; 2M0Z; -.
PDBsum; 2M10; -.
PDBsum; 3LNX; -.
PDBsum; 3LNY; -.
PDBsum; 3PDZ; -.
PDBsum; 5GLJ; -.
ProteinModelPortal; Q12923; -.
SMR; Q12923; -.
BioGrid; 111747; 53.
DIP; DIP-40449N; -.
ELM; Q12923; -.
IntAct; Q12923; 53.
MINT; Q12923; -.
STRING; 9606.ENSP00000394794; -.
BindingDB; Q12923; -.
ChEMBL; CHEMBL2976; -.
DEPOD; Q12923; -.
iPTMnet; Q12923; -.
PhosphoSitePlus; Q12923; -.
BioMuta; PTPN13; -.
DMDM; 12643716; -.
EPD; Q12923; -.
MaxQB; Q12923; -.
PaxDb; Q12923; -.
PeptideAtlas; Q12923; -.
PRIDE; Q12923; -.
ProteomicsDB; 59027; -.
ProteomicsDB; 59028; -. [Q12923-2]
ProteomicsDB; 59029; -. [Q12923-3]
ProteomicsDB; 59030; -. [Q12923-4]
DNASU; 5783; -.
Ensembl; ENST00000316707; ENSP00000322675; ENSG00000163629. [Q12923-2]
Ensembl; ENST00000411767; ENSP00000407249; ENSG00000163629. [Q12923-1]
Ensembl; ENST00000427191; ENSP00000408368; ENSG00000163629. [Q12923-3]
Ensembl; ENST00000436978; ENSP00000394794; ENSG00000163629. [Q12923-4]
Ensembl; ENST00000511467; ENSP00000426626; ENSG00000163629. [Q12923-4]
GeneID; 5783; -.
KEGG; hsa:5783; -.
UCSC; uc003hpy.4; human. [Q12923-1]
CTD; 5783; -.
DisGeNET; 5783; -.
EuPathDB; HostDB:ENSG00000163629.12; -.
GeneCards; PTPN13; -.
HGNC; HGNC:9646; PTPN13.
HPA; CAB002213; -.
HPA; HPA048888; -.
HPA; HPA065290; -.
MIM; 600267; gene.
neXtProt; NX_Q12923; -.
OpenTargets; ENSG00000163629; -.
PharmGKB; PA33988; -.
eggNOG; KOG0792; Eukaryota.
eggNOG; COG5599; LUCA.
GeneTree; ENSGT00920000148995; -.
HOVERGEN; HBG053756; -.
InParanoid; Q12923; -.
KO; K02374; -.
OMA; GCYVHDV; -.
OrthoDB; EOG091G0BZR; -.
PhylomeDB; Q12923; -.
TreeFam; TF315388; -.
BRENDA; 3.1.3.48; 2681.
Reactome; R-HSA-1660499; Synthesis of PIPs at the plasma membrane.
Reactome; R-HSA-9008059; Interleukin-37 signaling.
SIGNOR; Q12923; -.
ChiTaRS; PTPN13; human.
EvolutionaryTrace; Q12923; -.
GeneWiki; PTPN13; -.
GenomeRNAi; 5783; -.
PRO; PR:Q12923; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000163629; -.
ExpressionAtlas; Q12923; baseline and differential.
Genevisible; Q12923; HS.
GO; GO:0044297; C:cell body; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0036312; F:phosphatidylinositol 3-kinase regulatory subunit binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0071345; P:cellular response to cytokine stimulus; TAS:Reactome.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IMP:UniProtKB.
GO; GO:0006661; P:phosphatidylinositol biosynthetic process; TAS:Reactome.
GO; GO:0006470; P:protein dephosphorylation; IDA:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IDA:UniProtKB.
CDD; cd14473; FERM_B-lobe; 1.
Gene3D; 1.20.80.10; -; 1.
Gene3D; 2.30.29.30; -; 1.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR019749; Band_41_domain.
InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
InterPro; IPR035963; FERM_2.
InterPro; IPR019748; FERM_central.
InterPro; IPR000299; FERM_domain.
InterPro; IPR018979; FERM_N.
InterPro; IPR018980; FERM_PH-like_C.
InterPro; IPR011019; KIND_dom.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
InterPro; IPR011993; PH-like_dom_sf.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR012153; PTPN13.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
InterPro; IPR029071; Ubiquitin-like_domsf.
PANTHER; PTHR19134:SF197; PTHR19134:SF197; 2.
Pfam; PF09380; FERM_C; 1.
Pfam; PF00373; FERM_M; 1.
Pfam; PF09379; FERM_N; 1.
Pfam; PF00595; PDZ; 5.
Pfam; PF00102; Y_phosphatase; 1.
PIRSF; PIRSF000933; Tyr-Ptase_nr13; 1.
PRINTS; PR00935; BAND41.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00295; B41; 1.
SMART; SM01196; FERM_C; 1.
SMART; SM00750; KIND; 1.
SMART; SM00228; PDZ; 5.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF47031; SSF47031; 1.
SUPFAM; SSF50156; SSF50156; 5.
SUPFAM; SSF52799; SSF52799; 1.
SUPFAM; SSF54236; SSF54236; 1.
PROSITE; PS50057; FERM_3; 1.
PROSITE; PS51377; KIND; 1.
PROSITE; PS50106; PDZ; 5.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell projection; Coiled coil;
Complete proteome; Cytoplasm; Cytoskeleton; Hydrolase; Nucleus;
Phosphoprotein; Polymorphism; Protein phosphatase; Reference proteome;
Repeat.
CHAIN 1 2485 Tyrosine-protein phosphatase non-receptor
type 13.
/FTId=PRO_0000219435.
DOMAIN 3 190 KIND. {ECO:0000255|PROSITE-
ProRule:PRU00709}.
DOMAIN 572 872 FERM. {ECO:0000255|PROSITE-
ProRule:PRU00084}.
DOMAIN 1093 1178 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1368 1452 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1501 1588 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1788 1868 PDZ 4. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1882 1965 PDZ 5. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 2213 2467 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 2408 2414 Substrate.
REGION 2408 2414 Substrate binding. {ECO:0000250}.
COILED 469 504 {ECO:0000255}.
COMPBIAS 56 59 Poly-Leu.
COMPBIAS 1742 1749 Poly-Ser.
ACT_SITE 2408 2408 Phosphocysteine intermediate.
{ECO:0000305}.
BINDING 2378 2378 Substrate.
BINDING 2452 2452 Substrate. {ECO:0000250}.
MOD_RES 240 240 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 301 301 Phosphoserine.
{ECO:0000250|UniProtKB:Q64512}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000250|UniProtKB:Q64512}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 897 897 Phosphoserine.
{ECO:0000250|UniProtKB:Q64512}.
MOD_RES 908 908 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 911 911 Phosphoserine.
{ECO:0000250|UniProtKB:Q64512}.
MOD_RES 914 914 Phosphoserine.
{ECO:0000250|UniProtKB:Q64512}.
MOD_RES 1029 1029 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1033 1033 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1085 1085 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 884 1074 Missing (in isoform 2).
{ECO:0000303|PubMed:8287977}.
/FTId=VSP_000496.
VAR_SEQ 1056 1074 Missing (in isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:7929060,
ECO:0000303|PubMed:8287977}.
/FTId=VSP_000497.
VAR_SEQ 1383 1383 T -> TVLFDK (in isoform 4).
{ECO:0000303|PubMed:7536343,
ECO:0000303|PubMed:8071359}.
/FTId=VSP_007921.
VARIANT 1356 1356 F -> L (in dbSNP:rs10033029).
/FTId=VAR_048359.
VARIANT 1419 1419 L -> P (in dbSNP:rs749353184).
{ECO:0000269|PubMed:12436199}.
/FTId=VAR_016200.
VARIANT 1522 1522 I -> M (in dbSNP:rs2230600).
{ECO:0000269|PubMed:12436199}.
/FTId=VAR_016201.
VARIANT 1625 1625 E -> K (in dbSNP:rs12500797).
/FTId=VAR_024373.
VARIANT 1744 1744 S -> P (in dbSNP:rs17012064).
/FTId=VAR_048360.
VARIANT 2081 2081 Y -> D (in dbSNP:rs989902).
/FTId=VAR_024374.
VARIANT 2458 2458 I -> V (no effect on substrate affinity;
dbSNP:rs34226837).
{ECO:0000269|PubMed:15611135}.
/FTId=VAR_048361.
MUTAGEN 2154 2154 D->H: No effect on substrate affinity.
{ECO:0000269|PubMed:15611135}.
MUTAGEN 2205 2205 R->W: No effect on substrate affinity.
{ECO:0000269|PubMed:15611135}.
MUTAGEN 2221 2221 Q->M: Reduces substrate affinity 2 fold.
{ECO:0000269|PubMed:15611135}.
MUTAGEN 2307 2307 M->T: Reduces substrate affinity 7 fold.
{ECO:0000269|PubMed:15611135}.
MUTAGEN 2408 2408 C->S: Loss of catalytic activity.
{ECO:0000269|PubMed:15611135}.
MUTAGEN 2444 2444 R->E: Loss of catalytic activity.
{ECO:0000269|PubMed:15611135}.
MUTAGEN 2444 2444 R->K: Reduces substrate affinity 7 fold.
{ECO:0000269|PubMed:15611135}.
MUTAGEN 2444 2444 R->Q: Strongly decreases catalytic
activity. {ECO:0000269|PubMed:15611135}.
MUTAGEN 2448 2448 H->A: Reduces substrate affinity 2 fold.
{ECO:0000269|PubMed:15611135}.
MUTAGEN 2449 2449 G->V: Loss of catalytic activity.
{ECO:0000269|PubMed:15611135}.
MUTAGEN 2474 2474 E->D: No effect on substrate affinity.
{ECO:0000269|PubMed:15611135}.
CONFLICT 1134 1135 LD -> FH (in Ref. 3; CAA56563).
{ECO:0000305}.
CONFLICT 1216 1229 KDHHWSRGTLRHIS -> DLSRSHCHVYLAHL (in Ref.
5). {ECO:0000305}.
CONFLICT 1238 1239 GL -> A (in Ref. 5; CAA56124).
{ECO:0000305}.
CONFLICT 1357 1357 S -> P (in Ref. 5; CAA56124).
{ECO:0000305}.
CONFLICT 1362 1363 KP -> RS (in Ref. 5; CAA56124).
{ECO:0000305}.
CONFLICT 1538 1538 P -> A (in Ref. 3; CAA56563).
{ECO:0000305}.
CONFLICT 1649 1649 R -> K (in Ref. 5; CAA56124).
{ECO:0000305}.
CONFLICT 1698 1714 KSQEDTICTMFYYPQKI -> RVKKIPFVPCFTILRKR
(in Ref. 5; CAA56124). {ECO:0000305}.
CONFLICT 1797 1797 G -> A (in Ref. 3; CAA56563).
{ECO:0000305}.
CONFLICT 1856 1857 AA -> G (in Ref. 5; CAA56124).
{ECO:0000305}.
CONFLICT 2069 2069 A -> S (in Ref. 5; CAA56124).
{ECO:0000305}.
CONFLICT 2206 2210 GLLDQ -> VARS (in Ref. 5; CAA56124).
{ECO:0000305}.
STRAND 1090 1097 {ECO:0000244|PDB:5GLJ}.
TURN 1100 1102 {ECO:0000244|PDB:5GLJ}.
STRAND 1105 1109 {ECO:0000244|PDB:5GLJ}.
STRAND 1122 1126 {ECO:0000244|PDB:5GLJ}.
HELIX 1131 1135 {ECO:0000244|PDB:5GLJ}.
STRAND 1143 1147 {ECO:0000244|PDB:5GLJ}.
HELIX 1157 1166 {ECO:0000244|PDB:5GLJ}.
STRAND 1169 1177 {ECO:0000244|PDB:5GLJ}.
STRAND 1366 1372 {ECO:0000244|PDB:3LNY}.
STRAND 1374 1377 {ECO:0000244|PDB:1D5G}.
STRAND 1379 1384 {ECO:0000244|PDB:3LNY}.
STRAND 1385 1387 {ECO:0000244|PDB:2M0Z}.
STRAND 1388 1390 {ECO:0000244|PDB:3LNY}.
HELIX 1391 1393 {ECO:0000244|PDB:3LNY}.
STRAND 1395 1400 {ECO:0000244|PDB:3LNY}.
HELIX 1405 1409 {ECO:0000244|PDB:3LNY}.
STRAND 1417 1421 {ECO:0000244|PDB:3LNY}.
HELIX 1431 1439 {ECO:0000244|PDB:3LNY}.
STRAND 1443 1450 {ECO:0000244|PDB:3LNY}.
HELIX 2175 2179 {ECO:0000244|PDB:1WCH}.
STRAND 2188 2190 {ECO:0000244|PDB:1WCH}.
HELIX 2194 2209 {ECO:0000244|PDB:1WCH}.
HELIX 2212 2220 {ECO:0000244|PDB:1WCH}.
HELIX 2231 2233 {ECO:0000244|PDB:1WCH}.
HELIX 2235 2238 {ECO:0000244|PDB:1WCH}.
TURN 2257 2260 {ECO:0000244|PDB:1WCH}.
STRAND 2264 2272 {ECO:0000244|PDB:1WCH}.
STRAND 2275 2282 {ECO:0000244|PDB:1WCH}.
HELIX 2287 2289 {ECO:0000244|PDB:1WCH}.
HELIX 2290 2299 {ECO:0000244|PDB:1WCH}.
STRAND 2304 2307 {ECO:0000244|PDB:1WCH}.
STRAND 2311 2313 {ECO:0000244|PDB:1WCH}.
STRAND 2331 2346 {ECO:0000244|PDB:1WCH}.
STRAND 2348 2359 {ECO:0000244|PDB:1WCH}.
TURN 2360 2363 {ECO:0000244|PDB:1WCH}.
STRAND 2364 2373 {ECO:0000244|PDB:1WCH}.
HELIX 2385 2398 {ECO:0000244|PDB:1WCH}.
STRAND 2404 2407 {ECO:0000244|PDB:1WCH}.
STRAND 2409 2412 {ECO:0000244|PDB:1WCH}.
HELIX 2413 2429 {ECO:0000244|PDB:1WCH}.
HELIX 2436 2444 {ECO:0000244|PDB:1WCH}.
HELIX 2454 2475 {ECO:0000244|PDB:1WCH}.
SEQUENCE 2485 AA; 276906 MW; 8D1B31597C66962B CRC64;
MHVSLAEALE VRGGPLQEEE IWAVLNQSAE SLQELFRKVS LADPAALGFI ISPWSLLLLP
SGSVSFTDEN ISNQDLRAFT APEVLQNQSL TSLSDVEKIH IYSLGMTLYW GADYEVPQSQ
PIKLGDHLNS ILLGMCEDVI YARVSVRTVL DACSAHIRNS NCAPSFSYVK HLVKLVLGNL
SGTDQLSCNS EQKPDRSQAI RDRLRGKGLP TGRSSTSDVL DIQKPPLSHQ TFLNKGLSKS
MGFLSIKDTQ DENYFKDILS DNSGREDSEN TFSPYQFKTS GPEKKPIPGI DVLSKKKIWA
SSMDLLCTAD RDFSSGETAT YRRCHPEAVT VRTSTTPRKK EARYSDGSIA LDIFGPQKMD
PIYHTRELPT SSAISSALDR IRERQKKLQV LREAMNVEEP VRRYKTYHGD VFSTSSESPS
IISSESDFRQ VRRSEASKRF ESSSGLPGVD ETLSQGQSQR PSRQYETPFE GNLINQEIML
KRQEEELMQL QAKMALRQSR LSLYPGDTIK ASMLDITRDP LREIALETAM TQRKLRNFFG
PEFVKMTIEP FISLDLPRSI LTKKGKNEDN RRKVNIMLLN GQRLELTCDT KTICKDVFDM
VVAHIGLVEH HLFALATLKD NEYFFVDPDL KLTKVAPEGW KEEPKKKTKA TVNFTLFFRI
KFFMDDVSLI QHTLTCHQYY LQLRKDILEE RMHCDDETSL LLASLALQAE YGDYQPEVHG
VSYFRMEHYL PARVMEKLDL SYIKEELPKL HNTYVGASEK ETELEFLKVC QRLTEYGVHF
HRVHPEKKSQ TGILLGVCSK GVLVFEVHNG VRTLVLRFPW RETKKISFSK KKITLQNTSD
GIKHGFQTDN SKICQYLLHL CSYQHKFQLQ MRARQSNQDA QDIERASFRS LNLQAESVRG
FNMGRAISTG SLASSTLNKL AVRPLSVQAE ILKRLSCSEL SLYQPLQNSS KEKNDKASWE
EKPREMSKSY HDLSQASLYP HRKNVIVNME PPPQTVAELV GKPSHQMSRS DAESLAGVTK
LNNSKSVASL NRSPERRKHE SDSSSIEDPG QAYVLGMTMH SSGNSSSQVP LKENDVLHKR
WSIVSSPERE ITLVNLKKDA KYGLGFQIIG GEKMGRLDLG IFISSVAPGG PADLDGCLKP
GDRLISVNSV SLEGVSHHAA IEILQNAPED VTLVISQPKE KISKVPSTPV HLTNEMKNYM
KKSSYMQDSA IDSSSKDHHW SRGTLRHISE NSFGPSGGLR EGSLSSQDSR TESASLSQSQ
VNGFFASHLG DQTWQESQHG SPSPSVISKA TEKETFTDSN QSKTKKPGIS DVTDYSDRGD
SDMDEATYSS SQDHQTPKQE SSSSVNTSNK MNFKTFSSSP PKPGDIFEVE LAKNDNSLGI
SVTGGVNTSV RHGGIYVKAV IPQGAAESDG RIHKGDRVLA VNGVSLEGAT HKQAVETLRN
TGQVVHLLLE KGQSPTSKEH VPVTPQCTLS DQNAQGQGPE KVKKTTQVKD YSFVTEENTF
EVKLFKNSSG LGFSFSREDN LIPEQINASI VRVKKLFPGQ PAAESGKIDV GDVILKVNGA
SLKGLSQQEV ISALRGTAPE VFLLLCRPPP GVLPEIDTAL LTPLQSPAQV LPNSSKDSSQ
PSCVEQSTSS DENEMSDKSK KQCKSPSRRD SYSDSSGSGE DDLVTAPANI SNSTWSSALH
QTLSNMVSQA QSHHEAPKSQ EDTICTMFYY PQKIPNKPEF EDSNPSPLPP DMAPGQSYQP
QSESASSSSM DKYHIHHISE PTRQENWTPL KNDLENHLED FELEVELLIT LIKSEKGSLG
FTVTKGNQRI GCYVHDVIQD PAKSDGRLKP GDRLIKVNDT DVTNMTHTDA VNLLRAASKT
VRLVIGRVLE LPRIPMLPHL LPDITLTCNK EELGFSLCGG HDSLYQVVYI SDINPRSVAA
IEGNLQLLDV IHYVNGVSTQ GMTLEEVNRA LDMSLPSLVL KATRNDLPVV PSSKRSAVSA
PKSTKGNGSY SVGSCSQPAL TPNDSFSTVA GEEINEISYP KGKCSTYQIK GSPNLTLPKE
SYIQEDDIYD DSQEAEVIQS LLDVVDEEAQ NLLNENNAAG YSCGPGTLKM NGKLSEERTE
DTDCDGSPLP EYFTEATKMN GCEEYCEEKV KSESLIQKPQ EKKTDDDEIT WGNDELPIER
TNHEDSDKDH SFLTNDELAV LPVVKVLPSG KYTGANLKSV IRVLRGLLDQ GIPSKELENL
QELKPLDQCL IGQTKENRRK NRYKNILPYD ATRVPLGDEG GYINASFIKI PVGKEEFVYI
ACQGPLPTTV GDFWQMIWEQ KSTVIAMMTQ EVEGEKIKCQ RYWPNILGKT TMVSNRLRLA
LVRMQQLKGF VVRAMTLEDI QTREVRHISH LNFTAWPDHD TPSQPDDLLT FISYMRHIHR
SGPIITHCSA GIGRSGTLIC IDVVLGLISQ DLDFDISDLV RCMRLQRHGM VQTEDQYIFC
YQVILYVLTR LQAEEEQKQQ PQLLK


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