PTN11_CHICK
ID PTN11_CHICK Reviewed; 593 AA.
AC Q90687;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=Tyrosine-protein phosphatase non-receptor type 11;
DE EC=3.1.3.48 {ECO:0000250|UniProtKB:Q06124};
DE AltName: Full=SH-PTP2;
DE Short=cSH-PTP2;
GN Name=PTPN11;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Erythroblast {ECO:0000269|PubMed:8921851};
RX PubMed=8921851; DOI=10.1016/0378-1119(96)00278-8;
RA Park C.Y., LaMontagne K.R., Tonks N.K., Hayman M.J.;
RT "Cloning and expression of the chicken protein tyrosine phosphatase SH-
RT PTP2.";
RL Gene 177:93-97(1996).
CC -!- FUNCTION: This PTPase activity may directly link growth factor
CC receptors and other signaling proteins through protein-tyrosine
CC phosphorylation. The SH2 regions may interact with other cellular
CC components to modulate its own phosphatase activity against interacting
CC substrates (By similarity). May play a positive role during the stages
CC of erythroid cell proliferation (PubMed:8921851).
CC {ECO:0000250|UniProtKB:Q06124, ECO:0000303|PubMed:8921851}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] +
CC phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620; EC=3.1.3.48;
CC Evidence={ECO:0000250|UniProtKB:Q06124, ECO:0000255|PROSITE-
CC ProRule:PRU10044};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in embryonic fibroblast, hematopoietic,
CC erythroid, myeloid and lymphoid cells. {ECO:0000269|PubMed:8921851}.
CC -!- PTM: Phosphorylated by tyrosine-protein kinases.
CC {ECO:0000250|UniProtKB:Q06124}.
CC -!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family. Non-
CC receptor class 2 subfamily. {ECO:0000305}.
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DR EMBL; U38620; AAC60049.1; -; mRNA.
DR PIR; JC5167; JC5167.
DR RefSeq; NP_990299.1; NM_204968.1.
DR AlphaFoldDB; Q90687; -.
DR SMR; Q90687; -.
DR STRING; 9031.ENSGALP00000007692; -.
DR PaxDb; Q90687; -.
DR Ensembl; ENSGALT00000007704; ENSGALP00000007692; ENSGALG00000004821.
DR GeneID; 395815; -.
DR KEGG; gga:395815; -.
DR CTD; 5781; -.
DR VEuPathDB; HostDB:geneid_395815; -.
DR eggNOG; KOG0790; Eukaryota.
DR GeneTree; ENSGT00940000153876; -.
DR HOGENOM; CLU_001645_9_10_1; -.
DR InParanoid; Q90687; -.
DR OMA; KYYIATQ; -.
DR OrthoDB; 411281at2759; -.
DR PhylomeDB; Q90687; -.
DR Reactome; R-GGA-1059683; Interleukin-6 signaling.
DR Reactome; R-GGA-109704; PI3K Cascade.
DR Reactome; R-GGA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-GGA-1433557; Signaling by SCF-KIT.
DR Reactome; R-GGA-180292; GAB1 signalosome.
DR Reactome; R-GGA-186763; Downstream signal transduction.
DR Reactome; R-GGA-210990; PECAM1 interactions.
DR Reactome; R-GGA-210993; Tie2 Signaling.
DR Reactome; R-GGA-389513; CTLA4 inhibitory signaling.
DR Reactome; R-GGA-389948; PD-1 signaling.
DR Reactome; R-GGA-432142; Platelet sensitization by LDL.
DR Reactome; R-GGA-5654689; PI-3K cascade:FGFR1.
DR Reactome; R-GGA-5654693; FRS-mediated FGFR1 signaling.
DR Reactome; R-GGA-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-GGA-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-GGA-5654706; FRS-mediated FGFR3 signaling.
DR Reactome; R-GGA-5654710; PI-3K cascade:FGFR3.
DR Reactome; R-GGA-5654712; FRS-mediated FGFR4 signaling.
DR Reactome; R-GGA-5654720; PI-3K cascade:FGFR4.
DR Reactome; R-GGA-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-GGA-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-GGA-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-GGA-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-GGA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-GGA-8853659; RET signaling.
DR Reactome; R-GGA-8854691; Interleukin-20 family signaling.
DR Reactome; R-GGA-8865999; MET activates PTPN11.
DR Reactome; R-GGA-8934593; Regulation of RUNX1 Expression and Activity.
DR Reactome; R-GGA-912694; Regulation of IFNA/IFNB signaling.
DR Reactome; R-GGA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
DR Reactome; R-GGA-9674555; Signaling by CSF3 (G-CSF).
DR PRO; PR:Q90687; -.
DR Proteomes; UP000000539; Chromosome 15.
DR Bgee; ENSGALG00000004821; Expressed in brain and 14 other tissues.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0050839; F:cell adhesion molecule binding; IBA:GO_Central.
DR GO; GO:0004726; F:non-membrane spanning protein tyrosine phosphatase activity; IBA:GO_Central.
DR GO; GO:0004725; F:protein tyrosine phosphatase activity; ISS:UniProtKB.
DR GO; GO:0030971; F:receptor tyrosine kinase binding; IBA:GO_Central.
DR GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:UniProtKB.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0045778; P:positive regulation of ossification; ISS:UniProtKB.
DR GO; GO:0006470; P:protein dephosphorylation; IBA:GO_Central.
DR Gene3D; 3.30.505.10; -; 2.
DR Gene3D; 3.90.190.10; -; 1.
DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR InterPro; IPR000242; PTP_cat.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR016130; Tyr_Pase_AS.
DR InterPro; IPR003595; Tyr_Pase_cat.
DR InterPro; IPR000387; Tyr_Pase_dom.
DR InterPro; IPR012152; Tyr_Pase_non-rcpt_typ-6/11.
DR Pfam; PF00017; SH2; 2.
DR Pfam; PF00102; Y_phosphatase; 1.
DR PIRSF; PIRSF000929; Tyr-Ptase_nr_6; 1.
DR PRINTS; PR00700; PRTYPHPHTASE.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00194; PTPc; 1.
DR SMART; SM00404; PTPc_motif; 1.
DR SMART; SM00252; SH2; 2.
DR SUPFAM; SSF52799; SSF52799; 1.
DR SUPFAM; SSF55550; SSF55550; 2.
DR PROSITE; PS50001; SH2; 2.
DR PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
DR PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Phosphoprotein; Protein phosphatase;
KW Reference proteome; Repeat; SH2 domain.
FT CHAIN 1..593
FT /note="Tyrosine-protein phosphatase non-receptor type 11"
FT /id="PRO_0000094770"
FT DOMAIN 6..102
FT /note="SH2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191,
FT ECO:0000305"
FT DOMAIN 112..216
FT /note="SH2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191,
FT ECO:0000305"
FT DOMAIN 247..521
FT /note="Tyrosine-protein phosphatase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160"
FT REGION 548..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 459
FT /note="Phosphocysteine intermediate"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00160,
FT ECO:0000255|PROSITE-ProRule:PRU10044"
FT BINDING 425
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 459..465
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000250"
SQ SEQUENCE 593 AA; 67983 MW; 415231144BB43DDA CRC64;
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRTGA VTHIKIQNTG
DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY PLNCADPTSE RWFHGHLSGR
EAEKLLTEKG KHGSFLVRES QSHPGDFVLS VRTGDDKGES NDGKSKVTHV MIHCQDLKYD
VGGGEKFDSL TDLVEHYKKN PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT
DKVKQGFWEE FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS RVIVMTTKEV
ERGKSKCVKY WPDEYSLKEY GVMRVRNVKE SAAHDYTLRE LKLSKVGQGN TERTVWQYHF
RTWPDHGVPS DPGGVLDFLE EVHHKQESIS DAGPVVVHCS AGIGRTGTFI VIDILIDIIR
EKGVDCDIDV PKTIQMVRSQ RSGMVQTEAQ YRFIYMAVQH YIETLQRRIE EEQKSKRKGH
EYTNIKYSLS DQTSGDQSPL PPCTPTPTCP EMREDSARVY ENVGLMQQQK SFR
