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 24-JAN-2024, entry version 152. 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 (By similarity). The SH2 regions may interact with CC other cellular components to modulate its own phosphatase activity CC against interacting substrates (By similarity). May play a positive CC role during the stages of erythroid cell proliferation CC (PubMed:8921851). {ECO:0000250|UniProtKB:Q06124, CC ECO:0000269|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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 9031-ENSGALP00000007692; -. DR Ensembl; ENSGALT00000007704; ENSGALP00000007692; ENSGALG00000004821. DR Ensembl; ENSGALT00010050025.1; ENSGALP00010029554.1; ENSGALG00010020701.1. DR Ensembl; ENSGALT00015061804; ENSGALP00015037433; ENSGALG00015025343. 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; CEIDIHR; -. DR OrthoDB; 2911650at2759; -. 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-512988; Interleukin-3, Interleukin-5 and GM-CSF signaling. 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, IKBKE. 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 cell types or 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:0071310; P:cellular response to organic substance; IEA:UniProt. DR GO; GO:0016311; P:dephosphorylation; IEA:InterPro. 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 CDD; cd14605; PTPc-N11; 1. DR CDD; cd09931; SH2_C-SH2_SHP_like; 1. DR CDD; cd10340; SH2_N-SH2_SHP_like; 1. DR Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1. DR Gene3D; 3.30.505.10; SH2 domain; 2. 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 PANTHER; PTHR46559; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11; 1. DR PANTHER; PTHR46559:SF1; TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 11; 1. 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; (Phosphotyrosine protein) phosphatases II; 1. DR SUPFAM; SSF55550; SH2 domain; 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 //