Search Results

Overview

Uniprot IDQ06124
Protein NameTyrosine-protein phosphatase non-receptor type 11
Gene NamePTPN11
OrganismHomo sapiens

Kla Sites from experimental identification

Position Flanking peptide
124 LSGKEAEKLLTEKGK
198 TDLVEHYKKNPMVET
235 SRVRELSKLAETTDK
538 EEQKSKRKGHEYTNI
590 VGLMQQQKSFR****
91 HHGQLKEKNGDVIEL

Function

Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus (PubMed:10655584, PubMed:14739280, PubMed:18559669, PubMed:18829466, PubMed:26742426, PubMed:28074573, PubMed:32184441). Positively regulates MAPK signal transduction pathway (PubMed:28074573). Dephosphorylates GAB1, ARHGAP35 and EGFR (PubMed:28074573). Dephosphorylates ROCK2 at 'Tyr-722' resulting in stimulation of its RhoA binding activity (PubMed:18559669). Dephosphorylates CDC73 (PubMed:26742426). Dephosphorylates SOX9 on tyrosine residues, leading to inactivate SOX9 and promote ossification (By similarity). Dephosphorylates tyrosine-phosphorylated NEDD9/CAS-L (PubMed:19275884). Acts as an effector of PDCD1-mediated inhibition of T-cell response: recruited by phosphorylated PDCD1, mediating dephosphorylation of key T-cell receptor (TCR) proximal signaling molecules, leading to TCR signaling inhibition (PubMed:32184441)

Protein Sequence

10 MTSRRWFHPN 20 ITGVEAENLL 30 LTRGVDGSFL 40 ARPSKSNPGD 50 FTLSVRRNGA 60 VTHIKIQNTG 70 DYYDLYGGEK 80 FATLAELVQY 90 YMEHHGQLKE 100 KNGDVIELKY 110 PLNCADPTSE 120 RWFHGHLSGK 130 EAEKLLTEKG 140 KHGSFLVRES 150 QSHPGDFVLS 160 VRTGDDKGES 170 NDGKSKVTHV 180 MIRCQELKYD 190 VGGGERFDSL 200 TDLVEHYKKN 210 PMVETLGTVL 220 QLKQPLNTTR 230 INAAEIESRV 240 RELSKLAETT 250 DKVKQGFWEE 260 FETLQQQECK 270 LLYSRKEGQR 280 QENKNKNRYK 290 NILPFDHTRV 300 VLHDGDPNEP 310 VSDYINANII 320 MPEFETKCNN 330 SKPKKSYIAT 340 QGCLQNTVND 350 FWRMVFQENS 360 RVIVMTTKEV 370 ERGKSKCVKY 380 WPDEYALKEY 390 GVMRVRNVKE 400 SAAHDYTLRE 410 LKLSKVGQGN 420 TERTVWQYHF 430 RTWPDHGVPS 440 DPGGVLDFLE 450 EVHHKQESIM 460 DAGPVVVHCS 470 AGIGRTGTFI 480 VIDILIDIIR 490 EKGVDCDIDV 500 PKTIQMVRSQ 510 RSGMVQTEAQ 520 YRFIYMAVQH 530 YIETLQRRIE 540 EEQKSKRKGH 550 EYTNIKYSLA 560 DQTSGDQSPL 570 PPCTPTPPCA 580 EMREDSARVY 590 ENVGLMQQQK SFR

Gene Ontology

Classification GO ID Description
Biological Process GO:1902533 positive regulation of intracellular signal transduction
Biological Process GO:0031666 positive regulation of lipopolysaccharide-mediated signaling pathway
Biological Process GO:0045778 positive regulation of ossification
Cellular Component GO:0005737 cytoplasm
Cellular Component GO:0005829 cytosol
Cellular Component GO:0005925 focal adhesion
Cellular Component GO:0005739 mitochondrion
Cellular Component GO:0005730 nucleolus
Cellular Component GO:0005654 nucleoplasm
Cellular Component GO:0005634 nucleus
Cellular Component GO:0032991 protein-containing complex
Molecular Function GO:0045296 cadherin binding
Molecular Function GO:0050839 cell adhesion molecule binding
Molecular Function GO:0005158 insulin receptor binding
Molecular Function GO:0060090 molecular adaptor activity
Molecular Function GO:0004726 non-membrane spanning protein tyrosine phosphatase activity
Molecular Function GO:0051428 peptide hormone receptor binding
Molecular Function GO:0004721 phosphoprotein phosphatase activity
Molecular Function GO:0001784 phosphotyrosine residue binding
Molecular Function GO:0019901 protein kinase binding
Molecular Function GO:1990782 protein tyrosine kinase binding
Molecular Function GO:0004725 protein tyrosine phosphatase activity
Molecular Function GO:0030971 receptor tyrosine kinase binding
Molecular Function GO:0030159 signaling receptor complex adaptor activity
Biological Process GO:0036302 atrioventricular canal development
Biological Process GO:0007420 brain development
Biological Process GO:0071364 cellular response to epidermal growth factor stimulus
Biological Process GO:0071260 cellular response to mechanical stimulus
Biological Process GO:0019221 cytokine-mediated signaling pathway
Biological Process GO:0048013 ephrin receptor signaling pathway
Biological Process GO:0007173 epidermal growth factor receptor signaling pathway
Biological Process GO:0038127 ERBB signaling pathway
Biological Process GO:0060325 face morphogenesis
Biological Process GO:0008543 fibroblast growth factor receptor signaling pathway
Biological Process GO:0048806 genitalia development
Biological Process GO:0007507 heart development
Biological Process GO:0048839 inner ear development
Biological Process GO:0033629 negative regulation of cell adhesion mediated by integrin
Biological Process GO:0032331 negative regulation of chondrocyte differentiation
Biological Process GO:1902564 negative regulation of neutrophil activation
Biological Process GO:0050868 negative regulation of T cell activation
Biological Process GO:0042130 negative regulation of T cell proliferation
Biological Process GO:0050860 negative regulation of T cell receptor signaling pathway
Biological Process GO:0032480 negative regulation of type I interferon production
Biological Process GO:0035335 peptidyl-tyrosine dephosphorylation
Biological Process GO:0046326 positive regulation of D-glucose import across plasma membrane
Biological Process GO:0070374 positive regulation of ERK1 and ERK2 cascade
Biological Process GO:0046628 positive regulation of insulin receptor signaling pathway
Biological Process GO:0032728 positive regulation of interferon-beta production
Biological Process GO:0051897 positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction
Biological Process GO:0032760 positive regulation of tumor necrosis factor production
Biological Process GO:0043254 regulation of protein-containing complex assembly
Biological Process GO:0060338 regulation of type I interferon-mediated signaling pathway
Biological Process GO:0031295 T cell costimulation
Biological Process GO:0042311 vasodilation

Reference

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[2] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.

[3] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.

[4] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.

[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.