PTPN11
entrez
5781
canonical
uniprot
Q06124
canonical
ensembl
ENSG00000179295
resolver
ensp
ENSP00000340944
resolver
ensp
ENSP00000376376
resolver
ensp
ENSP00000489597
resolver
ensp
ENSP00000552574
resolver
ensp
ENSP00000552576
resolver
genesymbol
PTPN11
resolver
genesymbol_syn
PTP2C
resolver
genesymbol_syn
SHPTP2
resolver
hgnc
HGNC:9644
resolver
uniprot
A8K1D9
resolver
uniprot
Q96HD7
resolver
uniprot_entry
PTN11_HUMAN
resolver
uniprot_sec
A8K1D9
resolver
uniprot_sec
Q96HD7
resolver
amino_acid_sequence
MTSRRWFHPNITGVEAENLLLTRGVDGSFLARPSKSNPGDFTLSVRRNGAVTHIKIQNTGDYYDLYGGEKFATLAELVQYYMEHHGQLKEKNGDVIELKYPLNCADPTSERWFHGHLSGKEAEKLLTEKGKHGSFLVRESQSHPGDFVLSVRTGDDKGESNDGKSKVTHVMIRCQELKYDVGGGERFDSLTDLVEHYKKNPMVETLGTVLQLKQPLNTTRINAAEIESRVRELSKLAETTDKVKQGFWEEFETLQQQECKLLYSRKEGQRQENKNKNRYKNILPFDHTRVVLHDGDPNEPVSDYINANIIMPEFETKCNNSKPKKSYIATQGCLQNTVNDFWRMVFQENSRVIVMTTKEVERGKSKCVKYWPDEYALKEYGVMRVRNVKESAAHDYTLRELKLSKVGQGNTERTVWQYHFRTWPDHGVPSDPGGVLDFLEEVHHKQESIMDAGPVVVHCSAGIGRTGTFIVIDILIDIIREKGVDCDIDVPKTIQMVRSQRSGMVQTEAQYRFIYMAVQHYIETLQRRIEEEQKSKRKGHEYTNIKYSLADQTSGDQSPLPPCTPTPPCAEMREDSARVYENVGLMQQQKSFR
uniprot
proteins
disease_involvement
DISEASE: LEOPARD syndrome 1 (LPRD1) [MIM:151100]: A disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness. {ECO:0000269|PubMed:12058348, ECO:0000269|PubMed:14961557, ECO:0000269|PubMed:15121796, ECO:0000269|PubMed:15389709, ECO:0000269|PubMed:15520399, ECO:0000269|PubMed:15690106, ECO:0000269|PubMed:16679933, ECO:0000269|PubMed:16733669, ECO:0000269|PubMed:24891296, ECO:0000269|PubMed:26742426}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Noonan syndrome 1 (NS1) [MIM:163950]: A form of Noonan syndrome, a disease characterized by short stature, facial dysmorphic features such as hypertelorism, a downward eyeslant and low-set posteriorly rotated ears, and a high incidence of congenital heart defects and hypertrophic cardiomyopathy. Other features can include a short neck with webbing or redundancy of skin, deafness, motor delay, variable intellectual deficits, multiple skeletal defects, cryptorchidism, and bleeding diathesis. Individuals with Noonan syndrome are at risk of juvenile myelomonocytic leukemia, a myeloproliferative disorder characterized by excessive production of myelomonocytic cells. Some patients with NS1 develop multiple giant cell lesions of the jaw or other bony or soft tissues, which are classified as pigmented villonodular synovitis (PVNS) when occurring in the jaw or joints. {ECO:0000269|PubMed:11704759, ECO:0000269|PubMed:11992261, ECO:0000269|PubMed:12161469, ECO:0000269|PubMed:12325025, ECO:0000269|PubMed:12529711, ECO:0000269|PubMed:12634870, ECO:0000269|PubMed:12717436, ECO:0000269|PubMed:12739139, ECO:0000269|PubMed:12960218, ECO:0000269|PubMed:15384080, ECO:0000269|PubMed:15889278, ECO:0000269|PubMed:15948193, ECO:0000269|PubMed:19020799, ECO:0000269|PubMed:24891296, ECO:0000269|PubMed:28074573}. Note=The disease is caused by variants affecting the gene represented in this entry. Mutations in PTPN11 account for more than 50% of the cases.; DISEASE: Leukemia, juvenile myelomonocytic (JMML) [MIM:607785]: An aggressive pediatric myelodysplastic syndrome/myeloproliferative disorder characterized by malignant transformation in the hematopoietic stem cell compartment with proliferation of differentiated progeny. Patients have splenomegaly, enlarged lymph nodes, rashes, and hemorrhages. {ECO:0000269|PubMed:12717436, ECO:0000269|PubMed:26742426}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Metachondromatosis (MC) [MIM:156250]: A skeletal disorder with radiologic features of both multiple exostoses and Ollier disease, characterized by the presence of exostoses, commonly of the bones of the hands and feet, and enchondromas of the metaphyses of long bones and iliac crest. {ECO:0000269|PubMed:20577567}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
3.1.3.48
uniprot
proteins
function
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). {ECO:0000250|UniProtKB:P35235, ECO:0000269|PubMed:10655584, ECO:0000269|PubMed:14739280, ECO:0000269|PubMed:18559669, ECO:0000269|PubMed:18829466, ECO:0000269|PubMed:19275884, ECO:0000269|PubMed:26742426, ECO:0000269|PubMed:28074573, ECO:0000269|PubMed:32184441}.
uniprot
proteins
mass_dalton
68011
uniprot
proteins
mutagenesis
MUTAGEN 32; /note="R->A: Abolished binding to tyrosine-phosphorylated PDCD1 when associated with A-138."; /evidence="ECO:0000269|PubMed:32184441"; MUTAGEN 138; /note="R->A: Abolished binding to tyrosine-phosphorylated PDCD1 when associated with A-32."; /evidence="ECO:0000269|PubMed:32184441"; MUTAGEN 459; /note="C->S: Abolishes phosphatase activity. Enhances interaction with NEDD9."; /evidence="ECO:0000269|PubMed:19275884, ECO:0000269|PubMed:8216283
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Tyr-542 and Tyr-580 upon receptor protein tyrosine kinase activation; which creates a binding site for GRB2 and other SH2-containing proteins. Phosphorylated upon activation of the receptor-type kinase FLT3. Phosphorylated upon activation of the receptor-type kinase PDGFRA (By similarity). Phosphorylated by activated PDGFRB. {ECO:0000250, ECO:0000269|PubMed:20494825, ECO:0000269|PubMed:34310951, ECO:0000269|PubMed:7681217, ECO:0000269|PubMed:7691811, ECO:0000269|PubMed:8041791}.
uniprot
proteins
protein_family
Non-receptor class 2 subfamily
uniprot
proteins
protein_family
Protein-tyrosine phosphatase family
uniprot
proteins
pubmed
10068651
uniprot
proteins
pubmed
10209036
uniprot
proteins
pubmed
10655584
uniprot
proteins
pubmed
10681522
uniprot
proteins
pubmed
11162587
uniprot
proteins
pubmed
11389028
uniprot
proteins
pubmed
11414741
uniprot
proteins
pubmed
11433379
uniprot
proteins
pubmed
11704759
uniprot
proteins
pubmed
11992261
uniprot
proteins
pubmed
12058348
uniprot
proteins
pubmed
12161469
uniprot
proteins
pubmed
12325025
uniprot
proteins
pubmed
12529711
uniprot
proteins
pubmed
12634870
uniprot
proteins
pubmed
12717436
uniprot
proteins
pubmed
12739139
uniprot
proteins
pubmed
1280823
uniprot
proteins
pubmed
1281790
uniprot
proteins
pubmed
12960218
uniprot
proteins
pubmed
12972546
uniprot
proteins
pubmed
14597715
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14739280
uniprot
proteins
pubmed
14961557
uniprot
proteins
pubmed
15102829
uniprot
proteins
pubmed
15121796
uniprot
proteins
pubmed
15384080
uniprot
proteins
pubmed
15389709
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15520399
uniprot
proteins
pubmed
15526160
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
15690106
uniprot
proteins
pubmed
15889278
uniprot
proteins
pubmed
15948193
uniprot
proteins
pubmed
16679933
uniprot
proteins
pubmed
16733669
uniprot
proteins
pubmed
16885344
uniprot
proteins
pubmed
16956752
uniprot
proteins
pubmed
17213291
uniprot
proteins
pubmed
17562706
uniprot
proteins
pubmed
18559669
uniprot
proteins
pubmed
18604210
uniprot
proteins
pubmed
18829466
uniprot
proteins
pubmed
19020799
uniprot
proteins
pubmed
19167335
uniprot
proteins
pubmed
19275884
uniprot
proteins
pubmed
19342684
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19509291
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19843936
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20170098
uniprot
proteins
pubmed
20494825
uniprot
proteins
pubmed
20577567
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
23112346
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
24891296
uniprot
proteins
pubmed
26742426
uniprot
proteins
pubmed
28074573
uniprot
proteins
pubmed
32184441
uniprot
proteins
pubmed
34310951
uniprot
proteins
pubmed
7681217
uniprot
proteins
pubmed
7681589
uniprot
proteins
pubmed
7691811
uniprot
proteins
pubmed
8041791
uniprot
proteins
pubmed
8216283
uniprot
proteins
pubmed
8810330
uniprot
proteins
pubmed
9062191
uniprot
proteins
pubmed
9491886
uniprot
proteins
pubmed
9600074
uniprot
proteins
sequence_length
593
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26742426}. Nucleus {ECO:0000269|PubMed:26742426}.
uniprot
proteins