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Protein

Tyrosine-protein phosphatase non-receptor type 11

Gene

PTPN11

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei429 – 4291SubstrateBy similarity
Active sitei463 – 4631Phosphocysteine intermediate
Binding sitei510 – 5101SubstrateBy similarity

GO - Molecular functioni

  • insulin receptor binding Source: BHF-UCL
  • non-membrane spanning protein tyrosine phosphatase activity Source: UniProtKB
  • phosphoprotein phosphatase activity Source: UniProtKB
  • protein tyrosine phosphatase activity Source: UniProtKB
  • SH3/SH2 adaptor activity Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
ReactomeiREACT_111040. Signaling by SCF-KIT.
REACT_111080. Spry regulation of FGF signaling.
REACT_115697. Prolactin receptor signaling.
REACT_1183. ERK2 activation.
REACT_12519. PECAM1 interactions.
REACT_12578. GAB1 signalosome.
REACT_12621. Tie2 Signaling.
REACT_1391. ERK1 activation.
REACT_147727. Constitutive Signaling by Aberrant PI3K in Cancer.
REACT_169118. Signaling by Leptin.
REACT_17025. Downstream signal transduction.
REACT_19324. PD-1 signaling.
REACT_19344. Costimulation by the CD28 family.
REACT_19405. CTLA4 inhibitory signaling.
REACT_22384. Netrin mediated repulsion signals.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23879. Platelet sensitization by LDL.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
REACT_24980. Regulation of IFNG signaling.
REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
REACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.
REACT_27307. Interleukin-6 signaling.
REACT_355069. FRS-mediated FGFR2 signaling.
REACT_355144. Negative regulation of FGFR3 signaling.
REACT_355159. SHC-mediated cascade:FGFR4.
REACT_355160. PI-3K cascade:FGFR3.
REACT_355212. FRS-mediated FGFR3 signaling.
REACT_355218. Negative regulation of FGFR1 signaling.
REACT_355225. SHC-mediated cascade:FGFR2.
REACT_355227. Negative regulation of FGFR2 signaling.
REACT_355304. PI-3K cascade:FGFR4.
REACT_355450. PI-3K cascade:FGFR2.
REACT_355552. PI-3K cascade:FGFR1.
REACT_355580. FRS2-mediated FGFR4 signaling.
REACT_355584. FRS-mediated FGFR1 signaling.
REACT_355588. Negative regulation of FGFR4 signaling.
REACT_75829. PIP3 activates AKT signaling.
REACT_976. PI3K Cascade.
SignaLinkiQ06124.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase non-receptor type 11 (EC:3.1.3.48)
Alternative name(s):
Protein-tyrosine phosphatase 1D
Short name:
PTP-1D
Protein-tyrosine phosphatase 2C
Short name:
PTP-2C
SH-PTP2
Short name:
SHP-2
Short name:
Shp2
SH-PTP3
Gene namesi
Name:PTPN11
Synonyms:PTP2C, SHPTP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:9644. PTPN11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • mitochondrion Source: Ensembl
  • nucleus Source: UniProtKB
  • protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

LEOPARD syndrome 1 (LPRD1)8 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA disorder characterized by lentigines, electrocardiographic conduction abnormalities, ocular hypertelorism, pulmonic stenosis, abnormalities of genitalia, retardation of growth, and sensorineural deafness.

See also OMIM:151100
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti279 – 2791Y → C in NS1 and LPRD1. 6 Publications
VAR_015614
Natural varianti279 – 2791Y → S in LPRD1. 2 Publications
VAR_027188
Natural varianti465 – 4651A → T in LPRD1. 1 Publication
VAR_027190
Natural varianti468 – 4681G → A in LPRD1. 2 Publications
VAR_027191
Natural varianti472 – 4721T → M in LPRD1. 4 Publications
VAR_015621
Natural varianti502 – 5021R → L in LPRD1. 1 Publication
VAR_027192
Natural varianti502 – 5021R → W in LPRD1; reduced phosphatase activity. 2 Publications
VAR_027193
Natural varianti510 – 5101Q → P in LPRD1. 3 Publications
VAR_027194
Natural varianti514 – 5141Q → P in LPRD1. 1 Publication
VAR_027196
Noonan syndrome 1 (NS1)13 Publications

The disease is caused by mutations affecting the gene represented in this entry. Mutations in PTPN11 account for more than 50% of the cases.

Disease descriptionA 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.

See also OMIM:163950
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21T → I in NS1. 1 Publication
VAR_027183
Natural varianti42 – 421T → A in NS1. 2 Publications
VAR_015601
Natural varianti58 – 581N → K in NS1. 1 Publication
VAR_027184
Natural varianti59 – 591T → A in NS1. 1 Publication
VAR_066060
Natural varianti60 – 601G → A in NS1. 1 Publication
VAR_015602
Natural varianti61 – 611D → G in NS1. 4 Publications
VAR_015603
Natural varianti61 – 611D → N in NS1. 2 Publications
VAR_015604
Natural varianti62 – 621Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications
VAR_015605
Natural varianti63 – 631Y → C in NS1. 6 Publications
VAR_015606
Natural varianti69 – 691E → Q in NS1. 1 Publication
VAR_027185
Natural varianti72 – 721A → G in NS1. 3 Publications
VAR_015607
Natural varianti72 – 721A → S in NS1. 3 Publications
VAR_015608
Natural varianti73 – 731T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications
Corresponds to variant rs28933387 [ dbSNP | Ensembl ].
VAR_015609
Natural varianti76 – 761E → D in NS1. 3 Publications
VAR_015610
Natural varianti79 – 791Q → P in NS1. 1 Publication
VAR_027186
Natural varianti79 – 791Q → R in NS1. 4 Publications
VAR_015611
Natural varianti106 – 1061D → A in NS1. 2 Publications
VAR_015612
Natural varianti139 – 1391E → D in NS1. 2 Publications
VAR_015613
Natural varianti256 – 2561Q → R in NS1. 1 Publication
VAR_027187
Natural varianti279 – 2791Y → C in NS1 and LPRD1. 6 Publications
VAR_015614
Natural varianti282 – 2821I → V in NS1. 3 Publications
VAR_015615
Natural varianti285 – 2851F → L in NS1. 1 Publication
VAR_015617
Natural varianti285 – 2851F → S in NS1. 2 Publications
VAR_015616
Natural varianti308 – 3081N → D in NS1; common mutation. 5 Publications
VAR_015619
Natural varianti308 – 3081N → S in NS1; some patients also manifest giant cell lesions of bone and soft tissue. 2 Publications
VAR_015618
Natural varianti309 – 3091I → V in NS1; unknown pathological significance. 1 Publication
Corresponds to variant rs201787206 [ dbSNP | Ensembl ].
VAR_015620
Natural varianti415 – 4151T → M in NS1. 1 Publication
VAR_027189
Natural varianti495 – 4951P → S in NS1; increased phosphatase activity. 1 Publication
VAR_071706
Natural varianti505 – 5051R → K in NS1. 1 Publication
VAR_015622
Natural varianti506 – 5061S → T in NS1. 2 Publications
VAR_015623
Natural varianti507 – 5071G → R in NS1 and JMML; JMML patient also shows growth retardation and pulmonic stenosis. 2 Publications
VAR_016003
Natural varianti508 – 5081M → V in NS1. 3 Publications
VAR_015624
Natural varianti510 – 5101Q → R in NS1. 1 Publication
VAR_027195
Natural varianti564 – 5641L → F in NS1. 1 Publication
VAR_027197
Leukemia, juvenile myelomonocytic (JMML)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn 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.

See also OMIM:607785
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti61 – 611D → V in JMML; also in myelodysplastic syndrome. 1 Publication
VAR_015991
Natural varianti61 – 611D → Y in JMML. 1 Publication
VAR_015992
Natural varianti69 – 691E → K in JMML; also in myelodysplastic syndrome. 1 Publication
VAR_015993
Natural varianti72 – 721A → T in JMML. 1 Publication
VAR_015996
Natural varianti72 – 721A → V in JMML. 1 Publication
VAR_015997
Natural varianti76 – 761E → A in JMML; also in myelodysplastic syndrome. 1 Publication
VAR_015998
Natural varianti76 – 761E → G in JMML. 1 Publication
VAR_015999
Natural varianti76 – 761E → K in JMML. 1 Publication
Corresponds to variant rs28933388 [ dbSNP | Ensembl ].
VAR_016000
Natural varianti76 – 761E → V in JMML. 1 Publication
VAR_016001
Natural varianti507 – 5071G → A in JMML. 1 Publication
VAR_016002
Natural varianti507 – 5071G → R in NS1 and JMML; JMML patient also shows growth retardation and pulmonic stenosis. 2 Publications
VAR_016003
Metachondromatosis (MC)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA 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.

See also OMIM:156250

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi463 – 4631C → S: Abolishes phosphatase activity. 1 Publication

Keywords - Diseasei

Deafness, Disease mutation

Organism-specific databases

MIMi151100. phenotype.
156250. phenotype.
163950. phenotype.
607785. phenotype.
Orphaneti86834. Juvenile myelomonocytic leukemia.
500. LEOPARD syndrome.
2499. Metachondromatosis.
648. Noonan syndrome.
PharmGKBiPA33986.

Polymorphism and mutation databases

BioMutaiPTPN11.
DMDMi84028248.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 597596Tyrosine-protein phosphatase non-receptor type 11PRO_0000094767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei62 – 621Phosphotyrosine1 Publication
Modified residuei66 – 661PhosphotyrosineBy similarity
Modified residuei546 – 5461Phosphotyrosine; by PDGFRBy similarity
Modified residuei584 – 5841Phosphotyrosine; by PDGFR1 Publication

Post-translational modificationi

Phosphorylated on Tyr-546 and Tyr-584 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.By similarity4 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ06124.
PaxDbiQ06124.
PRIDEiQ06124.

PTM databases

DEPODiQ06124.
PhosphoSiteiQ06124.

Expressioni

Tissue specificityi

Widely expressed, with highest levels in heart, brain, and skeletal muscle.3 Publications

Gene expression databases

BgeeiQ06124.
CleanExiHS_PTPN11.
ExpressionAtlasiQ06124. baseline and differential.
GenevisibleiQ06124. HS.

Organism-specific databases

HPAiCAB005377.

Interactioni

Subunit structurei

Interacts with phosphorylated LIME1 and BCAR3. Interacts with SHB and INPP5D/SHIP1 (By similarity). Interacts with MILR1 (tyrosine-phosphorylated). Interacts with FLT1 (tyrosine-phosphorylated), FLT3 (tyrosine-phosphorylated), FLT4 (tyrosine-phosphorylated), KIT and GRB2. Interacts with PDGFRA (tyrosine phosphorylated). Interacts (via SH2 domain) with TEK/TIE2 (tyrosine phosphorylated) (By similarity). Interacts with PTPNS1 and CD84. Interacts with phosphorylated SIT1 and MPZL1. Interacts with FCRL3, FCRL4, FCRL6 and ANKHD1. Interacts with KIR2DL1; the interaction is enhanced by ARRB2. Interacts with GAB2. Interacts with TERT; the interaction retains TERT in the nucleus. Interacts with PECAM1 and FER. Interacts with EPHA2 (activated); participates in PTK2/FAK1 dephosphorylation in EPHA2 downstream signaling. Interacts with ROS1; mediates PTPN11 phosphorylation. Interacts with PDGFRB (tyrosine phosphorylated); this interaction increases the PTPN11 phosphatase activity. Interacts with GAREM isoform 1 (tyrosine phosphorylated); the interaction increases MAPK/ERK activity and does not affect the GRB2/SOS complex formation.By similarity24 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARP1027512EBI-297779,EBI-608057
CCKBRP322395EBI-297779,EBI-1753137
CD33P201385EBI-297779,EBI-3906571
DDR1Q083454EBI-297779,EBI-711879
EEF1A1P681052EBI-297779,EBI-7645934From a different organism.
EEF1A2Q71V392EBI-297779,EBI-7645815From a different organism.
ERBB2P046262EBI-297779,EBI-641062
FLT1P179482EBI-297779,EBI-1026718
GAB1Q1348039EBI-297779,EBI-517684
GAB2Q9UQC24EBI-297779,EBI-975200
GRB2P629936EBI-297779,EBI-401755
IGF1RP080693EBI-297779,EBI-475981
INSRP062132EBI-297779,EBI-475899
IRS1P355683EBI-297779,EBI-517592
Irs1P355703EBI-297779,EBI-520230From a different organism.
KIR2DL3P436284EBI-297779,EBI-8632435
KITP1072129EBI-297779,EBI-1379503
METP0858113EBI-297779,EBI-1039152
MPZL1O952974EBI-297779,EBI-963338
PDGFRBP096198EBI-297779,EBI-641237
PECAM1P162847EBI-297779,EBI-716404
PXNP490233EBI-297779,EBI-702209
RPIAP492474EBI-297779,EBI-744831
SirpaP977103EBI-297779,EBI-7945080From a different organism.
TRIM32Q130493EBI-297779,EBI-742790

Protein-protein interaction databases

BioGridi111745. 114 interactions.
DIPiDIP-516N.
IntActiQ06124. 64 interactions.
MINTiMINT-199832.
STRINGi9606.ENSP00000340944.

Structurei

Secondary structure

1
597
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni3 – 64Combined sources
Helixi13 – 2311Combined sources
Beta strandi28 – 336Combined sources
Beta strandi35 – 373Combined sources
Beta strandi41 – 477Combined sources
Beta strandi50 – 589Combined sources
Beta strandi59 – 613Combined sources
Beta strandi63 – 686Combined sources
Beta strandi71 – 733Combined sources
Helixi74 – 8310Combined sources
Beta strandi87 – 904Combined sources
Beta strandi91 – 933Combined sources
Helixi107 – 1093Combined sources
Beta strandi113 – 1164Combined sources
Helixi119 – 12810Combined sources
Beta strandi134 – 1396Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi147 – 1537Combined sources
Beta strandi166 – 17510Combined sources
Beta strandi178 – 1847Combined sources
Beta strandi187 – 1893Combined sources
Helixi190 – 19910Combined sources
Beta strandi203 – 2053Combined sources
Beta strandi208 – 2103Combined sources
Beta strandi218 – 2225Combined sources
Helixi223 – 2253Combined sources
Helixi226 – 2349Combined sources
Helixi251 – 2533Combined sources
Helixi259 – 2624Combined sources
Helixi266 – 2694Combined sources
Helixi271 – 2766Combined sources
Beta strandi277 – 2793Combined sources
Helixi286 – 2883Combined sources
Beta strandi289 – 2913Combined sources
Beta strandi304 – 3107Combined sources
Beta strandi327 – 3315Combined sources
Helixi335 – 3373Combined sources
Helixi338 – 34710Combined sources
Beta strandi352 – 3554Combined sources
Beta strandi359 – 3613Combined sources
Beta strandi364 – 3663Combined sources
Beta strandi376 – 3805Combined sources
Beta strandi383 – 39210Combined sources
Beta strandi394 – 40512Combined sources
Helixi413 – 4153Combined sources
Beta strandi417 – 4248Combined sources
Beta strandi429 – 4313Combined sources
Beta strandi434 – 4363Combined sources
Helixi437 – 45115Combined sources
Beta strandi459 – 4679Combined sources
Helixi468 – 48619Combined sources
Beta strandi490 – 4923Combined sources
Helixi494 – 5029Combined sources
Helixi512 – 52817Combined sources
Beta strandi585 – 5895Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2SHPX-ray2.00A/B1-529[»]
3B7OX-ray1.60A237-533[»]
3MOWX-ray2.30A262-532[»]
3O5XX-ray2.00A262-532[»]
3TKZX-ray1.80A1-106[»]
3TL0X-ray2.05A1-106[»]
3ZM0X-ray1.50A248-531[»]
3ZM1X-ray1.40A248-531[»]
3ZM2X-ray1.50A248-531[»]
3ZM3X-ray1.50A248-531[»]
4DGPX-ray2.30A1-532[»]
4DGXX-ray2.30A1-532[»]
4GWFX-ray2.10A/B1-543[»]
4H1OX-ray2.20A1-543[»]
4H34X-ray2.70A1-543[»]
4JE4X-ray2.31A1-103[»]
4JEGX-ray2.30A97-217[»]
4JMGX-ray1.40B579-591[»]
4NWFX-ray2.10A/B1-543[»]
4NWGX-ray2.45A/B1-543[»]
4OHDX-ray2.70A1-532[»]
4OHEX-ray2.51A1-467[»]
A469-532[»]
4OHHX-ray2.70A1-532[»]
4OHIX-ray2.20A1-532[»]
4OHLX-ray2.40A/B1-532[»]
4PVGX-ray2.40A240-532[»]
ProteinModelPortaliQ06124.
SMRiQ06124. Positions 3-595.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ06124.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini6 – 10297SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini112 – 216105SH2 2PROSITE-ProRule annotationAdd
BLAST
Domaini247 – 521275Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni463 – 4697Substrate bindingBy similarity

Domaini

The SH2 domains repress phosphatase activity. Binding of these domains to phosphotyrosine-containing proteins relieves this auto-inhibition, possibly by inducing a conformational change in the enzyme.

Sequence similaritiesi

Contains 2 SH2 domains.PROSITE-ProRule annotation
Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, SH2 domain

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273907.
HOVERGENiHBG000223.
InParanoidiQ06124.
KOiK07293.
OMAiKEYGAMR.
OrthoDBiEOG7NPFST.
PhylomeDBiQ06124.
TreeFamiTF351632.

Family and domain databases

Gene3Di3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000980. SH2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000929. Tyr-Ptase_nr_6. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
SMARTiSM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEiPS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q06124-1) [UniParc]FASTAAdd to basket

Also known as: PTP2Ci

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MTSRRWFHPN ITGVEAENLL LTRGVDGSFL ARPSKSNPGD FTLSVRRNGA
60 70 80 90 100
VTHIKIQNTG DYYDLYGGEK FATLAELVQY YMEHHGQLKE KNGDVIELKY
110 120 130 140 150
PLNCADPTSE RWFHGHLSGK EAEKLLTEKG KHGSFLVRES QSHPGDFVLS
160 170 180 190 200
VRTGDDKGES NDGKSKVTHV MIRCQELKYD VGGGERFDSL TDLVEHYKKN
210 220 230 240 250
PMVETLGTVL QLKQPLNTTR INAAEIESRV RELSKLAETT DKVKQGFWEE
260 270 280 290 300
FETLQQQECK LLYSRKEGQR QENKNKNRYK NILPFDHTRV VLHDGDPNEP
310 320 330 340 350
VSDYINANII MPEFETKCNN SKPKKSYIAT QGCLQNTVND FWRMVFQENS
360 370 380 390 400
RVIVMTTKEV ERGKSKCVKY WPDEYALKEY GVMRVRNVKE SAAHDYTLRE
410 420 430 440 450
LKLSKVGQAL LQGNTERTVW QYHFRTWPDH GVPSDPGGVL DFLEEVHHKQ
460 470 480 490 500
ESIMDAGPVV VHCSAGIGRT GTFIVIDILI DIIREKGVDC DIDVPKTIQM
510 520 530 540 550
VRSQRSGMVQ TEAQYRFIYM AVQHYIETLQ RRIEEEQKSK RKGHEYTNIK
560 570 580 590
YSLADQTSGD QSPLPPCTPT PPCAEMREDS ARVYENVGLM QQQKSFR
Length:597
Mass (Da):68,436
Last modified:December 20, 2005 - v2
Checksum:i37E8BFC7ECA2D03F
GO
Isoform 2 (identifier: Q06124-2) [UniParc]FASTAAdd to basket

Also known as: PTP2C

The sequence of this isoform differs from the canonical sequence as follows:
     408-411: Missing.

Show »
Length:593
Mass (Da):68,011
Checksum:i9CDBEFFA5E6CCB45
GO
Isoform 3 (identifier: Q06124-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     408-411: Missing.
     464-464: S → R
     465-597: Missing.

Show »
Length:460
Mass (Da):52,828
Checksum:iEB8E1553B37F1CC0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti539 – 5391S → R in BAA02740 (PubMed:8216283).Curated
Sequence conflicti552 – 5521S → P in BAA02740 (PubMed:8216283).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti2 – 21T → I in NS1. 1 Publication
VAR_027183
Natural varianti42 – 421T → A in NS1. 2 Publications
VAR_015601
Natural varianti58 – 581N → K in NS1. 1 Publication
VAR_027184
Natural varianti59 – 591T → A in NS1. 1 Publication
VAR_066060
Natural varianti60 – 601G → A in NS1. 1 Publication
VAR_015602
Natural varianti60 – 601G → V in myelodysplastic syndrome. 1 Publication
VAR_015990
Natural varianti61 – 611D → G in NS1. 4 Publications
VAR_015603
Natural varianti61 – 611D → N in NS1. 2 Publications
VAR_015604
Natural varianti61 – 611D → V in JMML; also in myelodysplastic syndrome. 1 Publication
VAR_015991
Natural varianti61 – 611D → Y in JMML. 1 Publication
VAR_015992
Natural varianti62 – 621Y → D in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications
VAR_015605
Natural varianti63 – 631Y → C in NS1. 6 Publications
VAR_015606
Natural varianti69 – 691E → K in JMML; also in myelodysplastic syndrome. 1 Publication
VAR_015993
Natural varianti69 – 691E → Q in NS1. 1 Publication
VAR_027185
Natural varianti71 – 711F → K in acute myeloid leukemia; requires 2 nucleotide substitutions. 1 Publication
VAR_015994
Natural varianti71 – 711F → L in myelodysplastic syndrome. 2 Publications
VAR_015995
Natural varianti72 – 721A → G in NS1. 3 Publications
VAR_015607
Natural varianti72 – 721A → S in NS1. 3 Publications
VAR_015608
Natural varianti72 – 721A → T in JMML. 1 Publication
VAR_015996
Natural varianti72 – 721A → V in JMML. 1 Publication
VAR_015997
Natural varianti73 – 731T → I in NS1; also in Noonan patients manifesting juvenile myelomonocytic leukemia. 4 Publications
Corresponds to variant rs28933387 [ dbSNP | Ensembl ].
VAR_015609
Natural varianti76 – 761E → A in JMML; also in myelodysplastic syndrome. 1 Publication
VAR_015998
Natural varianti76 – 761E → D in NS1. 3 Publications
VAR_015610
Natural varianti76 – 761E → G in JMML. 1 Publication
VAR_015999
Natural varianti76 – 761E → K in JMML. 1 Publication
Corresponds to variant rs28933388 [ dbSNP | Ensembl ].
VAR_016000
Natural varianti76 – 761E → V in JMML. 1 Publication
VAR_016001
Natural varianti79 – 791Q → P in NS1. 1 Publication
VAR_027186
Natural varianti79 – 791Q → R in NS1. 4 Publications
VAR_015611
Natural varianti106 – 1061D → A in NS1. 2 Publications
VAR_015612
Natural varianti139 – 1391E → D in NS1. 2 Publications
VAR_015613
Natural varianti256 – 2561Q → R in NS1. 1 Publication
VAR_027187
Natural varianti279 – 2791Y → C in NS1 and LPRD1. 6 Publications
VAR_015614
Natural varianti279 – 2791Y → S in LPRD1. 2 Publications
VAR_027188
Natural varianti282 – 2821I → V in NS1. 3 Publications
VAR_015615
Natural varianti285 – 2851F → L in NS1. 1 Publication
VAR_015617
Natural varianti285 – 2851F → S in NS1. 2 Publications
VAR_015616
Natural varianti308 – 3081N → D in NS1; common mutation. 5 Publications
VAR_015619
Natural varianti308 – 3081N → S in NS1; some patients also manifest giant cell lesions of bone and soft tissue. 2 Publications
VAR_015618
Natural varianti309 – 3091I → V in NS1; unknown pathological significance. 1 Publication
Corresponds to variant rs201787206 [ dbSNP | Ensembl ].
VAR_015620
Natural varianti415 – 4151T → M in NS1. 1 Publication
VAR_027189
Natural varianti465 – 4651A → T in LPRD1. 1 Publication
VAR_027190
Natural varianti468 – 4681G → A in LPRD1. 2 Publications
VAR_027191
Natural varianti472 – 4721T → M in LPRD1. 4 Publications
VAR_015621
Natural varianti495 – 4951P → S in NS1; increased phosphatase activity. 1 Publication
VAR_071706
Natural varianti502 – 5021R → L in LPRD1. 1 Publication
VAR_027192
Natural varianti502 – 5021R → W in LPRD1; reduced phosphatase activity. 2 Publications
VAR_027193
Natural varianti505 – 5051R → K in NS1. 1 Publication
VAR_015622
Natural varianti506 – 5061S → T in NS1. 2 Publications
VAR_015623
Natural varianti507 – 5071G → A in JMML. 1 Publication
VAR_016002
Natural varianti507 – 5071G → R in NS1 and JMML; JMML patient also shows growth retardation and pulmonic stenosis. 2 Publications
VAR_016003
Natural varianti508 – 5081M → V in NS1. 3 Publications
VAR_015624
Natural varianti510 – 5101Q → P in LPRD1. 3 Publications
VAR_027194
Natural varianti510 – 5101Q → R in NS1. 1 Publication
VAR_027195
Natural varianti514 – 5141Q → P in LPRD1. 1 Publication
VAR_027196
Natural varianti564 – 5641L → F in NS1. 1 Publication
VAR_027197

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei408 – 4114Missing in isoform 2 and isoform 3. 7 PublicationsVSP_016672
Alternative sequencei464 – 4641S → R in isoform 3. 2 PublicationsVSP_016673
Alternative sequencei465 – 597133Missing in isoform 3. 2 PublicationsVSP_016674Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13540 mRNA. Translation: BAA02740.2.
L03535 mRNA. Translation: AAA36611.1.
L07527 mRNA. Translation: AAA17022.1.
L08807 mRNA. No translation available.
X70766 mRNA. Translation: CAA50045.1.
BT007106 mRNA. Translation: AAP35770.1.
AK289854 mRNA. Translation: BAF82543.1.
CH471054 Genomic DNA. Translation: EAW98012.1.
BC008692 mRNA. Translation: AAH08692.1.
CCDSiCCDS58280.1. [Q06124-3]
CCDS9163.1. [Q06124-2]
PIRiJN0805.
RefSeqiNP_002825.3. NM_002834.3. [Q06124-2]
NP_542168.1. NM_080601.1. [Q06124-3]
XP_006719589.1. XM_006719526.1. [Q06124-1]
UniGeneiHs.506852.

Genome annotation databases

EnsembliENST00000351677; ENSP00000340944; ENSG00000179295. [Q06124-2]
ENST00000392597; ENSP00000376376; ENSG00000179295. [Q06124-3]
GeneIDi5781.
KEGGihsa:5781.
UCSCiuc001ttw.1. human. [Q06124-3]
uc001ttx.3. human. [Q06124-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D13540 mRNA. Translation: BAA02740.2.
L03535 mRNA. Translation: AAA36611.1.
L07527 mRNA. Translation: AAA17022.1.
L08807 mRNA. No translation available.
X70766 mRNA. Translation: CAA50045.1.
BT007106 mRNA. Translation: AAP35770.1.
AK289854 mRNA. Translation: BAF82543.1.
CH471054 Genomic DNA. Translation: EAW98012.1.
BC008692 mRNA. Translation: AAH08692.1.
CCDSiCCDS58280.1. [Q06124-3]
CCDS9163.1. [Q06124-2]
PIRiJN0805.
RefSeqiNP_002825.3. NM_002834.3. [Q06124-2]
NP_542168.1. NM_080601.1. [Q06124-3]
XP_006719589.1. XM_006719526.1. [Q06124-1]
UniGeneiHs.506852.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2SHPX-ray2.00A/B1-529[»]
3B7OX-ray1.60A237-533[»]
3MOWX-ray2.30A262-532[»]
3O5XX-ray2.00A262-532[»]
3TKZX-ray1.80A1-106[»]
3TL0X-ray2.05A1-106[»]
3ZM0X-ray1.50A248-531[»]
3ZM1X-ray1.40A248-531[