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P17706

- PTN2_HUMAN

UniProt

P17706 - PTN2_HUMAN

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Protein
Tyrosine-protein phosphatase non-receptor type 2
Gene
PTPN2, PTPT
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Non-receptor type tyrosine-specific phosphatase that dephosphorylates receptor protein tyrosine kinases including INSR, EGFR, CSF1R, PDGFR. Also dephosphorylates non-receptor protein tyrosine kinases like JAK1, JAK2, JAK3, Src family kinases, STAT1, STAT3, STAT5A, STAT5B and STAT6 either in the nucleus or the cytoplasm. Negatively regulates numerous signaling pathways and biological processes like hematopoiesis, inflammatory response, cell proliferation and differentiation, and glucose homeostasis. Plays a multifaceted and important role in the development of the immune system. Functions in T-cell receptor signaling through dephosphorylation of FYN and LCK to control T-cells differentiation and activation. Dephosphorylates CSF1R, negatively regulating its downstream signaling and macrophage differentiation. Negatively regulates cytokine (IL2/interleukin-2 and interferon)-mediated signaling through dephosphorylation of the cytoplasmic kinases JAK1, JAK3 and their substrate STAT1, that propagate signaling downstream of the cytokine receptors. Also regulates the IL6/interleukin-6 and IL4/interleukin-4 cytokine signaling through dephosphorylation of STAT3 and STAT6 respectively. Beside the immune system, it is involved in anchorage-dependent, negative regulation of EGF-stimulated cell growth. Activated by the integrin ITGA1/ITGB1, it dephosphorylates EGFR and negatively regulates EGF signaling. Dephosphorylates PDGFRB and negatively regulates platelet-derived growth factor receptor-beta signaling pathway and therefore cell proliferation. Negatively regulates tumor necrosis factor-mediated signaling downstream via MAPK through SRC dephosphorylation. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of the hepatocyte growth factor receptor MET. Plays also an important role in glucose homeostasis. For instance, negatively regulates the insulin receptor signaling pathway through the dephosphorylation of INSR and control gluconeogenesis and liver glucose production through negative regulation of the IL6 signaling pathways. Finally, it negatively regulates prolactin-mediated signaling pathway through dephosphorylation of STAT5A and STAT5B. May also bind DNA.11 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Kineticsi

  1. KM=0.48 mM for p-nitrophenyl phosphate (at pH 6.5 and 25 degrees Celsius)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei182 – 1821Substrate By similarity
Active sitei216 – 2161Phosphocysteine intermediate By similarity
Binding sitei260 – 2601Substrate By similarity

GO - Molecular functioni

  1. integrin binding Source: UniProtKB
  2. protein binding Source: UniProtKB
  3. protein kinase binding Source: UniProtKB
  4. protein tyrosine phosphatase activity Source: UniProtKB
  5. receptor tyrosine kinase binding Source: UniProtKB
  6. syntaxin binding Source: UniProtKB

GO - Biological processi

  1. B cell differentiation Source: UniProtKB
  2. T cell differentiation Source: UniProtKB
  3. cytokine-mediated signaling pathway Source: Reactome
  4. erythrocyte differentiation Source: UniProtKB
  5. glucose homeostasis Source: UniProtKB
  6. insulin receptor signaling pathway Source: UniProtKB
  7. interferon-gamma-mediated signaling pathway Source: Reactome
  8. negative regulation of ERK1 and ERK2 cascade Source: UniProtKB
  9. negative regulation of T cell receptor signaling pathway Source: UniProtKB
  10. negative regulation of cell proliferation Source: UniProtKB
  11. negative regulation of chemotaxis Source: UniProtKB
  12. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  13. negative regulation of inflammatory response Source: UniProtKB
  14. negative regulation of insulin receptor signaling pathway Source: UniProtKB
  15. negative regulation of interferon-gamma-mediated signaling pathway Source: UniProtKB
  16. negative regulation of interleukin-2-mediated signaling pathway Source: UniProtKB
  17. negative regulation of interleukin-4-mediated signaling pathway Source: Ensembl
  18. negative regulation of interleukin-6-mediated signaling pathway Source: Ensembl
  19. negative regulation of lipid storage Source: UniProtKB
  20. negative regulation of macrophage colony-stimulating factor signaling pathway Source: UniProtKB
  21. negative regulation of macrophage differentiation Source: UniProtKB
  22. negative regulation of platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  23. negative regulation of positive thymic T cell selection Source: UniProtKB
  24. negative regulation of prolactin signaling pathway Source: UniProtKB
  25. negative regulation of tumor necrosis factor-mediated signaling pathway Source: UniProtKB
  26. negative regulation of type I interferon-mediated signaling pathway Source: UniProtKB
  27. negative regulation of tyrosine phosphorylation of Stat1 protein Source: UniProtKB
  28. negative regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  29. negative regulation of tyrosine phosphorylation of Stat5 protein Source: UniProtKB
  30. negative regulation of tyrosine phosphorylation of Stat6 protein Source: Ensembl
  31. peptidyl-tyrosine dephosphorylation Source: GOC
  32. positive regulation of gluconeogenesis Source: UniProtKB
  33. regulation of hepatocyte growth factor receptor signaling pathway Source: UniProtKB
  34. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_24980. Regulation of IFNG signaling.
SignaLinkiP17706.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase non-receptor type 2 (EC:3.1.3.48)
Alternative name(s):
T-cell protein-tyrosine phosphatase
Short name:
TCPTP
Gene namesi
Name:PTPN2
Synonyms:PTPT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 18

Organism-specific databases

HGNCiHGNC:9650. PTPN2.

Subcellular locationi

Isoform 1 : Endoplasmic reticulum. Endoplasmic reticulum-Golgi intermediate compartment
Note: Targeted to the endoplasmic reticulum by its C-terminal hydrophobic region (1 Publication).5 Publications
Isoform 2 : Nucleus. Cytoplasm. Cell membrane
Note: Predominantly localizes to chromatin By similarity. Able to shuttle between the nucleus and the cytoplasm and to dephosphorylate plasma membrane receptors (1 Publication). Recruited by activated ITGA1 at the plasma membrane.5 Publications

GO - Cellular componenti

  1. endoplasmic reticulum Source: UniProtKB
  2. endoplasmic reticulum-Golgi intermediate compartment Source: UniProtKB
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
  5. plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi182 – 1821D → A: Substrate-trapping mutant; catalytically inactive it forms a stable complex with physiological substrates including INSR and EGFR. Accumulates in the cytoplasm upon stimulation by insulin or EGF; isoform 2. 2 Publications
Mutagenesisi222 – 2221R → M: Impairs phosphatase activity.
Mutagenesisi304 – 3041S → A: Alters phosphorylation by cyclin-dependent kinases of isoform 2 but has no effect on its phosphatase activity. 1 Publication
Mutagenesisi350 – 3523RKR → QQQ: Alters location to the endoplasmic reticulum; isoform 1. 1 Publication
Mutagenesisi380 – 3801K → Q: Prevents location to the nucleus; isoform 2. 1 Publication

Organism-specific databases

Orphaneti206. Crohn disease.
85408. Juvenile rheumatoid factor-negative polyarthritis.
85410. Oligoarticular juvenile arthritis.
771. Ulcerative colitis.
PharmGKBiPA33993.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 415415Tyrosine-protein phosphatase non-receptor type 2
PRO_0000094752Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei298 – 2981Phosphoserine1 Publication
Modified residuei304 – 3041Phosphoserine; by CDK1 and CDK2; in isoform 24 Publications

Post-translational modificationi

Isoform 2: Specifically phosphorylated in a cell cycle-dependent manner by cyclin-dependent kinases. Probably activated through phosphorylation by PKR.2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP17706.
PaxDbiP17706.
PRIDEiP17706.

PTM databases

PhosphoSiteiP17706.

Expressioni

Tissue specificityi

Ubiquitously expressed. Isoform 2 is probably the major isoform. Isoform 1 is expressed in T-cells and in placenta.2 Publications

Inductioni

Up-regulated by IL4/interleukin-4 (at protein level).2 Publications

Gene expression databases

ArrayExpressiP17706.
BgeeiP17706.
CleanExiHS_PTPN2.
GenevestigatoriP17706.

Organism-specific databases

HPAiHPA015004.
HPA046176.

Interactioni

Subunit structurei

Interacts with RMDN3. Isoform 1 interacts with TMED9. Isoform 1 interacts with STX17; dephosphorylates STX17. Interacts with ITGA1 (via cytoplasmic domain); activates the phosphatase activity towards EGFR. Interacts with TRAF2; probably involved in tumor necrosis factor-mediated signaling. Interacts with MET.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
GHRP109128EBI-984930,EBI-286316
TMED10P497555EBI-4409481,EBI-998422
TMED9Q9BVK65EBI-4409481,EBI-1056827

Protein-protein interaction databases

BioGridi111737. 14 interactions.
IntActiP17706. 14 interactions.
MINTiMINT-3975566.
STRINGi9606.ENSP00000311857.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 148
Helixi19 – 2810
Helixi35 – 384
Helixi40 – 456
Turni55 – 573
Beta strandi58 – 603
Beta strandi68 – 769
Helixi77 – 793
Beta strandi81 – 877
Turni91 – 933
Helixi94 – 10310
Beta strandi108 – 1114
Beta strandi129 – 1324
Beta strandi134 – 1363
Turni137 – 1404
Beta strandi141 – 15010
Beta strandi152 – 16312
Turni164 – 1663
Beta strandi169 – 1779
Beta strandi182 – 1843
Helixi190 – 20112
Turni202 – 2054
Beta strandi212 – 22110
Helixi222 – 23514
Beta strandi236 – 2394
Helixi244 – 2518
Turni252 – 2543
Helixi262 – 27514

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1L8KX-ray2.56A1-314[»]
ProteinModelPortaliP17706.
SMRiP17706. Positions 5-277.

Miscellaneous databases

EvolutionaryTraceiP17706.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 275271Tyrosine-protein phosphatase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni216 – 2227Substrate binding By similarity
Regioni346 – 41570Endoplasmic reticulum location
Add
BLAST
Regioni376 – 41540Mediates interaction with STX17
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5599.
HOGENOMiHOG000273908.
HOVERGENiHBG008321.
InParanoidiP17706.
KOiK18026.
OMAiNTAQKVQ.
OrthoDBiEOG7RV9G4.
PhylomeDBiP17706.
TreeFamiTF315897.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR012265. Ptpn1/Ptpn2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P17706-1) [UniParc]FASTAAdd to Basket

Also known as: PTPB, p48TC, TC48, TC-PTPb

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

MPTTIEREFE ELDTQRRWQP LYLEIRNESH DYPHRVAKFP ENRNRNRYRD    50
VSPYDHSRVK LQNAENDYIN ASLVDIEEAQ RSYILTQGPL PNTCCHFWLM 100
VWQQKTKAVV MLNRIVEKES VKCAQYWPTD DQEMLFKETG FSVKLLSEDV 150
KSYYTVHLLQ LENINSGETR TISHFHYTTW PDFGVPESPA SFLNFLFKVR 200
ESGSLNPDHG PAVIHCSAGI GRSGTFSLVD TCLVLMEKGD DINIKQVLLN 250
MRKYRMGLIQ TPDQLRFSYM AIIEGAKCIK GDSSIQKRWK ELSKEDLSPA 300
FDHSPNKIMT EKYNGNRIGL EEEKLTGDRC TGLSSKMQDT MEENSESALR 350
KRIREDRKAT TAQKVQQMKQ RLNENERKRK RWLYWQPILT KMGFMSVILV 400
GAFVGWTLFF QQNAL 415

Note: Minor isoform.

Length:415
Mass (Da):48,473
Last modified:May 5, 2009 - v2
Checksum:i0207694A4F058E68
GO
Isoform 2 (identifier: P17706-2) [UniParc]FASTAAdd to Basket

Also known as: PTPA, p45TC, TC45, TC-PTPa

The sequence of this isoform differs from the canonical sequence as follows:
     382-415: WLYWQPILTKMGFMSVILVGAFVGWTLFFQQNAL → PRLTDT

Note: Major isoform. Contains a nuclear location signal at positions 377-381 (PubMed:7593185) and an autoinhibitory region acting through intramolecular interactions is found at positions 353-387.

Show »
Length:387
Mass (Da):45,168
Checksum:i0F3E622EBA5A92CB
GO
Isoform 3 (identifier: P17706-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     347-380: Missing.
     382-415: WLYWQPILTKMGFMSVILVGAFVGWTLFFQQNAL → PRLTDT

Note: No experimental confirmation available.

Show »
Length:353
Mass (Da):40,990
Checksum:i5AE668EB7D76CB93
GO
Isoform 4 (identifier: P17706-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     165-165: N → NYIENLWITLYLKLLMLDVKRSLK
     382-415: WLYWQPILTKMGFMSVILVGAFVGWTLFFQQNAL → PRLTDT

Note: No experimental confirmation available. Gene prediction based on cDNA data.

Show »
Length:410
Mass (Da):48,017
Checksum:iD6463B9A0F952068
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei165 – 1651N → NYIENLWITLYLKLLMLDVK RSLK in isoform 4.
VSP_054821
Alternative sequencei347 – 38034Missing in isoform 3.
VSP_043383Add
BLAST
Alternative sequencei382 – 41534WLYWQ…QQNAL → PRLTDT in isoform 2, isoform 3 and isoform 4.
VSP_005125Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti407 – 4071T → R in AAA65997. 1 Publication
Sequence conflicti407 – 4071T → R in M81478. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M25393 mRNA. Translation: AAA65997.1.
AK292570 mRNA. Translation: BAF85259.1.
EF445017 Genomic DNA. Translation: ACA06062.1.
EF445017 Genomic DNA. Translation: ACA06064.1.
AP001077 Genomic DNA. No translation available.
AP002449 Genomic DNA. No translation available.
AP005482 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01532.1.
CH471113 Genomic DNA. Translation: EAX01539.1.
BC008244 mRNA. Translation: AAH08244.1.
BC016727 mRNA. Translation: AAH16727.1.
M81478 mRNA. No translation available.
CCDSiCCDS11863.1. [P17706-2]
CCDS11864.1. [P17706-3]
CCDS11865.1. [P17706-1]
CCDS59306.1. [P17706-4]
PIRiA33899.
RefSeqiNP_001193942.1. NM_001207013.1. [P17706-4]
NP_002819.2. NM_002828.3. [P17706-1]
NP_536347.1. NM_080422.2. [P17706-2]
NP_536348.1. NM_080423.2. [P17706-3]
UniGeneiHs.654527.
Hs.663373.

Genome annotation databases

EnsembliENST00000309660; ENSP00000311857; ENSG00000175354. [P17706-1]
ENST00000327283; ENSP00000320298; ENSG00000175354. [P17706-2]
ENST00000353319; ENSP00000320546; ENSG00000175354. [P17706-3]
ENST00000591115; ENSP00000466936; ENSG00000175354.
GeneIDi5771.
KEGGihsa:5771.
UCSCiuc002krm.3. human. [P17706-3]
uc002krp.3. human. [P17706-1]

Polymorphism databases

DMDMi229462762.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M25393 mRNA. Translation: AAA65997.1 .
AK292570 mRNA. Translation: BAF85259.1 .
EF445017 Genomic DNA. Translation: ACA06062.1 .
EF445017 Genomic DNA. Translation: ACA06064.1 .
AP001077 Genomic DNA. No translation available.
AP002449 Genomic DNA. No translation available.
AP005482 Genomic DNA. No translation available.
CH471113 Genomic DNA. Translation: EAX01532.1 .
CH471113 Genomic DNA. Translation: EAX01539.1 .
BC008244 mRNA. Translation: AAH08244.1 .
BC016727 mRNA. Translation: AAH16727.1 .
M81478 mRNA. No translation available.
CCDSi CCDS11863.1. [P17706-2 ]
CCDS11864.1. [P17706-3 ]
CCDS11865.1. [P17706-1 ]
CCDS59306.1. [P17706-4 ]
PIRi A33899.
RefSeqi NP_001193942.1. NM_001207013.1. [P17706-4 ]
NP_002819.2. NM_002828.3. [P17706-1 ]
NP_536347.1. NM_080422.2. [P17706-2 ]
NP_536348.1. NM_080423.2. [P17706-3 ]
UniGenei Hs.654527.
Hs.663373.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1L8K X-ray 2.56 A 1-314 [» ]
ProteinModelPortali P17706.
SMRi P17706. Positions 5-277.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111737. 14 interactions.
IntActi P17706. 14 interactions.
MINTi MINT-3975566.
STRINGi 9606.ENSP00000311857.

Chemistry

BindingDBi P17706.
ChEMBLi CHEMBL3807.

PTM databases

PhosphoSitei P17706.

Polymorphism databases

DMDMi 229462762.

Proteomic databases

MaxQBi P17706.
PaxDbi P17706.
PRIDEi P17706.

Protocols and materials databases

DNASUi 5771.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309660 ; ENSP00000311857 ; ENSG00000175354 . [P17706-1 ]
ENST00000327283 ; ENSP00000320298 ; ENSG00000175354 . [P17706-2 ]
ENST00000353319 ; ENSP00000320546 ; ENSG00000175354 . [P17706-3 ]
ENST00000591115 ; ENSP00000466936 ; ENSG00000175354 .
GeneIDi 5771.
KEGGi hsa:5771.
UCSCi uc002krm.3. human. [P17706-3 ]
uc002krp.3. human. [P17706-1 ]

Organism-specific databases

CTDi 5771.
GeneCardsi GC18M012864.
HGNCi HGNC:9650. PTPN2.
HPAi HPA015004.
HPA046176.
MIMi 176887. gene.
neXtProti NX_P17706.
Orphaneti 206. Crohn disease.
85408. Juvenile rheumatoid factor-negative polyarthritis.
85410. Oligoarticular juvenile arthritis.
771. Ulcerative colitis.
PharmGKBi PA33993.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
HOGENOMi HOG000273908.
HOVERGENi HBG008321.
InParanoidi P17706.
KOi K18026.
OMAi NTAQKVQ.
OrthoDBi EOG7RV9G4.
PhylomeDBi P17706.
TreeFami TF315897.

Enzyme and pathway databases

Reactomei REACT_24980. Regulation of IFNG signaling.
SignaLinki P17706.

Miscellaneous databases

ChiTaRSi PTPN2. human.
EvolutionaryTracei P17706.
GeneWikii PTPN2.
GenomeRNAii 5771.
NextBioi 22446.
PROi P17706.
SOURCEi Search...

Gene expression databases

ArrayExpressi P17706.
Bgeei P17706.
CleanExi HS_PTPN2.
Genevestigatori P17706.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR012265. Ptpn1/Ptpn2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA isolated from a human T-cell library encodes a member of the protein-tyrosine-phosphatase family."
    Cool D., Tonks N.K., Charbonneau H., Walsh K.A., Fischer E.H., Krebs E.G.
    Proc. Natl. Acad. Sci. U.S.A. 86:5257-5261(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY.
    Tissue: T-cell.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Testis.
  3. NHLBI resequencing and genotyping service (RS&G)
    Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
    Tissue: Brain and Eye.
  7. "Cloning and characterization of a mouse cDNA encoding a cytoplasmic protein-tyrosine-phosphatase."
    Mosinger B. Jr., Tillmann U., Westphal H., Tremblay M.L.
    Proc. Natl. Acad. Sci. U.S.A. 89:499-503(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 350-415 (ISOFORM 2), TISSUE SPECIFICITY.
  8. "COOH-terminal sequence motifs target the T cell protein tyrosine phosphatase to the ER and nucleus."
    Lorenzen J.A., Dadabay C.Y., Fischer E.H.
    J. Cell Biol. 131:631-643(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION (ISOFORMS 1 AND 2), MUTAGENESIS OF 350-ARG--ARG-352 AND LYS-380.
  9. "The noncatalytic C-terminal segment of the T cell protein tyrosine phosphatase regulates activity via an intramolecular mechanism."
    Hao L., Tiganis T., Tonks N.K., Charbonneau H.
    J. Biol. Chem. 272:29322-29329(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  10. "Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase."
    Tiganis T., Bennett A.M., Ravichandran K.S., Tonks N.K.
    Mol. Cell. Biol. 18:1622-1634(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF EGFR AND SHC1, MUTAGENESIS OF ASP-182, SUBCELLULAR LOCATION (ISOFORM 2).
  11. "Identification of tyrosine phosphatases that dephosphorylate the insulin receptor. A brute force approach based on 'substrate-trapping' mutants."
    Waelchli S., Curchod M.L., Gobert R.P., Arkinstall S., Hooft van Huijsduijnen R.
    J. Biol. Chem. 275:9792-9796(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF INSR.
  12. "The nuclear isoform of protein-tyrosine phosphatase TC-PTP regulates interleukin-6-mediated signaling pathway through STAT3 dephosphorylation."
    Yamamoto T., Sekine Y., Kashima K., Kubota A., Sato N., Aoki N., Matsuda T.
    Biochem. Biophys. Res. Commun. 297:811-817(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF STAT3(ISOFORM 2).
  13. "The T cell protein tyrosine phosphatase is a negative regulator of janus family kinases 1 and 3."
    Simoncic P.D., Lee-Loy A., Barber D.L., Tremblay M.L., McGlade C.J.
    Curr. Biol. 12:446-453(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF JAK1 AND JAK3, INTERACTION WITH JAK1 AND JAK3.
  14. Cited for: FUNCTION IN DEPHOSPHORYLATION OF STAT1.
  15. "Regulation of insulin receptor signaling by the protein tyrosine phosphatase TCPTP."
    Galic S., Klingler-Hoffmann M., Fodero-Tavoletti M.T., Puryer M.A., Meng T.C., Tonks N.K., Tiganis T.
    Mol. Cell. Biol. 23:2096-2108(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF INSR, MUTAGENESIS OF ASP-182, SUBCELLULAR LOCATION (ISOFORM 2).
  16. "The T-cell protein tyrosine phosphatase is phosphorylated on Ser-304 by cyclin-dependent protein kinases in mitosis."
    Bukczynska P., Klingler-Hoffmann M., Mitchelhill K.I., Lam M.H., Ciccomancini M., Tonks N.K., Sarcevic B., Kemp B.E., Tiganis T.
    Biochem. J. 380:939-949(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-304 BY CDK1 AND CDK2 (ISOFORM 2), MUTAGENESIS OF SER-304.
  17. "Site-selective regulation of platelet-derived growth factor beta receptor tyrosine phosphorylation by T-cell protein tyrosine phosphatase."
    Persson C., Saevenhed C., Bourdeau A., Tremblay M.L., Markova B., Boehmer F.D., Haj F.G., Neel B.G., Elson A., Heldin C.H., Roennstrand L., Ostman A., Hellberg C.
    Mol. Cell. Biol. 24:2190-2201(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF PDGFRB.
  18. "The novel protein PTPIP51 exhibits tissue- and cell-specific expression."
    Stenzinger A., Kajosch T., Tag C., Porsche A., Welte I., Hofer H.W., Steger K., Wimmer M.
    Histochem. Cell Biol. 123:19-28(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RMDN3.
  19. "Negative regulation of EGFR signalling through integrin-alpha1beta1-mediated activation of protein tyrosine phosphatase TCPTP."
    Mattila E., Pellinen T., Nevo J., Vuoriluoto K., Arjonen A., Ivaska J.
    Nat. Cell Biol. 7:78-85(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF EGFR, INTERACTION WITH ITGA1, SUBCELLULAR LOCATION.
  20. "Selective regulation of tumor necrosis factor-induced Erk signaling by Src family kinases and the T cell protein tyrosine phosphatase."
    van Vliet C., Bukczynska P.E., Puryer M.A., Sadek C.M., Shields B.J., Tremblay M.L., Tiganis T.
    Nat. Immunol. 6:253-260(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TRAF2.
  21. "The catalytic activity of the eukaryotic initiation factor-2alpha kinase PKR is required to negatively regulate Stat1 and Stat3 via activation of the T-cell protein-tyrosine phosphatase."
    Wang S., Raven J.F., Baltzis D., Kazemi S., Brunet D.V., Hatzoglou M., Tremblay M.L., Koromilas A.E.
    J. Biol. Chem. 281:9439-9449(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY PKR.
  22. "Evidence for a role of transmembrane protein p25 in localization of protein tyrosine phosphatase TC48 to the ER."
    Gupta V., Swarup G.
    J. Cell Sci. 119:1703-1714(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TMED9.
  23. "T-cell protein tyrosine phosphatase, distinctively expressed in activated-B-cell-like diffuse large B-cell lymphomas, is the nuclear phosphatase of STAT6."
    Lu X., Chen J., Sasmono R.T., Hsi E.D., Sarosiek K.A., Tiganis T., Lossos I.S.
    Mol. Cell. Biol. 27:2166-2179(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF STAT6 (ISOFORM 2), INDUCTION BY IL4.
  24. "Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase."
    Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A., Tremblay M.L., Park M.
    J. Biol. Chem. 283:34374-34383(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF MET, INTERACTION WITH MET.
  25. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 AND SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  26. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "T cell protein tyrosine phosphatase attenuates T cell signaling to maintain tolerance in mice."
    Wiede F., Shields B.J., Chew S.H., Kyparissoudis K., van Vliet C., Galic S., Tremblay M.L., Russell S.M., Godfrey D.I., Tiganis T.
    J. Clin. Invest. 121:4758-4774(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF LCK AND FYN.
  29. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-304, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Tyrosine phosphorylation of a SNARE protein, Syntaxin 17: Implications for membrane trafficking in the early secretory pathway."
    Muppirala M., Gupta V., Swarup G.
    Biochim. Biophys. Acta 1823:2109-2119(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STX17, SUBCELLULAR LOCATION.
  31. Cited for: X-RAY CRYSTALLOGRAPHY (2.56 ANGSTROMS) OF 1-314, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiPTN2_HUMAN
AccessioniPrimary (citable) accession number: P17706
Secondary accession number(s): A8K955
, A8MXU3, K7ENG3, Q96AU5, Q96HR2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: May 5, 2009
Last modified: September 3, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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