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P29350 (PTN6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 171. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosine-protein phosphatase non-receptor type 6

EC=3.1.3.48
Alternative name(s):
Hematopoietic cell protein-tyrosine phosphatase
Protein-tyrosine phosphatase 1C
Short name=PTP-1C
Protein-tyrosine phosphatase SHP-1
SH-PTP1
Gene names
Name:PTPN6
Synonyms:HCP, PTP1C
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length595 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Modulates signaling by tyrosine phosphorylated cell surface receptors such as KIT and the EGF receptor/EGFR. The SH2 regions may interact with other cellular components to modulate its own phosphatase activity against interacting substrates. Together with MTUS1, induces UBE2V2 expression upon angiotensin II stimulation. Plays a key role in hematopoiesis. Ref.20

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

Monomer. Interacts with MTUS1 By similarity. Interacts with MILR1 (tyrosine-phosphorylated). Interacts with KIT By similarity. Binds PTPNS1, LILRB1 and LILRB2. Interacts with FCRL2, FCRL3, FCRL4, CD300LF, CDK2 and CD84. Interacts with KIR2DL1; the interaction is enhanced by ARRB2. Interacts (via SH2 1 domain) with ROS1; the interaction is direct and promotes ROS1 dephosphorylation. Interacts with EGFR; inhibits EGFR-dependent activation of MAPK/ERK. Interacts with LYN. Interacts with the tyrosine phosphorylated form of PDPK1. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.21 Ref.22 Ref.25 Ref.26 Ref.29

Subcellular location

Cytoplasm. Nucleus. Note: In neurons, translocates into the nucleus after treatment with angiotensin II By similarity. Shuttles between the cytoplasm and nucleus via its association with PDPK1. Ref.26 Ref.29

Tissue specificity

Isoform 1 is expressed in hematopoietic cells. Isoform 2 is expressed in non-hematopoietic cells.

Domain

The N-terminal SH2 domain functions as an auto-inhibitory domain, blocking the catalytic domain in the ligand-free close conformation. Ref.31 Ref.33

Post-translational modification

Phosphorylated on tyrosine residues. Binding of KITLG/SCF to KIT increases tyrosine phosphorylation By similarity. Phosphorylation at Tyr-564 enhances phosphatase activity. Ref.13 Ref.17

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 2 subfamily.

Contains 2 SH2 domains.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DomainRepeat
SH2 domain
   Molecular functionHydrolase
Protein phosphatase
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

G-protein coupled receptor signaling pathway

Traceable author statement Ref.13. Source: ProtInc

JAK-STAT cascade involved in growth hormone signaling pathway

Traceable author statement. Source: Reactome

T cell costimulation

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement PubMed 10506221. Source: ProtInc

blood coagulation

Traceable author statement. Source: Reactome

cell differentiation

Inferred from direct assay Ref.20. Source: UniProtKB

cell proliferation

Inferred from direct assay Ref.20. Source: UniProtKB

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

leukocyte migration

Traceable author statement. Source: Reactome

natural killer cell mediated cytotoxicity

Inferred from electronic annotation. Source: Ensembl

negative regulation of MAP kinase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of T cell proliferation

Inferred from electronic annotation. Source: Ensembl

negative regulation of T cell receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of cell proliferation

Non-traceable author statement Ref.7. Source: UniProtKB

negative regulation of humoral immune response mediated by circulating immunoglobulin

Inferred from electronic annotation. Source: Ensembl

negative regulation of peptidyl-tyrosine phosphorylation

Inferred from mutant phenotype PubMed 19749791. Source: BHF-UCL

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 18802077Ref.14. Source: UniProtKB

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 19749791PubMed 19838216. Source: BHF-UCL

positive regulation of phosphatidylinositol 3-kinase signaling

Inferred from mutant phenotype PubMed 19838216. Source: BHF-UCL

protein dephosphorylation

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of B cell differentiation

Inferred from electronic annotation. Source: Ensembl

regulation of ERK1 and ERK2 cascade

Inferred from direct assay Ref.20. Source: UniProtKB

regulation of G1/S transition of mitotic cell cycle

Inferred from mutant phenotype PubMed 19838216. Source: BHF-UCL

regulation of interferon-gamma-mediated signaling pathway

Traceable author statement. Source: Reactome

regulation of type I interferon-mediated signaling pathway

Traceable author statement. Source: Reactome

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentalpha-beta T cell receptor complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay PubMed 10940933. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867PubMed 20458337. Source: UniProt

membrane

Traceable author statement PubMed 10506221. Source: ProtInc

nucleolus

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay PubMed 19838216. Source: BHF-UCL

   Molecular_functionprotein kinase binding

Inferred from physical interaction Ref.20. Source: UniProtKB

protein tyrosine phosphatase activity

Traceable author statement. Source: Reactome

transmembrane receptor protein tyrosine phosphatase activity

Inferred from direct assay Ref.20. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P29350-1)

Also known as: Long;

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.
Isoform 2 (identifier: P29350-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MVR → MLSRG
Isoform 3 (identifier: P29350-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-44: SLSVR → MLSRG
Isoform 4 (identifier: P29350-4)

Also known as: 70-kDa; SHP-1L;

The sequence of this isoform differs from the canonical sequence as follows:
     559-595: HKEDVYENLH...EKSKGSLKRK → SLESSAGTVA...CTLRTRGRRK

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 595595Tyrosine-protein phosphatase non-receptor type 6
PRO_0000094758

Regions

Domain4 – 10097SH2 1
Domain110 – 213104SH2 2
Domain244 – 515272Tyrosine-protein phosphatase
Region453 – 4597Substrate binding By similarity

Sites

Active site4531Phosphocysteine intermediate
Binding site4191Substrate By similarity
Binding site5001Substrate By similarity

Amino acid modifications

Modified residue641Phosphotyrosine Ref.27
Modified residue3771Phosphotyrosine By similarity
Modified residue5361Phosphotyrosine By similarity
Modified residue5641Phosphotyrosine; by LYN Ref.17

Natural variations

Alternative sequence1 – 3939Missing in isoform 3.
VSP_005129
Alternative sequence1 – 33MVR → MLSRG in isoform 2.
VSP_007775
Alternative sequence40 – 445SLSVR → MLSRG in isoform 3.
VSP_005130
Alternative sequence559 – 59537HKEDV…SLKRK → SLESSAGTVAASPVRRGGQR GLPVPGPPVLSPDLHQLPVL APLHPAADTRRMCMRTCTLR TRGRRK in isoform 4.
VSP_044447

Experimental info

Sequence conflict61H → L in AAA82880. Ref.5
Sequence conflict861L → V in AAA36610. Ref.4
Sequence conflict861L → V in AAD53317. Ref.7
Sequence conflict1461V → E in AAA82880. Ref.5
Sequence conflict1461V → E in AAA82879. Ref.5

Secondary structure

......................................................................................................... 595
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Long) [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 4D7736C21D3542D2

FASTA59567,561
        10         20         30         40         50         60 
MVRWFHRDLS GLDAETLLKG RGVHGSFLAR PSRKNQGDFS LSVRVGDQVT HIRIQNSGDF 

        70         80         90        100        110        120 
YDLYGGEKFA TLTELVEYYT QQQGVLQDRD GTIIHLKYPL NCSDPTSERW YHGHMSGGQA 

       130        140        150        160        170        180 
ETLLQAKGEP WTFLVRESLS QPGDFVLSVL SDQPKAGPGS PLRVTHIKVM CEGGRYTVGG 

       190        200        210        220        230        240 
LETFDSLTDL VEHFKKTGIE EASGAFVYLR QPYYATRVNA ADIENRVLEL NKKQESEDTA 

       250        260        270        280        290        300 
KAGFWEEFES LQKQEVKNLH QRLEGQRPEN KGKNRYKNIL PFDHSRVILQ GRDSNIPGSD 

       310        320        330        340        350        360 
YINANYIKNQ LLGPDENAKT YIASQGCLEA TVNDFWQMAW QENSRVIVMT TREVEKGRNK 

       370        380        390        400        410        420 
CVPYWPEVGM QRAYGPYSVT NCGEHDTTEY KLRTLQVSPL DNGDLIREIW HYQYLSWPDH 

       430        440        450        460        470        480 
GVPSEPGGVL SFLDQINQRQ ESLPHAGPII VHCSAGIGRT GTIIVIDMLM ENISTKGLDC 

       490        500        510        520        530        540 
DIDIQKTIQM VRAQRSGMVQ TEAQYKFIYV AIAQFIETTK KKLEVLQSQK GQESEYGNIT 

       550        560        570        580        590 
YPPAMKNAHA KASRTSSKHK EDVYENLHTK NKREEKVKKQ RSADKEKSKG SLKRK 

« Hide

Isoform 2 [UniParc].

Checksum: 6A291A2860159389
Show »

FASTA59767,719
Isoform 3 (Short) [UniParc].

Checksum: E903558D44643643
Show »

FASTA55663,125
Isoform 4 (70-kDa) (SHP-1L) [UniParc].

Checksum: CB73D33EA910A7A0
Show »

FASTA62470,131

References

« Hide 'large scale' references
[1]"Protein tyrosine phosphatase containing SH2 domains: characterization, preferential expression in hematopoietic cells, and localization to human chromosome 12p12-p13."
Yi T., Cleveland J.L., Ihle J.N.
Mol. Cell. Biol. 12:836-846(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"A protein-tyrosine phosphatase with sequence similarity to the SH2 domain of the protein-tyrosine kinases."
Shen S.H., Bastien L., Posner B.I., Chretien P.
Nature 352:736-739(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Mammary gland.
[3]Erratum
Shen S.H., Bastien L., Posner B.I., Chretien P.
Nature 353:868-868(1991)
Cited for: SEQUENCE REVISION.
[4]"Isolation of a src homology 2-containing tyrosine phosphatase."
Plutzky J., Neel B.G., Rosenberg R.D.
Proc. Natl. Acad. Sci. U.S.A. 89:1123-1127(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]"Human protein tyrosine phosphatase 1C (PTPN6) gene structure: alternate promoter usage and exon skipping generate multiple transcripts."
Banville D., Stocco R., Shen S.H.
Genomics 27:165-173(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[6]"Large-scale sequencing in human chromosome 12p13: experimental and computational gene structure determination."
Ansari-Lari M.A., Shen Y., Muzny D.M., Lee W., Gibbs R.A.
Genome Res. 7:268-280(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[7]"Human 70-kDa SHP-1L differs from 68-kDa SHP-1 in its C-terminal structure and catalytic activity."
Jin Y.J., Yu C.L., Burakoff S.J.
J. Biol. Chem. 274:28301-28307(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[8]"Gene silencing of SHP-1 gene in leukemias/lymphomas by aberrant methylation."
Oka T., Ouchida M.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1 AND 2).
[9]"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. expand/collapse author list , 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: Umbilical cord blood.
[10]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[11]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]"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] (ISOFORM 2).
Tissue: Placenta.
[13]"Tyrosine phosphorylation of an SH2-containing protein tyrosine phosphatase is coupled to platelet thrombin receptor via a pertussis toxin-sensitive heterotrimeric G-protein."
Li R.Y., Gaits F., Ragab A., Ragab-Thomas J.M.F., Chap H.
EMBO J. 14:2519-2526(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[14]"A novel immunoglobulin superfamily receptor for cellular and viral MHC class I molecules."
Cosman D., Fanger N., Borges L., Kubin M., Chin W., Peterson L., Hsu M.-L.
Immunity 7:273-282(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LILRB1.
[15]"The MHC class I binding proteins LIR-1 and LIR-2 inhibit Fc receptor-mediated signaling in monocytes."
Fanger N.A., Cosman D., Peterson L., Braddy S.C., Maliszewski C.R., Borges L.
Eur. J. Immunol. 28:3423-3434(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LILRB2.
[16]"High expression of inhibitory receptor SHPS-1 and its association with protein tyrosine phosphatase SHP-1 in macrophages."
Veillette A., Thibaudeau E., Latour S.
J. Biol. Chem. 273:22719-22728(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PTPNS1.
[17]"Functional interaction between SHPTP1 and the Lyn tyrosine kinase in the apoptotic response to DNA damage."
Yoshida K., Kharbanda S., Kufe D.
J. Biol. Chem. 274:34663-34668(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LYN, PHOSPHORYLATION AT TYR-564.
[18]"Molecular cloning and characterization of SPAP1, an inhibitory receptor."
Xu M.-J., Zhao R., Zhao Z.J.
Biochem. Biophys. Res. Commun. 280:768-775(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCRL2 AND FCRL3.
[19]"Distinct interactions of the X-linked lymphoproliferative syndrome gene product SAP with cytoplasmic domains of members of the CD2 receptor family."
Lewis J., Eiben L.J., Nelson D.L., Cohen J.I., Nichols K.E., Ochs H.D., Notarangelo L.D., Duckett C.S.
Clin. Immunol. 100:15-23(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD84.
[20]"Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1."
Keilhack H., Mueller M., Boehmer S.A., Frank C., Weidner K.M., Birchmeier W., Ligensa T., Berndt A., Kosmehl H., Guenther B., Mueller T., Birchmeier C., Boehmer F.D.
J. Cell Biol. 152:325-334(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ROS1 DEPHOSPHORYLATION, INTERACTION WITH ROS1.
[21]"The inhibitory potential of Fc receptor homolog 4 on memory B cells."
Ehrhardt G.R.A., Davis R.S., Hsu J.T., Leu C.-M., Ehrhardt A., Cooper M.D.
Proc. Natl. Acad. Sci. U.S.A. 100:13489-13494(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCRL4.
[22]"IgSF13, a novel human inhibitory receptor of the immunoglobulin superfamily, is preferentially expressed in dendritic cells and monocytes."
Sui L., Li N., Liu Q., Zhang W., Wan T., Wang B., Luo K., Sun H., Cao X.
Biochem. Biophys. Res. Commun. 319:920-928(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD300LF.
[23]"Signal transduction via the stem cell factor receptor/c-Kit."
Ronnstrand L.
Cell. Mol. Life Sci. 61:2535-2548(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[24]"Signaling by Kit protein-tyrosine kinase--the stem cell factor receptor."
Roskoski R. Jr.
Biochem. Biophys. Res. Commun. 337:1-13(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ROLE IN KIT SIGNALING.
[25]"An essential function for beta-arrestin 2 in the inhibitory signaling of natural killer cells."
Yu M.-C., Su L.-L., Zou L., Liu Y., Wu N., Kong L., Zhuang Z.-H., Sun L., Liu H.P., Hu J.-H., Li D., Strominger J.L., Zang J.-W., Pei G., Ge B.-X.
Nat. Immunol. 9:898-907(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KIR2DL1.
[26]"The nuclear localization of 3'-phosphoinositide-dependent kinase-1 is dependent on its association with the protein tyrosine phosphatase SHP-1."
Sephton C.F., Zhang D., Lehmann T.M., Pennington P.R., Scheid M.P., Mousseau D.D.
Cell. Signal. 21:1634-1644(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PDPK1.
[27]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[28]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[29]"Compartmentalized CDK2 is connected with SHP-1 and beta-catenin and regulates insulin internalization."
Fiset A., Xu E., Bergeron S., Marette A., Pelletier G., Siminovitch K.A., Olivier M., Beauchemin N., Faure R.L.
Cell. Signal. 23:911-919(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CDK2.
[30]"Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1."
Yang J., Liang X., Niu T., Meng W., Zhao Z., Zhou G.W.
J. Biol. Chem. 273:28199-28207(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 248-399.
[31]"Crystal structure of human protein-tyrosine phosphatase SHP-1."
Yang J., Liu L., He D., Song X., Liang X., Zhao Z.J., Zhou G.W.
J. Biol. Chem. 278:6516-6520(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-532, DOMAIN SH2.
[32]"Solution structures of the SH2 domain of human protein-tyrosine phosphatase SHP-1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 110-214.
[33]"Crystal structure of human protein tyrosine phosphatase SHP-1 in the open conformation."
Wang W., Liu L., Song X., Mo Y., Komma C., Bellamy H.D., Zhao Z.J., Zhou G.W.
J. Cell. Biochem. 112:2062-2071(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), DOMAIN SH2.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M74903 mRNA. Translation: AAA35963.1.
X62055 mRNA. Translation: CAA43982.1.
M77273 mRNA. Translation: AAA36610.1.
U15528 expand/collapse EMBL AC list , U15536, U15535, U15534, U15533, U15532, U15531, U15530, U15529 Genomic DNA. Translation: AAA82880.1.
U15528 expand/collapse EMBL AC list , U15537, U15535, U15534, U15533, U15532, U15531, U15530, U15529 Genomic DNA. Translation: AAA82879.1.
U47924 Genomic DNA. Translation: AAB51322.1.
U47924 Genomic DNA. Translation: AAB51323.1.
AF178946 mRNA. Translation: AAD53317.1.
AB079851 Genomic DNA. Translation: BAC81774.1.
AB079851 Genomic DNA. Translation: BAC81775.1.
AK290421 mRNA. Translation: BAF83110.1.
CH471116 Genomic DNA. Translation: EAW88703.1.
CH471116 Genomic DNA. Translation: EAW88704.1.
BC002523 mRNA. Translation: AAH02523.1.
BC007667 mRNA. Translation: AAH07667.1.
PIRS20825. B42031.
RefSeqNP_002822.2. NM_002831.5.
NP_536858.1. NM_080548.4.
NP_536859.1. NM_080549.3.
UniGeneHs.63489.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1FPRX-ray2.50A243-526[»]
1GWZX-ray2.50A243-541[»]
1X6CNMR-A110-214[»]
2B3OX-ray2.80A1-532[»]
2RMXNMR-A110-214[»]
2YU7NMR-A110-214[»]
3PS5X-ray3.10A1-595[»]
4GRYX-ray1.70A243-528[»]
4GRZX-ray1.37A243-528[»]
4GS0X-ray1.80A/B243-528[»]
4HJPX-ray1.40A243-528[»]
4HJQX-ray1.80A/B243-528[»]
ProteinModelPortalP29350.
SMRP29350. Positions 1-529.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111742. 58 interactions.
DIPDIP-31002N.
IntActP29350. 43 interactions.
MINTMINT-134053.
STRING9606.ENSP00000391592.

Chemistry

BindingDBP29350.
ChEMBLCHEMBL3166.

PTM databases

PhosphoSiteP29350.

Polymorphism databases

DMDM131469.

2D gel databases

OGPP29350.

Proteomic databases

PaxDbP29350.
PRIDEP29350.

Protocols and materials databases

DNASU5777.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000318974; ENSP00000326010; ENSG00000111679. [P29350-1]
ENST00000399448; ENSP00000382376; ENSG00000111679. [P29350-3]
ENST00000447931; ENSP00000415979; ENSG00000111679. [P29350-2]
ENST00000456013; ENSP00000391592; ENSG00000111679. [P29350-4]
ENST00000594686; ENSP00000468853; ENSG00000268954. [P29350-4]
ENST00000595623; ENSP00000472428; ENSG00000268954. [P29350-1]
ENST00000595832; ENSP00000469169; ENSG00000268954. [P29350-3]
ENST00000599028; ENSP00000470980; ENSG00000268954. [P29350-2]
GeneID5777.
KEGGhsa:5777.
UCSCuc001qsb.2. human. [P29350-1]
uc009zfl.1. human. [P29350-4]
uc010sfr.1. human. [P29350-2]

Organism-specific databases

CTD5777.
GeneCardsGC12P007055.
HGNCHGNC:9658. PTPN6.
HPACAB004572.
HPA001466.
MIM176883. gene.
neXtProtNX_P29350.
PharmGKBPA34002.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000273907.
HOVERGENHBG000223.
InParanoidP29350.
KOK05697.
OMAQAKGEPW.
PhylomeDBP29350.
TreeFamTF351632.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111155. Cell-Cell communication.
REACT_604. Hemostasis.
REACT_6900. Immune System.
SignaLinkP29350.

Gene expression databases

ArrayExpressP29350.
BgeeP29350.
CleanExHS_PTPN6.
GenevestigatorP29350.

Family and domain databases

Gene3D3.30.505.10. 2 hits.
InterProIPR000980. 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]
PfamPF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000929. Tyr-Ptase_nr_6. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
SMARTSM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view]
SUPFAMSSF55550. SSF55550. 2 hits.
PROSITEPS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN6. human.
EvolutionaryTraceP29350.
GeneWikiPTPN6.
GenomeRNAi5777.
NextBio22466.
PMAP-CutDBP29350.
PROP29350.
SOURCESearch...

Entry information

Entry namePTN6_HUMAN
AccessionPrimary (citable) accession number: P29350
Secondary accession number(s): A8K306 expand/collapse secondary AC list , G3V0F8, Q969V8, Q9UK67
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: April 16, 2014
This is version 171 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM