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P29350

- PTN6_HUMAN

UniProt

P29350 - PTN6_HUMAN

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Protein

Tyrosine-protein phosphatase non-receptor type 6

Gene

PTPN6

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

Functioni

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.1 Publication

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei419 – 4191SubstrateBy similarity
Active sitei453 – 4531Phosphocysteine intermediate
Binding sitei500 – 5001SubstrateBy similarity

GO - Molecular functioni

  1. protein kinase binding Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: Reactome
  3. transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. abortive mitotic cell cycle Source: Ensembl
  2. apoptotic process Source: ProtInc
  3. B cell receptor signaling pathway Source: Ensembl
  4. blood coagulation Source: Reactome
  5. cell differentiation Source: UniProtKB
  6. cell proliferation Source: UniProtKB
  7. cytokine-mediated signaling pathway Source: Reactome
  8. G-protein coupled receptor signaling pathway Source: ProtInc
  9. interferon-gamma-mediated signaling pathway Source: Reactome
  10. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  11. leukocyte migration Source: Reactome
  12. megakaryocyte development Source: Ensembl
  13. natural killer cell mediated cytotoxicity Source: Ensembl
  14. negative regulation of B cell receptor signaling pathway Source: Ensembl
  15. negative regulation of cell proliferation Source: UniProtKB
  16. negative regulation of humoral immune response mediated by circulating immunoglobulin Source: Ensembl
  17. negative regulation of MAP kinase activity Source: Ensembl
  18. negative regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  19. negative regulation of T cell proliferation Source: Ensembl
  20. negative regulation of T cell receptor signaling pathway Source: Ensembl
  21. peptidyl-tyrosine dephosphorylation Source: GOC
  22. peptidyl-tyrosine phosphorylation Source: UniProtKB
  23. platelet aggregation Source: Ensembl
  24. platelet formation Source: Ensembl
  25. positive regulation of cell adhesion mediated by integrin Source: Ensembl
  26. positive regulation of cell proliferation Source: BHF-UCL
  27. positive regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  28. protein dephosphorylation Source: UniProtKB
  29. regulation of B cell differentiation Source: Ensembl
  30. regulation of ERK1 and ERK2 cascade Source: UniProtKB
  31. regulation of G1/S transition of mitotic cell cycle Source: BHF-UCL
  32. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
  33. regulation of release of sequestered calcium ion into cytosol Source: Ensembl
  34. regulation of type I interferon-mediated signaling pathway Source: Reactome
  35. T cell costimulation Source: Reactome
  36. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_111133. Growth hormone receptor signaling.
REACT_111225. Regulation of KIT signaling.
REACT_12519. PECAM1 interactions.
REACT_19324. PD-1 signaling.
REACT_19344. Costimulation by the CD28 family.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23879. Platelet sensitization by LDL.
REACT_23891. Interleukin receptor SHC signaling.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
REACT_24980. Regulation of IFNG signaling.
REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.
SignaLinkiP29350.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PTPN6
Synonyms:HCP, PTP1C
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:9658. PTPN6.

Subcellular locationi

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.By similarity

GO - Cellular componenti

  1. alpha-beta T cell receptor complex Source: Ensembl
  2. cell-cell junction Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. cytosol Source: Reactome
  5. extracellular vesicular exosome Source: UniProt
  6. membrane Source: ProtInc
  7. nucleolus Source: HPA
  8. nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34002.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 595595Tyrosine-protein phosphatase non-receptor type 6PRO_0000094758Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei64 – 641Phosphotyrosine1 Publication
Modified residuei377 – 3771PhosphotyrosineBy similarity
Modified residuei536 – 5361PhosphotyrosineBy similarity
Modified residuei564 – 5641Phosphotyrosine; by LYN1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues. Binding of KITLG/SCF to KIT increases tyrosine phosphorylation (By similarity). Phosphorylation at Tyr-564 enhances phosphatase activity.By similarity3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP29350.
PaxDbiP29350.
PRIDEiP29350.

2D gel databases

OGPiP29350.

PTM databases

PhosphoSiteiP29350.

Miscellaneous databases

PMAP-CutDBP29350.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP29350.
CleanExiHS_PTPN6.
ExpressionAtlasiP29350. baseline and differential.
GenevestigatoriP29350.

Organism-specific databases

HPAiCAB004572.
HPA001466.

Interactioni

Subunit structurei

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.By similarity12 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CASP8Q147903EBI-78260,EBI-78060
CD22P202734EBI-78260,EBI-78277
CD33P201388EBI-78260,EBI-3906571
CD37P110494EBI-78260,EBI-6139068
EPORP1923511EBI-78260,EBI-617321
FCGR2BP319943EBI-78260,EBI-724784
KIR2DL1P436264EBI-78260,EBI-8684277
KIR2DL3P4362813EBI-78260,EBI-8632435
LAIR1Q6GTX85EBI-78260,EBI-965864
LCKP062395EBI-78260,EBI-1348
PECAM1P162844EBI-78260,EBI-716404
PILRAQ9UKJ15EBI-78260,EBI-965833
ROS1P089222EBI-78260,EBI-7371065
tirB7UM994EBI-78260,EBI-2504426From a different organism.
tirQ7DB772EBI-78260,EBI-6480811From a different organism.

Protein-protein interaction databases

BioGridi111742. 59 interactions.
DIPiDIP-31002N.
IntActiP29350. 43 interactions.
MINTiMINT-134053.
STRINGi9606.ENSP00000391592.

Structurei

Secondary structure

1
595
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi11 – 2111
Beta strandi26 – 316
Beta strandi33 – 4513
Beta strandi48 – 558
Beta strandi57 – 593
Beta strandi61 – 633
Beta strandi68 – 703
Helixi72 – 809
Beta strandi89 – 913
Helixi105 – 1073
Beta strandi111 – 1144
Helixi117 – 12711
Beta strandi132 – 1376
Beta strandi139 – 1413
Beta strandi145 – 15410
Beta strandi155 – 1573
Beta strandi162 – 1709
Helixi172 – 1743
Beta strandi175 – 1817
Beta strandi184 – 1863
Helixi187 – 19711
Beta strandi199 – 2013
Beta strandi202 – 2043
Beta strandi205 – 2073
Helixi221 – 2233
Beta strandi236 – 2383
Helixi244 – 25613
Turni257 – 2593
Helixi263 – 2664
Helixi268 – 2736
Beta strandi275 – 2784
Turni283 – 2853
Beta strandi286 – 2883
Beta strandi290 – 2923
Beta strandi294 – 2963
Turni297 – 3004
Beta strandi301 – 3077
Beta strandi309 – 3124
Helixi314 – 3163
Beta strandi321 – 3244
Helixi329 – 3313
Helixi332 – 34110
Beta strandi346 – 3494
Beta strandi353 – 3553
Beta strandi356 – 3583
Beta strandi371 – 3744
Beta strandi377 – 38610
Beta strandi388 – 39912
Helixi400 – 4023
Beta strandi403 – 4053
Beta strandi407 – 4148
Beta strandi419 – 4213
Beta strandi424 – 4263
Helixi427 – 44216
Beta strandi443 – 4453
Beta strandi449 – 4524
Beta strandi454 – 4574
Helixi458 – 47619
Helixi484 – 4929
Helixi502 – 52322

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP29350.
SMRiP29350. Positions 1-529.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29350.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini4 – 10097SH2 1PROSITE-ProRule annotationAdd
BLAST
Domaini110 – 213104SH2 2PROSITE-ProRule annotationAdd
BLAST
Domaini244 – 515272Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni453 – 4597Substrate bindingBy similarity

Domaini

The N-terminal SH2 domain functions as an auto-inhibitory domain, blocking the catalytic domain in the ligand-free close conformation.2 Publications

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.
GeneTreeiENSGT00760000118836.
HOGENOMiHOG000273907.
HOVERGENiHBG000223.
InParanoidiP29350.
KOiK05697.
OMAiQAKGEPW.
PhylomeDBiP29350.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P29350-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MVRWFHRDLS GLDAETLLKG RGVHGSFLAR PSRKNQGDFS LSVRVGDQVT
60 70 80 90 100
HIRIQNSGDF YDLYGGEKFA TLTELVEYYT QQQGVLQDRD GTIIHLKYPL
110 120 130 140 150
NCSDPTSERW YHGHMSGGQA ETLLQAKGEP WTFLVRESLS QPGDFVLSVL
160 170 180 190 200
SDQPKAGPGS PLRVTHIKVM CEGGRYTVGG LETFDSLTDL VEHFKKTGIE
210 220 230 240 250
EASGAFVYLR QPYYATRVNA ADIENRVLEL NKKQESEDTA KAGFWEEFES
260 270 280 290 300
LQKQEVKNLH QRLEGQRPEN KGKNRYKNIL PFDHSRVILQ GRDSNIPGSD
310 320 330 340 350
YINANYIKNQ LLGPDENAKT YIASQGCLEA TVNDFWQMAW QENSRVIVMT
360 370 380 390 400
TREVEKGRNK CVPYWPEVGM QRAYGPYSVT NCGEHDTTEY KLRTLQVSPL
410 420 430 440 450
DNGDLIREIW HYQYLSWPDH GVPSEPGGVL SFLDQINQRQ ESLPHAGPII
460 470 480 490 500
VHCSAGIGRT GTIIVIDMLM ENISTKGLDC DIDIQKTIQM VRAQRSGMVQ
510 520 530 540 550
TEAQYKFIYV AIAQFIETTK KKLEVLQSQK GQESEYGNIT YPPAMKNAHA
560 570 580 590
KASRTSSKHK EDVYENLHTK NKREEKVKKQ RSADKEKSKG SLKRK
Length:595
Mass (Da):67,561
Last modified:December 1, 1992 - v1
Checksum:i4D7736C21D3542D2
GO
Isoform 2 (identifier: P29350-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-3: MVR → MLSRG

Show »
Length:597
Mass (Da):67,719
Checksum:i6A291A2860159389
GO
Isoform 3 (identifier: P29350-2) [UniParc]FASTAAdd to Basket

Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     1-39: Missing.
     40-44: SLSVR → MLSRG

Show »
Length:556
Mass (Da):63,125
Checksum:iE903558D44643643
GO
Isoform 4 (identifier: P29350-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:624
Mass (Da):70,131
Checksum:iCB73D33EA910A7A0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti6 – 61H → L in AAA82880. (PubMed:7665165)Curated
Sequence conflicti86 – 861L → V in AAA36610. (PubMed:1736296)Curated
Sequence conflicti86 – 861L → V in AAD53317. (PubMed:10497187)Curated
Sequence conflicti146 – 1461V → E in AAA82880. (PubMed:7665165)Curated
Sequence conflicti146 – 1461V → E in AAA82879. (PubMed:7665165)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3939Missing in isoform 3. 1 PublicationVSP_005129Add
BLAST
Alternative sequencei1 – 33MVR → MLSRG in isoform 2. 1 PublicationVSP_007775
Alternative sequencei40 – 445SLSVR → MLSRG in isoform 3. 1 PublicationVSP_005130
Alternative sequencei559 – 59537HKEDV…SLKRK → SLESSAGTVAASPVRRGGQR GLPVPGPPVLSPDLHQLPVL APLHPAADTRRMCMRTCTLR TRGRRK in isoform 4. 1 PublicationVSP_044447Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M74903 mRNA. Translation: AAA35963.1.
X62055 mRNA. Translation: CAA43982.1.
M77273 mRNA. Translation: AAA36610.1.
U15528
, U15536, U15535, U15534, U15533, U15532, U15531, U15530, U15529 Genomic DNA. Translation: AAA82880.1.
U15528
, 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.
CCDSiCCDS41744.1. [P29350-3]
CCDS44820.1. [P29350-1]
CCDS44821.1. [P29350-4]
PIRiB42031. S20825.
RefSeqiNP_002822.2. NM_002831.5. [P29350-1]
NP_536858.1. NM_080548.4. [P29350-3]
NP_536859.1. NM_080549.3. [P29350-4]
UniGeneiHs.63489.

Genome annotation databases

EnsembliENST00000318974; ENSP00000326010; ENSG00000111679. [P29350-1]
ENST00000399448; ENSP00000382376; ENSG00000111679. [P29350-3]
ENST00000456013; ENSP00000391592; ENSG00000111679. [P29350-4]
GeneIDi5777.
KEGGihsa:5777.
UCSCiuc001qsb.2. human. [P29350-1]
uc009zfl.1. human. [P29350-4]
uc010sfr.1. human. [P29350-2]

Polymorphism databases

DMDMi131469.

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:
EMBL
GenBank
DDBJ
Links Updated
M74903 mRNA. Translation: AAA35963.1 .
X62055 mRNA. Translation: CAA43982.1 .
M77273 mRNA. Translation: AAA36610.1 .
U15528
, U15536 , U15535 , U15534 , U15533 , U15532 , U15531 , U15530 , U15529 Genomic DNA. Translation: AAA82880.1 .
U15528
, 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 .
CCDSi CCDS41744.1. [P29350-3 ]
CCDS44820.1. [P29350-1 ]
CCDS44821.1. [P29350-4 ]
PIRi B42031. S20825.
RefSeqi NP_002822.2. NM_002831.5. [P29350-1 ]
NP_536858.1. NM_080548.4. [P29350-3 ]
NP_536859.1. NM_080549.3. [P29350-4 ]
UniGenei Hs.63489.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1FPR X-ray 2.50 A 243-526 [» ]
1GWZ X-ray 2.50 A 243-541 [» ]
1X6C NMR - A 110-214 [» ]
2B3O X-ray 2.80 A 1-532 [» ]
2RMX NMR - A 110-214 [» ]
2YU7 NMR - A 110-214 [» ]
3PS5 X-ray 3.10 A 1-595 [» ]
4GRY X-ray 1.70 A 243-528 [» ]
4GRZ X-ray 1.37 A 243-528 [» ]
4GS0 X-ray 1.80 A/B 243-528 [» ]
4HJP X-ray 1.40 A 243-528 [» ]
4HJQ X-ray 1.80 A/B 243-528 [» ]
ProteinModelPortali P29350.
SMRi P29350. Positions 1-529.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111742. 59 interactions.
DIPi DIP-31002N.
IntActi P29350. 43 interactions.
MINTi MINT-134053.
STRINGi 9606.ENSP00000391592.

Chemistry

BindingDBi P29350.
ChEMBLi CHEMBL3166.

PTM databases

PhosphoSitei P29350.

Polymorphism databases

DMDMi 131469.

2D gel databases

OGPi P29350.

Proteomic databases

MaxQBi P29350.
PaxDbi P29350.
PRIDEi P29350.

Protocols and materials databases

DNASUi 5777.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000318974 ; ENSP00000326010 ; ENSG00000111679 . [P29350-1 ]
ENST00000399448 ; ENSP00000382376 ; ENSG00000111679 . [P29350-3 ]
ENST00000456013 ; ENSP00000391592 ; ENSG00000111679 . [P29350-4 ]
GeneIDi 5777.
KEGGi hsa:5777.
UCSCi uc001qsb.2. human. [P29350-1 ]
uc009zfl.1. human. [P29350-4 ]
uc010sfr.1. human. [P29350-2 ]

Organism-specific databases

CTDi 5777.
GeneCardsi GC12P007055.
HGNCi HGNC:9658. PTPN6.
HPAi CAB004572.
HPA001466.
MIMi 176883. gene.
neXtProti NX_P29350.
PharmGKBi PA34002.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118836.
HOGENOMi HOG000273907.
HOVERGENi HBG000223.
InParanoidi P29350.
KOi K05697.
OMAi QAKGEPW.
PhylomeDBi P29350.
TreeFami TF351632.

Enzyme and pathway databases

Reactomei REACT_111133. Growth hormone receptor signaling.
REACT_111225. Regulation of KIT signaling.
REACT_12519. PECAM1 interactions.
REACT_19324. PD-1 signaling.
REACT_19344. Costimulation by the CD28 family.
REACT_23837. Interleukin-3, 5 and GM-CSF signaling.
REACT_23879. Platelet sensitization by LDL.
REACT_23891. Interleukin receptor SHC signaling.
REACT_23916. Signal regulatory protein (SIRP) family interactions.
REACT_24980. Regulation of IFNG signaling.
REACT_25078. Interferon gamma signaling.
REACT_25162. Interferon alpha/beta signaling.
REACT_25216. Regulation of IFNA signaling.
SignaLinki P29350.

Miscellaneous databases

ChiTaRSi PTPN6. human.
EvolutionaryTracei P29350.
GeneWikii PTPN6.
GenomeRNAii 5777.
NextBioi 22466.
PMAP-CutDB P29350.
PROi P29350.
SOURCEi Search...

Gene expression databases

Bgeei P29350.
CleanExi HS_PTPN6.
ExpressionAtlasi P29350. baseline and differential.
Genevestigatori P29350.

Family and domain databases

Gene3Di 3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProi IPR029021. 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 ]
Pfami PF00017. SH2. 2 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000929. Tyr-Ptase_nr_6. 1 hit.
PRINTSi PR00700. PRTYPHPHTASE.
PR00401. SH2DOMAIN.
SMARTi SM00194. PTPc. 1 hit.
SM00252. SH2. 2 hits.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
SSF55550. SSF55550. 2 hits.
PROSITEi PS50001. SH2. 2 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
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Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiPTN6_HUMAN
AccessioniPrimary (citable) accession number: P29350
Secondary accession number(s): A8K306
, G3V0F8, Q969V8, Q9UK67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: October 29, 2014
This is version 177 of the entry and version 1 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 12
    Human chromosome 12: 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