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Protein

Tyrosine-protein phosphatase non-receptor type 6

Gene

PTPN6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Binding sitei419SubstrateBy similarity1
Active sitei453Phosphocysteine intermediate1
Binding sitei500SubstrateBy similarity1

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB
  • protein tyrosine phosphatase activity Source: Reactome
  • transmembrane receptor protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS03446-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1433559. Regulation of KIT signaling.
R-HSA-210990. PECAM1 interactions.
R-HSA-388841. Costimulation by the CD28 family.
R-HSA-389948. PD-1 signaling.
R-HSA-391160. Signal regulatory protein (SIRP) family interactions.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-512988. Interleukin-3, 5 and GM-CSF signaling.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-877300. Interferon gamma signaling.
R-HSA-877312. Regulation of IFNG signaling.
R-HSA-909733. Interferon alpha/beta signaling.
R-HSA-912526. Interleukin receptor SHC signaling.
R-HSA-912694. Regulation of IFNA signaling.
R-HSA-982772. Growth hormone receptor signaling.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP29350.
SIGNORiP29350.

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
Proteomesi
  • UP000005640 Componenti: 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

  • alpha-beta T cell receptor complex Source: Ensembl
  • cell-cell junction Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • membrane Source: ProtInc
  • nucleolus Source: HPA
  • nucleus Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

DisGeNETi5777.
OpenTargetsiENSG00000111679.
PharmGKBiPA34002.

Chemistry databases

ChEMBLiCHEMBL3166.

Polymorphism and mutation databases

BioMutaiPTPN6.
DMDMi131469.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000947581 – 595Tyrosine-protein phosphatase non-receptor type 6Add BLAST595

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei10PhosphoserineBy similarity1
Modified residuei57PhosphoserineBy similarity1
Modified residuei64PhosphotyrosineCombined sources1
Modified residuei377PhosphotyrosineBy similarity1
Modified residuei536PhosphotyrosineBy similarity1
Modified residuei564Phosphotyrosine; by LYN1 Publication1

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 similarity2 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP29350.
MaxQBiP29350.
PaxDbiP29350.
PeptideAtlasiP29350.
PRIDEiP29350.

2D gel databases

OGPiP29350.

PTM databases

DEPODiP29350.
iPTMnetiP29350.
PhosphoSitePlusiP29350.

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

BgeeiENSG00000111679.
CleanExiHS_PTPN6.
ExpressionAtlasiP29350. baseline and differential.
GenevisibleiP29350. HS.

Organism-specific databases

HPAiCAB004572.
CAB072845.
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. Interacts with CEACAM1 (via cytoplasmic domain); this interaction depends on the monomer/dimer equilibrium and is phosphorylation-dependent (By similarity).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
FHL3Q136433EBI-78260,EBI-741101
GRB2P629933EBI-78260,EBI-401755
KIR2DL1P436264EBI-78260,EBI-8684277
KIR2DL3P4362813EBI-78260,EBI-8632435
LAIR1Q6GTX85EBI-78260,EBI-965864
LCKP062395EBI-78260,EBI-1348
PECAM1P162844EBI-78260,EBI-716404
PILRAQ9UKJ15EBI-78260,EBI-965833
PTK2Q053973EBI-7399369,EBI-702142
ROS1P089222EBI-78260,EBI-7371065
THEMISQ8N1K54EBI-78260,EBI-2873538
tirB7UM994EBI-78260,EBI-2504426From a different organism.
tirQ7DB772EBI-78260,EBI-6480811From a different organism.

GO - Molecular functioni

  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111742. 68 interactors.
DIPiDIP-31002N.
IntActiP29350. 50 interactors.
MINTiMINT-134053.
STRINGi9606.ENSP00000391592.

Chemistry databases

BindingDBiP29350.

Structurei

Secondary structure

1595
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi11 – 21Combined sources11
Beta strandi26 – 31Combined sources6
Beta strandi33 – 45Combined sources13
Beta strandi48 – 55Combined sources8
Beta strandi57 – 59Combined sources3
Beta strandi61 – 63Combined sources3
Beta strandi68 – 70Combined sources3
Helixi72 – 80Combined sources9
Beta strandi89 – 91Combined sources3
Helixi105 – 107Combined sources3
Beta strandi111 – 114Combined sources4
Helixi117 – 127Combined sources11
Beta strandi132 – 137Combined sources6
Beta strandi139 – 141Combined sources3
Beta strandi145 – 154Combined sources10
Beta strandi155 – 157Combined sources3
Beta strandi162 – 170Combined sources9
Helixi172 – 174Combined sources3
Beta strandi175 – 181Combined sources7
Beta strandi184 – 186Combined sources3
Helixi187 – 197Combined sources11
Beta strandi199 – 201Combined sources3
Beta strandi202 – 204Combined sources3
Beta strandi205 – 207Combined sources3
Helixi221 – 223Combined sources3
Beta strandi236 – 238Combined sources3
Helixi244 – 256Combined sources13
Turni257 – 259Combined sources3
Helixi263 – 266Combined sources4
Helixi268 – 273Combined sources6
Beta strandi275 – 278Combined sources4
Turni283 – 285Combined sources3
Beta strandi286 – 288Combined sources3
Beta strandi290 – 292Combined sources3
Beta strandi294 – 296Combined sources3
Turni297 – 300Combined sources4
Beta strandi301 – 307Combined sources7
Beta strandi309 – 312Combined sources4
Helixi314 – 316Combined sources3
Beta strandi321 – 324Combined sources4
Helixi329 – 331Combined sources3
Helixi332 – 341Combined sources10
Beta strandi346 – 349Combined sources4
Beta strandi353 – 355Combined sources3
Beta strandi356 – 358Combined sources3
Beta strandi371 – 374Combined sources4
Beta strandi377 – 386Combined sources10
Beta strandi388 – 399Combined sources12
Helixi400 – 402Combined sources3
Beta strandi403 – 405Combined sources3
Beta strandi407 – 414Combined sources8
Beta strandi419 – 421Combined sources3
Beta strandi424 – 426Combined sources3
Helixi427 – 442Combined sources16
Beta strandi443 – 445Combined sources3
Beta strandi449 – 452Combined sources4
Beta strandi454 – 457Combined sources4
Helixi458 – 476Combined sources19
Helixi484 – 492Combined sources9
Helixi502 – 523Combined sources22

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29350.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini4 – 100SH2 1PROSITE-ProRule annotationAdd BLAST97
Domaini110 – 213SH2 2PROSITE-ProRule annotationAdd BLAST104
Domaini244 – 515Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST272

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni453 – 459Substrate bindingBy similarity7

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

eggNOGiKOG0790. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273907.
HOVERGENiHBG000223.
InParanoidiP29350.
KOiK05697.
OMAiQAKGEPW.
OrthoDBiEOG091G0VZ3.
PhylomeDBiP29350.
TreeFamiTF351632.

Family and domain databases

Gene3Di3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR000980. SH2.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
IPR000387. TYR_PHOSPHATASE_dom.
[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.
SM00404. PTPc_motif. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti6H → L in AAA82880 (PubMed:7665165).Curated1
Sequence conflicti86L → V in AAA36610 (PubMed:1736296).Curated1
Sequence conflicti86L → V in AAD53317 (PubMed:10497187).Curated1
Sequence conflicti146V → E in AAA82880 (PubMed:7665165).Curated1
Sequence conflicti146V → E in AAA82879 (PubMed:7665165).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0051291 – 39Missing in isoform 3. 1 PublicationAdd BLAST39
Alternative sequenceiVSP_0077751 – 3MVR → MLSRG in isoform 2. 1 Publication3
Alternative sequenceiVSP_00513040 – 44SLSVR → MLSRG in isoform 3. 1 Publication5
Alternative sequenceiVSP_044447559 – 595HKEDV…SLKRK → SLESSAGTVAASPVRRGGQR GLPVPGPPVLSPDLHQLPVL APLHPAADTRRMCMRTCTLR TRGRRK in isoform 4. 1 PublicationAdd BLAST37

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
XP_011519290.1. XM_011520988.1. [P29350-3]
UniGeneiHs.63489.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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]
XP_011519290.1. XM_011520988.1. [P29350-3]
UniGeneiHs.63489.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111742. 68 interactors.
DIPiDIP-31002N.
IntActiP29350. 50 interactors.
MINTiMINT-134053.
STRINGi9606.ENSP00000391592.

Chemistry databases

BindingDBiP29350.
ChEMBLiCHEMBL3166.

PTM databases

DEPODiP29350.
iPTMnetiP29350.
PhosphoSitePlusiP29350.

Polymorphism and mutation databases

BioMutaiPTPN6.
DMDMi131469.

2D gel databases

OGPiP29350.

Proteomic databases

EPDiP29350.
MaxQBiP29350.
PaxDbiP29350.
PeptideAtlasiP29350.
PRIDEiP29350.

Protocols and materials databases

DNASUi5777.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi5777.
DisGeNETi5777.
GeneCardsiPTPN6.
HGNCiHGNC:9658. PTPN6.
HPAiCAB004572.
CAB072845.
HPA001466.
MIMi176883. gene.
neXtProtiNX_P29350.
OpenTargetsiENSG00000111679.
PharmGKBiPA34002.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0790. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273907.
HOVERGENiHBG000223.
InParanoidiP29350.
KOiK05697.
OMAiQAKGEPW.
OrthoDBiEOG091G0VZ3.
PhylomeDBiP29350.
TreeFamiTF351632.

Enzyme and pathway databases

BioCyciZFISH:HS03446-MONOMER.
BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-114604. GPVI-mediated activation cascade.
R-HSA-1433559. Regulation of KIT signaling.
R-HSA-210990. PECAM1 interactions.
R-HSA-388841. Costimulation by the CD28 family.
R-HSA-389948. PD-1 signaling.
R-HSA-391160. Signal regulatory protein (SIRP) family interactions.
R-HSA-432142. Platelet sensitization by LDL.
R-HSA-512988. Interleukin-3, 5 and GM-CSF signaling.
R-HSA-5690714. CD22 mediated BCR regulation.
R-HSA-6798695. Neutrophil degranulation.
R-HSA-877300. Interferon gamma signaling.
R-HSA-877312. Regulation of IFNG signaling.
R-HSA-909733. Interferon alpha/beta signaling.
R-HSA-912526. Interleukin receptor SHC signaling.
R-HSA-912694. Regulation of IFNA signaling.
R-HSA-982772. Growth hormone receptor signaling.
R-HSA-983695. Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
SignaLinkiP29350.
SIGNORiP29350.

Miscellaneous databases

ChiTaRSiPTPN6. human.
EvolutionaryTraceiP29350.
GeneWikiiPTPN6.
GenomeRNAii5777.
PMAP-CutDBP29350.
PROiP29350.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000111679.
CleanExiHS_PTPN6.
ExpressionAtlasiP29350. baseline and differential.
GenevisibleiP29350. HS.

Family and domain databases

Gene3Di3.30.505.10. 2 hits.
3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR000980. SH2.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR012152. Tyr_Pase_non-rcpt_typ-6/11.
IPR000387. TYR_PHOSPHATASE_dom.
[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.
SM00404. PTPc_motif. 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]
ProtoNetiSearch...

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: November 30, 2016
This is version 201 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.