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Protein

Tyrosine-protein phosphatase non-receptor type 7

Gene

PTPN7

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

Functioni

Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction.6 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited in cells after FCER1A triggering.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei257Substrate1
Active sitei291Phosphocysteine intermediatePROSITE-ProRule annotation1 Publication1
Binding sitei335Substrate1

GO - Molecular functioni

  • protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  • protein dephosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BioCyciZFISH:HS07117-MONOMER.
BRENDAi3.1.3.48. 2681.
SIGNORiP35236.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase non-receptor type 7 (EC:3.1.3.48)
Alternative name(s):
Hematopoietic protein-tyrosine phosphatase
Short name:
HEPTP
Protein-tyrosine phosphatase LC-PTP
Gene namesi
Name:PTPN7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9659. PTPN7.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytoplasmic side of plasma membrane Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi44S → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation. 1 Publication1
Mutagenesisi44S → D: Reduces binding of MAP kinase. 1 Publication1
Mutagenesisi66T → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-93. 1 Publication1
Mutagenesisi93S → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-66. 1 Publication1
Mutagenesisi125Y → A: Strongly reduced catalytic activity. 1 Publication1
Mutagenesisi257D → A: Loss of catalytic activity. 1 Publication1
Mutagenesisi291C → S: Loss of catalytic activity. 1 Publication1
Mutagenesisi335Q → A: Reduced catalytic activity. 1 Publication1

Organism-specific databases

DisGeNETi5778.
OpenTargetsiENSG00000143851.
PharmGKBiPA34003.

Chemistry databases

ChEMBLiCHEMBL2219.

Polymorphism and mutation databases

DMDMi20141721.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000947611 – 360Tyrosine-protein phosphatase non-receptor type 7Add BLAST360

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei44PhosphoserineCombined sources2 Publications1
Modified residuei66PhosphothreonineCombined sources1 Publication1
Modified residuei93Phosphoserine1 Publication1
Modified residuei110PhosphoserineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Modified residuei291Cysteine sulfenic acid (-SOH)By similarity1

Post-translational modificationi

Phosphorylated on serine residues in resting T-cells. Phosphorylation increases upon exposure to stimuli that increase intracellular cAMP levels. Phosphorylation leads to dissociation of bound MAP kinases.3 Publications
Oxidized at active site cysteine. Treatment with pervanadate (vanadate and H2O2) or with antigen enhanced oxidation of active site cysteine (By similarity).By similarity

Keywords - PTMi

Oxidation, Phosphoprotein

Proteomic databases

EPDiP35236.
MaxQBiP35236.
PaxDbiP35236.
PeptideAtlasiP35236.
PRIDEiP35236.

PTM databases

DEPODiP35236.
iPTMnetiP35236.
PhosphoSitePlusiP35236.

Expressioni

Tissue specificityi

Expressed exclusively in thymus and spleen.2 Publications

Gene expression databases

BgeeiENSG00000143851.
CleanExiHS_PTPN7.
ExpressionAtlasiP35236. baseline and differential.
GenevisibleiP35236. HS.

Organism-specific databases

HPAiCAB009530.
HPA019118.

Interactioni

Subunit structurei

Monomer. Interacts with MAPK1, MAPK3 and several other MAP kinases.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC57Q2TAC23EBI-2265723,EBI-2808286
FLJ13057Q53SE73EBI-2265723,EBI-10172181
MAPK1P284826EBI-2265723,EBI-959949
Mapk14P478112EBI-2265723,EBI-298727From a different organism.

Protein-protein interaction databases

BioGridi111743. 6 interactors.
DIPiDIP-29118N.
IntActiP35236. 7 interactors.
MINTiMINT-8206881.
STRINGi9606.ENSP00000309116.

Chemistry databases

BindingDBiP35236.

Structurei

Secondary structure

1360
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi38 – 41Combined sources4
Helixi67 – 77Combined sources11
Beta strandi81 – 83Combined sources3
Helixi84 – 89Combined sources6
Helixi94 – 103Combined sources10
Helixi111 – 113Combined sources3
Helixi119 – 122Combined sources4
Helixi132 – 134Combined sources3
Beta strandi135 – 137Combined sources3
Beta strandi149 – 155Combined sources7
Helixi158 – 160Combined sources3
Beta strandi164 – 169Combined sources6
Helixi173 – 175Combined sources3
Helixi176 – 185Combined sources10
Beta strandi190 – 194Combined sources5
Beta strandi199 – 201Combined sources3
Beta strandi210 – 215Combined sources6
Beta strandi218 – 227Combined sources10
Beta strandi229 – 240Combined sources12
Beta strandi243 – 252Combined sources10
Helixi264 – 275Combined sources12
Beta strandi281 – 283Combined sources3
Beta strandi287 – 295Combined sources9
Helixi296 – 314Combined sources19
Beta strandi315 – 317Combined sources3
Helixi319 – 329Combined sources11
Helixi337 – 353Combined sources17

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZC0X-ray1.85A65-360[»]
2A3KX-ray2.55A65-358[»]
2GP0X-ray2.05A65-360[»]
2GPHX-ray1.90B37-52[»]
2HVLX-ray2.40A65-360[»]
2QDCX-ray2.00A65-360[»]
2QDMX-ray2.05A65-360[»]
2QDPX-ray2.72A65-360[»]
3D42X-ray2.46A65-360[»]
3D44X-ray1.90A65-360[»]
3O4SX-ray1.90A65-360[»]
3O4TX-ray2.60A65-360[»]
3O4UX-ray2.25A65-360[»]
ProteinModelPortaliP35236.
SMRiP35236.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35236.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini97 – 350Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST254

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni38 – 51Interaction with MAP kinasesAdd BLAST14
Regioni291 – 297Substrate binding7

Sequence similaritiesi

Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0789. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000294188.
HOVERGENiHBG001594.
InParanoidiP35236.
KOiK18019.
OrthoDBiEOG091G0HLB.
PhylomeDBiP35236.
TreeFamiTF331016.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR008356. Tyr_Pase_KIM-con.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR01778. KIMPTPASE.
PR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 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 (3)i

Sequence statusi: Complete.

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

Isoform 1 (identifier: P35236-1) [UniParc]FASTAAdd to basket

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
MVQAHGGRSR AQPLTLSLGA AMTQPPPEKT PAKKHVRLQE RRGSNVALML
60 70 80 90 100
DVRSLGAVEP ICSVNTPREV TLHFLRTAGH PLTRWALQRQ PPSPKQLEEE
110 120 130 140 150
FLKIPSNFVS PEDLDIPGHA SKDRYKTILP NPQSRVCLGR AQSQEDGDYI
160 170 180 190 200
NANYIRGYDG KEKVYIATQG PMPNTVSDFW EMVWQEEVSL IVMLTQLREG
210 220 230 240 250
KEKCVHYWPT EEETYGPFQI RIQDMKECPE YTVRQLTIQY QEERRSVKHI
260 270 280 290 300
LFSAWPDHQT PESAGPLLRL VAEVEESPET AAHPGPIVVH CSAGIGRTGC
310 320 330 340 350
FIATRIGCQQ LKARGEVDIL GIVCQLRLDR GGMIQTAEQY QFLHHTLALY
360
AGQLPEEPSP
Length:360
Mass (Da):40,529
Last modified:January 23, 2002 - v3
Checksum:i388A154CC55AC0EE
GO
Isoform 2 (identifier: P35236-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGASFWPIRQAREQQRRALSFRQTSWLSEPPLGPAPHLSM

Show »
Length:399
Mass (Da):45,002
Checksum:i16690FDF358E20C8
GO
Isoform 3 (identifier: P35236-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVGKAWPLTH...PLGPAPHLSM

Show »
Length:465
Mass (Da):52,284
Checksum:iAB2E025ECD392906
GO

Sequence cautioni

The sequence AAA59531 differs from that shown. Reason: Frameshift at position 5.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti235 – 236QL → HV in AAA59531 (PubMed:1530918).Curated2
Sequence conflicti337A → D in BAA01946 (PubMed:1510684).Curated1
Isoform 3 (identifier: P35236-3)
Sequence conflicti37Q → R in BAG54453 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0269251M → MGASFWPIRQAREQQRRALS FRQTSWLSEPPLGPAPHLSM in isoform 2. 1 Publication1
Alternative sequenceiVSP_0472751M → MVGKAWPLTHSQGTGPWAPE GHRREAADPWWQRQQAQEGR MQLGCAWVAARRGGGRKLAS WSLLSPQRQTDRQTDSWQEA AWGPQLLQQTSWLSEPPLGP APHLSM in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11327 mRNA. Translation: BAA01946.1.
M64322 mRNA. Translation: AAA59531.1. Frameshift.
BT009848 mRNA. Translation: AAP88850.1.
AK127214 mRNA. Translation: BAG54453.1.
AL592300 Genomic DNA. Translation: CAI13108.1.
BC001746 mRNA. Translation: AAH01746.2.
CCDSiCCDS1422.1. [P35236-2]
CCDS1423.2. [P35236-3]
PIRiJH0692.
RefSeqiNP_002823.3. NM_002832.3. [P35236-3]
NP_542155.1. NM_080588.2. [P35236-2]
UniGeneiHs.402773.

Genome annotation databases

EnsembliENST00000309017; ENSP00000309116; ENSG00000143851. [P35236-3]
ENST00000367279; ENSP00000356248; ENSG00000143851. [P35236-2]
ENST00000495688; ENSP00000420506; ENSG00000143851. [P35236-1]
GeneIDi5778.
KEGGihsa:5778.
UCSCiuc001gxl.2. human. [P35236-1]

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
D11327 mRNA. Translation: BAA01946.1.
M64322 mRNA. Translation: AAA59531.1. Frameshift.
BT009848 mRNA. Translation: AAP88850.1.
AK127214 mRNA. Translation: BAG54453.1.
AL592300 Genomic DNA. Translation: CAI13108.1.
BC001746 mRNA. Translation: AAH01746.2.
CCDSiCCDS1422.1. [P35236-2]
CCDS1423.2. [P35236-3]
PIRiJH0692.
RefSeqiNP_002823.3. NM_002832.3. [P35236-3]
NP_542155.1. NM_080588.2. [P35236-2]
UniGeneiHs.402773.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1ZC0X-ray1.85A65-360[»]
2A3KX-ray2.55A65-358[»]
2GP0X-ray2.05A65-360[»]
2GPHX-ray1.90B37-52[»]
2HVLX-ray2.40A65-360[»]
2QDCX-ray2.00A65-360[»]
2QDMX-ray2.05A65-360[»]
2QDPX-ray2.72A65-360[»]
3D42X-ray2.46A65-360[»]
3D44X-ray1.90A65-360[»]
3O4SX-ray1.90A65-360[»]
3O4TX-ray2.60A65-360[»]
3O4UX-ray2.25A65-360[»]
ProteinModelPortaliP35236.
SMRiP35236.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111743. 6 interactors.
DIPiDIP-29118N.
IntActiP35236. 7 interactors.
MINTiMINT-8206881.
STRINGi9606.ENSP00000309116.

Chemistry databases

BindingDBiP35236.
ChEMBLiCHEMBL2219.

PTM databases

DEPODiP35236.
iPTMnetiP35236.
PhosphoSitePlusiP35236.

Polymorphism and mutation databases

DMDMi20141721.

Proteomic databases

EPDiP35236.
MaxQBiP35236.
PaxDbiP35236.
PeptideAtlasiP35236.
PRIDEiP35236.

Protocols and materials databases

DNASUi5778.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000309017; ENSP00000309116; ENSG00000143851. [P35236-3]
ENST00000367279; ENSP00000356248; ENSG00000143851. [P35236-2]
ENST00000495688; ENSP00000420506; ENSG00000143851. [P35236-1]
GeneIDi5778.
KEGGihsa:5778.
UCSCiuc001gxl.2. human. [P35236-1]

Organism-specific databases

CTDi5778.
DisGeNETi5778.
GeneCardsiPTPN7.
H-InvDBHIX0001472.
HGNCiHGNC:9659. PTPN7.
HPAiCAB009530.
HPA019118.
MIMi176889. gene.
neXtProtiNX_P35236.
OpenTargetsiENSG00000143851.
PharmGKBiPA34003.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0789. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000294188.
HOVERGENiHBG001594.
InParanoidiP35236.
KOiK18019.
OrthoDBiEOG091G0HLB.
PhylomeDBiP35236.
TreeFamiTF331016.

Enzyme and pathway databases

BioCyciZFISH:HS07117-MONOMER.
BRENDAi3.1.3.48. 2681.
SIGNORiP35236.

Miscellaneous databases

ChiTaRSiPTPN7. human.
EvolutionaryTraceiP35236.
GeneWikiiPTPN7.
GenomeRNAii5778.
PROiP35236.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143851.
CleanExiHS_PTPN7.
ExpressionAtlasiP35236. baseline and differential.
GenevisibleiP35236. HS.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR008356. Tyr_Pase_KIM-con.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR01778. KIMPTPASE.
PR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 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]
ProtoNetiSearch...

Entry informationi

Entry nameiPTN7_HUMAN
AccessioniPrimary (citable) accession number: P35236
Secondary accession number(s): B3KXE1
, Q53XK4, Q5SXQ0, Q5SXQ1, Q9BV05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2002
Last modified: November 30, 2016
This is version 165 of the entry and version 3 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 1
    Human chromosome 1: 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.