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Protein

Tyrosine-protein phosphatase non-receptor type 1

Gene

Ptpn1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tyrosine-protein phosphatase which acts as a regulator of endoplasmic reticulum unfolded protein response. Mediates dephosphorylation of EIF2AK3/PERK; inactivating the protein kinase activity of EIF2AK3/PERK. May play an important role in CKII- and p60c-src-induced signal transduction cascades. May regulate the EFNA5-EPHA3 signaling pathway which modulates cell reorganization and cell-cell repulsion. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET (By similarity).By similarity

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei181SubstrateBy similarity1
Active sitei215Phosphocysteine intermediatePROSITE-ProRule annotation1
Binding sitei262SubstrateBy similarity1

GO - Molecular functioni

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • activation of JUN kinase activity Source: ParkinsonsUK-UCL
  • endoplasmic reticulum unfolded protein response Source: UniProtKB
  • insulin receptor signaling pathway Source: MGI
  • IRE1-mediated unfolded protein response Source: ParkinsonsUK-UCL
  • JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  • negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: ParkinsonsUK-UCL
  • negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • negative regulation of MAP kinase activity Source: MGI
  • negative regulation of PERK-mediated unfolded protein response Source: ParkinsonsUK-UCL
  • negative regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • peptidyl-tyrosine dephosphorylation Source: UniProtKB
  • peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: BHF-UCL
  • platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  • positive regulation of protein tyrosine kinase activity Source: MGI
  • positive regulation of receptor catabolic process Source: MGI
  • protein dephosphorylation Source: MGI
  • regulation of endocytosis Source: UniProtKB
  • regulation of hepatocyte growth factor receptor signaling pathway Source: MGI
  • regulation of insulin receptor signaling pathway Source: Ensembl
  • regulation of intracellular protein transport Source: MGI
  • regulation of signal transduction Source: UniProtKB
  • response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiR-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-6807004. Negative regulation of MET activity.
R-MMU-8849472. PTK6 Down-Regulation.
R-MMU-912694. Regulation of IFNA signaling.
R-MMU-982772. Growth hormone receptor signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase non-receptor type 1 (EC:3.1.3.48)
Alternative name(s):
Protein-tyrosine phosphatase 1B
Short name:
PTP-1B
Protein-tyrosine phosphatase HA2
Short name:
PTP-HA2
Gene namesi
Name:Ptpn1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97805. Ptpn1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: MGI
  • cytoplasm Source: ParkinsonsUK-UCL
  • cytoplasmic side of endoplasmic reticulum membrane Source: MGI
  • cytoplasmic vesicle Source: Ensembl
  • cytosol Source: Reactome
  • early endosome Source: UniProtKB
  • endoplasmic reticulum Source: ParkinsonsUK-UCL
  • plasma membrane Source: Ensembl
  • sorting endosome Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL3336.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000947491 – 432Tyrosine-protein phosphatase non-receptor type 1Add BLAST432

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei20PhosphotyrosineBy similarity1
Modified residuei50Phosphoserine; by CLK1, CLK2 and PKB/AKT1 or PKB/AKT2By similarity1
Modified residuei66Phosphotyrosine; by EGFRBy similarity1
Modified residuei215Cysteine persulfideBy similarity1
Modified residuei215S-nitrosocysteine; in reversibly inhibited formBy similarity1
Modified residuei242Phosphoserine; by CLK1 and CLK2By similarity1
Modified residuei243Phosphoserine; by CLK1 and CLK2By similarity1
Modified residuei335PhosphoserineCombined sources1
Modified residuei362PhosphoserineBy similarity1
Modified residuei364PhosphoserineBy similarity1
Modified residuei367PhosphothreonineBy similarity1

Post-translational modificationi

Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50 (By similarity).By similarity
S-nitrosylation of Cys-215 inactivates the enzyme activity.By similarity
Sulfhydration at Cys-215 following endoplasmic reticulum stress inactivates the enzyme activity, promoting EIF2AK3/PERK activity.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

EPDiP35821.
PaxDbiP35821.
PeptideAtlasiP35821.
PRIDEiP35821.

PTM databases

iPTMnetiP35821.
PhosphoSitePlusiP35821.
SwissPalmiP35821.

Expressioni

Tissue specificityi

Most abundant in testis. Also found in kidney, spleen, muscle, liver, heart and brain.

Gene expression databases

BgeeiENSMUSG00000027540.
CleanExiMM_PTPN1.
ExpressionAtlasiP35821. baseline and differential.
GenevisibleiP35821. MM.

Interactioni

Subunit structurei

Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts with MET.By similarity

GO - Molecular functioni

Protein-protein interaction databases

BioGridi202476. 1 interactor.
IntActiP35821. 2 interactors.
MINTiMINT-4996685.
STRINGi10090.ENSMUSP00000029053.

Structurei

3D structure databases

ProteinModelPortaliP35821.
SMRiP35821.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 277Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST275

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni215 – 221Substrate bindingBy similarity7

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0789. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273908.
HOVERGENiHBG008321.
InParanoidiP35821.
KOiK05696.
OMAiDGPIKEE.
OrthoDBiEOG091G082B.
PhylomeDBiP35821.
TreeFamiTF315897.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR012265. Ptpn1/Ptpn2.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSiPR00700. 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]

Sequencei

Sequence statusi: Complete.

P35821-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEMEKEFEEI DKAGNWAAIY QDIRHEASDF PCKVAKLPKN KNRNRYRDVS
60 70 80 90 100
PFDHSRIKLH QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW
110 120 130 140 150
EQKSRGVVML NRIMEKGSLK CAQYWPQQEE KEMVFDDTGL KLTLISEDVK
160 170 180 190 200
SYYTVRQLEL ENLTTKETRE ILHFHYTTWP DFGVPESPAS FLNFLFKVRE
210 220 230 240 250
SGSLSLEHGP IVVHCSAGIG RSGTFCLADT CLLLMDKRKD PSSVDIKKVL
260 270 280 290 300
LEMRRFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSREDLD
310 320 330 340 350
LPPEHVPPPP RPPKRTLEPH NGKCKELFSS HQWVSEETCG DEDSLAREEG
360 370 380 390 400
RAQSSAMHSV SSMSPDTEVR RRMVGGGLQS AQASVPTEEE LSSTEEEHKA
410 420 430
HWPSHWKPFL VNVCMATLLA TGAYLCYRVC FH
Length:432
Mass (Da):49,593
Last modified:November 1, 1997 - v2
Checksum:i4843D2DD4C288C48
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti48D → Y in M97590 (PubMed:1378268).Curated1
Sequence conflicti173H → P in AAA64615 (Ref. 3) Curated1
Sequence conflicti266 – 267QL → HV in AAA64615 (Ref. 3) Curated2

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97590 mRNA. No translation available.
L40595 mRNA. Translation: AAA64615.1.
U24700 mRNA. Translation: AAA98605.1.
Z23057 mRNA. Translation: CAA80592.1.
BC005729 mRNA. Translation: AAH05729.1.
BC010191 mRNA. Translation: AAH10191.1.
CCDSiCCDS17107.1.
PIRiJN0317.
RefSeqiNP_035331.3. NM_011201.3.
UniGeneiMm.277916.

Genome annotation databases

EnsembliENSMUST00000029053; ENSMUSP00000029053; ENSMUSG00000027540.
GeneIDi19246.
KEGGimmu:19246.
UCSCiuc008oaj.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97590 mRNA. No translation available.
L40595 mRNA. Translation: AAA64615.1.
U24700 mRNA. Translation: AAA98605.1.
Z23057 mRNA. Translation: CAA80592.1.
BC005729 mRNA. Translation: AAH05729.1.
BC010191 mRNA. Translation: AAH10191.1.
CCDSiCCDS17107.1.
PIRiJN0317.
RefSeqiNP_035331.3. NM_011201.3.
UniGeneiMm.277916.

3D structure databases

ProteinModelPortaliP35821.
SMRiP35821.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202476. 1 interactor.
IntActiP35821. 2 interactors.
MINTiMINT-4996685.
STRINGi10090.ENSMUSP00000029053.

Chemistry databases

ChEMBLiCHEMBL3336.

PTM databases

iPTMnetiP35821.
PhosphoSitePlusiP35821.
SwissPalmiP35821.

Proteomic databases

EPDiP35821.
PaxDbiP35821.
PeptideAtlasiP35821.
PRIDEiP35821.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029053; ENSMUSP00000029053; ENSMUSG00000027540.
GeneIDi19246.
KEGGimmu:19246.
UCSCiuc008oaj.1. mouse.

Organism-specific databases

CTDi5770.
MGIiMGI:97805. Ptpn1.

Phylogenomic databases

eggNOGiKOG0789. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273908.
HOVERGENiHBG008321.
InParanoidiP35821.
KOiK05696.
OMAiDGPIKEE.
OrthoDBiEOG091G082B.
PhylomeDBiP35821.
TreeFamiTF315897.

Enzyme and pathway databases

ReactomeiR-MMU-354192. Integrin alphaIIb beta3 signaling.
R-MMU-6807004. Negative regulation of MET activity.
R-MMU-8849472. PTK6 Down-Regulation.
R-MMU-912694. Regulation of IFNA signaling.
R-MMU-982772. Growth hormone receptor signaling.

Miscellaneous databases

ChiTaRSiPtpn1. mouse.
PROiP35821.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027540.
CleanExiMM_PTPN1.
ExpressionAtlasiP35821. baseline and differential.
GenevisibleiP35821. MM.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR012265. Ptpn1/Ptpn2.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSiPR00700. 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 nameiPTN1_MOUSE
AccessioniPrimary (citable) accession number: P35821
Secondary accession number(s): Q60840
, Q62131, Q64498, Q99JS1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: November 30, 2016
This is version 175 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.