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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei181 – 1811SubstrateBy similarity
Active sitei215 – 2151Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei262 – 2621SubstrateBy similarity

GO - Molecular functioni

  1. enzyme binding Source: MGI
  2. ephrin receptor binding Source: MGI
  3. poly(A) RNA binding Source: MGI
  4. protein kinase binding Source: MGI
  5. protein tyrosine phosphatase activity Source: UniProtKB
  6. receptor tyrosine kinase binding Source: MGI
  7. zinc ion binding Source: MGI

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. activation of JUN kinase activity Source: ParkinsonsUK-UCL
  3. endoplasmic reticulum unfolded protein response Source: UniProtKB
  4. insulin receptor signaling pathway Source: MGI
  5. negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  6. negative regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  7. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  8. peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: BHF-UCL
  9. platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  10. protein dephosphorylation Source: MGI
  11. regulation of endocytosis Source: UniProtKB
  12. regulation of hepatocyte growth factor receptor signaling pathway Source: MGI
  13. regulation of insulin receptor signaling pathway Source: Ensembl
  14. regulation of signal transduction Source: UniProtKB
  15. response to endoplasmic reticulum stress Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

ReactomeiREACT_317434. Growth hormone receptor signaling.
REACT_330010. Integrin alphaIIb beta3 signaling.
REACT_350917. Regulation of IFNA 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
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:97805. Ptpn1.

Subcellular locationi

Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
Note: Interacts with EPHA3 at the cell membrane.By similarity

GO - Cellular componenti

  1. cytoplasmic vesicle Source: Ensembl
  2. cytosol Source: Reactome
  3. early endosome Source: UniProtKB
  4. endoplasmic reticulum Source: MGI
  5. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  6. plasma membrane Source: Ensembl
  7. sorting endosome Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 432432Tyrosine-protein phosphatase non-receptor type 1PRO_0000094749Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei20 – 201PhosphotyrosineBy similarity
Modified residuei50 – 501Phosphoserine; by CLK1, CLK2 and PKB/AKT1 or PKB/AKT2By similarity
Modified residuei66 – 661Phosphotyrosine; by EGFRBy similarity
Modified residuei215 – 2151Cysteine persulfideBy similarity
Modified residuei215 – 2151S-nitrosocysteine; in reversibly inhibited formBy similarity
Modified residuei242 – 2421Phosphoserine; by CLK1 and CLK2By similarity
Modified residuei243 – 2431Phosphoserine; by CLK1 and CLK2By similarity

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

MaxQBiP35821.
PaxDbiP35821.
PRIDEiP35821.

PTM databases

PhosphoSiteiP35821.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP35821.
CleanExiMM_PTPN1.
ExpressionAtlasiP35821. baseline and differential.
GenevestigatoriP35821.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi202476. 1 interaction.
IntActiP35821. 2 interactions.
MINTiMINT-4996685.

Structurei

3D structure databases

ProteinModelPortaliP35821.
SMRiP35821. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 277275Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni215 – 2217Substrate bindingBy similarity

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5599.
HOGENOMiHOG000273908.
HOVERGENiHBG008321.
InParanoidiP35821.
KOiK05696.
OMAiMCMATVL.
OrthoDBiEOG7RV9G4.
PhylomeDBiP35821.
TreeFamiTF315897.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR012265. Ptpn1/Ptpn2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti48 – 481D → Y in M97590 (PubMed:1378268).Curated
Sequence conflicti173 – 1731H → P in AAA64615 (Ref. 3) Curated
Sequence conflicti266 – 2672QL → HV in AAA64615 (Ref. 3) Curated

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. Positions 1-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202476. 1 interaction.
IntActiP35821. 2 interactions.
MINTiMINT-4996685.

Chemistry

ChEMBLiCHEMBL3336.

PTM databases

PhosphoSiteiP35821.

Proteomic databases

MaxQBiP35821.
PaxDbiP35821.
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

eggNOGiCOG5599.
HOGENOMiHOG000273908.
HOVERGENiHBG008321.
InParanoidiP35821.
KOiK05696.
OMAiMCMATVL.
OrthoDBiEOG7RV9G4.
PhylomeDBiP35821.
TreeFamiTF315897.

Enzyme and pathway databases

ReactomeiREACT_317434. Growth hormone receptor signaling.
REACT_330010. Integrin alphaIIb beta3 signaling.
REACT_350917. Regulation of IFNA signaling.

Miscellaneous databases

ChiTaRSiPtpn1. mouse.
NextBioi296070.
PROiP35821.
SOURCEiSearch...

Gene expression databases

BgeeiP35821.
CleanExiMM_PTPN1.
ExpressionAtlasiP35821. baseline and differential.
GenevestigatoriP35821.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR012265. Ptpn1/Ptpn2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 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...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."
    Yi T., Cleveland J.L., Ihle J.N.
    Blood 78:2222-2228(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The cDNA cloning, nucleotide sequence and expression of an intracellular protein tyrosine phosphatase from mouse testis."
    Miyasaka H., Li S.S.L.
    Biochem. Biophys. Res. Commun. 185:818-825(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Testis.
  3. Liao K., Lane M.D.
    Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  4. Park K., Byun S.
    Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  5. "A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain."
    Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.
    Biochem. J. 305:499-504(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 102-213.
    Strain: BALB/c.
    Tissue: Brain.
  6. "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(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

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: April 1, 2015
This is version 157 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

External Data

Dasty 3

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 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.