Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P35821 (PTN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 146. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Ptpn1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Subunit structure

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

Subcellular location

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

Tissue specificity

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

Post-translational modification

Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50 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.

Sequence similarities

Belongs to the protein-tyrosine phosphatase family. Non-receptor class 1 subfamily.

Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
   Cellular componentEndoplasmic reticulum
Membrane
   Molecular functionHydrolase
Protein phosphatase
   PTMAcetylation
Phosphoprotein
S-nitrosylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin cytoskeleton reorganization

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Inferred from sequence or structural similarity. Source: UniProtKB

insulin receptor signaling pathway

Inferred from mutant phenotype PubMed 15632081. Source: MGI

peptidyl-tyrosine dephosphorylation

Inferred from mutant phenotype PubMed 14966296. Source: UniProtKB

platelet-derived growth factor receptor-beta signaling pathway

Inferred from mutant phenotype PubMed 14966296. Source: UniProtKB

protein dephosphorylation

Inferred from mutant phenotype PubMed 15632081. Source: MGI

regulation of endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of hepatocyte growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of insulin receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasmic vesicle

Inferred from electronic annotation. Source: Ensembl

cytosol

Traceable author statement. Source: Reactome

early endosome

Inferred from sequence or structural similarity. Source: UniProtKB

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionprotein tyrosine phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Tyrosine-protein phosphatase non-receptor type 1
PRO_0000094749

Regions

Domain3 – 277275Tyrosine-protein phosphatase
Region215 – 2217Substrate binding By similarity

Sites

Active site2151Phosphocysteine intermediate By similarity
Binding site1811Substrate By similarity
Binding site2621Substrate By similarity

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue201Phosphotyrosine By similarity
Modified residue501Phosphoserine; by CLK1, CLK2 and PKB/AKT1 or PKB/AKT2 By similarity
Modified residue661Phosphotyrosine; by EGFR By similarity
Modified residue2151Cysteine persulfide By similarity
Modified residue2151S-nitrosocysteine; in reversibly inhibited form By similarity
Modified residue2421Phosphoserine; by CLK1 and CLK2 By similarity
Modified residue2431Phosphoserine; by CLK1 and CLK2 By similarity

Experimental info

Sequence conflict481D → Y in M97590. Ref.2
Sequence conflict1731H → P in AAA64615. Ref.3
Sequence conflict266 – 2672QL → HV in AAA64615. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P35821 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 4843D2DD4C288C48

FASTA43249,593
        10         20         30         40         50         60 
MEMEKEFEEI DKAGNWAAIY QDIRHEASDF PCKVAKLPKN KNRNRYRDVS PFDHSRIKLH 

        70         80         90        100        110        120 
QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW EQKSRGVVML NRIMEKGSLK 

       130        140        150        160        170        180 
CAQYWPQQEE KEMVFDDTGL KLTLISEDVK SYYTVRQLEL ENLTTKETRE ILHFHYTTWP 

       190        200        210        220        230        240 
DFGVPESPAS FLNFLFKVRE SGSLSLEHGP IVVHCSAGIG RSGTFCLADT CLLLMDKRKD 

       250        260        270        280        290        300 
PSSVDIKKVL LEMRRFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSREDLD 

       310        320        330        340        350        360 
LPPEHVPPPP RPPKRTLEPH NGKCKELFSS HQWVSEETCG DEDSLAREEG RAQSSAMHSV 

       370        380        390        400        410        420 
SSMSPDTEVR RRMVGGGLQS AQASVPTEEE LSSTEEEHKA HWPSHWKPFL VNVCMATLLA 

       430 
TGAYLCYRVC FH 

« Hide

References

« Hide 'large scale' references
[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(1991) [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(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Testis.
[3]Liao K., Lane M.D.
Submitted (APR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]Park K., Byun S.
Submitted (MAY-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(1995) [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(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[7]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJN0317.
RefSeqNP_035331.3. NM_011201.3.
UniGeneMm.277916.

3D structure databases

ProteinModelPortalP35821.
SMRP35821. Positions 1-282.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202476. 1 interaction.
IntActP35821. 2 interactions.
MINTMINT-4996685.

Chemistry

ChEMBLCHEMBL3336.

PTM databases

PhosphoSiteP35821.

Proteomic databases

PaxDbP35821.
PRIDEP35821.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029053; ENSMUSP00000029053; ENSMUSG00000027540.
GeneID19246.
KEGGmmu:19246.
UCSCuc008oaj.1. mouse.

Organism-specific databases

CTD5770.
MGIMGI:97805. Ptpn1.

Phylogenomic databases

eggNOGCOG5599.
HOGENOMHOG000273908.
HOVERGENHBG008321.
InParanoidP35821.
KOK05696.
OMAMCMATVL.
OrthoDBEOG7RV9G4.
PhylomeDBP35821.
TreeFamTF315897.

Enzyme and pathway databases

ReactomeREACT_98458. Immune System.

Gene expression databases

ArrayExpressP35821.
BgeeP35821.
CleanExMM_PTPN1.
GenevestigatorP35821.

Family and domain databases

InterProIPR012265. Ptpn1/Ptpn2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFPIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSPR00700. PRTYPHPHTASE.
SMARTSM00194. PTPc. 1 hit.
[Graphical view]
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPTPN1. mouse.
NextBio296070.
PROP35821.
SOURCESearch...

Entry information

Entry namePTN1_MOUSE
AccessionPrimary (citable) accession number: P35821
Secondary accession number(s): Q60840 expand/collapse secondary AC list , Q62131, Q64498, Q99JS1
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 146 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

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