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P20417 (PTN1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 131. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·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
Gene names
Name:Ptpn1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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

Found in several tissues including central nervous system, liver and kidney. A high level of expression was found in the hippocampus.

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 electronic annotation. Source: Ensembl

platelet-derived growth factor receptor-beta signaling pathway

Inferred from electronic annotation. Source: Ensembl

protein dephosphorylation

Inferred from direct assay PubMed 7711057. Source: RGD

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 mutant phenotype PubMed 12941932. Source: RGD

regulation of signal transduction

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentanchored component of membrane

Non-traceable author statement Ref.1. Source: RGD

cytoplasmic vesicle

Inferred from direct assay PubMed 17563729. Source: RGD

cytosol

Inferred from direct assay PubMed 7711057. Source: RGD

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_functioninsulin receptor binding

Inferred from direct assay PubMed 7711057. Source: RGD

protein binding

Inferred from physical interaction PubMed 8940134. Source: UniProtKB

protein tyrosine phosphatase activity

Inferred from direct assay PubMed 7711057. Source: RGD

zinc ion binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EGFRP0053311EBI-916819,EBI-297353From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Tyrosine-protein phosphatase non-receptor type 1
PRO_0000094750

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 PKB/AKT1, CLK1 and CLK2 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

Sequences

Sequence LengthMass (Da)Tools
P20417 [UniParc].

Last modified February 1, 1991. Version 1.
Checksum: 0D5859A09B1885C1

FASTA43249,674
        10         20         30         40         50         60 
MEMEKEFEQI DKAGNWAAIY QDIRHEASDF PCRIAKLPKN KNRNRYRDVS PFDHSRIKLH 

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

       130        140        150        160        170        180 
CAQYWPQKEE KEMVFDDTNL KLTLISEDVK SYYTVRQLEL ENLATQEARE ILHFHYTTWP 

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

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

       310        320        330        340        350        360 
PPPEHVPPPP RPPKRTLEPH NGKCKELFSN HQWVSEESCE DEDILAREES RAPSIAVHSM 

       370        380        390        400        410        420 
SSMSQDTEVR KRMVGGGLQS AQASVPTEEE LSPTEEEQKA HRPVHWKPFL VNVCMATALA 

       430 
TGAYLCYRVC FH 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and expression of a protein-tyrosine-phosphatase."
Guan K., Haun R.S., Watson S.J., Geahlen R.L., Dixon J.E.
Proc. Natl. Acad. Sci. U.S.A. 87:1501-1505(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"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].
Tissue: Testis.
[3]"Insulin receptor and epidermal growth factor receptor dephosphorylation by three major rat liver protein-tyrosine phosphatases expressed in a recombinant bacterial system."
Hashimoto N., Zhang W.R., Goldstein B.J.
Biochem. J. 284:569-576(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 35-283.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M33962 mRNA. Translation: AAC79516.1.
BC081829 mRNA. Translation: AAH81829.1.
PIRA34845.
RefSeqNP_036769.1. NM_012637.2.
XP_006235700.1. XM_006235638.1.
UniGeneRn.11317.

3D structure databases

ProteinModelPortalP20417.
SMRP20417. Positions 1-299.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP20417. 3 interactions.
STRING10116.ENSRNOP00000014309.

Chemistry

BindingDBP20417.
ChEMBLCHEMBL2371.

Proteomic databases

PaxDbP20417.
PRIDEP20417.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000014309; ENSRNOP00000014309; ENSRNOG00000010574.
GeneID24697.
KEGGrno:24697.
UCSCRGD:61965. rat.

Organism-specific databases

CTD5770.
RGD61965. Ptpn1.

Phylogenomic databases

eggNOGCOG5599.
GeneTreeENSGT00750000117312.
HOGENOMHOG000273908.
HOVERGENHBG008321.
InParanoidP20417.
KOK05696.
OMAMCMATVL.
OrthoDBEOG7RV9G4.
PhylomeDBP20417.

Gene expression databases

ArrayExpressP20417.
GenevestigatorP20417.

Family and domain databases

Gene3D3.90.190.10. 1 hit.
InterProIPR029021. Prot-tyrosine_phosphatase-like.
IPR012265. 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]
SUPFAMSSF52799. SSF52799. 1 hit.
PROSITEPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio604151.
PROP20417.

Entry information

Entry namePTN1_RAT
AccessionPrimary (citable) accession number: P20417
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: February 1, 1991
Last modified: June 11, 2014
This is version 131 of the entry and version 1 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