Tyrosine-protein phosphatase non-receptor type 1

Contribute

Send feedback

Read comments (?) or add your own

P20417 (PTN1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 121. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

text xml rdf/xml gff fasta

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

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

Gene names

Name:

Ptpn1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 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.
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 component	Endoplasmic reticulum Membrane
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Phosphoprotein S-nitrosylation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin 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: Compara regulation of endocytosis Inferred from sequence or structural similarity. Source: UniProtKB regulation of insulin receptor signaling pathway Inferred from mutant phenotype PubMed 12941932. Source: RGD
Cellular_component	anchored to 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: Compara
Molecular_function	insulin receptor binding Inferred from direct assay PubMed 7711057. Source: RGD protein tyrosine phosphatase activity Inferred from direct assay PubMed 7711057. Source: RGD zinc ion binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 432

432

Tyrosine-protein phosphatase non-receptor type 1

PRO_0000094750

Regions

Domain

3 – 277

275

Tyrosine-protein phosphatase

Region

215 – 221

Substrate binding By similarity

Sites

Active site

215

Phosphocysteine intermediate By similarity

Binding site

181

Substrate By similarity

Binding site

262

Substrate By similarity

Amino acid modifications

Modified residue

N-acetylmethionine By similarity

Modified residue

Phosphotyrosine By similarity

Modified residue

Phosphoserine; by PKB/AKT1, CLK1 and CLK2 By similarity

Modified residue

Phosphotyrosine; by EGFR By similarity

Modified residue

215

Cysteine persulfide By similarity

Modified residue

215

S-nitrosocysteine; in reversibly inhibited form By similarity

Modified residue

242

Phosphoserine; by CLK1 and CLK2 By similarity

Modified residue

243

Phosphoserine; by CLK1 and CLK2 By similarity

Modified residue

392

Phosphoserine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P20417 [UniParc].

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

FASTA

432

49,674

        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' referencesShow '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.
IPI	IPI00199272.
PIR	A34845.
RefSeq	NP_036769.1. NM_012637.2.
UniGene	Rn.11317.
3D structure databases
ProteinModelPortal	P20417.
SMR	P20417. Positions 1-299.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20417. 1 interaction.
STRING	10116.ENSRNOP00000014309.
Proteomic databases
PaxDb	P20417.
PRIDE	P20417.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000014309; ENSRNOP00000014309; ENSRNOG00000010574.
GeneID	24697.
KEGG	rno:24697.
UCSC	RGD:61965. rat.
Organism-specific databases
CTD	5770.
RGD	61965. Ptpn1.
Phylogenomic databases
eggNOG	COG5599.
GeneTree	ENSGT00700000104092.
HOGENOM	HOG000273908.
HOVERGEN	HBG008321.
InParanoid	P20417.
KO	K05696.
OMA	DGPIKEE.
OrthoDB	EOG418BND.
Gene expression databases
Genevestigator	P20417.
GermOnline	ENSRNOG00000010574. Rattus norvegicus.
Family and domain databases
InterPro	IPR012265. Ptpn1/Ptpn2. IPR000387. Tyr/Dual-sp_Pase. IPR016130. Tyr_Pase_AS. IPR000242. Tyr_Pase_rcpt/non-rcpt. [Graphical view]
PANTHER	PTHR19134:SF57. PTHR19134:SF57. 1 hit.
Pfam	PF00102. Y_phosphatase. 1 hit. [Graphical view]
PIRSF	PIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTS	PR00700. PRTYPHPHTASE.
SMART	SM00194. PTPc. 1 hit. [Graphical view]
PROSITE	PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 1 hit. PS50055. TYR_PHOSPHATASE_PTP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
BindingDB	P20417.
ChEMBL	CHEMBL2371.
NextBio	604151.

Entry information

Entry name

PTN1_RAT

Accession

Primary (citable) accession number: P20417

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	February 1, 1991
Last modified:	May 29, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents