Tyrosine-protein phosphatase non-receptor type 1

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P35821 (PTN1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 136. History...

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

Documents (2) |

Third-party data

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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
Protein-tyrosine phosphatase HA2
Short name=PTP-HA2

Gene names

Name:

Ptpn1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	432 AA.
Sequence status	Complete.
Protein existence	Evidence 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 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	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 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 mutant phenotype PubMed 15632081. Source: MGI regulation of endocytosis Inferred from sequence or structural similarity. Source: UniProtKB regulation of insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara regulation of signal transduction Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoplasmic vesicle Inferred from electronic annotation. Source: Compara 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: Compara
Molecular_function	protein tyrosine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB 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_0000094749

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 CLK1, CLK2 and PKB/AKT1 or PKB/AKT2 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 Ref.7

Experimental info

Sequence conflict

D → Y in M97590. Ref.2

Sequence conflict

173

H → P in AAA64615. Ref.3

Sequence conflict

266 – 267

QL → HV in AAA64615. Ref.3

Sequences

Sequence

Length

Mass (Da)

Tools

P35821 [UniParc].

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

FASTA

432

49,593

        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' referencesShow '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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-392, MASS SPECTROMETRY. 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.
IPI	IPI00123039.
PIR	JN0317.
RefSeq	NP_035331.3. NM_011201.3.
UniGene	Mm.277916.
3D structure databases
ProteinModelPortal	P35821.
SMR	P35821. Positions 1-282.
ModBase	Search...
Protein-protein interaction databases
IntAct	P35821. 2 interactions.
MINT	MINT-5313580.
PTM databases
PhosphoSite	P35821.
Proteomic databases
PaxDb	P35821.
PRIDE	P35821.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000029053; ENSMUSP00000029053; ENSMUSG00000027540.
GeneID	19246.
KEGG	mmu:19246.
Organism-specific databases
CTD	5770.
MGI	MGI:97805. Ptpn1.
Phylogenomic databases
eggNOG	COG5599.
HOGENOM	HOG000273908.
HOVERGEN	HBG008321.
InParanoid	P35821.
KO	K05696.
OMA	DGPIKEE.
OrthoDB	EOG418BND.
Enzyme and pathway databases
Reactome	REACT_107772. Immune System.
Gene expression databases
ArrayExpress	P35821.
Bgee	P35821.
CleanEx	MM_PTPN1.
Genevestigator	P35821.
GermOnline	ENSMUSG00000027540. Mus musculus.
Family and domain databases
InterPro	IPR012265. Ptpn1/2. 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
ChEMBL	CHEMBL3336.
ChiTaRS	PTPN1. mouse.
NextBio	296070.
SOURCE	Search...

Entry information

Entry name

PTN1_MOUSE

Accession

Primary (citable) accession number: P35821
Secondary accession number(s): Q60840

Q99JS1

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 1, 1994
Last sequence update:	November 1, 1997
Last modified:	May 1, 2013
This is version 136 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

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

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents