Tyrosine-protein phosphatase non-receptor type 22

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P29352 (PTN22_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 109. History...

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

Documents (3) |

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 22
EC=3.1.3.48

Alternative name(s):
Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP
PEST-domain phosphatase
Short name=PEP

Gene names

Name:	Ptpn22
Synonyms:	Ptpn8

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	802 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as negative regulator of T-cell receptor (TCR) signaling by direct dephosphorylation of the Src family kinases LCK and FYN, ITAMs of the TCRz/CD3 complex, as well as ZAP70, VAV, VCP and other key signaling molecules. Associates with and probably dephosphorylates CBL. Dephosphorylates LCK at its activating 'Tyr-394' residue. Dephosphorylates ZAP70 at its activating 'Tyr-492' residue. Dephosphorylates the immune system activator SKAP2 By similarity. Ref.3
Catalytic activity	Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate.
Subunit structure	Interacts with CBL By similarity. Interacts with CSK. Interacts with LPXN. Ref.3 Ref.4
Subcellular location	Cytoplasm Ref.3.
Tissue specificity	Spleen, thymus, lymph node and bone marrow.
Post-translational modification	Phosphorylation on Ser-35 by PKC/PRKCD abrogates its ability to dephosphorylate and inactivate the SRC family kinases By similarity.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class 4 subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Biological process	Immunity
Cellular component	Cytoplasm
Molecular function	Hydrolase Protein phosphatase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	T cell differentiation Inferred from mutant phenotype PubMed 14752163. Source: MGI T cell receptor signaling pathway Inferred from mutant phenotype PubMed 14752163. Source: MGI negative regulation of T cell activation Inferred from mutant phenotype PubMed 21044313. Source: BHF-UCL negative regulation of T cell receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB phosphoanandamide dephosphorylation Inferred from direct assay PubMed 16938887. Source: BHF-UCL regulation of natural killer cell proliferation Inferred from sequence or structural similarity. Source: BHF-UCL
Cellular_component	internal side of plasma membrane Inferred from direct assay PubMed 10940933. Source: UniProtKB nucleus Inferred from direct assay PubMed 10940933. Source: UniProtKB perinuclear region of cytoplasm Inferred from sequence or structural similarity. Source: BHF-UCL
Molecular_function	protein tyrosine phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 802

802

Tyrosine-protein phosphatase non-receptor type 22

PRO_0000094776

Regions

Domain

24 – 289

266

Tyrosine-protein phosphatase

Region

227 – 233

Substrate binding By similarity

Region

613 – 621

Interaction with CSK

Sites

Active site

227

Phosphocysteine intermediate By similarity

Binding site

195

Substrate By similarity

Binding site

274

Substrate By similarity

Amino acid modifications

Modified residue

Phosphoserine; by PKC/PRKCD By similarity

Modified residue

405

Phosphoserine Ref.5

Modified residue

634

Phosphoserine Ref.5

Modified residue

687

Phosphoserine Ref.5

Experimental info

Sequence conflict

K → Q in AAH55377. Ref.2

Sequence conflict

141

R → H in AAH55377. Ref.2

Secondary structure

802

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P29352 [UniParc].

Last modified December 1, 1992. Version 1.
Checksum: 0F1E45339BD4613E
Show »

FASTA

802

89,714

        10         20         30         40         50         60 
MDQREILQQL LKEAQKKKLN SEEFASEFLK LKRQSTKYKA DKIYPTTVAQ RPKNIKKNRY 

        70         80         90        100        110        120 
KDILPYDHSL VELSLLTSDE DSSYINASFI KGVYGPKAYI ATQGPLSTTL LDFWRMIWEY 

       130        140        150        160        170        180 
RILVIVMACM EFEMGKKKCE RYWAEPGETQ LQFGPFSISC EAEKKKSDYK IRTLKAKFNN 

       190        200        210        220        230        240 
ETRIIYQFHY KNWPDHDVPS SIDPILQLIW DMRCYQEDDC VPICIHCSAG CGRTGVICAV 

       250        260        270        280        290        300 
DYTWMLLKDG IIPKNFSVFN LIQEMRTQRP SLVQTQEQYE LVYSAVLELF KRHMDVISDN 

       310        320        330        340        350        360 
HLGREIQAQC SIPEQSLTVE ADSCPLDLPK NAMRDVKTTN QHSKQGAEAE STGGSSLGLR 

       370        380        390        400        410        420 
TSTMNAEEEL VLHSAKSSPS FNCLELNCGC NNKAVITRNG QARASPVVGE PLQKYQSLDF 

       430        440        450        460        470        480 
GSMLFGSCPS ALPINTADRY HNSKGPVKRT KSTPFELIQQ RKTNDLAVGD GFSCLESQLH 

       490        500        510        520        530        540 
EHYSLRELQV QRVAHVSSEE LNYSLPGACD ASCVPRHSPG ALRVHLYTSL AEDPYFSSSP 

       550        560        570        580        590        600 
PNSADSKMSF DLPEKQDGAT SPGALLPASS TTSFFYSNPH DSLVMNTLTS FSPPLNQETA 

       610        620        630        640        650        660 
VEAPSRRTDD EIPPPLPERT PESFIVVEEA GEPSPRVTES LPLVVTFGAS PECSGTSEMK 

       670        680        690        700        710        720 
SHDSVGFTPS KNVKLRSPKS DRHQDGSPPP PLPERTLESF FLADEDCIQA QAVQTSSTSY 

       730        740        750        760        770        780 
PETTENSTSS KQTLRTPGKS FTRSKSLKIF RNMKKSVCNS SSPSKPTERV QPKNSSSFLN 

       790        800 
FGFGNRFSKP KGPRNPPSAW NM

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of hematopoietic intracellular protein tyrosine phosphatases: description of a phosphatase containing an SH2 domain and another enriched in proline-, glutamic acid-, serine-, and threonine-rich sequences." Matthews R.J., Bowne D.B., Flores E., Thomas M.L. Mol. Cell. Biol. 12:2396-2405(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[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]. Strain: C57BL/6NCr. Tissue: Hematopoietic stem cell.
[3]	"Association of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic cells." Cloutier J.-F., Veillette A. EMBO J. 15:4909-4918(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 495-789, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH CSK. Tissue: Splenocyte.
[4]	"Leupaxin binds to PEST domain tyrosine phosphatase PEP." Watanabe N., Amano N., Ishizuka H., Mashima K. Mol. Cell. Biochem. 269:13-17(2005) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH LPXN.
[5]	"The phagosomal proteome in interferon-gamma-activated macrophages." Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P. Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-405; SER-634 AND SER-687, MASS SPECTROMETRY. Tissue: Macrophage.
[6]	"A novel, specific interaction involving the Csk SH3 domain and its natural ligand." Ghose R., Shekhtman A., Goger M.J., Ji H., Cowburn D. Nat. Struct. Biol. 8:998-1004(2001) [PubMed] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 612-629 IN COMPLEX WITH CSK.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M90388 mRNA. Translation: AAA39994.1.
BC055377 mRNA. Translation: AAH55377.1.

IPI

IPI00124318.

PIR

B44390.

RefSeq

NP_033005.1. NM_008979.1.

UniGene

Mm.395.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JEG	NMR	-	B	605-629	[»]

ProteinModelPortal

P29352.

SMR

P29352. Positions 3-297.

ModBase

Search...

PTM databases

PhosphoSite

P29352.

Proteomic databases

PRIDE

P29352.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000029433; ENSMUSP00000029433; ENSMUSG00000027843.

GeneID

19260.

KEGG

mmu:19260.

UCSC

uc008qtv.1. mouse.

Organism-specific databases

CTD

26191.

MGI

MGI:107170. Ptpn22.

Phylogenomic databases

eggNOG

COG5599.

GeneTree

ENSGT00700000104095.

HOGENOM

HOG000252955.

HOVERGEN

HBG103877.

InParanoid

P29352.

K01104.

OMA

ADEDCMQ.

OrthoDB

EOG4V1705.

Gene expression databases

ArrayExpress

P29352.

Bgee

P29352.

Genevestigator

P29352.

GermOnline

ENSMUSG00000027843. Mus musculus.

Family and domain databases

InterPro

IPR016276. Non-rcpt_Tyr_Pase_8/22.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

Pfam

PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PIRSF

PIRSF000930. PTPN8_PTPN22. 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

ChiTaRS

PTPN22. mouse.

EvolutionaryTrace

P29352.

NextBio

296116.

SOURCE

Search...

Entry information

Entry name

PTN22_MOUSE

Accession

Primary (citable) accession number: P29352
Secondary accession number(s): Q7TMP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	December 1, 1992
Last modified:	April 3, 2013
This is version 109 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

MGD cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

PTM 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