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Q9Y2R2

- PTN22_HUMAN

UniProt

Q9Y2R2 - PTN22_HUMAN

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Protein

Tyrosine-protein phosphatase non-receptor type 22

Gene

PTPN22

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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-493' residue. Dephosphorylates the immune system activator SKAP2.4 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Enzyme regulationi

Down-regulated by phosphorylation.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei195 – 1951SubstrateBy similarity
Active sitei227 – 2271Phosphocysteine intermediatePROSITE-ProRule annotation
Binding sitei274 – 2741Substrate1 Publication

GO - Molecular functioni

  1. kinase binding Source: BHF-UCL
  2. protein tyrosine phosphatase activity Source: UniProtKB
  3. SH3 domain binding Source: BHF-UCL

GO - Biological processi

  1. negative regulation of T cell activation Source: BHF-UCL
  2. negative regulation of T cell receptor signaling pathway Source: UniProtKB
  3. peptidyl-tyrosine dephosphorylation Source: GOC
  4. phosphoanandamide dephosphorylation Source: BHF-UCL
  5. protein dephosphorylation Source: BHF-UCL
  6. regulation of B cell receptor signaling pathway Source: BHF-UCL
  7. regulation of innate immune response Source: BHF-UCL
  8. regulation of natural killer cell proliferation Source: BHF-UCL
  9. T cell differentiation Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Keywords - Biological processi

Immunity

Enzyme and pathway databases

SignaLinkiQ9Y2R2.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase non-receptor type 22 (EC:3.1.3.48)
Alternative name(s):
Hematopoietic cell protein-tyrosine phosphatase 70Z-PEP
Lymphoid phosphatase
Short name:
LyP
PEST-domain phosphatase
Short name:
PEP
Gene namesi
Name:PTPN22
Synonyms:PTPN8
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9652. PTPN22.

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic side of plasma membrane Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Systemic lupus erythematosus (SLE) [MIM:152700]: A chronic, relapsing, inflammatory, and often febrile multisystemic disorder of connective tissue, characterized principally by involvement of the skin, joints, kidneys and serosal membranes. It is of unknown etiology, but is thought to represent a failure of the regulatory mechanisms of the autoimmune system. The disease is marked by a wide range of system dysfunctions, an elevated erythrocyte sedimentation rate, and the formation of LE cells in the blood or bone marrow.1 Publication
Note: Disease susceptibility is associated with variations affecting the gene represented in this entry.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi35 – 351S → E: Loss of phosphorylation by PKC/PRKCD. 1 Publication
Mutagenesisi36 – 361T → E: No effect on phosphorylation by PKC/PRKCD. 1 Publication
Mutagenesisi129 – 1291C → S: Decreases activity 2 fold. 1 Publication
Mutagenesisi231 – 2311C → S: Decreases activity 7 fold. 1 Publication

Keywords - Diseasei

Systemic lupus erythematosus

Organism-specific databases

MIMi152700. phenotype.
Orphaneti397. Giant cell arteritis.
900. Granulomatosis with polyangiitis.
85408. Juvenile rheumatoid factor-negative polyarthritis.
85410. Oligoarticular juvenile arthritis.
93552. Pediatric systemic lupus erythematosus.
536. Systemic lupus erythematosus.
3437. Vogt-Koyanagi-Harada disease.
PharmGKBiPA33995.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 807807Tyrosine-protein phosphatase non-receptor type 22PRO_0000094775Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei35 – 351Phosphoserine; by PKC/PRKCD1 Publication
Disulfide bondi129 ↔ 2271 Publication
Modified residuei635 – 6351PhosphoserineBy similarity
Modified residuei684 – 6841PhosphoserineBy similarity
Modified residuei692 – 6921PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation on Ser-35 by PKC/PRKCD abrogates its ability to dephosphorylate and inactivate the SRC family kinases.1 Publication

Keywords - PTMi

Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiQ9Y2R2.
PaxDbiQ9Y2R2.
PRIDEiQ9Y2R2.

PTM databases

PhosphoSiteiQ9Y2R2.

Expressioni

Tissue specificityi

Both isoform 1 and 4 are predominantly expressed in lymphoid tissues and cells. Isoform 1 is expressed in thymocytes and both mature B and T-cells.

Gene expression databases

BgeeiQ9Y2R2.
CleanExiHS_PTPN22.
ExpressionAtlasiQ9Y2R2. baseline and differential.
GenevestigatoriQ9Y2R2.

Organism-specific databases

HPAiCAB012209.
HPA004912.
HPA013350.

Interactioni

Subunit structurei

Interacts with CSK. Interacts with LPXN (By similarity). Interacts with CBL.By similarity4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CD247P209634EBI-1211241,EBI-1165705
EGFRP005332EBI-1211241,EBI-297353
GRB2P629932EBI-1211241,EBI-401755
LCKP062395EBI-1211241,EBI-1348
PSTPIP1O435866EBI-1211241,EBI-1050964
ZAP70P434034EBI-1211241,EBI-1211276

Protein-protein interaction databases

BioGridi117604. 12 interactions.
DIPiDIP-29953N.
IntActiQ9Y2R2. 18 interactions.
STRINGi9606.ENSP00000352833.

Structurei

Secondary structure

1
807
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1614
Helixi21 – 4020
Helixi47 – 504
Helixi52 – 554
Beta strandi59 – 624
Helixi67 – 693
Beta strandi70 – 723
Turni80 – 834
Beta strandi86 – 927
Beta strandi95 – 1028
Helixi107 – 1093
Helixi110 – 11910
Beta strandi124 – 1274
Beta strandi131 – 1333
Beta strandi135 – 1373
Beta strandi146 – 1483
Beta strandi151 – 1533
Beta strandi156 – 16510
Beta strandi167 – 17812
Beta strandi181 – 19010
Beta strandi195 – 1973
Helixi199 – 2024
Helixi203 – 21513
Beta strandi218 – 2214
Beta strandi223 – 2264
Beta strandi228 – 2325
Helixi233 – 24816
Helixi258 – 2669
Helixi276 – 30126

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P6XX-ray1.90A/B1-302[»]
2QCJX-ray3.00A/B1-294[»]
2QCTX-ray2.80A/B1-294[»]
3BRHX-ray2.20A/B1-310[»]
3H2XX-ray2.20A1-302[»]
3OLRX-ray2.50A/B/C/D1-294[»]
3OMHX-ray2.90A/B/C/D1-294[»]
4J51X-ray2.30A/B1-303[»]
ProteinModelPortaliQ9Y2R2.
SMRiQ9Y2R2. Positions 1-335.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y2R2.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 289266Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni227 – 2337Substrate binding

Sequence similaritiesi

Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118836.
HOVERGENiHBG103877.
InParanoidiQ9Y2R2.
KOiK18024.
OrthoDBiEOG744T8Z.
PhylomeDBiQ9Y2R2.
TreeFamiTF351977.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR016276. PTPN22.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PANTHERiPTHR19134:SF260. PTHR19134:SF260. 1 hit.
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000930. PTPN8_PTPN22. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 1 hit.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9Y2R2-1) [UniParc]FASTAAdd to Basket

Also known as: LyP1

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDQREILQKF LDEAQSKKIT KEEFANEFLK LKRQSTKYKA DKTYPTTVAE
60 70 80 90 100
KPKNIKKNRY KDILPYDYSR VELSLITSDE DSSYINANFI KGVYGPKAYI
110 120 130 140 150
ATQGPLSTTL LDFWRMIWEY SVLIIVMACM EYEMGKKKCE RYWAEPGEMQ
160 170 180 190 200
LEFGPFSVSC EAEKRKSDYI IRTLKVKFNS ETRTIYQFHY KNWPDHDVPS
210 220 230 240 250
SIDPILELIW DVRCYQEDDS VPICIHCSAG CGRTGVICAI DYTWMLLKDG
260 270 280 290 300
IIPENFSVFS LIREMRTQRP SLVQTQEQYE LVYNAVLELF KRQMDVIRDK
310 320 330 340 350
HSGTESQAKH CIPEKNHTLQ ADSYSPNLPK STTKAAKMMN QQRTKMEIKE
360 370 380 390 400
SSSFDFRTSE ISAKEELVLH PAKSSTSFDF LELNYSFDKN ADTTMKWQTK
410 420 430 440 450
AFPIVGEPLQ KHQSLDLGSL LFEGCSNSKP VNAAGRYFNS KVPITRTKST
460 470 480 490 500
PFELIQQRET KEVDSKENFS YLESQPHDSC FVEMQAQKVM HVSSAELNYS
510 520 530 540 550
LPYDSKHQIR NASNVKHHDS SALGVYSYIP LVENPYFSSW PPSGTSSKMS
560 570 580 590 600
LDLPEKQDGT VFPSSLLPTS STSLFSYYNS HDSLSLNSPT NISSLLNQES
610 620 630 640 650
AVLATAPRID DEIPPPLPVR TPESFIVVEE AGEFSPNVPK SLSSAVKVKI
660 670 680 690 700
GTSLEWGGTS EPKKFDDSVI LRPSKSVKLR SPKSELHQDR SSPPPPLPER
710 720 730 740 750
TLESFFLADE DCMQAQSIET YSTSYPDTME NSTSSKQTLK TPGKSFTRSK
760 770 780 790 800
SLKILRNMKK SICNSCPPNK PAESVQSNNS SSFLNFGFAN RFSKPKGPRN

PPPTWNI
Length:807
Mass (Da):91,705
Last modified:March 27, 2002 - v2
Checksum:i1ABE8AE89C9D9FBF
GO
Isoform 2 (identifier: Q9Y2R2-2) [UniParc]FASTAAdd to Basket

Also known as: LyP2

The sequence of this isoform differs from the canonical sequence as follows:
     685-807: ELHQDRSSPP...PRNPPPTWNI → GKNFSWL

Note: Due to intron retention.

Show »
Length:691
Mass (Da):78,769
Checksum:iA85EF69FDFDE9D58
GO
Isoform 3 (identifier: Q9Y2R2-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     251-305: Missing.

Note: No experimental confirmation available.

Show »
Length:752
Mass (Da):85,138
Checksum:i826CAD31B7C20983
GO
Isoform 4 (identifier: Q9Y2R2-4) [UniParc]FASTAAdd to Basket

Also known as: LYP3

The sequence of this isoform differs from the canonical sequence as follows:
     647-674: Missing.

Show »
Length:779
Mass (Da):88,647
Checksum:iAEA60DFC0BB05C11
GO
Isoform 5 (identifier: Q9Y2R2-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     137-160: Missing.
     181-203: ETRTIYQFHYKNWPDHDVPSSID → VSVILAHQTSLQNLFSQITPAHF
     204-807: Missing.

Note: No experimental confirmation available.

Show »
Length:179
Mass (Da):20,932
Checksum:iE5F9FFCC426C6E2C
GO
Isoform 6 (identifier: Q9Y2R2-6) [UniParc]FASTAAdd to Basket

Also known as: PTPN22.6

The sequence of this isoform differs from the canonical sequence as follows:
     124-250: Missing.
     788-807: FANRFSKPKGPRNPPPTWNI → MCVILLKS

Note: Lacks most of the phosphatase domain and functions as a dominant negative isoform of the full length PTPN22.

Show »
Length:668
Mass (Da):75,488
Checksum:i93025ACF91033DAA
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti51 – 522KP → NA in AAD00904. (PubMed:10068674)Curated
Sequence conflicti51 – 522KP → NA in AAD00905. (PubMed:10068674)Curated
Sequence conflicti126 – 1261V → G in AAD27764. (PubMed:21044313)Curated
Sequence conflicti147 – 1471G → V in AAD27764. (PubMed:21044313)Curated
Sequence conflicti240 – 2401I → IV in AAD00905. (PubMed:10068674)Curated
Sequence conflicti372 – 3721A → V in AK310570. (PubMed:14702039)Curated
Sequence conflicti420 – 4201L → P in AAD27764. (PubMed:21044313)Curated
Sequence conflicti742 – 7421P → S in AAD27764. (PubMed:21044313)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti620 – 6201R → W Confers susceptibility to systemic lupus erythematosus and type 1 diabetes mellitus; affects CSK kinase binding. 6 Publications
Corresponds to variant rs2476601 [ dbSNP | Ensembl ].
VAR_022605

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei124 – 250127Missing in isoform 6. 1 PublicationVSP_044428Add
BLAST
Alternative sequencei137 – 16024Missing in isoform 5. 1 PublicationVSP_039725Add
BLAST
Alternative sequencei181 – 20323ETRTI…PSSID → VSVILAHQTSLQNLFSQITP AHF in isoform 5. 1 PublicationVSP_039726Add
BLAST
Alternative sequencei204 – 807604Missing in isoform 5. 1 PublicationVSP_039727Add
BLAST
Alternative sequencei251 – 30555Missing in isoform 3. 1 PublicationVSP_039728Add
BLAST
Alternative sequencei647 – 67428Missing in isoform 4. 1 PublicationVSP_039729Add
BLAST
Alternative sequencei685 – 807123ELHQD…PTWNI → GKNFSWL in isoform 2. 1 PublicationVSP_005134Add
BLAST
Alternative sequencei788 – 80720FANRF…PTWNI → MCVILLKS in isoform 6. 1 PublicationVSP_044429Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF001846 mRNA. Translation: AAD00904.1.
AF001847 mRNA. Translation: AAD00905.1.
GU479452 mRNA. Translation: ADD59979.1.
AF077031 mRNA. Translation: AAD27764.1.
AK310570 mRNA. No translation available.
EF064714 Genomic DNA. Translation: ABK41897.1.
AL137856 Genomic DNA. Translation: CAI19068.1.
CH471122 Genomic DNA. Translation: EAW56575.1.
CH471122 Genomic DNA. Translation: EAW56576.1.
BC017785 mRNA. Translation: AAH17785.1.
BC071670 mRNA. Translation: AAH71670.1.
CCDSiCCDS863.1. [Q9Y2R2-1]
CCDS864.2. [Q9Y2R2-3]
RefSeqiNP_001180360.1. NM_001193431.1. [Q9Y2R2-4]
NP_036543.4. NM_012411.4. [Q9Y2R2-3]
NP_057051.3. NM_015967.5. [Q9Y2R2-1]
UniGeneiHs.535276.

Genome annotation databases

EnsembliENST00000460620; ENSP00000433141; ENSG00000134242. [Q9Y2R2-5]
GeneIDi26191.
KEGGihsa:26191.
UCSCiuc001eds.3. human. [Q9Y2R2-1]
uc001edt.3. human. [Q9Y2R2-5]
uc009wgq.3. human. [Q9Y2R2-3]
uc009wgs.2. human. [Q9Y2R2-6]
uc021orx.1. human. [Q9Y2R2-4]

Polymorphism databases

DMDMi20139861.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF001846 mRNA. Translation: AAD00904.1 .
AF001847 mRNA. Translation: AAD00905.1 .
GU479452 mRNA. Translation: ADD59979.1 .
AF077031 mRNA. Translation: AAD27764.1 .
AK310570 mRNA. No translation available.
EF064714 Genomic DNA. Translation: ABK41897.1 .
AL137856 Genomic DNA. Translation: CAI19068.1 .
CH471122 Genomic DNA. Translation: EAW56575.1 .
CH471122 Genomic DNA. Translation: EAW56576.1 .
BC017785 mRNA. Translation: AAH17785.1 .
BC071670 mRNA. Translation: AAH71670.1 .
CCDSi CCDS863.1. [Q9Y2R2-1 ]
CCDS864.2. [Q9Y2R2-3 ]
RefSeqi NP_001180360.1. NM_001193431.1. [Q9Y2R2-4 ]
NP_036543.4. NM_012411.4. [Q9Y2R2-3 ]
NP_057051.3. NM_015967.5. [Q9Y2R2-1 ]
UniGenei Hs.535276.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2P6X X-ray 1.90 A/B 1-302 [» ]
2QCJ X-ray 3.00 A/B 1-294 [» ]
2QCT X-ray 2.80 A/B 1-294 [» ]
3BRH X-ray 2.20 A/B 1-310 [» ]
3H2X X-ray 2.20 A 1-302 [» ]
3OLR X-ray 2.50 A/B/C/D 1-294 [» ]
3OMH X-ray 2.90 A/B/C/D 1-294 [» ]
4J51 X-ray 2.30 A/B 1-303 [» ]
ProteinModelPortali Q9Y2R2.
SMRi Q9Y2R2. Positions 1-335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117604. 12 interactions.
DIPi DIP-29953N.
IntActi Q9Y2R2. 18 interactions.
STRINGi 9606.ENSP00000352833.

Chemistry

BindingDBi Q9Y2R2.
ChEMBLi CHEMBL2889.

PTM databases

PhosphoSitei Q9Y2R2.

Polymorphism databases

DMDMi 20139861.

Proteomic databases

MaxQBi Q9Y2R2.
PaxDbi Q9Y2R2.
PRIDEi Q9Y2R2.

Protocols and materials databases

DNASUi 26191.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000460620 ; ENSP00000433141 ; ENSG00000134242 . [Q9Y2R2-5 ]
GeneIDi 26191.
KEGGi hsa:26191.
UCSCi uc001eds.3. human. [Q9Y2R2-1 ]
uc001edt.3. human. [Q9Y2R2-5 ]
uc009wgq.3. human. [Q9Y2R2-3 ]
uc009wgs.2. human. [Q9Y2R2-6 ]
uc021orx.1. human. [Q9Y2R2-4 ]

Organism-specific databases

CTDi 26191.
GeneCardsi GC01M114356.
HGNCi HGNC:9652. PTPN22.
HPAi CAB012209.
HPA004912.
HPA013350.
MIMi 152700. phenotype.
600716. gene.
neXtProti NX_Q9Y2R2.
Orphaneti 397. Giant cell arteritis.
900. Granulomatosis with polyangiitis.
85408. Juvenile rheumatoid factor-negative polyarthritis.
85410. Oligoarticular juvenile arthritis.
93552. Pediatric systemic lupus erythematosus.
536. Systemic lupus erythematosus.
3437. Vogt-Koyanagi-Harada disease.
PharmGKBi PA33995.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118836.
HOVERGENi HBG103877.
InParanoidi Q9Y2R2.
KOi K18024.
OrthoDBi EOG744T8Z.
PhylomeDBi Q9Y2R2.
TreeFami TF351977.

Enzyme and pathway databases

SignaLinki Q9Y2R2.

Miscellaneous databases

EvolutionaryTracei Q9Y2R2.
GeneWikii PTPN22.
GenomeRNAii 26191.
NextBioi 35503189.
PROi Q9Y2R2.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y2R2.
CleanExi HS_PTPN22.
ExpressionAtlasi Q9Y2R2. baseline and differential.
Genevestigatori Q9Y2R2.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR016276. PTPN22.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
PANTHERi PTHR19134:SF260. PTHR19134:SF260. 1 hit.
Pfami PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000930. PTPN8_PTPN22. 1 hit.
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 1 hit.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of a lymphoid-specific, inducible human protein tyrosine phosphatase, Lyp."
    Cohen S., Dadi H., Shaoul E., Sharfe N., Roifman C.M.
    Blood 93:2013-2024(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), INTERACTION WITH CBL.
  2. "Identification of a variant form of tyrosine phosphatase LYP."
    Wang S., Dong H., Han J., Ho W.T., Fu X., Zhao Z.J.
    BMC Mol. Biol. 11:78-78(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), VARIANT TRP-620.
  3. "Human protein tyrosine phosphatase (70zpep) homolog."
    Liu T., Zhang J., Fu G., Zhang Q., Ye M., Zhou J., Wu J., Shen Y., Yu M., Chen S., Mao M., Chen Z.
    Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT TRP-620.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 6).
  5. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-620.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT TRP-620.
  8. "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] (ISOFORMS 3 AND 5).
    Tissue: Lymph.
  9. Cited for: FUNCTION.
  10. "Protein tyrosine phosphatase PTPN22 in human autoimmunity."
    Vang T., Miletic A.V., Bottini N., Mustelin T.
    Autoimmunity 40:453-461(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW ON FUNCTION.
  11. "PTPN22.6, a dominant negative isoform of PTPN22 and potential biomarker of rheumatoid arthritis."
    Chang H.H., Tai T.S., Lu B., Iannaccone C., Cernadas M., Weinblatt M., Shadick N., Miaw S.C., Ho I.C.
    PLoS ONE 7:E33067-E33067(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING (ISOFORM 6).
  12. "Structure, inhibitor, and regulatory mechanism of Lyp, a lymphoid-specific tyrosine phosphatase implicated in autoimmune diseases."
    Yu X., Sun J.P., He Y., Guo X., Liu S., Zhou B., Hudmon A., Zhang Z.Y.
    Proc. Natl. Acad. Sci. U.S.A. 104:19767-19772(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-294 IN COMPLEX WITH INHIBITOR, FUNCTION, PHOSPHORYLATION AT SER-35, MUTAGENESIS OF SER-35 AND THR-36.
  13. "Crystal structure of the human lymphoid tyrosine phosphatase catalytic domain: insights into redox regulation."
    Tsai S.J., Sen U., Zhao L., Greenleaf W.B., Dasgupta J., Fiorillo E., Orru V., Bottini N., Chen X.S.
    Biochemistry 48:4838-4845(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-302, DISULFIDE BOND, MUTAGENESIS OF CYS-129 AND CYS-231.
  14. "Large-scale structural analysis of the classical human protein tyrosine phosphatome."
    Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S.
    Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-302, FUNCTION.
  15. "Lyp/PTPN22 phosphatase domain: substrate recognition and specificity for Src family kinases."
    Seidel R.D., Love J., Piserchio A., Cowburn D.
    Submitted (DEC-2009) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-310 IN COMPLEX WITH SUBSTRATE.
  16. "Substrate specificity of lymphoid-specific tyrosine phosphatase (Lyp) and identification of Src kinase-associated protein of 55 kDa homolog (SKAP-HOM) as a Lyp substrate."
    Yu X., Chen M., Zhang S., Yu Z.H., Sun J.P., Wang L., Liu S., Imasaki T., Takagi Y., Zhang Z.Y.
    J. Biol. Chem. 286:30526-30534(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-294 OF MUTANT SER-227 ALONE AND IN COMPLEX WITH SKAP2 PEPTIDE, SUBSTRATE SPECIFICITY, FUNCTION.
  17. Cited for: VARIANT TRP-620, INVOLVEMENT IN SLE.
  18. Cited for: VARIANT TRP-620, CHARACTERIZATION OF VARIANT TRP-620.

Entry informationi

Entry nameiPTN22_HUMAN
AccessioniPrimary (citable) accession number: Q9Y2R2
Secondary accession number(s): A0N0K6
, B1ALC8, D4NZ71, E9PLD8, E9PPI1, O95063, O95064, Q6IPX8, Q8WVM1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 27, 2002
Last modified: October 29, 2014
This is version 131 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3