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P35236

- PTN7_HUMAN

UniProt

P35236 - PTN7_HUMAN

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Protein

Tyrosine-protein phosphatase non-receptor type 7

Gene

PTPN7

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

Functioni

Protein phosphatase that acts preferentially on tyrosine-phosphorylated MAPK1. Plays a role in the regulation of T and B-lymphocyte development and signal transduction.6 Publications

Catalytic activityi

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

Enzyme regulationi

Inhibited in cells after FCER1A triggering.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei257 – 2571Substrate
Active sitei291 – 2911Phosphocysteine intermediate1 PublicationPROSITE-ProRule annotation
Binding sitei335 – 3351Substrate

GO - Molecular functioni

  1. protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. peptidyl-tyrosine dephosphorylation Source: GOC
  2. protein dephosphorylation Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosine-protein phosphatase non-receptor type 7 (EC:3.1.3.48)
Alternative name(s):
Hematopoietic protein-tyrosine phosphatase
Short name:
HEPTP
Protein-tyrosine phosphatase LC-PTP
Gene namesi
Name:PTPN7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:9659. PTPN7.

Subcellular locationi

Cytoplasm 1 Publication. Cytoplasmcytoskeleton By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytoplasmic side of plasma membrane Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-KW
  4. cytosol Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi44 – 441S → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation. 1 Publication
Mutagenesisi44 – 441S → D: Reduces binding of MAP kinase. 1 Publication
Mutagenesisi66 – 661T → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-93. 1 Publication
Mutagenesisi93 – 931S → A: Prevents dissociation of bound MAP kinase and enhances their dephosphorylation; when associated with A-66. 1 Publication
Mutagenesisi125 – 1251Y → A: Strongly reduced catalytic activity. 1 Publication
Mutagenesisi257 – 2571D → A: Loss of catalytic activity. 1 Publication
Mutagenesisi291 – 2911C → S: Loss of catalytic activity. 1 Publication
Mutagenesisi335 – 3351Q → A: Reduced catalytic activity. 1 Publication

Organism-specific databases

PharmGKBiPA34003.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 360360Tyrosine-protein phosphatase non-receptor type 7PRO_0000094761Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei44 – 441Phosphoserine3 Publications
Modified residuei66 – 661Phosphothreonine2 Publications
Modified residuei93 – 931Phosphoserine1 Publication
Modified residuei143 – 1431Phosphoserine1 Publication
Modified residuei291 – 2911Cysteine sulfenic acid (-SOH)By similarity

Post-translational modificationi

Phosphorylated on serine residues in resting T-cells. Phosphorylation increases upon exposure to stimuli that increase intracellular cAMP levels. Phosphorylation leads to dissociation of bound MAP kinases.5 Publications
Oxidized at active site cysteine. Treatment with pervanadate (vanadate and H2O2) or with antigen enhanced oxidation of active site cysteine (By similarity).By similarity

Keywords - PTMi

Oxidation, Phosphoprotein

Proteomic databases

MaxQBiP35236.
PaxDbiP35236.
PRIDEiP35236.

PTM databases

PhosphoSiteiP35236.

Expressioni

Tissue specificityi

Expressed exclusively in thymus and spleen.2 Publications

Gene expression databases

BgeeiP35236.
CleanExiHS_PTPN7.
ExpressionAtlasiP35236. baseline and differential.
GenevestigatoriP35236.

Organism-specific databases

HPAiCAB009530.
HPA019118.

Interactioni

Subunit structurei

Monomer. Interacts with MAPK1, MAPK3 and several other MAP kinases.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAPK1P284826EBI-2265723,EBI-959949
MAPK14Q165392EBI-2265723,EBI-73946

Protein-protein interaction databases

BioGridi111743. 4 interactions.
DIPiDIP-29118N.
IntActiP35236. 4 interactions.
MINTiMINT-8206881.
STRINGi9606.ENSP00000356248.

Structurei

Secondary structure

1
360
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi38 – 414Combined sources
Helixi67 – 7711Combined sources
Beta strandi81 – 833Combined sources
Helixi84 – 896Combined sources
Helixi94 – 10310Combined sources
Helixi111 – 1133Combined sources
Helixi119 – 1224Combined sources
Helixi132 – 1343Combined sources
Beta strandi135 – 1373Combined sources
Beta strandi149 – 1557Combined sources
Helixi158 – 1603Combined sources
Beta strandi164 – 1696Combined sources
Helixi173 – 1753Combined sources
Helixi176 – 18510Combined sources
Beta strandi190 – 1945Combined sources
Beta strandi199 – 2013Combined sources
Beta strandi210 – 2156Combined sources
Beta strandi218 – 22710Combined sources
Beta strandi229 – 24012Combined sources
Beta strandi243 – 25210Combined sources
Helixi264 – 27512Combined sources
Beta strandi281 – 2833Combined sources
Beta strandi287 – 2959Combined sources
Helixi296 – 31419Combined sources
Beta strandi315 – 3173Combined sources
Helixi319 – 32911Combined sources
Helixi337 – 35317Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZC0X-ray1.85A65-360[»]
2A3KX-ray2.55A65-358[»]
2GP0X-ray2.05A65-360[»]
2GPHX-ray1.90B37-52[»]
2HVLX-ray2.40A65-360[»]
2QDCX-ray2.00A65-360[»]
2QDMX-ray2.05A65-360[»]
2QDPX-ray2.72A65-360[»]
3D42X-ray2.46A65-360[»]
3D44X-ray1.90A65-360[»]
3O4SX-ray1.90A65-360[»]
3O4TX-ray2.60A65-360[»]
3O4UX-ray2.25A65-360[»]
ProteinModelPortaliP35236.
SMRiP35236. Positions 65-357.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP35236.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini97 – 350254Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 5114Interaction with MAP kinasesAdd
BLAST
Regioni291 – 2977Substrate binding

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000294188.
HOVERGENiHBG001594.
InParanoidiP35236.
KOiK18019.
OrthoDBiEOG7288QX.
PhylomeDBiP35236.
TreeFamiTF331016.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR008356. Tyr_Pase_KIM-con.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR01778. KIMPTPASE.
PR00700. 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 (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P35236-1) [UniParc]FASTAAdd to Basket

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
MVQAHGGRSR AQPLTLSLGA AMTQPPPEKT PAKKHVRLQE RRGSNVALML
60 70 80 90 100
DVRSLGAVEP ICSVNTPREV TLHFLRTAGH PLTRWALQRQ PPSPKQLEEE
110 120 130 140 150
FLKIPSNFVS PEDLDIPGHA SKDRYKTILP NPQSRVCLGR AQSQEDGDYI
160 170 180 190 200
NANYIRGYDG KEKVYIATQG PMPNTVSDFW EMVWQEEVSL IVMLTQLREG
210 220 230 240 250
KEKCVHYWPT EEETYGPFQI RIQDMKECPE YTVRQLTIQY QEERRSVKHI
260 270 280 290 300
LFSAWPDHQT PESAGPLLRL VAEVEESPET AAHPGPIVVH CSAGIGRTGC
310 320 330 340 350
FIATRIGCQQ LKARGEVDIL GIVCQLRLDR GGMIQTAEQY QFLHHTLALY
360
AGQLPEEPSP
Length:360
Mass (Da):40,529
Last modified:January 23, 2002 - v3
Checksum:i388A154CC55AC0EE
GO
Isoform 2 (identifier: P35236-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGASFWPIRQAREQQRRALSFRQTSWLSEPPLGPAPHLSM

Show »
Length:399
Mass (Da):45,002
Checksum:i16690FDF358E20C8
GO
Isoform 3 (identifier: P35236-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MVGKAWPLTH...PLGPAPHLSM

Show »
Length:465
Mass (Da):52,284
Checksum:iAB2E025ECD392906
GO

Sequence cautioni

The sequence AAA59531.1 differs from that shown. Reason: Frameshift at position 5. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti235 – 2362QL → HV in AAA59531. (PubMed:1530918)Curated
Sequence conflicti337 – 3371A → D in BAA01946. (PubMed:1510684)Curated
Isoform 3 (identifier: P35236-3)
Sequence conflicti37 – 371Q → R in BAG54453. (PubMed:14702039)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MGASFWPIRQAREQQRRALS FRQTSWLSEPPLGPAPHLSM in isoform 2. 1 PublicationVSP_026925
Alternative sequencei1 – 11M → MVGKAWPLTHSQGTGPWAPE GHRREAADPWWQRQQAQEGR MQLGCAWVAARRGGGRKLAS WSLLSPQRQTDRQTDSWQEA AWGPQLLQQTSWLSEPPLGP APHLSM in isoform 3. 1 PublicationVSP_047275

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11327 mRNA. Translation: BAA01946.1.
M64322 mRNA. Translation: AAA59531.1. Frameshift.
BT009848 mRNA. Translation: AAP88850.1.
AK127214 mRNA. Translation: BAG54453.1.
AL592300 Genomic DNA. Translation: CAI13108.1.
BC001746 mRNA. Translation: AAH01746.2.
CCDSiCCDS1422.1. [P35236-2]
CCDS1423.2. [P35236-3]
PIRiJH0692.
RefSeqiNP_002823.3. NM_002832.3. [P35236-3]
NP_542155.1. NM_080588.2. [P35236-2]
UniGeneiHs.402773.

Genome annotation databases

EnsembliENST00000309017; ENSP00000309116; ENSG00000143851. [P35236-3]
ENST00000367279; ENSP00000356248; ENSG00000143851. [P35236-2]
ENST00000495688; ENSP00000420506; ENSG00000143851. [P35236-1]
GeneIDi5778.
KEGGihsa:5778.
UCSCiuc001gxl.2. human. [P35236-2]
uc001gxo.1. human. [P35236-1]

Polymorphism databases

DMDMi20141721.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D11327 mRNA. Translation: BAA01946.1 .
M64322 mRNA. Translation: AAA59531.1 . Frameshift.
BT009848 mRNA. Translation: AAP88850.1 .
AK127214 mRNA. Translation: BAG54453.1 .
AL592300 Genomic DNA. Translation: CAI13108.1 .
BC001746 mRNA. Translation: AAH01746.2 .
CCDSi CCDS1422.1. [P35236-2 ]
CCDS1423.2. [P35236-3 ]
PIRi JH0692.
RefSeqi NP_002823.3. NM_002832.3. [P35236-3 ]
NP_542155.1. NM_080588.2. [P35236-2 ]
UniGenei Hs.402773.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ZC0 X-ray 1.85 A 65-360 [» ]
2A3K X-ray 2.55 A 65-358 [» ]
2GP0 X-ray 2.05 A 65-360 [» ]
2GPH X-ray 1.90 B 37-52 [» ]
2HVL X-ray 2.40 A 65-360 [» ]
2QDC X-ray 2.00 A 65-360 [» ]
2QDM X-ray 2.05 A 65-360 [» ]
2QDP X-ray 2.72 A 65-360 [» ]
3D42 X-ray 2.46 A 65-360 [» ]
3D44 X-ray 1.90 A 65-360 [» ]
3O4S X-ray 1.90 A 65-360 [» ]
3O4T X-ray 2.60 A 65-360 [» ]
3O4U X-ray 2.25 A 65-360 [» ]
ProteinModelPortali P35236.
SMRi P35236. Positions 65-357.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111743. 4 interactions.
DIPi DIP-29118N.
IntActi P35236. 4 interactions.
MINTi MINT-8206881.
STRINGi 9606.ENSP00000356248.

Chemistry

BindingDBi P35236.
ChEMBLi CHEMBL2219.

PTM databases

PhosphoSitei P35236.

Polymorphism databases

DMDMi 20141721.

Proteomic databases

MaxQBi P35236.
PaxDbi P35236.
PRIDEi P35236.

Protocols and materials databases

DNASUi 5778.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000309017 ; ENSP00000309116 ; ENSG00000143851 . [P35236-3 ]
ENST00000367279 ; ENSP00000356248 ; ENSG00000143851 . [P35236-2 ]
ENST00000495688 ; ENSP00000420506 ; ENSG00000143851 . [P35236-1 ]
GeneIDi 5778.
KEGGi hsa:5778.
UCSCi uc001gxl.2. human. [P35236-2 ]
uc001gxo.1. human. [P35236-1 ]

Organism-specific databases

CTDi 5778.
GeneCardsi GC01M202116.
H-InvDB HIX0001472.
HGNCi HGNC:9659. PTPN7.
HPAi CAB009530.
HPA019118.
MIMi 176889. gene.
neXtProti NX_P35236.
PharmGKBi PA34003.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00770000120452.
HOGENOMi HOG000294188.
HOVERGENi HBG001594.
InParanoidi P35236.
KOi K18019.
OrthoDBi EOG7288QX.
PhylomeDBi P35236.
TreeFami TF331016.

Enzyme and pathway databases

BRENDAi 3.1.3.48. 2681.

Miscellaneous databases

ChiTaRSi PTPN7. human.
EvolutionaryTracei P35236.
GeneWikii PTPN7.
GenomeRNAii 5778.
NextBioi 22472.
PROi P35236.
SOURCEi Search...

Gene expression databases

Bgeei P35236.
CleanExi HS_PTPN7.
ExpressionAtlasi P35236. baseline and differential.
Genevestigatori P35236.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR008356. Tyr_Pase_KIM-con.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PRINTSi PR01778. KIMPTPASE.
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. "Molecular cloning and chromosomal mapping of a human protein-tyrosine phosphatase LC-PTP."
    Adachi M., Sekiya M., Isobe M., Kumura Y., Ogita Z.I., Hinoda Y., Imai K., Yachi A.
    Biochem. Biophys. Res. Commun. 186:1607-1615(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, FUNCTION.
  2. "Cloning and expression of an inducible lymphoid-specific, protein tyrosine phosphatase (HePTPase)."
    Zanke B., Suzuki H., Kishihara K., Mizzen L., Minden M., Pawson A., Mak T.W.
    Eur. J. Immunol. 22:235-239(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Lymphocyte.
  3. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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 3).
    Tissue: Hippocampus.
  5. "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], ALTERNATIVE SPLICING.
  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] (ISOFORM 2).
    Tissue: Lymph.
  7. "Negative regulation of T cell antigen receptor signal transduction by hematopoietic tyrosine phosphatase (HePTP)."
    Saxena M., Williams S., Gilman J., Mustelin T.
    J. Biol. Chem. 273:15340-15344(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAPK1, ACTIVE SITE, MUTAGENESIS OF CYS-291.
  8. "Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP)."
    Saxena M., Williams S., Brockdorff J., Gilman J., Mustelin T.
    J. Biol. Chem. 274:11693-11700(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAPK1 AND MAPK3, PHOSPHORYLATION AT THR-66 AND SER-93, MUTAGENESIS OF THR-66 AND SER-93.
  9. "Crosstalk between cAMP-dependent kinase and MAP kinase through a protein tyrosine phosphatase."
    Saxena M., Williams S., Tasken K., Mustelin T.
    Nat. Cell Biol. 1:305-311(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAPK1, PHOSPHORYLATION AT SER-44.
  10. "The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP."
    Pettiford S.M., Herbst R.
    Oncogene 19:858-869(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MAPK1 AND MAPK3.
  11. "Haematopoietic protein tyrosine phosphatase (HePTP) phosphorylation by cAMP-dependent protein kinase in T-cells: dynamics and subcellular location."
    Nika K., Hyunh H., Williams S., Paul S., Bottini N., Tasken K., Lombroso P.J., Mustelin T.
    Biochem. J. 378:335-342(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-44, MUTAGENESIS OF SER-44.
  12. "Molecular determinants of substrate recognition in hematopoietic protein-tyrosine phosphatase."
    Huang Z., Zhou B., Zhang Z.-Y.
    J. Biol. Chem. 279:52150-52159(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-125; ASP-257 AND GLN-335.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-66, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Platelet.
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-44 AND SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Structure of the hematopoietic tyrosine phosphatase (HePTP) catalytic domain: structure of a KIM phosphatase with phosphate bound at the active site."
    Mustelin T., Tautz L., Page R.
    J. Mol. Biol. 354:150-163(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 65-360 OF MUTANT ASP-246 IN COMPLEX WITH SUBSTRATE ANALOG.
  16. "Crystal structures and inhibitor identification for PTPN5, PTPRR and PTPN7: a family of human MAPK-specific protein tyrosine phosphatases."
    Eswaran J., von Kries J.P., Marsden B., Longman E., Debreczeni J.E., Ugochukwu E., Turnbull A., Lee W.H., Knapp S., Barr A.J.
    Biochem. J. 395:483-491(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 65-358 IN COMPLEX WITH SUBSTRATE ANALOG, SUBUNIT.
  17. "Docking interactions induce exposure of activation loop in the MAP kinase ERK2."
    Zhou T., Sun L., Humphreys J., Goldsmith E.J.
    Structure 14:1011-1019(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 37-52 IN COMPLEX WITH MAPK1.

Entry informationi

Entry nameiPTN7_HUMAN
AccessioniPrimary (citable) accession number: P35236
Secondary accession number(s): B3KXE1
, Q53XK4, Q5SXQ0, Q5SXQ1, Q9BV05
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2002
Last modified: November 26, 2014
This is version 147 of the entry and version 3 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. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3