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P18031

- PTN1_HUMAN

UniProt

P18031 - PTN1_HUMAN

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Protein

Tyrosine-protein phosphatase non-receptor type 1

Gene
PTPN1, PTP1B
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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. May also regulate the hepatocyte growth factor receptor signaling pathway through dephosphorylation of MET.3 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei181 – 1811Substrate
Active sitei215 – 2151Phosphocysteine intermediate
Binding sitei262 – 2621Substrate By similarity

GO - Molecular functioni

  1. enzyme binding Source: UniProtKB
  2. ephrin receptor binding Source: UniProtKB
  3. poly(A) RNA binding Source: UniProtKB
  4. protein binding Source: IntAct
  5. protein kinase binding Source: UniProtKB
  6. protein tyrosine phosphatase activity Source: UniProtKB
  7. receptor tyrosine kinase binding Source: UniProtKB
  8. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. actin cytoskeleton reorganization Source: UniProtKB
  2. blood coagulation Source: Reactome
  3. cytokine-mediated signaling pathway Source: Reactome
  4. endoplasmic reticulum unfolded protein response Source: UniProtKB
  5. insulin receptor signaling pathway Source: Ensembl
  6. interferon-gamma-mediated signaling pathway Source: Reactome
  7. JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  8. negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  9. negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  10. negative regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  11. peptidyl-tyrosine dephosphorylation Source: UniProtKB
  12. peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: BHF-UCL
  13. platelet activation Source: Reactome
  14. platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  15. regulation of endocytosis Source: UniProtKB
  16. regulation of hepatocyte growth factor receptor signaling pathway Source: UniProtKB
  17. regulation of interferon-gamma-mediated signaling pathway Source: Reactome
  18. regulation of signal transduction Source: UniProtKB
  19. regulation of type I interferon-mediated signaling pathway Source: Reactome
  20. type I interferon signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
ReactomeiREACT_111133. Growth hormone receptor signaling.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_24980. Regulation of IFNG signaling.
REACT_25216. Regulation of IFNA signaling.
SABIO-RKP18031.
SignaLinkiP18031.

Names & Taxonomyi

Protein namesi
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 namesi
Name:PTPN1
Synonyms:PTP1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:9642. PTPN1.

Subcellular locationi

Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side
Note: Interacts with EPHA3 at the cell membrane.2 Publications

GO - Cellular componenti

  1. cytoplasmic vesicle Source: Ensembl
  2. cytosol Source: Reactome
  3. early endosome Source: UniProtKB
  4. endoplasmic reticulum Source: HPA
  5. endoplasmic reticulum membrane Source: UniProtKB-SubCell
  6. sorting endosome Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi50 – 501S → A or D: No phosphorylation. 2 Publications
Mutagenesisi181 – 1811D → A: Substrate-trapping mutant. 1 Publication
Mutagenesisi215 – 2151C → S: Catalytically inactive mutant; abolishes sulfhydration. 1 Publication

Organism-specific databases

PharmGKBiPA33985.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 435435Tyrosine-protein phosphatase non-receptor type 1PRO_0000094748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei20 – 201Phosphotyrosine1 Publication
Modified residuei50 – 501Phosphoserine; by PKB/AKT1, CLK1 and CLK22 Publications
Modified residuei66 – 661Phosphotyrosine; by EGFR1 Publication
Cross-linki215 ↔ 216N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form
Modified residuei215 – 2151Cysteine persulfide1 Publication
Modified residuei215 – 2151S-nitrosocysteine; in reversibly inhibited form1 Publication
Modified residuei242 – 2421Phosphoserine; by CLK1 and CLK21 Publication
Modified residuei243 – 2431Phosphoserine; by CLK1 and CLK21 Publication
Modified residuei352 – 3521Phosphoserine3 Publications
Modified residuei378 – 3781Phosphoserine; by PKC2 Publications
Modified residuei386 – 3861Phosphoserine; by CDK11 Publication

Post-translational modificationi

Oxidized on Cys-215; the Cys-SOH formed in response to redox signaling reacts with the alpha-amido of the following residue to form a sulfenamide cross-link, triggering a conformational change that inhibits substrate binding and activity. The active site can be restored by reduction.
Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50.
S-nitrosylation of Cys-215 inactivates the enzyme activity.
Sulfhydration at Cys-215 following endoplasmic reticulum stress inactivates the enzyme activity, promoting EIF2AK3/PERK activity.

Keywords - PTMi

Acetylation, Oxidation, Phosphoprotein, S-nitrosylation

Proteomic databases

MaxQBiP18031.
PaxDbiP18031.
PeptideAtlasiP18031.
PRIDEiP18031.

2D gel databases

OGPiP18031.

PTM databases

PhosphoSiteiP18031.

Miscellaneous databases

PMAP-CutDBP18031.

Expressioni

Gene expression databases

ArrayExpressiP18031.
BgeeiP18031.
CleanExiHS_PTPN1.
GenevestigatoriP18031.

Organism-specific databases

HPAiCAB009329.
CAB015217.
HPA012542.

Interactioni

Subunit structurei

Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3 and may regulate its trafficking and function. Interacts with MET.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BCAR1P569455EBI-968788,EBI-702093
Bcar1Q611405EBI-968788,EBI-77088From a different organism.
Bcar1Q637675EBI-968788,EBI-1176801From a different organism.
BCRP11274-13EBI-968788,EBI-8658094
CAPN1P073844EBI-968788,EBI-1542113
CAV1Q031355EBI-968788,EBI-603614
Cdh2P151163EBI-968788,EBI-397974From a different organism.
CrkQ637682EBI-968788,EBI-8423843From a different organism.
CTTNQ142472EBI-968788,EBI-351886
EGFRP005334EBI-968788,EBI-297353
EPORP192353EBI-968788,EBI-617321
GHRP109125EBI-968788,EBI-286316
GRB2P629932EBI-968788,EBI-401755
Grb2P629943EBI-968788,EBI-401775From a different organism.
IGF1RP080693EBI-968788,EBI-475981
INSRP0621333EBI-968788,EBI-475899
Irs1P355703EBI-968788,EBI-520230From a different organism.
ITGB1P055562EBI-968788,EBI-703066
ITGB3P051064EBI-968788,EBI-702847
JAK2O606745EBI-968788,EBI-518647
LATO435613EBI-968788,EBI-1222766
METP085813EBI-968788,EBI-1039152
NTRK1P046292EBI-968788,EBI-1028226
PDGFRBP096193EBI-968788,EBI-641237
PdgfrbP056223EBI-968788,EBI-1554855From a different organism.
Plcg1P106864EBI-968788,EBI-520788From a different organism.
Ptk2P341522EBI-968788,EBI-77070From a different organism.
PxnQ8VI362EBI-968788,EBI-983394From a different organism.
ROS1P089223EBI-968788,EBI-7371065
SRCP1293114EBI-968788,EBI-621482
STAT3P407632EBI-968788,EBI-518675
STAT5AP422292EBI-968788,EBI-749537
Sumo1P631662EBI-968788,EBI-80152From a different organism.
TRPV6Q9H1D06EBI-968788,EBI-7198335

Protein-protein interaction databases

BioGridi111736. 37 interactions.
DIPiDIP-38014N.
IntActiP18031. 78 interactions.
MINTiMINT-441655.
STRINGi9606.ENSP00000360683.

Structurei

Secondary structure

1
435
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 1311
Helixi16 – 2611
Turni33 – 364
Helixi38 – 436
Beta strandi45 – 484
Turni53 – 553
Beta strandi56 – 583
Beta strandi61 – 633
Beta strandi66 – 749
Turni75 – 784
Beta strandi79 – 846
Turni89 – 913
Helixi92 – 10211
Beta strandi106 – 1094
Beta strandi113 – 1153
Beta strandi118 – 1214
Beta strandi128 – 1303
Beta strandi133 – 1353
Turni136 – 1394
Beta strandi140 – 14910
Beta strandi151 – 16212
Turni163 – 1653
Beta strandi168 – 1769
Beta strandi181 – 1833
Beta strandi186 – 1883
Helixi189 – 20012
Turni201 – 2044
Beta strandi211 – 22010
Helixi221 – 23717
Beta strandi238 – 2403
Helixi241 – 2433
Helixi246 – 2538
Turni254 – 2563
Helixi264 – 28118
Turni282 – 2843
Helixi287 – 2959
Turni296 – 2983

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1A5YX-ray2.50A1-330[»]
1AAXX-ray1.90A1-321[»]
1BZCX-ray2.35A1-321[»]
1BZHX-ray2.10A1-298[»]
1BZJX-ray2.25A2-298[»]
1C83X-ray1.80A1-298[»]
1C84X-ray2.35A1-298[»]
1C85X-ray2.72A1-298[»]
1C86X-ray2.30A1-298[»]
1C87X-ray2.10A1-298[»]
1C88X-ray1.80A1-298[»]
1ECVX-ray1.95A1-298[»]
1EENX-ray1.90A1-321[»]
1EEOX-ray1.80A1-321[»]
1G1FX-ray2.00A1-298[»]
1G1GX-ray2.20A1-298[»]
1G1HX-ray2.40A1-298[»]
1G7FX-ray1.80A1-298[»]
1G7GX-ray2.20A1-298[»]
1GFYX-ray2.13A1-298[»]
1I57X-ray2.10A1-298[»]
1JF7X-ray2.20A/B1-298[»]
1KAKX-ray2.50A1-298[»]
1KAVX-ray2.35A1-298[»]
1L8GX-ray2.50A1-321[»]
1LQFX-ray2.50A/B/C/D1-283[»]
1NL9X-ray2.40A1-321[»]
1NNYX-ray2.40A1-321[»]
1NO6X-ray2.40A1-321[»]
1NWEX-ray3.10A1-298[»]
1NWLX-ray2.40A1-298[»]
1NZ7X-ray2.40A1-321[»]
1OEMX-ray1.80X1-321[»]
1OEOX-ray2.15X1-321[»]
1OESX-ray2.20A1-321[»]
1OETX-ray2.30A1-321[»]
1OEUX-ray2.50A1-321[»]
1OEVX-ray2.20A1-321[»]
1ONYX-ray2.15A1-321[»]
1ONZX-ray2.40A1-321[»]
1PA1X-ray1.60A1-298[»]
1PH0X-ray2.20A1-321[»]
1PTTX-ray2.90A1-321[»]
1PTUX-ray2.60A1-321[»]
1PTVX-ray2.30A1-321[»]
1PTYX-ray1.85A1-321[»]
1PXHX-ray2.15A1-321[»]
1PYNX-ray2.20A1-321[»]
1Q1MX-ray2.60A1-321[»]
1Q6JX-ray2.20A1-298[»]
1Q6MX-ray2.20A1-298[»]
1Q6NX-ray2.10A/B1-298[»]
1Q6PX-ray2.30A/B1-298[»]
1Q6SX-ray2.20A/B1-298[»]
1Q6TX-ray2.30A/B1-298[»]
1QXKX-ray2.30A1-321[»]
1SUGX-ray1.95A1-321[»]
1T48X-ray2.20A1-298[»]
1T49X-ray1.90A1-298[»]
1T4JX-ray2.70A1-298[»]
1WAXX-ray2.20A1-321[»]
1XBOX-ray2.50A1-321[»]
2AZRX-ray2.00A1-299[»]
2B07X-ray2.10A1-299[»]
2B4SX-ray2.30A/C1-298[»]
2BGDX-ray2.40A1-321[»]
2BGEX-ray1.80A1-321[»]
2CM2X-ray1.50A2-298[»]
2CM3X-ray2.10A/B1-298[»]
2CM7X-ray2.10A1-321[»]
2CM8X-ray2.10A1-321[»]
2CMAX-ray2.30A1-321[»]
2CMBX-ray1.70A1-298[»]
2CMCX-ray2.20A1-298[»]
2CNEX-ray1.80A1-298[»]
2CNFX-ray2.20A1-321[»]
2CNGX-ray1.90A1-321[»]
2CNHX-ray1.80A1-321[»]
2CNIX-ray2.00A1-321[»]
2F6FX-ray2.00A1-298[»]
2F6TX-ray1.70A1-298[»]
2F6VX-ray1.70A1-298[»]
2F6WX-ray2.20A1-298[»]
2F6YX-ray2.15A1-298[»]
2F6ZX-ray1.70A1-298[»]
2F70X-ray2.12A1-298[»]
2F71X-ray1.55A1-298[»]
2FJMX-ray2.10A/B1-298[»]
2FJNX-ray2.20A/B1-298[»]
2H4GX-ray2.50A1-299[»]
2H4KX-ray2.30A1-299[»]
2HB1X-ray2.00A1-299[»]
2HNPX-ray2.85A1-321[»]
2HNQX-ray2.85A1-321[»]
2NT7X-ray2.10A1-299[»]
2NTAX-ray2.10A1-299[»]
2QBPX-ray2.50A1-299[»]
2QBQX-ray2.10A1-299[»]
2QBRX-ray2.30A1-299[»]
2QBSX-ray2.10A1-299[»]
2VEUX-ray2.40A1-321[»]
2VEVX-ray1.80A1-321[»]
2VEWX-ray2.00A1-321[»]
2VEXX-ray2.20A1-321[»]
2VEYX-ray2.20A1-321[»]
2ZMMX-ray2.10A1-299[»]
2ZN7X-ray2.10A1-299[»]
3A5JX-ray1.70A2-321[»]
3A5KX-ray1.85A2-298[»]
3CWEX-ray1.60A1-283[»]
3D9CX-ray2.30A1-321[»]
3EAXX-ray1.90A1-321[»]
3EB1X-ray2.40A1-321[»]
3EU0X-ray2.70A1-282[»]
3I7ZX-ray2.30A1-321[»]
3I80X-ray2.25A1-321[»]
3QKPX-ray2.05A1-321[»]
3QKQX-ray2.20A1-321[»]
3SMEX-ray1.70A1-298[»]
3ZMPX-ray2.62A/B1-321[»]
3ZMQX-ray3.30A1-321[»]
3ZV2X-ray2.80A1-320[»]
4BJOX-ray2.06A/B2-321[»]
4I8NX-ray2.50A1-320[»]
ProteinModelPortaliP18031.
SMRiP18031. Positions 2-417.

Miscellaneous databases

EvolutionaryTraceiP18031.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 277275Tyrosine-protein phosphataseAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni215 – 2217Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5599.
HOGENOMiHOG000273908.
HOVERGENiHBG008321.
InParanoidiP18031.
KOiK05696.
OMAiMCMATVL.
OrthoDBiEOG7RV9G4.
PhylomeDBiP18031.
TreeFamiTF315897.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR012265. Ptpn1/Ptpn2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000926. Tyr-Ptase_nr1. 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]

Sequencei

Sequence statusi: Complete.

P18031-1 [UniParc]FASTAAdd to Basket

« Hide

MEMEKEFEQI DKSGSWAAIY QDIRHEASDF PCRVAKLPKN KNRNRYRDVS    50
PFDHSRIKLH QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW 100
EQKSRGVVML NRVMEKGSLK CAQYWPQKEE KEMIFEDTNL KLTLISEDIK 150
SYYTVRQLEL ENLTTQETRE ILHFHYTTWP DFGVPESPAS FLNFLFKVRE 200
SGSLSPEHGP VVVHCSAGIG RSGTFCLADT CLLLMDKRKD PSSVDIKKVL 250
LEMRKFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE 300
PPPEHIPPPP RPPKRILEPH NGKCREFFPN HQWVKEETQE DKDCPIKEEK 350
GSPLNAAPYG IESMSQDTEV RSRVVGGSLR GAQAASPAKG EPSLPEKDED 400
HALSYWKPFL VNMCVATVLT AGAYLCYRFL FNSNT 435
Length:435
Mass (Da):49,967
Last modified:November 1, 1990 - v1
Checksum:i802377DCD33F41FD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti381 – 3811G → S.
Corresponds to variant rs16995304 [ dbSNP | Ensembl ].
VAR_022013
Natural varianti387 – 3871P → L Associated with low glucose tolerance. 1 Publication
Corresponds to variant rs16995309 [ dbSNP | Ensembl ].
VAR_022014

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31724 mRNA. Translation: AAA60223.1.
M33689 mRNA. Translation: AAA60157.1.
M33684
, M33688, M33687, M33686, M33685 Genomic DNA. Translation: AAA60158.1.
BT006752 mRNA. Translation: AAP35398.1.
AL133230, AL034429 Genomic DNA. Translation: CAC00618.2.
AL034429, AL133230 Genomic DNA. Translation: CAI23215.1.
BC015660 mRNA. Translation: AAH15660.1.
BC018164 mRNA. Translation: AAH18164.1.
CCDSiCCDS13430.1.
PIRiA35992. TPHUN1.
RefSeqiNP_001265547.1. NM_001278618.1.
NP_002818.1. NM_002827.3.
UniGeneiHs.417549.

Genome annotation databases

EnsembliENST00000371621; ENSP00000360683; ENSG00000196396.
GeneIDi5770.
KEGGihsa:5770.
UCSCiuc002xvl.3. human.

Polymorphism databases

DMDMi131467.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
M31724 mRNA. Translation: AAA60223.1 .
M33689 mRNA. Translation: AAA60157.1 .
M33684
, M33688 , M33687 , M33686 , M33685 Genomic DNA. Translation: AAA60158.1 .
BT006752 mRNA. Translation: AAP35398.1 .
AL133230 , AL034429 Genomic DNA. Translation: CAC00618.2 .
AL034429 , AL133230 Genomic DNA. Translation: CAI23215.1 .
BC015660 mRNA. Translation: AAH15660.1 .
BC018164 mRNA. Translation: AAH18164.1 .
CCDSi CCDS13430.1.
PIRi A35992. TPHUN1.
RefSeqi NP_001265547.1. NM_001278618.1.
NP_002818.1. NM_002827.3.
UniGenei Hs.417549.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A5Y X-ray 2.50 A 1-330 [» ]
1AAX X-ray 1.90 A 1-321 [» ]
1BZC X-ray 2.35 A 1-321 [» ]
1BZH X-ray 2.10 A 1-298 [» ]
1BZJ X-ray 2.25 A 2-298 [» ]
1C83 X-ray 1.80 A 1-298 [» ]
1C84 X-ray 2.35 A 1-298 [» ]
1C85 X-ray 2.72 A 1-298 [» ]
1C86 X-ray 2.30 A 1-298 [» ]
1C87 X-ray 2.10 A 1-298 [» ]
1C88 X-ray 1.80 A 1-298 [» ]
1ECV X-ray 1.95 A 1-298 [» ]
1EEN X-ray 1.90 A 1-321 [» ]
1EEO X-ray 1.80 A 1-321 [» ]
1G1F X-ray 2.00 A 1-298 [» ]
1G1G X-ray 2.20 A 1-298 [» ]
1G1H X-ray 2.40 A 1-298 [» ]
1G7F X-ray 1.80 A 1-298 [» ]
1G7G X-ray 2.20 A 1-298 [» ]
1GFY X-ray 2.13 A 1-298 [» ]
1I57 X-ray 2.10 A 1-298 [» ]
1JF7 X-ray 2.20 A/B 1-298 [» ]
1KAK X-ray 2.50 A 1-298 [» ]
1KAV X-ray 2.35 A 1-298 [» ]
1L8G X-ray 2.50 A 1-321 [» ]
1LQF X-ray 2.50 A/B/C/D 1-283 [» ]
1NL9 X-ray 2.40 A 1-321 [» ]
1NNY X-ray 2.40 A 1-321 [» ]
1NO6 X-ray 2.40 A 1-321 [» ]
1NWE X-ray 3.10 A 1-298 [» ]
1NWL X-ray 2.40 A 1-298 [» ]
1NZ7 X-ray 2.40 A 1-321 [» ]
1OEM X-ray 1.80 X 1-321 [» ]
1OEO X-ray 2.15 X 1-321 [» ]
1OES X-ray 2.20 A 1-321 [» ]
1OET X-ray 2.30 A 1-321 [» ]
1OEU X-ray 2.50 A 1-321 [» ]
1OEV X-ray 2.20 A 1-321 [» ]
1ONY X-ray 2.15 A 1-321 [» ]
1ONZ X-ray 2.40 A 1-321 [» ]
1PA1 X-ray 1.60 A 1-298 [» ]
1PH0 X-ray 2.20 A 1-321 [» ]
1PTT X-ray 2.90 A 1-321 [» ]
1PTU X-ray 2.60 A 1-321 [» ]
1PTV X-ray 2.30 A 1-321 [» ]
1PTY X-ray 1.85 A 1-321 [» ]
1PXH X-ray 2.15 A 1-321 [» ]
1PYN X-ray 2.20 A 1-321 [» ]
1Q1M X-ray 2.60 A 1-321 [» ]
1Q6J X-ray 2.20 A 1-298 [» ]
1Q6M X-ray 2.20 A 1-298 [» ]
1Q6N X-ray 2.10 A/B 1-298 [» ]
1Q6P X-ray 2.30 A/B 1-298 [» ]
1Q6S X-ray 2.20 A/B 1-298 [» ]
1Q6T X-ray 2.30 A/B 1-298 [» ]
1QXK X-ray 2.30 A 1-321 [» ]
1SUG X-ray 1.95 A 1-321 [» ]
1T48 X-ray 2.20 A 1-298 [» ]
1T49 X-ray 1.90 A 1-298 [» ]
1T4J X-ray 2.70 A 1-298 [» ]
1WAX X-ray 2.20 A 1-321 [» ]
1XBO X-ray 2.50 A 1-321 [» ]
2AZR X-ray 2.00 A 1-299 [» ]
2B07 X-ray 2.10 A 1-299 [» ]
2B4S X-ray 2.30 A/C 1-298 [» ]
2BGD X-ray 2.40 A 1-321 [» ]
2BGE X-ray 1.80 A 1-321 [» ]
2CM2 X-ray 1.50 A 2-298 [» ]
2CM3 X-ray 2.10 A/B 1-298 [» ]
2CM7 X-ray 2.10 A 1-321 [» ]
2CM8 X-ray 2.10 A 1-321 [» ]
2CMA X-ray 2.30 A 1-321 [» ]
2CMB X-ray 1.70 A 1-298 [» ]
2CMC X-ray 2.20 A 1-298 [» ]
2CNE X-ray 1.80 A 1-298 [» ]
2CNF X-ray 2.20 A 1-321 [» ]
2CNG X-ray 1.90 A 1-321 [» ]
2CNH X-ray 1.80 A 1-321 [» ]
2CNI X-ray 2.00 A 1-321 [» ]
2F6F X-ray 2.00 A 1-298 [» ]
2F6T X-ray 1.70 A 1-298 [» ]
2F6V X-ray 1.70 A 1-298 [» ]
2F6W X-ray 2.20 A 1-298 [» ]
2F6Y X-ray 2.15 A 1-298 [» ]
2F6Z X-ray 1.70 A 1-298 [» ]
2F70 X-ray 2.12 A 1-298 [» ]
2F71 X-ray 1.55 A 1-298 [» ]
2FJM X-ray 2.10 A/B 1-298 [» ]
2FJN X-ray 2.20 A/B 1-298 [» ]
2H4G X-ray 2.50 A 1-299 [» ]
2H4K X-ray 2.30 A 1-299 [» ]
2HB1 X-ray 2.00 A 1-299 [» ]
2HNP X-ray 2.85 A 1-321 [» ]
2HNQ X-ray 2.85 A 1-321 [» ]
2NT7 X-ray 2.10 A 1-299 [» ]
2NTA X-ray 2.10 A 1-299 [» ]
2QBP X-ray 2.50 A 1-299 [» ]
2QBQ X-ray 2.10 A 1-299 [» ]
2QBR X-ray 2.30 A 1-299 [» ]
2QBS X-ray 2.10 A 1-299 [» ]
2VEU X-ray 2.40 A 1-321 [» ]
2VEV X-ray 1.80 A 1-321 [» ]
2VEW X-ray 2.00 A 1-321 [» ]
2VEX X-ray 2.20 A 1-321 [» ]
2VEY X-ray 2.20 A 1-321 [» ]
2ZMM X-ray 2.10 A 1-299 [» ]
2ZN7 X-ray 2.10 A 1-299 [» ]
3A5J X-ray 1.70 A 2-321 [» ]
3A5K X-ray 1.85 A 2-298 [» ]
3CWE X-ray 1.60 A 1-283 [» ]
3D9C X-ray 2.30 A 1-321 [» ]
3EAX X-ray 1.90 A 1-321 [» ]
3EB1 X-ray 2.40 A 1-321 [» ]
3EU0 X-ray 2.70 A 1-282 [» ]
3I7Z X-ray 2.30 A 1-321 [» ]
3I80 X-ray 2.25 A 1-321 [» ]
3QKP X-ray 2.05 A 1-321 [» ]
3QKQ X-ray 2.20 A 1-321 [» ]
3SME X-ray 1.70 A 1-298 [» ]
3ZMP X-ray 2.62 A/B 1-321 [» ]
3ZMQ X-ray 3.30 A 1-321 [» ]
3ZV2 X-ray 2.80 A 1-320 [» ]
4BJO X-ray 2.06 A/B 2-321 [» ]
4I8N X-ray 2.50 A 1-320 [» ]
ProteinModelPortali P18031.
SMRi P18031. Positions 2-417.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111736. 37 interactions.
DIPi DIP-38014N.
IntActi P18031. 78 interactions.
MINTi MINT-441655.
STRINGi 9606.ENSP00000360683.

Chemistry

BindingDBi P18031.
ChEMBLi CHEMBL335.
DrugBanki DB00720. Clodronate.
DB01133. Tiludronate.

PTM databases

PhosphoSitei P18031.

Polymorphism databases

DMDMi 131467.

2D gel databases

OGPi P18031.

Proteomic databases

MaxQBi P18031.
PaxDbi P18031.
PeptideAtlasi P18031.
PRIDEi P18031.

Protocols and materials databases

DNASUi 5770.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000371621 ; ENSP00000360683 ; ENSG00000196396 .
GeneIDi 5770.
KEGGi hsa:5770.
UCSCi uc002xvl.3. human.

Organism-specific databases

CTDi 5770.
GeneCardsi GC20P049126.
H-InvDB HIX0027718.
HGNCi HGNC:9642. PTPN1.
HPAi CAB009329.
CAB015217.
HPA012542.
MIMi 176885. gene.
neXtProti NX_P18031.
PharmGKBi PA33985.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
HOGENOMi HOG000273908.
HOVERGENi HBG008321.
InParanoidi P18031.
KOi K05696.
OMAi MCMATVL.
OrthoDBi EOG7RV9G4.
PhylomeDBi P18031.
TreeFami TF315897.

Enzyme and pathway databases

BRENDAi 3.1.3.48. 2681.
Reactomei REACT_111133. Growth hormone receptor signaling.
REACT_15523. Integrin alphaIIb beta3 signaling.
REACT_24980. Regulation of IFNG signaling.
REACT_25216. Regulation of IFNA signaling.
SABIO-RK P18031.
SignaLinki P18031.

Miscellaneous databases

ChiTaRSi PTPN1. human.
EvolutionaryTracei P18031.
GeneWikii PTPN1.
GenomeRNAii 5770.
NextBioi 22442.
PMAP-CutDB P18031.
PROi P18031.
SOURCEi Search...

Gene expression databases

ArrayExpressi P18031.
Bgeei P18031.
CleanExi HS_PTPN1.
Genevestigatori P18031.

Family and domain databases

Gene3Di 3.90.190.10. 1 hit.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR012265. Ptpn1/Ptpn2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PIRSFi PIRSF000926. Tyr-Ptase_nr1. 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  2. "Molecular cloning and chromosome mapping of the human gene encoding protein phosphotyrosyl phosphatase 1B."
    Brown-Shimer S., Johnson K.A., Lawrence J.B., Johnson C., Bruskin A., Green N.R., Hill D.E.
    Proc. Natl. Acad. Sci. U.S.A. 87:5148-5152(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Tissue: Placenta.
  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 (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Eye and Lymph.
  6. "Human placenta protein-tyrosine-phosphatase: amino acid sequence and relationship to a family of receptor-like proteins."
    Charbonneau H., Tonks N.K., Kumar S., Diltz C.D., Harrylock M., Cool D.E., Krebs E.G., Fischer E.H., Walsh K.A.
    Proc. Natl. Acad. Sci. U.S.A. 86:5252-5256(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-321, ACETYLATION AT MET-1.
    Tissue: Placenta.
  7. "Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation."
    Flint A.J., Gebbink M.F.G.B., Franza B.R. Jr., Hill D.E., Tonks N.K.
    EMBO J. 12:1937-1946(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-352; SER-378 AND SER-386.
  8. "The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence."
    Frangioni J.V., Beahm P.H., Shifrin V., Jost C.A., Neel B.G.
    Cell 68:545-560(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  9. "Protein tyrosine phosphatase 1B interacts with and is tyrosine phosphorylated by the epidermal growth factor receptor."
    Liu F., Chernoff J.
    Biochem. J. 327:139-145(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT TYR-66.
  10. "The CLK family kinases, CLK1 and CLK2, phosphorylate and activate the tyrosine phosphatase, PTP-1B."
    Moeslein F.M., Myers M.P., Landreth G.E.
    J. Biol. Chem. 274:26697-26704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-50; SER-242 AND SER-243, MUTAGENESIS OF SER-50.
  11. "Phosphorylation of PTP1B at Ser(50) by Akt impairs its ability to dephosphorylate the insulin receptor."
    Ravichandran L.V., Chen H., Li Y., Quon M.J.
    Mol. Endocrinol. 15:1768-1780(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-50, MUTAGENESIS OF SER-50.
  12. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-20, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Regulation of the Met receptor-tyrosine kinase by the protein-tyrosine phosphatase 1B and T-cell phosphatase."
    Sangwan V., Paliouras G.N., Abella J.V., Dube N., Monast A., Tremblay M.L., Park M.
    J. Biol. Chem. 283:34374-34383(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEPHOSPHORYLATION OF MET, INTERACTION WITH MET.
  14. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: INTERACTION WITH EPHA3, FUNCTION IN EPHA3 DEPHOSPHORYLATION, SUBCELLULAR LOCATION.
  16. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-352, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "H2s-induced sulfhydration of the phosphatase PTP1B and its role in the endoplasmic reticulum stress response."
    Krishnan N., Fu C., Pappin D.J., Tonks N.K.
    Sci. Signal. 4:RA86-RA86(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SULFHYDRATION AT CYS-215, S-NITROSYLATION AT CYS-215, MUTAGENESIS OF CYS-215, MUTAGENESIS OF ASP-181 AND CYS-215.
  19. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. "Crystal structure of human protein tyrosine phosphatase 1B."
    Barford D., Flint A.J., Tonks N.K.
    Science 263:1397-1404(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-321.
  21. "Identification of a second aryl phosphate-binding site in protein-tyrosine phosphatase 1B: a paradigm for inhibitor design."
    Puius Y.A., Zhao Y., Sullivan M., Lawrence D.S., Almo S.C., Zhang Z.Y.
    Proc. Natl. Acad. Sci. U.S.A. 94:13420-13425(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 1-298 OF MUTANT SER-215.
  22. "Visualization of the cysteinyl-phosphate intermediate of a protein-tyrosine phosphatase by X-ray crystallography."
    Pannifer A.D., Flint A.J., Tonks N.K., Barford D.
    J. Biol. Chem. 273:10454-10462(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-285.
  23. "Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics."
    Groves M.R., Yao Z.-J., Roller P.P., Burke T.R. Jr., Barford D.
    Biochemistry 37:17773-17783(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 1-298.
  24. "Redox regulation of protein tyrosine phosphatase 1B involves a sulphenyl-amide intermediate."
    Salmeen A., Andersen J.N., Myers M.P., Meng T.-C., Hinks J.A., Tonks N.K., Barford D.
    Nature 423:769-773(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, CROSS-LINK 215-CYS-SER-216.
  25. "Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B."
    Van Montfort R.L.M., Congreve M., Tisi D., Carr R., Jhoti H.
    Nature 423:773-777(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-321, OXIDATION AT CYS-215, CROSS-LINK 215-CYS-SER-216.
  26. "Protein tyrosine phosphatase 1B variant associated with fat distribution and insulin metabolism."
    Ukkola O., Rankinen T., Lakka T., Leon A.S., Skinner J.S., Wilmore J.H., Rao D.C., Kesaeniemi Y.A., Bouchard C.
    Obes. Res. 13:829-834(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ASSOCIATION OF VARIANT LEU-387 WITH LOW GLUCOSE TOLERANCE.

Entry informationi

Entry nameiPTN1_HUMAN
AccessioniPrimary (citable) accession number: P18031
Secondary accession number(s): Q5TGD8, Q9BQV9, Q9NQQ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: September 3, 2014
This is version 184 of the entry and version 1 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: 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

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