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Protein

Tyrosine-protein phosphatase non-receptor type 1

Gene

PTPN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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.PROSITE-ProRule annotation

Sites

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

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • ephrin receptor binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • protein tyrosine phosphatase activity Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB
  • zinc ion binding Source: UniProtKB

GO - Biological processi

  • actin cytoskeleton reorganization Source: UniProtKB
  • activation of JUN kinase activity Source: Ensembl
  • activation of signaling protein activity involved in unfolded protein response Source: ParkinsonsUK-UCL
  • endoplasmic reticulum unfolded protein response Source: UniProtKB
  • insulin receptor signaling pathway Source: Ensembl
  • IRE1-mediated unfolded protein response Source: Ensembl
  • JAK-STAT cascade involved in growth hormone signaling pathway Source: Reactome
  • negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway Source: Ensembl
  • negative regulation of ERK1 and ERK2 cascade Source: BHF-UCL
  • negative regulation of insulin receptor signaling pathway Source: BHF-UCL
  • negative regulation of MAP kinase activity Source: CACAO
  • negative regulation of PERK-mediated unfolded protein response Source: ParkinsonsUK-UCL
  • negative regulation of signal transduction Source: Reactome
  • negative regulation of vascular endothelial growth factor receptor signaling pathway Source: BHF-UCL
  • peptidyl-tyrosine dephosphorylation Source: UniProtKB
  • peptidyl-tyrosine dephosphorylation involved in inactivation of protein kinase activity Source: BHF-UCL
  • platelet-derived growth factor receptor-beta signaling pathway Source: UniProtKB
  • positive regulation of IRE1-mediated unfolded protein response Source: ParkinsonsUK-UCL
  • positive regulation of protein tyrosine kinase activity Source: ParkinsonsUK-UCL
  • positive regulation of receptor catabolic process Source: CACAO
  • protein dephosphorylation Source: CACAO
  • regulation of endocytosis Source: UniProtKB
  • regulation of hepatocyte growth factor receptor signaling pathway Source: UniProtKB
  • regulation of intracellular protein transport Source: CACAO
  • regulation of signal transduction Source: UniProtKB
  • regulation of type I interferon-mediated signaling pathway Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-877312. Regulation of IFNG signaling.
R-HSA-8849472. PTK6 Down-Regulation.
R-HSA-912694. Regulation of IFNA signaling.
R-HSA-982772. Growth hormone receptor signaling.
SABIO-RKP18031.
SignaLinkiP18031.
SIGNORiP18031.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:9642. PTPN1.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • cytoplasmic side of endoplasmic reticulum membrane Source: ParkinsonsUK-UCL
  • cytoplasmic vesicle Source: Ensembl
  • cytosol Source: Reactome
  • early endosome Source: UniProtKB
  • endoplasmic reticulum Source: HPA
  • 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

MalaCardsiPTPN1.
PharmGKBiPA33985.

Chemistry

ChEMBLiCHEMBL335.
DrugBankiDB01133. Tiludronate.

Polymorphism and mutation databases

DMDMi131467.

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 – 201PhosphotyrosineCombined sources
Modified residuei50 – 501Phosphoserine; by PKB/AKT1, CLK1 and CLK2Combined sources2 Publications
Modified residuei66 – 661Phosphotyrosine; by EGFR1 Publication
Cross-linki215 ↔ 216N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form2 Publications
Modified residuei215 – 2151Cysteine persulfide; alternate1 Publication
Modified residuei215 – 2151Cysteine sulfenic acid (-SOH); alternate2 Publications
Modified residuei215 – 2151Cysteine sulfinic acid (-SO2H); alternate1 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 – 3521PhosphoserineCombined sources1 Publication
Modified residuei363 – 3631PhosphoserineCombined sources
Modified residuei365 – 3651PhosphoserineCombined sources
Modified residuei368 – 3681PhosphothreonineCombined sources
Modified residuei378 – 3781Phosphoserine; by PKCCombined sources1 Publication
Modified residuei386 – 3861Phosphoserine; by CDK1Combined sources1 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.2 Publications
Ser-50 is the major site of phosphorylation as compared to Ser-242 and Ser-243. Activated by phosphorylation at Ser-50.4 Publications
S-nitrosylation of Cys-215 inactivates the enzyme activity.1 Publication
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

EPDiP18031.
MaxQBiP18031.
PaxDbiP18031.
PeptideAtlasiP18031.
PRIDEiP18031.

2D gel databases

OGPiP18031.

PTM databases

DEPODiP18031.
iPTMnetiP18031.
PhosphoSiteiP18031.
SwissPalmiP18031.

Miscellaneous databases

PMAP-CutDBP18031.

Expressioni

Gene expression databases

BgeeiENSG00000196396.
CleanExiHS_PTPN1.
ExpressionAtlasiP18031. baseline and differential.
GenevisibleiP18031. HS.

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
EGFRP005337EBI-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.
RMDN3Q96TC74EBI-968788,EBI-1056589
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
TXNP105992EBI-968788,EBI-594644

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • ephrin receptor binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111736. 103 interactions.
DIPiDIP-38014N.
IntActiP18031. 128 interactions.
MINTiMINT-441655.
STRINGi9606.ENSP00000360683.

Chemistry

BindingDBiP18031.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4QAHX-ray2.40A1-299[»]
4QAPX-ray1.90A1-299[»]
4QBEX-ray2.29A1-298[»]
4QBWX-ray1.91A1-299[»]
4Y14X-ray1.90A/B2-301[»]
4ZRTX-ray1.74A1-298[»]
ProteinModelPortaliP18031.
SMRiP18031. Positions 2-299.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18031.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 277275Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0789. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273908.
HOVERGENiHBG008321.
InParanoidiP18031.
KOiK05696.
OMAiDGPIKEE.
OrthoDBiEOG091G082B.
PhylomeDBiP18031.
TreeFamiTF315897.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR012265. Ptpn1/Ptpn2.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 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

        10         20         30         40         50
MEMEKEFEQI DKSGSWAAIY QDIRHEASDF PCRVAKLPKN KNRNRYRDVS
60 70 80 90 100
PFDHSRIKLH QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW
110 120 130 140 150
EQKSRGVVML NRVMEKGSLK CAQYWPQKEE KEMIFEDTNL KLTLISEDIK
160 170 180 190 200
SYYTVRQLEL ENLTTQETRE ILHFHYTTWP DFGVPESPAS FLNFLFKVRE
210 220 230 240 250
SGSLSPEHGP VVVHCSAGIG RSGTFCLADT CLLLMDKRKD PSSVDIKKVL
260 270 280 290 300
LEMRKFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE
310 320 330 340 350
PPPEHIPPPP RPPKRILEPH NGKCREFFPN HQWVKEETQE DKDCPIKEEK
360 370 380 390 400
GSPLNAAPYG IESMSQDTEV RSRVVGGSLR GAQAASPAKG EPSLPEKDED
410 420 430
HALSYWKPFL VNMCVATVLT AGAYLCYRFL FNSNT
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.
Corresponds to variant rs16995309 [ dbSNP | Ensembl ].
VAR_022014

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.5. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4QAHX-ray2.40A1-299[»]
4QAPX-ray1.90A1-299[»]
4QBEX-ray2.29A1-298[»]
4QBWX-ray1.91A1-299[»]
4Y14X-ray1.90A/B2-301[»]
4ZRTX-ray1.74A1-298[»]
ProteinModelPortaliP18031.
SMRiP18031. Positions 2-299.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111736. 103 interactions.
DIPiDIP-38014N.
IntActiP18031. 128 interactions.
MINTiMINT-441655.
STRINGi9606.ENSP00000360683.

Chemistry

BindingDBiP18031.
ChEMBLiCHEMBL335.
DrugBankiDB01133. Tiludronate.

PTM databases

DEPODiP18031.
iPTMnetiP18031.
PhosphoSiteiP18031.
SwissPalmiP18031.

Polymorphism and mutation databases

DMDMi131467.

2D gel databases

OGPiP18031.

Proteomic databases

EPDiP18031.
MaxQBiP18031.
PaxDbiP18031.
PeptideAtlasiP18031.
PRIDEiP18031.

Protocols and materials databases

DNASUi5770.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371621; ENSP00000360683; ENSG00000196396.
GeneIDi5770.
KEGGihsa:5770.
UCSCiuc002xvl.5. human.

Organism-specific databases

CTDi5770.
GeneCardsiPTPN1.
H-InvDBHIX0027718.
HGNCiHGNC:9642. PTPN1.
HPAiCAB009329.
CAB015217.
HPA012542.
MalaCardsiPTPN1.
MIMi176885. gene.
neXtProtiNX_P18031.
PharmGKBiPA33985.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0789. Eukaryota.
COG5599. LUCA.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000273908.
HOVERGENiHBG008321.
InParanoidiP18031.
KOiK05696.
OMAiDGPIKEE.
OrthoDBiEOG091G082B.
PhylomeDBiP18031.
TreeFamiTF315897.

Enzyme and pathway databases

BRENDAi3.1.3.48. 2681.
ReactomeiR-HSA-354192. Integrin alphaIIb beta3 signaling.
R-HSA-877312. Regulation of IFNG signaling.
R-HSA-8849472. PTK6 Down-Regulation.
R-HSA-912694. Regulation of IFNA signaling.
R-HSA-982772. Growth hormone receptor signaling.
SABIO-RKP18031.
SignaLinkiP18031.
SIGNORiP18031.

Miscellaneous databases

ChiTaRSiPTPN1. human.
EvolutionaryTraceiP18031.
GeneWikiiPTPN1.
GenomeRNAii5770.
PMAP-CutDBP18031.
PROiP18031.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000196396.
CleanExiHS_PTPN1.
ExpressionAtlasiP18031. baseline and differential.
GenevisibleiP18031. HS.

Family and domain databases

Gene3Di3.90.190.10. 1 hit.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000242. PTPase_domain.
IPR012265. Ptpn1/Ptpn2.
IPR016130. Tyr_Pase_AS.
IPR003595. Tyr_Pase_cat.
IPR000387. TYR_PHOSPHATASE_dom.
[Graphical view]
PfamiPF00102. Y_phosphatase. 1 hit.
[Graphical view]
PIRSFiPIRSF000926. Tyr-Ptase_nr1. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 1 hit.
SM00404. PTPc_motif. 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]
ProtoNetiSearch...

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 7, 2016
This is version 206 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.