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Protein

Tyrosine-protein phosphatase non-receptor type 1

Gene

PTPN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
Binding sitei181Substrate1
Active sitei215Phosphocysteine intermediate1
Binding sitei262SubstrateBy similarity1

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • ephrin receptor binding Source: UniProtKB
  • insulin receptor binding Source: Ensembl
  • protein kinase binding Source: UniProtKB
  • protein tyrosine phosphatase activity Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB
  • RNA 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

Keywordsi

Molecular functionHydrolase, Protein phosphatase

Enzyme and pathway databases

BRENDAi3.1.3.48 2681
ReactomeiR-HSA-354192 Integrin alphaIIb beta3 signaling
R-HSA-6807004 Negative regulation of MET activity
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-RKiP18031
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

EuPathDBiHostDB:ENSG00000196396.9
HGNCiHGNC:9642 PTPN1
MIMi176885 gene
neXtProtiNX_P18031

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi50S → A or D: No phosphorylation. 2 Publications1
Mutagenesisi181D → A: Substrate-trapping mutant. 1 Publication1
Mutagenesisi215C → S: Catalytically inactive mutant; abolishes sulfhydration. 1 Publication1

Organism-specific databases

DisGeNETi5770
MalaCardsiPTPN1
OpenTargetsiENSG00000196396
PharmGKBiPA33985

Chemistry databases

ChEMBLiCHEMBL335
DrugBankiDB08783 (4-{(2S)-2-[(tert-butoxycarbonyl)amino]-3-methoxy-3-oxopropyl}phenyl)methaneseleninic acid
DB04800 1-METHYL-3-PHENYL-1H-PYRAZOL-5-YLSULFAMIC ACID
DB04525 2-(Carboxymethoxy)-5-[(2s)-2-({(2s)-2-[(3-Carboxypropanoyl)Amino] -3-Phenylpropanoyl}Amino)-3-Oxo-3-(Pentylamino)Propyl]Benzoic Acid
DB02622 2-(Oxalyl-Amino)-Benzoic Acid
DB07295 2-[(7-HYDROXY-NAPHTHALEN-1-YL)-OXALYL-AMINO]-BENZOIC ACID
DB02436 2-{4-[(2s)-2-[({[(1s)-1-Carboxy-2-Phenylethyl]Amino}Carbonyl)Amino]-3-Oxo-3-(Pentylamino)Propyl]Phenoxy}Malonic Acid
DB01734 3-(Oxalyl-Amino)-Naphthalene-2-Carboxylic Acid
DB03483 4-Benzoylamino-4-{1-{1-Carbamoyl-2-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Ethylcarbamoyl}-2-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Ethylcarbamoyl}-Butyric Acid
DB07197 4-BROMO-3-(CARBOXYMETHOXY)-5-(4-HYDROXYPHENYL)THIOPHENE-2-CARBOXYLIC ACID
DB06829 4-BROMO-3-(CARBOXYMETHOXY)-5-[3-(CYCLOHEXYLAMINO)PHENYL]THIOPHENE-2-CARBOXYLIC ACID
DB07130 4-BROMO-3-(CARBOXYMETHOXY)-5-PHENYLTHIOPHENE-2-CARBOXYLIC ACID
DB03714 4-Carbamoyl-4-{[6-(Difluoro-Phosphono-Methyl)-Naphthalene-2-Carbonyl]-Amino}-Butyric Acid
DB07480 4-PHOSPHONOOXY-PHENYL-METHYL-[4-PHOSPHONOOXY]BENZEN
DB08001 5-(3-{3-[3-HYDROXY-2-(METHOXYCARBONYL)PHENOXY]PROPENYL}PHENYL)-4-(HYDROXYMETHYL)ISOXAZOLE-3-CARBOXYLIC ACID
DB07289 5-[3-(BENZYLAMINO)PHENYL]-4-BROMO-3-(CARBOXYMETHOXY)THIOPHENE-2-CARBOXYLIC ACID
DB08397 6-(DIFLUORO-PHOSPHONO-METHYL)-NAPHTHALENE-2-CARBOXYLIC ACID
DB04001 6-(Oxalyl-Amino)-1h-Indole-5-Carboxylic Acid
DB04204 [(4-{4-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Butyl}-Phenyl)-Difluoro-Methyl]-Phosphonic Acid
DB02615 Compound 19
DB02014 Compound 9
DB03661 Cysteinesulfonic Acid
DB05506 ISIS 113715
DB08003 ISOTHIAZOLIDINONE ANALOG
DB04088 N-(Allyloxycarbonyl)-4-[N-(Carboxy-Formyl)-2-(Benzoic Acid)-Amino]-L-Phenylalaninyl-Amino-Butyloxy-(6-Hydroxy-Benzoic Acid Methyl Ester)
DB02784 N-[4-(2-{2-[3-(2-Bromo-Acetylamino)-Propionylamino]-3-Hydroxy-Propionylamino}-Ethyl)-Phenyl]-Oxalamic Acid
DB07651 N-ACETYL-L-PHENYLALANYL-4-[DIFLUORO(PHOSPHONO)METHYL]-L-PHENYLALANINAMIDE
DB03557 N-{1-[5-(1-Carbamoyl-2-Mercapto-Ethylcarbamoyl)-Pentylcarbamoyl]-2-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Ethyl}-3-{2-[4-(Difluoro-Phosphono-Methyl)-Phenyl]-Acetylamino}-Succinamic Acid
DB02662 Novo Nordisk a/S Compound
DB08371 PARA-(BENZOYL)-PHENYLALANINE
DB02977 PNU177836
DB02620 Sp7343-Sp7964
DB01133 Tiludronic acid
DB03154 {[7-(Difluoro-Phosphono-Methyl)-Naphthalen-2-Yl]-Difluoro-Methyl}-Phosphonic Acid
GuidetoPHARMACOLOGYi2976

Polymorphism and mutation databases

DMDMi131467

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000947481 – 435Tyrosine-protein phosphatase non-receptor type 1Add BLAST435

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionine1 Publication1
Modified residuei20PhosphotyrosineCombined sources1
Modified residuei50Phosphoserine; by PKB/AKT1, CLK1 and CLK2Combined sources2 Publications1
Modified residuei66Phosphotyrosine; by EGFR1 Publication1
Cross-linki215 ↔ 216N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form2 Publications
Modified residuei215Cysteine persulfide; alternate1 Publication1
Modified residuei215Cysteine sulfenic acid (-SOH); alternate2 Publications1
Modified residuei215Cysteine sulfinic acid (-SO2H); alternate1 Publication1
Modified residuei215S-nitrosocysteine; in reversibly inhibited form1 Publication1
Modified residuei242Phosphoserine; by CLK1 and CLK21 Publication1
Modified residuei243Phosphoserine; by CLK1 and CLK21 Publication1
Modified residuei352PhosphoserineCombined sources1 Publication1
Modified residuei363PhosphoserineCombined sources1
Modified residuei365PhosphoserineCombined sources1
Modified residuei368PhosphothreonineCombined sources1
Modified residuei378Phosphoserine; by PKCCombined sources1 Publication1
Modified residuei386Phosphoserine; by CDK1Combined sources1 Publication1

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
PhosphoSitePlusiP18031
SwissPalmiP18031

Miscellaneous databases

PMAP-CutDBiP18031

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

Show more details

GO - Molecular functioni

  • cadherin binding Source: BHF-UCL
  • enzyme binding Source: UniProtKB
  • ephrin receptor binding Source: UniProtKB
  • insulin receptor binding Source: Ensembl
  • protein kinase binding Source: UniProtKB
  • receptor tyrosine kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111736, 146 interactors
DIPiDIP-38014N
IntActiP18031, 141 interactors
MINTiP18031
STRINGi9606.ENSP00000360683

Chemistry databases

BindingDBiP18031

Structurei

Secondary structure

1435
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 13Combined sources11
Helixi16 – 26Combined sources11
Turni33 – 36Combined sources4
Helixi38 – 43Combined sources6
Beta strandi45 – 48Combined sources4
Turni53 – 55Combined sources3
Beta strandi56 – 58Combined sources3
Beta strandi61 – 63Combined sources3
Beta strandi66 – 74Combined sources9
Turni75 – 78Combined sources4
Beta strandi79 – 84Combined sources6
Turni89 – 91Combined sources3
Helixi92 – 102Combined sources11
Beta strandi106 – 109Combined sources4
Beta strandi113 – 115Combined sources3
Beta strandi118 – 121Combined sources4
Beta strandi127 – 131Combined sources5
Beta strandi133 – 135Combined sources3
Turni136 – 139Combined sources4
Beta strandi140 – 149Combined sources10
Beta strandi151 – 162Combined sources12
Turni163 – 165Combined sources3
Beta strandi168 – 176Combined sources9
Beta strandi181 – 183Combined sources3
Beta strandi186 – 188Combined sources3
Helixi189 – 200Combined sources12
Turni201 – 204Combined sources4
Beta strandi211 – 220Combined sources10
Helixi221 – 237Combined sources17
Beta strandi238 – 240Combined sources3
Helixi241 – 243Combined sources3
Helixi246 – 253Combined sources8
Turni254 – 256Combined sources3
Helixi264 – 281Combined sources18
Turni282 – 284Combined sources3
Helixi287 – 295Combined sources9
Turni296 – 298Combined sources3
Beta strandi316 – 318Combined sources3
Beta strandi321 – 324Combined sources4
Beta strandi331 – 333Combined sources3
Beta strandi336 – 338Combined sources3
Turni340 – 342Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
5K9VX-ray1.90A1-301[»]
5K9WX-ray2.01A1-301[»]
5KA0X-ray1.99A1-284[»]
5KA1X-ray1.84A1-284[»]
5KA2X-ray2.07A1-301[»]
5KA3X-ray2.14A1-301[»]
5KA4X-ray2.19A1-301[»]
5KA7X-ray2.06A1-301[»]
5KA8X-ray1.97A1-301[»]
5KA9X-ray2.07A1-301[»]
5KAAX-ray1.97A1-284[»]
5KABX-ray1.97A1-284[»]
5KACX-ray1.90A1-301[»]
5KADX-ray1.90A/B1-301[»]
5T19X-ray2.10A1-321[»]
ProteinModelPortaliP18031
SMRiP18031
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP18031

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 277Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd BLAST275

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni215 – 221Substrate bindingBy similarity7

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG0789 Eukaryota
COG5599 LUCA
GeneTreeiENSGT00900000140785
HOGENOMiHOG000273908
HOVERGENiHBG008321
InParanoidiP18031
KOiK05696
OMAiPHNGKCK
OrthoDBiEOG091G082B
PhylomeDBiP18031
TreeFamiTF315897

Family and domain databases

Gene3Di3.90.190.10, 1 hit
InterProiView protein in InterPro
IPR029021 Prot-tyrosine_phosphatase-like
IPR000242 PTPase_domain
IPR012265 Ptpn1/Ptpn2
IPR016130 Tyr_Pase_AS
IPR003595 Tyr_Pase_cat
IPR000387 TYR_PHOSPHATASE_dom
PfamiView protein in Pfam
PF00102 Y_phosphatase, 1 hit
PIRSFiPIRSF000926 Tyr-Ptase_nr1, 1 hit
PRINTSiPR00700 PRTYPHPHTASE
SMARTiView protein in SMART
SM00194 PTPc, 1 hit
SM00404 PTPc_motif, 1 hit
SUPFAMiSSF52799 SSF52799, 1 hit
PROSITEiView protein in PROSITE
PS00383 TYR_PHOSPHATASE_1, 1 hit
PS50056 TYR_PHOSPHATASE_2, 1 hit
PS50055 TYR_PHOSPHATASE_PTP, 1 hit

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)DescriptionActionsGraphical viewLength
Natural variantiVAR_022013381G → S. Corresponds to variant dbSNP:rs16995304Ensembl.1
Natural variantiVAR_022014387P → L Associated with low glucose tolerance. Corresponds to variant dbSNP:rs16995309Ensembl.1

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 Genomic DNA No translation available.
AL034429 Genomic DNA No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiPTN1_HUMAN
AccessioniPrimary (citable) accession number: P18031
Secondary accession number(s): Q5TGD8, Q9BQV9, Q9NQQ4
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 23, 2018
This is version 224 of the entry and version 1 of the sequence. See 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

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