P18031 (PTN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	PTPN1
Synonyms:	PTP1B

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	435 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.14 Ref.17
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Interacts with EPHA3 (phosphorylated); dephosphorylates EPHA3 and may regulate its trafficking and function. Ref.14
Subcellular location	Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Note: Interacts with EPHA3 at the cell membrane. Ref.8 Ref.14
Post-translational modification	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.
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Non-receptor class 1 subfamily. Contains 1 tyrosine-protein phosphatase domain.

Ontologies

Keywords
Cellular component	Endoplasmic reticulum Membrane
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protein phosphatase
PTM	Acetylation Oxidation Phosphoprotein S-nitrosylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade involved in growth hormone signaling pathway Traceable author statement. Source: Reactome actin cytoskeleton reorganization Inferred from mutant phenotype Ref.14. Source: UniProtKB endoplasmic reticulum unfolded protein response Inferred from direct assay Ref.17. Source: UniProtKB insulin receptor signaling pathway Inferred from electronic annotation. Source: Compara interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome negative regulation of insulin receptor signaling pathway Non-traceable author statement PubMed 11742412. Source: BHF-UCL platelet activation Traceable author statement. Source: Reactome regulation of endocytosis Inferred from direct assay Ref.14. Source: UniProtKB regulation of interferon-gamma-mediated signaling pathway Traceable author statement. Source: Reactome regulation of type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome type I interferon-mediated signaling pathway Traceable author statement. Source: Reactome
Cellular_component	cytoplasmic vesicle Inferred from electronic annotation. Source: Compara cytosol Traceable author statement. Source: Reactome early endosome Inferred from direct assay Ref.14. Source: UniProtKB endoplasmic reticulum Inferred from direct assay. Source: HPA endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	protein tyrosine phosphatase activity Inferred from direct assay PubMed 18074158Ref.17. Source: UniProtKB zinc ion binding Inferred from direct assay PubMed 18074158. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Cdh2	P15116	3	EBI-968788,EBI-397974	From a different organism.
GHR	P10912	5	EBI-968788,EBI-286316
Sumo1	P63166	2	EBI-968788,EBI-80152	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 435

435

Tyrosine-protein phosphatase non-receptor type 1

PRO_0000094748

Regions

Domain

3 – 277

275

Tyrosine-protein phosphatase

Region

215 – 221

7

Substrate binding By similarity

Sites

Active site

215

1

Phosphocysteine intermediate

Binding site

181

1

Substrate

Binding site

262

1

Substrate By similarity

Amino acid modifications

Modified residue

1

1

N-acetylmethionine Ref.6

Modified residue

20

1

Phosphotyrosine Ref.12

Modified residue

50

1

Phosphoserine; by PKB/AKT1, CLK1 and CLK2 Ref.10 Ref.11

Modified residue

66

1

Phosphotyrosine; by EGFR Ref.9

Modified residue

215

1

Cysteine persulfide Ref.17

Modified residue

215

1

S-nitrosocysteine; in reversibly inhibited form Ref.17

Modified residue

242

1

Phosphoserine; by CLK1 and CLK2 Ref.10

Modified residue

243

1

Phosphoserine; by CLK1 and CLK2 Ref.10

Modified residue

352

1

Phosphoserine Ref.7 Ref.13 Ref.15

Modified residue

378

1

Phosphoserine; by PKC Ref.7 Ref.18

Modified residue

386

1

Phosphoserine; by CDK1 Ref.7

Modified residue

393

1

Phosphoserine By similarity

Cross-link

215 ↔ 216

N,N-(cysteine-1,S-diyl)serine (Cys-Ser); in inhibited form

Natural variations

Natural variant

381

1

G → S.
Corresponds to variant rs16995304 [ dbSNP | Ensembl ].

VAR_022013

Natural variant

387

1

P → L Associated with low glucose tolerance. Ref.25
Corresponds to variant rs16995309 [ dbSNP | Ensembl ].

VAR_022014

Experimental info

Mutagenesis

50

1

S → A or D: No phosphorylation. Ref.10 Ref.11

Mutagenesis

181

1

D → A: Substrate-trapping mutant. Ref.17

Mutagenesis

215

1

C → S: Catalytically inactive mutant; abolishes sulfhydration. Ref.17

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

435

Helix Strand Turn

Details...

Helix

3 – 13

11

Helix

16 – 26

11

Turn

33 – 36

4

Helix

38 – 43

6

Beta strand

45 – 48

4

Turn

53 – 55

3

Beta strand

56 – 58

3

Beta strand

61 – 63

3

Beta strand

66 – 74

9

Turn

75 – 78

4

Beta strand

79 – 84

6

Turn

89 – 91

3

Helix

92 – 102

11

Beta strand

106 – 109

4

Beta strand

113 – 115

3

Beta strand

118 – 121

4

Beta strand

128 – 130

3

Beta strand

133 – 135

3

Turn

136 – 139

4

Beta strand

140 – 149

10

Beta strand

151 – 162

12

Turn

163 – 165

3

Beta strand

168 – 176

9

Beta strand

181 – 183

3

Beta strand

186 – 188

3

Helix

189 – 200

12

Turn

201 – 204

4

Beta strand

211 – 220

10

Helix

221 – 237

17

Beta strand

238 – 240

3

Helix

241 – 243

3

Helix

246 – 253

8

Turn

254 – 256

3

Helix

264 – 281

18

Turn

282 – 284

3

Helix

287 – 295

9

Turn

296 – 298

3

Sequences

	Sequence		Length	Mass (Da)
	P18031 [UniParc]. Last modified November 1, 1990. Version 1. Checksum: 802377DCD33F41FD	FASTA	435	49,967
	10 20 30 40 50 60 MEMEKEFEQI DKSGSWAAIY QDIRHEASDF PCRVAKLPKN KNRNRYRDVS PFDHSRIKLH 70 80 90 100 110 120 QEDNDYINAS LIKMEEAQRS YILTQGPLPN TCGHFWEMVW EQKSRGVVML NRVMEKGSLK 130 140 150 160 170 180 CAQYWPQKEE KEMIFEDTNL KLTLISEDIK SYYTVRQLEL ENLTTQETRE ILHFHYTTWP 190 200 210 220 230 240 DFGVPESPAS FLNFLFKVRE SGSLSPEHGP VVVHCSAGIG RSGTFCLADT CLLLMDKRKD 250 260 270 280 290 300 PSSVDIKKVL LEMRKFRMGL IQTADQLRFS YLAVIEGAKF IMGDSSVQDQ WKELSHEDLE 310 320 330 340 350 360 PPPEHIPPPP RPPKRILEPH NGKCREFFPN HQWVKEETQE DKDCPIKEEK GSPLNAAPYG 370 380 390 400 410 420 IESMSQDTEV RSRVVGGSLR GAQAASPAKG EPSLPEKDED HALSYWKPFL VNMCVATVLT 430 AGAYLCYRFL FNSNT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning of a cDNA for a major human protein-tyrosine-phosphatase." Chernoff J., Schievella A.R., Jost C.A., Erikson R.L., Neel B.G. Proc. Natl. Acad. Sci. U.S.A. 87:2735-2739(1990) [PubMed] [Europe PMC] [Abstract] 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. 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, MASS SPECTROMETRY.
[13]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"PTP1B regulates Eph receptor function and trafficking." Nievergall E., Janes P.W., Stegmayer C., Vail M.E., Haj F.G., Teng S.W., Neel B.G., Bastiaens P.I., Lackmann M. J. Cell Biol. 191:1189-1203(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH EPHA3, FUNCTION IN EPHA3 DEPHOSPHORYLATION, SUBCELLULAR LOCATION.
[15]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[16]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[17]	"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.
[18]	"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, MASS SPECTROMETRY.
[19]	"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.
[20]	"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.
[21]	"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.
[22]	"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.
[23]	"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.
[24]	"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.
[25]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00297261.

PIR

TPHUN1. A35992.

RefSeq

NP_002818.1. NM_002827.2.

UniGene

Hs.417549.

3D structure databases

PDBe
RCSB PDB
PDBj

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	1-321	[»]
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	[»]
3ZV2	X-ray	2.80	A	1-320	[»]
4I8N	X-ray	2.50	A	1-320	[»]

ProteinModelPortal

P18031.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38014N.

IntAct

P18031. 14 interactions.

MINT

MINT-441655.

STRING

9606.ENSP00000360683.

PTM databases

PhosphoSite

P18031.

Polymorphism databases

DMDM

131467.

2D gel databases

OGP

P18031.

Proteomic databases

PaxDb

P18031.

PeptideAtlas

P18031.

PRIDE

P18031.

Protocols and materials databases

DNASU

5770.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000371621; ENSP00000360683; ENSG00000196396.

GeneID

5770.

KEGG

hsa:5770.

UCSC

uc002xvl.3. human.

Organism-specific databases

CTD

5770.

GeneCards

GC20P049126.

H-InvDB

HIX0027718.

HGNC

HGNC:9642. PTPN1.

HPA

CAB009329.
CAB015217.
HPA012542.

MIM

176885. gene.

neXtProt

NX_P18031.

PharmGKB

PA33985.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOGENOM

HOG000273908.

HOVERGEN

HBG008321.

InParanoid

P18031.

KO

K05696.

OMA

DGPIKEE.

OrthoDB

EOG418BND.

PhylomeDB

P18031.

Enzyme and pathway databases

BRENDA

3.1.3.48. 2681.

Pathway_Interaction_DB

nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
igf1_pathway. IGF1 pathway.
insulin_pathway. Insulin Pathway.
pdgfrbpathway. PDGFR-beta signaling pathway.
ptp1bpathway. Signaling events mediated by PTP1B.

Reactome

REACT_111102. Signal Transduction.
REACT_604. Hemostasis.
REACT_6900. Immune System.

SABIO-RK

P18031.

Gene expression databases

ArrayExpress

P18031.

Bgee

P18031.

CleanEx

HS_PTPN1.

Genevestigator

P18031.

GermOnline

ENSG00000196396. Homo sapiens.

Family and domain databases

InterPro

IPR012265. Ptpn1/2.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]

PANTHER

PTHR19134:SF57. PTHR19134:SF57. 1 hit.

Pfam

PF00102. Y_phosphatase. 1 hit.
[Graphical view]

PIRSF

PIRSF000926. Tyr-Ptase_nr1. 1 hit.

PRINTS

PR00700. PRTYPHPHTASE.

SMART

SM00194. PTPc. 1 hit.
[Graphical view]

PROSITE

PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P18031.

ChEMBL

CHEMBL335.

ChiTaRS

PTPN1. human.

DrugBank

DB00720. Clodronate.
DB01133. Tiludronate.

EvolutionaryTrace

P18031.

GenomeRNAi

5770.

NextBio

22442.

PMAP-CutDB

P18031.

SOURCE

Search...

Entry information

Entry name

PTN1_HUMAN

Accession

Primary (citable) accession number: P18031
Secondary accession number(s): Q5TGD8, Q9BQV9, Q9NQQ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1990
Last sequence update:	November 1, 1990
Last modified:	May 1, 2013
This is version 170 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.