P23469 (PTPRE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Receptor-type tyrosine-protein phosphatase epsilon
Short name=Protein-tyrosine phosphatase epsilon
Short name=R-PTP-epsilon
EC=3.1.3.48

Gene names

Name:

PTPRE

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	700 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Isoform 1 plays a critical role in signaling transduction pathways and phosphoprotein network topology in red blood cells. May play a role in osteoclast formation and function By similarity. Isoform 2 acts as a negative regulator of insulin receptor (IR) signaling in skeletal muscle. Regulates insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1), phosphorylation of protein kinase B and glycogen synthase kinase-3 and insulin induced stimulation of glucose uptake By similarity. Isoform 1 and isoform 2 act as a negative regulator of FceRI-mediated signal transduction leading to cytokine production and degranulation, most likely by acting at the level of SYK to affect downstream events such as phosphorylation of SLP76 and LAT and mobilization of Ca2+ By similarity.
Catalytic activity	Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.
Subunit structure	Monomer. Isoform 2: Homodimer. Can form oligomers. Dimerization is increased by oxidative stress and decreased by EGFR. Isoform 2 interacts with GRB2 By similarity. Ref.10 Ref.12
Subcellular location	Isoform 1: Cell membrane; Single-pass type I membrane protein Ref.7 Ref.10. Isoform 2: Cytoplasm Ref.7 Ref.10. Note: Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin induces translocation to the membrane By similarity. Ref.7 Ref.10 Isoform 3: Cytoplasm Ref.7 Ref.10.
Tissue specificity	Expressed in giant cell tumor (osteoclastoma rich in multinucleated osteoclastic cells). Ref.8
Induction	Up-regulated by 12-O-tetradecanoylphorbol-13-acetate (TPA) in HL-60 cells. Ref.7
Domain	The tyrosine-protein phosphatase 2 domain (D2) mediates dimerization. The extreme N- and C- termini of the D2 domain act to inhibit dimerization and removal of these sequences increases dimerization and inhibits enzyme activity By similarity.
Post-translational modification	A catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3. Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu. Ref.10 Isoform 1 is glycosylated. Ref.10
Sequence similarities	Belongs to the protein-tyrosine phosphatase family. Receptor class 4 subfamily. Contains 2 tyrosine-protein phosphatase domains.
Sequence caution	The sequence AAC50324.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

Ontologies

Keywords
Cellular component	Cell membrane Cytoplasm Membrane
Coding sequence diversity	Alternative initiation Alternative promoter usage
Domain	Repeat Signal Transmembrane Transmembrane helix
Molecular function	Hydrolase Protein phosphatase
PTM	Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	negative regulation of insulin receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB regulation of mast cell activation Inferred from electronic annotation. Source: Compara transmembrane receptor protein tyrosine phosphatase signaling pathway Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasm Inferred from direct assay Ref.10Ref.7. Source: UniProtKB integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW intermediate filament cytoskeleton Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.10. Source: UniProtKB plasma membrane Inferred from direct assay Ref.10. Source: UniProtKB
Molecular_function	transmembrane receptor protein tyrosine phosphatase activity Traceable author statement Ref.1. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative promoter usage and alternative initiation. [Align] [Select]

Isoform 1 (identifier: P23469-1)

Also known as: PTPeM; RPTPe; tm-PTPe;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: Produced by alternative promoter usage.

Isoform 2 (identifier: P23469-2)

Also known as: PTPeC; cyt-PTPe;

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: MEPLCPLLLV...VLLLAAYFFR → MSNRSSFSRLTW

Note: Produced by alternative promoter usage.

Isoform 3 (identifier: P23469-3)

Also known as: p67;

The sequence of this isoform differs from the canonical sequence as follows:
     1-85: Missing.

Note: Produced by alternative initiation at Met-86 of isoform 1.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 19

19

Potential

Chain

20 – 700

681

Receptor-type tyrosine-protein phosphatase epsilon

PRO_0000025439

Regions

Topological domain

20 – 46

27

Extracellular Potential

Transmembrane

47 – 69

23

Helical; Potential

Topological domain

70 – 700

631

Cytoplasmic Potential

Domain

135 – 394

260

Tyrosine-protein phosphatase 1

Domain

426 – 689

264

Tyrosine-protein phosphatase 2

Region

335 – 341

7

Substrate binding By similarity

Sites

Active site

335

1

Phosphocysteine intermediate By similarity

Active site

630

1

Phosphocysteine intermediate By similarity

Binding site

303

1

Substrate By similarity

Binding site

379

1

Substrate By similarity

Amino acid modifications

Modified residue

696

1

Phosphotyrosine Ref.11

Glycosylation

23

1

N-linked (GlcNAc...) Potential

Glycosylation

30

1

N-linked (GlcNAc...) Potential

Natural variations

Alternative sequence

1 – 85

85

Missing in isoform 3.

VSP_038490

Alternative sequence

1 – 70

70

MEPLC…AYFFR → MSNRSSFSRLTW in isoform 2.

VSP_007778

Experimental info

Sequence conflict

516

1

E → D in CAC86583. Ref.2

Secondary structure

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700

Helix Strand Turn

Details...

Helix

117 – 119

3

Helix

120 – 126

7

Helix

139 – 141

3

Turn

152 – 155

4

Helix

157 – 162

6

Beta strand

172 – 177

6

Turn

185 – 188

4

Beta strand

189 – 197

9

Beta strand

200 – 207

8

Helix

212 – 214

3

Helix

215 – 224

10

Beta strand

229 – 232

4

Beta strand

236 – 238

3

Beta strand

250 – 256

7

Beta strand

259 – 268

10

Beta strand

270 – 280

11

Beta strand

291 – 298

8

Beta strand

303 – 305

3

Helix

311 – 323

13

Beta strand

331 – 334

4

Beta strand

336 – 340

5

Helix

341 – 358

18

Beta strand

359 – 361

3

Helix

363 – 371

9

Helix

381 – 396

16

Helix

426 – 434

9

Helix

444 – 447

4

Helix

449 – 452

4

Beta strand

464 – 469

6

Beta strand

481 – 487

7

Beta strand

490 – 492

3

Beta strand

496 – 499

4

Turn

504 – 506

3

Helix

507 – 516

10

Beta strand

521 – 524

4

Beta strand

528 – 530

3

Beta strand

542 – 548

7

Beta strand

551 – 560

10

Beta strand

562 – 573

12

Beta strand

584 – 592

9

Beta strand

597 – 599

3

Helix

605 – 620

16

Beta strand

626 – 629

4

Beta strand

631 – 635

5

Helix

636 – 653

18

Beta strand

654 – 656

3

Helix

658 – 666

9

Helix

676 – 690

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (PTPeM) (RPTPe) (tm-PTPe) [UniParc]. Last modified November 1, 1991. Version 1. Checksum: D096BCADCEA65708	FASTA	700	80,642
	10 20 30 40 50 60 MEPLCPLLLV GFSLPLARAL RGNETTADSN ETTTTSGPPD PGASQPLLAW LLLPLLLLLL 70 80 90 100 110 120 VLLLAAYFFR FRKQRKAVVS TSDKKMPNGI LEEQEQQRVM LLSRSPSGPK KYFPIPVEHL 130 140 150 160 170 180 EEEIRIRSAD DCKQFREEFN SLPSGHIQGT FELANKEENR EKNRYPNILP NDHSRVILSQ 190 200 210 220 230 240 LDGIPCSDYI NASYIDGYKE KNKFIAAQGP KQETVNDFWR MVWEQKSATI VMLTNLKERK 250 260 270 280 290 300 EEKCHQYWPD QGCWTYGNIR VCVEDCVVLV DYTIRKFCIQ PQLPDGCKAP RLVSQLHFTS 310 320 330 340 350 360 WPDFGVPFTP IGMLKFLKKV KTLNPVHAGP IVVHCSAGVG RTGTFIVIDA MMAMMHAEQK 370 380 390 400 410 420 VDVFEFVSRI RNQRPQMVQT DMQYTFIYQA LLEYYLYGDT ELDVSSLEKH LQTMHGTTTH 430 440 450 460 470 480 FDKIGLEEEF RKLTNVRIMK ENMRTGNLPA NMKKARVIQI IPYDFNRVIL SMKRGQEYTD 490 500 510 520 530 540 YINASFIDGY RQKDYFIATQ GPLAHTVEDF WRMIWEWKSH TIVMLTEVQE REQDKCYQYW 550 560 570 580 590 600 PTEGSVTHGE ITIEIKNDTL SEAISIRDFL VTLNQPQARQ EEQVRVVRQF HFHGWPEIGI 610 620 630 640 650 660 PAEGKGMIDL IAAVQKQQQQ TGNHPITVHC SAGAGRTGTF IALSNILERV KAEGLLDVFQ 670 680 690 700 AVKSLRLQRP HMVQTLEQYE FCYKVVQDFI DIFSDYANFK
	Isoform 2 (PTPeC) (cyt-PTPe) [UniParc]. Checksum: D39B2835A8D7D949	FASTA	642	74,595
	10 20 30 40 50 60 MSNRSSFSRL TWFRKQRKAV VSTSDKKMPN GILEEQEQQR VMLLSRSPSG PKKYFPIPVE 70 80 90 100 110 120 HLEEEIRIRS ADDCKQFREE FNSLPSGHIQ GTFELANKEE NREKNRYPNI LPNDHSRVIL 130 140 150 160 170 180 SQLDGIPCSD YINASYIDGY KEKNKFIAAQ GPKQETVNDF WRMVWEQKSA TIVMLTNLKE 190 200 210 220 230 240 RKEEKCHQYW PDQGCWTYGN IRVCVEDCVV LVDYTIRKFC IQPQLPDGCK APRLVSQLHF 250 260 270 280 290 300 TSWPDFGVPF TPIGMLKFLK KVKTLNPVHA GPIVVHCSAG VGRTGTFIVI DAMMAMMHAE 310 320 330 340 350 360 QKVDVFEFVS RIRNQRPQMV QTDMQYTFIY QALLEYYLYG DTELDVSSLE KHLQTMHGTT 370 380 390 400 410 420 THFDKIGLEE EFRKLTNVRI MKENMRTGNL PANMKKARVI QIIPYDFNRV ILSMKRGQEY 430 440 450 460 470 480 TDYINASFID GYRQKDYFIA TQGPLAHTVE DFWRMIWEWK SHTIVMLTEV QEREQDKCYQ 490 500 510 520 530 540 YWPTEGSVTH GEITIEIKND TLSEAISIRD FLVTLNQPQA RQEEQVRVVR QFHFHGWPEI 550 560 570 580 590 600 GIPAEGKGMI DLIAAVQKQQ QQTGNHPITV HCSAGAGRTG TFIALSNILE RVKAEGLLDV 610 620 630 640 FQAVKSLRLQ RPHMVQTLEQ YEFCYKVVQD FIDIFSDYAN FK
	Isoform 3 (p67) [UniParc]. Checksum: F4FD48DDAAA0B302	FASTA	615	71,382
	10 20 30 40 50 60 MPNGILEEQE QQRVMLLSRS PSGPKKYFPI PVEHLEEEIR IRSADDCKQF REEFNSLPSG 70 80 90 100 110 120 HIQGTFELAN KEENREKNRY PNILPNDHSR VILSQLDGIP CSDYINASYI DGYKEKNKFI 130 140 150 160 170 180 AAQGPKQETV NDFWRMVWEQ KSATIVMLTN LKERKEEKCH QYWPDQGCWT YGNIRVCVED 190 200 210 220 230 240 CVVLVDYTIR KFCIQPQLPD GCKAPRLVSQ LHFTSWPDFG VPFTPIGMLK FLKKVKTLNP 250 260 270 280 290 300 VHAGPIVVHC SAGVGRTGTF IVIDAMMAMM HAEQKVDVFE FVSRIRNQRP QMVQTDMQYT 310 320 330 340 350 360 FIYQALLEYY LYGDTELDVS SLEKHLQTMH GTTTHFDKIG LEEEFRKLTN VRIMKENMRT 370 380 390 400 410 420 GNLPANMKKA RVIQIIPYDF NRVILSMKRG QEYTDYINAS FIDGYRQKDY FIATQGPLAH 430 440 450 460 470 480 TVEDFWRMIW EWKSHTIVML TEVQEREQDK CYQYWPTEGS VTHGEITIEI KNDTLSEAIS 490 500 510 520 530 540 IRDFLVTLNQ PQARQEEQVR VVRQFHFHGW PEIGIPAEGK GMIDLIAAVQ KQQQQTGNHP 550 560 570 580 590 600 ITVHCSAGAG RTGTFIALSN ILERVKAEGL LDVFQAVKSL RLQRPHMVQT LEQYEFCYKV 610 VQDFIDIFSD YANFK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Structural diversity and evolution of human receptor-like protein tyrosine phosphatases." Krueger N.X., Streuli M., Saito H. EMBO J. 9:3241-3252(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Placenta.
[2]	"Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase." Wabakken T.K., Hauge H., Finne E.F., Wiedlocha A., Aasheim H.-C. Scand. J. Immunol. 56:195-203(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Brain.
[7]	"Identification of a cytoplasmic, phorbol ester-inducible isoform of protein tyrosine phosphatase epsilon." Elson A., Leder P. Proc. Natl. Acad. Sci. U.S.A. 92:12235-12239(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-98 (ISOFORM 2), SUBCELLULAR LOCATION, INDUCTION.
[8]	"Protein-tyrosine phosphatase activity regulates osteoclast formation and function: inhibition by alendronate." Schmidt A., Rutledge S.J., Endo N., Opas E., Tanaka H., Wesolowski G., Leu C.T., Huang Z., Ramachandaran C., Rodan S.B., Rodan G.A. Proc. Natl. Acad. Sci. U.S.A. 93:3068-3073(1996) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY.
[9]	"Distinct promoters control transmembrane and cytosolic protein tyrosine phosphatase epsilon expression during macrophage differentiation." Tanuma N., Nakamura K., Kikuchi K. Eur. J. Biochem. 259:46-54(1999) [PubMed] [Europe PMC] [Abstract] Cited for: ALTERNATIVE PROMOTER USAGE.
[10]	"Generation of novel cytoplasmic forms of protein tyrosine phosphatase epsilon by proteolytic processing and translational control." Gil-Henn H., Volohonsky G., Toledano-Katchalski H., Gandre S., Elson A. Oncogene 19:4375-4384(2000) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION (ISOFORM 3), ALTERNATIVE INITIATION, SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, PHOSPHORYLATION, GLYCOSYLATION, INTERACTION WITH GRB2.
[11]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-696, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Large-scale structural analysis of the classical human protein tyrosine phosphatome." Barr A.J., Ugochukwu E., Lee W.H., King O.N.F., Filippakopoulos P., Alfano I., Savitsky P., Burgess-Brown N.A., Mueller S., Knapp S. Cell 136:352-363(2009) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 107-697, SUBUNIT.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X54134 mRNA. Translation: CAA38069.1.
AJ315969 mRNA. Translation: CAC86583.1.
AK291828 mRNA. Translation: BAF84517.1.
AL390236 Genomic DNA. Translation: CAH73173.1.
AL390236 Genomic DNA. Translation: CAH73174.1.
CH471066 Genomic DNA. Translation: EAW49180.1.
CH471066 Genomic DNA. Translation: EAW49181.1.
CH471066 Genomic DNA. Translation: EAW49182.1.
CH471066 Genomic DNA. Translation: EAW49184.1.
BC050062 mRNA. Translation: AAH50062.1.
U36623 mRNA. Translation: AAC50324.1. Sequence problems.

IPI

IPI00011644.
IPI00334825.
IPI00954465.

PIR

S12053.

RefSeq

NP_006495.1. NM_006504.4.
NP_569119.1. NM_130435.3.

UniGene

Hs.127022.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2JJD	X-ray	3.20	A/B/C/D/E/F	107-697	[»]

ProteinModelPortal

P23469.

ModBase

Search...

Protein-protein interaction databases

IntAct

P23469. 1 interaction.

MINT

MINT-1349810.

STRING

9606.ENSP00000254667.

PTM databases

PhosphoSite

P23469.

Polymorphism databases

DMDM

126471.

Proteomic databases

PaxDb

P23469.

PRIDE

P23469.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000254667; ENSP00000254667; ENSG00000132334.
ENST00000306042; ENSP00000303350; ENSG00000132334.
ENST00000419012; ENSP00000402337; ENSG00000132334.

GeneID

5791.

KEGG

hsa:5791.

UCSC

uc001lkb.3. human.
uc001lkd.3. human.

Organism-specific databases

CTD

5791.

GeneCards

GC10P129705.

HGNC

HGNC:9669. PTPRE.

HPA

HPA015870.
HPA021872.

MIM

600926. gene.

neXtProt

NX_P23469.

PharmGKB

PA34014.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5599.

HOGENOM

HOG000231465.

HOVERGEN

HBG053758.

InParanoid

P23469.

KO

K01104.

OMA

PDGCKAP.

OrthoDB

EOG44BB1S.

PhylomeDB

P23469.

Enzyme and pathway databases

Pathway_Interaction_DB

il6_7pathway. IL6-mediated signaling events.

Gene expression databases

ArrayExpress

P23469.

Bgee

P23469.

CleanEx

HS_PTPRE.

Genevestigator

P23469.

GermOnline

ENSG00000132334. Homo sapiens.

Family and domain databases

InterPro

IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR016336. Tyr_Pase_rcpt_a/e-type.
[Graphical view]

Pfam

PF00102. Y_phosphatase. 2 hits.
[Graphical view]

PIRSF

PIRSF002006. PTPR_alpha_epsilon. 1 hit.

PRINTS

PR00700. PRTYPHPHTASE.

SMART

SM00194. PTPc. 2 hits.
[Graphical view]

PROSITE

PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P23469.

ChEMBL

CHEMBL4850.

EvolutionaryTrace

P23469.

GenomeRNAi

5791.

NextBio

22544.

SOURCE

Search...

Entry information

Entry name

PTPRE_HUMAN

Accession

Primary (citable) accession number: P23469
Secondary accession number(s): Q13345 , Q5VWH3, Q5VWH4, Q96KQ6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	November 1, 1991
Last modified:	May 1, 2013
This is version 132 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.