Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P23469

- PTPRE_HUMAN

UniProt

P23469 - PTPRE_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Receptor-type tyrosine-protein phosphatase epsilon

Gene

PTPRE

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

Functioni

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.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.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 activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.PROSITE-ProRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei303 – 3031SubstrateBy similarity
Active sitei335 – 3351Phosphocysteine intermediateBy similarity
Binding sitei379 – 3791SubstrateBy similarity
Active sitei630 – 6301Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. transmembrane receptor protein tyrosine phosphatase activity Source: ProtInc

GO - Biological processi

  1. negative regulation of insulin receptor signaling pathway Source: UniProtKB
  2. peptidyl-tyrosine dephosphorylation Source: GOC
  3. protein dephosphorylation Source: ProtInc
  4. regulation of mast cell activation Source: Ensembl
  5. transmembrane receptor protein tyrosine phosphatase signaling pathway Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Enzyme and pathway databases

SignaLinkiP23469.

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase epsilon (EC:3.1.3.48)
Short name:
Protein-tyrosine phosphatase epsilon
Short name:
R-PTP-epsilon
Gene namesi
Name:PTPRE
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:9669. PTPRE.

Subcellular locationi

Isoform 2 : Cytoplasm
Note: Predominantly cytoplasmic. A small fraction is also associated with nucleus and membrane. Insulin induces translocation to the membrane By similarity.By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. nucleus Source: UniProtKB
  4. plasma membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA34014.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 700681Receptor-type tyrosine-protein phosphatase epsilonPRO_0000025439Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi23 – 231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi30 – 301N-linked (GlcNAc...)Sequence Analysis
Modified residuei696 – 6961Phosphotyrosine1 Publication

Post-translational modificationi

A catalytically active cytoplasmic form (p65) is produced by proteolytic cleavage of either isoform 1, isoform 2 or isoform 3.1 Publication
Isoform 1 and isoform 2 are phosphorylated on tyrosine residues by tyrosine kinase Neu.2 Publications
Isoform 1 is glycosylated.1 Publication

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP23469.
PaxDbiP23469.
PRIDEiP23469.

PTM databases

PhosphoSiteiP23469.

Expressioni

Tissue specificityi

Expressed in giant cell tumor (osteoclastoma rich in multinucleated osteoclastic cells).1 Publication

Inductioni

Up-regulated by 12-O-tetradecanoylphorbol-13-acetate (TPA) in HL-60 cells.1 Publication

Gene expression databases

BgeeiP23469.
CleanExiHS_PTPRE.
ExpressionAtlasiP23469. baseline and differential.
GenevestigatoriP23469.

Organism-specific databases

HPAiHPA015870.
HPA021872.

Interactioni

Subunit structurei

Monomer. Isoform 2: Homodimer. Can form oligomers. Dimerization is increased by oxidative stress and decreased by EGFR. Isoform 2 interacts with GRB2 By similarity.By similarity

Protein-protein interaction databases

BioGridi111755. 5 interactions.
IntActiP23469. 3 interactions.
MINTiMINT-1349810.
STRINGi9606.ENSP00000254667.

Structurei

Secondary structure

1
700
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi117 – 1193
Helixi120 – 1267
Helixi139 – 1413
Turni152 – 1554
Helixi157 – 1626
Beta strandi172 – 1776
Turni185 – 1884
Beta strandi189 – 1979
Beta strandi200 – 2078
Helixi212 – 2143
Helixi215 – 22410
Beta strandi229 – 2324
Beta strandi236 – 2383
Beta strandi250 – 2567
Beta strandi259 – 26810
Beta strandi270 – 28011
Beta strandi291 – 2988
Beta strandi303 – 3053
Helixi311 – 32313
Beta strandi331 – 3344
Beta strandi336 – 3405
Helixi341 – 35818
Beta strandi359 – 3613
Helixi363 – 3719
Helixi381 – 39616
Helixi426 – 4349
Helixi444 – 4474
Helixi449 – 4524
Beta strandi464 – 4696
Beta strandi481 – 4877
Beta strandi490 – 4923
Beta strandi496 – 4994
Turni504 – 5063
Helixi507 – 51610
Beta strandi521 – 5244
Beta strandi528 – 5303
Beta strandi542 – 5487
Beta strandi551 – 56010
Beta strandi562 – 57312
Beta strandi584 – 5929
Beta strandi597 – 5993
Helixi605 – 62016
Beta strandi626 – 6294
Beta strandi631 – 6355
Helixi636 – 65318
Beta strandi654 – 6563
Helixi658 – 6669
Helixi676 – 69015

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2JJDX-ray3.20A/B/C/D/E/F107-697[»]
ProteinModelPortaliP23469.
SMRiP23469. Positions 111-691.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP23469.

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 4627ExtracellularSequence AnalysisAdd
BLAST
Topological domaini70 – 700631CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei47 – 6923HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini135 – 394260Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini426 – 689264Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni335 – 3417Substrate bindingBy similarity

Domaini

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.By similarity

Sequence similaritiesi

Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118900.
HOGENOMiHOG000231465.
HOVERGENiHBG053758.
InParanoidiP23469.
KOiK18033.
OMAiIVIDAMI.
OrthoDBiEOG7B31M8.
PhylomeDBiP23469.
TreeFamiTF351829.

Family and domain databases

Gene3Di3.90.190.10. 2 hits.
InterProiIPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR016336. Tyr_Pase_rcpt_a/e-type.
[Graphical view]
PfamiPF00102. Y_phosphatase. 2 hits.
[Graphical view]
PIRSFiPIRSF002006. PTPR_alpha_epsilon. 1 hit.
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00194. PTPc. 2 hits.
[Graphical view]
SUPFAMiSSF52799. SSF52799. 2 hits.
PROSITEiPS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative promoter usage and alternative initiation. Align

Isoform 1 (identifier: P23469-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MEPLCPLLLV GFSLPLARAL RGNETTADSN ETTTTSGPPD PGASQPLLAW
60 70 80 90 100
LLLPLLLLLL VLLLAAYFFR FRKQRKAVVS TSDKKMPNGI LEEQEQQRVM
110 120 130 140 150
LLSRSPSGPK KYFPIPVEHL EEEIRIRSAD DCKQFREEFN SLPSGHIQGT
160 170 180 190 200
FELANKEENR EKNRYPNILP NDHSRVILSQ LDGIPCSDYI NASYIDGYKE
210 220 230 240 250
KNKFIAAQGP KQETVNDFWR MVWEQKSATI VMLTNLKERK EEKCHQYWPD
260 270 280 290 300
QGCWTYGNIR VCVEDCVVLV DYTIRKFCIQ PQLPDGCKAP RLVSQLHFTS
310 320 330 340 350
WPDFGVPFTP IGMLKFLKKV KTLNPVHAGP IVVHCSAGVG RTGTFIVIDA
360 370 380 390 400
MMAMMHAEQK VDVFEFVSRI RNQRPQMVQT DMQYTFIYQA LLEYYLYGDT
410 420 430 440 450
ELDVSSLEKH LQTMHGTTTH FDKIGLEEEF RKLTNVRIMK ENMRTGNLPA
460 470 480 490 500
NMKKARVIQI IPYDFNRVIL SMKRGQEYTD YINASFIDGY RQKDYFIATQ
510 520 530 540 550
GPLAHTVEDF WRMIWEWKSH TIVMLTEVQE REQDKCYQYW PTEGSVTHGE
560 570 580 590 600
ITIEIKNDTL SEAISIRDFL VTLNQPQARQ EEQVRVVRQF HFHGWPEIGI
610 620 630 640 650
PAEGKGMIDL IAAVQKQQQQ TGNHPITVHC SAGAGRTGTF IALSNILERV
660 670 680 690 700
KAEGLLDVFQ AVKSLRLQRP HMVQTLEQYE FCYKVVQDFI DIFSDYANFK

Note: Produced by alternative promoter usage.

Length:700
Mass (Da):80,642
Last modified:November 1, 1991 - v1
Checksum:iD096BCADCEA65708
GO
Isoform 2 (identifier: P23469-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:642
Mass (Da):74,595
Checksum:iD39B2835A8D7D949
GO
Isoform 3 (identifier: P23469-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:615
Mass (Da):71,382
Checksum:iF4FD48DDAAA0B302
GO

Sequence cautioni

The sequence AAC50324.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the C-terminal part.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti516 – 5161E → D in CAC86583. (PubMed:12121439)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8585Missing in isoform 3. CuratedVSP_038490Add
BLAST
Alternative sequencei1 – 7070MEPLC…AYFFR → MSNRSSFSRLTW in isoform 2. 2 PublicationsVSP_007778Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS7657.1. [P23469-1]
CCDS7658.1. [P23469-2]
PIRiS12053.
RefSeqiNP_006495.1. NM_006504.4. [P23469-1]
NP_569119.1. NM_130435.3. [P23469-2]
XP_005252748.1. XM_005252691.1. [P23469-1]
XP_005252749.1. XM_005252692.1. [P23469-1]
UniGeneiHs.127022.

Genome annotation databases

EnsembliENST00000254667; ENSP00000254667; ENSG00000132334. [P23469-1]
ENST00000306042; ENSP00000303350; ENSG00000132334. [P23469-2]
GeneIDi5791.
KEGGihsa:5791.
UCSCiuc001lkb.3. human. [P23469-1]
uc001lkd.3. human. [P23469-2]

Polymorphism databases

DMDMi126471.

Keywords - Coding sequence diversityi

Alternative initiation, Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS7657.1. [P23469-1 ]
CCDS7658.1. [P23469-2 ]
PIRi S12053.
RefSeqi NP_006495.1. NM_006504.4. [P23469-1 ]
NP_569119.1. NM_130435.3. [P23469-2 ]
XP_005252748.1. XM_005252691.1. [P23469-1 ]
XP_005252749.1. XM_005252692.1. [P23469-1 ]
UniGenei Hs.127022.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2JJD X-ray 3.20 A/B/C/D/E/F 107-697 [» ]
ProteinModelPortali P23469.
SMRi P23469. Positions 111-691.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111755. 5 interactions.
IntActi P23469. 3 interactions.
MINTi MINT-1349810.
STRINGi 9606.ENSP00000254667.

Chemistry

BindingDBi P23469.
ChEMBLi CHEMBL4850.
DrugBanki DB00630. Alendronate.

PTM databases

PhosphoSitei P23469.

Polymorphism databases

DMDMi 126471.

Proteomic databases

MaxQBi P23469.
PaxDbi P23469.
PRIDEi P23469.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000254667 ; ENSP00000254667 ; ENSG00000132334 . [P23469-1 ]
ENST00000306042 ; ENSP00000303350 ; ENSG00000132334 . [P23469-2 ]
GeneIDi 5791.
KEGGi hsa:5791.
UCSCi uc001lkb.3. human. [P23469-1 ]
uc001lkd.3. human. [P23469-2 ]

Organism-specific databases

CTDi 5791.
GeneCardsi GC10P129705.
HGNCi HGNC:9669. PTPRE.
HPAi HPA015870.
HPA021872.
MIMi 600926. gene.
neXtProti NX_P23469.
PharmGKBi PA34014.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118900.
HOGENOMi HOG000231465.
HOVERGENi HBG053758.
InParanoidi P23469.
KOi K18033.
OMAi IVIDAMI.
OrthoDBi EOG7B31M8.
PhylomeDBi P23469.
TreeFami TF351829.

Enzyme and pathway databases

SignaLinki P23469.

Miscellaneous databases

EvolutionaryTracei P23469.
GeneWikii PTPRE.
GenomeRNAii 5791.
NextBioi 22544.
PROi P23469.
SOURCEi Search...

Gene expression databases

Bgeei P23469.
CleanExi HS_PTPRE.
ExpressionAtlasi P23469. baseline and differential.
Genevestigatori P23469.

Family and domain databases

Gene3Di 3.90.190.10. 2 hits.
InterProi IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
IPR016336. Tyr_Pase_rcpt_a/e-type.
[Graphical view ]
Pfami PF00102. Y_phosphatase. 2 hits.
[Graphical view ]
PIRSFi PIRSF002006. PTPR_alpha_epsilon. 1 hit.
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00194. PTPc. 2 hits.
[Graphical view ]
SUPFAMi SSF52799. SSF52799. 2 hits.
PROSITEi PS00383. TYR_PHOSPHATASE_1. 2 hits.
PS50056. TYR_PHOSPHATASE_2. 2 hits.
PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    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.

Entry informationi

Entry nameiPTPRE_HUMAN
AccessioniPrimary (citable) accession number: P23469
Secondary accession number(s): Q13345
, Q5VWH3, Q5VWH4, Q96KQ6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1991
Last sequence update: November 1, 1991
Last modified: October 29, 2014
This is version 147 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, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3