Skip Header

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

P49446

- PTPRE_MOUSE

UniProt

P49446 - PTPRE_MOUSE

(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
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Isoform 1 acts as a negative regulator of insulin receptor (IR) signaling and is involved in insulin-induced glucose metabolism mainly through direct dephosphorylation and inactivation of IR in hepatocytes and liver (By similarity). 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.
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+.

Catalytic activityi

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

Enzyme regulationi

Isoform 1 is inhibited by alendronate (ALN), orthovanadate, and phenylarsine oxide (PAO).1 Publication

Kineticsi

  1. KM=70 µM for fluorescein diphosphate (isoform 1)1 Publication

Vmax=6 µmol/min/mg enzyme for fluorescein diphosphate (isoform 1)1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei302 – 3021SubstrateBy similarity
Active sitei334 – 3341Phosphocysteine intermediateBy similarity
Binding sitei378 – 3781SubstrateBy similarity
Active sitei629 – 6291Phosphocysteine intermediateBy similarity

GO - Molecular functioni

  1. protein homodimerization activity Source: MGI
  2. protein tyrosine phosphatase activity Source: MGI

GO - Biological processi

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

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

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
Synonyms:Ptpe
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 7

Organism-specific databases

MGIiMGI:97813. Ptpre.

Subcellular locationi

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini20 – 4526ExtracellularSequence AnalysisAdd
BLAST
Transmembranei46 – 6823HelicalSequence AnalysisAdd
BLAST
Topological domaini69 – 699631CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice show greater insulin-induced tyrosine phosphorylation of insulin receptor (IR) and insulin receptor substrate 1 (IRS-1) in the skeletal muscle. Antigen- and IgE-mediated passive systemic anaphylactic reactions are enhanced. Erythrocytes exhibit abnormal morphology, increased Ca2+-activated-K+ channel activity and marked perturbation of the erythrocyte membrane tyrosine phosphoproteome.3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1919Sequence AnalysisAdd
BLAST
Chaini20 – 699680Receptor-type tyrosine-protein phosphatase epsilonPRO_0000025440Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi23 – 231N-linked (GlcNAc...)Sequence Analysis
Glycosylationi31 – 311N-linked (GlcNAc...)Sequence Analysis
Modified residuei695 – 6951Phosphotyrosine2 Publications

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.By similarity
Isoform 1 is glycosylated.By similarity

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP49446.
PaxDbiP49446.
PRIDEiP49446.

PTM databases

PhosphoSiteiP49446.

Expressioni

Tissue specificityi

Isoform 2 is expressed in the spleen and thymus (at protein level). Detected in fibroblasts, myeloid cells, macrophages, and T-cells but not in B-cell lines. Isoform 1 and isoform 2 are expressed predominantly in the brain, testes, and lungs, with lower levels present in lymph nodes, thymus, spleen, heart and mammary glands. Isoform 1 is expressed in osteoclasts and not in osteoblasts and its expression is related to osteoclast differentiation. It is also expressed in the erythrocytes. Isoform 2 is strongly expressed in skeletal muscle and L6 skeletal muscle cell line.5 Publications

Inductioni

Isoform 2 is induced by 12-O-tetradecanoylphorbol-13-acetate (TPA) and its induction is dependent upon PKC activity.1 Publication

Gene expression databases

BgeeiP49446.
CleanExiMM_PTPRE.
GenevestigatoriP49446.

Interactioni

Subunit structurei

Monomer (By similarity). 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

BioGridi202496. 1 interaction.
IntActiP49446. 6 interactions.

Structurei

3D structure databases

ProteinModelPortaliP49446.
SMRiP49446. Positions 110-690.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini134 – 393260Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
BLAST
Domaini425 – 688264Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni334 – 3407Substrate 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.1 Publication

Sequence similaritiesi

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

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
GeneTreeiENSGT00760000118900.
HOVERGENiHBG053758.
InParanoidiP49446.
KOiK18033.
OMAiIVIDAMI.
OrthoDBiEOG7B31M8.
PhylomeDBiP49446.
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: P49446-1) [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
MEPFCPLLLA SFSLSLARAG QGNDTTPTES NWTSTTAGPP DPGASQPLLT
60 70 80 90 100
WLLLPLLLLL FLLAAYFFRF RKQRKAVVSS NDKKMPNGIL EEQEQQRVML
110 120 130 140 150
LSRSPSGPKK FFPIPVEHLE EEIRVRSADD CKRFREEFNS LPSGHIQGTF
160 170 180 190 200
ELANKEENRE KNRYPNILPN DHCRVILSQV DGIPCSDYIN ASYIDGYKEK
210 220 230 240 250
NKFIAAQGPK QETVNDFWRM VWEQRSATIV MLTNLKERKE EKCYQYWPDQ
260 270 280 290 300
GCWTYGNIRV CVEDCVVLVD YTIRKFCIHP QLPDSCKAPR LVSQLHFTSW
310 320 330 340 350
PDFGVPFTPI GMLKFLKKVK TLNPSHAGPI VVHCSAGVGR TGTFIVIDAM
360 370 380 390 400
MDMIHSEQKV DVFEFVSRIR NQRPQMVQTD VQYTFIYQAL LEYYLYGDTE
410 420 430 440 450
LDVSSLERHL QTLHSTATHF DKIGLEEEFR KLTNVRIMKE NMRTGNLPAN
460 470 480 490 500
MKKARVIQII PYDFNRVILS MKRGQEFTDY INASFIDGYR QKDYFMATQG
510 520 530 540 550
PLAHTVEDFW RMVWEWKSHT IVMLTEVQER EQDKCYQYWP TEGSVTHGDI
560 570 580 590 600
TIEIKSDTLS EAISVRDFLV TFKQPLARQE EQVRMVRQFH FHGWPEVGIP
610 620 630 640 650
AEGKGMIDLI AAVQKQQQQT GNHPITVHCS AGAGRTGTFI ALSNILERVK
660 670 680 690
AEGLLDVFQA VKSLRLQRPH MVQTLEQYEF CYKVVQDFID IFSDYANFK

Note: Produced by alternative promoter usage.

Length:699
Mass (Da):80,688
Last modified:December 15, 2009 - v3
Checksum:i581EF9CB881BC05B
GO
Isoform 2 (identifier: P49446-2) [UniParc]FASTAAdd to Basket

Also known as: PTPeC, cyt-PTPe

The sequence of this isoform differs from the canonical sequence as follows:
     1-69: MEPFCPLLLA...LFLLAAYFFR → MSSRKNFSRLTW

Note: Produced by alternative promoter usage.

Show »
Length:642
Mass (Da):74,735
Checksum:i92F99E9729D8F1F3
GO
Isoform 3 (identifier: P49446-3) [UniParc]FASTAAdd to Basket

Also known as: p67

The sequence of this isoform differs from the canonical sequence as follows:
     1-84: Missing.

Note: Produced by alternative initiation at Met-85 of isoform 1.

Show »
Length:615
Mass (Da):71,467
Checksum:i56E0BE70BB2BB59C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti137 – 1371E → K in BAE32920. (PubMed:16141072)Curated
Sequence conflicti500 – 5001G → A in BAA11927. 1 PublicationCurated
Sequence conflicti506 – 5061V → G in AAC52281. (PubMed:7592814)Curated
Sequence conflicti506 – 5061V → G in AAC52331. (PubMed:8618876)Curated
Sequence conflicti506 – 5061V → G in AAB04553. 1 PublicationCurated
Sequence conflicti521 – 5222IV → ML in BAA11927. 1 PublicationCurated
Sequence conflicti606 – 6061M → I in AAC52281. (PubMed:7592814)Curated
Sequence conflicti606 – 6061M → I in AAC52331. (PubMed:8618876)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 8484Missing in isoform 3. CuratedVSP_038491Add
BLAST
Alternative sequencei1 – 6969MEPFC…AYFFR → MSSRKNFSRLTW in isoform 2. 2 PublicationsVSP_038492Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35368 mRNA. Translation: AAC52281.1.
U36758 mRNA. Translation: AAC52331.1.
U40280 mRNA. Translation: AAB02190.1.
D83484 mRNA. Translation: BAA11927.1.
U62387 mRNA. Translation: AAB04553.1.
AK154910 mRNA. Translation: BAE32920.1.
CH466531 Genomic DNA. Translation: EDL17805.1.
CH466531 Genomic DNA. Translation: EDL17807.1.
Z23052 mRNA. Translation: CAA80587.1.
Z23053 mRNA. Translation: CAA80588.1.
CCDSiCCDS21944.1. [P49446-1]
PIRiB61180.
JC6132.
S40284.
RefSeqiNP_035342.3. NM_011212.3. [P49446-1]
XP_006507522.1. XM_006507459.1. [P49446-1]
XP_006507523.1. XM_006507460.1. [P49446-1]
XP_006507524.1. XM_006507461.1. [P49446-2]
UniGeneiMm.945.

Genome annotation databases

EnsembliENSMUST00000073961; ENSMUSP00000073616; ENSMUSG00000041836. [P49446-1]
GeneIDi19267.
KEGGimmu:19267.
UCSCiuc009kee.1. mouse. [P49446-1]
uc009kek.1. mouse. [P49446-2]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative promoter usage

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U35368 mRNA. Translation: AAC52281.1 .
U36758 mRNA. Translation: AAC52331.1 .
U40280 mRNA. Translation: AAB02190.1 .
D83484 mRNA. Translation: BAA11927.1 .
U62387 mRNA. Translation: AAB04553.1 .
AK154910 mRNA. Translation: BAE32920.1 .
CH466531 Genomic DNA. Translation: EDL17805.1 .
CH466531 Genomic DNA. Translation: EDL17807.1 .
Z23052 mRNA. Translation: CAA80587.1 .
Z23053 mRNA. Translation: CAA80588.1 .
CCDSi CCDS21944.1. [P49446-1 ]
PIRi B61180.
JC6132.
S40284.
RefSeqi NP_035342.3. NM_011212.3. [P49446-1 ]
XP_006507522.1. XM_006507459.1. [P49446-1 ]
XP_006507523.1. XM_006507460.1. [P49446-1 ]
XP_006507524.1. XM_006507461.1. [P49446-2 ]
UniGenei Mm.945.

3D structure databases

ProteinModelPortali P49446.
SMRi P49446. Positions 110-690.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202496. 1 interaction.
IntActi P49446. 6 interactions.

PTM databases

PhosphoSitei P49446.

Proteomic databases

MaxQBi P49446.
PaxDbi P49446.
PRIDEi P49446.

Protocols and materials databases

DNASUi 19267.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000073961 ; ENSMUSP00000073616 ; ENSMUSG00000041836 . [P49446-1 ]
GeneIDi 19267.
KEGGi mmu:19267.
UCSCi uc009kee.1. mouse. [P49446-1 ]
uc009kek.1. mouse. [P49446-2 ]

Organism-specific databases

CTDi 5791.
MGIi MGI:97813. Ptpre.

Phylogenomic databases

eggNOGi COG5599.
GeneTreei ENSGT00760000118900.
HOVERGENi HBG053758.
InParanoidi P49446.
KOi K18033.
OMAi IVIDAMI.
OrthoDBi EOG7B31M8.
PhylomeDBi P49446.
TreeFami TF351829.

Miscellaneous databases

ChiTaRSi Ptpre. mouse.
NextBioi 296146.
PROi P49446.
SOURCEi Search...

Gene expression databases

Bgeei P49446.
CleanExi MM_PTPRE.
Genevestigatori P49446.

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. "Protein-tyrosine phosphatase epsilon. An isoform specifically expressed in mouse mammary tumors initiated by v-Ha-ras OR neu."
    Elson A., Leder P.
    J. Biol. Chem. 270:26116-26122(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: FVB/N.
  2. "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] (ISOFORM 2), INDUCTION, TISSUE SPECIFICITY.
  3. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, TISSUE SPECIFICITY.
    Tissue: Osteoclast.
  4. Mukouyama Y.
    Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: DBA/2.
  5. Hou E.W., Li S.L.
    Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Strain: C57BL/6.
    Tissue: Brain and Lung.
  6. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Strain: NOD.
  7. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "Identification and typing of members of the protein-tyrosine phosphatase gene family expressed in mouse brain."
    Schepens J., Zeeuwen P., Wieringa B., Hendriks W.
    Mol. Biol. Rep. 16:241-248(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
    Strain: BALB/c.
    Tissue: Brain.
  9. "Identification of novel protein tyrosine phosphatases of hematopoietic cells by polymerase chain reaction amplification."
    Yi T., Cleveland J.L., Ihle J.N.
    Blood 78:2222-2228(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-332, TISSUE SPECIFICITY.
    Strain: BALB/c.
    Tissue: Myeloid leukemia cell.
  10. "A novel receptor-type protein tyrosine phosphatase with a single catalytic domain is specifically expressed in mouse brain."
    Hendriks W., Schepens J., Brugman C., Zeeuwen P., Wieringa B.
    Biochem. J. 305:499-504(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 224-332.
    Strain: BALB/c.
    Tissue: Brain.
  11. "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.
  12. "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.
  13. "Dimerization in vivo and inhibition of the nonreceptor form of protein tyrosine phosphatase epsilon."
    Toledano-Katchalski H., Tiran Z., Sines T., Shani G., Granot-Attas S., den Hertog J., Elson A.
    Mol. Cell. Biol. 23:5460-5471(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, DOMAIN.
  14. "Quantitative time-resolved phosphoproteomic analysis of mast cell signaling."
    Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y., Kawakami T., Salomon A.R.
    J. Immunol. 179:5864-5876(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Mast cell.
  15. "Cytosolic protein tyrosine phosphatase-epsilon is a negative regulator of insulin signaling in skeletal muscle."
    Aga-Mizrachi S., Brutman-Barazani T., Jacob A.I., Bak A., Elson A., Sampson S.R.
    Endocrinology 149:605-614(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 2), SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  16. "PTPepsilon has a critical role in signaling transduction pathways and phosphoprotein network topology in red cells."
    De Franceschi L., Biondani A., Carta F., Turrini F., Laudanna C., Deana R., Brunati A.M., Turretta L., Iolascon A., Perrotta S., Elson A., Bulato C., Brugnara C.
    Proteomics 8:4695-4708(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  17. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-695, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Protein tyrosine phosphatase epsilon is a negative regulator of FcepsilonRI-mediated mast cell responses."
    Akimoto M., Mishra K., Lim K.-T., Tani N., Hisanaga S.-I., Katagiri T., Elson A., Mizuno K., Yakura H.
    Scand. J. Immunol. 69:401-411(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiPTPRE_MOUSE
AccessioniPrimary (citable) accession number: P49446
Secondary accession number(s): Q3U369
, Q60986, Q61042, Q62134, Q62444, Q64496
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: December 15, 2009
Last modified: November 26, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3