SubmitCancel

Skip Header

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

Q64455

- PTPRJ_MOUSE

UniProt

Q64455 - PTPRJ_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 eta
Gene
Ptprj, Byp, Scc1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Tyrosine phosphatase which dephosphorylates or contributes to the dephosphorylation of CTNND1, FLT3, PDGFRB, MET, RET, KDR, LYN, SRC, MAPK1, MAPK3, EGFR, TJP1, OCLN, PIK3R1 and PIK3R2. Plays a role in cell adhesion, migration, proliferation and differentiation. Involved in vascular development. May be involved in the mechanism of contact inhibition of cell growth. Regulator of macrophage adhesion and spreading. Positively affects cell-matrix adhesion. Positive regulator of platelet activation and thrombosis. Negative regulator of cell proliferation. Negative regulator of PDGF-stimulated cell migration; through dephosphorylation of PDGFR. Positive regulator of endothelial cell survival, as well as of VEGF-induced SRC and AKT activation; through KDR dephosphorylation. Negative regulator of EGFR signaling pathway; through EGFR dephosphorylation. Enhances the barrier function of epithelial junctions during reassembly. Negatively regulates T-cell receptor (TCR) signaling. Upon T-cell TCR activation, it is up-regulated and excluded from the immunological synapses, while upon T-cell-antigen presenting cells (APC) disengagement, it is no longer excluded and can dephosphorylate PLCG1 and LAT to down-regulate prolongation of signaling.7 Publications

Catalytic activityi

Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1106 – 11061Substrate By similarity
Active sitei1140 – 11401Phosphocysteine intermediate By similarity
Binding sitei1184 – 11841Substrate By similarity

GO - Molecular functioni

  1. phosphatase activity Source: UniProtKB
  2. protein tyrosine phosphatase activity Source: UniProtKB

GO - Biological processi

  1. blood coagulation Source: UniProtKB
  2. heart development Source: MGI
  3. negative regulation of MAP kinase activity Source: UniProtKB
  4. negative regulation of T cell receptor signaling pathway Source: UniProtKB
  5. negative regulation of cell growth Source: Ensembl
  6. negative regulation of cell migration Source: UniProtKB
  7. negative regulation of cell proliferation Source: UniProtKB
  8. negative regulation of epidermal growth factor receptor signaling pathway Source: UniProtKB
  9. negative regulation of platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  10. negative regulation of protein kinase B signaling Source: UniProtKB
  11. negative regulation of receptor activity Source: UniProtKB
  12. negative regulation of vascular permeability Source: Ensembl
  13. oligodendrocyte differentiation Source: MGI
  14. platelet-derived growth factor receptor signaling pathway Source: UniProtKB
  15. positive chemotaxis Source: Ensembl
  16. positive regulation of cell-matrix adhesion Source: UniProtKB
  17. positive regulation of focal adhesion assembly Source: UniProtKB
  18. positive regulation of macrophage chemotaxis Source: UniProtKB
  19. positive regulation of platelet activation Source: UniProtKB
  20. positive regulation of protein kinase B signaling Source: Ensembl
  21. vasculogenesis Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protein phosphatase

Names & Taxonomyi

Protein namesi
Recommended name:
Receptor-type tyrosine-protein phosphatase eta (EC:3.1.3.48)
Short name:
Protein-tyrosine phosphatase eta
Short name:
R-PTP-eta
Alternative name(s):
HPTP beta-like tyrosine phosphatase
Protein-tyrosine phosphatase receptor type J
Short name:
R-PTP-J
Susceptibility to colon cancer 1
CD_antigen: CD148
Gene namesi
Name:Ptprj
Synonyms:Byp, Scc1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Unplaced

Organism-specific databases

MGIiMGI:104574. Ptprj.

Subcellular locationi

Cell membrane; Single-pass type I membrane protein. Cell projectionruffle membrane. Cell junction
Note: After T-cell stimulation, it is temporarily excluded from immunological synapses. Found at cell borders.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini29 – 876848Extracellular Reviewed prediction
Add
BLAST
Transmembranei877 – 89721Helical; Reviewed prediction
Add
BLAST
Topological domaini898 – 1238341Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. cell surface Source: Ensembl
  2. cell-cell junction Source: UniProtKB
  3. immunological synapse Source: UniProtKB
  4. integral component of membrane Source: UniProtKB-KW
  5. plasma membrane Source: UniProtKB
  6. ruffle membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1106 – 11061D → A: Substrate trapping with much higher affinity for substrate. 1 Publication
Mutagenesisi1140 – 11401C → S: Catalytically inactive and substrate trapping with higher affinity for substrate. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828 Reviewed prediction
Add
BLAST
Chaini29 – 12381210Receptor-type tyrosine-protein phosphatase eta
PRO_0000025445Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi62 – 621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi78 – 781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi85 – 851N-linked (GlcNAc...) Reviewed prediction
Glycosylationi90 – 901N-linked (GlcNAc...) Reviewed prediction
Glycosylationi110 – 1101N-linked (GlcNAc...) Reviewed prediction
Glycosylationi114 – 1141N-linked (GlcNAc...) Reviewed prediction
Glycosylationi145 – 1451N-linked (GlcNAc...)1 Publication
Glycosylationi164 – 1641N-linked (GlcNAc...) Reviewed prediction
Glycosylationi173 – 1731N-linked (GlcNAc...) Reviewed prediction
Glycosylationi182 – 1821N-linked (GlcNAc...) Reviewed prediction
Glycosylationi198 – 1981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi207 – 2071N-linked (GlcNAc...) Reviewed prediction
Glycosylationi244 – 2441N-linked (GlcNAc...) Reviewed prediction
Glycosylationi253 – 2531N-linked (GlcNAc...) Reviewed prediction
Glycosylationi267 – 2671N-linked (GlcNAc...) Reviewed prediction
Glycosylationi278 – 2781N-linked (GlcNAc...) Reviewed prediction
Glycosylationi313 – 3131N-linked (GlcNAc...)1 Publication
Glycosylationi317 – 3171N-linked (GlcNAc...)1 Publication
Glycosylationi333 – 3331N-linked (GlcNAc...) Reviewed prediction
Glycosylationi366 – 3661N-linked (GlcNAc...) Reviewed prediction
Glycosylationi379 – 3791N-linked (GlcNAc...) Reviewed prediction
Glycosylationi398 – 3981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi403 – 4031N-linked (GlcNAc...) Reviewed prediction
Glycosylationi437 – 4371N-linked (GlcNAc...) Reviewed prediction
Glycosylationi452 – 4521N-linked (GlcNAc...) Reviewed prediction
Glycosylationi488 – 4881N-linked (GlcNAc...) Reviewed prediction
Glycosylationi506 – 5061N-linked (GlcNAc...) Reviewed prediction
Glycosylationi538 – 5381N-linked (GlcNAc...)1 Publication
Glycosylationi572 – 5721N-linked (GlcNAc...) Reviewed prediction
Glycosylationi576 – 5761N-linked (GlcNAc...) Reviewed prediction
Glycosylationi662 – 6621N-linked (GlcNAc...) Reviewed prediction
Glycosylationi668 – 6681N-linked (GlcNAc...) Reviewed prediction
Glycosylationi685 – 6851N-linked (GlcNAc...) Reviewed prediction
Glycosylationi691 – 6911N-linked (GlcNAc...) Reviewed prediction
Glycosylationi725 – 7251N-linked (GlcNAc...) Reviewed prediction
Glycosylationi811 – 8111N-linked (GlcNAc...) Reviewed prediction
Glycosylationi838 – 8381N-linked (GlcNAc...) Reviewed prediction

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ64455.
PaxDbiQ64455.
PRIDEiQ64455.

PTM databases

PhosphoSiteiQ64455.

Expressioni

Tissue specificityi

Expressed at high levels in brain, kidney, spleen and intestine, and at lower levels in liver, lung, thymus and heart. Expressed at a high level in the myeloid cell line FDC-P2, and at a lower level in the pre-B lymphoid cell line WEHI-231 and the T hybridoma cell line HB21.7.31. Not expressed in the fibroblast cell line NIH3T3 or the erythroid cell line F5-5. Expressed in macrophages.3 Publications

Developmental stagei

Expressed at 11.5 dpc in presumptive macrophages concentrated in the liver and scattered throughout the embryonic mesenchyme. Expressed at 11.5 and 12.5 dpc in the developing eye and in the ganglia and processes of cranial and spinal nerves constituting the PNS.1 Publication

Gene expression databases

ArrayExpressiQ64455.
BgeeiQ64455.
CleanExiMM_PTPRJ.
GenevestigatoriQ64455.

Interactioni

Subunit structurei

Monomer. Interacts with CTNNB1 (phosphorylated) and JUP (phosphorylated). Interacts with FLT3 (phosphorylated). Interacts with GAB1 and GRB2 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ64455.
SMRiQ64455. Positions 44-108, 126-154, 217-605, 716-758, 919-1204.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini39 – 12284Fibronectin type-III 1
Add
BLAST
Domaini170 – 26697Fibronectin type-III 2
Add
BLAST
Domaini270 – 35889Fibronectin type-III 3
Add
BLAST
Domaini359 – 44385Fibronectin type-III 4
Add
BLAST
Domaini444 – 52784Fibronectin type-III 5
Add
BLAST
Domaini528 – 62194Fibronectin type-III 6
Add
BLAST
Domaini622 – 71897Fibronectin type-III 7
Add
BLAST
Domaini717 – 80387Fibronectin type-III 8
Add
BLAST
Domaini942 – 1199258Tyrosine-protein phosphatase
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1140 – 11467Substrate binding By similarity

Sequence similaritiesi

Keywords - Domaini

Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5599.
HOGENOMiHOG000232054.
HOVERGENiHBG053761.
InParanoidiQ541R5.
KOiK05698.

Family and domain databases

Gene3Di2.60.40.10. 7 hits.
3.90.190.10. 1 hit.
InterProiIPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view]
PfamiPF00041. fn3. 4 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view]
PRINTSiPR00700. PRTYPHPHTASE.
SMARTiSM00060. FN3. 8 hits.
SM00194. PTPc. 1 hit.
[Graphical view]
SUPFAMiSSF49265. SSF49265. 5 hits.
SSF52799. SSF52799. 1 hit.
PROSITEiPS50853. FN3. 6 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q64455-1 [UniParc]FASTAAdd to Basket

« Hide

MKPAARETRT PPRSPGLRWA LLPLLLLLRQ GQVLCAGAAP NPIFDIEAVV     50
SPTSVLLTWK HNDSGASECR IENKMESNLT FPVKNQTSCN ITGLSPGTSY 100
TFSIISVTTN ETLNKTITTE PWPVSDLHVT SVGVTQARLT WSNANGTASY 150
RMLIEELTTH SSVNISGLKP GTNNSFAFPE SNETQADFAV AEEVPDANGT 200
KRIPVTNLSQ LHKNSLVSVD PPSGQDPSLT EILLTDLKPD TQYNATIYSQ 250
AANGTEGQPR NKVFKTNSTQ VSDVRAMNIS ASSMTLTWKS NYDGSRTSIV 300
YKIHVAGGTH SVNQTVNKTE AIILGLSSST LYNITVHPFL GQTEGTPGFL 350
QVYTSPDQVS DFRVTNVSTR AIGLAWRSND SKSFEIFIKQ DGGEKHRNAS 400
TGNQSYMVED LKPGTSYHFE IIPRGPDGTE GLSSTVNGST DPSAVTDIRV 450
VNISTTEMQL EWQNTDDASG YTYHLVLESK SGSIIRTNSS QKWITVGSLT 500
PGTLYNVTIF PEVDQIQGIS NSITQYTRPS SVSHIEVNTT TTTAAIRWKN 550
EDAASASYAY SVLILKTGDG SNVTSNFTKD PSILIPELIP GVSYTVKILT 600
QVGDGTTSLV PGWNLFCTEP EPVTSFHCEV VPKEPALVLK WACPFGMYTG 650
FELGVRSDSW DNMTRLENCT SDDDTECRTE VAYLNFSTSY NISIATLSCG 700
KMALPAQNIC TTGITDPPTP DGSPNITSVS HNSVKVKFSG FEASHGPIKA 750
YAVILTTGEA AQPSADVLKY TYEDFKRGAS DTYVTYLIRI EEKGQSQGLS 800
EVLNYEIDVG NQSTTLGYYN GRLEPLGSYR ACVAGFTNIT YNLQNDGLIN 850
GDESYVSFSP YSEAVFLPQD PGVICGAVFG CIFGALAITA VGGFIFWRKK 900
RTDAKNNEVS FSQIKPKKSK LIRVENFEAY FKKQQADSNC GFAEEYEDLK 950
LIGISLPKYT AEIAENRGKN RYNNVLPYDI SRVKLSVQTH STDDYINANY 1000
MPGYHSKKDF IATQGPLPNT LKDFWRMVWE KNVYAIVMLT KCVEQGRTKC 1050
EEYWPSKQAQ DYGDITVAMT SEVVLPEWTI RDFVVKNMQN SESHPLRQFH 1100
FTSWPDHGVP DTTDLLINFR YLVRDYMKQI PPESPILVHC SAGVGRTGTF 1150
IAIDRLIYQI ENENTVDVYG IVYDLRMHRP LMVQTEDQYV FLNQCVLDII 1200
RAQKDSKVDL IYQNTTAMTI YENLEPVSMF GKTNGYIA 1238
Length:1,238
Mass (Da):136,769
Last modified:December 15, 2009 - v2
Checksum:iE525D346A2C60335
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti175 – 1751S → T in BAA08146. 1 Publication
Sequence conflicti175 – 1751S → T in AAK96030. 1 Publication
Sequence conflicti175 – 1751S → T in AAK98640. 1 Publication
Sequence conflicti211 – 2111L → P in AAK98640. 1 Publication
Sequence conflicti217 – 2171V → A in AAK98640. 1 Publication
Sequence conflicti463 – 4631Q → H in BAE27842. 1 Publication
Sequence conflicti553 – 5531A → T in AAK98640. 1 Publication
Sequence conflicti622 – 6221P → S in AAK98640. 1 Publication
Sequence conflicti1061 – 10611D → E in AAK98640. 1 Publication
Sequence conflicti1126 – 11261Y → D in AAN11409. 1 Publication
Sequence conflicti1133 – 11331E → K in AAN11409. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D45212 mRNA. Translation: BAA08146.1.
AY038877, AY038861 Genomic DNA. Translation: AAN11409.1.
AY038891 mRNA. Translation: AAK96030.1.
AY039232 mRNA. Translation: AAK98640.1.
DQ133576 mRNA. Translation: ABA07808.1.
AK147318 mRNA. Translation: BAE27842.1.
AK147556 mRNA. Translation: BAE27993.1.
PIRiS68700.
RefSeqiNP_033008.3. NM_008982.5.
UniGeneiMm.330393.

Genome annotation databases

GeneIDi19271.
KEGGimmu:19271.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D45212 mRNA. Translation: BAA08146.1 .
AY038877 , AY038861 Genomic DNA. Translation: AAN11409.1 .
AY038891 mRNA. Translation: AAK96030.1 .
AY039232 mRNA. Translation: AAK98640.1 .
DQ133576 mRNA. Translation: ABA07808.1 .
AK147318 mRNA. Translation: BAE27842.1 .
AK147556 mRNA. Translation: BAE27993.1 .
PIRi S68700.
RefSeqi NP_033008.3. NM_008982.5.
UniGenei Mm.330393.

3D structure databases

ProteinModelPortali Q64455.
SMRi Q64455. Positions 44-108, 126-154, 217-605, 716-758, 919-1204.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q64455.

Proteomic databases

MaxQBi Q64455.
PaxDbi Q64455.
PRIDEi Q64455.

Protocols and materials databases

DNASUi 19271.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 19271.
KEGGi mmu:19271.

Organism-specific databases

CTDi 5795.
MGIi MGI:104574. Ptprj.

Phylogenomic databases

eggNOGi COG5599.
HOGENOMi HOG000232054.
HOVERGENi HBG053761.
InParanoidi Q541R5.
KOi K05698.

Miscellaneous databases

NextBioi 296158.
PROi Q64455.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q64455.
Bgeei Q64455.
CleanExi MM_PTPRJ.
Genevestigatori Q64455.

Family and domain databases

Gene3Di 2.60.40.10. 7 hits.
3.90.190.10. 1 hit.
InterProi IPR003961. Fibronectin_type3.
IPR013783. Ig-like_fold.
IPR029021. Prot-tyrosine_phosphatase-like.
IPR000387. Tyr/Dual-sp_Pase.
IPR016130. Tyr_Pase_AS.
IPR000242. Tyr_Pase_rcpt/non-rcpt.
[Graphical view ]
Pfami PF00041. fn3. 4 hits.
PF00102. Y_phosphatase. 1 hit.
[Graphical view ]
PRINTSi PR00700. PRTYPHPHTASE.
SMARTi SM00060. FN3. 8 hits.
SM00194. PTPc. 1 hit.
[Graphical view ]
SUPFAMi SSF49265. SSF49265. 5 hits.
SSF52799. SSF52799. 1 hit.
PROSITEi PS50853. FN3. 6 hits.
PS00383. TYR_PHOSPHATASE_1. 1 hit.
PS50056. TYR_PHOSPHATASE_2. 1 hit.
PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and characterization of Byp, a murine receptor-type tyrosine phosphatase similar to human DEP-1."
    Kuramochi S., Matsuda S., Matsuda Y., Saitoh T., Ohsugi M., Yamamoto T.
    FEBS Lett. 378:7-14(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: MRL-LPR/LPR.
    Tissue: Lymph node.
  2. Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
    Strain: 129/SvSl and BALB/c.
  3. "Phenotypic consequences of the germ-line loss of the putative tumor suppressor Ptprj (Scc1)."
    Csikos T., Snoek M., de Boer T., Drenth T., Krimpenfort P., van Amerongen R., Zevenhoven J., van der Valk M., Hellberg C., Ostman A., Demant P., Berns A.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 129P2.
  4. "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].
    Strain: C57BL/6 and C57BL/6J.
    Tissue: Brain.
  5. "Identification of novel protein-tyrosine phosphatases in a human leukemia cell line, F-36P."
    Honda H., Shibuya M., Chiba S., Yazaki Y., Hirai H.
    Leukemia 7:742-746(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY.
  6. "Murine DEP-1, a receptor protein tyrosine phosphatase, is expressed in macrophages and is regulated by CSF-1 and LPS."
    Osborne J.M., den Elzen N., Lichanska A.M., Costelloe E.O., Yamada T., Cassady A.I., Hume D.A.
    J. Leukoc. Biol. 64:692-701(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  7. "Contact inhibition of VEGF-induced proliferation requires vascular endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148."
    Grazia Lampugnani M., Zanetti A., Corada M., Takahashi T., Balconi G., Breviario F., Orsenigo F., Cattelino A., Kemler R., Daniel T.O., Dejana E.
    J. Cell Biol. 161:793-804(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF ASP-1106 AND CYS-1140.
  8. "The tyrosine phosphatase CD148 is excluded from the immunologic synapse and down-regulates prolonged T cell signaling."
    Lin J., Weiss A.
    J. Cell Biol. 162:673-682(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  9. Cited for: FUNCTION.
  10. "The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell-matrix adhesion."
    Jandt E., Denner K., Kovalenko M., Ostman A., Bohmer F.D.
    Oncogene 22:4175-4185(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF CYS-1140.
  11. "Structurally distinct phosphatases CD45 and CD148 both regulate B cell and macrophage immunoreceptor signaling."
    Zhu J.W., Brdicka T., Katsumoto T.R., Lin J., Weiss A.
    Immunity 28:183-196(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "The tyrosine phosphatase CD148 is an essential positive regulator of platelet activation and thrombosis."
    Senis Y.A., Tomlinson M.G., Ellison S., Mazharian A., Lim J., Zhao Y., Kornerup K.N., Auger J.M., Thomas S.G., Dhanjal T., Kalia N., Zhu J.W., Weiss A., Watson S.P.
    Blood 113:4942-4954(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "CD148/DEP-1 association with areas of cytoskeletal organisation in macrophages."
    Dave R.K., Hume D.A., Elsegood C., Kellie S.
    Exp. Cell Res. 315:1734-1744(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  14. "Mass-spectrometric identification and relative quantification of N-linked cell surface glycoproteins."
    Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., Schiess R., Aebersold R., Watts J.D.
    Nat. Biotechnol. 27:378-386(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-145; ASN-313; ASN-317 AND ASN-538.

Entry informationi

Entry nameiPTPRJ_MOUSE
AccessioniPrimary (citable) accession number: Q64455
Secondary accession number(s): Q3UH64
, Q3UHL5, Q541R5, Q8CIW9, Q8K3Q2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 2009
Last modified: September 3, 2014
This is version 127 of the entry and version 2 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

Similar proteinsi