Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

B2RU80

- PTPRB_MOUSE

UniProt

B2RU80 - PTPRB_MOUSE

Protein

Receptor-type tyrosine-protein phosphatase beta

Gene

Ptprb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 56 (01 Oct 2014)
      Sequence version 1 (01 Jul 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Plays an important role in blood vessel remodeling and angiogenesis. Not necessary for the initial formation of blood vessels, but is essential for their maintenance and remodeling. Can induce dephosphorylation of TEK/TIE2, CDH5/VE-cadherin and KDR/VEGFR-2. Regulates angiopoietin-TIE2 signaling in endothelial cells. Acts as a negative regulator of TIE2, and controls TIE2 driven endothelial cell proliferation, which in turn affects blood vessel remodeling during embryonic development and determines blood vessel size during perinatal growth. Essential for the maintenance of endothelial cell contact integrity and for the adhesive function of VE-cadherin in endothelial cells and this requires the presence of plakoglobin.6 Publications

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1871 – 18711SubstrateBy similarity
    Active sitei1905 – 19051Phosphocysteine intermediatePROSITE-ProRule annotation
    Binding sitei1949 – 19491SubstrateBy similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein tyrosine phosphatase activity Source: UniProtKB-EC

    GO - Biological processi

    1. angiogenesis Source: UniProtKB
    2. dephosphorylation Source: UniProtKB

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase

    Keywords - Biological processi

    Angiogenesis

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase beta (EC:3.1.3.48)
    Short name:
    Protein-tyrosine phosphatase beta
    Short name:
    R-PTP-beta
    Alternative name(s):
    Vascular endothelial protein tyrosine phosphatase
    Short name:
    VE-PTP
    Gene namesi
    Name:Ptprb
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 10

    Organism-specific databases

    MGIiMGI:97809. Ptprb.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. receptor complex Source: MGI

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Disruption phenotypei

    Mice show severe cardiovascular defects and embryonic lethality by E10. Vasculogenesis occurs normally however, angiogenesis is abnormal. Angiogenic defects are most pronounced in the yolk sac and include a complete failure to elaborate the primitive vascular scaffold into higher-order branched arteries, veins, and capillaries.1 Publication

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1911 – 19111R → A: Loss of activity and dephosphorylation of CDH5. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Sequence AnalysisAdd
    BLAST
    Chaini23 – 19981976Receptor-type tyrosine-protein phosphatase betaPRO_0000390401Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi28 – 281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi53 – 531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi173 – 1731N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi199 – 1991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi268 – 2681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi415 – 4151N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi422 – 4221N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi480 – 4801N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi575 – 5751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi599 – 5991N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi653 – 6531N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi830 – 8301N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1041 – 10411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1097 – 10971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1164 – 11641N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1186 – 11861N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1213 – 12131N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1275 – 12751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1368 – 13681N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1471 – 14711N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1475 – 14751N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1519 – 15191N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    PaxDbiB2RU80.
    PRIDEiB2RU80.

    PTM databases

    PhosphoSiteiB2RU80.

    Expressioni

    Tissue specificityi

    Expression is very high in the vasculature of lung, spleen, and kidney, as well as in the heart valves, and is also present in the endothelium of arterioles and venules. Also expressed in tumor vasculature.3 Publications

    Developmental stagei

    Expressed in both arterial and venous vascular endothelium in embryos, although more strongly in arterial vessels. Highly expressed in the developing outflow tract of the heart and later is expressed in developing heart valves.3 Publications

    Gene expression databases

    ArrayExpressiB2RU80.
    BgeeiB2RU80.
    GenevestigatoriB2RU80.

    Interactioni

    Subunit structurei

    Monomer By similarity. Interacts with TEK. Interacts via fibronectin type-III 17 domain with CDH5.By similarity4 Publications

    Protein-protein interaction databases

    IntActiB2RU80. 1 interaction.
    MINTiMINT-8298798.

    Structurei

    3D structure databases

    ProteinModelPortaliB2RU80.
    SMRiB2RU80. Positions 31-1434, 1688-1968.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini23 – 16221600ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1644 – 1997354CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1623 – 164321HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini23 – 10987Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini113 – 20694Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini207 – 29185Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini292 – 38493Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini378 – 46689Fibronectin type-III 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini470 – 55687Fibronectin type-III 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini557 – 64286Fibronectin type-III 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini643 – 73391Fibronectin type-III 8PROSITE-ProRule annotationAdd
    BLAST
    Domaini734 – 82188Fibronectin type-III 9PROSITE-ProRule annotationAdd
    BLAST
    Domaini822 – 91392Fibronectin type-III 10PROSITE-ProRule annotationAdd
    BLAST
    Domaini908 – 99487Fibronectin type-III 11PROSITE-ProRule annotationAdd
    BLAST
    Domaini995 – 108894Fibronectin type-III 12PROSITE-ProRule annotationAdd
    BLAST
    Domaini1086 – 117388Fibronectin type-III 13PROSITE-ProRule annotationAdd
    BLAST
    Domaini1176 – 126388Fibronectin type-III 14PROSITE-ProRule annotationAdd
    BLAST
    Domaini1264 – 135794Fibronectin type-III 15PROSITE-ProRule annotationAdd
    BLAST
    Domaini1358 – 144992Fibronectin type-III 16PROSITE-ProRule annotationAdd
    BLAST
    Domaini1449 – 1551103Fibronectin type-III 17PROSITE-ProRule annotationAdd
    BLAST
    Domaini1704 – 1964261Tyrosine-protein phosphatasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1905 – 19117Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 17 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 tyrosine-protein phosphatase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00750000117631.
    HOGENOMiHOG000060224.
    HOVERGENiHBG053759.
    InParanoidiQ3UGZ7.
    KOiK05694.
    OMAiPEQQHPL.
    OrthoDBiEOG7PCJFZ.
    PhylomeDBiB2RU80.
    TreeFamiTF351926.

    Family and domain databases

    Gene3Di2.60.40.10. 15 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. 15 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view]
    PRINTSiPR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 16 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 16 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEiPS50853. FN3. 12 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.

    B2RU80-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLRHGALTAL WITLSVVQTG VAEQVKCNFT LLESRVSSLS ASIQWRTFAS     50
    PCNFSLIYSS DTSGPMWCHP IRIDNFTYGC NPKDLQAGTV YNFRIVSLDG 100
    EESTLVLQTD PLPPARFEVN REKTASTTLQ VRWTPSSGKV SWYEVQLFDH 150
    NNQKIQEVQV QESTTWSQYT FLNLTEGNSY KVAITAVSGE KRSFPVYING 200
    STVPSPVKDL GISPNPNSLL ISWSRGSGNV EQYRLVLMDK GAIVQDTNVD 250
    RRDTSYAFHE LTPGHLYNLT IVTMASGLQN SRWKLVRTAP MEVSNLKVTN 300
    DGRLTSLNVK WQKPPGDVDS YSITLSHQGT IKESKTLAPP VTETQFKDLV 350
    PGRLYQVTIS CISGELSAEK SAAGRTVPEK VRNLVSYNEI WMKSFTVNWT 400
    PPAGDWEHYR IVLFNESLVL LNTTVGKEET HYALDGLELI PGRQYEIEVI 450
    VESGNLRNSE RCQGRTVPLA VLQLRVKHAN ETSLGITWRA PLGEWEKYII 500
    SLMDRELLVI HKSLSKDAKE FTFTDLMPGR NYKATVTSMS GDLKQSSSIK 550
    GRTVPAQVTD LHVNNQGMTS SLFTNWTKAL GDVEFYQVLL IHENVVVKNE 600
    SVSSDTSRYS FRALKPGSLY SVVVTTVSGG ISSRQVVAEG RTVPSSVSGV 650
    TVNNSGRNDY LSVSWLPAPG EVDHYVVSLS HEGKVDQFLI IAKSVSECSF 700
    SSLTPGRLYN VTVTTKSGNY ASHSFTEERT VPDKVQGISV SNSARSDYLK 750
    VSWVHATGDF DHYEVTIKNR ESFIQTKTIP KSENECEFIE LVPGRLYSVT 800
    VSTKSGQYEA SEQGTGRTIP EPVKDLTLLN RSTEDLHVTW SRANGDVDQY 850
    EVQLLFNDMK VFPHIHLVNT ATEYKFTALT PGRHYKILVL TISGDVQQSA 900
    FIEGLTVPST VKNIHISANG ATDRLMVTWS PGGGDVDSYV VSAFRQDEKV 950
    DSQTIPKHAS EHTFHRLEAG AKYRIAIVSV SGSLRNQIDA LGQTVPASVQ 1000
    GVVAANAYSS NSLTVSWQKA LGVAERYDIL LLNENGLLLS NVSEPATARQ 1050
    HKFEDLTPGK KYKMQILTVS GGLFSKESQA EGRTVPAAVT NLRITENSSR 1100
    YLSFGWTASE GELSWYNIFL YNPDRTLQER AQVDPLVQSF SFQNLLQGRM 1150
    YKMVIVTHSG ELSNESFIFG RTVPAAVNHL KGSHRNTTDS LWFSWSPASG 1200
    DFDFYELILY NPNGTKKENW KEKDVTEWRF QGLVPGRKYT LYVVTHSGDL 1250
    SNKVTGEGRT APSPPSLLSF ADVANTSLAI TWKGPPDWTD YNDFELQWFP 1300
    GDALTIFNPY SSRKSEGRIV YGLHPGRSYQ FSVKTVSGDS WKTYSKPISG 1350
    SVRTKPDKIQ NLHCRPQNST AIACSWIPPD SDFDGYSIEC RKMDTQEIEF 1400
    SRKLEKEKSL LNIMMLVPHK RYLVSIKVQS AGMTSEVVED STITMIDRPP 1450
    QPPPHIRVNE KDVLISKSSI NFTVNCSWFS DTNGAVKYFA VVVREADSMD 1500
    ELKPEQQHPL PSYLEYRHNA SIRVYQTNYF ASKCAESPDS SSKSFNIKLG 1550
    AEMDSLGGKC DPSQQKFCDG PLKPHTAYRI SIRAFTQLFD EDLKEFTKPL 1600
    YSDTFFSMPI TTESEPLFGV IEGVSAGLFL IGMLVALVAF FICRQKASHS 1650
    RERPSARLSI RRDRPLSVHL NLGQKGNRKT SCPIKINQFE GHFMKLQADS 1700
    NYLLSKEYED LKDVGRSQSC DIALLPENRG KNRYNNILPY DASRVKLCNV 1750
    DDDPCSDYIN ASYIPGNNFR REYIATQGPL PGTKDDFWKM AWEQNVHNIV 1800
    MVTQCVEKGR VKCDHYWPAD QDPLYYGDLI LQMVSESVLP EWTIREFKIC 1850
    SEEQLDAHRL IRHFHYTVWP DHGVPETTQS LIQFVRTVRD YINRSPGAGP 1900
    TVVHCSAGVG RTGTFVALDR ILQQLDSKDS VDIYGAVHDL RLHRVHMVQT 1950
    ECQYVYLHQC VRDVLRAKKL RNEQENPLFP IYENVNPEYH RDAIYSRH 1998
    Length:1,998
    Mass (Da):224,495
    Last modified:July 1, 2008 - v1
    Checksum:i066EE7141F942887
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti647 – 6471V → A in BAE28060. (PubMed:16141072)Curated
    Sequence conflicti647 – 6471V → A in BAE27912. (PubMed:16141072)Curated
    Sequence conflicti906 – 9061T → P in AAL75813. (PubMed:12234928)Curated
    Sequence conflicti1037 – 10371L → F in BAE28060. (PubMed:16141072)Curated
    Sequence conflicti1037 – 10371L → F in BAE27912. (PubMed:16141072)Curated
    Sequence conflicti1168 – 11681I → V in BAE28060. (PubMed:16141072)Curated
    Sequence conflicti1168 – 11681I → V in BAE27912. (PubMed:16141072)Curated
    Sequence conflicti1748 – 17481C → S in AAL75813. (PubMed:12234928)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY077755 mRNA. Translation: AAL75813.1.
    AK147439 mRNA. Translation: BAE27912.1.
    AK147668 mRNA. Translation: BAE28060.1.
    CH466539 Genomic DNA. Translation: EDL21786.1.
    BC141006 mRNA. Translation: AAI41007.1.
    BC145111 mRNA. Translation: AAI45112.1.
    CCDSiCCDS36063.1.
    RefSeqiNP_084204.2. NM_029928.2.
    UniGeneiMm.37213.
    Mm.489025.

    Genome annotation databases

    EnsembliENSMUST00000092167; ENSMUSP00000089805; ENSMUSG00000020154.
    GeneIDi19263.
    KEGGimmu:19263.
    UCSCiuc007hbv.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY077755 mRNA. Translation: AAL75813.1 .
    AK147439 mRNA. Translation: BAE27912.1 .
    AK147668 mRNA. Translation: BAE28060.1 .
    CH466539 Genomic DNA. Translation: EDL21786.1 .
    BC141006 mRNA. Translation: AAI41007.1 .
    BC145111 mRNA. Translation: AAI45112.1 .
    CCDSi CCDS36063.1.
    RefSeqi NP_084204.2. NM_029928.2.
    UniGenei Mm.37213.
    Mm.489025.

    3D structure databases

    ProteinModelPortali B2RU80.
    SMRi B2RU80. Positions 31-1434, 1688-1968.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi B2RU80. 1 interaction.
    MINTi MINT-8298798.

    PTM databases

    PhosphoSitei B2RU80.

    Proteomic databases

    PaxDbi B2RU80.
    PRIDEi B2RU80.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000092167 ; ENSMUSP00000089805 ; ENSMUSG00000020154 .
    GeneIDi 19263.
    KEGGi mmu:19263.
    UCSCi uc007hbv.2. mouse.

    Organism-specific databases

    CTDi 5787.
    MGIi MGI:97809. Ptprb.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00750000117631.
    HOGENOMi HOG000060224.
    HOVERGENi HBG053759.
    InParanoidi Q3UGZ7.
    KOi K05694.
    OMAi PEQQHPL.
    OrthoDBi EOG7PCJFZ.
    PhylomeDBi B2RU80.
    TreeFami TF351926.

    Miscellaneous databases

    NextBioi 296128.
    PROi B2RU80.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi B2RU80.
    Bgeei B2RU80.
    Genevestigatori B2RU80.

    Family and domain databases

    Gene3Di 2.60.40.10. 15 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. 15 hits.
    PF00102. Y_phosphatase. 1 hit.
    [Graphical view ]
    PRINTSi PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 16 hits.
    SM00194. PTPc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 16 hits.
    SSF52799. SSF52799. 1 hit.
    PROSITEi PS50853. FN3. 12 hits.
    PS00383. TYR_PHOSPHATASE_1. 1 hit.
    PS50056. TYR_PHOSPHATASE_2. 1 hit.
    PS50055. TYR_PHOSPHATASE_PTP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "VE-PTP and VE-cadherin ectodomains interact to facilitate regulation of phosphorylation and cell contacts."
      Nawroth R., Poell G., Ranft A., Kloep S., Samulowitz U., Fachinger G., Golding M., Shima D.T., Deutsch U., Vestweber D.
      EMBO J. 21:4885-4895(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH CDH5, DOMAIN, MUTAGENESIS OF ARG-1911.
      Strain: Swiss Webster / NIH.
    2. "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.
    3. 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].
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Brain.
    5. "Functional interaction of vascular endothelial-protein-tyrosine phosphatase with the angiopoietin receptor Tie-2."
      Fachinger G., Deutsch U., Risau W.
      Oncogene 18:5948-5953(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH TEK, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    6. "Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development."
      Bauemer S., Keller L., Holtmann A., Funke R., August B., Gamp A., Wolburg H., Wolburg-Buchholz K., Deutsch U., Vestweber D.
      Blood 107:4754-4762(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Vascular endothelial tyrosine phosphatase (VE-PTP)-null mice undergo vasculogenesis but die embryonically because of defects in angiogenesis."
      Dominguez M.G., Hughes V.C., Pan L., Simmons M., Daly C., Anderson K., Noguera-Troise I., Murphy A.J., Valenzuela D.M., Davis S., Thurston G., Yancopoulos G.D., Gale N.W.
      Proc. Natl. Acad. Sci. U.S.A. 104:3243-3248(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    8. "VE-PTP maintains the endothelial barrier via plakoglobin and becomes dissociated from VE-cadherin by leukocytes and by VEGF."
      Nottebaum A.F., Cagna G., Winderlich M., Gamp A.C., Linnepe R., Polaschegg C., Filippova K., Lyck R., Engelhardt B., Kamenyeva O., Bixel M.G., Butz S., Vestweber D.
      J. Exp. Med. 205:2929-2945(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CDH5.
    9. Cited for: FUNCTION, INTERACTION WITH TEK.

    Entry informationi

    Entry nameiPTPRB_MOUSE
    AccessioniPrimary (citable) accession number: B2RU80
    Secondary accession number(s): Q3UGZ7, Q8CIW2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 2009
    Last sequence update: July 1, 2008
    Last modified: October 1, 2014
    This is version 56 of the entry and version 1 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