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B2RU80

- PTPRB_MOUSE

UniProt

B2RU80 - PTPRB_MOUSE

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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

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei1871 – 18711Substrate By similarity
Active sitei1905 – 19051Phosphocysteine intermediate By similarity
Binding sitei1949 – 19491Substrate By 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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini23 – 16221600Extracellular Reviewed prediction
Add
BLAST
Transmembranei1623 – 164321Helical; Reviewed prediction
Add
BLAST
Topological domaini1644 – 1997354Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

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

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 – 2222 Reviewed prediction
Add
BLAST
Chaini23 – 19981976Receptor-type tyrosine-protein phosphatase beta
PRO_0000390401Add
BLAST

Amino acid modifications

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

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 CDH5.4 Publications

Protein-protein interaction databases

IntActiB2RU80. 1 interaction.
MINTiMINT-8298798.

Structurei

3D structure databases

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

Family & Domainsi

Domains and Repeats

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

Region

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

Sequence similaritiesi

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti647 – 6471V → A in BAE28060. 1 Publication
Sequence conflicti647 – 6471V → A in BAE27912. 1 Publication
Sequence conflicti906 – 9061T → P in AAL75813. 1 Publication
Sequence conflicti1037 – 10371L → F in BAE28060. 1 Publication
Sequence conflicti1037 – 10371L → F in BAE27912. 1 Publication
Sequence conflicti1168 – 11681I → V in BAE28060. 1 Publication
Sequence conflicti1168 – 11681I → V in BAE27912. 1 Publication
Sequence conflicti1748 – 17481C → S in AAL75813. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 55 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

Similar proteinsi