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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.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 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 – 16221600ExtracellularSequence AnalysisAdd
BLAST
Transmembranei1623 – 164321HelicalSequence AnalysisAdd
BLAST
Topological domaini1644 – 1997354CytoplasmicSequence AnalysisAdd
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 – 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

BgeeiB2RU80.
ExpressionAtlasiB2RU80. baseline and differential.
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...

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.
GeneTreeiENSGT00770000120452.
HOGENOMiHOG000060224.
HOVERGENiHBG053759.
InParanoidiB2RU80.
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

        10         20         30         40         50
MLRHGALTAL WITLSVVQTG VAEQVKCNFT LLESRVSSLS ASIQWRTFAS
60 70 80 90 100
PCNFSLIYSS DTSGPMWCHP IRIDNFTYGC NPKDLQAGTV YNFRIVSLDG
110 120 130 140 150
EESTLVLQTD PLPPARFEVN REKTASTTLQ VRWTPSSGKV SWYEVQLFDH
160 170 180 190 200
NNQKIQEVQV QESTTWSQYT FLNLTEGNSY KVAITAVSGE KRSFPVYING
210 220 230 240 250
STVPSPVKDL GISPNPNSLL ISWSRGSGNV EQYRLVLMDK GAIVQDTNVD
260 270 280 290 300
RRDTSYAFHE LTPGHLYNLT IVTMASGLQN SRWKLVRTAP MEVSNLKVTN
310 320 330 340 350
DGRLTSLNVK WQKPPGDVDS YSITLSHQGT IKESKTLAPP VTETQFKDLV
360 370 380 390 400
PGRLYQVTIS CISGELSAEK SAAGRTVPEK VRNLVSYNEI WMKSFTVNWT
410 420 430 440 450
PPAGDWEHYR IVLFNESLVL LNTTVGKEET HYALDGLELI PGRQYEIEVI
460 470 480 490 500
VESGNLRNSE RCQGRTVPLA VLQLRVKHAN ETSLGITWRA PLGEWEKYII
510 520 530 540 550
SLMDRELLVI HKSLSKDAKE FTFTDLMPGR NYKATVTSMS GDLKQSSSIK
560 570 580 590 600
GRTVPAQVTD LHVNNQGMTS SLFTNWTKAL GDVEFYQVLL IHENVVVKNE
610 620 630 640 650
SVSSDTSRYS FRALKPGSLY SVVVTTVSGG ISSRQVVAEG RTVPSSVSGV
660 670 680 690 700
TVNNSGRNDY LSVSWLPAPG EVDHYVVSLS HEGKVDQFLI IAKSVSECSF
710 720 730 740 750
SSLTPGRLYN VTVTTKSGNY ASHSFTEERT VPDKVQGISV SNSARSDYLK
760 770 780 790 800
VSWVHATGDF DHYEVTIKNR ESFIQTKTIP KSENECEFIE LVPGRLYSVT
810 820 830 840 850
VSTKSGQYEA SEQGTGRTIP EPVKDLTLLN RSTEDLHVTW SRANGDVDQY
860 870 880 890 900
EVQLLFNDMK VFPHIHLVNT ATEYKFTALT PGRHYKILVL TISGDVQQSA
910 920 930 940 950
FIEGLTVPST VKNIHISANG ATDRLMVTWS PGGGDVDSYV VSAFRQDEKV
960 970 980 990 1000
DSQTIPKHAS EHTFHRLEAG AKYRIAIVSV SGSLRNQIDA LGQTVPASVQ
1010 1020 1030 1040 1050
GVVAANAYSS NSLTVSWQKA LGVAERYDIL LLNENGLLLS NVSEPATARQ
1060 1070 1080 1090 1100
HKFEDLTPGK KYKMQILTVS GGLFSKESQA EGRTVPAAVT NLRITENSSR
1110 1120 1130 1140 1150
YLSFGWTASE GELSWYNIFL YNPDRTLQER AQVDPLVQSF SFQNLLQGRM
1160 1170 1180 1190 1200
YKMVIVTHSG ELSNESFIFG RTVPAAVNHL KGSHRNTTDS LWFSWSPASG
1210 1220 1230 1240 1250
DFDFYELILY NPNGTKKENW KEKDVTEWRF QGLVPGRKYT LYVVTHSGDL
1260 1270 1280 1290 1300
SNKVTGEGRT APSPPSLLSF ADVANTSLAI TWKGPPDWTD YNDFELQWFP
1310 1320 1330 1340 1350
GDALTIFNPY SSRKSEGRIV YGLHPGRSYQ FSVKTVSGDS WKTYSKPISG
1360 1370 1380 1390 1400
SVRTKPDKIQ NLHCRPQNST AIACSWIPPD SDFDGYSIEC RKMDTQEIEF
1410 1420 1430 1440 1450
SRKLEKEKSL LNIMMLVPHK RYLVSIKVQS AGMTSEVVED STITMIDRPP
1460 1470 1480 1490 1500
QPPPHIRVNE KDVLISKSSI NFTVNCSWFS DTNGAVKYFA VVVREADSMD
1510 1520 1530 1540 1550
ELKPEQQHPL PSYLEYRHNA SIRVYQTNYF ASKCAESPDS SSKSFNIKLG
1560 1570 1580 1590 1600
AEMDSLGGKC DPSQQKFCDG PLKPHTAYRI SIRAFTQLFD EDLKEFTKPL
1610 1620 1630 1640 1650
YSDTFFSMPI TTESEPLFGV IEGVSAGLFL IGMLVALVAF FICRQKASHS
1660 1670 1680 1690 1700
RERPSARLSI RRDRPLSVHL NLGQKGNRKT SCPIKINQFE GHFMKLQADS
1710 1720 1730 1740 1750
NYLLSKEYED LKDVGRSQSC DIALLPENRG KNRYNNILPY DASRVKLCNV
1760 1770 1780 1790 1800
DDDPCSDYIN ASYIPGNNFR REYIATQGPL PGTKDDFWKM AWEQNVHNIV
1810 1820 1830 1840 1850
MVTQCVEKGR VKCDHYWPAD QDPLYYGDLI LQMVSESVLP EWTIREFKIC
1860 1870 1880 1890 1900
SEEQLDAHRL IRHFHYTVWP DHGVPETTQS LIQFVRTVRD YINRSPGAGP
1910 1920 1930 1940 1950
TVVHCSAGVG RTGTFVALDR ILQQLDSKDS VDIYGAVHDL RLHRVHMVQT
1960 1970 1980 1990
ECQYVYLHQC VRDVLRAKKL RNEQENPLFP IYENVNPEYH RDAIYSRH
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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 ENSGT00770000120452.
HOGENOMi HOG000060224.
HOVERGENi HBG053759.
InParanoidi B2RU80.
KOi K05694.
OMAi PEQQHPL.
OrthoDBi EOG7PCJFZ.
PhylomeDBi B2RU80.
TreeFami TF351926.

Miscellaneous databases

ChiTaRSi Ptprb. mouse.
NextBioi 296128.
PROi B2RU80.
SOURCEi Search...

Gene expression databases

Bgeei B2RU80.
ExpressionAtlasi B2RU80. baseline and differential.
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: November 26, 2014
This is version 58 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