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)

B1AUH1

- PTPRU_MOUSE

UniProt

B1AUH1 - PTPRU_MOUSE

Protein

Receptor-type tyrosine-protein phosphatase U

Gene

Ptpru

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 64 (01 Oct 2014)
      Sequence version 1 (08 Apr 2008)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Tyrosine-protein phosphatase which dephosphorylates CTNNB1. Regulates CTNNB1 function both in cell adhesion and signaling. May function in cell proliferation and migration and play a role in the maintenance of epithelial integrity. May play a role in megakaryocytopoiesis By similarity.By similarity

    Catalytic activityi

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei1053 – 10531SubstrateSequence Analysis
    Active sitei1085 – 10851Phosphocysteine intermediateBy similarity
    Binding sitei1129 – 11291SubstrateBy similarity
    Active sitei1380 – 13801Phosphocysteine intermediateBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. canonical Wnt signaling pathway Source: Ensembl
    2. cell differentiation Source: UniProtKB-KW
    3. homotypic cell-cell adhesion Source: MGI
    4. negative regulation of cell migration Source: Ensembl
    5. negative regulation of cell proliferation Source: Ensembl
    6. organ regeneration Source: Ensembl
    7. protein localization to cell surface Source: Ensembl
    8. response to glucocorticoid Source: Ensembl

    Keywords - Molecular functioni

    Hydrolase, Protein phosphatase, Receptor

    Keywords - Biological processi

    Cell adhesion, Differentiation

    Enzyme and pathway databases

    ReactomeiREACT_188578. Signaling by SCF-KIT.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor-type tyrosine-protein phosphatase U (EC:3.1.3.48)
    Short name:
    R-PTP-U
    Alternative name(s):
    Ftp-1
    Pancreatic carcinoma phosphatase 2
    Short name:
    PCP-2
    Protein-tyrosine phosphatase-lamda
    Short name:
    PTP-lambda
    Short name:
    PTPlambda
    Receptor-type protein-tyrosine phosphatase psi
    Short name:
    R-PTP-psi
    Gene namesi
    Name:Ptpru
    Synonyms:Pcp2, Ptpf
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 4

    Organism-specific databases

    MGIiMGI:1321151. Ptpru.

    Subcellular locationi

    Cell junction By similarity. Cell membrane By similarity; Single-pass type I membrane protein By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: Ensembl
    2. integral component of membrane Source: UniProtKB-KW
    3. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 14461428Receptor-type tyrosine-protein phosphatase UPRO_0000371659Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi75 – 751N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi210 ↔ 264Sequence Analysis
    Glycosylationi410 – 4101N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi685 – 6851N-linked (GlcNAc...)Sequence Analysis
    Modified residuei848 – 8481PhosphoserineBy similarity
    Modified residuei853 – 8531PhosphoserineBy similarity

    Post-translational modificationi

    The extracellular domain is proteolytically processed through cleavage within the fibronectin type-III 4 domain. In addition to the 190 kDa full-length protein, proteolytic products of 100 kDa, 80 kDa and 73 kDa are observed By similarity.By similarity
    N-glycosylated.By similarity
    Phosphorylated on tyrosine residues upon activation of KIT with stem cell factor (SCF). The 73 kDa proteolytic product is not phosphorylated By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PRIDEiB1AUH1.

    Expressioni

    Tissue specificityi

    Transcripts of different sizes are differentially expressed in a subset of tissues. Detected in brain, lung, skeletal muscle, heart, kidney and placenta. In brain; expressed in olfactory bulb, cerebral cortex, hippocampus and cerebellum.3 Publications

    Developmental stagei

    Expressed throughout embryonic development. First detected at E7.1 Publication

    Gene expression databases

    ArrayExpressiB1AUH1.
    BgeeiB1AUH1.
    GenevestigatoriB1AUH1.

    Interactioni

    Subunit structurei

    Forms homooligomeric complexes which mediate cell homotypic adhesion Probable. Interacts (via the cytoplasmic juxtamembrane domain) with CTNNB1; may mediate interaction with the cadherin/catenin adhesion complex. Interacts with KIT By similarity. May interact with AP3B1 By similarity.By similarityCurated

    Structurei

    3D structure databases

    ProteinModelPortaliB1AUH1.
    SMRiB1AUH1. Positions 22-591, 871-1440.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini19 – 749731ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini771 – 1446676CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei750 – 77021HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 188164MAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini190 – 27586Ig-like C2-typeAdd
    BLAST
    Domaini288 – 38396Fibronectin type-III 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini386 – 48499Fibronectin type-III 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini485 – 591107Fibronectin type-III 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini592 – 66877Fibronectin type-III 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini888 – 1144257Tyrosine-protein phosphatase 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini1176 – 1439264Tyrosine-protein phosphatase 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni771 – 887117Mediates interaction with CTNNB1Add
    BLAST
    Regioni1085 – 10917Substrate bindingBy similarity

    Sequence similaritiesi

    Contains 4 fibronectin type-III domains.PROSITE-ProRule annotation
    Contains 1 MAM domain.PROSITE-ProRule annotation
    Contains 2 tyrosine-protein phosphatase domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG5599.
    GeneTreeiENSGT00640000091300.
    HOGENOMiHOG000049029.
    InParanoidiQ66JV9.
    KOiK16662.
    OMAiLTDSYTR.
    OrthoDBiEOG70KGNP.
    PhylomeDBiB1AUH1.
    TreeFamiTF312900.

    Family and domain databases

    Gene3Di2.60.40.10. 4 hits.
    3.90.190.10. 2 hits.
    InterProiIPR008985. ConA-like_lec_gl_sf.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR000998. MAM_dom.
    IPR029021. Prot-tyrosine_phosphatase-like.
    IPR000387. Tyr/Dual-sp_Pase.
    IPR016130. Tyr_Pase_AS.
    IPR000242. Tyr_Pase_rcpt/non-rcpt.
    [Graphical view]
    PfamiPF00041. fn3. 2 hits.
    PF00629. MAM. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view]
    PRINTSiPR00020. MAMDOMAIN.
    PR00700. PRTYPHPHTASE.
    SMARTiSM00060. FN3. 3 hits.
    SM00409. IG. 1 hit.
    SM00137. MAM. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view]
    SUPFAMiSSF49265. SSF49265. 2 hits.
    SSF49899. SSF49899. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEiPS50853. FN3. 3 hits.
    PS50060. MAM_2. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: B1AUH1-1) [UniParc]FASTAAdd to Basket

    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

    MARAQALVLA LTFQFCAPET ETPAAGCTFE EASDPVVPCE FSQAQYDDFQ     50
    WEQVRIHPGT RTPEDLPHGA YLMVNASQHA PGQRAHIIFQ TLSENDTHCV 100
    QFSYFLYSRD GHSPGTLGVY VRVNGGPLGS AVWNMTGSHG RQWHQAELAV 150
    STFWPNEYQV LFEALISPDH KGYIGLDDIL LFSYPCAKAP HFSRLGDVEV 200
    NAGQNASFQC MAAGRAAEAE HFFLQRQSGV LVPAAGVRHI SHRRFLATFP 250
    LASVGRSEQD LYRCVSQAPR GAGVSNFAEL IVKEPPTPIA PPQLLRAGPT 300
    YLIIQLNTNS IIGDGPIVRK EIEYRMARGP WAEVHAVNLQ TYKLWHLDPD 350
    TEYEISVLLT RPGDGGTGRP GPPLISRTKC AEPTRAPKGL AFAEIQARQL 400
    TLQWEPLGYN VTRCHTYAVS LCYRYTLGGS HNQTIRECVK MERGASRYTI 450
    KNLLPFRNIH VRLILTNPEG RKEGKEVTFQ TDEDVPGGIA AESLTFTPLE 500
    DMIFLKWEEP QEPNGLITQY EISYQSIESS DPAVNVPGPR RTISKLRNET 550
    YHVFSNLHPG TTYLFSVRAR TSKGFGQAAL TEITTNISAP SFDYADMPSP 600
    LGESENTITV LLRPAQGRGA PISVYQVVVE EERPRRLRRE PGAQDCFSVP 650
    LTFETALARG LVHYFGAELA ASSLLEAMPF TVGDNQTYRG FWNPPLEPRK 700
    AYLIYFQAAS HLKGETRLNC IRIARKAACK ESKRPLEVSQ RSEEMGLILG 750
    ICAGGLAVLI LLLGAIIVII RKGRDRYAYS YYPKPVNMTK ATVNYRQEKT 800
    HMMSAVDRSF TDQSTLQEDE RLGLSFMDAP GYSPRGDQRS GGVTEASSLL 850
    GGSPRRPCGR KGSPYHTGQL HPAVRVADLL QHINQMKTAE GYGFKQEYES 900
    FFEGWDATKK KDKLKGGRQE PVSAYDRHHV KLHPMLADPD ADYISANYID 950
    GYHRSNHFIA TQGPKPEMIY DFWRMVWQEQ CASIVMITKL VEVGRVKCSR 1000
    YWPEDSDMYG DIKITLVKTE TLAEYVVRTF ALERRGYSAR HEVRQFHFTA 1050
    WPEHGVPYHA TGLLAFIRRV KASTPPDAGP IVIHCSAGTG RTGCYIVLDV 1100
    MLDMAECEGV VDIYNCVKTL CSRRVNMIQT EEQYIFIHDA ILEACLCGET 1150
    TIPVNEFKAT YREMIRIDPQ SNSSQLREEF QTLNSVTPPL DVEECSIALL 1200
    PRNRDKNRSM DVLPPDRCLP FLISSDGDPN NYINAALTDS YTRSAAFIVT 1250
    LHPLQSTTPD FWRLVYDYGC TSIVMLNQLN QSNSAWPCLQ YWPEPGRQQY 1300
    GLMEVEFVSG TANEDLVSRV FRVQNSSRLQ EGHLLVRHFQ FLRWSAYRDT 1350
    PDSRKAFLHL LAEVDKWQAE SGDGRTVVHC LNGGGRSGTF CACATVLEMI 1400
    RCHSLVDVFF AAKTLRNYKP NMVETMDQYH FCYDVALEYL EALELR 1446
    Length:1,446
    Mass (Da):162,494
    Last modified:April 8, 2008 - v1
    Checksum:iCBF639D8150D0D0B
    GO
    Isoform 2 (identifier: B1AUH1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         774-783: Missing.

    Show »
    Length:1,436
    Mass (Da):161,158
    Checksum:i8D406DE4948643FF
    GO

    Sequence cautioni

    The sequence AAH80736.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.
    The sequence BAE43351.1 differs from that shown. Reason: Intron retention.
    The sequence AAH80736.1 differs from that shown. Reason: Erroneous termination at position 618. Translated as Arg.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti80 – 801A → T in AAB17895. (PubMed:9054423)Curated
    Sequence conflicti158 – 1581Y → F in AAB17895. (PubMed:9054423)Curated
    Sequence conflicti265 – 2651V → A in AAH80736. (PubMed:15489334)Curated
    Sequence conflicti387 – 3871P → S in AAH80736. (PubMed:15489334)Curated
    Sequence conflicti506 – 5061K → R in AAH80736. (PubMed:15489334)Curated
    Sequence conflicti1158 – 11581K → R in AAB17895. (PubMed:9054423)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei774 – 78310Missing in isoform 2. 4 PublicationsVSP_037086

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88187 mRNA. Translation: BAA23475.1.
    U55057 mRNA. Translation: AAB17895.1.
    AL670959 Genomic DNA. Translation: CAM27391.1.
    AL670959 Genomic DNA. Translation: CAM27392.1.
    CH466552 Genomic DNA. Translation: EDL30128.1.
    AK052720 mRNA. Translation: BAE43351.1. Sequence problems.
    BC080736 mRNA. Translation: AAH80736.1. Sequence problems.
    CCDSiCCDS18714.1. [B1AUH1-2]
    CCDS38896.1. [B1AUH1-1]
    RefSeqiNP_001076588.1. NM_001083119.2. [B1AUH1-1]
    NP_035344.2. NM_011214.2. [B1AUH1-2]
    UniGeneiMm.4860.

    Genome annotation databases

    EnsembliENSMUST00000030741; ENSMUSP00000030741; ENSMUSG00000028909. [B1AUH1-1]
    ENSMUST00000105987; ENSMUSP00000101607; ENSMUSG00000028909. [B1AUH1-2]
    GeneIDi19273.
    KEGGimmu:19273.
    UCSCiuc008vaa.1. mouse. [B1AUH1-1]
    uc008vab.1. mouse. [B1AUH1-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D88187 mRNA. Translation: BAA23475.1 .
    U55057 mRNA. Translation: AAB17895.1 .
    AL670959 Genomic DNA. Translation: CAM27391.1 .
    AL670959 Genomic DNA. Translation: CAM27392.1 .
    CH466552 Genomic DNA. Translation: EDL30128.1 .
    AK052720 mRNA. Translation: BAE43351.1 . Sequence problems.
    BC080736 mRNA. Translation: AAH80736.1 . Sequence problems.
    CCDSi CCDS18714.1. [B1AUH1-2 ]
    CCDS38896.1. [B1AUH1-1 ]
    RefSeqi NP_001076588.1. NM_001083119.2. [B1AUH1-1 ]
    NP_035344.2. NM_011214.2. [B1AUH1-2 ]
    UniGenei Mm.4860.

    3D structure databases

    ProteinModelPortali B1AUH1.
    SMRi B1AUH1. Positions 22-591, 871-1440.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi B1AUH1.

    Protocols and materials databases

    DNASUi 19273.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000030741 ; ENSMUSP00000030741 ; ENSMUSG00000028909 . [B1AUH1-1 ]
    ENSMUST00000105987 ; ENSMUSP00000101607 ; ENSMUSG00000028909 . [B1AUH1-2 ]
    GeneIDi 19273.
    KEGGi mmu:19273.
    UCSCi uc008vaa.1. mouse. [B1AUH1-1 ]
    uc008vab.1. mouse. [B1AUH1-2 ]

    Organism-specific databases

    CTDi 10076.
    MGIi MGI:1321151. Ptpru.

    Phylogenomic databases

    eggNOGi COG5599.
    GeneTreei ENSGT00640000091300.
    HOGENOMi HOG000049029.
    InParanoidi Q66JV9.
    KOi K16662.
    OMAi LTDSYTR.
    OrthoDBi EOG70KGNP.
    PhylomeDBi B1AUH1.
    TreeFami TF312900.

    Enzyme and pathway databases

    Reactomei REACT_188578. Signaling by SCF-KIT.

    Miscellaneous databases

    NextBioi 296166.
    PROi B1AUH1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi B1AUH1.
    Bgeei B1AUH1.
    Genevestigatori B1AUH1.

    Family and domain databases

    Gene3Di 2.60.40.10. 4 hits.
    3.90.190.10. 2 hits.
    InterProi IPR008985. ConA-like_lec_gl_sf.
    IPR003961. Fibronectin_type3.
    IPR013783. Ig-like_fold.
    IPR003599. Ig_sub.
    IPR000998. MAM_dom.
    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. 2 hits.
    PF00629. MAM. 1 hit.
    PF00102. Y_phosphatase. 2 hits.
    [Graphical view ]
    PRINTSi PR00020. MAMDOMAIN.
    PR00700. PRTYPHPHTASE.
    SMARTi SM00060. FN3. 3 hits.
    SM00409. IG. 1 hit.
    SM00137. MAM. 1 hit.
    SM00194. PTPc. 2 hits.
    [Graphical view ]
    SUPFAMi SSF49265. SSF49265. 2 hits.
    SSF49899. SSF49899. 1 hit.
    SSF52799. SSF52799. 2 hits.
    PROSITEi PS50853. FN3. 3 hits.
    PS50060. MAM_2. 1 hit.
    PS00383. TYR_PHOSPHATASE_1. 2 hits.
    PS50056. TYR_PHOSPHATASE_2. 2 hits.
    PS50055. TYR_PHOSPHATASE_PTP. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a novel receptor-type protein tyrosine phosphatase from murine fetal liver."
      Yoneya T., Yamada Y., Kakeda M., Osawa M., Arai E., Hayashi K., Nishi N., Inoue H., Nishikawa M.
      Gene 194:241-247(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY.
      Tissue: Fetal liver.
    2. "A novel protein-tyrosine phosphatase related to the homotypically adhering kappa and mu receptors."
      Cheng J., Wu K., Armanini M., O'Rourke N., Dowbenko D., Lasky L.A.
      J. Biol. Chem. 272:7264-7277(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), HOMOOLIGOMERIZATION, INTERACTION WITH CTNNB1, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, PROTEOLYTIC PROCESSING.
      Tissue: Lung.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] OF 1-1286 (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Kidney.
    6. "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] OF 1-911 (ISOFORM 2).
      Strain: C57BL/6J.
      Tissue: Embryo.
    7. "Genomic structure and alternative splicing of murine R2B receptor protein tyrosine phosphatases (PTPkappa, mu, rho and PCP-2)."
      Besco J., Popesco M.C., Davuluri R.V., Frostholm A., Rotter A.
      BMC Genomics 5:14-14(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiPTPRU_MOUSE
    AccessioniPrimary (citable) accession number: B1AUH1
    Secondary accession number(s): O35564
    , P70125, Q3V312, Q66JV9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 5, 2009
    Last sequence update: April 8, 2008
    Last modified: October 1, 2014
    This is version 64 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