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Q62009

- POSTN_MOUSE

UniProt

Q62009 - POSTN_MOUSE

Protein

Periostin

Gene

Postn

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 114 (01 Oct 2014)
      Sequence version 2 (02 Feb 2004)
      Previous versions | rss
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    Functioni

    Induces cell attachment and spreading and plays a role in cell adhesion. May play a role in extracellular matrix mineralization. Enhances incorporation of BMP1 in the fibronectin matrix of connective tissues, and subsequent proteolytic activation of lysyl oxidase LOX.2 Publications

    GO - Molecular functioni

    1. heparin binding Source: UniProtKB

    GO - Biological processi

    1. cell adhesion Source: UniProtKB
    2. extracellular matrix organization Source: MGI
    3. regulation of Notch signaling pathway Source: MGI
    4. tissue development Source: MGI

    Keywords - Biological processi

    Cell adhesion

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Periostin
    Short name:
    PN
    Alternative name(s):
    Osteoblast-specific factor 2
    Short name:
    OSF-2
    Gene namesi
    Name:Postn
    Synonyms:Osf2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 3

    Organism-specific databases

    MGIiMGI:1926321. Postn.

    Subcellular locationi

    Golgi apparatus. Secretedextracellular spaceextracellular matrix
    Note: Colocalizes with BMP1 in the Golgi.

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB-SubCell
    2. proteinaceous extracellular matrix Source: UniProtKB

    Keywords - Cellular componenti

    Extracellular matrix, Golgi apparatus, Secreted

    Pathology & Biotechi

    Disruption phenotypei

    Reduced amount of collagen cross-linking in femur and periosteum.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 838815PeriostinPRO_0000008790Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi46 ↔ 82PROSITE-ProRule annotation
    Disulfide bondi62 ↔ 71PROSITE-ProRule annotation
    Disulfide bondi81 ↔ 94PROSITE-ProRule annotation
    Modified residuei126 – 12614-carboxyglutamateSequence Analysis
    Modified residuei127 – 12714-carboxyglutamateSequence Analysis
    Modified residuei129 – 12914-carboxyglutamateSequence Analysis
    Modified residuei142 – 14214-carboxyglutamateSequence Analysis
    Modified residuei156 – 15614-carboxyglutamateSequence Analysis
    Modified residuei162 – 16214-carboxyglutamateSequence Analysis
    Modified residuei244 – 24414-carboxyglutamateSequence Analysis
    Modified residuei246 – 24614-carboxyglutamateSequence Analysis
    Modified residuei263 – 26314-carboxyglutamateSequence Analysis
    Modified residuei279 – 27914-carboxyglutamateSequence Analysis
    Modified residuei282 – 28214-carboxyglutamateSequence Analysis
    Modified residuei290 – 29014-carboxyglutamateSequence Analysis
    Modified residuei300 – 30014-carboxyglutamateSequence Analysis
    Modified residuei315 – 31514-carboxyglutamateSequence Analysis
    Modified residuei324 – 32414-carboxyglutamateSequence Analysis
    Modified residuei327 – 32714-carboxyglutamateSequence Analysis
    Modified residuei498 – 49814-carboxyglutamateSequence Analysis
    Modified residuei519 – 51914-carboxyglutamateSequence Analysis
    Modified residuei549 – 54914-carboxyglutamateSequence Analysis
    Modified residuei550 – 55014-carboxyglutamateSequence Analysis
    Modified residuei552 – 55214-carboxyglutamateSequence Analysis
    Modified residuei580 – 58014-carboxyglutamateSequence Analysis
    Glycosylationi601 – 6011N-linked (GlcNAc...)1 Publication

    Post-translational modificationi

    Gamma-carboxyglutamate residues are formed by vitamin K dependent carboxylation. These residues are essential for the binding of calcium.1 Publication

    Keywords - PTMi

    Disulfide bond, Gamma-carboxyglutamic acid, Glycoprotein

    Proteomic databases

    MaxQBiQ62009.
    PaxDbiQ62009.
    PRIDEiQ62009.

    PTM databases

    PhosphoSiteiQ62009.

    Expressioni

    Tissue specificityi

    Preferentially expressed in periosteum and periodontal ligament. Also expressed in the developing and adult heart.2 Publications

    Developmental stagei

    In the heart, expressed from embryonic day 10.5. Continues to be strongly expressed throughout cardiac development and into adulthood.1 Publication

    Inductioni

    By TGF-beta.1 Publication

    Gene expression databases

    BgeeiQ62009.
    CleanExiMM_POSTN.
    GenevestigatoriQ62009.

    Interactioni

    Subunit structurei

    Interacts with BMP1 and fibronectin.1 Publication

    Protein-protein interaction databases

    IntActiQ62009. 1 interaction.
    MINTiMINT-4108229.

    Structurei

    3D structure databases

    ProteinModelPortaliQ62009.
    SMRiQ62009. Positions 124-238, 241-369, 500-632.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini42 – 9655EMIPROSITE-ProRule annotationAdd
    BLAST
    Domaini99 – 232134FAS1 1CuratedPROSITE-ProRule annotationAdd
    BLAST
    Domaini236 – 367132FAS1 2CuratedPROSITE-ProRule annotationAdd
    BLAST
    Domaini370 – 494125FAS1 3CuratedPROSITE-ProRule annotationAdd
    BLAST
    Domaini498 – 630133FAS1 4CuratedPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 EMI domain.PROSITE-ProRule annotation
    Contains 4 FAS1 domains.CuratedPROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiCOG2335.
    GeneTreeiENSGT00530000063860.
    HOGENOMiHOG000220865.
    HOVERGENiHBG000715.
    InParanoidiQ62009.
    OMAiHGEPIIK.
    OrthoDBiEOG7N8ZV1.
    PhylomeDBiQ62009.
    TreeFamiTF316269.

    Family and domain databases

    Gene3Di2.30.180.10. 4 hits.
    InterProiIPR011489. EMI_domain.
    IPR000782. FAS1_domain.
    IPR016666. TGFb-ind_bIGH3/osteoblast_fac2.
    [Graphical view]
    PfamiPF02469. Fasciclin. 4 hits.
    [Graphical view]
    PIRSFiPIRSF016553. BIGH3_OSF2. 1 hit.
    SMARTiSM00554. FAS1. 4 hits.
    [Graphical view]
    SUPFAMiSSF82153. SSF82153. 4 hits.
    PROSITEiPS51041. EMI. 1 hit.
    PS50213. FAS1. 4 hits.
    [Graphical view]

    Sequences (5)i

    Sequence statusi: Complete.

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

    This entry describes 5 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q62009-1) [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

    MVPLLPLYAL LLLFLCDINP ANANSYYDKV LAHSRIRGRD QGPNVCALQQ    50
    ILGTKKKYFS SCKNWYQGAI CGKKTTVLYE CCPGYMRMEG MKGCPAVMPI 100
    DHVYGTLGIV GATTTQHYSD VSKLREEIEG KGSYTYFAPS NEAWENLDSD 150
    IRRGLENNVN VELLNALHSH MVNKRMLTKD LKHGMVIPSM YNNLGLFINH 200
    YPNGVVTVNC ARVIHGNQIA TNGVVHVIDR VLTQIGTSIQ DFLEAEDDLS 250
    SFRAAAITSD LLESLGRDGH FTLFAPTNEA FEKLPRGVLE RIMGDKVASE 300
    ALMKYHILNT LQCSEAITGG AVFETMEGNT IEIGCEGDSI SINGIKMVNK 350
    KDIVTKNGVI HLIDEVLIPD SAKQVIELAG KQQTTFTDLV AQLGLASSLK 400
    PDGEYTLLAP VNNAFSDDTL SMDQRLLKLI LQNHILKVKV GLSDLYNGQI 450
    LETIGGKQLR VFVYRTAICI ENSCMVRGSK QGRNGAIHIF REIIQPAEKS 500
    LHDKLRQDKR FSIFLSLLEA ADLKDLLTQP GDWTLFAPTN DAFKGMTSEE 550
    RELLIGDKNA LQNIILYHLT PGVYIGKGFE PGVTNILKTT QGSKIYLKGV 600
    NETLLVNELK SKESDIMTTN GVIHVVDKLL YPADIPVGND QLLELLNKLI 650
    KYIQIKFVRG STFKEIPMTV YTTKIITKVV EPKIKVIQGS LQPIIKTEGP 700
    AMTKIQIEGD PDFRLIKEGE TVTEVIHGEP VIKKYTKIID GVPVEITEKQ 750
    TREERIITGP EIKYTRISTG GGETGETLQK FLQKEVSKVT KFIEGGDGHL 800
    FEDEEIKRLL QGDTPAKKIP ANKRVQGPRR RSREGRSQ 838
    Length:838
    Mass (Da):93,144
    Last modified:February 2, 2004 - v2
    Checksum:i907FEB37942EADEC
    GO
    Isoform 21 Publication (identifier: Q62009-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         672-699: TTKIITKVVEPKIKVIQGSLQPIIKTEG → R

    Show »
    Length:811
    Mass (Da):90,255
    Checksum:iDA5CE8F8B9380234
    GO
    Isoform 31 Publication (identifier: Q62009-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         785-812: Missing.

    Show »
    Length:810
    Mass (Da):89,987
    Checksum:i7CF602BDD3BAB995
    GO
    Isoform 41 Publication (identifier: Q62009-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         759-812: Missing.

    Show »
    Length:784
    Mass (Da):87,166
    Checksum:i915027B89E47A6C3
    GO
    Isoform 5Curated (identifier: Q62009-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         672-699: TTKIITKVVEPKIKVIQGSLQPIIKTEG → R
         785-812: Missing.

    Note: No experimental confirmation available.Curated

    Show »
    Length:783
    Mass (Da):87,099
    Checksum:i24B93AB348C9A7FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti346 – 3461K → R in BAC27122. (PubMed:16141072)Curated
    Sequence conflicti541 – 5411D → N in BAC27122. (PubMed:16141072)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei672 – 69928TTKII…IKTEG → R in isoform 2 and isoform 5. 3 PublicationsVSP_050666Add
    BLAST
    Alternative sequencei759 – 81254Missing in isoform 4. 1 PublicationVSP_050667Add
    BLAST
    Alternative sequencei785 – 81228Missing in isoform 3 and isoform 5. 3 PublicationsVSP_050668Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13664 mRNA. Translation: BAA02835.1.
    AK030756 mRNA. Translation: BAC27122.1.
    BC031449 mRNA. Translation: AAH31449.1.
    CCDSiCCDS17351.1. [Q62009-2]
    CCDS57211.1. [Q62009-3]
    CCDS57212.1. [Q62009-5]
    PIRiS36109.
    RefSeqiNP_001185694.1. NM_001198765.1. [Q62009-3]
    NP_001185695.1. NM_001198766.1. [Q62009-5]
    NP_056599.1. NM_015784.3. [Q62009-2]
    XP_006501716.1. XM_006501653.1. [Q62009-1]
    XP_006501717.1. XM_006501654.1. [Q62009-4]
    UniGeneiMm.236067.

    Genome annotation databases

    EnsembliENSMUST00000073012; ENSMUSP00000072773; ENSMUSG00000027750. [Q62009-2]
    ENSMUST00000081564; ENSMUSP00000080276; ENSMUSG00000027750. [Q62009-1]
    ENSMUST00000107985; ENSMUSP00000103619; ENSMUSG00000027750. [Q62009-3]
    ENSMUST00000117373; ENSMUSP00000112735; ENSMUSG00000027750. [Q62009-5]
    GeneIDi50706.
    KEGGimmu:50706.
    UCSCiuc008pfh.2. mouse. [Q62009-2]
    uc008pfi.2. mouse. [Q62009-3]
    uc008pfj.2. mouse. [Q62009-5]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D13664 mRNA. Translation: BAA02835.1 .
    AK030756 mRNA. Translation: BAC27122.1 .
    BC031449 mRNA. Translation: AAH31449.1 .
    CCDSi CCDS17351.1. [Q62009-2 ]
    CCDS57211.1. [Q62009-3 ]
    CCDS57212.1. [Q62009-5 ]
    PIRi S36109.
    RefSeqi NP_001185694.1. NM_001198765.1. [Q62009-3 ]
    NP_001185695.1. NM_001198766.1. [Q62009-5 ]
    NP_056599.1. NM_015784.3. [Q62009-2 ]
    XP_006501716.1. XM_006501653.1. [Q62009-1 ]
    XP_006501717.1. XM_006501654.1. [Q62009-4 ]
    UniGenei Mm.236067.

    3D structure databases

    ProteinModelPortali Q62009.
    SMRi Q62009. Positions 124-238, 241-369, 500-632.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q62009. 1 interaction.
    MINTi MINT-4108229.

    PTM databases

    PhosphoSitei Q62009.

    Proteomic databases

    MaxQBi Q62009.
    PaxDbi Q62009.
    PRIDEi Q62009.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000073012 ; ENSMUSP00000072773 ; ENSMUSG00000027750 . [Q62009-2 ]
    ENSMUST00000081564 ; ENSMUSP00000080276 ; ENSMUSG00000027750 . [Q62009-1 ]
    ENSMUST00000107985 ; ENSMUSP00000103619 ; ENSMUSG00000027750 . [Q62009-3 ]
    ENSMUST00000117373 ; ENSMUSP00000112735 ; ENSMUSG00000027750 . [Q62009-5 ]
    GeneIDi 50706.
    KEGGi mmu:50706.
    UCSCi uc008pfh.2. mouse. [Q62009-2 ]
    uc008pfi.2. mouse. [Q62009-3 ]
    uc008pfj.2. mouse. [Q62009-5 ]

    Organism-specific databases

    CTDi 10631.
    MGIi MGI:1926321. Postn.

    Phylogenomic databases

    eggNOGi COG2335.
    GeneTreei ENSGT00530000063860.
    HOGENOMi HOG000220865.
    HOVERGENi HBG000715.
    InParanoidi Q62009.
    OMAi HGEPIIK.
    OrthoDBi EOG7N8ZV1.
    PhylomeDBi Q62009.
    TreeFami TF316269.

    Miscellaneous databases

    NextBioi 307557.
    PROi Q62009.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q62009.
    CleanExi MM_POSTN.
    Genevestigatori Q62009.

    Family and domain databases

    Gene3Di 2.30.180.10. 4 hits.
    InterProi IPR011489. EMI_domain.
    IPR000782. FAS1_domain.
    IPR016666. TGFb-ind_bIGH3/osteoblast_fac2.
    [Graphical view ]
    Pfami PF02469. Fasciclin. 4 hits.
    [Graphical view ]
    PIRSFi PIRSF016553. BIGH3_OSF2. 1 hit.
    SMARTi SM00554. FAS1. 4 hits.
    [Graphical view ]
    SUPFAMi SSF82153. SSF82153. 4 hits.
    PROSITEi PS51041. EMI. 1 hit.
    PS50213. FAS1. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Osteoblast-specific factor 2: cloning of a putative bone adhesion protein with homology with the insect protein fasciclin I."
      Takeshita S., Kikuno R., Tezuka K., Amann E.
      Biochem. J. 294:271-278(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Strain: C57BL/61 Publication.
      Tissue: Calvaria1 Publication.
    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] (ISOFORM 3).
      Strain: C57BL/6J.
    3. "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] (ISOFORM 5).
      Tissue: Mammary glandImported.
    4. "Identification and characterization of a novel protein, periostin, with restricted expression to periosteum and periodontal ligament and increased expression by transforming growth factor beta."
      Horiuchi K., Amizuka N., Takeshita S., Takamatsu H., Katsuura M., Ozawa H., Toyama Y., Bonewald L.F., Kudo A.
      J. Bone Miner. Res. 14:1239-1249(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: PARTIAL NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3 AND 4), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
    5. "Expression and characterization of murine osteoblast-specific factor 2 (OSF-2) in a baculovirus expression system."
      Sugiura T., Takamatsu H., Kudo A., Amann E.
      Protein Expr. Purif. 6:305-311(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: HEPARIN-BINDING ACTIVITY, GLYCOSYLATION.
    6. "Periostin (an osteoblast-specific factor) is expressed within the embryonic mouse heart during valve formation."
      Kruzynska-Frejtag A., Machnicki M., Rogers R., Markwald R.R., Conway S.J.
      Mech. Dev. 103:183-188(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    7. "Periostin, a member of a novel family of vitamin K-dependent proteins, is expressed by mesenchymal stromal cells."
      Coutu D.L., Wu J.H., Monette A., Rivard G.-E., Blostein M.D., Galipeau J.
      J. Biol. Chem. 283:17991-18001(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GAMMA-CARBOXYGLUTAMATION.
    8. "Interaction between periostin and BMP-1 promotes proteolytic activation of lysyl oxidase."
      Maruhashi T., Kii I., Saito M., Kudo A.
      J. Biol. Chem. 285:13294-13303(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH BMP1 AND FIBRONECTIN, DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiPOSTN_MOUSE
    AccessioniPrimary (citable) accession number: Q62009
    Secondary accession number(s): Q8BMJ6, Q8K1K0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: February 2, 2004
    Last modified: October 1, 2014
    This is version 114 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