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Q9DBX1

- RGCC_MOUSE

UniProt

Q9DBX1 - RGCC_MOUSE

Protein

Regulator of cell cycle RGCC

Gene

Rgcc

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Modulates the activity of cell cycle-specific kinases. Enhances CDK1 activity. May contribute to the regulation of the cell cycle. May inhibit growth of glioma cells by promoting arrest of mitotic progression at the G2/M transition. Fibrogenic factor contributing to the pathogenesis of renal fibrosis through fibroblast activation.1 Publication

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. protein kinase activator activity Source: MGI

    GO - Biological processi

    1. cellular response to hypoxia Source: Ensembl
    2. complement activation Source: Ensembl
    3. fibroblast activation Source: UniProtKB
    4. G1/S transition of mitotic cell cycle Source: MGI
    5. mitotic cell cycle arrest Source: Ensembl
    6. negative regulation of angiogenesis Source: Ensembl
    7. negative regulation of blood vessel endothelial cell migration Source: Ensembl
    8. negative regulation of cell-cell adhesion mediated by cadherin Source: Ensembl
    9. negative regulation of cytokine secretion Source: Ensembl
    10. negative regulation of endothelial cell proliferation Source: Ensembl
    11. negative regulation of exit from mitosis Source: Ensembl
    12. negative regulation of fibroblast growth factor production Source: Ensembl
    13. negative regulation of mitotic cell cycle phase transition Source: Ensembl
    14. positive regulation of cell cycle arrest Source: Ensembl
    15. positive regulation of collagen biosynthetic process Source: Ensembl
    16. positive regulation of cyclin-dependent protein serine/threonine kinase activity involved in G1/S transition of mitotic cell cycle Source: Ensembl
    17. positive regulation of cytokine secretion Source: Ensembl
    18. positive regulation of DNA biosynthetic process Source: Ensembl
    19. positive regulation of endothelial cell apoptotic process Source: Ensembl
    20. positive regulation of epithelial to mesenchymal transition Source: Ensembl
    21. positive regulation of extracellular matrix constituent secretion Source: Ensembl
    22. positive regulation of gene expression involved in extracellular matrix organization Source: Ensembl
    23. positive regulation of mitosis Source: Ensembl
    24. positive regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
    25. positive regulation of stress fiber assembly Source: Ensembl

    Keywords - Biological processi

    Cell cycle

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Regulator of cell cycle RGCC
    Alternative name(s):
    Response gene to complement 32 protein
    Short name:
    RGC-32
    Gene namesi
    Name:Rgcc
    Synonyms:Rgc32
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 14

    Organism-specific databases

    MGIiMGI:1913464. Rgcc.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Cytoplasmcytoskeletonmicrotubule organizing centercentrosome By similarity
    Note: Cytoplasmic in unstimulated cells. Nuclear after activation by complement. Associated with the centrosome during prometaphase and metaphase By similarity.By similarity

    GO - Cellular componenti

    1. centrosome Source: Ensembl
    2. cytoplasm Source: MGI
    3. nucleolus Source: Ensembl
    4. nucleus Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 137137Regulator of cell cycle RGCCPRO_0000274702Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei69 – 691PhosphoserineBy similarity
    Modified residuei71 – 711PhosphoserineBy similarity
    Modified residuei75 – 751PhosphoserineBy similarity
    Modified residuei97 – 971PhosphoserineBy similarity
    Modified residuei111 – 1111Phosphothreonine; by CDK1By similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9DBX1.
    PaxDbiQ9DBX1.
    PRIDEiQ9DBX1.

    PTM databases

    PhosphoSiteiQ9DBX1.

    Expressioni

    Gene expression databases

    BgeeiQ9DBX1.
    CleanExiMM_1190002H23RIK.
    GenevestigatoriQ9DBX1.

    Interactioni

    Subunit structurei

    Interacts with CDK1 and PLK1 By similarity. Interacts with SMAD3.By similarity1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBX1.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi11 – 2616Ala-richAdd
    BLAST
    Compositional biasi64 – 10845Ser/Thr-richAdd
    BLAST

    Phylogenomic databases

    eggNOGiNOG39648.
    GeneTreeiENSGT00390000011709.
    HOGENOMiHOG000294092.
    HOVERGENiHBG060999.
    InParanoidiQ9DBX1.
    OMAiFRYDEHL.
    OrthoDBiEOG7ZGX5S.
    PhylomeDBiQ9DBX1.
    TreeFamiTF336312.

    Family and domain databases

    InterProiIPR029252. RGCC.
    [Graphical view]
    PfamiPF15151. RGCC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9DBX1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKPPSAQSSP AAVAAAAPAM DSAAAADLTD VLCEFDAVLA DFASPFHERH    50
    FHYEEHLERM KRRSSASVSD SSGFSDSESA DSVYRDSFTF SDEKLNSPTN 100
    SSPALLPSAV TPRKAKLGDT KELEDFIADL DRTLASM 137
    Length:137
    Mass (Da):14,717
    Last modified:June 1, 2001 - v1
    Checksum:i01646F247F8B284A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti68 – 681V → I in BAB23310. (PubMed:16141072)Curated
    Sequence conflicti70 – 701D → N in BAB23310. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF276981 mRNA. Translation: AAK69442.1.
    AK004451 mRNA. Translation: BAB23310.1.
    AK004705 mRNA. Translation: BAB23490.1.
    CT010403 mRNA. Translation: CAJ18609.1.
    BC049580 mRNA. Translation: AAH49580.1.
    BC050935 mRNA. Translation: AAH50935.1.
    CCDSiCCDS49552.1.
    RefSeqiNP_079703.2. NM_025427.2.
    UniGeneiMm.29811.

    Genome annotation databases

    EnsembliENSMUST00000022595; ENSMUSP00000022595; ENSMUSG00000022018.
    GeneIDi66214.
    KEGGimmu:66214.
    UCSCiuc007ust.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF276981 mRNA. Translation: AAK69442.1 .
    AK004451 mRNA. Translation: BAB23310.1 .
    AK004705 mRNA. Translation: BAB23490.1 .
    CT010403 mRNA. Translation: CAJ18609.1 .
    BC049580 mRNA. Translation: AAH49580.1 .
    BC050935 mRNA. Translation: AAH50935.1 .
    CCDSi CCDS49552.1.
    RefSeqi NP_079703.2. NM_025427.2.
    UniGenei Mm.29811.

    3D structure databases

    ProteinModelPortali Q9DBX1.
    ModBasei Search...
    MobiDBi Search...

    PTM databases

    PhosphoSitei Q9DBX1.

    Proteomic databases

    MaxQBi Q9DBX1.
    PaxDbi Q9DBX1.
    PRIDEi Q9DBX1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000022595 ; ENSMUSP00000022595 ; ENSMUSG00000022018 .
    GeneIDi 66214.
    KEGGi mmu:66214.
    UCSCi uc007ust.1. mouse.

    Organism-specific databases

    CTDi 28984.
    MGIi MGI:1913464. Rgcc.

    Phylogenomic databases

    eggNOGi NOG39648.
    GeneTreei ENSGT00390000011709.
    HOGENOMi HOG000294092.
    HOVERGENi HBG060999.
    InParanoidi Q9DBX1.
    OMAi FRYDEHL.
    OrthoDBi EOG7ZGX5S.
    PhylomeDBi Q9DBX1.
    TreeFami TF336312.

    Miscellaneous databases

    NextBioi 320993.
    PROi Q9DBX1.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9DBX1.
    CleanExi MM_1190002H23RIK.
    Genevestigatori Q9DBX1.

    Family and domain databases

    InterProi IPR029252. RGCC.
    [Graphical view ]
    Pfami PF15151. RGCC. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RGC-32 increases p34CDC2 kinase activity and entry of aortic smooth muscle cells into S-phase."
      Badea T., Niculescu F., Soane L., Fosbrink M., Sorana H., Rus V., Shin M.L., Rus H.
      J. Biol. Chem. 277:502-508(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    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/6J.
      Tissue: Embryo and Lung.
    3. "Cloning of mouse full open reading frames in Gateway(R) system entry vector (pDONR201)."
      Ebert L., Muenstermann E., Schatten R., Henze S., Bohn E., Mollenhauer J., Wiemann S., Schick M., Korn B.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    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].
      Strain: C57BL/6.
      Tissue: Brain and Testis.
    5. "Response gene to complement 32 is essential for fibroblast activation in renal fibrosis."
      Li Z., Xie W.B., Escano C.S., Asico L.D., Xie Q., Jose P.A., Chen S.Y.
      J. Biol. Chem. 286:41323-41330(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH SMAD3.

    Entry informationi

    Entry nameiRGCC_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBX1
    Secondary accession number(s): Q9D0U0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 6, 2007
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 84 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

    External Data

    Dasty 3