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Q9CXW3

- CYBP_MOUSE

UniProt

Q9CXW3 - CYBP_MOUSE

Protein

Calcyclin-binding protein

Gene

Cacybp

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1) By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. aging Source: Ensembl
    2. cardiac muscle cell differentiation Source: Ensembl
    3. cellular response to calcium ion Source: Ensembl
    4. negative regulation of cell death Source: Ensembl
    5. positive regulation of DNA replication Source: Ensembl
    6. response to growth hormone Source: Ensembl

    Keywords - Biological processi

    Ubl conjugation pathway

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcyclin-binding protein
    Short name:
    CacyBP
    Alternative name(s):
    Siah-interacting protein
    Gene namesi
    Name:Cacybp
    Synonyms:Sip
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1270839. Cacybp.

    Subcellular locationi

    Nucleus 1 Publication. Cytoplasm 1 Publication
    Note: Cytoplasmic in unstimulated cultured neurons. Upon increase of calcium, it localizes to a ring around the nucleus. In neuroblastoma cells, after a Retinoic acid (RA) induction and calcium increase, it localizes in both the nucleus and cytoplasm. The nuclear and perinuclear fractions may be phosphorylated.

    GO - Cellular componenti

    1. beta-catenin destruction complex Source: UniProtKB
    2. cell body Source: Ensembl
    3. cytoplasm Source: MGI
    4. neuron projection Source: Ensembl
    5. nuclear envelope lumen Source: MGI

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 229228Calcyclin-binding proteinPRO_0000185390Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei10 – 101N6-acetyllysineBy similarity
    Modified residuei21 – 211N6-acetyllysineBy similarity
    Modified residuei86 – 861N6-acetyllysineBy similarity
    Modified residuei119 – 1191N6-acetyllysineBy similarity

    Post-translational modificationi

    Phosphorylated on serine residues. Phosphorylated upon induction by RA or at high calcium concentrations.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9CXW3.
    PaxDbiQ9CXW3.
    PRIDEiQ9CXW3.

    2D gel databases

    REPRODUCTION-2DPAGEQ9CXW3.

    PTM databases

    PhosphoSiteiQ9CXW3.

    Expressioni

    Tissue specificityi

    Highly expressed in brain and EAT cells. Expressed at low level in heart, muscle, and at very low level in the liver, spleen, lung, kidney and stomach.1 Publication

    Gene expression databases

    BgeeiQ9CXW3.
    CleanExiMM_CACYBP.
    GenevestigatoriQ9CXW3.

    Interactioni

    Subunit structurei

    Monomer or homodimer. Component of some large E3 complex at least composed of UBE2D1, SIAH1, CACYBP/SIP, SKP1, APC and TBL1X. Interacts directly with SIAH1, SIAH2 and SKP1 By similarity. Interacts with proteins of the S100 family S100A1, S100A6, S100B, S100P and S100A12 in a calcium-dependent manner By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    S100A1P026394EBI-767146,EBI-6477285From a different organism.
    S100a6P140694EBI-767146,EBI-6478740
    S100BP026384EBI-767146,EBI-458452From a different organism.
    S100PP258152EBI-767146,EBI-743700From a different organism.

    Protein-protein interaction databases

    BioGridi198445. 8 interactions.
    IntActiQ9CXW3. 11 interactions.
    MINTiMINT-238999.

    Structurei

    Secondary structure

    1
    229
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi2 – 2120
    Turni22 – 265
    Helixi27 – 4721
    Helixi192 – 2009
    Helixi207 – 21610

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YSMNMR-A1-77[»]
    2JTTNMR-C/D189-219[»]
    DisProtiDP00226.
    ProteinModelPortaliQ9CXW3.
    SMRiQ9CXW3. Positions 1-55, 62-181, 189-219.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9CXW3.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini74 – 16895CSPROSITE-ProRule annotationAdd
    BLAST
    Domaini169 – 22961SGSPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 8180Interaction with SIAH1By similarityAdd
    BLAST
    Regioni74 – 229156Interaction with SKP1By similarityAdd
    BLAST
    Regioni155 – 22975Interaction with S100A6Add
    BLAST

    Sequence similaritiesi

    Contains 1 CS domain.PROSITE-ProRule annotation
    Contains 1 SGS domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG247905.
    GeneTreeiENSGT00390000016470.
    HOGENOMiHOG000238284.
    HOVERGENiHBG003242.
    InParanoidiQ9CXW3.
    KOiK04507.
    OMAiVNFTERS.
    OrthoDBiEOG7K9K4J.
    PhylomeDBiQ9CXW3.
    TreeFamiTF323891.

    Family and domain databases

    Gene3Di2.60.40.790. 1 hit.
    InterProiIPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR007699. SGS.
    IPR015120. Siah-Interact_N.
    [Graphical view]
    PfamiPF04969. CS. 1 hit.
    PF05002. SGS. 1 hit.
    PF09032. Siah-Interact_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF49764. SSF49764. 1 hit.
    PROSITEiPS51203. CS. 1 hit.
    PS51048. SGS. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9CXW3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MASVLEELQK DLEEVKVLLE KSTRKRLRDT LTSEKSKIET ELKNKMQQKS    50
    QKKPELDNEK PAAVVAPLTT GYTVKISNYG WDQSDKFVKI YITLTGVHQV 100
    PTENVQVHFT ERSFDLLVKN LNGKNYSMIV NNLLKPISVE SSSKKVKTDT 150
    VIILCRKKAE NTRWDYLTQV EKECKEKEKP SYDTEADPSE GLMNVLKKIY 200
    EDGDDDMKRT INKAWVESRE KQAREDTEF 229
    Length:229
    Mass (Da):26,510
    Last modified:June 1, 2001 - v1
    Checksum:i2B04B54D0054ACE0
    GO

    Sequence cautioni

    The sequence AAC16757.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97327 mRNA. Translation: AAC16757.1. Different initiation.
    AK013924 mRNA. No translation available.
    BC025948 mRNA. Translation: AAH25948.1.
    CCDSiCCDS15406.1.
    RefSeqiNP_033916.1. NM_009786.2.
    UniGeneiMm.10702.

    Genome annotation databases

    EnsembliENSMUST00000014370; ENSMUSP00000014370; ENSMUSG00000014226.
    GeneIDi12301.
    KEGGimmu:12301.
    UCSCiuc007deg.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U97327 mRNA. Translation: AAC16757.1 . Different initiation.
    AK013924 mRNA. No translation available.
    BC025948 mRNA. Translation: AAH25948.1 .
    CCDSi CCDS15406.1.
    RefSeqi NP_033916.1. NM_009786.2.
    UniGenei Mm.10702.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YSM NMR - A 1-77 [» ]
    2JTT NMR - C/D 189-219 [» ]
    DisProti DP00226.
    ProteinModelPortali Q9CXW3.
    SMRi Q9CXW3. Positions 1-55, 62-181, 189-219.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198445. 8 interactions.
    IntActi Q9CXW3. 11 interactions.
    MINTi MINT-238999.

    PTM databases

    PhosphoSitei Q9CXW3.

    2D gel databases

    REPRODUCTION-2DPAGE Q9CXW3.

    Proteomic databases

    MaxQBi Q9CXW3.
    PaxDbi Q9CXW3.
    PRIDEi Q9CXW3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000014370 ; ENSMUSP00000014370 ; ENSMUSG00000014226 .
    GeneIDi 12301.
    KEGGi mmu:12301.
    UCSCi uc007deg.2. mouse.

    Organism-specific databases

    CTDi 27101.
    MGIi MGI:1270839. Cacybp.

    Phylogenomic databases

    eggNOGi NOG247905.
    GeneTreei ENSGT00390000016470.
    HOGENOMi HOG000238284.
    HOVERGENi HBG003242.
    InParanoidi Q9CXW3.
    KOi K04507.
    OMAi VNFTERS.
    OrthoDBi EOG7K9K4J.
    PhylomeDBi Q9CXW3.
    TreeFami TF323891.

    Miscellaneous databases

    EvolutionaryTracei Q9CXW3.
    NextBioi 280826.
    PROi Q9CXW3.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CXW3.
    CleanExi MM_CACYBP.
    Genevestigatori Q9CXW3.

    Family and domain databases

    Gene3Di 2.60.40.790. 1 hit.
    InterProi IPR007052. CS_dom.
    IPR008978. HSP20-like_chaperone.
    IPR007699. SGS.
    IPR015120. Siah-Interact_N.
    [Graphical view ]
    Pfami PF04969. CS. 1 hit.
    PF05002. SGS. 1 hit.
    PF09032. Siah-Interact_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF49764. SSF49764. 1 hit.
    PROSITEi PS51203. CS. 1 hit.
    PS51048. SGS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning and expression of a mouse brain cDNA encoding a novel protein target of calcyclin."
      Filipek A., Kuznicki J.
      J. Neurochem. 70:1793-1798(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 17-22; 73-85 AND 222-229, TISSUE SPECIFICITY, INTERACTION WITH S100A6.
      Tissue: Brain.
    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.
    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].
    4. "Characterization of the interaction of calcyclin (S100A6) and calcyclin-binding protein."
      Nowotny M., Bhattacharya S., Filipek A., Krezel A.M., Chazin W., Kuznicki J.
      J. Biol. Chem. 275:31178-31182(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH S100A6.
    5. "Ca2+-dependent translocation of the calcyclin-binding protein in neurons and neuroblastoma NB-2a cells."
      Filipek A., Jastrzebska B., Nowotny M., Kwiatkowska K., Hetman M., Surmacz L., Wyroba E., Kuznicki J.
      J. Biol. Chem. 277:21103-21109(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION.
    6. "The modular structure of SIP facilitates its role in stabilizing multiprotein assemblies."
      Bhattacharya S., Lee Y.-T., Michowski W., Jastrzebska B., Filipek A., Kuznicki J., Chazin W.J.
      Biochemistry 44:9462-9471(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-77, INTERACTION WITH SKP1 AND S100A6, SUBUNIT.
    7. "Structure of the S100A6 complex with a fragment from the C-terminal domain of Siah-1 interacting protein: a novel mode for S100 protein target recognition."
      Lee Y.-T., Dimitrova Y.N., Schneider G., Ridenour W.B., Bhattacharya S., Soss S.E., Caprioli R.M., Filipek A., Chazin W.J.
      Biochemistry 47:10921-10932(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 189-219 IN COMPLEX WITH S100A6, INTERACTION WITH S100A6.

    Entry informationi

    Entry nameiCYBP_MOUSE
    AccessioniPrimary (citable) accession number: Q9CXW3
    Secondary accession number(s): O70140
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 105 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

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3