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P27790

- CENPB_MOUSE

UniProt

P27790 - CENPB_MOUSE

Protein

Major centromere autoantigen B

Gene

Cenpb

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 115 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    Functioni

    Interacts with centromeric heterochromatin in chromosomes and binds to a specific subset of alphoid satellite DNA, called the CENP-B box. May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in mammalian chromosomes By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    DNA bindingi28 – 4821H-T-H motifBy similarityAdd
    BLAST
    DNA bindingi97 – 12933H-T-H motifBy similarityAdd
    BLAST

    GO - Molecular functioni

    1. chromatin binding Source: InterPro
    2. DNA binding Source: UniProtKB-KW

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: InterPro

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Major centromere autoantigen B
    Alternative name(s):
    Centromere protein B
    Short name:
    CENP-B
    Gene namesi
    Name:Cenpb
    Synonyms:Cenp-b
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 2

    Organism-specific databases

    MGIiMGI:88376. Cenpb.

    Subcellular locationi

    GO - Cellular componenti

    1. chromosome, centromeric region Source: MGI
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 599598Major centromere autoantigen BPRO_0000126126Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N,N,N-trimethylglycineBy similarity
    Modified residuei165 – 1651PhosphoserineBy similarity
    Modified residuei398 – 3981PhosphothreonineBy similarity

    Post-translational modificationi

    Poly-ADP-ribosylated by PARP1.
    N-terminally methylated by METTL11A/NTM1. Alpha-N-methylation is stimulated in response to extracellular stimuli, including increased cell density and heat shock, and seems to facilitate binding to CENP-B boxes. Chromatin-bound CENP-B is primarily trimethylated By similarity.By similarity

    Keywords - PTMi

    ADP-ribosylation, Methylation, Phosphoprotein

    Proteomic databases

    PRIDEiP27790.

    PTM databases

    PhosphoSiteiP27790.

    Expressioni

    Gene expression databases

    BgeeiP27790.
    CleanExiMM_CENPB.
    GenevestigatoriP27790.

    Interactioni

    Subunit structurei

    Antiparallel homodimer. Interacts with CENPT By similarity.By similarity

    Protein-protein interaction databases

    BioGridi198675. 1 interaction.
    IntActiP27790. 1 interaction.
    MINTiMINT-237475.

    Structurei

    3D structure databases

    ProteinModelPortaliP27790.
    SMRiP27790. Positions 1-129, 540-585.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 5251HTH psq-typePROSITE-ProRule annotationAdd
    BLAST
    Domaini65 – 13672HTH CENPB-typePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni536 – 59964HomodimerizationBy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi404 – 46562Glu-rich (acidic)Add
    BLAST
    Compositional biasi508 – 53831Asp/Glu-rich (acidic)Add
    BLAST

    Sequence similaritiesi

    Contains 1 HTH CENPB-type DNA-binding domain.PROSITE-ProRule annotation
    Contains 1 HTH psq-type DNA-binding domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG241149.
    GeneTreeiENSGT00740000115260.
    HOGENOMiHOG000111537.
    HOVERGENiHBG050890.
    KOiK11496.
    OMAiKRRQLTF.
    OrthoDBiEOG7HTHGS.
    TreeFamiTF101131.

    Family and domain databases

    Gene3Di1.10.10.60. 2 hits.
    InterProiIPR015115. Centromere_CenpB_dimerisation.
    IPR004875. DDE_SF_endonuclease_CENPB-like.
    IPR009057. Homeodomain-like.
    IPR006600. HTH_CenpB_DNA-bd_dom.
    IPR007889. HTH_Psq.
    [Graphical view]
    PfamiPF09026. CENP-B_dimeris. 1 hit.
    PF04218. CENP-B_N. 1 hit.
    PF03184. DDE_1. 1 hit.
    PF03221. HTH_Tnp_Tc5. 1 hit.
    [Graphical view]
    SMARTiSM00674. CENPB. 1 hit.
    [Graphical view]
    SUPFAMiSSF46689. SSF46689. 2 hits.
    PROSITEiPS51253. HTH_CENPB. 1 hit.
    PS50960. HTH_PSQ. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P27790-1 [UniParc]FASTAAdd to Basket

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    MGPKRRQLTF REKSRIIQEV EENPDLRKGE IARRFNIPPS TLSTILKNKR    50
    AILASERKYG VASTCRKTNK LSPYDKLEGL LIAWFQQIRA AGLPVKGIIL 100
    KEKALRIAEE LGMDDFTASN GWLDRFRRRH GVVACSGVTR SRARSSAPRA 150
    PAAPAGPATV PSEGSGGSTP GWHTREEQPP SVAEGYASQD VFSATETSLW 200
    YDFLSDQASG LWGGDGPARQ ATQRLSVLLC ANADGSEKLP PLVAGKSAKP 250
    RAGQGGLPCD YTANSKGGVT TQALAKYLKA LDTRMAAESR RVLLLAGRLA 300
    AQSLDTSGLR HVQLAFFPPG TVHPLERGVV QQVKGHYRQA MLLKAMAALE 350
    GQDPSGLQLG LVEALHFVAA AWQAVEPSDI ATCFREAGFG GGLNATITTS 400
    FKSEGEEEEE EEEEEEEEEE EEGEGEEEEE EEEEGEEEGG EGEEEGEEEV 450
    EEEGEVDDSD EEEEESSSEG LEAEDWAQGV VEASGGFGGY SVQEEAQFPT 500
    LHFLEGGEDS DSDSDEEEDD EEEDEEDEDE EDDEDGDEVP VPSFGEAMAY 550
    FAMVKRYLTS FPIDDRVQSH ILHLEHDLVH VTRKNHARQA GVRGLGHQS 599
    Length:599
    Mass (Da):65,381
    Last modified:July 27, 2011 - v2
    Checksum:iEBDB7C76BA87DC73
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti145 – 1451S → T in CAA38878. (PubMed:1893793)Curated
    Sequence conflicti150 – 1523APA → PQP in CAA38878. (PubMed:1893793)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55038 Genomic DNA. Translation: CAA38878.1.
    AL831736 Genomic DNA. No translation available.
    BC053333 mRNA. Translation: AAH53333.1.
    BC071269 mRNA. Translation: AAH71269.1.
    BC075733 mRNA. Translation: AAH75733.1.
    CCDSiCCDS16757.1.
    RefSeqiNP_031708.2. NM_007682.2.
    UniGeneiMm.440169.

    Genome annotation databases

    EnsembliENSMUST00000089510; ENSMUSP00000086938; ENSMUSG00000068267.
    GeneIDi12616.
    KEGGimmu:12616.
    UCSCiuc008mkx.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55038 Genomic DNA. Translation: CAA38878.1 .
    AL831736 Genomic DNA. No translation available.
    BC053333 mRNA. Translation: AAH53333.1 .
    BC071269 mRNA. Translation: AAH71269.1 .
    BC075733 mRNA. Translation: AAH75733.1 .
    CCDSi CCDS16757.1.
    RefSeqi NP_031708.2. NM_007682.2.
    UniGenei Mm.440169.

    3D structure databases

    ProteinModelPortali P27790.
    SMRi P27790. Positions 1-129, 540-585.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198675. 1 interaction.
    IntActi P27790. 1 interaction.
    MINTi MINT-237475.

    PTM databases

    PhosphoSitei P27790.

    Proteomic databases

    PRIDEi P27790.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000089510 ; ENSMUSP00000086938 ; ENSMUSG00000068267 .
    GeneIDi 12616.
    KEGGi mmu:12616.
    UCSCi uc008mkx.1. mouse.

    Organism-specific databases

    CTDi 1059.
    MGIi MGI:88376. Cenpb.

    Phylogenomic databases

    eggNOGi NOG241149.
    GeneTreei ENSGT00740000115260.
    HOGENOMi HOG000111537.
    HOVERGENi HBG050890.
    KOi K11496.
    OMAi KRRQLTF.
    OrthoDBi EOG7HTHGS.
    TreeFami TF101131.

    Miscellaneous databases

    NextBioi 281782.
    PROi P27790.
    SOURCEi Search...

    Gene expression databases

    Bgeei P27790.
    CleanExi MM_CENPB.
    Genevestigatori P27790.

    Family and domain databases

    Gene3Di 1.10.10.60. 2 hits.
    InterProi IPR015115. Centromere_CenpB_dimerisation.
    IPR004875. DDE_SF_endonuclease_CENPB-like.
    IPR009057. Homeodomain-like.
    IPR006600. HTH_CenpB_DNA-bd_dom.
    IPR007889. HTH_Psq.
    [Graphical view ]
    Pfami PF09026. CENP-B_dimeris. 1 hit.
    PF04218. CENP-B_N. 1 hit.
    PF03184. DDE_1. 1 hit.
    PF03221. HTH_Tnp_Tc5. 1 hit.
    [Graphical view ]
    SMARTi SM00674. CENPB. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46689. SSF46689. 2 hits.
    PROSITEi PS51253. HTH_CENPB. 1 hit.
    PS50960. HTH_PSQ. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "CENP-B is a highly conserved mammalian centromere protein with homology to the helix-loop-helix family of proteins."
      Sullivan K.F., Glass C.A.
      Chromosoma 100:360-370(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: C57BL/6.
      Tissue: Liver.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      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].
      Strain: FVB/N.
      Tissue: Colon, Embryo, Jaw and Limb.
    4. "Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose) polymerase-1 protein and are poly(ADP-ribosyl)ated."
      Saxena A., Saffery R., Wong L.H., Kalitsis P., Choo K.H.
      J. Biol. Chem. 277:26921-26926(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: POLY-ADP-RIBOSYLATION BY PARP1.

    Entry informationi

    Entry nameiCENPB_MOUSE
    AccessioniPrimary (citable) accession number: P27790
    Secondary accession number(s): Q7TSG8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 115 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