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P07199

- CENPB_HUMAN

UniProt

P07199 - CENPB_HUMAN

Protein

Major centromere autoantigen B

Gene

CENPB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 161 (01 Oct 2014)
      Sequence version 2 (01 Aug 1992)
      Previous versions | rss
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    Functioni

    Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp 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.

    Regions

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

    GO - Molecular functioni

    1. centromeric DNA binding Source: BHF-UCL
    2. chromatin binding Source: UniProtKB
    3. satellite DNA binding Source: UniProtKB
    4. sequence-specific DNA binding Source: BHF-UCL

    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
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:1852. CENPB.

    Subcellular locationi

    Nucleus 1 PublicationPROSITE-ProRule annotation. Chromosomecentromere 1 Publication

    GO - Cellular componenti

    1. chromosome, centromeric region Source: BHF-UCL
    2. nucleus Source: HPA

    Keywords - Cellular componenti

    Centromere, Chromosome, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi4 – 41K → Q: Abolishes N-terminal methylation. 1 Publication

    Organism-specific databases

    PharmGKBiPA26397.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 599598Major centromere autoantigen BPRO_0000126125Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N,N,N-trimethylglycine; alternate1 Publication
    Modified residuei2 – 21N,N-dimethylglycine; alternate1 Publication
    Modified residuei2 – 21N-methylglycine; alternate1 Publication
    Modified residuei156 – 1561Phosphoserine2 Publications
    Modified residuei165 – 1651Phosphoserine1 Publication
    Modified residuei398 – 3981Phosphothreonine1 Publication

    Post-translational modificationi

    Poly-ADP-ribosylated by PARP1.By similarity
    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.1 Publication

    Keywords - PTMi

    ADP-ribosylation, Methylation, Phosphoprotein

    Proteomic databases

    MaxQBiP07199.
    PaxDbiP07199.
    PeptideAtlasiP07199.
    PRIDEiP07199.

    PTM databases

    PhosphoSiteiP07199.

    Expressioni

    Gene expression databases

    ArrayExpressiP07199.
    BgeeiP07199.
    CleanExiHS_CENPB.
    GenevestigatoriP07199.

    Organism-specific databases

    HPAiCAB011626.
    HPA053507.
    HPA054405.

    Interactioni

    Subunit structurei

    Antiparallel homodimer. Interacts with CENPT.4 Publications

    Protein-protein interaction databases

    BioGridi107488. 21 interactions.
    IntActiP07199. 18 interactions.
    MINTiMINT-2857560.
    STRINGi9606.ENSP00000369075.

    Structurei

    Secondary structure

    1
    599
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 63
    Helixi10 – 2213
    Beta strandi24 – 263
    Helixi28 – 358
    Helixi39 – 479
    Helixi49 – 5911
    Helixi60 – 645
    Helixi75 – 8814
    Helixi89 – 913
    Helixi97 – 11115
    Helixi120 – 12910
    Helixi544 – 55815
    Helixi565 – 58420

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1BW6NMR-A1-56[»]
    1HLVX-ray2.50A1-129[»]
    1UFIX-ray1.65A/B/C/D540-599[»]
    ProteinModelPortaliP07199.
    SMRiP07199. Positions 1-129, 540-585.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP07199.

    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 – 59964HomodimerizationAdd
    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.
    HOGENOMiHOG000111537.
    HOVERGENiHBG050890.
    InParanoidiP07199.
    KOiK11496.
    OMAiKRRQLTF.
    OrthoDBiEOG7HTHGS.
    PhylomeDBiP07199.
    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.

    P07199-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGPKRRQLTF REKSRIIQEV EENPDLRKGE IARRFNIPPS TLSTILKNKR    50
    AILASERKYG VASTCRKTNK LSPYDKLEGL LIAWFQQIRA AGLPVKGIIL 100
    KEKALRIAEE LGMDDFTASN GWLDRFRRRH GVVSCSGVAR ARARNAAPRT 150
    PAAPASPAAV PSEGSGGSTT GWRAREEQPP SVAEGYASQD VFSATETSLW 200
    YDFLPDQAAG LCGGDGRPRQ ATQRLSVLLC ANADGSEKLP PLVAGKSAKP 250
    RAGQAGLPCD YTANSKGGVT TQALAKYLKA LDTRMAAESR RVLLLAGRLA 300
    AQSLDTSGLR HVQLAFFPPG TVHPLERGVV QQVKGHYRQA MLLKAMAALE 350
    GQDPSGLQLG LTEALHFVAA AWQAVEPSDI AACFREAGFG GGPNATITTS 400
    LKSEGEEEEE EEEEEEEEEG EGEEEEEEGE EEEEEGGEGE ELGEEEEVEE 450
    EGDVDSDEEE EEDEESSSEG LEAEDWAQGV VEAGGSFGAY GAQEEAQCPT 500
    LHFLEGGEDS DSDSEEEDDE EEDDEDEDDD DDEEDGDEVP VPSFGEAMAY 550
    FAMVKRYLTS FPIDDRVQSH ILHLEHDLVH VTRKNHARQA GVRGLGHQS 599
    Length:599
    Mass (Da):65,171
    Last modified:August 1, 1992 - v2
    Checksum:i9B4B7DB957A914AA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti583 – 5831R → M in CAA28918. (PubMed:2435739)Curated
    Sequence conflicti592 – 5932VR → LL in CAA28918. (PubMed:2435739)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55039 Genomic DNA. Translation: CAA38879.1.
    AL109804 Genomic DNA. Translation: CAC17547.1.
    BC012297 mRNA. Translation: AAH12297.1.
    BC053847 mRNA. Translation: AAH53847.1.
    X05299 mRNA. Translation: CAA28918.1.
    CCDSiCCDS13064.1.
    PIRiS18735.
    RefSeqiNP_001801.1. NM_001810.5.
    UniGeneiHs.516855.
    Hs.713340.

    Genome annotation databases

    EnsembliENST00000379751; ENSP00000369075; ENSG00000125817.
    GeneIDi1059.
    KEGGihsa:1059.
    UCSCiuc002wjk.3. human.

    Polymorphism databases

    DMDMi116109.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X55039 Genomic DNA. Translation: CAA38879.1 .
    AL109804 Genomic DNA. Translation: CAC17547.1 .
    BC012297 mRNA. Translation: AAH12297.1 .
    BC053847 mRNA. Translation: AAH53847.1 .
    X05299 mRNA. Translation: CAA28918.1 .
    CCDSi CCDS13064.1.
    PIRi S18735.
    RefSeqi NP_001801.1. NM_001810.5.
    UniGenei Hs.516855.
    Hs.713340.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BW6 NMR - A 1-56 [» ]
    1HLV X-ray 2.50 A 1-129 [» ]
    1UFI X-ray 1.65 A/B/C/D 540-599 [» ]
    ProteinModelPortali P07199.
    SMRi P07199. Positions 1-129, 540-585.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107488. 21 interactions.
    IntActi P07199. 18 interactions.
    MINTi MINT-2857560.
    STRINGi 9606.ENSP00000369075.

    PTM databases

    PhosphoSitei P07199.

    Polymorphism databases

    DMDMi 116109.

    Proteomic databases

    MaxQBi P07199.
    PaxDbi P07199.
    PeptideAtlasi P07199.
    PRIDEi P07199.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000379751 ; ENSP00000369075 ; ENSG00000125817 .
    GeneIDi 1059.
    KEGGi hsa:1059.
    UCSCi uc002wjk.3. human.

    Organism-specific databases

    CTDi 1059.
    GeneCardsi GC20M003764.
    HGNCi HGNC:1852. CENPB.
    HPAi CAB011626.
    HPA053507.
    HPA054405.
    MIMi 117140. gene.
    neXtProti NX_P07199.
    PharmGKBi PA26397.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG241149.
    HOGENOMi HOG000111537.
    HOVERGENi HBG050890.
    InParanoidi P07199.
    KOi K11496.
    OMAi KRRQLTF.
    OrthoDBi EOG7HTHGS.
    PhylomeDBi P07199.
    TreeFami TF101131.

    Miscellaneous databases

    EvolutionaryTracei P07199.
    GeneWikii Centromere_protein_B.
    GenomeRNAii 1059.
    NextBioi 4432.
    PROi P07199.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07199.
    Bgeei P07199.
    CleanExi HS_CENPB.
    Genevestigatori P07199.

    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].
    2. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    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].
      Tissue: Uterus.
    4. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-599.
    5. "A human centromere protein, CENP-B, has a DNA binding domain containing four potential alpha helices at the NH2 terminus, which is separable from dimerizing activity."
      Yoda K., Kitagawa K., Masumoto H., Muro Y., Okazaki T.
      J. Cell Biol. 119:1413-1427(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBUNIT, DOMAINS.
    6. "Assembly of the inner kinetochore proteins CENP-A and CENP-B in living human cells."
      Orthaus S., Biskup C., Hoffmann B., Hoischen C., Ohndorf S., Benndorf K., Diekmann S.
      ChemBioChem 9:77-92(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    7. "Live-cell imaging reveals sustained centromere binding of CENP-T via CENP-A and CENP-B."
      Hellwig D., Muench S., Orthaus S., Hoischen C., Hemmerich P., Diekmann S.
      J. Biophotonics 1:245-254(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CENPT.
    8. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
      Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
      J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156; SER-165 AND THR-398, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. "Identification of novel alpha-n-methylation of CENP-B that regulates its binding to the centromeric DNA."
      Dai X., Otake K., You C., Cai Q., Wang Z., Masumoto H., Wang Y.
      J. Proteome Res. 12:4167-4175(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE OF INITIATOR METHIONINE, METHYLATION AT GLY-2, MUTAGENESIS OF LYS-4.
    12. "A helix-turn-helix structure unit in human centromere protein B (CENP-B)."
      Iwahara J., Kigawa T., Kitagawa K., Masumoto H., Okazaki T., Yokoyama S.
      EMBO J. 17:827-837(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 1-56.
    13. "Crystal structure of the CENP-B protein-DNA complex: the DNA-binding domains of CENP-B induce kinks in the CENP-B box DNA."
      Tanaka Y., Nureki O., Kurumizaka H., Fukai S., Kawaguchi S., Ikuta M., Iwahara J., Okazaki T., Yokoyama S.
      EMBO J. 20:6612-6618(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-129 IN COMPLEX WITH DNA, H-T-H MOTIF.
    14. "Crystal structure of the human centromere protein B (CENP-B) dimerization domain at 1.65-A resolution."
      Tawaramoto M.S., Park S.Y., Tanaka Y., Nureki O., Kurumizaka H., Yokoyama S.
      J. Biol. Chem. 278:51454-51461(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 536-599, SUBUNIT.

    Entry informationi

    Entry nameiCENPB_HUMAN
    AccessioniPrimary (citable) accession number: P07199
    Secondary accession number(s): Q96EI4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: August 1, 1992
    Last modified: October 1, 2014
    This is version 161 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3