ID   CENPB_HUMAN             Reviewed;         599 AA.
AC   P07199;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1992, sequence version 2.
DT   14-DEC-2011, entry version 136.
DE   RecName: Full=Major centromere autoantigen B;
DE   AltName: Full=Centromere protein B;
DE            Short=CENP-B;
GN   Name=CENPB;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91372020; PubMed=1893793; DOI=10.1007/BF00337514;
RA   Sullivan K.F., Glass C.A.;
RT   "CENP-B is a highly conserved mammalian centromere protein with
RT   homology to the helix-loop-helix family of proteins.";
RL   Chromosoma 100:360-370(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=21638749; PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
RA   Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA   Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA   Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA   Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA   Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA   Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
RA   Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA   Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA   Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA   Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA   Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA   Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA   Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 6-599.
RX   MEDLINE=87166180; PubMed=2435739; DOI=10.1083/jcb.104.4.817;
RA   Earnshaw W.C., Sullivan K.F., Machlin P.S., Cooke C.A., Kaiser D.A.,
RA   Pollard T.D., Rothfield N.F., Cleveland D.W.;
RT   "Molecular cloning of cDNA for CENP-B, the major human centromere
RT   autoantigen.";
RL   J. Cell Biol. 104:817-829(1987).
RN   [5]
RP   SUBUNIT, AND DOMAINS.
RX   MEDLINE=93107144; PubMed=1469042; DOI=10.1083/jcb.119.6.1413;
RA   Yoda K., Kitagawa K., Masumoto H., Muro Y., Okazaki T.;
RT   "A human centromere protein, CENP-B, has a DNA binding domain
RT   containing four potential alpha helices at the NH2 terminus, which is
RT   separable from dimerizing activity.";
RL   J. Cell Biol. 119:1413-1427(1992).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-165, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Cervix adenocarcinoma;
RX   PubMed=16565220; DOI=10.1073/pnas.0507066103;
RA   Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
RT   "Phosphoproteome analysis of the human mitotic spindle.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-486, AND
RP   MASS SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=19007248; DOI=10.1021/ac801708p;
RA   Wang B., Malik R., Nigg E.A., Korner R.;
RT   "Evaluation of the low-specificity protease elastase for large-scale
RT   phosphoproteome analysis.";
RL   Anal. Chem. 80:9526-9533(2008).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=18072184; DOI=10.1002/cbic.200700358;
RA   Orthaus S., Biskup C., Hoffmann B., Hoischen C., Ohndorf S.,
RA   Benndorf K., Diekmann S.;
RT   "Assembly of the inner kinetochore proteins CENP-A and CENP-B in
RT   living human cells.";
RL   ChemBioChem 9:77-92(2008).
RN   [9]
RP   INTERACTION WITH CENPT.
RX   PubMed=19412974; DOI=10.1002/jbio.200810014;
RA   Hellwig D., Muench S., Orthaus S., Hoischen C., Hemmerich P.,
RA   Diekmann S.;
RT   "Live-cell imaging reveals sustained centromere binding of CENP-T via
RT   CENP-A and CENP-B.";
RL   J. Biophotonics 1:245-254(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA   Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT   efficient phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA   Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT   a refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [12]
RP   STRUCTURE BY NMR OF 1-56.
RX   MEDLINE=98119825; PubMed=9451007; DOI=10.1093/emboj/17.3.827;
RA   Iwahara J., Kigawa T., Kitagawa K., Masumoto H., Okazaki T.,
RA   Yokoyama S.;
RT   "A helix-turn-helix structure unit in human centromere protein B
RT   (CENP-B).";
RL   EMBO J. 17:827-837(1998).
CC   -!- FUNCTION: Interacts with centromeric heterochromatin in
CC       chromosomes and binds to a specific subset of alphoid satellite
CC       DNA, called the CENP-B box. May organize arrays of centromere
CC       satellite DNA into a higher order structure which then directs
CC       centromere formation and kinetochore assembly in mammalian
CC       chromosomes.
CC   -!- SUBUNIT: Homodimer. Interacts with CENPT.
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere.
CC   -!- PTM: Poly-ADP-ribosylated by PARP1 (By similarity).
CC   -!- SIMILARITY: Contains 1 HTH CENPB-type DNA-binding domain.
CC   -!- SIMILARITY: Contains 1 HTH psq-type DNA-binding domain.
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DR   EMBL; X55039; CAA38879.1; -; Genomic_DNA.
DR   EMBL; AL109804; CAC17547.1; -; Genomic_DNA.
DR   EMBL; BC053847; AAH53847.1; -; mRNA.
DR   EMBL; X05299; CAA28918.1; -; mRNA.
DR   IPI; IPI00010388; -.
DR   PIR; S18735; S18735.
DR   RefSeq; NP_001801.1; NM_001810.5.
DR   UniGene; Hs.516855; -.
DR   PDB; 1BW6; NMR; -; A=1-56.
DR   PDB; 1HLV; X-ray; 2.50 A; A=1-129.
DR   PDB; 1UFI; X-ray; 1.65 A; A/B/C/D=540-599.
DR   PDBsum; 1BW6; -.
DR   PDBsum; 1HLV; -.
DR   PDBsum; 1UFI; -.
DR   ProteinModelPortal; P07199; -.
DR   SMR; P07199; 1-129, 540-585.
DR   IntAct; P07199; 8.
DR   MINT; MINT-2857560; -.
DR   STRING; P07199; -.
DR   PhosphoSite; P07199; -.
DR   DMDM; 116109; -.
DR   PeptideAtlas; P07199; -.
DR   PRIDE; P07199; -.
DR   Ensembl; ENST00000379751; ENSP00000369075; ENSG00000125817.
DR   GeneID; 1059; -.
DR   KEGG; hsa:1059; -.
DR   UCSC; uc002wjk.1; human.
DR   CTD; 1059; -.
DR   GeneCards; GC20M003712; -.
DR   H-InvDB; HIX0203068; -.
DR   HGNC; HGNC:1852; CENPB.
DR   HPA; CAB011626; -.
DR   MIM; 117140; gene.
DR   neXtProt; NX_P07199; -.
DR   PharmGKB; PA26397; -.
DR   eggNOG; prNOG11878; -.
DR   HOGENOM; HBG282807; -.
DR   HOVERGEN; HBG050890; -.
DR   InParanoid; P07199; -.
DR   OMA; TASNGWL; -.
DR   OrthoDB; EOG444KK8; -.
DR   PhylomeDB; P07199; -.
DR   Pathway_Interaction_DB; foxm1pathway; FOXM1 transcription factor network.
DR   NextBio; 4432; -.
DR   ArrayExpress; P07199; -.
DR   Bgee; P07199; -.
DR   CleanEx; HS_CENPB; -.
DR   Genevestigator; P07199; -.
DR   GermOnline; ENSG00000125817; Homo sapiens.
DR   GO; GO:0000775; C:chromosome, centromeric region; IDA:BHF-UCL.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019237; F:centromeric DNA binding; IC:BHF-UCL.
DR   GO; GO:0003682; F:chromatin binding; NAS:UniProtKB.
DR   GO; GO:0003696; F:satellite DNA binding; NAS:UniProtKB.
DR   GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro.
DR   InterPro; IPR015115; Centromere_CenpB_dimerisation.
DR   InterPro; IPR006695; Centromere_CenpB_DNA-db_1.
DR   InterPro; IPR004875; DDE_SF_endonuclease_CENPB-like.
DR   InterPro; IPR009057; Homeodomain-like.
DR   InterPro; IPR012287; Homeodomain-rel.
DR   InterPro; IPR011526; HTH_psq-like.
DR   InterPro; IPR006600; Pogo/CenpB/PDC2_DNA-bd_HTH.
DR   Gene3D; G3DSA:1.10.10.60; Homeodomain-rel; 2.
DR   KO; K11496; -.
DR   Pfam; PF09026; Cenp-B_dimeris; 1.
DR   Pfam; PF04218; CENP-B_N; 1.
DR   Pfam; PF03184; DDE_1; 1.
DR   Pfam; PF03221; HTH_Tnp_Tc5; 1.
DR   SMART; SM00674; CENPB; 1.
DR   SUPFAM; SSF46689; Homeodomain_like; 2.
DR   PROSITE; PS51253; HTH_CENPB; 1.
DR   PROSITE; PS50960; HTH_PSQ; 1.
PE   1: Evidence at protein level;
KW   3D-structure; ADP-ribosylation; Centromere; Chromosome;
KW   Complete proteome; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome.
FT   CHAIN         1    599       Major centromere autoantigen B.
FT                                /FTId=PRO_0000126125.
FT   DOMAIN        1     52       HTH psq-type.
FT   DOMAIN       65    136       HTH CENPB-type.
FT   DNA_BIND     28     48       H-T-H motif.
FT   DNA_BIND     97    129       H-T-H motif.
FT   COMPBIAS    404    465       Glu-rich (acidic).
FT   COMPBIAS    508    538       Asp/Glu-rich (acidic).
FT   MOD_RES     156    156       Phosphoserine.
FT   MOD_RES     165    165       Phosphoserine.
FT   MOD_RES     486    486       Phosphoserine.
FT   CONFLICT    583    583       R -> M (in Ref. 4; CAA28918).
FT   CONFLICT    592    593       VR -> LL (in Ref. 4; CAA28918).
FT   HELIX        10     22
FT   HELIX        28     35
FT   HELIX        39     47
FT   HELIX        49     59
FT   HELIX        60     64
FT   HELIX        75     88
FT   HELIX        89     91
FT   HELIX        97    111
FT   HELIX       544    558
FT   HELIX       565    584
SQ   SEQUENCE   599 AA;  65171 MW;  9B4B7DB957A914AA CRC64;
     MGPKRRQLTF REKSRIIQEV EENPDLRKGE IARRFNIPPS TLSTILKNKR AILASERKYG
     VASTCRKTNK LSPYDKLEGL LIAWFQQIRA AGLPVKGIIL KEKALRIAEE LGMDDFTASN
     GWLDRFRRRH GVVSCSGVAR ARARNAAPRT PAAPASPAAV PSEGSGGSTT GWRAREEQPP
     SVAEGYASQD VFSATETSLW YDFLPDQAAG LCGGDGRPRQ ATQRLSVLLC ANADGSEKLP
     PLVAGKSAKP RAGQAGLPCD YTANSKGGVT TQALAKYLKA LDTRMAAESR RVLLLAGRLA
     AQSLDTSGLR HVQLAFFPPG TVHPLERGVV QQVKGHYRQA MLLKAMAALE GQDPSGLQLG
     LTEALHFVAA AWQAVEPSDI AACFREAGFG GGPNATITTS LKSEGEEEEE EEEEEEEEEG
     EGEEEEEEGE EEEEEGGEGE ELGEEEEVEE EGDVDSDEEE EEDEESSSEG LEAEDWAQGV
     VEAGGSFGAY GAQEEAQCPT LHFLEGGEDS DSDSEEEDDE EEDDEDEDDD DDEEDGDEVP
     VPSFGEAMAY FAMVKRYLTS FPIDDRVQSH ILHLEHDLVH VTRKNHARQA GVRGLGHQS
//