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P07199 (CENPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 157. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Major centromere autoantigen B
Alternative name(s):
Centromere protein B
Short name=CENP-B
Gene names
Name:CENPB
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length599 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

Antiparallel homodimer. Interacts with CENPT. Ref.5 Ref.7 Ref.14

Subcellular location

Nucleus. Chromosomecentromere Ref.6.

Post-translational modification

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. Ref.11

Sequence similarities

Contains 1 HTH CENPB-type DNA-binding domain.

Contains 1 HTH psq-type DNA-binding domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.11
Chain2 – 599598Major centromere autoantigen B
PRO_0000126125

Regions

Domain2 – 5251HTH psq-type
Domain65 – 13672HTH CENPB-type
DNA binding28 – 4821H-T-H motif
DNA binding97 – 12933H-T-H motif
Region536 – 59964Homodimerization
Compositional bias404 – 46562Glu-rich (acidic)
Compositional bias508 – 53831Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue21N,N,N-trimethylglycine; alternate Ref.11
Modified residue21N,N-dimethylglycine; alternate Ref.11
Modified residue21N-methylglycine; alternate Ref.11
Modified residue1561Phosphoserine Ref.8 Ref.10
Modified residue1651Phosphoserine Ref.10
Modified residue3981Phosphothreonine Ref.10

Experimental info

Mutagenesis41K → Q: Abolishes N-terminal methylation. Ref.11
Sequence conflict5831R → M in CAA28918. Ref.4
Sequence conflict592 – 5932VR → LL in CAA28918. Ref.4

Secondary structure

......................... 599
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07199 [UniParc].

Last modified August 1, 1992. Version 2.
Checksum: 9B4B7DB957A914AA

FASTA59965,171
        10         20         30         40         50         60 
MGPKRRQLTF REKSRIIQEV EENPDLRKGE IARRFNIPPS TLSTILKNKR AILASERKYG 

        70         80         90        100        110        120 
VASTCRKTNK LSPYDKLEGL LIAWFQQIRA AGLPVKGIIL KEKALRIAEE LGMDDFTASN 

       130        140        150        160        170        180 
GWLDRFRRRH GVVSCSGVAR ARARNAAPRT PAAPASPAAV PSEGSGGSTT GWRAREEQPP 

       190        200        210        220        230        240 
SVAEGYASQD VFSATETSLW YDFLPDQAAG LCGGDGRPRQ ATQRLSVLLC ANADGSEKLP 

       250        260        270        280        290        300 
PLVAGKSAKP RAGQAGLPCD YTANSKGGVT TQALAKYLKA LDTRMAAESR RVLLLAGRLA 

       310        320        330        340        350        360 
AQSLDTSGLR HVQLAFFPPG TVHPLERGVV QQVKGHYRQA MLLKAMAALE GQDPSGLQLG 

       370        380        390        400        410        420 
LTEALHFVAA AWQAVEPSDI AACFREAGFG GGPNATITTS LKSEGEEEEE EEEEEEEEEG 

       430        440        450        460        470        480 
EGEEEEEEGE EEEEEGGEGE ELGEEEEVEE EGDVDSDEEE EEDEESSSEG LEAEDWAQGV 

       490        500        510        520        530        540 
VEAGGSFGAY GAQEEAQCPT LHFLEGGEDS DSDSEEEDDE EEDDEDEDDD DDEEDGDEVP 

       550        560        570        580        590 
VPSFGEAMAY FAMVKRYLTS FPIDDRVQSH ILHLEHDLVH VTRKNHARQA GVRGLGHQS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Molecular cloning of cDNA for CENP-B, the major human centromere autoantigen."
Earnshaw W.C., Sullivan K.F., Machlin P.S., Cooke C.A., Kaiser D.A., Pollard T.D., Rothfield N.F., Cleveland D.W.
J. Cell Biol. 104:817-829(1987) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS18735.
RefSeqNP_001801.1. NM_001810.5.
UniGeneHs.516855.
Hs.713340.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BW6NMR-A1-56[»]
1HLVX-ray2.50A1-129[»]
1UFIX-ray1.65A/B/C/D536-599[»]
ProteinModelPortalP07199.
SMRP07199. Positions 1-129, 540-585.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107488. 20 interactions.
IntActP07199. 18 interactions.
MINTMINT-2857560.
STRING9606.ENSP00000369075.

PTM databases

PhosphoSiteP07199.

Polymorphism databases

DMDM116109.

Proteomic databases

PaxDbP07199.
PeptideAtlasP07199.
PRIDEP07199.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000379751; ENSP00000369075; ENSG00000125817.
GeneID1059.
KEGGhsa:1059.
UCSCuc002wjk.3. human.

Organism-specific databases

CTD1059.
GeneCardsGC20M003764.
HGNCHGNC:1852. CENPB.
HPACAB011626.
HPA053507.
HPA054405.
MIM117140. gene.
neXtProtNX_P07199.
PharmGKBPA26397.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG241149.
HOGENOMHOG000111537.
HOVERGENHBG050890.
InParanoidP07199.
KOK11496.
OMAKRRQLTF.
OrthoDBEOG7HTHGS.
PhylomeDBP07199.
TreeFamTF101131.

Gene expression databases

ArrayExpressP07199.
BgeeP07199.
CleanExHS_CENPB.
GenevestigatorP07199.

Family and domain databases

Gene3D1.10.10.60. 2 hits.
InterProIPR015115. Centromere_CenpB_dimerisation.
IPR004875. DDE_SF_endonuclease_CENPB-like.
IPR009057. Homeodomain-like.
IPR006600. HTH_CenpB_DNA-bd_dom.
IPR007889. HTH_Psq.
[Graphical view]
PfamPF09026. CENP-B_dimeris. 1 hit.
PF04218. CENP-B_N. 1 hit.
PF03184. DDE_1. 1 hit.
PF03221. HTH_Tnp_Tc5. 1 hit.
[Graphical view]
SMARTSM00674. CENPB. 1 hit.
[Graphical view]
SUPFAMSSF46689. SSF46689. 2 hits.
PROSITEPS51253. HTH_CENPB. 1 hit.
PS50960. HTH_PSQ. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP07199.
GeneWikiCentromere_protein_B.
GenomeRNAi1059.
NextBio4432.
PROP07199.
SOURCESearch...

Entry information

Entry nameCENPB_HUMAN
AccessionPrimary (citable) accession number: P07199
Secondary accession number(s): Q96EI4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: August 1, 1992
Last modified: April 16, 2014
This is version 157 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 20

Human chromosome 20: entries, gene names and cross-references to MIM