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P07199

- CENPB_HUMAN

UniProt

P07199 - CENPB_HUMAN

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Protein

Major centromere autoantigen B

Gene

CENPB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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 Source: UniProtKB
  2. chromosome, centromeric region Source: UniProtKB
  3. nucleus Source: HPA
Complete GO annotation...

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

BgeeiP07199.
CleanExiHS_CENPB.
ExpressionAtlasiP07199. baseline and differential.
GenevestigatoriP07199.

Organism-specific databases

HPAiCAB011626.
HPA053507.
HPA054405.

Interactioni

Subunit structurei

Antiparallel homodimer. Interacts with CENPT.4 Publications

Protein-protein interaction databases

BioGridi107488. 23 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 – 63Combined sources
Helixi10 – 2213Combined sources
Beta strandi24 – 263Combined sources
Helixi28 – 358Combined sources
Helixi39 – 479Combined sources
Helixi49 – 5911Combined sources
Helixi60 – 645Combined sources
Helixi75 – 8814Combined sources
Helixi89 – 913Combined sources
Helixi97 – 11115Combined sources
Helixi120 – 12910Combined sources
Helixi544 – 55815Combined sources
Helixi565 – 58420Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
GeneTreeiENSGT00760000119149.
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

        10         20         30         40         50
MGPKRRQLTF REKSRIIQEV EENPDLRKGE IARRFNIPPS TLSTILKNKR
60 70 80 90 100
AILASERKYG VASTCRKTNK LSPYDKLEGL LIAWFQQIRA AGLPVKGIIL
110 120 130 140 150
KEKALRIAEE LGMDDFTASN GWLDRFRRRH GVVSCSGVAR ARARNAAPRT
160 170 180 190 200
PAAPASPAAV PSEGSGGSTT GWRAREEQPP SVAEGYASQD VFSATETSLW
210 220 230 240 250
YDFLPDQAAG LCGGDGRPRQ ATQRLSVLLC ANADGSEKLP PLVAGKSAKP
260 270 280 290 300
RAGQAGLPCD YTANSKGGVT TQALAKYLKA LDTRMAAESR RVLLLAGRLA
310 320 330 340 350
AQSLDTSGLR HVQLAFFPPG TVHPLERGVV QQVKGHYRQA MLLKAMAALE
360 370 380 390 400
GQDPSGLQLG LTEALHFVAA AWQAVEPSDI AACFREAGFG GGPNATITTS
410 420 430 440 450
LKSEGEEEEE EEEEEEEEEG EGEEEEEEGE EEEEEGGEGE ELGEEEEVEE
460 470 480 490 500
EGDVDSDEEE EEDEESSSEG LEAEDWAQGV VEAGGSFGAY GAQEEAQCPT
510 520 530 540 550
LHFLEGGEDS DSDSEEEDDE EEDDEDEDDD DDEEDGDEVP VPSFGEAMAY
560 570 580 590
FAMVKRYLTS FPIDDRVQSH ILHLEHDLVH VTRKNHARQA GVRGLGHQS
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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. 23 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.
GeneTreei ENSGT00760000119149.
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

Bgeei P07199.
CleanExi HS_CENPB.
ExpressionAtlasi P07199. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 163 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