Reviewed, UniProtKB/Swiss-Prot P07199 (CENPB_HUMAN)

Names and origin

Protein names

Recommended name:
    Major centromere autoantigen B
      Short name=Centromere protein B
Alternative name(s):
    CENP-B

Gene names

Name:

CENPB

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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.
Subunit structure	Homodimer. Interacts with CENPT. Ref.5 Ref.9
Subcellular location	Nucleus. Centromere. Ref.8
Sequence similarities	Contains 1 HTH CENPB-type DNA-binding domain. Contains 1 HTH psq-type DNA-binding domain.

Ontologies

Keywords
Cellular component	Centromere Chromosomal protein Nucleus
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	regulation of transcription Inferred from electronic annotation. Source: InterPro
Cellular component	chromosome, centromeric region Ref.1 Non-traceable author statement. Source: UniProtKB nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chromatin binding Ref.1 Non-traceable author statement. Source: UniProtKB satellite DNA binding Ref.1 Non-traceable author statement. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 599

599

Major centromere autoantigen B

PRO_0000126125

Regions

Domain

1 – 52

52

HTH psq-type

Domain

65 – 136

72

HTH CENPB-type

DNA binding

28 – 48

21

H-T-H motif

DNA binding

97 – 129

33

H-T-H motif

Compositional bias

404 – 465

62

Glu-rich (acidic)

Compositional bias

508 – 538

31

Asp/Glu-rich (acidic)

Amino acid modifications

Modified residue

156

1

Phosphoserine Ref.6 Ref.7 Ref.10

Modified residue

165

1

Phosphoserine Ref.6

Modified residue

486

1

Phosphoserine Ref.7

Experimental info

Sequence conflict

583

1

R → M in CAA28918. Ref.4

Sequence conflict

592 – 593

2

VR → LL in CAA28918. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

599

Helix Strand Turn

Details...

Helix

10 – 22

13

Helix

28 – 35

8

Helix

39 – 47

9

Helix

49 – 59

11

Helix

60 – 64

5

Helix

75 – 88

14

Helix

89 – 91

3

Helix

97 – 111

15

Helix

544 – 558

15

Helix

565 – 584

20

Sequences

	Sequence		Length	Mass (Da)
	P07199-1 [UniParc]. Last modified August 1, 1992. Version 2. Checksum: 9B4B7DB957A914AA	FASTA	599	65,171
	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

References

	« Hide 'large scale' referencesShow '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: 1893793] [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: 11780052] [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: 15489334] [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: 2435739] [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: 1469042] [Abstract] Cited for: SUBUNIT, DOMAINS.
[6]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-165, MASS SPECTROMETRY. Tissue: Epithelium.
[7]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156 AND SER-486, MASS SPECTROMETRY.
[8]	"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: 18072184] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"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: 19412974] [Abstract] Cited for: INTERACTION WITH CENPT.
[10]	"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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-156, MASS SPECTROMETRY.
[11]	"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: 9451007] [Abstract] Cited for: STRUCTURE BY NMR OF 1-56.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X55039 Genomic DNA. Translation: CAA38879.1.
AL109804 Genomic DNA. Translation: CAC17547.1.
BC053847 mRNA. Translation: AAH53847.1.
X05299 mRNA. Translation: CAA28918.1.

IPI

IPI00010388.

PIR

S18735.

RefSeq

NP_001801.1.

UniGene

Hs.516855

3D structure databases

PDBPDBe

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	[»]

SMR

P07199. Positions 539-585.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07199. 3 interactions.

STRING

P07199.

PTM databases

PhosphoSite

P07199.

Proteomic databases

PeptideAtlas

P07199.

PRIDE

P07199.

Genome annotation databases

Ensembl

ENST00000379751; ENSP00000369075; ENSG00000125817; Homo sapiens. [Genome view]

GeneID

1059.

KEGG

hsa:1059.

UCSC

uc002wjk.1. human.

Organism-specific databases

CTD

1059.

GeneCards

GC20M003712.

H-InvDB

HIX0027657.

HGNC

HGNC:1852. CENPB.

HPA

CAB011626.

MIM

117140. gene.

PharmGKB

PA26397.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P07199.

HOVERGEN

P07199.

OMA

TASNGWL.

Enzyme and pathway databases

Pathway_Interaction_DB

foxm1pathway. FOXM1 transcription factor network.

Gene expression databases

ArrayExpress

P07199.

Bgee

P07199.

CleanEx

HS_CENPB.

Genevestigator

P07199.

GermOnline

ENSG00000125817. Homo sapiens.

Family and domain databases

InterPro

IPR015115. Centromere_CenpB_dimerisation.
IPR006695. Centromere_CenpB_DNA-db_1.
IPR015175. Centromere_CenpB_DNA-db_2.
IPR006600. Centromere_CenpB_HTH.
IPR004875. DDE_SF_endonuclease_CENPB-like.
IPR012287. Homeodomain-rel.
IPR011526. HTH_psq-like.
[Graphical view]

Gene3D

G3DSA:1.10.10.60. Homeodomain-rel. 2 hits.

Pfam

PF09026. Cenp-B_dimeris. 1 hit.
PF04218. CENP-B_N. 1 hit.
PF09091. CenpB-DNA-bind. 1 hit.
PF03184. DDE. 1 hit.
[Graphical view]

SMART

SM00674. CENPB. 1 hit.
[Graphical view]

PROSITE

PS51253. HTH_CENPB. 1 hit.
PS50960. HTH_PSQ. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

4432.

SOURCE

Search...

Entry information

Entry name

CENPB_HUMAN

Accession

Primary (citable) accession number: P07199

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	August 1, 1992
Last modified:	November 3, 2009
This is version 115 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Disclaimer

Any 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.