P07199 (CENPB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Major centromere autoantigen B

Alternative name(s):
Centromere protein B
Short name=CENP-B

Gene names

Name:

CENPB

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	599 AA.
Sequence status	Complete.
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.7
Subcellular location	Nucleus. Chromosome › centromere Ref.6.
Post-translational modification	Poly-ADP-ribosylated by PARP1 By similarity.
Sequence similarities	Contains 1 HTH CENPB-type DNA-binding domain. Contains 1 HTH psq-type DNA-binding domain.

Ontologies

Keywords
Cellular component	Centromere Chromosome Nucleus
Ligand	DNA-binding
PTM	ADP-ribosylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular_component	chromosome, centromeric region Inferred from direct assay PubMed 11682612. Source: BHF-UCL nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	centromeric DNA binding Inferred by curator PubMed 11682612. Source: BHF-UCL chromatin binding Non-traceable author statement Ref.1. Source: UniProtKB satellite DNA binding Non-traceable author statement Ref.1. 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.8 Ref.9

Modified residue

165

1

Phosphoserine Ref.9

Modified residue

398

1

Phosphothreonine Ref.9

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

.

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599

Helix Strand Turn

Details...

Beta strand

4 – 6

3

Helix

10 – 22

13

Beta strand

24 – 26

3

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

120 – 129

10

Helix

544 – 558

15

Helix

565 – 584

20

Sequences

	Sequence		Length	Mass (Da)
	P07199 [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] [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]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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. NM_001810.5.

UniGene

Hs.516855.
Hs.713340.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P07199.

ModBase

Search...

Protein-protein interaction databases

IntAct

P07199. 8 interactions.

MINT

MINT-2857560.

STRING

9606.ENSP00000369075.

PTM databases

PhosphoSite

P07199.

Polymorphism databases

DMDM

116109.

Proteomic databases

PaxDb

P07199.

PeptideAtlas

P07199.

PRIDE

P07199.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379751; ENSP00000369075; ENSG00000125817.

GeneID

1059.

KEGG

hsa:1059.

UCSC

uc002wjk.3. human.

Organism-specific databases

CTD

1059.

GeneCards

GC20M003764.

HGNC

HGNC:1852. CENPB.

HPA

CAB011626.

MIM

117140. gene.

neXtProt

NX_P07199.

PharmGKB

PA26397.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG241149.

HOGENOM

HOG000111537.

HOVERGEN

HBG050890.

InParanoid

P07199.

KO

K11496.

OMA

KRRQLTF.

OrthoDB

EOG444KK8.

PhylomeDB

P07199.

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

Gene3D

1.10.10.60. 2 hits.

InterPro

IPR015115. Centromere_CenpB_dimerisation.
IPR004875. DDE_SF_endonuclease_CENPB-like.
IPR009057. Homeodomain-like.
IPR006600. HTH_CenpB_DNA-bd_dom.
IPR007889. HTH_Psq.
[Graphical view]

Pfam

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]

SMART

SM00674. CENPB. 1 hit.
[Graphical view]

SUPFAM

SSF46689. Homeodomain_like. 2 hits.

PROSITE

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

ProtoNet

Search...

Other

EvolutionaryTrace

P07199.

GenomeRNAi

1059.

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:	May 1, 2013
This is version 149 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

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.