CENPB_MOUSE
ID CENPB_MOUSE Reviewed; 599 AA.
AC P27790; Q7TSG8;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Major centromere autoantigen B;
DE AltName: Full=Centromere protein B;
DE Short=CENP-B;
GN Name=Cenpb; Synonyms=Cenp-b;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Liver;
RX PubMed=1893793; DOI=10.1007/bf00337514;
RA Sullivan K.F., Glass C.A.;
RT "CENP-B is a highly conserved mammalian centromere protein with homology to
RT the helix-loop-helix family of proteins.";
RL Chromosoma 100:360-370(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Colon, Embryo, Jaw, and Limb;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP POLY-ADP-RIBOSYLATION BY PARP1.
RX PubMed=12011073; DOI=10.1074/jbc.m200620200;
RA Saxena A., Saffery R., Wong L.H., Kalitsis P., Choo K.H.;
RT "Centromere proteins Cenpa, Cenpb, and Bub3 interact with poly(ADP-ribose)
RT polymerase-1 protein and are poly(ADP-ribosyl)ated.";
RL J. Biol. Chem. 277:26921-26926(2002).
CC -!- FUNCTION: Interacts with centromeric heterochromatin in chromosomes and
CC binds to a specific 17 bp subset of alphoid satellite DNA, called the
CC CENP-B box. May organize arrays of centromere satellite DNA into a
CC higher-order structure which then directs centromere formation and
CC kinetochore assembly in mammalian chromosomes.
CC {ECO:0000250|UniProtKB:P07199}.
CC -!- SUBUNIT: Antiparallel homodimer. Interacts with CENPT. Identified in a
CC centromere complex containing histones H2A, H2B and H4, and at least
CC CENPA, CENPB, CENPC, CENPT, CENPN, HJURP, SUPT16H, SSRP1 and RSF1.
CC {ECO:0000250|UniProtKB:P07199}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P07199}.
CC Chromosome, centromere {ECO:0000250|UniProtKB:P07199}.
CC -!- PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000269|PubMed:12011073}.
CC -!- PTM: N-terminally methylated by METTL11A/NTM1. Alpha-N-methylation is
CC stimulated in response to extracellular stimuli, including increased
CC cell density and heat shock, and seems to facilitate binding to CENP-B
CC boxes. Chromatin-bound CENP-B is primarily trimethylated.
CC {ECO:0000250|UniProtKB:P07199}.
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DR EMBL; X55038; CAA38878.1; -; Genomic_DNA.
DR EMBL; AL831736; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC053333; AAH53333.1; -; mRNA.
DR EMBL; BC071269; AAH71269.1; -; mRNA.
DR EMBL; BC075733; AAH75733.1; -; mRNA.
DR CCDS; CCDS16757.1; -.
DR RefSeq; NP_031708.2; NM_007682.3.
DR AlphaFoldDB; P27790; -.
DR SMR; P27790; -.
DR BioGRID; 198675; 2.
DR IntAct; P27790; 1.
DR STRING; 10090.ENSMUSP00000086938; -.
DR iPTMnet; P27790; -.
DR PhosphoSitePlus; P27790; -.
DR MaxQB; P27790; -.
DR PaxDb; P27790; -.
DR PeptideAtlas; P27790; -.
DR PRIDE; P27790; -.
DR ProteomicsDB; 280058; -.
DR Antibodypedia; 23700; 138 antibodies from 20 providers.
DR Ensembl; ENSMUST00000089510; ENSMUSP00000086938; ENSMUSG00000068267.
DR GeneID; 12616; -.
DR KEGG; mmu:12616; -.
DR UCSC; uc008mkx.1; mouse.
DR CTD; 1059; -.
DR MGI; MGI:88376; Cenpb.
DR VEuPathDB; HostDB:ENSMUSG00000068267; -.
DR eggNOG; KOG3105; Eukaryota.
DR GeneTree; ENSGT00940000162810; -.
DR HOGENOM; CLU_018294_10_0_1; -.
DR InParanoid; P27790; -.
DR OMA; GGLPCDY; -.
DR OrthoDB; 1343623at2759; -.
DR PhylomeDB; P27790; -.
DR TreeFam; TF101131; -.
DR BioGRID-ORCS; 12616; 4 hits in 76 CRISPR screens.
DR ChiTaRS; Cenpb; mouse.
DR PRO; PR:P27790; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; P27790; protein.
DR Bgee; ENSMUSG00000068267; Expressed in hindlimb stylopod muscle and 228 other tissues.
DR Genevisible; P27790; MM.
DR GO; GO:0005694; C:chromosome; ISO:MGI.
DR GO; GO:0000775; C:chromosome, centromeric region; ISO:MGI.
DR GO; GO:0000779; C:condensed chromosome, centromeric region; IDA:MGI.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005721; C:pericentric heterochromatin; IDA:MGI.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0003696; F:satellite DNA binding; IEA:InterPro.
DR Gene3D; 1.10.287.1090; -; 1.
DR InterPro; IPR033062; CENP-B.
DR InterPro; IPR015115; CenpB_C.
DR InterPro; IPR004875; DDE_SF_endonuclease_dom.
DR InterPro; IPR034882; Dimerisation_CENP-B_sf.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR006600; HTH_CenpB_DNA-bd_dom.
DR InterPro; IPR007889; HTH_Psq.
DR PANTHER; PTHR19303:SF25; PTHR19303:SF25; 1.
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; SSF101160; SSF101160; 1.
DR SUPFAM; SSF46689; SSF46689; 2.
DR PROSITE; PS51253; HTH_CENPB; 1.
DR PROSITE; PS50960; HTH_PSQ; 1.
PE 2: Evidence at transcript level;
KW ADP-ribosylation; Centromere; Chromosome; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07199"
FT CHAIN 2..599
FT /note="Major centromere autoantigen B"
FT /id="PRO_0000126126"
FT DOMAIN 2..52
FT /note="HTH psq-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00320"
FT DOMAIN 65..136
FT /note="HTH CENPB-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00583"
FT DNA_BIND 28..48
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT DNA_BIND 97..129
FT /note="H-T-H motif"
FT /evidence="ECO:0000250"
FT REGION 143..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..543
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 536..599
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 404..471
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 509..540
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N,N,N-trimethylglycine"
FT /evidence="ECO:0000250|UniProtKB:P07199"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P07199"
FT MOD_RES 396
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07199"
FT MOD_RES 398
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P07199"
FT CROSSLNK 246
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P07199"
FT CONFLICT 145
FT /note="S -> T (in Ref. 1; CAA38878)"
FT /evidence="ECO:0000305"
FT CONFLICT 150..152
FT /note="APA -> PQP (in Ref. 1; CAA38878)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 599 AA; 65381 MW; EBDB7C76BA87DC73 CRC64;
MGPKRRQLTF REKSRIIQEV EENPDLRKGE IARRFNIPPS TLSTILKNKR AILASERKYG
VASTCRKTNK LSPYDKLEGL LIAWFQQIRA AGLPVKGIIL KEKALRIAEE LGMDDFTASN
GWLDRFRRRH GVVACSGVTR SRARSSAPRA PAAPAGPATV PSEGSGGSTP GWHTREEQPP
SVAEGYASQD VFSATETSLW YDFLSDQASG LWGGDGPARQ ATQRLSVLLC ANADGSEKLP
PLVAGKSAKP RAGQGGLPCD YTANSKGGVT TQALAKYLKA LDTRMAAESR RVLLLAGRLA
AQSLDTSGLR HVQLAFFPPG TVHPLERGVV QQVKGHYRQA MLLKAMAALE GQDPSGLQLG
LVEALHFVAA AWQAVEPSDI ATCFREAGFG GGLNATITTS FKSEGEEEEE EEEEEEEEEE
EEGEGEEEEE EEEEGEEEGG EGEEEGEEEV EEEGEVDDSD EEEEESSSEG LEAEDWAQGV
VEASGGFGGY SVQEEAQFPT LHFLEGGEDS DSDSDEEEDD EEEDEEDEDE EDDEDGDEVP
VPSFGEAMAY FAMVKRYLTS FPIDDRVQSH ILHLEHDLVH VTRKNHARQA GVRGLGHQS
