CENPB_CRIGR
ID CENPB_CRIGR Reviewed; 606 AA.
AC P48988;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Major centromere autoantigen B;
DE Short=Centromere protein B;
DE AltName: Full=CENP-B;
GN Name=CENPB;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Ovary;
RX PubMed=8652663; DOI=10.1016/0167-4781(96)00039-5;
RA Bejarano L.A., Valdivia M.M.;
RT "Molecular cloning of an intronless gene for the hamster centromere antigen
RT CENP-B.";
RL Biochim. Biophys. Acta 1307:21-25(1996).
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:0000250|UniProtKB:P27790}.
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U20951; AAB06494.1; -; Genomic_DNA.
DR PIR; S70358; S70358.
DR RefSeq; NP_001231328.1; NM_001244399.1.
DR AlphaFoldDB; P48988; -.
DR SMR; P48988; -.
DR STRING; 10029.NP_001231328.1; -.
DR GeneID; 100689274; -.
DR KEGG; cge:100689274; -.
DR CTD; 1059; -.
DR eggNOG; KOG3105; Eukaryota.
DR OrthoDB; 1343623at2759; -.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003682; F:chromatin binding; IEA:InterPro.
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 3: Inferred from homology;
KW ADP-ribosylation; Centromere; Chromosome; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P07199"
FT CHAIN 2..606
FT /note="Major centromere autoantigen B"
FT /id="PRO_0000126124"
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 138..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 504..549
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 543..606
FT /note="Homodimerization"
FT /evidence="ECO:0000250"
FT COMPBIAS 404..477
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 515..547
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"
SQ SEQUENCE 606 AA; 66407 MW; 63D0EEEE5551D48E CRC64;
MGPKRRQLTF REKSRIIQEV EENPDLRKGE IARRFNIPPS TLSTILKNKR AILASERKYG
VASTCRKTNK LSPYDKLEGL LIAWFQQIRA AGLPVKGIIL KEKALRIAEE LGMDDFTASN
GWLDRFRRRH GVVACSGVTR SRARTSTPRA PAAPAGPAAV PSEGSGGSTP GWRTREEQPP
SVAEGYASQD VFSATETSLW YDFLSDQASG LWGGDGTARQ ATQRLSVLLC ANRDGSEKLP
PLVAGKSAKP RASQGGLPCD YTANSKGGVT TQALAKYLKA LDTRMAAESR RVLLLAGRLA
AQSLDTSGLR HVQLAFFPPG TVHPLERGVV QQVKGHYRQA MLLKAMAALE GQDPSGLQLG
LVEALHFVAA AWQAVEPADI ATCFREAGFG GGLNATITTS FKSEGEEEEE EEEEEEEEEE
EEGEGEEEEE EEEEGEEEGG EGEEVGEEEE VEEEGDESDE EEEEEEEEEE ESSSEGLEAE
DWAQGVVEAS GGFGGYSVQE EAQCPTLHFL EGGEDSDSDS DEEEEDEEED EEDEEDDDDD
EDGDEVPVPS FGEAMAYFAM VKRYLTSFPI DDRVQSHILH LEHDLVHVTR KNHAWQAGVR
GLGHQS
