CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-002451
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Major centromere autoantigen B 
Protein Synonyms/Alias
 Centromere protein B; CENP-B 
Gene Name
 CENPB 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
58AILASERKYGVASTCubiquitination[1]
96RAAGLPVKGIILKEKubiquitination[1]
266CDYTANSKGGVTTQAubiquitination[1, 2, 3, 4, 5]
276VTTQALAKYLKALDTubiquitination[1, 6, 7]
279QALAKYLKALDTRMAubiquitination[1]
334RGVVQQVKGHYRQAMubiquitination[6, 7]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [3] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [4] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [6] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [7] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789
Functional Description
 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. 
Sequence Annotation
 DOMAIN 1 52 HTH psq-type.
 DOMAIN 65 136 HTH CENPB-type.
 DNA_BIND 28 48 H-T-H motif.
 DNA_BIND 97 129 H-T-H motif.
 MOD_RES 156 156 Phosphoserine.
 MOD_RES 165 165 Phosphoserine.
 MOD_RES 398 398 Phosphothreonine.  
Keyword
 3D-structure; ADP-ribosylation; Centromere; Chromosome; Complete proteome; DNA-binding; Nucleus; Phosphoprotein; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 599 AA 
Protein Sequence
MGPKRRQLTF REKSRIIQEV EENPDLRKGE IARRFNIPPS TLSTILKNKR AILASERKYG 60
VASTCRKTNK LSPYDKLEGL LIAWFQQIRA AGLPVKGIIL KEKALRIAEE LGMDDFTASN 120
GWLDRFRRRH GVVSCSGVAR ARARNAAPRT PAAPASPAAV PSEGSGGSTT GWRAREEQPP 180
SVAEGYASQD VFSATETSLW YDFLPDQAAG LCGGDGRPRQ ATQRLSVLLC ANADGSEKLP 240
PLVAGKSAKP RAGQAGLPCD YTANSKGGVT TQALAKYLKA LDTRMAAESR RVLLLAGRLA 300
AQSLDTSGLR HVQLAFFPPG TVHPLERGVV QQVKGHYRQA MLLKAMAALE GQDPSGLQLG 360
LTEALHFVAA AWQAVEPSDI AACFREAGFG GGPNATITTS LKSEGEEEEE EEEEEEEEEG 420
EGEEEEEEGE EEEEEGGEGE ELGEEEEVEE EGDVDSDEEE EEDEESSSEG LEAEDWAQGV 480
VEAGGSFGAY GAQEEAQCPT LHFLEGGEDS DSDSEEEDDE EEDDEDEDDD DDEEDGDEVP 540
VPSFGEAMAY FAMVKRYLTS FPIDDRVQSH ILHLEHDLVH VTRKNHARQA GVRGLGHQS 599 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; IDA:BHF-UCL.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0019237; F:centromeric DNA binding; IC:BHF-UCL.
 GO:0003682; F:chromatin binding; NAS:UniProtKB.
 GO:0003696; F:satellite DNA binding; NAS:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:InterPro. 
Interpro
 IPR015115; Centromere_CenpB_dimerisation.
 IPR004875; DDE_SF_endonuclease_CENPB-like.
 IPR009057; Homeodomain-like.
 IPR006600; HTH_CenpB_DNA-bd_dom.
 IPR007889; HTH_Psq. 
Pfam
 PF09026; Cenp-B_dimeris
 PF04218; CENP-B_N
 PF03184; DDE_1
 PF03221; HTH_Tnp_Tc5 
SMART
 SM00674; CENPB 
PROSITE
 PS51253; HTH_CENPB
 PS50960; HTH_PSQ 
PRINTS