CFDP1_HUMAN
ID CFDP1_HUMAN Reviewed; 299 AA.
AC Q9UEE9; O00393; O00404; Q9UEF0; Q9UEF1; Q9UEF8;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Craniofacial development protein 1;
DE AltName: Full=Bucentaur;
GN Name=CFDP1; Synonyms=BCNT, CENP-29;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE [MRNA] OF
RP 23-299 (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
RX PubMed=9006920; DOI=10.1074/jbc.272.5.2801;
RA Nobukuni T., Kobayashi M., Omori A., Ichinose S., Iwanaga T., Takahashi I.,
RA Hashimoto K., Hattori S., Kaibuchi K., Miyata Y., Masui T., Iwashita S.;
RT "An Alu-linked repetitive sequence corresponding to 280 amino acids is
RT expressed in a novel bovine protein, but not in its human homologue.";
RL J. Biol. Chem. 272:2801-2807(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [GENOMIC DNA]
RP OF 23-299, AND TISSUE SPECIFICITY.
RX PubMed=9602175; DOI=10.1016/s0378-1119(98)00136-x;
RA Takahashi I., Nobukuni T., Ohmori H., Kobayashi M., Tanaka S., Ohshima K.,
RA Okada N., Masui T., Hashimoto K., Iwashita S.;
RT "Existence of a bovine LINE repetitive insert that appears in the cDNA of
RT bovine protein BCNT in ruminant, but not in human, genomes.";
RL Gene 211:387-394(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta;
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 [6]
RP PHOSPHORYLATION.
RX PubMed=10350657; DOI=10.1016/s0304-4165(99)00049-5;
RA Iwashita S., Nobukuni T., Tanaka S., Kobayashi M., Iwanaga T., Tamate H.B.,
RA Masui T., Takahashi I., Hashimoto K.;
RT "Partial nuclear localization of a bovine phosphoprotein, BCNT, that
RT includes a region derived from a LINE repetitive sequence in Ruminantia.";
RL Biochim. Biophys. Acta 1427:408-416(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-250, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=20813266; DOI=10.1016/j.cell.2010.07.047;
RA Ohta S., Bukowski-Wills J.C., Sanchez-Pulido L., Alves Fde L., Wood L.,
RA Chen Z.A., Platani M., Fischer L., Hudson D.F., Ponting C.P., Fukagawa T.,
RA Earnshaw W.C., Rappsilber J.;
RT "The protein composition of mitotic chromosomes determined using
RT multiclassifier combinatorial proteomics.";
RL Cell 142:810-821(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [12]
RP METHYLATION [LARGE SCALE ANALYSIS] AT LYS-219, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-150, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: May play a role during embryogenesis. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:20813266}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9UEE9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UEE9-2; Sequence=VSP_016242;
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9602175}.
CC -!- PTM: Phosphorylated by CK2 (casein kinase II) in vitro.
CC {ECO:0000269|PubMed:10350657}.
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DR EMBL; D85939; BAA20069.1; -; mRNA.
DR EMBL; D86549; BAA20070.1; -; mRNA.
DR EMBL; AB004907; BAA31860.1; -; Genomic_DNA.
DR EMBL; AB009269; BAA31864.1; -; Genomic_DNA.
DR EMBL; AB009270; BAA31865.1; -; Genomic_DNA.
DR EMBL; AB009285; BAA31867.1; -; mRNA.
DR EMBL; BT009819; AAP88821.1; -; mRNA.
DR EMBL; CR542111; CAG46908.1; -; mRNA.
DR EMBL; BC000991; AAH00991.1; -; mRNA.
DR CCDS; CCDS10916.1; -. [Q9UEE9-1]
DR RefSeq; NP_006315.1; NM_006324.2. [Q9UEE9-1]
DR AlphaFoldDB; Q9UEE9; -.
DR SMR; Q9UEE9; -.
DR BioGRID; 115697; 59.
DR IntAct; Q9UEE9; 21.
DR MINT; Q9UEE9; -.
DR STRING; 9606.ENSP00000283882; -.
DR iPTMnet; Q9UEE9; -.
DR MetOSite; Q9UEE9; -.
DR PhosphoSitePlus; Q9UEE9; -.
DR BioMuta; CFDP1; -.
DR DMDM; 74734998; -.
DR EPD; Q9UEE9; -.
DR jPOST; Q9UEE9; -.
DR MassIVE; Q9UEE9; -.
DR MaxQB; Q9UEE9; -.
DR PaxDb; Q9UEE9; -.
DR PeptideAtlas; Q9UEE9; -.
DR PRIDE; Q9UEE9; -.
DR ProteomicsDB; 84142; -. [Q9UEE9-1]
DR ProteomicsDB; 84143; -. [Q9UEE9-2]
DR Antibodypedia; 30309; 271 antibodies from 26 providers.
DR DNASU; 10428; -.
DR Ensembl; ENST00000283882.4; ENSP00000283882.3; ENSG00000153774.9. [Q9UEE9-1]
DR GeneID; 10428; -.
DR KEGG; hsa:10428; -.
DR MANE-Select; ENST00000283882.4; ENSP00000283882.3; NM_006324.3; NP_006315.1.
DR UCSC; uc002fdy.4; human. [Q9UEE9-1]
DR CTD; 10428; -.
DR DisGeNET; 10428; -.
DR GeneCards; CFDP1; -.
DR HGNC; HGNC:1873; CFDP1.
DR HPA; ENSG00000153774; Low tissue specificity.
DR MIM; 608108; gene.
DR neXtProt; NX_Q9UEE9; -.
DR OpenTargets; ENSG00000153774; -.
DR PharmGKB; PA26422; -.
DR VEuPathDB; HostDB:ENSG00000153774; -.
DR eggNOG; KOG4776; Eukaryota.
DR GeneTree; ENSGT00390000018141; -.
DR HOGENOM; CLU_080190_0_0_1; -.
DR InParanoid; Q9UEE9; -.
DR OMA; LDWAAYV; -.
DR OrthoDB; 1372508at2759; -.
DR PhylomeDB; Q9UEE9; -.
DR TreeFam; TF313182; -.
DR PathwayCommons; Q9UEE9; -.
DR SignaLink; Q9UEE9; -.
DR BioGRID-ORCS; 10428; 334 hits in 1087 CRISPR screens.
DR ChiTaRS; CFDP1; human.
DR GeneWiki; CFDP1; -.
DR GenomeRNAi; 10428; -.
DR Pharos; Q9UEE9; Tbio.
DR PRO; PR:Q9UEE9; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9UEE9; protein.
DR Bgee; ENSG00000153774; Expressed in ganglionic eminence and 208 other tissues.
DR ExpressionAtlas; Q9UEE9; baseline and differential.
DR Genevisible; Q9UEE9; HS.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0044346; P:fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:2000270; P:negative regulation of fibroblast apoptotic process; IEA:Ensembl.
DR GO; GO:0042127; P:regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
DR InterPro; IPR011421; BCNT-C.
DR InterPro; IPR027124; Swc5/CFDP1/2.
DR PANTHER; PTHR23227; PTHR23227; 1.
DR Pfam; PF07572; BCNT; 1.
DR PROSITE; PS51279; BCNT_C; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Centromere; Chromosome; Developmental protein;
KW Isopeptide bond; Kinetochore; Methylation; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..299
FT /note="Craniofacial development protein 1"
FT /id="PRO_0000212494"
FT DOMAIN 218..299
FT /note="BCNT-C"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00610"
FT REGION 1..156
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..217
FT /note="Hydrophilic"
FT REGION 192..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..97
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..115
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..156
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75UQ2"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75UQ2"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q75UQ2"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="N6-methyllysine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 150
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 218..299
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9006920"
FT /id="VSP_016242"
FT VARIANT 60
FT /note="A -> T (in dbSNP:rs16963331)"
FT /id="VAR_048408"
FT CONFLICT 23..24
FT /note="GE -> IP (in Ref. 1; BAA20070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 299 AA; 33593 MW; F4A9E928B669451A CRC64;
MEEFDSEDFS TSEEDEDYVP SGGEYSEDDV NELVKEDEVD GEEQTQKTQG KKRKAQSIPA
RKRRQGGLSL EEEEEEDANS ESEGSSSEEE DDAAEQEKGI GSEDARKKKE DELWASFLND
VGPKSKVPPS TQVKKGEETE ETSSSKLLVK AEELEKPKET EKVKITKVFD FAGEEVRVTK
EVDATSKEAK SFFKQNEKEK PQANVPSALP SLPAGSGLKR SSGMSSLLGK IGAKKQKMST
LEKSKLDWES FKEEEGIGEE LAIHNRGKEG YIERKAFLDR VDHRQFEIER DLRLSKMKP
