CEMP1_HUMAN
ID CEMP1_HUMAN Reviewed; 247 AA.
AC Q6PRD7; B2RUY1;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Cementoblastoma-derived protein 1 {ECO:0000305};
DE AltName: Full=Cementum protein 1 {ECO:0000303|PubMed:17509525};
DE AltName: Full=Cementum protein 23 {ECO:0000303|PubMed:16263347};
DE Short=CP-23 {ECO:0000303|PubMed:16263347};
GN Name=CEMP1 {ECO:0000312|HGNC:HGNC:32553};
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], SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Cementoblast;
RX PubMed=16263347; DOI=10.1016/j.bone.2005.09.009;
RA Alvarez-Perez M.A., Narayanan S., Zeichner-David M., Rodriguez Carmona B.,
RA Arzate H.;
RT "Molecular cloning, expression and immunolocalization of a novel human
RT cementum-derived protein (CP-23).";
RL Bone 38:409-419(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [3]
RP FUNCTION.
RX PubMed=17509525; DOI=10.1016/j.bbrc.2007.04.204;
RA Carmona-Rodriguez B., Alvarez-Perez M.A., Narayanan A.S.,
RA Zeichner-David M., Reyes-Gasga J., Molina-Guarneros J.,
RA Garcia-Hernandez A.L., Suarez-Franco J.L., Chavarria I.G.,
RA Villarreal-Ramirez E., Arzate H.;
RT "Human cementum protein 1 induces expression of bone and cementum proteins
RT by human gingival fibroblasts.";
RL Biochem. Biophys. Res. Commun. 358:763-769(2007).
RN [4]
RP FUNCTION, GLYCOSYLATION, AND PHOSPHORYLATION.
RX PubMed=19393626; DOI=10.1016/j.bbrc.2009.04.072;
RA Villarreal-Ramirez E., Moreno A., Mas-Oliva J., Chavez-Pacheco J.L.,
RA Narayanan A.S., Gil-Chavarria I., Zeichner-David M., Arzate H.;
RT "Characterization of recombinant human cementum protein 1 (hrCEMP1):
RT primary role in biomineralization.";
RL Biochem. Biophys. Res. Commun. 384:49-54(2009).
RN [5]
RP FUNCTION.
RX PubMed=21929512; DOI=10.1042/cbi20110168;
RA Hoz L., Romo E., Zeichner-David M., Sanz M., Nunez J., Gaitan L.,
RA Mercado G., Arzate H.;
RT "Cementum protein 1 (CEMP1) induces differentiation by human periodontal
RT ligament cells under three-dimensional culture conditions.";
RL Cell Biol. Int. 36:129-136(2012).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21465469; DOI=10.1002/jcp.22770;
RA Komaki M., Iwasaki K., Arzate H., Narayanan A.S., Izumi Y., Morita I.;
RT "Cementum protein 1 (CEMP1) induces a cementoblastic phenotype and reduces
RT osteoblastic differentiation in periodontal ligament cells.";
RL J. Cell. Physiol. 227:649-657(2012).
RN [7]
RP INDUCTION BY HYPOXIA.
RX PubMed=24117017; DOI=10.1089/ten.tea.2013.0132;
RA Choi H., Jin H., Kim J.Y., Lim K.T., Choung H.W., Park J.Y., Chung J.H.,
RA Choung P.H.;
RT "Hypoxia promotes CEMP1 expression and induces cementoblastic
RT differentiation of human dental stem cells in an HIF-1-dependent manner.";
RL Tissue Eng. Part A 20:410-423(2014).
RN [8]
RP FUNCTION.
RX PubMed=26011628; DOI=10.1371/journal.pone.0127286;
RA Bermudez M., Imaz-Rosshandler I., Rangel-Escareno C., Zeichner-David M.,
RA Arzate H., Mercado-Celis G.E.;
RT "CEMP1 induces transformation in human gingival fibroblasts.";
RL PLoS ONE 10:E0127286-E0127286(2015).
CC -!- FUNCTION: May play a role in development of the periodontium which
CC surrounds and supports the teeth by promoting the differentiation of
CC multi-potent cells from the periodontal ligament into cementoblasts to
CC form the cementum (PubMed:21929512, PubMed:17509525, PubMed:21465469).
CC Binds hydroxyapatite and may promote the biomineralization of the
CC cementum (PubMed:19393626). Also promotes cell proliferation
CC (PubMed:17509525, PubMed:21929512, PubMed:26011628).
CC {ECO:0000269|PubMed:17509525, ECO:0000269|PubMed:19393626,
CC ECO:0000269|PubMed:21465469, ECO:0000269|PubMed:21929512,
CC ECO:0000269|PubMed:26011628}.
CC -!- INTERACTION:
CC Q6PRD7; Q53EP0-3: FNDC3B; NbExp=3; IntAct=EBI-12907646, EBI-10242151;
CC Q6PRD7; B2RUY7: VWC2L; NbExp=3; IntAct=EBI-12907646, EBI-11747707;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16263347,
CC ECO:0000269|PubMed:21465469}. Nucleus {ECO:0000269|PubMed:21465469}.
CC Note=Localizes to the nucleus of some cementoblasts.
CC {ECO:0000269|PubMed:21465469}.
CC -!- TISSUE SPECIFICITY: Expressed by cementoblasts, a subpopulation of
CC periodontal ligament cells and cells located around vessels in
CC periodontium (at protein level). {ECO:0000269|PubMed:16263347,
CC ECO:0000269|PubMed:21465469}.
CC -!- INDUCTION: Up-regulated by hypoxia (at protein level).
CC {ECO:0000269|PubMed:24117017}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:19393626}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:19393626}.
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; AY584596; AAT01221.1; -; mRNA.
DR EMBL; BC146925; AAI46926.1; -; mRNA.
DR EMBL; BC146926; AAI46927.1; -; mRNA.
DR CCDS; CCDS42108.1; -.
DR RefSeq; NP_001041677.1; NM_001048212.3.
DR AlphaFoldDB; Q6PRD7; -.
DR BioGRID; 612783; 7.
DR IntAct; Q6PRD7; 2.
DR STRING; 9606.ENSP00000457380; -.
DR iPTMnet; Q6PRD7; -.
DR PhosphoSitePlus; Q6PRD7; -.
DR BioMuta; CEMP1; -.
DR DMDM; 74709987; -.
DR EPD; Q6PRD7; -.
DR PaxDb; Q6PRD7; -.
DR PeptideAtlas; Q6PRD7; -.
DR PRIDE; Q6PRD7; -.
DR Antibodypedia; 57697; 30 antibodies from 13 providers.
DR DNASU; 752014; -.
DR Ensembl; ENST00000567119.1; ENSP00000457380.1; ENSG00000205923.3.
DR GeneID; 752014; -.
DR KEGG; hsa:752014; -.
DR MANE-Select; ENST00000567119.1; ENSP00000457380.1; NM_001048212.3; NP_001041677.1.
DR UCSC; uc002cqr.3; human.
DR CTD; 752014; -.
DR DisGeNET; 752014; -.
DR GeneCards; CEMP1; -.
DR HGNC; HGNC:32553; CEMP1.
DR HPA; ENSG00000205923; Low tissue specificity.
DR MIM; 611113; gene.
DR neXtProt; NX_Q6PRD7; -.
DR OpenTargets; ENSG00000205923; -.
DR PharmGKB; PA162382169; -.
DR VEuPathDB; HostDB:ENSG00000205923; -.
DR eggNOG; ENOG502TEMU; Eukaryota.
DR GeneTree; ENSGT00410000029488; -.
DR HOGENOM; CLU_1124235_0_0_1; -.
DR InParanoid; Q6PRD7; -.
DR OrthoDB; 1120344at2759; -.
DR PhylomeDB; Q6PRD7; -.
DR TreeFam; TF343729; -.
DR PathwayCommons; Q6PRD7; -.
DR SignaLink; Q6PRD7; -.
DR BioGRID-ORCS; 752014; 8 hits in 1037 CRISPR screens.
DR ChiTaRS; CEMP1; human.
DR GenomeRNAi; 752014; -.
DR Pharos; Q6PRD7; Tbio.
DR PRO; PR:Q6PRD7; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q6PRD7; protein.
DR Bgee; ENSG00000205923; Expressed in mucosa of transverse colon and 115 other tissues.
DR ExpressionAtlas; Q6PRD7; baseline and differential.
DR Genevisible; Q6PRD7; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0046848; F:hydroxyapatite binding; IDA:UniProtKB.
DR GO; GO:0031214; P:biomineral tissue development; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; IDA:UniProtKB.
DR GO; GO:0042476; P:odontogenesis; IDA:UniProtKB.
PE 1: Evidence at protein level;
KW Cytoplasm; Differentiation; Nucleus; Reference proteome.
FT CHAIN 1..247
FT /note="Cementoblastoma-derived protein 1"
FT /id="PRO_0000264475"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 147..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..32
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VARIANT 55
FT /note="K -> E (in dbSNP:rs13331643)"
FT /id="VAR_050792"
SQ SEQUENCE 247 AA; 25959 MW; 81FEEA1D26E47022 CRC64;
MGTSSTDSQQ AGHRRCSTSN TSAENLTCLS LPGSPGKTAP LPGPAQAGAG QPLPKGCAAV
KAEVGIPAPH TSQEVRIHIR RLLSWAAPGA CGLRSTPCAL PQALPQARPC PGRWFFPGCS
LPTGGAQTIL SLWTWRHFLN WALQQREENS GRARRVPPVP RTAPVSKGEG SHPPQNSNGE
KVKTITPDVG LHQSLTSDPT VAVLRAKRAP EAHPPRSCSG SLTARVCHMG VCQGQGDTED
GRMTLMG
