CETN3_HUMAN
ID CETN3_HUMAN Reviewed; 167 AA.
AC O15182; Q53YD2; Q9BS23;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 03-AUG-2022, entry version 187.
DE RecName: Full=Centrin-3;
GN Name=CETN3; Synonyms=CEN3;
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 VARIANT LEU-10.
RX PubMed=9256449; DOI=10.1073/pnas.94.17.9141;
RA Middendorp S., Paoletti A., Schiebel E., Bornens M.;
RT "Identification of a new mammalian centrin gene, more closely related to
RT Saccharomyces cerevisiae CDC31 gene.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:9141-9146(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Testis;
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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [6]
RP INTERACTION WITH TREX-2 COMPLEX, AND FUNCTION.
RX PubMed=22307388; DOI=10.1093/nar/gks059;
RA Jani D., Lutz S., Hurt E., Laskey R.A., Stewart M., Wickramasinghe V.O.;
RT "Functional and structural characterization of the mammalian TREX-2 complex
RT that links transcription with nuclear messenger RNA export.";
RL Nucleic Acids Res. 40:4562-4573(2012).
RN [7]
RP FUNCTION, IDENTIFICATION IN THE TREX-2 COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=23591820; DOI=10.1242/jcs.118000;
RA Umlauf D., Bonnet J., Waharte F., Fournier M., Stierle M., Fischer B.,
RA Brino L., Devys D., Tora L.;
RT "The human TREX-2 complex is stably associated with the nuclear pore
RT basket.";
RL J. Cell Sci. 126:2656-2667(2013).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-135, 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 [9]
RP SUBCELLULAR LOCATION.
RX PubMed=26337392; DOI=10.1091/mbc.e15-04-0235;
RA Van de Mark D., Kong D., Loncarek J., Stearns T.;
RT "MDM1 is a microtubule-binding protein that negatively regulates centriole
RT duplication.";
RL Mol. Biol. Cell 26:3788-3802(2015).
CC -!- FUNCTION: Plays a fundamental role in microtubule-organizing center
CC structure and function.
CC -!- FUNCTION: As a component of the TREX-2 complex, involved in the export
CC of mRNAs to the cytoplasm through the nuclear pores.
CC {ECO:0000269|PubMed:22307388, ECO:0000305|PubMed:23591820}.
CC -!- SUBUNIT: Monomer (By similarity). Component of the nuclear pore complex
CC (NPC)-associated TREX-2 complex (transcription and export complex 2),
CC composed of at least GANP, 2 copies of ENY2, PCID2, SEM1/DSS1, and
CC either centrin CETN2 or centrin CETN3. The TREX-2 complex also
CC associates with ALYREF/ALY and with the nucleoporin NUP153
CC (PubMed:22307388, PubMed:23591820). {ECO:0000250,
CC ECO:0000269|PubMed:22307388, ECO:0000269|PubMed:23591820}.
CC -!- INTERACTION:
CC O15182; O95994: AGR2; NbExp=3; IntAct=EBI-712959, EBI-712648;
CC O15182; P17540: CKMT2; NbExp=3; IntAct=EBI-712959, EBI-712973;
CC O15182; P13473-2: LAMP2; NbExp=3; IntAct=EBI-712959, EBI-21591415;
CC O15182; O43679: LDB2; NbExp=3; IntAct=EBI-712959, EBI-2865580;
CC O15182; Q8NA72: POC5; NbExp=6; IntAct=EBI-712959, EBI-2561090;
CC O15182; Q8NA72-3: POC5; NbExp=8; IntAct=EBI-712959, EBI-11751537;
CC O15182; Q15293: RCN1; NbExp=5; IntAct=EBI-712959, EBI-948278;
CC O15182; O00141: SGK1; NbExp=3; IntAct=EBI-712959, EBI-1042854;
CC O15182; Q2NKQ1-4: SGSM1; NbExp=6; IntAct=EBI-712959, EBI-10182463;
CC O15182; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-712959, EBI-2623095;
CC O15182; P19237: TNNI1; NbExp=3; IntAct=EBI-712959, EBI-746692;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:9256449}. Nucleus, nucleolus
CC {ECO:0000303|PubMed:22307388}. Nucleus envelope
CC {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex
CC {ECO:0000269|PubMed:23591820}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriole {ECO:0000269|PubMed:23591820,
CC ECO:0000269|PubMed:26337392}. Note=Centrosome of interphase and mitotic
CC cells (PubMed:9256449). Localizes to centriole distal lumen
CC (PubMed:26337392). Localization at the nuclear pore complex requires
CC NUP153 and TPR (PubMed:23591820). {ECO:0000269|PubMed:23591820,
CC ECO:0000269|PubMed:26337392, ECO:0000269|PubMed:9256449}.
CC -!- SIMILARITY: Belongs to the centrin family. {ECO:0000305}.
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DR EMBL; Y12473; CAA73077.1; -; mRNA.
DR EMBL; BT006688; AAP35334.1; -; mRNA.
DR EMBL; AC093510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC005383; AAH05383.1; -; mRNA.
DR EMBL; BC093793; AAH93793.1; -; mRNA.
DR EMBL; BC112040; AAI12041.1; -; mRNA.
DR CCDS; CCDS4066.1; -.
DR RefSeq; NP_001284697.1; NM_001297768.1.
DR RefSeq; NP_004356.2; NM_004365.3.
DR AlphaFoldDB; O15182; -.
DR SMR; O15182; -.
DR BioGRID; 107497; 62.
DR IntAct; O15182; 36.
DR MINT; O15182; -.
DR iPTMnet; O15182; -.
DR MetOSite; O15182; -.
DR PhosphoSitePlus; O15182; -.
DR BioMuta; CETN3; -.
DR EPD; O15182; -.
DR jPOST; O15182; -.
DR MassIVE; O15182; -.
DR MaxQB; O15182; -.
DR PaxDb; O15182; -.
DR PeptideAtlas; O15182; -.
DR PRIDE; O15182; -.
DR ProteomicsDB; 48497; -.
DR Antibodypedia; 24818; 191 antibodies from 24 providers.
DR DNASU; 1070; -.
DR Ensembl; ENST00000283122.8; ENSP00000283122.3; ENSG00000153140.9.
DR GeneID; 1070; -.
DR KEGG; hsa:1070; -.
DR MANE-Select; ENST00000283122.8; ENSP00000283122.3; NM_004365.4; NP_004356.2.
DR UCSC; uc003kjo.4; human.
DR CTD; 1070; -.
DR DisGeNET; 1070; -.
DR GeneCards; CETN3; -.
DR HGNC; HGNC:1868; CETN3.
DR HPA; ENSG00000153140; Tissue enhanced (testis).
DR MIM; 602907; gene.
DR neXtProt; NX_O15182; -.
DR OpenTargets; ENSG00000153140; -.
DR PharmGKB; PA26421; -.
DR VEuPathDB; HostDB:ENSG00000153140; -.
DR GeneTree; ENSGT00940000157995; -.
DR InParanoid; O15182; -.
DR OMA; MIMKQST; -.
DR PhylomeDB; O15182; -.
DR TreeFam; TF101141; -.
DR PathwayCommons; O15182; -.
DR SignaLink; O15182; -.
DR SIGNOR; O15182; -.
DR BioGRID-ORCS; 1070; 24 hits in 1049 CRISPR screens.
DR ChiTaRS; CETN3; human.
DR GeneWiki; CETN3; -.
DR GenomeRNAi; 1070; -.
DR Pharos; O15182; Tbio.
DR PRO; PR:O15182; -.
DR Proteomes; UP000005640; Chromosome 5.
DR RNAct; O15182; protein.
DR Bgee; ENSG00000153140; Expressed in oocyte and 211 other tissues.
DR ExpressionAtlas; O15182; baseline and differential.
DR Genevisible; O15182; HS.
DR GO; GO:0005814; C:centriole; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0036064; C:ciliary basal body; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR GO; GO:0044615; C:nuclear pore nuclear basket; IDA:UniProtKB.
DR GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IEA:Ensembl.
DR GO; GO:0070390; C:transcription export complex 2; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0031683; F:G-protein beta/gamma-subunit complex binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0007098; P:centrosome cycle; TAS:ProtInc.
DR GO; GO:0051028; P:mRNA transport; IEA:UniProtKB-KW.
DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-KW.
DR CDD; cd00051; EFh; 1.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR Pfam; PF13499; EF-hand_7; 2.
DR SMART; SM00054; EFh; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 4.
PE 1: Evidence at protein level;
KW Calcium; Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Metal-binding;
KW Mitosis; mRNA transport; Nuclear pore complex; Nucleus; Phosphoprotein;
KW Protein transport; Reference proteome; Repeat; Translocation; Transport.
FT CHAIN 1..167
FT /note="Centrin-3"
FT /id="PRO_0000073563"
FT DOMAIN 25..60
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 61..96
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 98..133
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 134..167
FT /note="EF-hand 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 147
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 149
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 151
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 153
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 158
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 135
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VARIANT 10
FT /note="V -> L (in dbSNP:rs4873)"
FT /evidence="ECO:0000269|PubMed:9256449"
FT /id="VAR_030846"
SQ SEQUENCE 167 AA; 19550 MW; EF67724B2D6C2680 CRC64;
MSLALRSELV VDKTKRKKRR ELSEEQKQEI KDAFELFDTD KDEAIDYHEL KVAMRALGFD
VKKADVLKIL KDYDREATGK ITFEDFNEVV TDWILERDPH EEILKAFKLF DDDDSGKISL
RNLRRVAREL GENMSDEELR AMIEEFDKDG DGEINQEEFI AIMTGDI
