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DNA replication factor Cdt1 (Double parked homolog) (DUP)

 CDT1_HUMAN              Reviewed;         546 AA.
Q9H211; Q86XX9; Q96CJ5; Q96GK5; Q96H67; Q96HE6; Q9BWM0;
07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
05-OCT-2010, sequence version 3.
23-MAY-2018, entry version 144.
RecName: Full=DNA replication factor Cdt1;
AltName: Full=Double parked homolog;
Short=DUP;
Name=CDT1 {ECO:0000312|EMBL:AAG45181.1};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1] {ECO:0000305, ECO:0000312|EMBL:AAG45181.1}
NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE, SUBCELLULAR
LOCATION, INTERACTION WITH GMNN, AND VARIANTS ARG-234 AND ALA-262.
PubMed=11125146; DOI=10.1126/science.290.5500.2309;
Wohlschlegel J.A., Dwyer B.T., Dhar S.K., Cvetic C., Walter J.C.,
Dutta A.;
"Inhibition of eukaryotic DNA replication by geminin binding to
Cdt1.";
Science 290:2309-2312(2000).
[2] {ECO:0000312|EMBL:BAB61878.1}
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS ARG-234 AND ALA-262.
PubMed=10766248; DOI=10.1038/35007110;
Nishitani H., Lygerou Z., Nishimoto T., Nurse P.;
"The Cdt1 protein is required to license DNA for replication in
fission yeast.";
Nature 404:625-628(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15616553; DOI=10.1038/nature03187;
Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
Rubin E.M., Pennacchio L.A.;
"The sequence and analysis of duplication-rich human chromosome 16.";
Nature 432:988-994(2004).
[4] {ECO:0000312|EMBL:AAH14202.2}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-234 AND
ALA-262.
TISSUE=Brain {ECO:0000312|EMBL:AAH08860.2},
Cervix {ECO:0000312|EMBL:AAH00137.2},
Eye {ECO:0000312|EMBL:AAH08676.1},
Kidney {ECO:0000312|EMBL:AAH14202.2},
Liver {ECO:0000312|EMBL:AAH49205.1}, and
Uterus {ECO:0000312|EMBL:AAH09410.1};
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 136-546, AND VARIANT
ARG-234.
TISSUE=Brain;
Yu W., Gibbs R.A.;
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[6]
INDUCTION.
PubMed=14990995; DOI=10.1038/sj.onc.1207488;
Yoshida K., Inoue I.;
"Regulation of Geminin and Cdt1 expression by E2F transcription
factors.";
Oncogene 23:3802-3812(2004).
[7]
INTERACTION WITH KAT7.
PubMed=18832067; DOI=10.1101/gad.1674108;
Miotto B., Struhl K.;
"HBO1 histone acetylase is a coactivator of the replication licensing
factor Cdt1.";
Genes Dev. 22:2633-2638(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-394, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-318, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[10]
PHOSPHORYLATION AT THR-29; SER-93 AND SER-318 BY MAPK8/JNK1, AND
FUNCTION.
PubMed=21856198; DOI=10.1016/j.molcel.2011.06.021;
Miotto B., Struhl K.;
"JNK1 phosphorylation of Cdt1 inhibits recruitment of HBO1 histone
acetylase and blocks replication licensing in response to stress.";
Mol. Cell 44:62-71(2011).
[11]
UBIQUITINATION, AND INTERACTION WITH GMNN.
PubMed=15257290; DOI=10.1038/sj.emboj.7600314;
Ballabeni A., Melixetian M., Zamponi R., Masiero L., Marinoni F.,
Helin K.;
"Human geminin promotes pre-RC formation and DNA replication by
stabilizing CDT1 in mitosis.";
EMBO J. 23:3122-3132(2004).
[12]
FUNCTION, AND INTERACTION WITH MCM2; GMNN AND CDC6.
PubMed=14672932; DOI=10.1074/jbc.M311933200;
Cook J.G., Chasse D.A.D., Nevins J.R.;
"The regulated association of Cdt1 with minichromosome maintenance
proteins and Cdc6 in mammalian cells.";
J. Biol. Chem. 279:9625-9633(2004).
[13]
FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF 68-ARG--LEU-70, AND
INTERACTION WITH SKP2; GMNN AND CYCLIN A-DEPENDENT KINASES.
PubMed=14993212; DOI=10.1074/jbc.M313175200;
Sugimoto N., Tatsumi Y., Tsurumi T., Matsukage A., Kiyono T.,
Nishitani H., Fujita M.;
"Cdt1 phosphorylation by cyclin A-dependent kinases negatively
regulates its function without affecting geminin binding.";
J. Biol. Chem. 279:19691-19697(2004).
[14]
UBIQUITINATION, AND INTERACTION WITH PCNA.
PubMed=16861906; DOI=10.4161/cc.5.15.3149;
Higa L.A., Banks D., Wu M., Kobayashi R., Sun H., Zhang H.;
"L2DTL/CDT2 interacts with the CUL4/DDB1 complex and PCNA and
regulates CDT1 proteolysis in response to DNA damage.";
Cell Cycle 5:1675-1680(2006).
[15]
UBIQUITINATION.
PubMed=17085480; DOI=10.1101/gad.1482106;
Sansam C.L., Shepard J.L., Lai K., Ianari A., Danielian P.S.,
Amsterdam A., Hopkins N., Lees J.A.;
"DTL/CDT2 is essential for both CDT1 regulation and the early G2/M
checkpoint.";
Genes Dev. 20:3117-3129(2006).
[16]
UBIQUITINATION.
PubMed=16949367; DOI=10.1016/j.molcel.2006.08.010;
Jin J., Arias E.E., Chen J., Harper J.W., Walter J.C.;
"A family of diverse Cul4-Ddb1-interacting proteins includes Cdt2,
which is required for S phase destruction of the replication factor
Cdt1.";
Mol. Cell 23:709-721(2006).
[17]
INTERACTION WITH GMNN, AND MUTAGENESIS OF TYR-170.
PubMed=21543332; DOI=10.1074/jbc.M110.207688;
Pefani D.E., Dimaki M., Spella M., Karantzelis N., Mitsiki E.,
Kyrousi C., Symeonidou I.E., Perrakis A., Taraviras S., Lygerou Z.;
"Idas, a novel phylogenetically conserved geminin-related protein,
binds to geminin and is required for cell cycle progression.";
J. Biol. Chem. 286:23234-23246(2011).
[18]
INTERACTION WITH LRWD1, AND PHOSPHORYLATION DURING MITOSIS.
PubMed=22645314; DOI=10.1128/MCB.00362-12;
Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V.,
Prasanth S.G.;
"Dynamic association of ORCA with prereplicative complex components
regulates DNA replication initiation.";
Mol. Cell. Biol. 32:3107-3120(2012).
[19]
FUNCTION IN MITOSIS, SUBCELLULAR LOCATION, AND INTERACTION WITH NDC80.
PubMed=22581055; DOI=10.1038/ncb2489;
Varma D., Chandrasekaran S., Sundin L.J., Reidy K.T., Wan X.,
Chasse D.A., Nevis K.R., DeLuca J.G., Salmon E.D., Cook J.G.;
"Recruitment of the human Cdt1 replication licensing protein by the
loop domain of Hec1 is required for stable kinetochore-microtubule
attachment.";
Nat. Cell Biol. 14:593-603(2012).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31 AND SER-380, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
INTERACTION WITH GRWD1.
PubMed=25990725; DOI=10.1093/nar/gkv509;
Sugimoto N., Maehara K., Yoshida K., Yasukouchi S., Osano S.,
Watanabe S., Aizawa M., Yugawa T., Kiyono T., Kurumizaka H.,
Ohkawa Y., Fujita M.;
"Cdt1-binding protein GRWD1 is a novel histone-binding protein that
facilitates MCM loading through its influence on chromatin
architecture.";
Nucleic Acids Res. 43:5898-5911(2015).
[22]
DEUBIQUITINATION BY USP37, AND DEVELOPMENTAL STAGE.
PubMed=27296872; DOI=10.1016/j.molonc.2016.05.008;
Hernandez-Perez S., Cabrera E., Amoedo H., Rodriguez-Acebes S.,
Koundrioukoff S., Debatisse M., Mendez J., Freire R.;
"USP37 deubiquitinates Cdt1 and contributes to regulate DNA
replication.";
Mol. Oncol. 10:1196-1206(2016).
[23]
FUNCTION, INTERACTION WITH FAF1, AND SUBCELLULAR LOCATION.
PubMed=26842564; DOI=10.1038/ncomms10612;
Franz A., Pirson P.A., Pilger D., Halder S., Achuthankutty D.,
Kashkar H., Ramadan K., Hoppe T.;
"Chromatin-associated degradation is defined by UBXN-3/FAF1 to
safeguard DNA replication fork progression.";
Nat. Commun. 7:10612-10612(2016).
[24]
VARIANTS MGORS4 THR-66; HIS-117; TRP-453 AND GLN-462.
PubMed=21358632; DOI=10.1038/ng.775;
Bicknell L.S., Bongers E.M., Leitch A., Brown S., Schoots J.,
Harley M.E., Aftimos S., Al-Aama J.Y., Bober M., Brown P.A.,
van Bokhoven H., Dean J., Edrees A.Y., Feingold M., Fryer A.,
Hoefsloot L.H., Kau N., Knoers N.V., Mackenzie J., Opitz J.M.,
Sarda P., Ross A., Temple I.K., Toutain A., Wise C.A., Wright M.,
Jackson A.P.;
"Mutations in the pre-replication complex cause Meier-Gorlin
syndrome.";
Nat. Genet. 43:356-359(2011).
[25]
VARIANT MGORS4 LYS-468.
PubMed=21358631; DOI=10.1038/ng.777;
Guernsey D.L., Matsuoka M., Jiang H., Evans S., Macgillivray C.,
Nightingale M., Perry S., Ferguson M., LeBlanc M., Paquette J.,
Patry L., Rideout A.L., Thomas A., Orr A., McMaster C.R.,
Michaud J.L., Deal C., Langlois S., Superneau D.W., Parkash S.,
Ludman M., Skidmore D.L., Samuels M.E.;
"Mutations in origin recognition complex gene ORC4 cause Meier-Gorlin
syndrome.";
Nat. Genet. 43:360-364(2011).
-!- FUNCTION: Required for both DNA replication and mitosis
(PubMed:11125146, PubMed:22581055, PubMed:21856198,
PubMed:14993212, PubMed:26842564). DNA replication licensing
factor, required for pre-replication complex assembly. Cooperates
with CDC6 and the origin recognition complex (ORC) during G1 phase
of the cell cycle to promote the loading of the mini-chromosome
maintenance (MCM) complex onto DNA to generate pre-replication
complexes (pre-RC)(PubMed:14672932). Required also for mitosis by
promoting stable kinetochore-microtubule attachments
(PubMed:22581055). Potential oncogene (By similarity).
{ECO:0000250|UniProtKB:Q8R4E9, ECO:0000269|PubMed:11125146,
ECO:0000269|PubMed:14672932, ECO:0000269|PubMed:14993212,
ECO:0000269|PubMed:21856198, ECO:0000269|PubMed:22581055,
ECO:0000269|PubMed:26842564}.
-!- SUBUNIT: Interacts with GMNN; inhibits binding of the MCM complex
to origins of replication (PubMed:11125146, PubMed:14672932,
PubMed:14993212, PubMed:15257290). Interacts with CDC6; are
mutually dependent on one another for loading MCM complexes onto
chromatin (PubMed:14672932). Interacts with PCNA
(PubMed:16861906). Interacts with LRWD1 during G1 phase and during
mitosis (PubMed:22645314). Interacts with NDC80 subunit of the
NDC80 complex; leading to kinetochore localization
(PubMed:22581055). Interacts with GRWD1; origin binding of GRWD1
is dependent on CDT1 (PubMed:25990725). Interacts with KAT7
(PubMed:18832067). Interacts with ubiquitin-binding protein FAF1;
the interaction is likely to promote CDT1 degradation
(PubMed:26842564). {ECO:0000269|PubMed:11125146,
ECO:0000269|PubMed:14672932, ECO:0000269|PubMed:14993212,
ECO:0000269|PubMed:15257290, ECO:0000269|PubMed:16861906,
ECO:0000269|PubMed:18832067, ECO:0000269|PubMed:21543332,
ECO:0000269|PubMed:22581055, ECO:0000269|PubMed:22645314,
ECO:0000269|PubMed:25990725, ECO:0000269|PubMed:26842564}.
-!- INTERACTION:
Q99741:CDC6; NbExp=3; IntAct=EBI-456953, EBI-374862;
O75496:GMNN; NbExp=20; IntAct=EBI-456953, EBI-371669;
Q14566:MCM6; NbExp=4; IntAct=EBI-456953, EBI-374900;
O14777:NDC80; NbExp=7; IntAct=EBI-456953, EBI-715849;
P12004:PCNA; NbExp=2; IntAct=EBI-456953, EBI-358311;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11125146,
ECO:0000269|PubMed:26842564}. Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:22581055}. Note=Transiently localizes to
kinetochores during prometaphase and metaphase.
{ECO:0000269|PubMed:22581055}.
-!- DEVELOPMENTAL STAGE: Present during G1 and early S phase of the
cell cycle. Degraded during the late S, G2, and M phases.
{ECO:0000269|PubMed:11125146, ECO:0000269|PubMed:27296872}.
-!- INDUCTION: Induced by E2F transcription factors (PubMed:14990995).
{ECO:0000269|PubMed:14990995}.
-!- DOMAIN: The PIP-box K+4 motif mediates both the interaction with
PCNA and the recruitment of the DCX(DTL) complex: while the PIP-
box interacts with PCNA, the presence of the K+4 submotif,
recruits the DCX(DTL) complex, leading to its ubiquitination.
{ECO:0000250|UniProtKB:Q9I9A7}.
-!- PTM: Two independent E3 ubiquitin ligase complexes, SCF(SKP2) and
the DCX(DTL) complex, mediated CDT1 degradation in S phase.
Ubiquitinated by the DCX(DTL) complex, in response to DNA damage,
leading to its degradation. Ubiquitination by the DCX(DTL) complex
is necessary to ensure proper cell cycle regulation and is PCNA-
dependent: interacts with PCNA via its PIP-box, while the presence
of the containing the 'K+4' motif in the PIP box, recruit the
DCX(DTL) complex, leading to its degradation. Phosphorylation at
Thr-29 by CDK2 targets CDT1 for ubiquitination by SCF(SKP2) E3
ubiquitin ligase and subsequent degradation (PubMed:14993212). The
interaction with GMNN protects it against ubiquitination.
Deubiquitinated by USP37 (PubMed:27296872).
{ECO:0000269|PubMed:14993212, ECO:0000269|PubMed:15257290,
ECO:0000269|PubMed:16861906, ECO:0000269|PubMed:16949367,
ECO:0000269|PubMed:17085480, ECO:0000269|PubMed:27296872}.
-!- PTM: Phosphorylation by cyclin A-dependent kinases at Thr-29
targets CDT1 for ubiquitynation by SCF(SKP2) E3 ubiquitin ligase
and subsequent degradation (PubMed:14993212). Phosphorylated at
Thr-29 by MAPK8/JNK1, which blocks replication licensing in
response to stress (PubMed:21856198). Binding to GMNN is not
affected by phosphorylation. {ECO:0000250|UniProtKB:Q8R4E9,
ECO:0000269|PubMed:14993212, ECO:0000269|PubMed:21856198,
ECO:0000269|PubMed:22645314}.
-!- DISEASE: Meier-Gorlin syndrome 4 (MGORS4) [MIM:613804]: A syndrome
characterized by bilateral microtia, aplasia/hypoplasia of the
patellae, and severe intrauterine and postnatal growth retardation
with short stature and poor weight gain. Additional clinical
findings include anomalies of cranial sutures, microcephaly,
apparently low-set and simple ears, microstomia, full lips, highly
arched or cleft palate, micrognathia, genitourinary tract
anomalies, and various skeletal anomalies. While almost all cases
have primordial dwarfism with substantial prenatal and postnatal
growth retardation, not all cases have microcephaly, and microtia
and absent/hypoplastic patella are absent in some. Despite the
presence of microcephaly, intellect is usually normal.
{ECO:0000269|PubMed:21358631, ECO:0000269|PubMed:21358632}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- SIMILARITY: Belongs to the Cdt1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AF070552; Type=Frameshift; Positions=278, 312; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CDT1ID44175ch16q24.html";
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EMBL; AF321125; AAG45181.1; -; mRNA.
EMBL; AB053172; BAB61878.1; -; mRNA.
EMBL; AC092384; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000137; AAH00137.2; -; mRNA.
EMBL; BC008676; AAH08676.1; -; mRNA.
EMBL; BC008860; AAH08860.2; -; mRNA.
EMBL; BC009410; AAH09410.1; -; mRNA.
EMBL; BC014202; AAH14202.2; -; mRNA.
EMBL; BC049205; AAH49205.1; -; mRNA.
EMBL; AF070552; -; NOT_ANNOTATED_CDS; mRNA.
CCDS; CCDS32510.1; -.
RefSeq; NP_112190.2; NM_030928.3.
UniGene; Hs.122908; -.
PDB; 2LE8; NMR; -; B=413-440.
PDB; 2WVR; X-ray; 3.30 A; C=1-546.
PDBsum; 2LE8; -.
PDBsum; 2WVR; -.
ProteinModelPortal; Q9H211; -.
SMR; Q9H211; -.
BioGrid; 123555; 66.
CORUM; Q9H211; -.
DIP; DIP-31089N; -.
IntAct; Q9H211; 28.
MINT; Q9H211; -.
STRING; 9606.ENSP00000301019; -.
MoonProt; Q9H211; -.
iPTMnet; Q9H211; -.
PhosphoSitePlus; Q9H211; -.
BioMuta; CDT1; -.
DMDM; 308153620; -.
EPD; Q9H211; -.
MaxQB; Q9H211; -.
PaxDb; Q9H211; -.
PeptideAtlas; Q9H211; -.
PRIDE; Q9H211; -.
Ensembl; ENST00000301019; ENSP00000301019; ENSG00000167513.
GeneID; 81620; -.
KEGG; hsa:81620; -.
UCSC; uc002flu.4; human.
CTD; 81620; -.
DisGeNET; 81620; -.
EuPathDB; HostDB:ENSG00000167513.8; -.
GeneCards; CDT1; -.
H-InvDB; HIX0013345; -.
HGNC; HGNC:24576; CDT1.
HPA; HPA017224; -.
MalaCards; CDT1; -.
MIM; 605525; gene.
MIM; 613804; phenotype.
neXtProt; NX_Q9H211; -.
OpenTargets; ENSG00000167513; -.
Orphanet; 2554; Ear-patella-short stature syndrome.
PharmGKB; PA145008572; -.
eggNOG; KOG4762; Eukaryota.
eggNOG; ENOG410XT37; LUCA.
GeneTree; ENSGT00390000012337; -.
HOVERGEN; HBG050872; -.
InParanoid; Q9H211; -.
KO; K10727; -.
OMA; GMLHNRS; -.
OrthoDB; EOG091G07YA; -.
PhylomeDB; Q9H211; -.
TreeFam; TF101159; -.
Reactome; R-HSA-539107; Activation of E2F1 target genes at G1/S.
Reactome; R-HSA-68827; CDT1 association with the CDC6:ORC:origin complex.
Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
Reactome; R-HSA-68949; Orc1 removal from chromatin.
Reactome; R-HSA-68962; Activation of the pre-replicative complex.
SIGNOR; Q9H211; -.
EvolutionaryTrace; Q9H211; -.
GeneWiki; DNA_replication_factor_CDT1; -.
GenomeRNAi; 81620; -.
PRO; PR:Q9H211; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000167513; -.
CleanEx; HS_CDT1; -.
ExpressionAtlas; Q9H211; baseline and differential.
Genevisible; Q9H211; HS.
GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:CAFA.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0051315; P:attachment of mitotic spindle microtubules to kinetochore; IMP:UniProtKB.
GO; GO:0051301; P:cell division; IMP:CAFA.
GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
GO; GO:1902426; P:deactivation of mitotic spindle assembly checkpoint; IMP:CAFA.
GO; GO:0000076; P:DNA replication checkpoint; IDA:UniProtKB.
GO; GO:0071163; P:DNA replication preinitiation complex assembly; IDA:CAFA.
GO; GO:0000082; P:G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0051383; P:kinetochore organization; IMP:CAFA.
GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
GO; GO:1905341; P:negative regulation of protein localization to kinetochore; IMP:CAFA.
GO; GO:0035563; P:positive regulation of chromatin binding; IDA:CAFA.
GO; GO:0045740; P:positive regulation of DNA replication; IMP:UniProtKB.
GO; GO:2000105; P:positive regulation of DNA-dependent DNA replication; IDA:CAFA.
GO; GO:2001178; P:positive regulation of mediator complex assembly; IDA:CAFA.
GO; GO:0031334; P:positive regulation of protein complex assembly; IMP:CAFA.
GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IMP:CAFA.
GO; GO:0033044; P:regulation of chromosome organization; IMP:CAFA.
GO; GO:1902595; P:regulation of DNA replication origin binding; IDA:CAFA.
GO; GO:0030174; P:regulation of DNA-dependent DNA replication initiation; IDA:UniProtKB.
GO; GO:0033262; P:regulation of nuclear cell cycle DNA replication; IEA:Ensembl.
GO; GO:0000083; P:regulation of transcription involved in G1/S transition of mitotic cell cycle; TAS:Reactome.
GO; GO:0072708; P:response to sorbitol; IDA:CAFA.
InterPro; IPR032054; Cdt1_C.
InterPro; IPR014939; CDT1_Gemini-bd-like.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF08839; CDT1; 1.
Pfam; PF16679; CDT1_C; 1.
SMART; SM01075; CDT1; 1.
SUPFAM; SSF46785; SSF46785; 1.
1: Evidence at protein level;
3D-structure; Cell cycle; Cell division; Centromere; Chromosome;
Complete proteome; Disease mutation; DNA replication; Dwarfism;
Kinetochore; Mitosis; Nucleus; Phosphoprotein; Polymorphism;
Proto-oncogene; Reference proteome; Ubl conjugation.
CHAIN 1 546 DNA replication factor Cdt1.
/FTId=PRO_0000191619.
REGION 150 190 Interaction with GMNN.
REGION 451 546 Interaction with LRWD1.
{ECO:0000269|PubMed:22645314}.
MOTIF 1 23 PIP-box K+4 motif.
MOTIF 68 70 Cyclin-binding motif.
MOD_RES 29 29 Phosphothreonine; by MAPK8.
{ECO:0000269|PubMed:21856198}.
MOD_RES 31 31 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 93 93 Phosphoserine; by MAPK8.
{ECO:0000269|PubMed:21856198}.
MOD_RES 318 318 Phosphoserine; by MAPK8.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:21856198}.
MOD_RES 380 380 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VARIANT 66 66 A -> T (in MGORS4; dbSNP:rs387906918).
{ECO:0000269|PubMed:21358632}.
/FTId=VAR_065488.
VARIANT 117 117 Q -> H (in MGORS4; dbSNP:rs779871947).
{ECO:0000269|PubMed:21358632}.
/FTId=VAR_065489.
VARIANT 135 135 A -> V (in dbSNP:rs3218725).
/FTId=VAR_029163.
VARIANT 172 172 R -> C (in dbSNP:rs3218727).
/FTId=VAR_029164.
VARIANT 234 234 C -> R (in dbSNP:rs507329).
{ECO:0000269|PubMed:10766248,
ECO:0000269|PubMed:11125146,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.5}.
/FTId=VAR_054504.
VARIANT 262 262 T -> A (in dbSNP:rs480727).
{ECO:0000269|PubMed:10766248,
ECO:0000269|PubMed:11125146,
ECO:0000269|PubMed:15489334}.
/FTId=VAR_054505.
VARIANT 453 453 R -> W (in MGORS4; dbSNP:rs200672589).
{ECO:0000269|PubMed:21358632}.
/FTId=VAR_065490.
VARIANT 456 456 E -> A (in dbSNP:rs3218729).
/FTId=VAR_029165.
VARIANT 462 462 R -> Q (in MGORS4; dbSNP:rs387906917).
{ECO:0000269|PubMed:21358632}.
/FTId=VAR_065491.
VARIANT 468 468 E -> K (in MGORS4; dbSNP:rs200652608).
{ECO:0000269|PubMed:21358631}.
/FTId=VAR_065492.
VARIANT 537 537 A -> V (in dbSNP:rs3218721).
/FTId=VAR_024408.
MUTAGEN 68 70 RRL->AAA: Abolishes binding of cyclin A-
dependent protein kinases.
{ECO:0000269|PubMed:14993212}.
MUTAGEN 170 170 Y->A: Alters interaction with GMNN.
{ECO:0000269|PubMed:21543332}.
CONFLICT 494 494 E -> K (in Ref. 4; AAH49205).
{ECO:0000305}.
HELIX 169 172 {ECO:0000244|PDB:2WVR}.
HELIX 174 177 {ECO:0000244|PDB:2WVR}.
STRAND 180 182 {ECO:0000244|PDB:2WVR}.
HELIX 188 209 {ECO:0000244|PDB:2WVR}.
HELIX 216 227 {ECO:0000244|PDB:2WVR}.
HELIX 233 242 {ECO:0000244|PDB:2WVR}.
HELIX 244 246 {ECO:0000244|PDB:2WVR}.
STRAND 247 251 {ECO:0000244|PDB:2WVR}.
STRAND 269 273 {ECO:0000244|PDB:2WVR}.
HELIX 288 314 {ECO:0000244|PDB:2WVR}.
TURN 315 319 {ECO:0000244|PDB:2WVR}.
HELIX 325 327 {ECO:0000244|PDB:2WVR}.
HELIX 420 423 {ECO:0000244|PDB:2LE8}.
HELIX 425 435 {ECO:0000244|PDB:2LE8}.
SEQUENCE 546 AA; 60390 MW; 8179D0330C135FB7 CRC64;
MEQRRVTDFF ARRRPGPPRI APPKLACRTP SPARPALRAP ASATSGSRKR ARPPAAPGRD
QARPPARRRL RLSVDEVSSP STPEAPDIPA CPSPGQKIKK STPAAGQPPH LTSAQDQDTI
SELASCLQRA RELGARVRAL KASAQDAGES CTPEAEGRPE EPCGEKAPAY QRFHALAQPG
LPGLVLPYKY QVLAEMFRSM DTIVGMLHNR SETPTFAKVQ RGVQDMMRRR FEECNVGQIK
TVYPASYRFR QERSVPTFKD GTRRSDYQLT IEPLLEQEAD GAAPQLTASR LLQRRQIFSQ
KLVEHVKEHH KAFLASLSPA MVVPEDQLTR WHPRFNVDEV PDIEPAALPQ PPATEKLTTA
QEVLARARNL ISPRMEKALS QLALRSAAPS SPGSPRPALP ATPPATPPAA SPSALKGVSQ
DLLERIRAKE AQKQLAQMTR CPEQEQRLQR LERLPELARV LRSVFVSERK PALSMEVACA
RMVGSCCTIM SPGEMEKHLL LLSELLPDWL SLHRIRTDTY VKLDKAADLA HITARLAHQT
RAEEGL


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