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Protein timeless homolog (hTIM)

 TIM_HUMAN               Reviewed;        1208 AA.
Q9UNS1; B2ZAV0; O94802; Q86VM1; Q8IWH3;
15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
07-NOV-2018, entry version 156.
RecName: Full=Protein timeless homolog;
Short=hTIM;
Name=TIMELESS {ECO:0000312|EMBL:AAH50557.1};
Synonyms=TIM {ECO:0000303|PubMed:9856465},
TIM1 {ECO:0000303|PubMed:9891984},
TIMELESS1 {ECO:0000303|PubMed:9891984};
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:BAA36499.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT LEU-455.
TISSUE=Brain {ECO:0000312|EMBL:BAA36499.1};
PubMed=9891984; DOI=10.1016/S0014-5793(98)01597-X;
Koike N., Hida A., Numano R., Hirose M., Sakaki Y., Tei H.;
"Identification of the mammalian homologues of the Drosophila timeless
gene, Timeless1.";
FEBS Lett. 441:427-431(1998).
[2] {ECO:0000305, ECO:0000312|EMBL:AAC80011.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, AND VARIANTS LEU-455 AND GLN-831.
TISSUE=Placenta {ECO:0000269|PubMed:9856465};
PubMed=9856465; DOI=10.1016/S0896-6273(00)80627-3;
Sangoram A.M., Saez L., Antoch M.P., Gekakis N., Staknis D.,
Whiteley A., Fruechte E.M., Vitaterna M.H., Shimomura K., King D.P.,
Young M.W., Weitz C.J., Takahashi J.S.;
"Mammalian circadian autoregulatory loop: a timeless ortholog and
mPer1 interact and negatively regulate CLOCK-ARTNL/BMAL1-induced
transcription.";
Neuron 21:1101-1113(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-129; LEU-455;
SER-471; GLN-831; VAL-870; HIS-922; TRP-924; THR-1017 AND LEU-1018.
NIEHS SNPs program;
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[5] {ECO:0000305, ECO:0000312|EMBL:AAH50557.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS GLN-831 AND LEU-1018.
TISSUE=Duodenum {ECO:0000312|EMBL:AAH50557.1}, and
Skin {ECO:0000312|EMBL:AAH39842.1};
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).
[6]
INTERACTION WITH ATR; ATRIP; CHEK1 AND CRY2, AND INDUCTION.
PubMed=15798197; DOI=10.1128/MCB.25.8.3109-3116.2005;
Uensal-Kacmaz K., Mullen T.E., Kaufmann W.K., Sancar A.;
"Coupling of human circadian and cell cycles by the timeless
protein.";
Mol. Cell. Biol. 25:3109-3116(2005).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[9]
INTERACTION WITH TIPIN.
PubMed=17116885; DOI=10.1073/pnas.0609251103;
Chou D.M., Elledge S.J.;
"Tipin and Timeless form a mutually protective complex required for
genotoxic stress resistance and checkpoint function.";
Proc. Natl. Acad. Sci. U.S.A. 103:18143-18147(2006).
[10]
INTERACTION WITH TIPIN.
PubMed=17102137; DOI=10.1074/jbc.M605596200;
Yoshizawa-Sugata N., Masai H.;
"Human Tim/Timeless-interacting protein, Tipin, is required for
efficient progression of S phase and DNA replication checkpoint.";
J. Biol. Chem. 282:2729-2740(2007).
[11]
SUBCELLULAR LOCATION, INTERACTION WITH CLSPN, AND FUNCTION.
PubMed=17141802; DOI=10.1016/j.jmb.2006.10.097;
Gotter A.L., Suppa C., Emanuel B.S.;
"Mammalian TIMELESS and Tipin are evolutionarily conserved replication
fork-associated factors.";
J. Mol. Biol. 366:36-52(2007).
[12]
INTERACTION WITH TIPIN, AND FUNCTION.
PubMed=17296725; DOI=10.1128/MCB.02190-06;
Uensal-Kacmaz K., Chastain P.D., Qu P.-P., Minoo P.,
Cordeiro-Stone M., Sancar A., Kaufmann W.K.;
"The human Tim/Tipin complex coordinates an Intra-S checkpoint
response to UV that slows replication fork displacement.";
Mol. Cell. Biol. 27:3131-3142(2007).
[13]
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).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149 AND SER-1173, 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).
[16]
REVIEW.
PubMed=20139726; DOI=10.4161/cc.9.4.10676;
McFarlane R.J., Mian S., Dalgaard J.Z.;
"The many facets of the Tim-Tipin protein families' roles in
chromosome biology.";
Cell Cycle 9:700-705(2010).
[17]
INTERACTION WITH DDX11.
PubMed=20124417; DOI=10.1242/jcs.057984;
Leman A.R., Noguchi C., Lee C.Y., Noguchi E.;
"Human Timeless and Tipin stabilize replication forks and facilitate
sister-chromatid cohesion.";
J. Cell Sci. 123:660-670(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149 AND SER-1173, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
REVIEW.
PubMed=21670590; DOI=10.4161/cc.10.14.15853;
Diaz-Martinez L.A., Clarke D.J.;
"Timeless makes some time for itself.";
Cell Cycle 10:2254-2254(2011).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149 AND SER-1173, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-281; SER-1074; SER-1087;
THR-1089; SER-1149 AND SER-1173, 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).
[23]
FUNCTION.
PubMed=23418588; DOI=10.1371/journal.pone.0056623;
Engelen E., Janssens R.C., Yagita K., Smits V.A., van der Horst G.T.,
Tamanini F.;
"Mammalian TIMELESS is involved in period determination and DNA
damage-dependent phase advancing of the circadian clock.";
PLoS ONE 8:E56623-E56623(2013).
[24]
INTERACTION WITH DDX11.
PubMed=26503245; DOI=10.1093/nar/gkv1112;
Cali F., Bharti S.K., Di Perna R., Brosh R.M. Jr., Pisani F.M.;
"Tim/Timeless, a member of the replication fork protection complex,
operates with the Warsaw breakage syndrome DNA helicase DDX11 in the
same fork recovery pathway.";
Nucleic Acids Res. 44:705-717(2016).
[25]
VARIANTS [LARGE SCALE ANALYSIS] ASP-429 AND GLU-1008.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Plays an important role in the control of DNA
replication, maintenance of replication fork stability,
maintenance of genome stability throughout normal DNA replication
and in the regulation of the circadian clock. Involved in the
determination of period length and in the DNA damage-dependent
phase advancing of the circadian clock. Negatively regulates
CLOCK|NPAS2-ARTNL/BMAL1|ARTNL2/BMAL2-induced transactivation of
PER1 possibly via translocation of PER1 into the nucleus. Forms a
complex with TIPIN and this complex regulates DNA replication
processes under both normal and stress conditions, stabilizes
replication forks and influences both CHEK1 phosphorylation and
the intra-S phase checkpoint in response to genotoxic stress.
Timeless promotes TIPIN nuclear localization. Involved in cell
survival after DNA damage or replication stress. May be
specifically required for the ATR-CHEK1 pathway in the replication
checkpoint induced by hydroxyurea or ultraviolet light. May also
play an important role in epithelial cell morphogenesis and
formation of branching tubules. {ECO:0000269|PubMed:17141802,
ECO:0000269|PubMed:17296725, ECO:0000269|PubMed:23418588,
ECO:0000269|PubMed:9856465}.
-!- SUBUNIT: Homodimer or homomultimer (By similarity). Component of
the circadian core oscillator, which includes the CRY proteins,
CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSKN1D and/or CSNK1E,
TIMELESS, and the PER proteins. Interacts directly with PER2; the
interaction with PER2 is via its second PAS domain. Interacts
directly with PER1 and PER3 (By similarity). Interacts with CRY2,
CHEK1, ATR and ATRIP (PubMed:15798197). Interacts with CRY1 (By
similarity). Interacts with CLSPN (PubMed:17141802). Interacts
with TIPIN (PubMed:17116885, PubMed:17102137, PubMed:17296725).
Interacts with DDX11; this interaction increases recruitment of
both proteins onto chromatin in response to replication stress
induction by hydroxyurea (PubMed:20124417).
{ECO:0000250|UniProtKB:Q9R1X4, ECO:0000269|PubMed:15798197,
ECO:0000269|PubMed:17102137, ECO:0000269|PubMed:17116885,
ECO:0000269|PubMed:17141802, ECO:0000269|PubMed:17296725,
ECO:0000269|PubMed:20124417, ECO:0000269|PubMed:26503245}.
-!- INTERACTION:
O14757:CHEK1; NbExp=2; IntAct=EBI-2212315, EBI-974488;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17141802}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1 {ECO:0000269|PubMed:9856465, ECO:0000269|PubMed:9891984};
IsoId=Q9UNS1-1; Sequence=Displayed;
Name=2 {ECO:0000269|PubMed:9856465};
IsoId=Q9UNS1-2; Sequence=VSP_051693;
-!- TISSUE SPECIFICITY: Expressed in all tissues examined including
brain, heart, lung, liver, skeletal muscle, kidney, placenta,
pancreas, spleen, thymus and testis. Highest levels of expression
in placenta, pancreas, thymus and testis.
{ECO:0000269|PubMed:9856465, ECO:0000269|PubMed:9891984}.
-!- INDUCTION: Regulated by the cell cycle. High levels in S, G(2) and
M phases, with highest level in S phase. Low expression in G(0)
and G(1) phases. {ECO:0000269|PubMed:15798197}.
-!- SIMILARITY: Belongs to the timeless family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH39842.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/timeless/";
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EMBL; AB015597; BAA36499.1; -; mRNA.
EMBL; AF098162; AAC80011.1; -; mRNA.
EMBL; EU627094; ACD11488.1; -; Genomic_DNA.
EMBL; AC024884; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC039842; AAH39842.1; ALT_SEQ; mRNA.
EMBL; BC050557; AAH50557.1; -; mRNA.
CCDS; CCDS81699.1; -. [Q9UNS1-2]
CCDS; CCDS8918.1; -. [Q9UNS1-1]
RefSeq; NP_001317224.1; NM_001330295.1. [Q9UNS1-2]
RefSeq; NP_003911.2; NM_003920.4. [Q9UNS1-1]
UniGene; Hs.118631; -.
PDB; 4XHT; X-ray; 1.65 A; A/B/C/D=1000-1098.
PDB; 4XHU; X-ray; 2.09 A; B/D=1000-1098.
PDB; 4XHW; X-ray; 2.85 A; A/B/C/D=1000-1098.
PDB; 5MQI; X-ray; 1.85 A; A=1-238, A=331-463.
PDBsum; 4XHT; -.
PDBsum; 4XHU; -.
PDBsum; 4XHW; -.
PDBsum; 5MQI; -.
ProteinModelPortal; Q9UNS1; -.
SMR; Q9UNS1; -.
BioGrid; 114428; 77.
DIP; DIP-47395N; -.
IntAct; Q9UNS1; 14.
MINT; Q9UNS1; -.
STRING; 9606.ENSP00000450607; -.
iPTMnet; Q9UNS1; -.
PhosphoSitePlus; Q9UNS1; -.
BioMuta; TIMELESS; -.
DMDM; 296452931; -.
EPD; Q9UNS1; -.
PaxDb; Q9UNS1; -.
PeptideAtlas; Q9UNS1; -.
PRIDE; Q9UNS1; -.
ProteomicsDB; 85326; -.
ProteomicsDB; 85327; -. [Q9UNS1-2]
Ensembl; ENST00000229201; ENSP00000229201; ENSG00000111602. [Q9UNS1-2]
Ensembl; ENST00000553532; ENSP00000450607; ENSG00000111602. [Q9UNS1-1]
GeneID; 8914; -.
KEGG; hsa:8914; -.
UCSC; uc001slf.3; human. [Q9UNS1-1]
CTD; 8914; -.
DisGeNET; 8914; -.
EuPathDB; HostDB:ENSG00000111602.11; -.
GeneCards; TIMELESS; -.
H-InvDB; HIX0010725; -.
HGNC; HGNC:11813; TIMELESS.
HPA; HPA060655; -.
MIM; 603887; gene.
neXtProt; NX_Q9UNS1; -.
OpenTargets; ENSG00000111602; -.
PharmGKB; PA36520; -.
eggNOG; KOG1974; Eukaryota.
eggNOG; ENOG410XQM6; LUCA.
GeneTree; ENSGT00390000015124; -.
HOGENOM; HOG000133002; -.
HOVERGEN; HBG079258; -.
InParanoid; Q9UNS1; -.
KO; K03155; -.
OMA; DSMVPFD; -.
OrthoDB; EOG091G00YS; -.
PhylomeDB; Q9UNS1; -.
TreeFam; TF312802; -.
Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
ChiTaRS; TIMELESS; human.
GenomeRNAi; 8914; -.
PRO; PR:Q9UNS1; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000111602; Expressed in 163 organ(s), highest expression level in embryo.
CleanEx; HS_TIMELESS; -.
Genevisible; Q9UNS1; HS.
GO; GO:0000790; C:nuclear chromatin; IDA:HGNC.
GO; GO:0000228; C:nuclear chromosome; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:HGNC.
GO; GO:0031298; C:replication fork protection complex; IBA:GO_Central.
GO; GO:0003677; F:DNA binding; IBA:GO_Central.
GO; GO:0046982; F:protein heterodimerization activity; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IEA:Ensembl.
GO; GO:0044770; P:cell cycle phase transition; IMP:BHF-UCL.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:1904976; P:cellular response to bleomycin; IMP:UniProtKB.
GO; GO:0072719; P:cellular response to cisplatin; IMP:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0072711; P:cellular response to hydroxyurea; IMP:UniProtKB.
GO; GO:0007623; P:circadian rhythm; ISS:UniProtKB.
GO; GO:0009582; P:detection of abiotic stimulus; TAS:ProtInc.
GO; GO:0006281; P:DNA repair; IBA:GO_Central.
GO; GO:0000076; P:DNA replication checkpoint; IBA:GO_Central.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0002009; P:morphogenesis of an epithelium; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:2000781; P:positive regulation of double-strand break repair; IMP:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
GO; GO:0043111; P:replication fork arrest; IBA:GO_Central.
GO; GO:0048478; P:replication fork protection; IBA:GO_Central.
InterPro; IPR006906; Timeless.
InterPro; IPR007725; TIMELESS_C.
Pfam; PF04821; TIMELESS; 1.
Pfam; PF05029; TIMELESS_C; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Biological rhythms; Cell cycle;
Cell division; Complete proteome; Developmental protein; DNA damage;
Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome;
Transcription; Transcription regulation.
CHAIN 1 1208 Protein timeless homolog.
/FTId=PRO_0000072538.
REGION 1 309 Required for homodimerization and for
interaction with CRY1 and CHEK1.
{ECO:0000250}.
REGION 1082 1208 Required for nuclear localization.
{ECO:0000250}.
COMPBIAS 661 688 Glu-rich.
MOD_RES 281 281 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1074 1074 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1087 1087 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1089 1089 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1149 1149 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1173 1173 Phosphoserine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 177 177 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:9856465}.
/FTId=VSP_051693.
VARIANT 129 129 A -> S (in dbSNP:rs72478986).
{ECO:0000269|Ref.3}.
/FTId=VAR_047879.
VARIANT 429 429 A -> D (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036435.
VARIANT 455 455 I -> L (in dbSNP:rs774027).
{ECO:0000269|PubMed:9856465,
ECO:0000269|PubMed:9891984,
ECO:0000269|Ref.3}.
/FTId=VAR_021483.
VARIANT 471 471 N -> S (in dbSNP:rs72478993).
{ECO:0000269|Ref.3}.
/FTId=VAR_047880.
VARIANT 831 831 R -> Q (in dbSNP:rs774047).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9856465,
ECO:0000269|Ref.3}.
/FTId=VAR_021484.
VARIANT 870 870 M -> V (in dbSNP:rs61733875).
{ECO:0000269|Ref.3}.
/FTId=VAR_047881.
VARIANT 922 922 R -> H (in dbSNP:rs72478999).
{ECO:0000269|Ref.3}.
/FTId=VAR_047882.
VARIANT 924 924 R -> W (in dbSNP:rs72479000).
{ECO:0000269|Ref.3}.
/FTId=VAR_047883.
VARIANT 1008 1008 Q -> E (in a breast cancer sample;
somatic mutation; dbSNP:rs151188513).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036436.
VARIANT 1017 1017 I -> T (in dbSNP:rs61376834).
{ECO:0000269|Ref.3}.
/FTId=VAR_047884.
VARIANT 1018 1018 P -> L (in dbSNP:rs2291739).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.3}.
/FTId=VAR_021485.
HELIX 8 15 {ECO:0000244|PDB:5MQI}.
STRAND 17 21 {ECO:0000244|PDB:5MQI}.
STRAND 24 27 {ECO:0000244|PDB:5MQI}.
HELIX 31 43 {ECO:0000244|PDB:5MQI}.
HELIX 50 58 {ECO:0000244|PDB:5MQI}.
HELIX 60 63 {ECO:0000244|PDB:5MQI}.
HELIX 65 71 {ECO:0000244|PDB:5MQI}.
HELIX 76 89 {ECO:0000244|PDB:5MQI}.
HELIX 93 97 {ECO:0000244|PDB:5MQI}.
HELIX 106 123 {ECO:0000244|PDB:5MQI}.
HELIX 127 142 {ECO:0000244|PDB:5MQI}.
HELIX 145 147 {ECO:0000244|PDB:5MQI}.
HELIX 150 168 {ECO:0000244|PDB:5MQI}.
HELIX 184 195 {ECO:0000244|PDB:5MQI}.
HELIX 198 207 {ECO:0000244|PDB:5MQI}.
HELIX 209 214 {ECO:0000244|PDB:5MQI}.
HELIX 215 225 {ECO:0000244|PDB:5MQI}.
TURN 226 228 {ECO:0000244|PDB:5MQI}.
HELIX 231 234 {ECO:0000244|PDB:5MQI}.
HELIX 336 352 {ECO:0000244|PDB:5MQI}.
HELIX 354 367 {ECO:0000244|PDB:5MQI}.
HELIX 369 371 {ECO:0000244|PDB:5MQI}.
HELIX 376 391 {ECO:0000244|PDB:5MQI}.
HELIX 396 402 {ECO:0000244|PDB:5MQI}.
HELIX 405 424 {ECO:0000244|PDB:5MQI}.
HELIX 426 428 {ECO:0000244|PDB:5MQI}.
HELIX 429 451 {ECO:0000244|PDB:5MQI}.
HELIX 1008 1012 {ECO:0000244|PDB:4XHT}.
HELIX 1016 1033 {ECO:0000244|PDB:4XHT}.
STRAND 1042 1044 {ECO:0000244|PDB:4XHW}.
HELIX 1049 1055 {ECO:0000244|PDB:4XHT}.
HELIX 1058 1067 {ECO:0000244|PDB:4XHT}.
TURN 1074 1076 {ECO:0000244|PDB:4XHT}.
STRAND 1078 1082 {ECO:0000244|PDB:4XHW}.
HELIX 1088 1096 {ECO:0000244|PDB:4XHT}.
SEQUENCE 1208 AA; 138658 MW; 16C6C07DDC6D2701 CRC64;
MDLHMMNCEL LATCSALGYL EGDTYHKEPD CLESVKDLIR YLRHEDETRD VRQQLGAAQI
LQSDLLPILT QHHQDKPLFD AVIRLMVNLT QPALLCFGNL PKEPSFRHHF LQVLTYLQAY
KEAFASEKAF GVLSETLYEL LQLGWEERQE EDNLLIERIL LLVRNILHVP ADLDQEKKID
DDASAHDQLL WAIHLSGLDD LLLFLASSSA EEQWSLHVLE IVSLMFRDQN PEQLAGVGQG
RLAQERSADF AELEVLRQRE MAEKKTRALQ RGNRHSRFGG SYIVQGLKSI GERDLIFHKG
LHNLRNYSSD LGKQPKKVPK RRQAARELSI QRRSALNVRL FLRDFCSEFL ENCYNRLMGS
VKDHLLREKA QQHDETYYMW ALAFFMAFNR AASFRPGLVS ETLSVRTFHF IEQNLTNYYE
MMLTDRKEAA SWARRMHLAL KAYQELLATV NEMDISPDEA VRESSRIIKN NIFYVMEYRE
LFLALFRKFD ERCQPRSFLR DLVETTHLFL KMLERFCRSR GNLVVQNKQK KRRKKKKKVL
DQAIVSGNVP SSPEEVEAVW PALAEQLQCC AQNSELSMDS VVPFDAASEV PVEEQRAEAM
VRIQDCLLAG QAPQALTLLR SAREVWPEGD VFGSQDISPE EEIQLLKQIL SAPLPRQQGP
EERGAEEEEE EEEEEEEELQ VVQVSEKEFN FLDYLKRFAC STVVRAYVLL LRSYQQNSAH
TNHCIVKMLH RLAHDLKMEA LLFQLSVFCL FNRLLSDPAA GAYKELVTFA KYILGKFFAL
AAVNQKAFVE LLFWKNTAVV REMTEGYGSL DDRSSSRRAP TWSPEEEAHL RELYLANKDV
EGQDVVEAIL AHLNTVPRTR KQIIHHLVQM GLADSVKDFQ RKGTHIVLWT GDQELELQRL
FEEFRDSDDV LGHIMKNITA KRSRARIVDK LLALGLVAER RELYKKRQKK LASSILPNGA
ESLKDFCQED LEEEENLPEE DSEEEEEGGS EAEQVQGSLV LSNENLGQSL HQEGFSIPLL
WLQNCLIRAA DDREEDGCSQ AVPLVPLTEE NEEAMENEQF QQLLRKLGVR PPASGQETFW
RIPAKLSPTQ LRRAAASLSQ PEEEQKLQPE LQPKVPGEQG SDEEHCKEHR AQALRALLLA
HKKKAGLASP EEEDAVGKEP LKAAPKKRQL LDSDEEQEED EGRNRAPELG APGIQKKKRY
QIEDDEDD


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