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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.
13-FEB-2019, entry version 158.
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: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]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, AND VARIANTS LEU-455 AND GLN-831.
TISSUE=Placenta;
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]
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]
FUNCTION, 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]
FUNCTION, AND INTERACTION WITH PARP1.
PubMed=30356214; DOI=10.1038/s41586-018-0629-6;
Liu H., Zhang H., Wu X., Ma D., Wu J., Wang L., Jiang Y., Fei Y.,
Zhu C., Tan R., Jungblut P., Pei G., Dorhoi A., Yan Q., Zhang F.,
Zheng R., Liu S., Liang H., Liu Z., Yang H., Chen J., Wang P.,
Tang T., Peng W., Hu Z., Xu Z., Huang X., Wang J., Li H., Zhou Y.,
Liu F., Yan D., Kaufmann S.H.E., Chen C., Mao Z., Ge B.;
"Nuclear cGAS suppresses DNA repair and promotes tumorigenesis.";
Nature 563:131-136(2018).
[26] {ECO:0000244|PDB:4XHT, ECO:0000244|PDB:4XHU, ECO:0000244|PDB:4XHW}
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1000-1098 IN COMPLEX WITH
PARP1, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PARP1, AND
MUTAGENESIS OF ARG-1081.
PubMed=26344098; DOI=10.1016/j.molcel.2015.07.031;
Xie S., Mortusewicz O., Ma H.T., Herr P., Poon R.Y., Helleday T.,
Qian C.;
"Timeless interacts with PARP-1 to promote homologous recombination
repair.";
Mol. Cell 60:163-176(2015).
[27]
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,
DNA repair and in the regulation of the circadian clock
(PubMed:9856465, PubMed:17141802, PubMed:17296725,
PubMed:23418588, PubMed:26344098). Required to stabilize
replication forks during DNA replication by forming a complex with
TIPIN: 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 (PubMed:17141802,
PubMed:17296725). TIMELESS promotes TIPIN nuclear localization
(PubMed:17141802, PubMed:17296725). Involved in cell survival
after DNA damage or replication stress by promoting DNA repair
(PubMed:17141802, PubMed:17296725, PubMed:26344098,
PubMed:30356214). In response to double-strand breaks (DSBs),
accumulates at DNA damage sites and promotes homologous
recombination repair via its interaction with PARP1
(PubMed:26344098, PubMed:30356214). May be specifically required
for the ATR-CHEK1 pathway in the replication checkpoint induced by
hydroxyurea or ultraviolet light (PubMed:15798197). Involved in
the determination of period length and in the DNA damage-dependent
phase advancing of the circadian clock (PubMed:23418588).
Negatively regulates CLOCK|NPAS2-ARTNL/BMAL1|ARTNL2/BMAL2-induced
transactivation of PER1 possibly via translocation of PER1 into
the nucleus (PubMed:9856465). May also play an important role in
epithelial cell morphogenesis and formation of branching tubules
(By similarity). {ECO:0000250|UniProtKB:Q9R1X4,
ECO:0000269|PubMed:15798197, ECO:0000269|PubMed:17141802,
ECO:0000269|PubMed:17296725, ECO:0000269|PubMed:23418588,
ECO:0000269|PubMed:26344098, ECO:0000269|PubMed:30356214,
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 (PubMed:9856465). Interacts
directly with PER2; the interaction with PER2 is via its second
PAS domain (By similarity). 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:17102137, PubMed:17116885, PubMed:17296725). Interacts
with DDX11; this interaction increases recruitment of both
proteins onto chromatin in response to replication stress
induction by hydroxyurea (PubMed:20124417, PubMed:26503245).
Interacts with PARP1; interaction is direct and independent of
poly-ADP-ribose (PubMed:26344098, PubMed:30356214).
{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:26344098,
ECO:0000269|PubMed:26503245, ECO:0000269|PubMed:30356214,
ECO:0000269|PubMed:9856465}.
-!- INTERACTION:
O14757:CHEK1; NbExp=2; IntAct=EBI-2212315, EBI-974488;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17141802}.
Chromosome {ECO:0000269|PubMed:26344098}. Note=In response to
double-strand breaks (DSBs), accumulates at DNA damage sites via
its interaction with PARP1. {ECO:0000269|PubMed:26344098}.
-!- 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; 78.
DIP; DIP-47395N; -.
IntAct; Q9UNS1; 15.
MINT; Q9UNS1; -.
STRING; 9606.ENSP00000450607; -.
iPTMnet; Q9UNS1; -.
PhosphoSitePlus; Q9UNS1; -.
BioMuta; TIMELESS; -.
DMDM; 296452931; -.
EPD; Q9UNS1; -.
jPOST; 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; 839367at2759; -.
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.
Genevisible; Q9UNS1; HS.
GO; GO:0000790; C:nuclear chromatin; IDA:HGNC.
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:0035861; C:site of double-strand break; IDA:UniProtKB.
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:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA: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; Chromosome; Complete proteome; Developmental protein;
DNA damage; DNA repair; 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|UniProtKB:Q9R1X4}.
REGION 1000 1098 Interaction with PARP1.
{ECO:0000269|PubMed:26344098}.
REGION 1082 1208 Required for nuclear localization.
{ECO:0000250|UniProtKB:Q9R1X4}.
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.
MUTAGEN 1081 1081 R->G: Abolishes interaction with PARP1.
{ECO:0000269|PubMed:26344098}.
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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Kits Elisa; taq POLYMERASE

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Gentaur; yes we can

Pathways :
WP1049: G Protein Signaling Pathways
WP1165: G Protein Signaling Pathways
WP1371: G Protein Signaling Pathways
WP1438: Influenza A virus infection
WP1493: Carbon assimilation C4 pathway
WP1502: Mitochondrial biogenesis
WP1531: Vitamin D synthesis
WP1566: Citrate cycle (TCA cycle)
WP1613: 1,4-Dichlorobenzene degradation
WP1616: ABC transporters
WP1624: Bacterial secretion system
WP1625: Base excision repair
WP1644: DNA replication
WP1650: Fluorobenzoate degradation
WP1654: gamma-Hexachlorocyclohexane degradation
WP1657: Glycerolipid metabolism
WP1659: Glycine, serine and threonine metabolism
WP1661: Glyoxylate and dicarboxylate metabolism
WP1663: Homologous recombination
WP1665: Limonene and pinene degradation
WP1672: Mismatch repair
WP1673: Naphthalene and anthracene degradation
WP1675: Nitrogen metabolism
WP1676: Non-homologous end-joining
WP1678: Nucleotide excision repair

Related Genes :
[TIMELESS TIM TIM1 TIMELESS1] Protein timeless homolog (hTIM)
[Timeless Tim1 Timeless1] Protein timeless homolog (mTim)
[Timeless] Protein timeless homolog (rTIM) (Timeless-like protein) (rTLP)
[tim-1 Y75B8A.22] Protein timeless homolog
[Per1 Per Rigui] Period circadian protein homolog 1 (mPER1) (Circadian clock protein PERIOD 1) (Circadian pacemaker protein Rigui)
[Per2] Period circadian protein homolog 2 (rPER2) (Circadian clock protein PERIOD 2)
[TIPIN] TIMELESS-interacting protein
[Per2] Period circadian protein homolog 2 (mPER2) (Circadian clock protein PERIOD 2)
[Per3] Period circadian protein homolog 3 (mPER3) (Circadian clock protein PERIOD 3)
[PER2 KIAA0347] Period circadian protein homolog 2 (hPER2) (Circadian clock protein PERIOD 2)
[CHEK1 CHK1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Cell cycle checkpoint kinase) (Checkpoint kinase-1)
[PER1 KIAA0482 PER RIGUI] Period circadian protein homolog 1 (hPER1) (Circadian clock protein PERIOD 1) (Circadian pacemaker protein Rigui)
[Tipin] TIMELESS-interacting protein
[Chek1 Chk1] Serine/threonine-protein kinase Chk1 (EC 2.7.11.1) (CHK1 checkpoint homolog) (Checkpoint kinase-1)
[PER3 GIG13] Period circadian protein homolog 3 (hPER3) (Cell growth-inhibiting gene 13 protein) (Circadian clock protein PERIOD 3)
[PER2] Period circadian protein homolog 2 (sPER2) (Circadian clock protein PERIOD 2)
[Per1] Period circadian protein homolog 1 (rPER1) (Circadian clock protein PERIOD 1)
[NTG2 SCR2 YOL043C] Endonuclease III homolog 2 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 2) (DNA glycosylase/AP lyase 2) (Endonuclease III-like glycosylase 2) (Redoxyendonuclease 2)
[NAV3 KIAA0938 POMFIL1 STEERIN3] Neuron navigator 3 (Pore membrane and/or filament-interacting-like protein 1) (Steerin-3) (Unc-53 homolog 3) (unc53H3)
[nth1 SPAC30D11.07] Endonuclease III homolog (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[NTG1 OGG2 SCR1 YAL015C FUN33] Endonuclease III homolog 1 (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase 1) (DNA glycosylase/AP lyase 1) (Endonuclease III-like glycosylase 1) (Redoxyendonuclease 1)
[NEIL2] Endonuclease 8-like 2 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil2) (DNA-(apurinic or apyrimidinic site) lyase Neil2) (Endonuclease VIII-like 2) (Nei homolog 2) (NEH2) (Nei-like protein 2)
[nth-1 R10E4.5] Endonuclease III homolog (CeNTH) (EC 3.2.2.-) (EC 4.2.99.18) (Bifunctional DNA N-glycosylase/DNA-(apurinic or apyrimidinic site) lyase) (DNA glycosylase/AP lyase)
[NAV2 HELAD1 KIAA1419 POMFIL2 RAINB1 STEERIN2] Neuron navigator 2 (EC 3.6.4.12) (Helicase APC down-regulated 1) (Pore membrane and/or filament-interacting-like protein 2) (Retinoic acid inducible in neuroblastoma 1) (Steerin-2) (Unc-53 homolog 2) (unc53H2)
[KMT2A ALL1 CXXC7 HRX HTRX MLL MLL1 TRX1] Histone-lysine N-methyltransferase 2A (Lysine N-methyltransferase 2A) (EC 2.1.1.43) (ALL-1) (CXXC-type zinc finger protein 7) (Myeloid/lymphoid or mixed-lineage leukemia) (Myeloid/lymphoid or mixed-lineage leukemia protein 1) (Trithorax-like protein) (Zinc finger protein HRX) [Cleaved into: MLL cleavage product N320 (N-terminal cleavage product of 320 kDa) (p320); MLL cleavage product C180 (C-terminal cleavage product of 180 kDa) (p180)]
[NEIL1] Endonuclease 8-like 1 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil1) (DNA-(apurinic or apyrimidinic site) lyase Neil1) (Endonuclease VIII-like 1) (FPG1) (Nei homolog 1) (NEH1) (Nei-like protein 1)
[Neil1 Nei1] Endonuclease 8-like 1 (EC 3.2.2.-) (EC 4.2.99.18) (DNA glycosylase/AP lyase Neil1) (DNA-(apurinic or apyrimidinic site) lyase Neil1) (Endonuclease VIII-like 1) (Nei homolog 1) (NEH1) (Nei-like protein 1)
[DDX11 CHL1 CHLR1 KRG2] ATP-dependent DNA helicase DDX11 (EC 3.6.4.12) (CHL1-related protein 1) (hCHLR1) (DEAD/H-box protein 11) (Keratinocyte growth factor-regulated gene 2 protein) (KRG-2)
[SMAD3 MADH3] Mothers against decapentaplegic homolog 3 (MAD homolog 3) (Mad3) (Mothers against DPP homolog 3) (hMAD-3) (JV15-2) (SMAD family member 3) (SMAD 3) (Smad3) (hSMAD3)
[Smad7 Madh7 Madh8] Mothers against decapentaplegic homolog 7 (MAD homolog 7) (Mothers against DPP homolog 7) (Mothers against decapentaplegic homolog 8) (MAD homolog 8) (Mothers against DPP homolog 8) (SMAD family member 7) (SMAD 7) (Smad7)

Bibliography :