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Q9UNS1

- TIM_HUMAN

UniProt

Q9UNS1 - TIM_HUMAN

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Protein

Protein timeless homolog

Gene

TIMELESS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.4 Publications

GO - Biological processi

  1. branching morphogenesis of an epithelial tube Source: Ensembl
  2. cell cycle phase transition Source: BHF-UCL
  3. cellular response to DNA damage stimulus Source: UniProtKB
  4. circadian rhythm Source: UniProtKB
  5. detection of abiotic stimulus Source: ProtInc
  6. lung development Source: Ensembl
  7. mitotic nuclear division Source: UniProtKB-KW
  8. morphogenesis of an epithelium Source: UniProtKB
  9. negative regulation of transcription, DNA-templated Source: UniProtKB
  10. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  11. regulation of circadian rhythm Source: UniProtKB
  12. response to abiotic stimulus Source: ProtInc
  13. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Biological rhythms, Cell cycle, Cell division, DNA damage, Mitosis, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Protein timeless homolog
Short name:
hTIM
Gene namesi
Name:TIMELESSImported
Synonyms:TIM1 Publication, TIM11 Publication, TIMELESS11 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:11813. TIMELESS.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nuclear chromatin Source: HGNC
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36520.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12081208Protein timeless homologPRO_0000072538Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1149 – 11491Phosphoserine3 Publications
Modified residuei1173 – 11731Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UNS1.
PaxDbiQ9UNS1.
PRIDEiQ9UNS1.

PTM databases

PhosphoSiteiQ9UNS1.

Expressioni

Tissue specificityi

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.2 Publications

Inductioni

Regulated by the cell cycle. High levels in S, G2 and M phases, with highest level in S phase. Low expression in G0 and G1 phases.1 Publication

Gene expression databases

BgeeiQ9UNS1.
CleanExiHS_TIMELESS.
GenevestigatoriQ9UNS1.

Organism-specific databases

HPAiHPA060655.

Interactioni

Subunit structurei

Homodimer or homomultimer. 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 PER1, PER2 and PER3; the interaction with PER2 is via its second PAS domain. Interacts with CRY1, CRY2, CHEK1, ATR and ATRIP. Interacts with CLSPN and TIPIN.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CHEK1O147572EBI-2212315,EBI-974488

Protein-protein interaction databases

BioGridi114428. 25 interactions.
IntActiQ9UNS1. 7 interactions.
STRINGi9606.ENSP00000229201.

Structurei

3D structure databases

ProteinModelPortaliQ9UNS1.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 309309Required for homodimerization and for interaction with CRY1 and CHEK1By similarityAdd
BLAST
Regioni1082 – 1208127Required for nuclear localizationBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi661 – 68828Glu-richAdd
BLAST

Sequence similaritiesi

Belongs to the timeless family.Curated

Phylogenomic databases

eggNOGiNOG328380.
GeneTreeiENSGT00390000015124.
HOGENOMiHOG000133002.
HOVERGENiHBG079258.
InParanoidiQ9UNS1.
KOiK03155.
OMAiRKGTQIV.
PhylomeDBiQ9UNS1.
TreeFamiTF312802.

Family and domain databases

InterProiIPR006906. Timeless.
IPR007725. TIMELESS_C.
[Graphical view]
PfamiPF04821. TIMELESS. 1 hit.
PF05029. TIMELESS_C. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 12 Publications (identifier: Q9UNS1-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MDLHMMNCEL LATCSALGYL EGDTYHKEPD CLESVKDLIR YLRHEDETRD
60 70 80 90 100
VRQQLGAAQI LQSDLLPILT QHHQDKPLFD AVIRLMVNLT QPALLCFGNL
110 120 130 140 150
PKEPSFRHHF LQVLTYLQAY KEAFASEKAF GVLSETLYEL LQLGWEERQE
160 170 180 190 200
EDNLLIERIL LLVRNILHVP ADLDQEKKID DDASAHDQLL WAIHLSGLDD
210 220 230 240 250
LLLFLASSSA EEQWSLHVLE IVSLMFRDQN PEQLAGVGQG RLAQERSADF
260 270 280 290 300
AELEVLRQRE MAEKKTRALQ RGNRHSRFGG SYIVQGLKSI GERDLIFHKG
310 320 330 340 350
LHNLRNYSSD LGKQPKKVPK RRQAARELSI QRRSALNVRL FLRDFCSEFL
360 370 380 390 400
ENCYNRLMGS VKDHLLREKA QQHDETYYMW ALAFFMAFNR AASFRPGLVS
410 420 430 440 450
ETLSVRTFHF IEQNLTNYYE MMLTDRKEAA SWARRMHLAL KAYQELLATV
460 470 480 490 500
NEMDISPDEA VRESSRIIKN NIFYVMEYRE LFLALFRKFD ERCQPRSFLR
510 520 530 540 550
DLVETTHLFL KMLERFCRSR GNLVVQNKQK KRRKKKKKVL DQAIVSGNVP
560 570 580 590 600
SSPEEVEAVW PALAEQLQCC AQNSELSMDS VVPFDAASEV PVEEQRAEAM
610 620 630 640 650
VRIQDCLLAG QAPQALTLLR SAREVWPEGD VFGSQDISPE EEIQLLKQIL
660 670 680 690 700
SAPLPRQQGP EERGAEEEEE EEEEEEEELQ VVQVSEKEFN FLDYLKRFAC
710 720 730 740 750
STVVRAYVLL LRSYQQNSAH TNHCIVKMLH RLAHDLKMEA LLFQLSVFCL
760 770 780 790 800
FNRLLSDPAA GAYKELVTFA KYILGKFFAL AAVNQKAFVE LLFWKNTAVV
810 820 830 840 850
REMTEGYGSL DDRSSSRRAP TWSPEEEAHL RELYLANKDV EGQDVVEAIL
860 870 880 890 900
AHLNTVPRTR KQIIHHLVQM GLADSVKDFQ RKGTHIVLWT GDQELELQRL
910 920 930 940 950
FEEFRDSDDV LGHIMKNITA KRSRARIVDK LLALGLVAER RELYKKRQKK
960 970 980 990 1000
LASSILPNGA ESLKDFCQED LEEEENLPEE DSEEEEEGGS EAEQVQGSLV
1010 1020 1030 1040 1050
LSNENLGQSL HQEGFSIPLL WLQNCLIRAA DDREEDGCSQ AVPLVPLTEE
1060 1070 1080 1090 1100
NEEAMENEQF QQLLRKLGVR PPASGQETFW RIPAKLSPTQ LRRAAASLSQ
1110 1120 1130 1140 1150
PEEEQKLQPE LQPKVPGEQG SDEEHCKEHR AQALRALLLA HKKKAGLASP
1160 1170 1180 1190 1200
EEEDAVGKEP LKAAPKKRQL LDSDEEQEED EGRNRAPELG APGIQKKKRY

QIEDDEDD
Length:1,208
Mass (Da):138,658
Last modified:May 18, 2010 - v2
Checksum:i16C6C07DDC6D2701
GO
Isoform 21 Publication (identifier: Q9UNS1-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     177-177: Missing.

Show »
Length:1,207
Mass (Da):138,530
Checksum:iC116D7FF6F29B326
GO

Sequence cautioni

The sequence AAH39842.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291A → S.1 Publication
Corresponds to variant rs72478986 [ dbSNP | Ensembl ].
VAR_047879
Natural varianti429 – 4291A → D in a breast cancer sample; somatic mutation. 1 Publication
VAR_036435
Natural varianti455 – 4551I → L.3 Publications
Corresponds to variant rs774027 [ dbSNP | Ensembl ].
VAR_021483
Natural varianti471 – 4711N → S.1 Publication
Corresponds to variant rs72478993 [ dbSNP | Ensembl ].
VAR_047880
Natural varianti831 – 8311R → Q.3 Publications
Corresponds to variant rs774047 [ dbSNP | Ensembl ].
VAR_021484
Natural varianti870 – 8701M → V.1 Publication
Corresponds to variant rs61733875 [ dbSNP | Ensembl ].
VAR_047881
Natural varianti922 – 9221R → H.1 Publication
Corresponds to variant rs72478999 [ dbSNP | Ensembl ].
VAR_047882
Natural varianti924 – 9241R → W.1 Publication
Corresponds to variant rs72479000 [ dbSNP | Ensembl ].
VAR_047883
Natural varianti1008 – 10081Q → E in a breast cancer sample; somatic mutation. 1 Publication
VAR_036436
Natural varianti1017 – 10171I → T.1 Publication
Corresponds to variant rs61376834 [ dbSNP | Ensembl ].
VAR_047884
Natural varianti1018 – 10181P → L.2 Publications
Corresponds to variant rs2291739 [ dbSNP | Ensembl ].
VAR_021485

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei177 – 1771Missing in isoform 2. 2 PublicationsVSP_051693

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015597 mRNA. Translation: BAA36499.1.
AF098162 mRNA. Translation: AAC80011.1.
EU627094 Genomic DNA. Translation: ACD11488.1.
AC024884 Genomic DNA. No translation available.
BC039842 mRNA. Translation: AAH39842.1. Sequence problems.
BC050557 mRNA. Translation: AAH50557.1.
CCDSiCCDS8918.1. [Q9UNS1-1]
RefSeqiNP_003911.2. NM_003920.3. [Q9UNS1-1]
UniGeneiHs.118631.

Genome annotation databases

EnsembliENST00000229201; ENSP00000229201; ENSG00000111602. [Q9UNS1-2]
ENST00000553532; ENSP00000450607; ENSG00000111602. [Q9UNS1-1]
GeneIDi8914.
KEGGihsa:8914.
UCSCiuc001slf.2. human. [Q9UNS1-1]

Polymorphism databases

DMDMi296452931.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB015597 mRNA. Translation: BAA36499.1 .
AF098162 mRNA. Translation: AAC80011.1 .
EU627094 Genomic DNA. Translation: ACD11488.1 .
AC024884 Genomic DNA. No translation available.
BC039842 mRNA. Translation: AAH39842.1 . Sequence problems.
BC050557 mRNA. Translation: AAH50557.1 .
CCDSi CCDS8918.1. [Q9UNS1-1 ]
RefSeqi NP_003911.2. NM_003920.3. [Q9UNS1-1 ]
UniGenei Hs.118631.

3D structure databases

ProteinModelPortali Q9UNS1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114428. 25 interactions.
IntActi Q9UNS1. 7 interactions.
STRINGi 9606.ENSP00000229201.

PTM databases

PhosphoSitei Q9UNS1.

Polymorphism databases

DMDMi 296452931.

Proteomic databases

MaxQBi Q9UNS1.
PaxDbi Q9UNS1.
PRIDEi Q9UNS1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229201 ; ENSP00000229201 ; ENSG00000111602 . [Q9UNS1-2 ]
ENST00000553532 ; ENSP00000450607 ; ENSG00000111602 . [Q9UNS1-1 ]
GeneIDi 8914.
KEGGi hsa:8914.
UCSCi uc001slf.2. human. [Q9UNS1-1 ]

Organism-specific databases

CTDi 8914.
GeneCardsi GC12M056810.
H-InvDB HIX0010725.
HGNCi HGNC:11813. TIMELESS.
HPAi HPA060655.
MIMi 603887. gene.
neXtProti NX_Q9UNS1.
PharmGKBi PA36520.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG328380.
GeneTreei ENSGT00390000015124.
HOGENOMi HOG000133002.
HOVERGENi HBG079258.
InParanoidi Q9UNS1.
KOi K03155.
OMAi RKGTQIV.
PhylomeDBi Q9UNS1.
TreeFami TF312802.

Miscellaneous databases

ChiTaRSi TIMELESS. human.
GenomeRNAii 8914.
NextBioi 33532.
PROi Q9UNS1.
SOURCEi Search...

Gene expression databases

Bgeei Q9UNS1.
CleanExi HS_TIMELESS.
Genevestigatori Q9UNS1.

Family and domain databases

InterProi IPR006906. Timeless.
IPR007725. TIMELESS_C.
[Graphical view ]
Pfami PF04821. TIMELESS. 1 hit.
PF05029. TIMELESS_C. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of the mammalian homologues of the Drosophila timeless gene, Timeless1."
    Koike N., Hida A., Numano R., Hirose M., Sakaki Y., Tei H.
    FEBS Lett. 441:427-431(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, VARIANT LEU-455.
    Tissue: BrainImported.
  2. "Mammalian circadian autoregulatory loop: a timeless ortholog and mPer1 interact and negatively regulate CLOCK-ARTNL/BMAL1-induced transcription."
    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.
    Neuron 21:1101-1113(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, TISSUE SPECIFICITY, VARIANTS LEU-455 AND GLN-831.
    Tissue: Placenta1 Publication.
  3. NIEHS SNPs program
    Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-129; LEU-455; SER-471; GLN-831; VAL-870; HIS-922; TRP-924; THR-1017 AND LEU-1018.
  4. "The finished DNA sequence of human chromosome 12."
    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.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS GLN-831 AND LEU-1018.
    Tissue: DuodenumImported and SkinImported.
  6. "Coupling of human circadian and cell cycles by the timeless protein."
    Uensal-Kacmaz K., Mullen T.E., Kaufmann W.K., Sancar A.
    Mol. Cell. Biol. 25:3109-3116(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ATR; ATRIP; CHEK1 AND CRY2, INDUCTION.
  7. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Tipin and Timeless form a mutually protective complex required for genotoxic stress resistance and checkpoint function."
    Chou D.M., Elledge S.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:18143-18147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIPIN.
  10. "Human Tim/Timeless-interacting protein, Tipin, is required for efficient progression of S phase and DNA replication checkpoint."
    Yoshizawa-Sugata N., Masai H.
    J. Biol. Chem. 282:2729-2740(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIPIN.
  11. "Mammalian TIMELESS and Tipin are evolutionarily conserved replication fork-associated factors."
    Gotter A.L., Suppa C., Emanuel B.S.
    J. Mol. Biol. 366:36-52(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CLSPN, FUNCTION.
  12. "The human Tim/Tipin complex coordinates an Intra-S checkpoint response to UV that slows replication fork displacement."
    Uensal-Kacmaz K., Chastain P.D., Qu P.-P., Minoo P., Cordeiro-Stone M., Sancar A., Kaufmann W.K.
    Mol. Cell. Biol. 27:3131-3142(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIPIN, FUNCTION.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149 AND SER-1173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  16. "The many facets of the Tim-Tipin protein families' roles in chromosome biology."
    McFarlane R.J., Mian S., Dalgaard J.Z.
    Cell Cycle 9:700-705(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    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.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149 AND SER-1173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Timeless makes some time for itself."
    Diaz-Martinez L.A., Clarke D.J.
    Cell Cycle 10:2254-2254(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1149 AND SER-1173, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Mammalian TIMELESS is involved in period determination and DNA damage-dependent phase advancing of the circadian clock."
    Engelen E., Janssens R.C., Yagita K., Smits V.A., van der Horst G.T., Tamanini F.
    PLoS ONE 8:E56623-E56623(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-429 AND GLU-1008.

Entry informationi

Entry nameiTIM_HUMAN
AccessioniPrimary (citable) accession number: Q9UNS1
Secondary accession number(s): B2ZAV0
, O94802, Q86VM1, Q8IWH3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 15, 2005
Last sequence update: May 18, 2010
Last modified: November 26, 2014
This is version 120 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3