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[1]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
DOI=10.1006/geno.1998.5675; PubMed=10198158 [NCBI, ExPASy, EBI, Israel, Japan]
Steeves T.D.L.,
King D.P.,
Zhao Y.,
Sangoram A.M.,
Du F.,
Bowcock A.M.,
Moore R.Y.,
Takahashi J.S.;
"Molecular cloning and characterization of the human CLOCK gene: expression in the suprachiasmatic nuclei.";
Genomics 57:189-200(1999).
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[2]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1093/dnares/4.2.141; PubMed=9205841 [NCBI, ExPASy, EBI, Israel, Japan]
Nagase T.,
Ishikawa K.,
Nakajima D.,
Ohira M.,
Seki N.,
Miyajima N.,
Tanaka A.,
Kotani H.,
Nomura N.,
Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
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[3]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[4]
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NUCLEOTIDE SEQUENCE [MRNA] OF 1-349.
TISSUE=Brain;
Ikeda M.,
Takehara N.,
Ebisawa T.,
Yamauchi T.,
Nomura M.;
"Molecular cloning of human Clock cDNA 5'-end.";
Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases.
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[5]
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MUTAGENESIS OF GLU-116; GLY-332; HIS-360; GLU-367; VAL-601 AND PRO-840.
DOI=10.1038/ng1745; PubMed=16474406 [NCBI, ExPASy, EBI, Israel, Japan]
Sato T.K.,
Yamada R.G.,
Ukai H.,
Baggs J.E.,
Miraglia L.J.,
Kobayashi T.J.,
Welsh D.K.,
Kay S.A.,
Ueda H.R.,
Hogenesch J.B.;
"Feedback repression is required for mammalian circadian clock function.";
Nat. Genet. 38:312-319(2006).
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- FUNCTION: ARNTL/2-CLOCK heterodimers activate E-box element (3'-CACGTG-5') transcription of a number of proteins of the circadian clock. Activates transcription of PER1 and PER2. This transcription is inhibited in a feedback loop by PER and CRY proteins. Has intrinsic histone acetyltransferase activity and this enzymatic function contributes to chromatin-remodeling events implicated in circadian control of gene expression (By similarity). Acetylates primarily histones H3 and H4 (By similarity). Acetylates also a non-histone substrate: ARNTL (By similarity).
- CATALYTIC ACTIVITY: Acetyl-CoA + histone = CoA + acetylhistone.
- SUBUNIT: Component of the circadian clock oscillator which includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1D and/or CSNK1E, TIMELESS and the PER proteins. Efficient DNA binding requires dimerization with another bHLH protein. Heterodimerization with ARNTL is required for E-box-dependent transactivation, for CLOCK nuclear translocation and degradation, and, for phosphorylation of both CLOCK and ARNTL. Interaction with PER and CRY proteins requires translocation to the nucleus. Interaction of the CLOCK-ARNTL heterodimer with PER or CRY inhibits transcription activation. Binds weakly ARNTL and ARNTL2 to form heterodimers which bind poorly to the E-box motif (By similarity).
- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By similarity). Note=Shuffling between the cytoplasm and the nucleus is under circadian regulation and is ARNTL-dependent. Phosphorylated form located in the nucleus (By similarity).
- TISSUE SPECIFICITY: Expressed in all tissues examined including spleen, thymus, prostate, testis, ovary, small intestine, colon, leukocytes, heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Highest levels in testis and skeletal muscle. Low levels in thymus, lung and liver. Expressed in all brain regions with highest levels in cerebellum. Highly expressed in the suprachiasmatic nucleus (SCN).
- PTM: Phosphorylation is dependent on CLOCK-ARNTL heterodimer formation (By similarity).
- MISCELLANEOUS: CLOCK-ARNTL double mutations within the PAS domains result in syngernistic desensitization to high levels of CRY on repression of CLOCK-ARNTL transcriptional activity of PER1 and, disrupt circadian rhythmicity.
- SIMILARITY: Contains 1 basic helix-loop-helix (bHLH) domain.
- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 846 AA [This is the length of the unprocessed precursor] |
Molecular weight: 95304 Da [This is the MW of the unprocessed precursor] |
CRC64: C292B451A33E4CBF [This is a checksum on the sequence] |
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10 20 30 40 50 60
MLFTVSCSKM SSIVDRDDSS IFDGLVEEDD KDKAKRVSRN KSEKKRRDQF NVLIKELGSM
70 80 90 100 110 120
LPGNARKMDK STVLQKSIDF LRKHKEITAQ SDASEIRQDW KPTFLSNEEF TQLMLEALDG
130 140 150 160 170 180
FFLAIMTDGS IIYVSESVTS LLEHLPSDLV DQSIFNFIPE GEHSEVYKIL STHLLESDSL
190 200 210 220 230 240
TPEYLKSKNQ LEFCCHMLRG TIDPKEPSTY EYVKFIGNFK SLNSVSSSAH NGFEGTIQRT
250 260 270 280 290 300
HRPSYEDRVC FVATVRLATP QFIKEMCTVE EPNEEFTSRH SLEWKFLFLD HRAPPIIGYL
310 320 330 340 350 360
PFEVLGTSGY DYYHVDDLEN LAKCHEHLMQ YGKGKSCYYR FLTKGQQWIW LQTHYYITYH
370 380 390 400 410 420
QWNSRPEFIV CTHTVVSYAE VRAERRRELG IEESLPETAA DKSQDSGSDN RINTVSLKEA
430 440 450 460 470 480
LERFDHSPTP SASSRSSRKS SHTAVSDPSS TPTKIPTDTS TPPRQHLPAH EKMVQRRSSF
490 500 510 520 530 540
SSQSINSQSV GSSLTQPVMS QATNLPIPQG MSQFQFSAQL GAMQHLKDQL EQRTRMIEAN
550 560 570 580 590 600
IHRQQEELRK IQEQLQMVHG QGLQMFLQQS NPGLNFGSVQ LSSGNSSNIQ QLAPINMQGQ
610 620 630 640 650 660
VVPTNQIQSG MNTGHIGTTQ HMIQQQTLQS TSTQSQQNVL SGHSQQTSLP SQTQSTLTAP
670 680 690 700 710 720
LYNTMVISQP AAGSMVQIPS SMPQNSTQSA AVTTFTQDRQ IRFSQGQQLV TKLVTAPVAC
730 740 750 760 770 780
GAVMVPSTML MGQVVTAYPT FATQQQQSQT LSVTQQQQQQ SSQEQQLTSV QQPSQAQLTQ
790 800 810 820 830 840
PPQQFLQTSR LLHGNPSTQL ILSAAFPLQQ STFPQSHHQQ HQSQQQQQLS RHRTDSLPDP
SKVQPQ
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O15516 in FASTA format |
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ExPASy Home page
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