[1]
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NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
TISSUE=Heart;
DOI=10.1016/S0092-8674(00)80366-9; PubMed=9323128 [NCBI, ExPASy, EBI, Israel, Japan]
Sun Z.S.,
Albrecht U.,
Zhuchenko O.,
Bailey J.,
Eichele G.,
Lee C.C.;
"Rigui, a putative mammalian ortholog of the Drosophila period gene.";
Cell 90:1003-1011(1997).
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[2]
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NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
DOI=10.1038/39086; PubMed=9333243 [NCBI, ExPASy, EBI, Israel, Japan]
Tei H.,
Okamura H.,
Shigeyoshi Y.,
Fukuhara C.,
Ozawa R.,
Hirose M.,
Sakaki Y.;
"Circadian oscillation of a mammalian homologue of the Drosophila period gene.";
Nature 389:512-516(1997).
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[3]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0378-1119(00)00248-1; PubMed=10940553 [NCBI, ExPASy, EBI, Israel, Japan]
Taruscio D.,
Zoraqi G.K.,
Falchi M.,
Iosi F.,
Paradisi S.,
Di Fiore B.,
Lavia P.,
Falbo V.;
"The human Per1 gene: genomic organization and promoter analysis of the first human orthologue of the Drosophila period gene.";
Gene 253:161-170(2000).
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[4]
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NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1006/geno.2000.6166; PubMed=10857746 [NCBI, ExPASy, EBI, Israel, Japan]
Hida A.,
Koike N.,
Hirose M.,
Hattori M.,
Sakaki Y.,
Tei H.;
"The human and mouse Period1 genes: five well-conserved E-boxes additively contribute to the enhancement of mPer1 transcription.";
Genomics 65:224-233(2000).
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[5]
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NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1093/dnares/4.5.345; PubMed=9455484 [NCBI, ExPASy, EBI, Israel, Japan]
Seki N.,
Ohira M.,
Nagase T.,
Ishikawa K.,
Miyajima N.,
Nakajima D.,
Nomura N.,
Ohara O.;
"Characterization of cDNA clones in size-fractionated cDNA libraries from human brain.";
DNA Res. 4:345-349(1997).
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[6]
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SEQUENCE REVISION.
Nagase T.,
Kikuno R.,
Ohara O.;
Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
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[7]
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TISSUE SPECIFICITY.
DOI=10.1016/S0896-6273(00)80417-1; PubMed=9427249 [NCBI, ExPASy, EBI, Israel, Japan]
Shearman L.P.,
Zylka M.J.,
Weaver D.R.,
Kolakowski L.F. Jr.,
Reppert S.M.;
"Two period homologs: circadian expression and photic regulation in the suprachiasmatic nuclei.";
Neuron 19:1261-1269(1997).
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[8]
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PHOSPHORYLATION, AND INTERACTION WITH CSNK1E.
PubMed=10790862 [NCBI, ExPASy, EBI, Israel, Japan]
Keesler G.A.,
Camacho F.,
Guo Y.,
Virshup D.,
Mondadori C.,
Yao Z.;
"Phosphorylation and destabilization of human period I clock protein by human casein kinase I epsilon.";
NeuroReport 11:951-955(2000).
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[9]
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PHOSPHORYLATION, AND INTERACTION WITH CSNK1D.
DOI=10.1016/S0014-5793(00)02434-0; PubMed=11165242 [NCBI, ExPASy, EBI, Israel, Japan]
Camacho F.,
Cilio M.,
Guo Y.,
Virshup D.M.,
Patel K.,
Khorkova O.,
Styren S.,
Morse B.,
Yao Z.,
Keesler G.A.;
"Human casein kinase Idelta phosphorylation of human circadian clock proteins period 1 and 2.";
FEBS Lett. 489:159-165(2001).
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[10]
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PHOSPHORYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION.
DOI=10.1042/BJ20031308; PubMed=14750904 [NCBI, ExPASy, EBI, Israel, Japan]
Miyazaki K.,
Nagase T.,
Mesaki M.,
Narukawa J.,
Ohara O.,
Ishida N.;
"Phosphorylation of clock protein PER1 regulates its circadian degradation in normal human fibroblasts.";
Biochem. J. 380:95-103(2004).
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[11]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979; SER-980; SER-1100; SER-1103 AND SER-1104, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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[12]
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PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1262 AND SER-1263, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
Matsuoka S.,
Ballif B.A.,
Smogorzewska A.,
McDonald E.R. III,
Hurov K.E.,
Luo J.,
Bakalarski C.E.,
Zhao Z.,
Solimini N.,
Lerenthal Y.,
Shiloh Y.,
Gygi S.P.,
Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
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[13]
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VARIANTS [LARGE SCALE ANALYSIS] GLN-696; SER-985 AND LEU-1060.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
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).
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- FUNCTION: Component of the circadian clock mechanism which is essential for generating circadian rhythms. Negative element in the circadian transcriptional loop. Influences clock function by interacting with other circadian regulatory proteins and transporting them to the nucleus. Negatively regulates CLOCK|NPAS2-BMAL1|BMAL2-induced transactivation (By similarity).
- SUBUNIT: Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, BMAL1 or BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts directly with TIMELESS, PER2, PER3 and, through a C-terminal domain, with CRY1 and CRY2. Interaction with CSNK1D or CSNK1E promotes nuclear location of PER proteins. Interacts with GPRASP1 (By similarity).
- SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By similarity). Note=Mainly nuclear. Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Retention of PER1 in the cytoplasm occurs through PER1-PER2 heterodimer formation or by interaction with CSNK1E and/or phosphorylation which appears to mask the PER1 nuclear localization signal. Also translocated to the nucleus by CRY1 or CRY2 (By similarity).
- ALTERNATIVE PRODUCTS:
3 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.
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| Name | Rigui 3.0 |
| Isoform ID | O15534-2 |
| The sequence of this isoform is not described. |
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| Name | Rigui 6.6 |
| Synonyms | Truncated |
| Isoform ID | O15534-3 |
| The sequence of this isoform is not described. |
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- TISSUE SPECIFICITY: Widely expressed. Found in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, kidney, spleen, thymus, prostate, testis, ovary and small intestine. Highest level in skeletal muscle. Low level in kidney.
- INDUCTION: Serum-induced levels in fibroblasts show circadian oscillations. Maximum levels after 1 hour stimulation, minimum levels after 12 hours. Another peak is then observed after 20 hours. Protein levels show maximum levels at 6 hours, decrease to reach minimum levels at 20 hours, and increase again to reach a second peak after 26 hours. Levels then decrease slightly and then increase to maximum levels at 32 hours. Levels of phosphorylated form increase between 3 hours and 12 hours.
- PTM: Phosphorylated on serine residues by CSNK1E. Also can be phosphorylated by the delta isoform. Phosphorylation by CSNK1 retains PER1 in the cytoplasm and leads to its ubiquitination and subsequent degradation. Phosphorylated upon DNA damage, probably by ATM or ATR.
- PTM: Ubiquitinated (By similarity).
- SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
- SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains.
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