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O35973 (PER1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Period circadian protein homolog 1

Short name=mPER1
Alternative name(s):
Circadian clock protein PERIOD 1
Circadian pacemaker protein Rigui
Gene names
Name:Per1
Synonyms:Per, Rigui
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1291 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1, NR1D2, RORA, RORB and RORG, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. Regulates circadian target genes expression at post-transcriptional levels, but may not be required for the repression at transcriptional level. Controls PER2 protein decay. Represses CRY2 preventing its repression on CLOCK/ARNTL target genes such as FXYD5 and SCNN1A in kidney and PPARA in liver. Besides its involvement in the maintenance of the circadian clock, has an important function in the regulation of several processes. Participates in the repression of glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) by ARNTL:CLOCK. Plays a role in the modulation of the neuroinflammatory state via the regulation of inflammatory mediators release, such as CCL2 and IL6. In spinal astrocytes, negatively regulates the MAPK14/p38 and MAPK8/JNK MAPK cascades as well as the subsequent activation of NFkappaB. Coordinately regulates the expression of multiple genes that are involved in the regulation of renal sodium reabsorption. Can act as gene expression activator in a gene and tissue specific manner, in kidney enhances WNK1 and SLC12A3 expression in collaboration with CLOCK. Modulates hair follicle cycling. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1. Ref.6 Ref.13 Ref.16 Ref.19 Ref.24 Ref.25 Ref.28 Ref.29 Ref.31

Subunit structure

Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/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. Interacts with ARNTL and clock. Interacts with GPRASP1. Interacts (phosphorylated) with BTRC and FBXW11; the interactions trigger proteasomal degradation. Interacts with NONO and WDR5. Ref.6 Ref.8 Ref.9 Ref.10 Ref.14 Ref.18 Ref.20 Ref.25 Ref.31

Subcellular location

Nucleus. Cytoplasm. Note: 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. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.20 Ref.22 Ref.23 Ref.24 Ref.28

Tissue specificity

In brain, highest expression is observed in the SCN. Highly expressed in the pyramidal cell layer of the piriform cortex, the periventricular part of the caudate-putamen, many thalamic nuclei, and the granular layer of the cerebellar cortex. Weaker expression is detected in most area of the brain, including cortical and non cortical structures. Expression but no oscillations occurs in the glomerular and mitral cell layers of the olfactory bulb, the internal granular layer of the cerebellum, the cornu ammonis and dentate gyrus of the hyppocampus, the cerebral and piriform cortices. Expressed in the renal cortex (at protein level). Also found in heart, brain, bladder, lumbar spinal cord, spleen, lung, liver, skeletal muscle and testis. Ref.2 Ref.5 Ref.7 Ref.21 Ref.25 Ref.27 Ref.28

Developmental stage

Expressed in the suprachiasmatic nucleus (SCN) during late fetal and early neonatal life.

Induction

In the suprachiasmatic nucleus (SCN), behaves like a day-type oscillator, with maximum expression during the light period. Oscillations are maintained under constant darkness and are responsive to changes of the light/dark cycles. There is a 4 hour time delay between PER1 and PER2 oscillations. The expression rhythms appear to originate from retina. In liver, peak levels at CT9. In the SCN, levels increase by light exposure during subjective night. Circadian oscillations also observed in skeletal muscle, bladder, lumbar spinal cord and liver but not in testis. Ref.1 Ref.2 Ref.5 Ref.7 Ref.11 Ref.21 Ref.27

Post-translational modification

Phosphorylated on serine residues by CSNK1D, CSNK1E and probably also by CSNK1G2. Phosphorylation by CSNK1D or CSNK1E promotes nuclear location of PER proteins as well as ubiquitination and subsequent degradation. May be dephosphorylated by PP1. Ref.10 Ref.11 Ref.15 Ref.17 Ref.18 Ref.22 Ref.23 Ref.24

Ubiquitinated; requires phosphorylation by CSNK1E and interaction with BTRC and FBXW11. Ref.15

Disruption phenotype

Animals show disrupted circadian behavior. The prolongation of light exposure produces larger phase delay of behavioral rhythm compared to wild-types. Double knocknouts for PER2 and PER1 show an abrupt loss of rhythmicity immediately upon transfer to exprosure to constant darkness. Animals have largely affected the water intake (polydipsia) and urine volume (polyuria). Ref.13 Ref.19 Ref.27

Sequence similarities

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   DomainRepeat
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcircadian regulation of gene expression

Inferred from direct assay PubMed 20159955. Source: UniProtKB

circadian regulation of translation

Inferred from mutant phenotype Ref.13. Source: UniProtKB

circadian rhythm

Inferred from expression pattern PubMed 14645221PubMed 23785138. Source: UniProtKB

entrainment of circadian clock by photoperiod

Inferred from mutant phenotype Ref.19. Source: UniProtKB

histone H3 acetylation

Inferred from direct assay PubMed 14645221. Source: UniProtKB

histone H3 deacetylation

Inferred from mutant phenotype PubMed 21680841. Source: UniProtKB

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of JNK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glucocorticoid receptor signaling pathway

Inferred from mutant phenotype Ref.29. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.28. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12397359PubMed 18316400Ref.6. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.28. Source: UniProtKB

posttranscriptional regulation of gene expression

Inferred from mutant phenotype Ref.19. Source: UniProtKB

regulation of circadian rhythm

Inferred from mutant phenotype Ref.13. Source: UniProtKB

regulation of cytokine production involved in inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of hair cycle

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of p38MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of sodium ion transport

Inferred from mutant phenotype Ref.28. Source: UniProtKB

response to light stimulus

Inferred from expression pattern PubMed 15038852. Source: BHF-UCL

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.25. Source: UniProtKB

   Molecular_functionE-box binding

Inferred from electronic annotation. Source: Ensembl

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

chromatin DNA binding

Inferred from direct assay Ref.28. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.9Ref.18Ref.22PubMed 21680841Ref.25Ref.6. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

transcription factor binding

Inferred from physical interaction Ref.25. Source: UniProtKB

transcription factor binding transcription factor activity

Inferred from direct assay PubMed 15147242. Source: BHF-UCL

transcription regulatory region sequence-specific DNA binding

Inferred from direct assay PubMed 24413057. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TimelessQ9R1X43EBI-1266764,EBI-1793117

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12911291Period circadian protein homolog 1
PRO_0000162628

Regions

Domain208 – 27568PAS 1
Domain348 – 41467PAS 2
Domain422 – 46544PAC
Region1 – 151151Interaction with BTRC By similarity
Region596 – 815220Required for phosphorylation by CSNK1E
Region1148 – 1291144CRY binding domain
Motif138 – 14710Nuclear export signal 1 By similarity
Motif489 – 49810Nuclear export signal 3
Motif824 – 84017Nuclear localization signal Ref.10
Motif981 – 9888Nuclear export signal 2 By similarity
Motif1042 – 10465LXXLL
Compositional bias49 – 12981Ser-rich
Compositional bias653 – 6564Poly-Ser
Compositional bias841 – 8444Poly-His
Compositional bias847 – 971125Pro-rich
Compositional bias1029 – 110375Ser-rich
Compositional bias1224 – 127754Gly-rich
Compositional bias1270 – 12734Poly-Glu

Amino acid modifications

Modified residue1211Phosphothreonine; by CSNK1E Potential
Modified residue1221Phosphoserine; by CSNK1E Potential
Modified residue1261Phosphoserine; by CSNK1E Potential
Modified residue6611Phosphoserine Ref.17
Modified residue6631Phosphoserine Ref.17
Modified residue7041Phosphoserine By similarity
Modified residue8151Phosphoserine By similarity
Modified residue9781Phosphoserine By similarity
Modified residue9791Phosphoserine By similarity

Experimental info

Mutagenesis2671Y → E: No effect on homodimerization. Abolishes homodimerization; when associated with E-444. Ref.31
Mutagenesis4441F → E: Reduces homodimerization. Abolishes homodimerization; when associated with E-267. Ref.31
Mutagenesis4481W → E: Abolishes homodimerization. Ref.31
Mutagenesis6611S → A: Reduced phosphorylation. No nuclear entry of PER1, CRY1 nor CKSN1E; when associated with A-663.
Mutagenesis6631S → A: Reduced phosphorylation. No nuclear entry PER1, CRY1 nor CKSN1E; when associated with A-661.
Mutagenesis831 – 8333HCR → ACA: No effect on nuclear import.
Mutagenesis835 – 8384KAKR → AAKA: Abolishes nuclear accumulation. Ref.10
Mutagenesis902 – 91514TSVSP…SPLVT → AAVAPAAFPAPLVA: No effect on nuclear import.
Sequence conflict11991T → M in AAC53355. Ref.1
Sequence conflict11991T → M in BAA22634. Ref.2
Sequence conflict11991T → M in BAA94086. Ref.3

Secondary structure

........................................................... 1291
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O35973 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 77FB9BC71EDF31A6

FASTA1,291136,373
        10         20         30         40         50         60 
MSGPLEGADG GGDPRPGEPF CPGGVPSPGA PQHRPCPGPS LADDTDANSN GSSGNESNGP 

        70         80         90        100        110        120 
ESRGASQRSS HSSSSGNGKD SALLETTESS KSTNSQSPSP PSSSIAYSLL SASSEQDNPS 

       130        140        150        160        170        180 
TSGCSSEQSA RARTQKELMT ALRELKLRLP PERRGKGRSG TLATLQYALA CVKQVQANQE 

       190        200        210        220        230        240 
YYQQWSLEEG EPCAMDMSTY TLEELEHITS EYTLRNQDTF SVAVSFLTGR IVYISEQAGV 

       250        260        270        280        290        300 
LLRCKRDVFR GARFSELLAP QDVGVFYGST TPSRLPTWGT GTSAGSGLKD FTQEKSVFCR 

       310        320        330        340        350        360 
IRGGPDRDPG PRYQPFRLTP YVTKIRVSDG APAQPCCLLI AERIHSGYEA PRIPPDKRIF 

       370        380        390        400        410        420 
TTRHTPSCLF QDVDERAAPL LGYLPQDLLG APVLLFLHPE DRPLMLAIHK KILQLAGQPF 

       430        440        450        460        470        480 
DHSPIRFCAR NGEYVTMDTS WAGFVHPWSR KVAFVLGRHK VRTAPLNEDV FTPPAPSPAP 

       490        500        510        520        530        540 
SLDSDIQELS EQIHRLLLQP VHSSSPTGLC GVGPLMSPGP LHSPGSSSDS NGGDAEGPGP 

       550        560        570        580        590        600 
PAPVTFQQIC KDVHLVKHQG QQLFIESRAK PPPRPRLLAT GTFKAKVLPC QSPNPELEVA 

       610        620        630        640        650        660 
PVPDQASLAL APEEPERKET SGCSYQQINC LDSILRYLES CNIPSTTKRK CASSSSYTAS 

       670        680        690        700        710        720 
SASDDDKQRA GPVPVGAKKD PSSAMLSGEG ATPRKEPVVG GTLSPLALAN KAESVVSVTS 

       730        740        750        760        770        780 
QCSFSSTIVH VGDKKPPESD IIMMEDLPGL APGPAPSPAP SPTVAPDPTP DAYRPVGLTK 

       790        800        810        820        830        840 
AVLSLHTQKE EQAFLNRFRD LGRLRGLDTS SVAPSAPGCH HGPIPPGRRH HCRSKAKRSR 

       850        860        870        880        890        900 
HHHHQTPRPE TPCYVSHPSP VPSSGPWPPP PATTPFPAMV QPYPLPVFSP RGGPQPLPPA 

       910        920        930        940        950        960 
PTSVSPATFP SPLVTPMVAL VLPNYLFPTP PSYPYGVSQA PVEGPPTPAS HSPSPSLPPP 

       970        980        990       1000       1010       1020 
PLSPPHRPDS PLFNSRCSSP LQLNLLQLEE SPRTEGGAAA GGPGSSAGPL PPSEETAEPE 

      1030       1040       1050       1060       1070       1080 
ARLVEVTESS NQDALSGSSD LLELLLQEDS RSGTGSAASG SLGSGLGSGS GSGSHEGGST 

      1090       1100       1110       1120       1130       1140 
SASITRSSQS SHTSKYFGSI DSSEAEAGAA RARTEPGDQV IKCVLQDPIW LLMANADQRV 

      1150       1160       1170       1180       1190       1200 
MMTYQVPSRD AASVLKQDRE RLRAMQKQQP RFSEDQRREL GAVHSWVRKG QLPRALDVTA 

      1210       1220       1230       1240       1250       1260 
CVDCGSSVQD PGHSDDPLFS ELDGLGLEPM EEGGGEGGGC GVGGGGGDGG EEAQTQIGAK 

      1270       1280       1290 
GSSSQDSAME EEEQGGGSSS PALPAEENST S 

« Hide

References

« Hide 'large scale' references
[1]"Rigui, a putative mammalian ortholog of the Drosophila period gene."
Sun Z.S., Albrecht U., Zhuchenko O., Bailey J., Eichele G., Lee C.C.
Cell 90:1003-1011(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Tissue: Brain.
[2]"Circadian oscillation of a mammalian homologue of the Drosophila period gene."
Tei H., Okamura H., Shigeyoshi Y., Fukuhara C., Ozawa R., Hirose M., Sakaki Y.
Nature 389:512-516(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
Strain: BALB/c.
Tissue: Brain.
[3]"The human and mouse Period1 genes: five well-conserved E-boxes additively contribute to the enhancement of mPer1 transcription."
Hida A., Koike N., Hirose M., Hattori M., Sakaki Y., Tei H.
Genomics 65:224-233(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[5]"Two period homologs: circadian expression and photic regulation in the suprachiasmatic nuclei."
Shearman L.P., Zylka M.J., Weaver D.R., Kolakowski L.F. Jr., Reppert S.M.
Neuron 19:1261-1269(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[6]"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: FUNCTION, INTERACTION WITH TIMELESS.
[7]"Circadian regulation of cryptochrome genes in the mouse."
Miyamoto Y., Sancar A.
Brain Res. Mol. Brain Res. 71:238-243(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[8]"mCRY1 and mCRY2 are essential components of the negative limb of the circadian clock feedback loop."
Kume K., Zylka M.J., Sriram S., Shearman L.P., Weaver D.R., Jin X., Maywood E.S., Hastings M.H., Reppert S.M.
Cell 98:193-205(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PER3; CRY1 AND CRY2, SUBCELLULAR LOCATION.
[9]"A mammalian ortholog of Drosophila timeless, highly expressed in SCN and retina, forms a complex with mPER1."
Takumi T., Nagamine Y., Miyake S., Matsubara C., Taguchi K., Takekida S., Sakakida Y., Nishikawa K., Kishimoto T., Niwa S., Okumura K., Okamura H.
Genes Cells 4:67-75(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TIMELESS, SUBCELLULAR LOCATION.
[10]"Nuclear entry of the circadian regulator mPER1 is controlled by mammalian casein kinase I epsilon."
Vielhaber E., Eide E., Rivers A., Gao Z.-H., Virshup D.M.
Mol. Cell. Biol. 20:4888-4899(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PER2, PHOSPHORYLATION BY CKSN1E, NUCLEAR LOCALIZATION SIGNAL, SUBCELLULAR LOCATION, MUTAGENESIS OF 831-HIS--ARG-833; 835-LYS--ARG-838 AND 902-THR--THR-914.
[11]"Posttranslational mechanisms regulate the mammalian circadian clock."
Lee C., Etchegaray J.-P., Cagampang F.R.A., Loudon A.S.I., Reppert S.M.
Cell 107:855-867(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, SUBCELLULAR LOCATION, INDUCTION.
[12]"Nuclear export of mammalian PERIOD proteins."
Vielhaber E.L., Duricka D., Ullman K.S., Virshup D.M.
J. Biol. Chem. 276:45921-45927(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL.
[13]"Differential functions of mPer1, mPer2, and mPer3 in the SCN circadian clock."
Bae K., Jin X., Maywood E.S., Hastings M.H., Reppert S.M., Weaver D.R.
Neuron 30:525-536(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION REPRESSOR OF TRANSLATION, DISRUPTION PHENOTYPE.
[14]"The circadian regulatory proteins BMAL1 and cryptochromes are substrates of casein kinase Iepsilon."
Eide E.J., Vielhaber E.L., Hinz W.A., Virshup D.M.
J. Biol. Chem. 277:17248-17254(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRY1 AND CRY2, SUBCELLULAR LOCATION.
[15]"Control of intracellular dynamics of mammalian period proteins by casein kinase I epsilon (CKIepsilon) and CKIdelta in cultured cells."
Akashi M., Tsuchiya Y., Yoshino T., Nishida E.
Mol. Cell. Biol. 22:1693-1703(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION BY CSNK1D AND CKSN1E, UBIQUITINATION.
[16]"A novel autofeedback loop of Dec1 transcription involved in circadian rhythm regulation."
Kawamoto T., Noshiro M., Sato F., Maemura K., Takeda N., Nagai R., Iwata T., Fujimoto K., Furukawa M., Miyazaki K., Honma S., Honma K.I., Kato Y.
Biochem. Biophys. Res. Commun. 313:117-124(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Identification of mPer1 phosphorylation sites responsible for the nuclear entry."
Takano A., Isojima Y., Nagai K.
J. Biol. Chem. 279:32578-32585(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-661 AND SER-663, SUBCELLULAR LOCATION, MUTAGENESIS OF 661-SER--SER-663.
[18]"Direct association between mouse PERIOD and CKIepsilon is critical for a functioning circadian clock."
Lee C., Weaver D.R., Reppert S.M.
Mol. Cell. Biol. 24:584-594(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PER2; PER3; CRY1 AND CRY2, PHOSPHORYLATION BY CSNK1E.
[19]"Mouse Period1 (mPER1) acts as a circadian adaptor to entrain the oscillator to environmental light/dark cycles by regulating mPER2 protein."
Masubuchi S., Kataoka N., Sassone-Corsi P., Okamura H.
J. Neurosci. 25:4719-4724(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PER2 REGULATOR, DISRUPTION PHENOTYPE.
[20]"Functional evolution of the photolyase/cryptochrome protein family: importance of the C terminus of mammalian CRY1 for circadian core oscillator performance."
Chaves I., Yagita K., Barnhoorn S., Okamura H., van der Horst G.T.J., Tamanini F.
Mol. Cell. Biol. 26:1743-1753(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CRY1 AND CRY2, SUBCELLULAR LOCATION.
[21]"Posttranslational regulation of the mammalian circadian clock by cryptochrome and protein phosphatase 5."
Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.
Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY, INDUCTION.
[22]"Casein kinase 1 delta regulates the pace of the mammalian circadian clock."
Etchegaray J.P., Machida K.K., Noton E., Constance C.M., Dallmann R., Di Napoli M.N., DeBruyne J.P., Lambert C.M., Yu E.A., Reppert S.M., Weaver D.R.
Mol. Cell. Biol. 29:3853-3866(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION BY CSNK1D AND CSNK1E.
[23]"Protein phosphatase 1 (PP1) is a post-translational regulator of the mammalian circadian clock."
Schmutz I., Wendt S., Schnell A., Kramer A., Mansuy I.M., Albrecht U.
PLoS ONE 6:E21325-E21325(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, DEPHOSPHORYLATION.
[24]"The period of the circadian oscillator is primarily determined by the balance between casein kinase 1 and protein phosphatase 1."
Lee H.M., Chen R., Kim H., Etchegaray J.P., Weaver D.R., Lee C.
Proc. Natl. Acad. Sci. U.S.A. 108:16451-16456(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CIRCADIAN CLOCK, PHOSPHORYLATION BY CSNK1D AND CKSN1E, SUBCELLULAR LOCATION.
[25]"A role for the circadian clock protein Per1 in the regulation of aldosterone levels and renal Na+ retention."
Richards J., Cheng K.Y., All S., Skopis G., Jeffers L., Lynch I.J., Wingo C.S., Gumz M.L.
Am. J. Physiol. 305:F1697-F1704(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION CRY2 REPRESSOR, INTERACTION WITH CRY2; CLOCK AND ARNTL, TISSUE SPECIFICITY.
[26]"Metabolism and the circadian clock converge."
Eckel-Mahan K., Sassone-Corsi P.
Physiol. Rev. 93:107-135(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[27]"Presence of multiple peripheral circadian oscillators in the tissues controlling voiding function in mice."
Noh J.Y., Han D.H., Kim M.H., Ko I.G., Kim S.E., Park N., Kyoung Choe H., Kim K.H., Kim K., Kim C.J., Cho S.
Exp. Mol. Med. 46:E81-E81(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION, TISSUE SPECIFICITY, DISRUPTION PHENOTYPE.
[28]"A Role for the circadian clock protein Per1 in the regulation of the NaCl Co-transporter (NCC) and the with-no-lysine kinase (WNK) cascade in mouse distal convoluted tubule cells."
Richards J., Ko B., All S., Cheng K.Y., Hoover R.S., Gumz M.L.
J. Biol. Chem. 289:11791-11806(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS TRANSCRIPTIONAL ACTIVATOR, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
[29]"Modulation of glucocorticoid receptor induction properties by core circadian clock proteins."
Han D.H., Lee Y.J., Kim K., Kim C.J., Cho S.
Mol. Cell. Endocrinol. 383:170-180(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN GR REPRESSION.
[30]"Molecular architecture of the mammalian circadian clock."
Partch C.L., Green C.B., Takahashi J.S.
Trends Cell Biol. 24:90-99(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[31]"Unwinding the differences of the mammalian PERIOD clock proteins from crystal structure to cellular function."
Kucera N., Schmalen I., Hennig S., Ollinger R., Strauss H.M., Grudziecki A., Wieczorek C., Kramer A., Wolf E.
Proc. Natl. Acad. Sci. U.S.A. 109:3311-3316(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.75 ANGSTROMS) OF 191-502, MUTAGENESIS OF TYR-267; PHE-444 AND TRP-448, FUNCTION IN HEME BINDING, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF022992 mRNA. Translation: AAC53355.1.
AB002108 mRNA. Translation: BAA22634.1.
AB030818 Genomic DNA. Translation: BAA94086.1.
AL645527 Genomic DNA. Translation: CAI35245.1.
CCDSCCDS24882.1.
PIRT00019.
RefSeqNP_001152839.1. NM_001159367.1.
NP_035195.2. NM_011065.4.
XP_006532543.1. XM_006532480.1.
UniGeneMm.7373.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4DJ2X-ray2.75A/B/C/D191-502[»]
ProteinModelPortalO35973.
SMRO35973. Positions 196-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202111. 24 interactions.
DIPDIP-38519N.
IntActO35973. 8 interactions.

PTM databases

PhosphoSiteO35973.

Proteomic databases

PaxDbO35973.
PRIDEO35973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000021271; ENSMUSP00000021271; ENSMUSG00000020893.
ENSMUST00000166748; ENSMUSP00000132635; ENSMUSG00000020893.
GeneID18626.
KEGGmmu:18626.
UCSCuc007jpg.2. mouse.

Organism-specific databases

CTD5187.
MGIMGI:1098283. Per1.

Phylogenomic databases

eggNOGNOG253593.
GeneTreeENSGT00510000046467.
HOVERGENHBG008167.
InParanoidB1ASX0.
KOK02633.
OMAELGAVHS.
TreeFamTF318445.

Enzyme and pathway databases

ReactomeREACT_109335. Circadian Clock.
REACT_24972. Circadian Clock.

Gene expression databases

ArrayExpressO35973.
BgeeO35973.
CleanExMM_PER1.
GenevestigatorO35973.

Family and domain databases

InterProIPR001610. PAC.
IPR000014. PAS.
IPR022728. Period_circadian-like_C.
[Graphical view]
PfamPF12114. Period_C. 1 hit.
[Graphical view]
SMARTSM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF55785. SSF55785. 1 hit.
PROSITEPS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio294576.
PROO35973.
SOURCESearch...

Entry information

Entry namePER1_MOUSE
AccessionPrimary (citable) accession number: O35973
Secondary accession number(s): B1ASX0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot