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Protein

Period circadian protein homolog 1

Gene

Per1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 NR1D1/2 and RORA/B/G, 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/DEC1.9 Publications

GO - Molecular functioni

  • chromatin DNA binding Source: UniProtKB
  • E-box binding Source: MGI
  • kinase binding Source: UniProtKB
  • RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: MGI
  • transcription factor activity, transcription factor binding Source: BHF-UCL
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region sequence-specific DNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI

GO - Biological processi

  • circadian regulation of gene expression Source: UniProtKB
  • circadian regulation of translation Source: UniProtKB
  • circadian rhythm Source: UniProtKB
  • entrainment of circadian clock by photoperiod Source: UniProtKB
  • histone H3 acetylation Source: UniProtKB
  • histone H3 deacetylation Source: UniProtKB
  • histone H4 acetylation Source: MGI
  • negative regulation of glucocorticoid receptor signaling pathway Source: UniProtKB
  • negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  • negative regulation of JNK cascade Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • posttranscriptional regulation of gene expression Source: UniProtKB
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of cytokine production involved in inflammatory response Source: UniProtKB
  • regulation of hair cycle Source: UniProtKB
  • regulation of p38MAPK cascade Source: UniProtKB
  • regulation of sodium ion transport Source: UniProtKB
  • response to cAMP Source: UniProtKB
  • response to light stimulus Source: BHF-UCL
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-400253. Circadian Clock.
R-MMU-508751. Circadian Clock.

Names & Taxonomyi

Protein namesi
Recommended name:
Period circadian protein homolog 1
Short name:
mPER1
Alternative name(s):
Circadian clock protein PERIOD 1
Circadian pacemaker protein Rigui
Gene namesi
Name:Per1
Synonyms:Per, Rigui
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1098283. Per1.

Subcellular locationi

  • 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.

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

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).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi267 – 2671Y → E: No effect on homodimerization. Abolishes homodimerization; when associated with E-444. 1 Publication
Mutagenesisi444 – 4441F → E: Reduces homodimerization. Abolishes homodimerization; when associated with E-267. 1 Publication
Mutagenesisi448 – 4481W → E: Abolishes homodimerization. 1 Publication
Mutagenesisi661 – 6611S → A: Reduced phosphorylation. No nuclear entry of PER1, CRY1 nor CKSN1E; when associated with A-663.
Mutagenesisi663 – 6631S → A: Reduced phosphorylation. No nuclear entry PER1, CRY1 nor CKSN1E; when associated with A-661.
Mutagenesisi831 – 8333HCR → ACA: No effect on nuclear import. 1 Publication
Mutagenesisi835 – 8384KAKR → AAKA: Abolishes nuclear accumulation. 1 Publication
Mutagenesisi902 – 91514TSVSP…SPLVT → AAVAPAAFPAPLVA: No effect on nuclear import. Add
BLAST

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12911291Period circadian protein homolog 1PRO_0000162628Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211Phosphothreonine; by CSNK1ESequence analysis
Modified residuei122 – 1221Phosphoserine; by CSNK1ESequence analysis
Modified residuei126 – 1261Phosphoserine; by CSNK1ESequence analysis
Modified residuei661 – 6611Phosphoserine1 Publication
Modified residuei663 – 6631Phosphoserine1 Publication
Modified residuei704 – 7041PhosphoserineCombined sources
Modified residuei815 – 8151PhosphoserineBy similarity
Modified residuei978 – 9781PhosphoserineBy similarity
Modified residuei979 – 9791PhosphoserineBy similarity

Post-translational modificationi

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 PP1.1 Publication
Ubiquitinated; requires phosphorylation by CSNK1E and interaction with BTRC and FBXW11. Deubiquitinated by USP2.2 Publications

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO35973.
MaxQBiO35973.
PaxDbiO35973.
PRIDEiO35973.

PTM databases

iPTMnetiO35973.
PhosphoSiteiO35973.

Expressioni

Tissue specificityi

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.7 Publications

Developmental stagei

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

Inductioni

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.7 Publications

Gene expression databases

BgeeiENSMUSG00000020893.
CleanExiMM_PER1.
ExpressionAtlasiO35973. baseline and differential.
GenevisibleiO35973. MM.

Interactioni

Subunit structurei

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/BMAL1 and CLOCK. Interacts with GPRASP1. Interacts (phosphorylated) with BTRC and FBXW11; the interactions trigger proteasomal degradation. Interacts with NONO, WDR5 and SFPQ. Interacts with U2af1l4 (Isoform 3). Interacts with USP2.13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
TimelessQ9R1X43EBI-1266764,EBI-1793117

GO - Molecular functioni

  • kinase binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: MGI

Protein-protein interaction databases

BioGridi202111. 23 interactions.
DIPiDIP-38519N.
IntActiO35973. 8 interactions.
STRINGi10090.ENSMUSP00000021271.

Structurei

Secondary structure

1
1291
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi198 – 2003Combined sources
Helixi202 – 21211Combined sources
Beta strandi217 – 2259Combined sources
Turni226 – 2283Combined sources
Beta strandi230 – 2345Combined sources
Helixi237 – 2426Combined sources
Turni247 – 2515Combined sources
Helixi254 – 2574Combined sources
Helixi260 – 26910Combined sources
Turni272 – 2743Combined sources
Beta strandi297 – 3015Combined sources
Beta strandi314 – 32512Combined sources
Beta strandi334 – 34310Combined sources
Beta strandi347 – 3515Combined sources
Helixi355 – 3573Combined sources
Beta strandi359 – 3646Combined sources
Beta strandi369 – 3735Combined sources
Helixi377 – 3815Combined sources
Helixi385 – 3884Combined sources
Helixi393 – 3964Combined sources
Helixi399 – 4013Combined sources
Helixi402 – 41211Combined sources
Beta strandi415 – 4173Combined sources
Beta strandi425 – 4284Combined sources
Beta strandi430 – 4323Combined sources
Beta strandi434 – 4385Combined sources
Beta strandi440 – 4456Combined sources
Turni447 – 4493Combined sources
Beta strandi451 – 46313Combined sources
Helixi485 – 49814Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DJ2X-ray2.75A/B/C/D191-502[»]
ProteinModelPortaliO35973.
SMRiO35973. Positions 196-502, 1124-1204.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini208 – 27568PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini348 – 41467PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini422 – 46544PACAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 151151Interaction with BTRCBy similarityAdd
BLAST
Regioni596 – 815220Required for phosphorylation by CSNK1EAdd
BLAST
Regioni1148 – 1291144CRY binding domainAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi138 – 14710Nuclear export signal 1By similarity
Motifi489 – 49810Nuclear export signal 21 Publication
Motifi824 – 84017Nuclear localization signal1 PublicationAdd
BLAST
Motifi981 – 9888Nuclear export signal 3By similarity
Motifi1042 – 10465LXXLL

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 12981Ser-richAdd
BLAST
Compositional biasi653 – 6564Poly-Ser
Compositional biasi841 – 8444Poly-His
Compositional biasi847 – 971125Pro-richAdd
BLAST
Compositional biasi1029 – 110375Ser-richAdd
BLAST
Compositional biasi1224 – 127754Gly-richAdd
BLAST
Compositional biasi1270 – 12734Poly-Glu

Sequence similaritiesi

Contains 2 PAS (PER-ARNT-SIM) domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiENOG410IMRF. Eukaryota.
ENOG410ZBUP. LUCA.
GeneTreeiENSGT00510000046467.
HOVERGENiHBG008167.
InParanoidiO35973.
KOiK02633.
OMAiAPGCHHG.
OrthoDBiEOG091G00PA.
TreeFamiTF318445.

Family and domain databases

InterProiIPR000014. PAS.
IPR013655. PAS_fold_3.
IPR022728. Period_circadian-like_C.
[Graphical view]
PfamiPF08447. PAS_3. 1 hit.
PF12114. Period_C. 1 hit.
[Graphical view]
SMARTiSM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
PROSITEiPS50112. PAS. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35973-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGPLEGADG GGDPRPGEPF CPGGVPSPGA PQHRPCPGPS LADDTDANSN
60 70 80 90 100
GSSGNESNGP ESRGASQRSS HSSSSGNGKD SALLETTESS KSTNSQSPSP
110 120 130 140 150
PSSSIAYSLL SASSEQDNPS TSGCSSEQSA RARTQKELMT ALRELKLRLP
160 170 180 190 200
PERRGKGRSG TLATLQYALA CVKQVQANQE YYQQWSLEEG EPCAMDMSTY
210 220 230 240 250
TLEELEHITS EYTLRNQDTF SVAVSFLTGR IVYISEQAGV LLRCKRDVFR
260 270 280 290 300
GARFSELLAP QDVGVFYGST TPSRLPTWGT GTSAGSGLKD FTQEKSVFCR
310 320 330 340 350
IRGGPDRDPG PRYQPFRLTP YVTKIRVSDG APAQPCCLLI AERIHSGYEA
360 370 380 390 400
PRIPPDKRIF TTRHTPSCLF QDVDERAAPL LGYLPQDLLG APVLLFLHPE
410 420 430 440 450
DRPLMLAIHK KILQLAGQPF DHSPIRFCAR NGEYVTMDTS WAGFVHPWSR
460 470 480 490 500
KVAFVLGRHK VRTAPLNEDV FTPPAPSPAP SLDSDIQELS EQIHRLLLQP
510 520 530 540 550
VHSSSPTGLC GVGPLMSPGP LHSPGSSSDS NGGDAEGPGP PAPVTFQQIC
560 570 580 590 600
KDVHLVKHQG QQLFIESRAK PPPRPRLLAT GTFKAKVLPC QSPNPELEVA
610 620 630 640 650
PVPDQASLAL APEEPERKET SGCSYQQINC LDSILRYLES CNIPSTTKRK
660 670 680 690 700
CASSSSYTAS SASDDDKQRA GPVPVGAKKD PSSAMLSGEG ATPRKEPVVG
710 720 730 740 750
GTLSPLALAN KAESVVSVTS QCSFSSTIVH VGDKKPPESD IIMMEDLPGL
760 770 780 790 800
APGPAPSPAP SPTVAPDPTP DAYRPVGLTK AVLSLHTQKE EQAFLNRFRD
810 820 830 840 850
LGRLRGLDTS SVAPSAPGCH HGPIPPGRRH HCRSKAKRSR HHHHQTPRPE
860 870 880 890 900
TPCYVSHPSP VPSSGPWPPP PATTPFPAMV QPYPLPVFSP RGGPQPLPPA
910 920 930 940 950
PTSVSPATFP SPLVTPMVAL VLPNYLFPTP PSYPYGVSQA PVEGPPTPAS
960 970 980 990 1000
HSPSPSLPPP PLSPPHRPDS PLFNSRCSSP LQLNLLQLEE SPRTEGGAAA
1010 1020 1030 1040 1050
GGPGSSAGPL PPSEETAEPE ARLVEVTESS NQDALSGSSD LLELLLQEDS
1060 1070 1080 1090 1100
RSGTGSAASG SLGSGLGSGS GSGSHEGGST SASITRSSQS SHTSKYFGSI
1110 1120 1130 1140 1150
DSSEAEAGAA RARTEPGDQV IKCVLQDPIW LLMANADQRV MMTYQVPSRD
1160 1170 1180 1190 1200
AASVLKQDRE RLRAMQKQQP RFSEDQRREL GAVHSWVRKG QLPRALDVTA
1210 1220 1230 1240 1250
CVDCGSSVQD PGHSDDPLFS ELDGLGLEPM EEGGGEGGGC GVGGGGGDGG
1260 1270 1280 1290
EEAQTQIGAK GSSSQDSAME EEEQGGGSSS PALPAEENST S
Length:1,291
Mass (Da):136,373
Last modified:July 27, 2011 - v2
Checksum:i77FB9BC71EDF31A6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1199 – 11991T → M in AAC53355 (PubMed:9323128).Curated
Sequence conflicti1199 – 11991T → M in BAA22634 (PubMed:9333243).Curated
Sequence conflicti1199 – 11991T → M in BAA94086 (PubMed:10857746).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022992 mRNA. Translation: AAC53355.1.
AB002108 mRNA. Translation: BAA22634.1.
AB030818 Genomic DNA. Translation: BAA94086.1.
AL645527 Genomic DNA. Translation: CAI35245.1.
CCDSiCCDS24882.1.
PIRiT00019.
RefSeqiNP_001152839.1. NM_001159367.1.
NP_035195.2. NM_011065.4.
XP_006532543.1. XM_006532480.2.
UniGeneiMm.7373.

Genome annotation databases

EnsembliENSMUST00000021271; ENSMUSP00000021271; ENSMUSG00000020893.
ENSMUST00000166748; ENSMUSP00000132635; ENSMUSG00000020893.
GeneIDi18626.
KEGGimmu:18626.
UCSCiuc007jpg.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF022992 mRNA. Translation: AAC53355.1.
AB002108 mRNA. Translation: BAA22634.1.
AB030818 Genomic DNA. Translation: BAA94086.1.
AL645527 Genomic DNA. Translation: CAI35245.1.
CCDSiCCDS24882.1.
PIRiT00019.
RefSeqiNP_001152839.1. NM_001159367.1.
NP_035195.2. NM_011065.4.
XP_006532543.1. XM_006532480.2.
UniGeneiMm.7373.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4DJ2X-ray2.75A/B/C/D191-502[»]
ProteinModelPortaliO35973.
SMRiO35973. Positions 196-502, 1124-1204.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202111. 23 interactions.
DIPiDIP-38519N.
IntActiO35973. 8 interactions.
STRINGi10090.ENSMUSP00000021271.

PTM databases

iPTMnetiO35973.
PhosphoSiteiO35973.

Proteomic databases

EPDiO35973.
MaxQBiO35973.
PaxDbiO35973.
PRIDEiO35973.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000021271; ENSMUSP00000021271; ENSMUSG00000020893.
ENSMUST00000166748; ENSMUSP00000132635; ENSMUSG00000020893.
GeneIDi18626.
KEGGimmu:18626.
UCSCiuc007jpg.2. mouse.

Organism-specific databases

CTDi5187.
MGIiMGI:1098283. Per1.

Phylogenomic databases

eggNOGiENOG410IMRF. Eukaryota.
ENOG410ZBUP. LUCA.
GeneTreeiENSGT00510000046467.
HOVERGENiHBG008167.
InParanoidiO35973.
KOiK02633.
OMAiAPGCHHG.
OrthoDBiEOG091G00PA.
TreeFamiTF318445.

Enzyme and pathway databases

ReactomeiR-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-400253. Circadian Clock.
R-MMU-508751. Circadian Clock.

Miscellaneous databases

PROiO35973.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000020893.
CleanExiMM_PER1.
ExpressionAtlasiO35973. baseline and differential.
GenevisibleiO35973. MM.

Family and domain databases

InterProiIPR000014. PAS.
IPR013655. PAS_fold_3.
IPR022728. Period_circadian-like_C.
[Graphical view]
PfamiPF08447. PAS_3. 1 hit.
PF12114. Period_C. 1 hit.
[Graphical view]
SMARTiSM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
PROSITEiPS50112. PAS. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPER1_MOUSE
AccessioniPrimary (citable) accession number: O35973
Secondary accession number(s): B1ASX0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 27, 2011
Last modified: September 7, 2016
This is version 141 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.