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Protein

Period circadian protein homolog 2

Gene

Per2

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 syndrome 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. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby transcriptional activation. Required for fatty acid and lipid metabolism, is involved as well in the regulation of circulating insulin levels. Plays an important role in the maintenance of cardiovascular functions through the regulation of NO and vasodilatatory prostaglandins production in aortas. Controls circadian glutamate uptake in synaptic vesicles through the regulation of VGLUT1 expression. May also be involved in the regulation of inflammatory processes. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and ATF4. Negatively regulates the formation of the TIMELESS-CRY1 complex by competing with TIMELESS for binding to CRY1.17 Publications

GO - Molecular functioni

  • core promoter binding Source: UniProtKB
  • histone deacetylase binding Source: UniProtKB
  • histone methyltransferase binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • pre-mRNA binding Source: UniProtKB
  • RNA polymerase binding Source: UniProtKB
  • transcription coactivator activity Source: UniProtKB
  • transcription corepressor binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • transcription regulatory region sequence-specific DNA binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • circadian regulation of gene expression Source: UniProtKB
  • circadian regulation of translation Source: UniProtKB
  • circadian rhythm Source: UniProtKB
  • fatty acid metabolic process Source: UniProtKB
  • gluconeogenesis Source: UniProtKB
  • glycogen biosynthetic process Source: UniProtKB
  • histone H3 deacetylation Source: UniProtKB
  • lactate biosynthetic process Source: UniProtKB
  • negative regulation of circadian rhythm Source: UniProtKB
  • negative regulation of DNA-templated transcription, termination Source: UniProtKB
  • negative regulation of fat cell proliferation Source: UniProtKB
  • negative regulation of protein ubiquitination Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • negative regulation of transcription regulatory region DNA binding Source: UniProtKB
  • regulation of cell cycle Source: UniProtKB
  • regulation of circadian rhythm Source: UniProtKB
  • regulation of glutamate uptake involved in transmission of nerve impulse Source: UniProtKB
  • regulation of insulin secretion Source: UniProtKB
  • regulation of neurogenesis Source: UniProtKB
  • regulation of vasoconstriction Source: UniProtKB
  • response to ischemia Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
  • white fat cell differentiation Source: UniProtKB
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 2
Short name:
mPER2
Alternative name(s):
Circadian clock protein PERIOD 2
Gene namesi
Name:Per2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1195265. Per2.

Subcellular locationi

  • Nucleus 1 Publication
  • Cytoplasm 1 Publication
  • Cytoplasmperinuclear region

  • Note: Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2. PML regulates its nuclear localization.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Animals show severely disrupted circadian behavior. During myocardial ischemia, they have larger infarct sizes with deficient lactate production. Mice show reduced muscle strength under stress conditions, show endothelial dysfunctions and have a mean arterial pressure significantly lower compared to wild types. They have elevated circulatory insulin levels associated with enhanced glucose-stimulated insulin secretion and impaired insulin clearance. Animals also have increased levels of liver glycogen and impaired hepatic gluconeogenesis. They display altered lipid metabolism with drastic reduction of total triacylglycerides and non-esterified fatty acids. Double knockouts for PER2 and PER1 show an abrupt loss of rhythmicity immediately upon transfer to exposure to constant darkness. Animals have largely affected the water intake (polydipsia) and urine volume (polyuria). Double knocknouts for PER2 and PER3 show the same phenotype as PER2 simple knockouts. Double knockout for NR1D1 and PER2 show a significantly shorter period length compared with wild type or single knockouts for both genes. 50% of double knockouts animals show a stable circadian throughout at least 5 weeks in constant darkness. The other 50% of animals lose their circadian rhythmicity when held in constant darkness for an average of 21 days. Animals have blunted steady-state levels of glycogen in the liver in spite of normal patterns of food consumption.8 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi113 – 1164LKEL → AKEA: Accumulates in the nucleus. Exlcusively nuclear; when associated with 464-A--A-467 and 985-A--A-990. 1 Publication
Mutagenesisi306 – 3105LCCLL → ACCAA: Abolishes interaction with PPARA and NR1D1. No effect on interaction with CRY1. Abolishes interaction with PPARA and NR1D1 as well as reduces the amplitude of ARNTL expression; when associated with 1052-E--A-1055. 1 Publication
Mutagenesisi306 – 3105Missing : Abolishes interaction with NR1D1. 1 Publication
Mutagenesisi415 – 4151F → E: Abolishes dimerization. 1 Publication
Mutagenesisi419 – 4191W → E: Abolishes dimerization. 1 Publication
Mutagenesisi427 – 4271I → E: Abolishes dimerization. 1 Publication
Mutagenesisi464 – 4674IHRL → AHRA: Accumulates in the nucleus. Exlcusively nuclear; when associated with 113-A--A-116 and 985-A--A-990. 1 Publication
Mutagenesisi985 – 9906LNLLQL → ANAAQA: Slightly accumulates in the nucleus. Exlcusively nuclear; when associated with 464-A--A-467 and 985-A--A-990. 1 Publication
Mutagenesisi1052 – 10554NLLL → EAAA: No effect on interaction with PPARA. Abolishes interaction with PPARA and NR1D1 as well as reduces the amplitude of ARNTL expression; when associated with 306-A--A-310. 1 Publication
Mutagenesisi1052 – 10554Missing : No effect on interaction with NR1D1. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12571257Period circadian protein homolog 2PRO_0000162631Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei525 – 5251Phosphoserine1 Publication
Modified residuei528 – 5281Phosphoserine1 Publication
Modified residuei531 – 5311Phosphoserine1 Publication
Modified residuei538 – 5381Phosphoserine1 Publication
Modified residuei544 – 5441Phosphoserine1 Publication
Modified residuei554 – 5541Phosphothreonine1 Publication
Modified residuei659 – 6591PhosphoserineBy similarity
Modified residuei693 – 6931PhosphoserineCombined sources
Modified residuei697 – 6971PhosphoserineCombined sources
Modified residuei706 – 7061Phosphoserine1 Publication
Modified residuei758 – 7581Phosphoserine1 Publication
Modified residuei763 – 7631Phosphoserine1 Publication
Modified residuei858 – 8581Phosphothreonine1 Publication
Modified residuei939 – 9391Phosphoserine1 Publication
Modified residuei964 – 9641Phosphothreonine1 Publication
Modified residuei971 – 9711Phosphoserine1 Publication
Modified residuei1126 – 11261Phosphoserine1 Publication

Post-translational modificationi

Acetylated. Deacetylated by SIRT1, resulting in decreased protein stability.1 Publication
Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation. May be dephosphorylated by PP1.5 Publications
Ubiquitinated, leading to its proteasomal degradation. Ubiquitination may be inhibited by CRY1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiO54943.
PRIDEiO54943.

PTM databases

iPTMnetiO54943.
PhosphoSiteiO54943.

Expressioni

Tissue specificityi

In the brain, high expression in SCN during the subjective day. Constitutive expression in the cornu ammonis and in the dentate gyrus of the hyppocampus. Also expressed in the piriform cortex and the glomeruli of the olfactory bulb, and at a lower extent in the cerebral cortex. Not expressed in the pars tuberalis and the Purkinje neurons. Also expressed in adipose tissue (white and brown), heart, kidney, bladder, lumbar spinal cord, skeletal muscle, spleen, lung, pancreas and liver with highest levels in skeletal muscle and liver and lowest levels in spleen.7 Publications

Developmental stagei

Expressed in the SCN during late fetal and early neonatal life. Expression increases during adipogenesis.2 Publications

Inductioni

Oscillates diurnally in several tissues, mainly in central nervous system and liver (at protein levels) but also in pancreas, bladder and lumbar spinal cord. Rhythmic levels are critical for the generation of circadian rhythms in central as well as peripheral clocks. Targeted degradation of PER and CRY proteins enables the reactivation of CLOCK-ARTNL/BMAL1, thus initiating a new circadian transcriptional cycle with an intrinsic period of 24 hours.7 Publications

Gene expression databases

BgeeiENSMUSG00000055866.
CleanExiMM_PER2.

Interactioni

Subunit structurei

Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts with CLOCK-ARNTL/BMAL1 (off DNA). Interacts with ARNTL2/BMAL2. Interacts directly with PER1 and PER3, and through a C-terminal domain, with CRY1 and CRY2. Interacts, via its second PAS domain, with TIMELESS in vitro. Interacts with NFIL3. Different large complexes have been identified with different repressive functions. The core of PER complexes is composed of at least PER1, PER2, PER3, CRY1, CRY2, CSNK1D and/or CSNK1E. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex. Interacts with SETX; the interaction inhibits termination of circadian target genes. Interacts with the nuclear receptors HNF4A, NR1D1, NR4A2, RORA, PPARA, PPARG and THRA; the interaction with at least PPARG is ligand dependent. Interacts with PML. Interacts (phosphorylated) with BTRC and FBXW11; the interactions trigger proteasomal degradation. Interacts with NONO and SFPQ. Interacts with SIRT1. Interacts with PRKCDBP. Interacts with MAGEL2.25 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ArntlQ9WTL88EBI-1266779,EBI-644534
ClockO0878510EBI-1266779,EBI-79859
Cry1P9778415EBI-1266779,EBI-1266607
Cry2Q9R1944EBI-1266779,EBI-1266619
Fbxl3Q8C4V42EBI-1266779,EBI-1266589
PrkcdbpQ91VJ24EBI-1266779,EBI-8094261

GO - Molecular functioni

  • histone deacetylase binding Source: UniProtKB
  • histone methyltransferase binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • RNA polymerase binding Source: UniProtKB
  • transcription corepressor binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi202112. 26 interactions.
DIPiDIP-38518N.
IntActiO54943. 19 interactions.
STRINGi10090.ENSMUSP00000066620.

Structurei

Secondary structure

1
1257
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni173 – 1764Combined sources
Beta strandi190 – 1956Combined sources
Turni197 – 1993Combined sources
Beta strandi201 – 2055Combined sources
Turni207 – 2126Combined sources
Helixi225 – 2284Combined sources
Turni231 – 2333Combined sources
Helixi234 – 2407Combined sources
Beta strandi268 – 2725Combined sources
Beta strandi285 – 29511Combined sources
Beta strandi306 – 3149Combined sources
Beta strandi320 – 3223Combined sources
Helixi326 – 3283Combined sources
Beta strandi330 – 3356Combined sources
Beta strandi340 – 3445Combined sources
Helixi348 – 3525Combined sources
Helixi356 – 3594Combined sources
Helixi364 – 3674Combined sources
Helixi373 – 38513Combined sources
Turni386 – 3883Combined sources
Beta strandi391 – 3999Combined sources
Beta strandi405 – 41612Combined sources
Turni418 – 4203Combined sources
Beta strandi423 – 43412Combined sources
Beta strandi437 – 4393Combined sources
Helixi455 – 46713Combined sources
Beta strandi1132 – 11354Combined sources
Helixi1138 – 11414Combined sources
Helixi1147 – 11526Combined sources
Helixi1160 – 117415Combined sources
Helixi1175 – 11773Combined sources
Helixi1183 – 11897Combined sources
Turni1190 – 11923Combined sources
Helixi1195 – 11984Combined sources
Helixi1203 – 12053Combined sources
Beta strandi1207 – 12093Combined sources
Turni1211 – 12133Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GDIX-ray2.40A/B170-473[»]
4CT0X-ray2.45B1132-1252[»]
4U8HX-ray2.80B/D1095-1215[»]
ProteinModelPortaliO54943.
SMRiO54943. Positions 113-473, 1132-1214.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO54943.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini179 – 24668PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini319 – 38567PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini393 – 43644PACAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni478 – 4825Important for protein stabilityBy similarity
Regioni510 – 709200CSNK1E binding domainAdd
BLAST
Regioni882 – 1067186Interaction with PPARG1 PublicationAdd
BLAST
Regioni1157 – 1257101CRY binding domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi109 – 11810Nuclear export signal 11 Publication
Motifi306 – 3105LXXLL
Motifi460 – 46910Nuclear export signal 21 Publication
Motifi778 – 79417Nuclear localization signal1 PublicationAdd
BLAST
Motifi983 – 9908Nuclear export signal 31 Publication
Motifi1051 – 10555LXXLL

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi831 – 961131Pro-richAdd
BLAST
Compositional biasi1061 – 111151Ser-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG3753. Eukaryota.
ENOG410Y118. LUCA.
HOVERGENiHBG008167.
InParanoidiO54943.
KOiK02633.
PhylomeDBiO54943.
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.

O54943-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGYVDFSPS PTSPTKEPGA PQPTQAVLQE DVDMSSGSSG NENCSTGRDS
60 70 80 90 100
QGSDCDDNGK ELRMLVESSN THPSPDDAFR LMMTEAEHNP STSGCSSEQS
110 120 130 140 150
AKADAHKELI RTLKELKVHL PADKKAKGKA STLATLKYAL RSVKQVKANE
160 170 180 190 200
EYYQLLMSSE SQPCSVDVPS YSMEQVEGIT SEYIVKNADM FAVAVSLVSG
210 220 230 240 250
KILYISNQVA SIFHCKKDAF SDAKFVEFLA PHDVSVFHSY TTPYKLPPWS
260 270 280 290 300
VCSGLDSFTQ ECMEEKSFFC RVSVGKHHEN EIRYQPFRMT PYLVKVQEQQ
310 320 330 340 350
GAESQLCCLL LAERVHSGYE APRIPPEKRI FTTTHTPNCL FQAVDERAVP
360 370 380 390 400
LLGYLPQDLI ETPVLVQLHP SDRPLMLAIH KKILQAGGQP FDYSPIRFRT
410 420 430 440 450
RNGEYITLDT SWSSFINPWS RKISFIIGRH KVRVGPLNED VFAAPPCPEE
460 470 480 490 500
KTPHPSVQEL TEQIHRLLMQ PVPHSGSSGY GSLGSNGSHE HLMSQTSSSD
510 520 530 540 550
SNGQEESHRR RSGIFKTSGK IQTKSHVSHE SGGQKEASVA EMQSSPPAQV
560 570 580 590 600
KAVTTIERDS SGASLPKASF PEELAYKNQP PCSYQQISCL DSVIRYLESC
610 620 630 640 650
SEAATLKRKC EFPANIPSRK ATVSPGLHSG EAARPSKVTS HTEVSAHLSS
660 670 680 690 700
LTLPGKAESV VSLTSQCSYS STIVHVGDKK PQPELETVED MASGPESLDG
710 720 730 740 750
AAGGLSQEKG PLQKLGLTKE VLAAHTQKEE QGFLQRFREV SRLSALQAHC
760 770 780 790 800
QNYLQERSRA QASDRGLRNT SGLESSWKKT GKNRKLKSKR VKTRDSSEST
810 820 830 840 850
GSGGPVSHRP PLMGLNATAW SPSDTSQSSC PSAPFPTAVP AYPLPVFQAP
860 870 880 890 900
GIVSTPGTVV APPAATHTGF TMPVVPMGTQ PEFAVQPLPF AAPLAPVMAF
910 920 930 940 950
MLPSYPFPPA TPNLPQAFLP SQPHFPAHPT LASEITPASQ AEFPSRTSTL
960 970 980 990 1000
RQPCACPVTP PAGTVALGRA SPPLFQSRGS SPLQLNLLQL EEAPEGSTGA
1010 1020 1030 1040 1050
AGTLGTTGTA ASGLDCTSGT SRDRQPKAPP TCNEPSDTQN SDAISTSSDL
1060 1070 1080 1090 1100
LNLLLGEDLC SATGSALSRS GASATSDSLG SSSLGFGTSQ SGAGSSDTSH
1110 1120 1130 1140 1150
TSKYFGSIDS SENNHKAKMI PDTEESEQFI KYVLQDPIWL LMANTDDSIM
1160 1170 1180 1190 1200
MTYQLPSRDL QAVLKEDQEK LKLLQRSQPR FTEGQRRELR EVHPWVHTGG
1210 1220 1230 1240 1250
LPTAIDVTGC VYCESEEKGN ICLPYEEDSP SPGLCDTSEA KEEEGEQLTG

PRIEAQT
Length:1,257
Mass (Da):135,881
Last modified:July 15, 1999 - v3
Checksum:i554B8AFF036CF7FB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti445 – 4451P → S in AAC53592 (PubMed:9427249).Curated
Sequence conflicti728 – 7281K → R in AAC53592 (PubMed:9427249).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036893 mRNA. Translation: AAC39942.1.
AF035830 mRNA. Translation: AAC53592.1.
CCDSiCCDS35663.1.
PIRiT09493.
RefSeqiNP_035196.2. NM_011066.3.
UniGeneiMm.482463.

Genome annotation databases

GeneIDi18627.
KEGGimmu:18627.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF036893 mRNA. Translation: AAC39942.1.
AF035830 mRNA. Translation: AAC53592.1.
CCDSiCCDS35663.1.
PIRiT09493.
RefSeqiNP_035196.2. NM_011066.3.
UniGeneiMm.482463.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3GDIX-ray2.40A/B170-473[»]
4CT0X-ray2.45B1132-1252[»]
4U8HX-ray2.80B/D1095-1215[»]
ProteinModelPortaliO54943.
SMRiO54943. Positions 113-473, 1132-1214.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi202112. 26 interactions.
DIPiDIP-38518N.
IntActiO54943. 19 interactions.
STRINGi10090.ENSMUSP00000066620.

PTM databases

iPTMnetiO54943.
PhosphoSiteiO54943.

Proteomic databases

PaxDbiO54943.
PRIDEiO54943.

Protocols and materials databases

DNASUi18627.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi18627.
KEGGimmu:18627.

Organism-specific databases

CTDi8864.
MGIiMGI:1195265. Per2.

Phylogenomic databases

eggNOGiKOG3753. Eukaryota.
ENOG410Y118. LUCA.
HOVERGENiHBG008167.
InParanoidiO54943.
KOiK02633.
PhylomeDBiO54943.
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

ChiTaRSiPer2. mouse.
EvolutionaryTraceiO54943.
PROiO54943.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000055866.
CleanExiMM_PER2.

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.
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Entry informationi

Entry nameiPER2_MOUSE
AccessioniPrimary (citable) accession number: O54943
Secondary accession number(s): O54954
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 15, 1999
Last modified: September 7, 2016
This is version 135 of the entry and version 3 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.