UniProtKB - O54943 (PER2_MOUSE)

>sp|O54943|PER2_MOUSE Period circadian protein homolog 2 OS=Mus musculus OX=10090 GN=Per2 PE=1 SV=3
MNGYVDFSPSPTSPTKEPGAPQPTQAVLQEDVDMSSGSSGNENCSTGRDSQGSDCDDNGK
ELRMLVESSNTHPSPDDAFRLMMTEAEHNPSTSGCSSEQSAKADAHKELIRTLKELKVHL
PADKKAKGKASTLATLKYALRSVKQVKANEEYYQLLMSSESQPCSVDVPSYSMEQVEGIT
SEYIVKNADMFAVAVSLVSGKILYISNQVASIFHCKKDAFSDAKFVEFLAPHDVSVFHSY
TTPYKLPPWSVCSGLDSFTQECMEEKSFFCRVSVGKHHENEIRYQPFRMTPYLVKVQEQQ
GAESQLCCLLLAERVHSGYEAPRIPPEKRIFTTTHTPNCLFQAVDERAVPLLGYLPQDLI
ETPVLVQLHPSDRPLMLAIHKKILQAGGQPFDYSPIRFRTRNGEYITLDTSWSSFINPWS
RKISFIIGRHKVRVGPLNEDVFAAPPCPEEKTPHPSVQELTEQIHRLLMQPVPHSGSSGY
GSLGSNGSHEHLMSQTSSSDSNGQEESHRRRSGIFKTSGKIQTKSHVSHESGGQKEASVA
EMQSSPPAQVKAVTTIERDSSGASLPKASFPEELAYKNQPPCSYQQISCLDSVIRYLESC
SEAATLKRKCEFPANIPSRKATVSPGLHSGEAARPSKVTSHTEVSAHLSSLTLPGKAESV
VSLTSQCSYSSTIVHVGDKKPQPELETVEDMASGPESLDGAAGGLSQEKGPLQKLGLTKE
VLAAHTQKEEQGFLQRFREVSRLSALQAHCQNYLQERSRAQASDRGLRNTSGLESSWKKT
GKNRKLKSKRVKTRDSSESTGSGGPVSHRPPLMGLNATAWSPSDTSQSSCPSAPFPTAVP
AYPLPVFQAPGIVSTPGTVVAPPAATHTGFTMPVVPMGTQPEFAVQPLPFAAPLAPVMAF
MLPSYPFPPATPNLPQAFLPSQPHFPAHPTLASEITPASQAEFPSRTSTLRQPCACPVTP
PAGTVALGRASPPLFQSRGSSPLQLNLLQLEEAPEGSTGAAGTLGTTGTAASGLDCTSGT
SRDRQPKAPPTCNEPSDTQNSDAISTSSDLLNLLLGEDLCSATGSALSRSGASATSDSLG
SSSLGFGTSQSGAGSSDTSHTSKYFGSIDSSENNHKAKMIPDTEESEQFIKYVLQDPIWL
LMANTDDSIMMTYQLPSRDLQAVLKEDQEKLKLLQRSQPRFTEGQRRELREVHPWVHTGG
LPTAIDVTGCVYCESEEKGNICLPYEEDSPSPGLCDTSEAKEEEGEQLTGPRIEAQT

Entry version 159 (22 Apr 2020)
Sequence version 3 (15 Jul 1999)
Previous versions | rss

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Protein

Period circadian protein homolog 2

Gene

Per2

Organism

Mus musculus (Mouse)

Status

Reviewed-Annotation score: -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

Complete GO annotation on QuickGO ...

GO - Biological processⁱ

Complete GO annotation on QuickGO ...

Keywordsⁱ

Biological process	Biological rhythms, Transcription, Transcription regulation

Biological process

Biological rhythms, Transcription, Transcription regulation

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
Organismⁱ	Mus musculus (Mouse)
Taxonomic identifierⁱ	10090 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
Proteomesⁱ	UP000000589 Componentⁱ: Unplaced

Organism-specific databases

MGIⁱ	MGI:1195265 Per2

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 key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	113 – 116	LKEL → AKEA: Accumulates in the nucleus. Exlcusively nuclear; when associated with 464-A--A-467 and 985-A--A-990. 1 Publication	4
Mutagenesisⁱ	306 – 310	LCCLL → 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	5
Mutagenesisⁱ	306 – 310	Missing : Abolishes interaction with NR1D1. 1 Publication	5
Mutagenesisⁱ	415	F → E: Abolishes dimerization. 1 Publication	1
Mutagenesisⁱ	419	W → E: Abolishes dimerization. 1 Publication	1
Mutagenesisⁱ	427	I → E: Abolishes dimerization. 1 Publication	1
Mutagenesisⁱ	464 – 467	IHRL → AHRA: Accumulates in the nucleus. Exlcusively nuclear; when associated with 113-A--A-116 and 985-A--A-990. 1 Publication	4
Mutagenesisⁱ	985 – 990	LNLLQL → ANAAQA: Slightly accumulates in the nucleus. Exlcusively nuclear; when associated with 464-A--A-467 and 985-A--A-990. 1 Publication	6
Mutagenesisⁱ	1052 – 1055	NLLL → 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	4
Mutagenesisⁱ	1052 – 1055	Missing : No effect on interaction with NR1D1. 1 Publication	4

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
ChainⁱPRO_0000162631	1 – 1257	Period circadian protein homolog 2Add BLAST		1257

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	525	Phosphoserine1 Publication	1
Modified residueⁱ	528	Phosphoserine1 Publication	1
Modified residueⁱ	531	Phosphoserine1 Publication	1
Modified residueⁱ	538	Phosphoserine1 Publication	1
Modified residueⁱ	544	Phosphoserine1 Publication	1
Modified residueⁱ	554	Phosphothreonine1 Publication	1
Modified residueⁱ	659	PhosphoserineBy similarity	1
Modified residueⁱ	693	PhosphoserineCombined sources	1
Modified residueⁱ	697	PhosphoserineCombined sources	1
Modified residueⁱ	706	Phosphoserine1 Publication	1
Modified residueⁱ	758	Phosphoserine1 Publication	1
Modified residueⁱ	763	Phosphoserine1 Publication	1
Modified residueⁱ	858	Phosphothreonine1 Publication	1
Modified residueⁱ	939	Phosphoserine1 Publication	1
Modified residueⁱ	964	Phosphothreonine1 Publication	1
Modified residueⁱ	971	Phosphoserine1 Publication	1
Modified residueⁱ	1126	Phosphoserine1 Publication	1

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

PaxDbⁱ	O54943
PRIDEⁱ	O54943

PTM databases

iPTMnetⁱ	O54943
PhosphoSitePlusⁱ	O54943

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

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 (PubMed:11779462).

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 CAVIN3.

Interacts with MAGEL2.

Interacts with MAP1LC3B (PubMed:29937374).

Interacts with HNF4A (By similarity).

By similarity27 Publications

Binary interactionsⁱ

With	#Exp.	IntAct
itself	5	EBI-1266779,EBI-1266779
Arntl [Q9WTL8]	9	EBI-1266779,EBI-644534
Cavin3 [Q91VJ2]	4	EBI-1266779,EBI-8094261
CIART [Q8N365] from Homo sapiens.	4	EBI-1266779,EBI-10265133
Ciart [Q3TQ03]	2	EBI-1266779,EBI-16101489
Clock [O08785]	10	EBI-1266779,EBI-79859
Cry1 [P97784]	22	EBI-1266779,EBI-1266607
Cry2 [Q9R194]	8	EBI-1266779,EBI-1266619
Csnk1e [Q9JMK2]	4	EBI-1266779,EBI-771709
Fbxl3 [Q8C4V4]	2	EBI-1266779,EBI-1266589
NR1D1 [P20393] from Homo sapiens.	2	EBI-1266779,EBI-2811738
Per1 [O35973]	3	EBI-1266779,EBI-1266764

Show more details

GO - Molecular functionⁱ

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

BioGridⁱ	202112, 25 interactors
ComplexPortalⁱ	CPX-3209 Cry1-Per2 complex CPX-3210 Cry2-Per2 complex
CORUMⁱ	O54943
Database of interacting proteins More...DIPⁱ	DIP-38518N
ELMⁱ	O54943
IntActⁱ	O54943, 33 interactors
Molecular INTeraction database More...MINTⁱ	O54943
STRINGⁱ	10090.ENSMUSP00000066620

Miscellaneous databases

RNActⁱ	O54943 protein

RNActⁱ

O54943 protein

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Turnⁱ	173 – 176	Combined sources	4
Beta strandⁱ	190 – 195	Combined sources	6
Turnⁱ	197 – 199	Combined sources	3
Beta strandⁱ	201 – 205	Combined sources	5
Turnⁱ	207 – 212	Combined sources	6
Helixⁱ	225 – 228	Combined sources	4
Turnⁱ	231 – 233	Combined sources	3
Helixⁱ	234 – 240	Combined sources	7
Beta strandⁱ	268 – 272	Combined sources	5
Beta strandⁱ	285 – 295	Combined sources	11
Beta strandⁱ	306 – 314	Combined sources	9
Beta strandⁱ	320 – 322	Combined sources	3
Helixⁱ	326 – 328	Combined sources	3
Beta strandⁱ	330 – 335	Combined sources	6
Beta strandⁱ	340 – 344	Combined sources	5
Helixⁱ	348 – 352	Combined sources	5
Helixⁱ	356 – 359	Combined sources	4
Helixⁱ	364 – 367	Combined sources	4
Helixⁱ	373 – 385	Combined sources	13
Turnⁱ	386 – 388	Combined sources	3
Beta strandⁱ	391 – 399	Combined sources	9
Beta strandⁱ	405 – 416	Combined sources	12
Turnⁱ	418 – 420	Combined sources	3
Beta strandⁱ	423 – 434	Combined sources	12
Beta strandⁱ	437 – 439	Combined sources	3
Helixⁱ	455 – 467	Combined sources	13
Beta strandⁱ	1132 – 1135	Combined sources	4
Helixⁱ	1138 – 1141	Combined sources	4
Helixⁱ	1147 – 1152	Combined sources	6
Helixⁱ	1160 – 1174	Combined sources	15
Helixⁱ	1175 – 1177	Combined sources	3
Helixⁱ	1183 – 1189	Combined sources	7
Turnⁱ	1190 – 1192	Combined sources	3
Helixⁱ	1195 – 1198	Combined sources	4
Helixⁱ	1203 – 1205	Combined sources	3
Beta strandⁱ	1207 – 1209	Combined sources	3
Turnⁱ	1211 – 1213	Combined sources	3

Show more details

3D structure databases

SMRⁱ	O54943
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	O54943

EvolutionaryTraceⁱ

O54943

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Length
Domainⁱ	179 – 246	PAS 1PROSITE-ProRule annotationAdd BLAST	68
Domainⁱ	319 – 385	PAS 2PROSITE-ProRule annotationAdd BLAST	67
Domainⁱ	393 – 436	PACAdd BLAST	44

Region

Feature key	Position(s)	DescriptionActions	Length
Regionⁱ	478 – 482	Important for protein stabilityBy similarity	5
Regionⁱ	510 – 709	CSNK1E binding domainAdd BLAST	200
Regionⁱ	882 – 1067	Interaction with PPARG1 PublicationAdd BLAST	186
Regionⁱ	1157 – 1257	CRY binding domainBy similarityAdd BLAST	101

Motif

Feature key	Position(s)	DescriptionActions	Length
Motifⁱ	109 – 118	Nuclear export signal 11 Publication	10
Motifⁱ	306 – 310	LXXLL	5
Motifⁱ	460 – 469	Nuclear export signal 21 Publication	10
Motifⁱ	778 – 794	Nuclear localization signal1 PublicationAdd BLAST	17
Motifⁱ	983 – 990	Nuclear export signal 31 Publication	8
Motifⁱ	1051 – 1055	LXXLL	5

Compositional bias

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Compositional biasⁱ	831 – 961	Pro-richAdd BLAST		131
Compositional biasⁱ	1061 – 1111	Ser-richAdd BLAST		51

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	KOG3753 Eukaryota ENOG410Y118 LUCA
InParanoidⁱ	O54943
KEGG Orthology (KO) More...KOⁱ	K02633
Database of Orthologous Groups More...OrthoDBⁱ	145617at2759
PhylomeDBⁱ	O54943
TreeFamⁱ	TF318445

Family and domain databases

Conserved Domains Database More...CDDⁱ	cd00130 PAS, 1 hit
InterProⁱ	View protein in InterPro IPR000014 PAS IPR035965 PAS-like_dom_sf IPR013655 PAS_fold_3 IPR022728 Period_circadian-like_C
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF08447 PAS_3, 1 hit PF12114 Period_C, 1 hit
SMARTⁱ	View protein in SMART SM00091 PAS, 2 hits
SUPFAMⁱ	SSF55785 SSF55785, 1 hit
PROSITEⁱ	View protein in PROSITE PS50112 PAS, 1 hit

Sequence (1+)ⁱ

Sequence statusⁱ: Complete.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show all Align All

O54943-1 [UniParc]FASTA Add to basket

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        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

Computationally mapped potential isoform sequencesⁱ

There is 1 potential isoform mapped to this entry.BLAST Align Show all Add to basket

	Entry	Entry name		Protein names	Gene names	Length	Annotation

	A0A0R4J0U3	A0A0R4J0U3_MOUSE		Period circadian protein homolog 2 Period circadian protein homolog 2	Per2	1,257	Annotation score:

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	445	P → S in AAC53592 (PubMed:9427249).Curated		1
Sequence conflictⁱ	728	K → R in AAC53592 (PubMed:9427249).Curated		1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF036893 mRNA Translation: AAC39942.1 AF035830 mRNA Translation: AAC53592.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS35663.1
PIRⁱ	T09493
NCBI Reference Sequences More...RefSeqⁱ	NP_035196.2, NM_011066.3

Genome annotation databases

GeneIDⁱ	18627
KEGGⁱ	mmu:18627

Similar proteinsⁱ

90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
O54943	Period circadian protein homolog 2		RAT		1257	UniRef90_O54943
MKIAA0347 protein (Fragment)		MOUSE		1267
Period 2 (Fragment)		little Indian field mouse		87
Period circadian protein-like 2		CRIGR		1262
Period circadian protein 2 (Fragment)		CRICR		59
+30

Protein	Similar proteins		Species	Score	Length	Source
O54943	Period circadian protein homolog 2		RAT		1257	UniRef50_O54943
Period circadian protein homolog 2		HUMAN		1255
MKIAA0347 protein (Fragment)		MOUSE		1267
Period 2 (Fragment)		little Indian field mouse		87
Period circadian protein-like 2		CRIGR		1262
+239

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF036893 mRNA Translation: AAC39942.1 AF035830 mRNA Translation: AAC53592.1
CCDSⁱ	CCDS35663.1
PIRⁱ	T09493
RefSeqⁱ	NP_035196.2, NM_011066.3

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	3GDI	X-ray	2.40	A/B	170-473	[»]
	4CT0	X-ray	2.45	B	1132-1252	[»]
	4U8H	X-ray	2.80	B/D	1095-1215	[»]
SMRⁱ	O54943
ModBaseⁱ	Search...
PDBe-KBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	202112, 25 interactors
ComplexPortalⁱ	CPX-3209 Cry1-Per2 complex CPX-3210 Cry2-Per2 complex
CORUMⁱ	O54943
DIPⁱ	DIP-38518N
ELMⁱ	O54943
IntActⁱ	O54943, 33 interactors
MINTⁱ	O54943
STRINGⁱ	10090.ENSMUSP00000066620

PTM databases

iPTMnetⁱ	O54943
PhosphoSitePlusⁱ	O54943

Proteomic databases

PaxDbⁱ	O54943
PRIDEⁱ	O54943

Protocols and materials databases

The DNASU plasmid repository More...DNASUⁱ	18627

DNASUⁱ

18627

Genome annotation databases

GeneIDⁱ	18627
KEGGⁱ	mmu:18627

Organism-specific databases

CTDⁱ	8864
MGIⁱ	MGI:1195265 Per2

Phylogenomic databases

eggNOGⁱ	KOG3753 Eukaryota ENOG410Y118 LUCA
InParanoidⁱ	O54943
KOⁱ	K02633
OrthoDBⁱ	145617at2759
PhylomeDBⁱ	O54943
TreeFamⁱ	TF318445

Miscellaneous databases

ChiTaRSⁱ	Per2 mouse
EvolutionaryTraceⁱ	O54943
Protein Ontology More...PROⁱ	PR:O54943
RNActⁱ	O54943 protein
SOURCEⁱ	Search...

Family and domain databases

CDDⁱ	cd00130 PAS, 1 hit
InterProⁱ	View protein in InterPro IPR000014 PAS IPR035965 PAS-like_dom_sf IPR013655 PAS_fold_3 IPR022728 Period_circadian-like_C
Pfamⁱ	View protein in Pfam PF08447 PAS_3, 1 hit PF12114 Period_C, 1 hit
SMARTⁱ	View protein in SMART SM00091 PAS, 2 hits
SUPFAMⁱ	SSF55785 SSF55785, 1 hit
PROSITEⁱ	View protein in PROSITE PS50112 PAS, 1 hit
ProtoNetⁱ	Search...
MobiDBⁱ	Search...

Entry informationⁱ

Entry nameⁱ	PER2_MOUSE
Accessionⁱ	O54943Primary (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:	April 22, 2020
	This is version 159 of the entry and version 3 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Reference proteome

Documents

MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references

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UniProtKB - O54943 (PER2_MOUSE)

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Period circadian protein homolog 2

Per2

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<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

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Amino acid modifications

Keywords - PTMi

Proteomic databases

PTM databases

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<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

O54943

GO - Molecular functioni

Protein-protein interaction databases

Miscellaneous databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

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Protocols and materials databases

Genome annotation databases

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

Interactionⁱ

GO - Molecular functionⁱ

Structureⁱ

Family & Domainsⁱ

Keywords - Domainⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ