UniProtKB - O54943 (PER2_MOUSE)
Period circadian protein homolog 2
Per2
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 G6PC1. 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 PublicationsGO - Molecular functioni
- DNA-binding transcription factor binding Source: UniProtKB
- histone deacetylase binding Source: UniProtKB
- histone methyltransferase binding Source: UniProtKB
- identical protein binding Source: IntAct
- kinase binding Source: UniProtKB
- nuclear receptor binding Source: UniProtKB
- pre-mRNA binding Source: UniProtKB
- RNA polymerase binding Source: UniProtKB
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: UniProtKB
- transcription cis-regulatory region binding Source: UniProtKB
- transcription coactivator activity Source: UniProtKB
- transcription corepressor binding Source: UniProtKB
GO - Biological processi
- circadian regulation of gene expression Source: UniProtKB
- circadian regulation of translation Source: UniProtKB
- circadian rhythm Source: MGI
- entrainment of circadian clock by photoperiod Source: GO_Central
- 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 by RNA polymerase II Source: MGI
- negative regulation of transcription regulatory region DNA binding Source: UniProtKB
- positive regulation of cold-induced thermogenesis Source: YuBioLab
- 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
- white fat cell differentiation Source: UniProtKB
Keywordsi
Biological process | Biological rhythms, Transcription, Transcription regulation |
Names & Taxonomyi
Protein namesi | Recommended name: Period circadian protein homolog 2Short name: mPER2 Alternative name(s): Circadian clock protein PERIOD 2 |
Gene namesi | Name:Per2 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:1195265, Per2 |
Subcellular locationi
Nucleus
- Nucleus 2 Publications
Cytoplasm and Cytosol
- Cytoplasm 2 Publications
Other locations
- perinuclear region 1 Publication
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 (PubMed:22274616).1 Publication
Cytosol
- cytosol Source: MGI
Nucleus
- nucleoplasm Source: MGI
- nucleus Source: UniProtKB
Other locations
- cytoplasm Source: UniProtKB
- perinuclear region of cytoplasm Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, NucleusPathology & Biotechi
Disruption phenotypei
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | 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 | Graphical view | 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
Keywords - PTMi
Acetylation, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | O54943 |
PRIDEi | O54943 |
ProteomicsDBi | 288029 |
PTM databases
iPTMneti | O54943 |
PhosphoSitePlusi | O54943 |
Expressioni
Tissue specificityi
Developmental stagei
Inductioni
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 CAVIN3.
Interacts with MAGEL2.
Interacts with MAP1LC3B (PubMed:29937374).
Interacts with HNF4A (By similarity).
By similarity27 PublicationsBinary interactionsi
O54943
GO - Molecular functioni
- DNA-binding transcription factor binding Source: UniProtKB
- histone deacetylase binding Source: UniProtKB
- histone methyltransferase binding Source: UniProtKB
- identical protein binding Source: IntAct
- kinase binding Source: UniProtKB
- nuclear receptor binding Source: UniProtKB
- RNA polymerase binding Source: UniProtKB
- transcription corepressor binding Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 202112, 31 interactors |
ComplexPortali | CPX-3209, Cry1-Per2 complex CPX-3210, Cry2-Per2 complex |
CORUMi | O54943 |
DIPi | DIP-38518N |
ELMi | O54943 |
IntActi | O54943, 38 interactors |
MINTi | O54943 |
STRINGi | 10090.ENSMUSP00000066620 |
Miscellaneous databases
RNActi | O54943, protein |
Structurei
Secondary structure
3D structure databases
AlphaFoldDBi | O54943 |
SMRi | O54943 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O54943 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | 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 | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 60 | DisorderedSequence analysisAdd BLAST | 60 | |
Regioni | 471 – 565 | DisorderedSequence analysisAdd BLAST | 95 | |
Regioni | 478 – 482 | Important for protein stabilityBy similarity | 5 | |
Regioni | 510 – 709 | CSNK1E binding domain1 PublicationAdd BLAST | 200 | |
Regioni | 617 – 638 | DisorderedSequence analysisAdd BLAST | 22 | |
Regioni | 757 – 832 | DisorderedSequence analysisAdd BLAST | 76 | |
Regioni | 882 – 1067 | Interaction with PPARG1 PublicationAdd BLAST | 186 | |
Regioni | 994 – 1044 | DisorderedSequence analysisAdd BLAST | 51 | |
Regioni | 1070 – 1115 | DisorderedSequence analysisAdd BLAST | 46 | |
Regioni | 1157 – 1257 | CRY binding domainBy similarityAdd BLAST | 101 | |
Regioni | 1224 – 1257 | DisorderedSequence analysisAdd BLAST | 34 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | 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 | 28 – 52 | Polar residuesSequence analysisAdd BLAST | 25 | |
Compositional biasi | 475 – 502 | Polar residuesSequence analysisAdd BLAST | 28 | |
Compositional biasi | 537 – 562 | Polar residuesSequence analysisAdd BLAST | 26 | |
Compositional biasi | 757 – 777 | Polar residuesSequence analysisAdd BLAST | 21 | |
Compositional biasi | 818 – 832 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 1000 – 1044 | Polar residuesSequence analysisAdd BLAST | 45 | |
Compositional biasi | 1070 – 1114 | Polar residuesSequence analysisAdd BLAST | 45 |
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG3753, Eukaryota |
InParanoidi | O54943 |
OrthoDBi | 145617at2759 |
PhylomeDBi | O54943 |
TreeFami | TF318445 |
Family and domain databases
CDDi | cd00130, PAS, 1 hit |
IDEALi | IID50265 |
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 |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All
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
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA0A0R4J0U3 | A0A0R4J0U3_MOUSE | 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 |
CCDSi | CCDS35663.1 |
PIRi | T09493 |
RefSeqi | NP_035196.2, NM_011066.3 |
Genome annotation databases
GeneIDi | 18627 |
KEGGi | mmu:18627 |
Similar proteinsi
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: PDBei RCSB PDBi 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 | [»] | |
AlphaFoldDBi | O54943 | |||||
SMRi | O54943 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 202112, 31 interactors |
ComplexPortali | CPX-3209, Cry1-Per2 complex CPX-3210, Cry2-Per2 complex |
CORUMi | O54943 |
DIPi | DIP-38518N |
ELMi | O54943 |
IntActi | O54943, 38 interactors |
MINTi | O54943 |
STRINGi | 10090.ENSMUSP00000066620 |
PTM databases
iPTMneti | O54943 |
PhosphoSitePlusi | O54943 |
Proteomic databases
PaxDbi | O54943 |
PRIDEi | O54943 |
ProteomicsDBi | 288029 |
Protocols and materials databases
DNASUi | 18627 |
Genome annotation databases
GeneIDi | 18627 |
KEGGi | mmu:18627 |
Organism-specific databases
CTDi | 8864 |
MGIi | MGI:1195265, Per2 |
Phylogenomic databases
eggNOGi | KOG3753, Eukaryota |
InParanoidi | O54943 |
OrthoDBi | 145617at2759 |
PhylomeDBi | O54943 |
TreeFami | TF318445 |
Miscellaneous databases
BioGRID-ORCSi | 18627, 1 hit in 72 CRISPR screens |
ChiTaRSi | Per2, mouse |
EvolutionaryTracei | O54943 |
PROi | PR:O54943 |
RNActi | O54943, protein |
SOURCEi | Search... |
Family and domain databases
CDDi | cd00130, PAS, 1 hit |
IDEALi | IID50265 |
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 |
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: | May 25, 2022 | |
This is version 167 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 proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references