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Period circadian protein homolog 2 (hPER2) (Circadian clock protein PERIOD 2)

 PER2_HUMAN              Reviewed;        1255 AA.
O15055; A2I2P7; Q4ZG49; Q6DT41; Q9UQ45;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
11-JUL-2001, sequence version 2.
18-JUL-2018, entry version 175.
RecName: Full=Period circadian protein homolog 2;
Short=hPER2;
AltName: Full=Circadian clock protein PERIOD 2;
Name=PER2; Synonyms=KIAA0347;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Brain;
Ikeda M., Takehara N., Ebisawa T., Yamauchi T., Nomura M.;
"cDNA cloning and characterization of Per2S, an alternatively spliced
human Per2 variant.";
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, AND
INTERACTION WITH CSNK1D.
TISSUE=Brain;
PubMed=11165242; DOI=10.1016/S0014-5793(00)02434-0;
Camacho F., Cilio M., Guo Y., Virshup D.M., Patel K., Khorkova O.,
Styren S., Morse B., Yao Z., Keesler G.A.;
"Human casein kinase Idelta phosphorylation of human circadian clock
proteins period 1 and 2.";
FEBS Lett. 489:159-165(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NHLBI resequencing and genotyping service (RS&G);
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
PubMed=9205841; DOI=10.1093/dnares/4.2.141;
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N.,
Tanaka A., Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. VII.
The complete sequences of 100 new cDNA clones from brain which can
code for large proteins in vitro.";
DNA Res. 4:141-150(1997).
[5]
SEQUENCE REVISION TO C-TERMINUS.
Nagase T., Ishikawa K., Seki N., Nakajima D., Ohira M., Miyajima N.,
Kotani H., Nomura N., Ohara O.;
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
Carpen J.D., Archer S.N., Skene D.J., Smits M., von Schantz M.;
"A single-nucleotide polymorphism in the 5'-untranslated region of the
hPER2 gene is associated with diurnal preference.";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[9]
TISSUE SPECIFICITY.
PubMed=9427249; DOI=10.1016/S0896-6273(00)80417-1;
Shearman L.P., Zylka M.J., Weaver D.R., Kolakowski L.F. Jr.,
Reppert S.M.;
"Two period homologs: circadian expression and photic regulation in
the suprachiasmatic nuclei.";
Neuron 19:1261-1269(1997).
[10]
INDUCTION.
PubMed=14750904; DOI=10.1042/BJ20031308;
Miyazaki K., Nagase T., Mesaki M., Narukawa J., Ohara O., Ishida N.;
"Phosphorylation of clock protein PER1 regulates its circadian
degradation in normal human fibroblasts.";
Biochem. J. 380:95-103(2004).
[11]
SUBCELLULAR LOCATION, AND INTERACTION WITH PML.
PubMed=22274616; DOI=10.1038/emboj.2012.1;
Miki T., Xu Z., Chen-Goodspeed M., Liu M., Van Oort-Jansen A.,
Rea M.A., Zhao Z., Lee C.C., Chang K.S.;
"PML regulates PER2 nuclear localization and circadian function.";
EMBO J. 31:1427-1439(2012).
[12]
ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2),
AND TISSUE SPECIFICITY (ISOFORM 2).
PubMed=24202686; DOI=10.1007/s00018-013-1503-1;
Avitabile D., Genovese L., Ponti D., Ranieri D., Raffa S.,
Calogero A., Torrisi M.R.;
"Nucleolar localization and circadian regulation of Per2S, a novel
splicing variant of the Period 2 gene.";
Cell. Mol. Life Sci. 71:2547-2559(2014).
[13]
REVIEW.
PubMed=23303907; DOI=10.1152/physrev.00016.2012;
Eckel-Mahan K., Sassone-Corsi P.;
"Metabolism and the circadian clock converge.";
Physiol. Rev. 93:107-135(2013).
[14]
REVIEW.
PubMed=23916625; DOI=10.1016/j.tcb.2013.07.002;
Partch C.L., Green C.B., Takahashi J.S.;
"Molecular architecture of the mammalian circadian clock.";
Trends Cell Biol. 24:90-99(2014).
[15]
VARIANT FASPS1 GLY-662, PHOSPHORYLATION AT SER-662, AND MUTAGENESIS OF
SER-662.
PubMed=11232563; DOI=10.1126/science.1057499;
Toh K.L., Jones C.R., He Y., Eide E.J., Hinz W.A., Virshup D.M.,
Ptacek L.J., Fu Y.-H.;
"An hPer2 phosphorylation site mutation in familial advanced sleep
phase syndrome.";
Science 291:1040-1043(2001).
[16]
VARIANT [LARGE SCALE ANALYSIS] VAL-823.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Transcriptional repressor which forms a core component
of the circadian clock. The circadian clock, an internal time-
keeping system, regulates various physiological processes through
the generation of approximately 24 hour circadian rhythms in gene
expression, which are translated into rhythms in metabolism and
behavior. It is derived from the Latin roots 'circa' (about) and
'diem' (day) and acts as an important regulator of a wide array of
physiological functions including metabolism, sleep, body
temperature, blood pressure, endocrine, immune, cardiovascular,
and renal function. Consists of two major components: the central
clock, residing in the suprachiasmatic nucleus (SCN) of the brain,
and the peripheral clocks that are present in nearly every tissue
and organ system. Both the central and peripheral clocks can be
reset by environmental cues, also known as Zeitgebers (German for
'timegivers'). The predominant Zeitgeber for the central clock is
light, which is sensed by retina and signals directly to the SCN.
The central clock entrains the peripheral clocks through neuronal
and hormonal signals, body temperature and feeding-related cues,
aligning all clocks with the external light/dark cycle. Circadian
rhythms allow an organism to achieve temporal homeostasis with its
environment at the molecular level by regulating gene expression
to create a peak of protein expression once every 24 hours to
control when a particular physiological process is most active
with respect to the solar day. Transcription and translation of
core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2,
PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm
generation, whereas delays imposed by post-translational
modifications (PTMs) are important for determining the period
(tau) of the rhythms (tau refers to the period of a rhythm and is
the length, in time, of one complete cycle). A diurnal rhythm is
synchronized with the day/night cycle, while the ultradian and
infradian rhythms have a period shorter and longer than 24 hours,
respectively. Disruptions in the circadian rhythms contribute to
the pathology of cardiovascular diseases, cancer, metabolic
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
inhibiting 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.
{ECO:0000250|UniProtKB:O54943}.
-!- SUBUNIT: 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 and CAVIN3 (By similarity). Interacts with
MAGEL2 (By similarity). {ECO:0000250|UniProtKB:O54943,
ECO:0000269|PubMed:11165242, ECO:0000269|PubMed:22274616}.
-!- INTERACTION:
P48730:CSNK1D; NbExp=3; IntAct=EBI-1054296, EBI-751621;
P49674:CSNK1E; NbExp=4; IntAct=EBI-1054296, EBI-749343;
-!- SUBCELLULAR LOCATION: Isoform 1: Nucleus. Cytoplasm
{ECO:0000250|UniProtKB:O54943}. Cytoplasm, perinuclear region
{ECO:0000250}. 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.
-!- SUBCELLULAR LOCATION: Isoform 2: Nucleus, nucleolus
{ECO:0000269|PubMed:24202686}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O15055-1; Sequence=Displayed;
Name=2; Synonyms=PER2S;
IsoId=O15055-2; Sequence=VSP_021653, VSP_021654;
-!- TISSUE SPECIFICITY: Widely expressed. Found in heart, brain,
placenta, lung, liver, skeleatal muscle, kidney and pancreas. High
levels in skeletal muscle and pancreas. Low levels in lung.
Isoform 2 is expressed in keratinocytes (at protein level).
{ECO:0000269|PubMed:9427249}.
-!- INDUCTION: Oscillates diurnally. 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. {ECO:0000269|PubMed:14750904}.
-!- PTM: Acetylated. Deacetylated by SIRT1, resulting in decreased
protein stability. {ECO:0000250|UniProtKB:O54943}.
-!- PTM: Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results
in PER2 protein degradation. May be dephosphorylated by PP1.
{ECO:0000269|PubMed:11165242, ECO:0000269|PubMed:11232563}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation.
Ubiquitination may be inhibited by CRY1.
{ECO:0000250|UniProtKB:O54943}.
-!- DISEASE: Advanced sleep phase syndrome, familial, 1 (FASPS1)
[MIM:604348]: A disorder characterized by very early sleep onset
and offset. Individuals are 'morning larks' with a 4 hours advance
of the sleep, temperature and melatonin rhythms.
{ECO:0000269|PubMed:11232563}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=BAA20804.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; AB012614; BAA83709.1; -; mRNA.
EMBL; EF015905; ABM64216.1; -; Genomic_DNA.
EMBL; AB002345; BAA20804.2; ALT_INIT; mRNA.
EMBL; AC012485; AAX88976.1; -; Genomic_DNA.
EMBL; CH471063; EAW71155.1; -; Genomic_DNA.
EMBL; AY647991; AAT68170.1; -; Genomic_DNA.
CCDS; CCDS2528.1; -. [O15055-1]
RefSeq; NP_073728.1; NM_022817.2. [O15055-1]
RefSeq; XP_005246168.1; XM_005246111.4. [O15055-1]
RefSeq; XP_006712887.1; XM_006712824.3. [O15055-1]
UniGene; Hs.58756; -.
ProteinModelPortal; O15055; -.
SMR; O15055; -.
BioGrid; 114387; 20.
ComplexPortal; CPX-3219; Cry1-Per2 complex.
ComplexPortal; CPX-3220; Cry-Per2 complex.
DIP; DIP-38051N; -.
IntAct; O15055; 10.
STRING; 9606.ENSP00000254657; -.
BindingDB; O15055; -.
ChEMBL; CHEMBL3751648; -.
iPTMnet; O15055; -.
PhosphoSitePlus; O15055; -.
BioMuta; PER2; -.
EPD; O15055; -.
MaxQB; O15055; -.
PaxDb; O15055; -.
PeptideAtlas; O15055; -.
PRIDE; O15055; -.
ProteomicsDB; 48405; -.
ProteomicsDB; 48406; -. [O15055-2]
DNASU; 8864; -.
Ensembl; ENST00000254657; ENSP00000254657; ENSG00000132326. [O15055-1]
GeneID; 8864; -.
KEGG; hsa:8864; -.
UCSC; uc002vyc.4; human. [O15055-1]
CTD; 8864; -.
DisGeNET; 8864; -.
EuPathDB; HostDB:ENSG00000132326.11; -.
GeneCards; PER2; -.
H-InvDB; HIX0030280; -.
HGNC; HGNC:8846; PER2.
HPA; HPA060510; -.
MalaCards; PER2; -.
MIM; 603426; gene.
MIM; 604348; phenotype.
neXtProt; NX_O15055; -.
OpenTargets; ENSG00000132326; -.
Orphanet; 164736; Familial advanced sleep-phase syndrome.
PharmGKB; PA33185; -.
eggNOG; KOG3753; Eukaryota.
eggNOG; ENOG410Y118; LUCA.
GeneTree; ENSGT00510000046467; -.
HOGENOM; HOG000231111; -.
HOVERGEN; HBG008167; -.
InParanoid; O15055; -.
KO; K02633; -.
OMA; TSHTSKY; -.
OrthoDB; EOG091G00PA; -.
PhylomeDB; O15055; -.
TreeFam; TF318445; -.
Reactome; R-HSA-400253; Circadian Clock.
SIGNOR; O15055; -.
ChiTaRS; PER2; human.
GeneWiki; PER2; -.
GenomeRNAi; 8864; -.
PRO; PR:O15055; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000132326; -.
CleanEx; HS_PER2; -.
ExpressionAtlas; O15055; baseline and differential.
Genevisible; O15055; HS.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0000976; F:transcription regulatory region sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0032922; P:circadian regulation of gene expression; ISS:UniProtKB.
GO; GO:0097167; P:circadian regulation of translation; ISS:UniProtKB.
GO; GO:0007623; P:circadian rhythm; TAS:ProtInc.
GO; GO:0006631; P:fatty acid metabolic process; ISS:UniProtKB.
GO; GO:0006094; P:gluconeogenesis; ISS:UniProtKB.
GO; GO:0005978; P:glycogen biosynthetic process; ISS:UniProtKB.
GO; GO:0070932; P:histone H3 deacetylation; ISS:UniProtKB.
GO; GO:0019249; P:lactate biosynthetic process; ISS:UniProtKB.
GO; GO:0042754; P:negative regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0070345; P:negative regulation of fat cell proliferation; ISS:UniProtKB.
GO; GO:0031397; P:negative regulation of protein ubiquitination; ISS:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
GO; GO:2000678; P:negative regulation of transcription regulatory region DNA binding; ISS:UniProtKB.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
GO; GO:0051946; P:regulation of glutamate uptake involved in transmission of nerve impulse; ISS:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0050767; P:regulation of neurogenesis; ISS:UniProtKB.
GO; GO:0019229; P:regulation of vasoconstriction; ISS:UniProtKB.
GO; GO:0002931; P:response to ischemia; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0050872; P:white fat cell differentiation; ISS:UniProtKB.
CDD; cd00130; PAS; 1.
InterPro; IPR000014; PAS.
InterPro; IPR035965; PAS-like_dom_sf.
InterPro; IPR013655; PAS_fold_3.
InterPro; IPR022728; Period_circadian-like_C.
Pfam; PF08447; PAS_3; 1.
Pfam; PF12114; Period_C; 1.
SMART; SM00091; PAS; 2.
SUPFAM; SSF55785; SSF55785; 1.
PROSITE; PS50112; PAS; 1.
1: Evidence at protein level;
Acetylation; Alternative splicing; Biological rhythms;
Complete proteome; Cytoplasm; Disease mutation; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 1255 Period circadian protein homolog 2.
/FTId=PRO_0000162630.
DOMAIN 181 248 PAS 1. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 321 387 PAS 2. {ECO:0000255|PROSITE-
ProRule:PRU00140}.
DOMAIN 395 438 PAC.
REGION 480 484 Important for protein stability.
{ECO:0000250}.
REGION 557 771 CSNK1E binding domain. {ECO:0000250}.
REGION 888 1071 Interaction with PPARG.
{ECO:0000250|UniProtKB:O54943}.
REGION 1155 1255 CRY binding domain.
{ECO:0000250|UniProtKB:Q9Z301}.
MOTIF 111 120 Nuclear export signal 1.
{ECO:0000250|UniProtKB:O54943}.
MOTIF 308 312 LXXLL.
MOTIF 462 471 Nuclear export signal 2.
{ECO:0000250|UniProtKB:O54943}.
MOTIF 789 805 Nuclear localization signal.
{ECO:0000250|UniProtKB:O54943}.
MOTIF 989 996 Nuclear export signal 3.
{ECO:0000250|UniProtKB:O54943}.
MOTIF 1057 1061 LXXLL.
COMPBIAS 510 513 Poly-Arg.
COMPBIAS 842 979 Pro-rich.
MOD_RES 527 527 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 530 530 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 533 533 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 540 540 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 662 662 Phosphoserine.
{ECO:0000269|PubMed:11232563}.
MOD_RES 696 696 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 700 700 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 714 714 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 766 766 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 771 771 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 945 945 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 977 977 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
MOD_RES 1124 1124 Phosphoserine.
{ECO:0000250|UniProtKB:O54943}.
VAR_SEQ 349 404 RAVPLLGYLPQDLIETPVLVQLHPSDRPLMLAIHKKILQSG
GQPFDYSPIRFRARN -> SPAVRRAAFRLFSHSVSRPERR
VHHVGHQLVQLHQPMEQENLLHHWEAQSQGGPFE (in
isoform 2). {ECO:0000303|Ref.1}.
/FTId=VSP_021653.
VAR_SEQ 405 1255 Missing (in isoform 2).
{ECO:0000303|Ref.1}.
/FTId=VSP_021654.
VARIANT 5 5 A -> S (in dbSNP:rs35572922).
/FTId=VAR_051575.
VARIANT 662 662 S -> G (in FASPS1; reduced in vitro
phosphorylation by CSNK1E;
dbSNP:rs121908635).
{ECO:0000269|PubMed:11232563}.
/FTId=VAR_029080.
VARIANT 729 729 V -> I (in dbSNP:rs4429421).
/FTId=VAR_051576.
VARIANT 823 823 L -> V (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036041.
VARIANT 903 903 V -> I (in dbSNP:rs35333999).
/FTId=VAR_051577.
VARIANT 949 949 F -> Y (in dbSNP:rs35998480).
/FTId=VAR_051578.
VARIANT 1244 1244 G -> E (in dbSNP:rs934945).
/FTId=VAR_024558.
MUTAGEN 662 662 S->D: Restores CSNK1E-dependent
phosphorylation of variant G-662.
{ECO:0000269|PubMed:11232563}.
SEQUENCE 1255 AA; 136579 MW; 2AEF2C6BD4B6CBB0 CRC64;
MNGYAEFPPS PSNPTKEPVE PQPSQVPLQE DVDMSSGSSG HETNENCSTG RDSQGSDCDD
SGKELGMLVE PPDARQSPDT FSLMMAKSEH NPSTSGCSSD QSSKVDTHKE LIKTLKELKV
HLPADKKAKG KASTLATLKY ALRSVKQVKA NEEYYQLLMS SEGHPCGADV PSYTVEEMES
VTSEHIVKNA DMFAVAVSLV SGKILYISDQ VASIFHCKRD AFSDAKFVEF LAPHDVGVFH
SFTSPYKLPL WSMCSGADSF TQECMEEKSF FCRVSVRKSH ENEIRYHPFR MTPYLVKVRD
QQGAESQLCC LLLAERVHSG YEAPRIPPEK RIFTTTHTPN CLFQDVDERA VPLLGYLPQD
LIETPVLVQL HPSDRPLMLA IHKKILQSGG QPFDYSPIRF RARNGEYITL DTSWSSFINP
WSRKISFIIG RHKVRVGPLN EDVFAAHPCT EEKALHPSIQ ELTEQIHRLL LQPVPHSGSS
GYGSLGSNGS HEHLMSQTSS SDSNGHEDSR RRRAEICKNG NKTKNRSHYS HESGEQKKKS
VTEMQTNPPA EKKAVPAMEK DSLGVSFPEE LACKNQPTCS YQQISCLDSV IRYLESCNEA
ATLKRKCEFP ANVPALRSSD KRKATVSPGP HAGEAEPPSR VNSRTGVGTH LTSLALPGKA
ESVASLTSQC SYSSTIVHVG DKKPQPELEM VEDAASGPES LDCLAGPALA CGLSQEKEPF
KKLGLTKEVL AAHTQKEEQS FLQKFKEIRK LSIFQSHCHY YLQERSKGQP SERTAPGLRN
TSGIDSPWKK TGKNRKLKSK RVKPRDSSES TGSGGPVSAR PPLVGLNATA WSPSDTSQSS
CPAVPFPAPV PAAYSLPVFP APGTVAAPPA PPHASFTVPA VPVDLQHQFA VQPPPFPAPL
APVMAFMLPS YSFPSGTPNL PQAFFPSQPQ FPSHPTLTSE MASASQPEFP SRTSIPRQPC
ACPATRATPP SAMGRASPPL FQSRSSSPLQ LNLLQLEEAP EGGTGAMGTT GATETAAVGA
DCKPGTSRDQ QPKAPLTRDE PSDTQNSDAL STSSGLLNLL LNEDLCSASG SAASESLGSG
SLGCDASPSG AGSSDTSHTS KYFGSIDSSE NNHKAKMNTG MEESEHFIKC VLQDPIWLLM
ADADSSVMMT YQLPSRNLEA VLKEDREKLK LLQKLQPRFT ESQKQELREV HQWMQTGGLP
AAIDVAECVY CENKEKGNIC IPYEEDIPSL GLSEVSDTKE DENGSPLNHR IEEQT


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