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O15055 (PER2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Period circadian protein homolog 2

Short name=hPER2
Alternative name(s):
Circadian clock protein PERIOD 2
Gene names
Name:PER2
Synonyms:KIAA0347
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1255 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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, NR1D2, RORA, RORB and RORG, 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.

Subunit structure

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 of the 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. Ref.2 Ref.12

Subcellular location

Isoform 1: Nucleus. Cytoplasm By similarity. Cytoplasmperinuclear region By similarity. 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. Ref.12 Ref.13

Isoform 2: Nucleusnucleolus Ref.12 Ref.13.

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). Ref.9 Ref.13

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. Ref.10

Post-translational modification

Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation. May be dephosphorylated by PP1. Ref.2 Ref.16

Ubiquitinated, leading to its proteasomal degradation. Ubiquitination may be inhibit by CRY1 By similarity.

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Contains 1 PAC (PAS-associated C-terminal) domain.

Contains 2 PAS (PER-ARNT-SIM) domains.

Sequence caution

The sequence BAA20804.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processBiological rhythms
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
   PTMPhosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcircadian regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

circadian regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

circadian rhythm

Traceable author statement Ref.9. Source: ProtInc

fatty acid metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

gluconeogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

glycogen biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3 deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

lactate biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of fat cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription regulatory region DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of glutamate uptake involved in transmission of nerve impulse

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of insulin secretion

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of neurogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of vasoconstriction

Inferred from sequence or structural similarity. Source: UniProtKB

response to ischemia

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

white fat cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay. Source: HPA

nucleus

Inferred from direct assay Ref.12. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionprotein binding

Inferred from physical interaction Ref.12. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

transcription coactivator activity

Inferred from sequence or structural similarity. Source: UniProtKB

transcription factor binding transcription factor activity

Inferred from sequence or structural similarity. Source: BHF-UCL

transcription regulatory region sequence-specific DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O15055-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O15055-2)

Also known as: PER2S;

The sequence of this isoform differs from the canonical sequence as follows:
     349-404: RAVPLLGYLP...YSPIRFRARN → SPAVRRAAFR...EAQSQGGPFE
     405-1255: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12551255Period circadian protein homolog 2
PRO_0000162630

Regions

Domain181 – 24868PAS 1
Domain321 – 38767PAS 2
Domain395 – 43844PAC
Region480 – 4845Important for protein stability By similarity
Region557 – 771215CSNK1E binding domain By similarity
Region888 – 1071184Interaction with PPARG By similarity
Region1155 – 1255101CRY binding domain By similarity
Motif111 – 12010Nuclear export signal 1 By similarity
Motif308 – 3125LXXLL
Motif462 – 47110Nuclear export signal 3 By similarity
Motif789 – 80517Nuclear localization signal By similarity
Motif989 – 9968Nuclear export signal 2 By similarity
Motif1057 – 10615LXXLL
Compositional bias510 – 5134Poly-Arg
Compositional bias842 – 979138Pro-rich

Amino acid modifications

Modified residue5271Phosphoserine By similarity
Modified residue5301Phosphoserine By similarity
Modified residue5331Phosphoserine By similarity
Modified residue5401Phosphoserine By similarity
Modified residue6621Phosphoserine Ref.16
Modified residue6961Phosphoserine By similarity
Modified residue7001Phosphoserine By similarity
Modified residue7141Phosphoserine By similarity
Modified residue7661Phosphoserine By similarity
Modified residue7711Phosphoserine By similarity
Modified residue9451Phosphoserine By similarity
Modified residue9771Phosphoserine By similarity
Modified residue11241Phosphoserine By similarity

Natural variations

Alternative sequence349 – 40456RAVPL…FRARN → SPAVRRAAFRLFSHSVSRPE RRVHHVGHQLVQLHQPMEQE NLLHHWEAQSQGGPFE in isoform 2.
VSP_021653
Alternative sequence405 – 1255851Missing in isoform 2.
VSP_021654
Natural variant51A → S.
Corresponds to variant rs35572922 [ dbSNP | Ensembl ].
VAR_051575
Natural variant6621S → G in FASPS1; reduced in vitro phosphorylation by CSNK1E. Ref.16
VAR_029080
Natural variant7291V → I.
Corresponds to variant rs4429421 [ dbSNP | Ensembl ].
VAR_051576
Natural variant8231L → V in a breast cancer sample; somatic mutation. Ref.17
VAR_036041
Natural variant9031V → I.
Corresponds to variant rs35333999 [ dbSNP | Ensembl ].
VAR_051577
Natural variant9491F → Y.
Corresponds to variant rs35998480 [ dbSNP | Ensembl ].
VAR_051578
Natural variant12441G → E.
Corresponds to variant rs934945 [ dbSNP | Ensembl ].
VAR_024558

Experimental info

Mutagenesis6621S → D: Restores CSNK1E-dependent phosphorylation of variant G-662. Ref.16

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 11, 2001. Version 2.
Checksum: 2AEF2C6BD4B6CBB0

FASTA1,255136,579
        10         20         30         40         50         60 
MNGYAEFPPS PSNPTKEPVE PQPSQVPLQE DVDMSSGSSG HETNENCSTG RDSQGSDCDD 

        70         80         90        100        110        120 
SGKELGMLVE PPDARQSPDT FSLMMAKSEH NPSTSGCSSD QSSKVDTHKE LIKTLKELKV 

       130        140        150        160        170        180 
HLPADKKAKG KASTLATLKY ALRSVKQVKA NEEYYQLLMS SEGHPCGADV PSYTVEEMES 

       190        200        210        220        230        240 
VTSEHIVKNA DMFAVAVSLV SGKILYISDQ VASIFHCKRD AFSDAKFVEF LAPHDVGVFH 

       250        260        270        280        290        300 
SFTSPYKLPL WSMCSGADSF TQECMEEKSF FCRVSVRKSH ENEIRYHPFR MTPYLVKVRD 

       310        320        330        340        350        360 
QQGAESQLCC LLLAERVHSG YEAPRIPPEK RIFTTTHTPN CLFQDVDERA VPLLGYLPQD 

       370        380        390        400        410        420 
LIETPVLVQL HPSDRPLMLA IHKKILQSGG QPFDYSPIRF RARNGEYITL DTSWSSFINP 

       430        440        450        460        470        480 
WSRKISFIIG RHKVRVGPLN EDVFAAHPCT EEKALHPSIQ ELTEQIHRLL LQPVPHSGSS 

       490        500        510        520        530        540 
GYGSLGSNGS HEHLMSQTSS SDSNGHEDSR RRRAEICKNG NKTKNRSHYS HESGEQKKKS 

       550        560        570        580        590        600 
VTEMQTNPPA EKKAVPAMEK DSLGVSFPEE LACKNQPTCS YQQISCLDSV IRYLESCNEA 

       610        620        630        640        650        660 
ATLKRKCEFP ANVPALRSSD KRKATVSPGP HAGEAEPPSR VNSRTGVGTH LTSLALPGKA 

       670        680        690        700        710        720 
ESVASLTSQC SYSSTIVHVG DKKPQPELEM VEDAASGPES LDCLAGPALA CGLSQEKEPF 

       730        740        750        760        770        780 
KKLGLTKEVL AAHTQKEEQS FLQKFKEIRK LSIFQSHCHY YLQERSKGQP SERTAPGLRN 

       790        800        810        820        830        840 
TSGIDSPWKK TGKNRKLKSK RVKPRDSSES TGSGGPVSAR PPLVGLNATA WSPSDTSQSS 

       850        860        870        880        890        900 
CPAVPFPAPV PAAYSLPVFP APGTVAAPPA PPHASFTVPA VPVDLQHQFA VQPPPFPAPL 

       910        920        930        940        950        960 
APVMAFMLPS YSFPSGTPNL PQAFFPSQPQ FPSHPTLTSE MASASQPEFP SRTSIPRQPC 

       970        980        990       1000       1010       1020 
ACPATRATPP SAMGRASPPL FQSRSSSPLQ LNLLQLEEAP EGGTGAMGTT GATETAAVGA 

      1030       1040       1050       1060       1070       1080 
DCKPGTSRDQ QPKAPLTRDE PSDTQNSDAL STSSGLLNLL LNEDLCSASG SAASESLGSG 

      1090       1100       1110       1120       1130       1140 
SLGCDASPSG AGSSDTSHTS KYFGSIDSSE NNHKAKMNTG MEESEHFIKC VLQDPIWLLM 

      1150       1160       1170       1180       1190       1200 
ADADSSVMMT YQLPSRNLEA VLKEDREKLK LLQKLQPRFT ESQKQELREV HQWMQTGGLP 

      1210       1220       1230       1240       1250 
AAIDVAECVY CENKEKGNIC IPYEEDIPSL GLSEVSDTKE DENGSPLNHR IEEQT 

« Hide

Isoform 2 (PER2S) [UniParc].

Checksum: B6DED6DD2AC3F971
Show »

FASTA40445,175

References

« Hide 'large scale' references
[1]"cDNA cloning and characterization of Per2S, an alternatively spliced human Per2 variant."
Ikeda M., Takehara N., Ebisawa T., Yamauchi T., Nomura M.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Brain.
[2]"Human casein kinase Idelta phosphorylation of human circadian clock proteins period 1 and 2."
Camacho F., Cilio M., Guo Y., Virshup D.M., Patel K., Khorkova O., Styren S., Morse B., Yao Z., Keesler G.A.
FEBS Lett. 489:159-165(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PHOSPHORYLATION, INTERACTION WITH CSNK1D.
Tissue: Brain.
[3]NHLBI resequencing and genotyping service (RS&G)
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]"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."
Nagase T., Ishikawa K., Nakajima D., Ohira M., Seki N., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 4:141-150(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]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
Cited for: SEQUENCE REVISION TO C-TERMINUS.
[6]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
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. expand/collapse author list , 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.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]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. expand/collapse author list , 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
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"A single-nucleotide polymorphism in the 5'-untranslated region of the hPER2 gene is associated with diurnal preference."
Carpen J.D., Archer S.N., Skene D.J., Smits M., von Schantz M.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-65.
[9]"Two period homologs: circadian expression and photic regulation in the suprachiasmatic nuclei."
Shearman L.P., Zylka M.J., Weaver D.R., Kolakowski L.F. Jr., Reppert S.M.
Neuron 19:1261-1269(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: TISSUE SPECIFICITY.
[10]"Phosphorylation of clock protein PER1 regulates its circadian degradation in normal human fibroblasts."
Miyazaki K., Nagase T., Mesaki M., Narukawa J., Ohara O., Ishida N.
Biochem. J. 380:95-103(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"PML regulates PER2 nuclear localization and circadian function."
Miki T., Xu Z., Chen-Goodspeed M., Liu M., Van Oort-Jansen A., Rea M.A., Zhao Z., Lee C.C., Chang K.S.
EMBO J. 31:1427-1439(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH PML.
[13]"Nucleolar localization and circadian regulation of Per2S, a novel splicing variant of the Period 2 gene."
Avitabile D., Genovese L., Ponti D., Ranieri D., Raffa S., Calogero A., Torrisi M.R.
Cell. Mol. Life Sci. 0:0-0(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION (ISOFORM 2), TISSUE SPECIFICITY (ISOFORM 2).
[14]"Metabolism and the circadian clock converge."
Eckel-Mahan K., Sassone-Corsi P.
Physiol. Rev. 93:107-135(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[15]"Molecular architecture of the mammalian circadian clock."
Partch C.L., Green C.B., Takahashi J.S.
Trends Cell Biol. 24:90-99(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[16]"An hPer2 phosphorylation site mutation in familial advanced sleep phase syndrome."
Toh K.L., Jones C.R., He Y., Eide E.J., Hinz W.A., Virshup D.M., Ptacek L.J., Fu Y.-H.
Science 291:1040-1043(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FASPS1 GLY-662, PHOSPHORYLATION AT SER-662, MUTAGENESIS OF SER-662.
[17]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-823.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB012614 mRNA. Translation: BAA83709.1.
EF015905 Genomic DNA. Translation: ABM64216.1.
AB002345 mRNA. Translation: BAA20804.2. Different initiation.
AC012485 Genomic DNA. Translation: AAX88976.1.
CH471063 Genomic DNA. Translation: EAW71155.1.
AY647991 Genomic DNA. Translation: AAT68170.1.
CCDSCCDS2528.1. [O15055-1]
RefSeqNP_073728.1. NM_022817.2. [O15055-1]
XP_005246168.1. XM_005246111.2. [O15055-1]
XP_006712887.1. XM_006712824.1. [O15055-1]
UniGeneHs.58756.

3D structure databases

ProteinModelPortalO15055.
SMRO15055. Positions 115-475.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114387. 10 interactions.
DIPDIP-38051N.
IntActO15055. 2 interactions.
STRING9606.ENSP00000254657.

PTM databases

PhosphoSiteO15055.

Proteomic databases

MaxQBO15055.
PaxDbO15055.
PRIDEO15055.

Protocols and materials databases

DNASU8864.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000254657; ENSP00000254657; ENSG00000132326. [O15055-1]
ENST00000254658; ENSP00000254658; ENSG00000132326. [O15055-2]
ENST00000355768; ENSP00000348013; ENSG00000132326. [O15055-2]
GeneID8864.
KEGGhsa:8864.
UCSCuc002vyc.3. human. [O15055-1]
uc010fyx.1. human. [O15055-2]

Organism-specific databases

CTD8864.
GeneCardsGC02M239188.
H-InvDBHIX0030280.
HGNCHGNC:8846. PER2.
HPAHPA053136.
MIM603426. gene.
604348. phenotype.
neXtProtNX_O15055.
Orphanet164736. Familial advanced sleep-phase syndrome.
PharmGKBPA33185.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253593.
HOGENOMHOG000231111.
HOVERGENHBG008167.
InParanoidO15055.
KOK02633.
OMANATAWSP.
OrthoDBEOG78SQH2.
PhylomeDBO15055.
TreeFamTF318445.

Enzyme and pathway databases

ReactomeREACT_24941. Circadian Clock.

Gene expression databases

ArrayExpressO15055.
BgeeO15055.
CleanExHS_PER2.
GenevestigatorO15055.

Family and domain databases

InterProIPR001610. PAC.
IPR000014. PAS.
IPR022728. Period_circadian-like_C.
[Graphical view]
PfamPF12114. Period_C. 1 hit.
[Graphical view]
SMARTSM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMSSF55785. SSF55785. 1 hit.
PROSITEPS50112. PAS. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPER2.
GenomeRNAi8864.
NextBio33285.
PROO15055.
SOURCESearch...

Entry information

Entry namePER2_HUMAN
AccessionPrimary (citable) accession number: O15055
Secondary accession number(s): A2I2P7 expand/collapse secondary AC list , Q4ZG49, Q6DT41, Q9UQ45
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 11, 2001
Last modified: July 9, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM