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O15055

- PER2_HUMAN

UniProt

O15055 - PER2_HUMAN

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Protein

Period circadian protein homolog 2

Gene

PER2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndrome and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. PER1 and PER2 proteins transport CRY1 and CRY2 into the nucleus with appropriate circadian timing, but also contribute directly to repression of clock-controlled target genes through interaction with several classes of RNA-binding proteins, helicases and others transcriptional repressors. PER appears to regulate circadian control of transcription by at least three different modes. First, interacts directly with the CLOCK-ARTNL/BMAL1 at the tail end of the nascent transcript peak to recruit complexes containing the SIN3-HDAC that remodel chromatin to repress transcription. Second, brings H3K9 methyltransferases such as SUV39H1 and SUV39H2 to the E-box elements of the circadian target genes, like PER2 itself or PER1. The recruitment of each repressive modifier to the DNA seems to be very precisely temporally orchestrated by the large PER complex, the deacetylases acting before than the methyltransferases. Additionally, large PER complexes are also recruited to the target genes 3' termination site through interactions with RNA-binding proteins and helicases that may play a role in transcription termination to regulate transcription independently of CLOCK-ARTNL/BMAL1 interactions. Recruitment of large PER complexes to the elongating polymerase at PER and CRY termination sites inhibited SETX action, impeding RNA polymerase II release and thereby repressing transcriptional reinitiation. May propagate clock information to metabolic pathways via the interaction with nuclear receptors. Coactivator of PPARA and corepressor of NR1D1, binds rhythmically at the promoter of nuclear receptors target genes like ARNTL or G6PC. Directly and specifically represses PPARG proadipogenic activity by blocking PPARG recruitment to target promoters and thereby 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.By similarity

GO - Molecular functioni

  1. pre-mRNA binding Source: Ensembl
  2. signal transducer activity Source: InterPro
  3. transcription coactivator activity Source: UniProtKB
  4. transcription factor binding transcription factor activity Source: BHF-UCL
  5. transcription regulatory region sequence-specific DNA binding Source: UniProtKB
  6. ubiquitin binding Source: UniProtKB

GO - Biological processi

  1. circadian regulation of gene expression Source: UniProtKB
  2. circadian regulation of translation Source: UniProtKB
  3. circadian rhythm Source: ProtInc
  4. fatty acid metabolic process Source: UniProtKB
  5. gluconeogenesis Source: UniProtKB
  6. glycogen biosynthetic process Source: UniProtKB
  7. histone H3 deacetylation Source: UniProtKB
  8. lactate biosynthetic process Source: UniProtKB
  9. negative regulation of circadian rhythm Source: UniProtKB
  10. negative regulation of DNA-templated transcription, termination Source: Ensembl
  11. negative regulation of fat cell proliferation Source: UniProtKB
  12. negative regulation of protein ubiquitination Source: UniProtKB
  13. negative regulation of transcription, DNA-templated Source: UniProtKB
  14. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  15. negative regulation of transcription regulatory region DNA binding Source: UniProtKB
  16. regulation of cell cycle Source: UniProtKB
  17. regulation of circadian rhythm Source: UniProtKB
  18. regulation of glutamate uptake involved in transmission of nerve impulse Source: UniProtKB
  19. regulation of insulin secretion Source: UniProtKB
  20. regulation of neurogenesis Source: UniProtKB
  21. regulation of vasoconstriction Source: UniProtKB
  22. response to ischemia Source: UniProtKB
  23. transcription, DNA-templated Source: UniProtKB-KW
  24. white fat cell differentiation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Biological rhythms, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_24941. Circadian Clock.

Names & Taxonomyi

Protein namesi
Recommended name:
Period circadian protein homolog 2
Short name:
hPER2
Alternative name(s):
Circadian clock protein PERIOD 2
Gene namesi
Name:PER2
Synonyms:KIAA0347
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:8846. PER2.

Subcellular locationi

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.
Isoform 2 : Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleus Source: UniProtKB
  3. perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti662 – 6621S → G in FASPS1; reduced in vitro phosphorylation by CSNK1E. 1 Publication
VAR_029080

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi662 – 6621S → D: Restores CSNK1E-dependent phosphorylation of variant G-662. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi604348. phenotype.
Orphaneti164736. Familial advanced sleep-phase syndrome.
PharmGKBiPA33185.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12551255Period circadian protein homolog 2PRO_0000162630Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei527 – 5271PhosphoserineBy similarity
Modified residuei530 – 5301PhosphoserineBy similarity
Modified residuei533 – 5331PhosphoserineBy similarity
Modified residuei540 – 5401PhosphoserineBy similarity
Modified residuei662 – 6621Phosphoserine1 Publication
Modified residuei696 – 6961PhosphoserineBy similarity
Modified residuei700 – 7001PhosphoserineBy similarity
Modified residuei714 – 7141PhosphoserineBy similarity
Modified residuei766 – 7661PhosphoserineBy similarity
Modified residuei771 – 7711PhosphoserineBy similarity
Modified residuei945 – 9451PhosphoserineBy similarity
Modified residuei977 – 9771PhosphoserineBy similarity
Modified residuei1124 – 11241PhosphoserineBy similarity

Post-translational modificationi

Acetylated. Deacetylated by SIRT1, resulting in decreased protein stabilty.By similarity
Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation. May be dephosphorylated by PP1.2 Publications
Ubiquitinated, leading to its proteasomal degradation. Ubiquitination may be inhibited by CRY1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO15055.
PaxDbiO15055.
PRIDEiO15055.

PTM databases

PhosphoSiteiO15055.

Expressioni

Tissue specificityi

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).1 Publication

Inductioni

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.1 Publication

Gene expression databases

BgeeiO15055.
CleanExiHS_PER2.
ExpressionAtlasiO15055. baseline and differential.
GenevestigatoriO15055.

Organism-specific databases

HPAiHPA053136.

Interactioni

Subunit structurei

Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARTNL/BMAL1 or ARTNL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts with CLOCK-ARNTL/BMAL1 (off DNA).Interacts with ARNTL2/BMAL2. Interacts directly with PER1 and PER3, and through a C-terminal domain, with CRY1 and CRY2. Interacts, via its second PAS domain, with TIMELESS in vitro. Interacts with NFIL3. Different large complexes have been identified with different repressive functions. The core of PER complexes is composed of at least PER1, PER2, PER3, CRY1, CRY2, CSNK1D and/or CSNK1E. The large PER complex involved in the repression of transcriptional termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1 and POLR2A (active). The large PER complex involved in the histone deacetylation is composed of at least HDAC1, PER2, SFPQ and SIN3A. The large PER complex involved in the histone methylation is composed of at least PER2, CBX3, TRIM28, SUV39H1 and/or SUV39H2; CBX3 mediates the formation of the complex. Interacts with SETX; the interaction inhibits termination of circadian target genes. Interacts with the nuclear receptors HNF4A, NR1D1, NR4A2, RORA, PPARA, PPARG and THRA; the interaction with at least PPARG is ligand dependent. Interacts with PML. Interacts (phosphorylated) with BTRC and FBXW11; the interactions trigger proteasomal degradation. Interacts with NONO and SFPQ. Interacts with SIRT1 (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi114387. 13 interactions.
DIPiDIP-38051N.
IntActiO15055. 2 interactions.
STRINGi9606.ENSP00000254657.

Structurei

3D structure databases

ProteinModelPortaliO15055.
SMRiO15055. Positions 115-475, 1131-1212.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini181 – 24868PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini321 – 38767PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini395 – 43844PACAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni480 – 4845Important for protein stabilityBy similarity
Regioni557 – 771215CSNK1E binding domainBy similarityAdd
BLAST
Regioni888 – 1071184Interaction with PPARGBy similarityAdd
BLAST
Regioni1155 – 1255101CRY binding domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi111 – 12010Nuclear export signal 1By similarity
Motifi308 – 3125LXXLL
Motifi462 – 47110Nuclear export signal 2By similarity
Motifi789 – 80517Nuclear localization signalBy similarityAdd
BLAST
Motifi989 – 9968Nuclear export signal 3By similarity
Motifi1057 – 10615LXXLL

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi510 – 5134Poly-Arg
Compositional biasi842 – 979138Pro-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG253593.
GeneTreeiENSGT00510000046467.
HOGENOMiHOG000231111.
HOVERGENiHBG008167.
InParanoidiO15055.
KOiK02633.
OMAiNATAWSP.
OrthoDBiEOG78SQH2.
PhylomeDBiO15055.
TreeFamiTF318445.

Family and domain databases

InterProiIPR001610. PAC.
IPR000014. PAS.
IPR022728. Period_circadian-like_C.
[Graphical view]
PfamiPF12114. Period_C. 1 hit.
[Graphical view]
SMARTiSM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]
SUPFAMiSSF55785. SSF55785. 1 hit.
PROSITEiPS50112. PAS. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O15055-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MNGYAEFPPS PSNPTKEPVE PQPSQVPLQE DVDMSSGSSG HETNENCSTG
60 70 80 90 100
RDSQGSDCDD SGKELGMLVE PPDARQSPDT FSLMMAKSEH NPSTSGCSSD
110 120 130 140 150
QSSKVDTHKE LIKTLKELKV HLPADKKAKG KASTLATLKY ALRSVKQVKA
160 170 180 190 200
NEEYYQLLMS SEGHPCGADV PSYTVEEMES VTSEHIVKNA DMFAVAVSLV
210 220 230 240 250
SGKILYISDQ VASIFHCKRD AFSDAKFVEF LAPHDVGVFH SFTSPYKLPL
260 270 280 290 300
WSMCSGADSF TQECMEEKSF FCRVSVRKSH ENEIRYHPFR MTPYLVKVRD
310 320 330 340 350
QQGAESQLCC LLLAERVHSG YEAPRIPPEK RIFTTTHTPN CLFQDVDERA
360 370 380 390 400
VPLLGYLPQD LIETPVLVQL HPSDRPLMLA IHKKILQSGG QPFDYSPIRF
410 420 430 440 450
RARNGEYITL DTSWSSFINP WSRKISFIIG RHKVRVGPLN EDVFAAHPCT
460 470 480 490 500
EEKALHPSIQ ELTEQIHRLL LQPVPHSGSS GYGSLGSNGS HEHLMSQTSS
510 520 530 540 550
SDSNGHEDSR RRRAEICKNG NKTKNRSHYS HESGEQKKKS VTEMQTNPPA
560 570 580 590 600
EKKAVPAMEK DSLGVSFPEE LACKNQPTCS YQQISCLDSV IRYLESCNEA
610 620 630 640 650
ATLKRKCEFP ANVPALRSSD KRKATVSPGP HAGEAEPPSR VNSRTGVGTH
660 670 680 690 700
LTSLALPGKA ESVASLTSQC SYSSTIVHVG DKKPQPELEM VEDAASGPES
710 720 730 740 750
LDCLAGPALA CGLSQEKEPF KKLGLTKEVL AAHTQKEEQS FLQKFKEIRK
760 770 780 790 800
LSIFQSHCHY YLQERSKGQP SERTAPGLRN TSGIDSPWKK TGKNRKLKSK
810 820 830 840 850
RVKPRDSSES TGSGGPVSAR PPLVGLNATA WSPSDTSQSS CPAVPFPAPV
860 870 880 890 900
PAAYSLPVFP APGTVAAPPA PPHASFTVPA VPVDLQHQFA VQPPPFPAPL
910 920 930 940 950
APVMAFMLPS YSFPSGTPNL PQAFFPSQPQ FPSHPTLTSE MASASQPEFP
960 970 980 990 1000
SRTSIPRQPC ACPATRATPP SAMGRASPPL FQSRSSSPLQ LNLLQLEEAP
1010 1020 1030 1040 1050
EGGTGAMGTT GATETAAVGA DCKPGTSRDQ QPKAPLTRDE PSDTQNSDAL
1060 1070 1080 1090 1100
STSSGLLNLL LNEDLCSASG SAASESLGSG SLGCDASPSG AGSSDTSHTS
1110 1120 1130 1140 1150
KYFGSIDSSE NNHKAKMNTG MEESEHFIKC VLQDPIWLLM ADADSSVMMT
1160 1170 1180 1190 1200
YQLPSRNLEA VLKEDREKLK LLQKLQPRFT ESQKQELREV HQWMQTGGLP
1210 1220 1230 1240 1250
AAIDVAECVY CENKEKGNIC IPYEEDIPSL GLSEVSDTKE DENGSPLNHR

IEEQT
Length:1,255
Mass (Da):136,579
Last modified:July 11, 2001 - v2
Checksum:i2AEF2C6BD4B6CBB0
GO
Isoform 2 (identifier: O15055-2) [UniParc]FASTAAdd to Basket

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.

Show »
Length:404
Mass (Da):45,175
Checksum:iB6DED6DD2AC3F971
GO

Sequence cautioni

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51A → S.
Corresponds to variant rs35572922 [ dbSNP | Ensembl ].
VAR_051575
Natural varianti662 – 6621S → G in FASPS1; reduced in vitro phosphorylation by CSNK1E. 1 Publication
VAR_029080
Natural varianti729 – 7291V → I.
Corresponds to variant rs4429421 [ dbSNP | Ensembl ].
VAR_051576
Natural varianti823 – 8231L → V in a breast cancer sample; somatic mutation. 1 Publication
VAR_036041
Natural varianti903 – 9031V → I.
Corresponds to variant rs35333999 [ dbSNP | Ensembl ].
VAR_051577
Natural varianti949 – 9491F → Y.
Corresponds to variant rs35998480 [ dbSNP | Ensembl ].
VAR_051578
Natural varianti1244 – 12441G → E.
Corresponds to variant rs934945 [ dbSNP | Ensembl ].
VAR_024558

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei349 – 40456RAVPL…FRARN → SPAVRRAAFRLFSHSVSRPE RRVHHVGHQLVQLHQPMEQE NLLHHWEAQSQGGPFE in isoform 2. 1 PublicationVSP_021653Add
BLAST
Alternative sequencei405 – 1255851Missing in isoform 2. 1 PublicationVSP_021654Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS2528.1. [O15055-1]
RefSeqiNP_073728.1. NM_022817.2. [O15055-1]
XP_005246168.1. XM_005246111.2. [O15055-1]
XP_006712887.1. XM_006712824.1. [O15055-1]
UniGeneiHs.58756.

Genome annotation databases

EnsembliENST00000254657; ENSP00000254657; ENSG00000132326. [O15055-1]
ENST00000355768; ENSP00000348013; ENSG00000132326. [O15055-2]
GeneIDi8864.
KEGGihsa:8864.
UCSCiuc002vyc.3. human. [O15055-1]
uc010fyx.1. human. [O15055-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS2528.1. [O15055-1 ]
RefSeqi NP_073728.1. NM_022817.2. [O15055-1 ]
XP_005246168.1. XM_005246111.2. [O15055-1 ]
XP_006712887.1. XM_006712824.1. [O15055-1 ]
UniGenei Hs.58756.

3D structure databases

ProteinModelPortali O15055.
SMRi O15055. Positions 115-475, 1131-1212.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114387. 13 interactions.
DIPi DIP-38051N.
IntActi O15055. 2 interactions.
STRINGi 9606.ENSP00000254657.

PTM databases

PhosphoSitei O15055.

Proteomic databases

MaxQBi O15055.
PaxDbi O15055.
PRIDEi O15055.

Protocols and materials databases

DNASUi 8864.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000254657 ; ENSP00000254657 ; ENSG00000132326 . [O15055-1 ]
ENST00000355768 ; ENSP00000348013 ; ENSG00000132326 . [O15055-2 ]
GeneIDi 8864.
KEGGi hsa:8864.
UCSCi uc002vyc.3. human. [O15055-1 ]
uc010fyx.1. human. [O15055-2 ]

Organism-specific databases

CTDi 8864.
GeneCardsi GC02M239206.
H-InvDB HIX0030280.
HGNCi HGNC:8846. PER2.
HPAi HPA053136.
MIMi 603426. gene.
604348. phenotype.
neXtProti NX_O15055.
Orphaneti 164736. Familial advanced sleep-phase syndrome.
PharmGKBi PA33185.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253593.
GeneTreei ENSGT00510000046467.
HOGENOMi HOG000231111.
HOVERGENi HBG008167.
InParanoidi O15055.
KOi K02633.
OMAi NATAWSP.
OrthoDBi EOG78SQH2.
PhylomeDBi O15055.
TreeFami TF318445.

Enzyme and pathway databases

Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
REACT_24941. Circadian Clock.

Miscellaneous databases

GeneWikii PER2.
GenomeRNAii 8864.
NextBioi 33285.
PROi O15055.
SOURCEi Search...

Gene expression databases

Bgeei O15055.
CleanExi HS_PER2.
ExpressionAtlasi O15055. baseline and differential.
Genevestigatori O15055.

Family and domain databases

InterProi IPR001610. PAC.
IPR000014. PAS.
IPR022728. Period_circadian-like_C.
[Graphical view ]
Pfami PF12114. Period_C. 1 hit.
[Graphical view ]
SMARTi SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view ]
SUPFAMi SSF55785. SSF55785. 1 hit.
PROSITEi PS50112. PAS. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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. 71:2547-2559(2014) [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. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-823.

Entry informationi

Entry nameiPER2_HUMAN
AccessioniPrimary (citable) accession number: O15055
Secondary accession number(s): A2I2P7
, Q4ZG49, Q6DT41, Q9UQ45
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: July 11, 2001
Last modified: October 29, 2014
This is version 140 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3