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O15534

- PER1_HUMAN

UniProt

O15534 - PER1_HUMAN

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Protein

Period circadian protein homolog 1

Gene

PER1

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 syndromes 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. Regulates circadian target genes expression at post-transcriptional levels, but may not be required for the repression at transcriptional level. Controls PER2 protein decay. Represses CRY2 preventing its repression on CLOCK/ARNTL target genes such as FXYD5 and SCNN1A in kidney and PPARA in liver. Besides its involvement in the maintenance of the circadian clock, has an important function in the regulation of several processes. Participates in the repression of glucocorticoid receptor NR3C1/GR-induced transcriptional activity by reducing the association of NR3C1/GR to glucocorticoid response elements (GREs) by ARNTL:CLOCK. Plays a role in the modulation of the neuroinflammatory state via the regulation of inflammatory mediators release, such as CCL2 and IL6. In spinal astrocytes, negatively regulates the MAPK14/p38 and MAPK8/JNK MAPK cascades as well as the subsequent activation of NFkappaB. Coordinately regulates the expression of multiple genes that are involved in the regulation of renal sodium reabsorption. Can act as gene expression activator in a gene and tissue specific manner, in kidney enhances WNK1 and SLC12A3 expression in collaboration with CLOCK. Modulates hair follicle cycling. Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1.1 Publication

GO - Molecular functioni

  1. chromatin DNA binding Source: UniProtKB
  2. E-box binding Source: BHF-UCL
  3. kinase binding Source: UniProtKB
  4. RNA polymerase II core promoter proximal region sequence-specific DNA binding Source: BHF-UCL
  5. signal transducer activity Source: InterPro
  6. transcription factor binding transcription factor activity Source: BHF-UCL
  7. ubiquitin protein ligase 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: UniProtKB
  4. entrainment of circadian clock Source: ProtInc
  5. entrainment of circadian clock by photoperiod Source: UniProtKB
  6. histone H3 acetylation Source: UniProtKB
  7. histone H3 deacetylation Source: UniProtKB
  8. histone H4 acetylation Source: UniProtKB
  9. negative regulation of glucocorticoid receptor signaling pathway Source: UniProtKB
  10. negative regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
  11. negative regulation of JNK cascade Source: UniProtKB
  12. negative regulation of transcription, DNA-templated Source: UniProtKB
  13. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  14. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  15. posttranscriptional regulation of gene expression Source: UniProtKB
  16. regulation of circadian rhythm Source: UniProtKB
  17. regulation of cytokine production involved in inflammatory response Source: UniProtKB
  18. regulation of hair cycle Source: UniProtKB
  19. regulation of p38MAPK cascade Source: UniProtKB
  20. regulation of sodium ion transport Source: UniProtKB
  21. transcription, DNA-templated Source: UniProtKB-KW
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 1
Short name:
hPER1
Alternative name(s):
Circadian clock protein PERIOD 1
Circadian pacemaker protein Rigui
Gene namesi
Name:PER1
Synonyms:KIAA0482, PER, RIGUI
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:8845. PER1.

Subcellular locationi

Nucleus. Cytoplasm
Note: Nucleocytoplasmic shuttling is effected by interaction with other circadian core oscillator proteins and/or by phosphorylation. Retention of PER1 in the cytoplasm occurs through PER1-PER2 heterodimer formation. Translocate to the nucleus after phosphorylation by CSNK1D or CSNK1E. Also translocated to the nucleus by CRY1 or CRY2 (By similarity).By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi121 – 1266TSGCSS → AAGCSA: Strongly decreases interaction with BTRC and FBXW11 and inhibits degradation promoted by CSNK1E.
Mutagenesisi210 – 2134SEYT → AEYA: No effect on interaction with BTRC and FBXW11. 1 Publication
Mutagenesisi714 – 72613SVVSV…CSFSS → AVVAVTAQCAFAA: No effect on interaction with BTRC and FBXW11. 1 PublicationAdd
BLAST
Mutagenesisi794 – 7985FLSRF → ALSRA: Strongly decreases interaction with BTRC and FBXW11. 1 Publication

Organism-specific databases

PharmGKBiPA33184.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 12901290Period circadian protein homolog 1PRO_0000162627Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei121 – 1211Phosphothreonine; by CSNK1ESequence Analysis
Modified residuei122 – 1221Phosphoserine; by CSNK1ESequence Analysis
Modified residuei126 – 1261Phosphoserine; by CSNK1ESequence Analysis
Modified residuei661 – 6611PhosphoserineBy similarity
Modified residuei663 – 6631PhosphoserineBy similarity
Modified residuei704 – 7041Phosphoserine2 Publications
Modified residuei815 – 8151Phosphoserine2 Publications
Modified residuei979 – 9791Phosphoserine1 Publication
Modified residuei980 – 9801Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine residues by CSNK1D, CSNK1E and probably also by CSNK1G2. Phosphorylation by CSNK1D or CSNK1E promotes nuclear location of PER proteins as well as ubiquitination and subsequent degradation. May be dephosphorylated by PP1.1 Publication
Ubiquitinated; requires phosphorylation by CSNK1E and interaction with BTRC and FBXW11.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO15534.
PaxDbiO15534.
PRIDEiO15534.

PTM databases

PhosphoSiteiO15534.

Expressioni

Tissue specificityi

Widely expressed. Expressed in hair follicles (at protein level).Found in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, kidney, spleen, thymus, prostate, testis, ovary and small intestine. Highest level in skeletal muscle.4 Publications

Inductioni

Serum-induced levels in fibroblasts show circadian oscillations. Maximum levels after 1 hour stimulation, minimum levels after 12 hours. Another peak is then observed after 20 hours. Protein levels show maximum levels at 6 hours, decrease to reach minimum levels at 20 hours, and increase again to reach a second peak after 26 hours. Levels then decrease slightly and then increase to maximum levels at 32 hours. Levels of phosphorylated form increase between 3 hours and 12 hours.1 Publication

Gene expression databases

BgeeiO15534.
CleanExiHS_PER1.
ExpressionAtlasiO15534. baseline and differential.
GenevestigatoriO15534.

Interactioni

Subunit structurei

Homodimer. Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts directly with TIMELESS, PER2, PER3 and, through a C-terminal domain, with CRY1 and CRY2. Interacts with ARNTL/BMAL1 and CLOCK. Interacts with GPRASP1. Interacts (phosphorylated) with BTRC and FBXW11; the interactions trigger proteasomal degradation. Interacts with NONO, WDR5 and SFPQ.1 Publication

Protein-protein interaction databases

BioGridi111210. 29 interactions.
DIPiDIP-56603N.
IntActiO15534. 4 interactions.
STRINGi9606.ENSP00000314420.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1UL6model-A830-845[»]
ProteinModelPortaliO15534.
SMRiO15534. Positions 196-502, 1124-1205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini208 – 27568PAS 1PROSITE-ProRule annotationAdd
BLAST
Domaini348 – 41467PAS 2PROSITE-ProRule annotationAdd
BLAST
Domaini422 – 46544PACAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 151151Interaction with BTRC1 PublicationAdd
BLAST
Regioni596 – 815220Required for phosphorylation by CSNK1EBy similarityAdd
BLAST
Regioni1149 – 1290142CRY binding domainBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi138 – 14710Nuclear export signal 1By similarity
Motifi489 – 49810Nuclear export signal 2By similarity
Motifi827 – 84317Nuclear localization signalBy similarityAdd
BLAST
Motifi982 – 9898Nuclear export signal 3By similarity
Motifi1043 – 10475LXXLL

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi49 – 12981Ser-richAdd
BLAST
Compositional biasi653 – 6564Poly-Ser
Compositional biasi848 – 1013166Pro-richAdd
BLAST
Compositional biasi1030 – 110475Ser-richAdd
BLAST
Compositional biasi1269 – 12735Poly-Glu
Compositional biasi1276 – 12794Poly-Ser

Sequence similaritiesi

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

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG253593.
GeneTreeiENSGT00510000046467.
HOGENOMiHOG000231111.
HOVERGENiHBG008167.
InParanoidiO15534.
KOiK02633.
OMAiELGAVHS.
PhylomeDBiO15534.
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 (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform Rigui 4.7 (identifier: O15534-1) [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
MSGPLEGADG GGDPRPGESF CPGGVPSPGP PQHRPCPGPS LADDTDANSN
60 70 80 90 100
GSSGNESNGH ESRGASQRSS HSSSSGNGKD SALLETTESS KSTNSQSPSP
110 120 130 140 150
PSSSIAYSLL SASSEQDNPS TSGCSSEQSA RARTQKELMT ALRELKLRLP
160 170 180 190 200
PERRGKGRSG TLATLQYALA CVKQVQANQE YYQQWSLEEG EPCSMDMSTY
210 220 230 240 250
TLEELEHITS EYTLQNQDTF SVAVSFLTGR IVYISEQAAV LLRCKRDVFR
260 270 280 290 300
GTRFSELLAP QDVGVFYGST APSRLPTWGT GASAGSGLRD FTQEKSVFCR
310 320 330 340 350
IRGGPDRDPG PRYQPFRLTP YVTKIRVSDG APAQPCCLLI AERIHSGYEA
360 370 380 390 400
PRIPPDKRIF TTRHTPSCLF QDVDERAAPL LGYLPQDLLG APVLLFLHPE
410 420 430 440 450
DRPLMLAIHK KILQLAGQPF DHSPIRFCAR NGEYVTMDTS WAGFVHPWSR
460 470 480 490 500
KVAFVLGRHK VRTAPLNEDV FTPPAPSPAP SLDTDIQELS EQIHRLLLQP
510 520 530 540 550
VHSPSPTGLC GVGAVTSPGP LHSPGSSSDS NGGDAEGPGP PAPVTFQQIC
560 570 580 590 600
KDVHLVKHQG QQLFIESRAR PQSRPRLPAT GTFKAKALPC QSPDPELEAG
610 620 630 640 650
SAPVQAPLAL VPEEAERKEA SSCSYQQINC LDSILRYLES CNLPSTTKRK
660 670 680 690 700
CASSSSYTTS SASDDDRQRT GPVSVGTKKD PPSAALSGEG ATPRKEPVVG
710 720 730 740 750
GTLSPLALAN KAESVVSVTS QCSFSSTIVH VGDKKPPESD IIMMEDLPGL
760 770 780 790 800
APGPAPSPAP SPTVAPDPAP DAYRPVGLTK AVLSLHTQKE EQAFLSRFRD
810 820 830 840 850
LGRLRGLDSS STAPSALGER GCHHGPAPPS RRHHCRSKAK RSRHHQNPRA
860 870 880 890 900
EAPCYVSHPS PVPPSTPWPT PPATTPFPAV VQPYPLPVFS PRGGPQPLPP
910 920 930 940 950
APTSVPPAAF PAPLVTPMVA LVLPNYLFPT PSSYPYGALQ TPAEGPPTPA
960 970 980 990 1000
SHSPSPSLPA LAPSPPHRPD SPLFNSRCSS PLQLNLLQLE ELPRAEGAAV
1010 1020 1030 1040 1050
AGGPGSSAGP PPPSAEAAEP EARLAEVTES SNQDALSGSS DLLELLLQED
1060 1070 1080 1090 1100
SRSGTGSAAS GSLGSGLGSG SGSGSHEGGS TSASITRSSQ SSHTSKYFGS
1110 1120 1130 1140 1150
IDSSEAEAGA ARGGAEPGDQ VIKYVLQDPI WLLMANADQR VMMTYQVPSR
1160 1170 1180 1190 1200
DMTSVLKQDR ERLRAMQKQQ PRFSEDQRRE LGAVHSWVRK GQLPRALDVM
1210 1220 1230 1240 1250
ACVDCGSSTQ DPGHPDDPLF SELDGLGLEP MEEGGGEQGS SGGGSGEGEG
1260 1270 1280 1290
CEEAQGGAKA SSSQDLAMEE EEEGRSSSSP ALPTAGNCTS
Length:1,290
Mass (Da):136,212
Last modified:December 16, 2008 - v2
Checksum:i60B844468EEF4D1B
GO
Isoform Rigui 3.0 (identifier: O15534-2)

Sequence is not available
Length:
Mass (Da):
Isoform Rigui 6.6 (identifier: O15534-3)

Also known as: Truncated

Sequence is not available
Length:
Mass (Da):
Isoform 2 (identifier: O15534-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-32: MSGPLEGADGGGDPRPGESFCPGGVPSPGPPQ → MLEVLEEIWSVRARRA
     822-875: CHHGPAPPSR...TPWPTPPATT → SHLGPPGACP...GTGPSLASPH
     876-1290: Missing.

Note: No experimental confirmation available.

Show »
Length:859
Mass (Da):91,644
Checksum:i08F94197E204DEE5
GO

Sequence cautioni

The sequence BAC06326.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti696 – 6961E → Q in a breast cancer sample; somatic mutation. 1 Publication
VAR_036038
Natural varianti962 – 9621A → P.7 Publications
Corresponds to variant rs2585405 [ dbSNP | Ensembl ].
VAR_047899
Natural varianti968 – 9681R → H.
Corresponds to variant rs3027193 [ dbSNP | Ensembl ].
VAR_047900
Natural varianti985 – 9851N → S in a breast cancer sample; somatic mutation. 1 Publication
VAR_036039
Natural varianti1060 – 10601S → L in a colorectal cancer sample; somatic mutation. 1 Publication
VAR_036040

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3232MSGPL…PGPPQ → MLEVLEEIWSVRARRA in isoform 2. 1 PublicationVSP_056205Add
BLAST
Alternative sequencei822 – 87554CHHGP…PPATT → SHLGPPGACPLPSLGLDCWG VGLKGGVSAPGTQAGVASTT RPCLGTGPSLASPH in isoform 2. 1 PublicationVSP_056206Add
BLAST
Alternative sequencei876 – 1290415Missing in isoform 2. 1 PublicationVSP_056207Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF022991 mRNA. Translation: AAC51765.1.
AB002107 mRNA. Translation: BAA22633.1.
AF102137 Genomic DNA. Translation: AAF15544.1.
AB030817 Genomic DNA. Translation: BAA94085.1.
AB088477 mRNA. Translation: BAC06326.2. Different initiation.
AK295410 mRNA. Translation: BAG58361.1.
AC129492 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90090.1.
CH471108 Genomic DNA. Translation: EAW90091.1.
BC137346 mRNA. Translation: AAI37347.1.
CCDSiCCDS11131.1. [O15534-1]
PIRiT00018.
RefSeqiNP_002607.2. NM_002616.2. [O15534-1]
XP_005256746.1. XM_005256689.1. [O15534-1]
UniGeneiHs.445534.

Genome annotation databases

EnsembliENST00000317276; ENSP00000314420; ENSG00000179094. [O15534-1]
ENST00000354903; ENSP00000346979; ENSG00000179094. [O15534-4]
GeneIDi5187.
KEGGihsa:5187.
UCSCiuc002gkd.3. human. [O15534-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF022991 mRNA. Translation: AAC51765.1 .
AB002107 mRNA. Translation: BAA22633.1 .
AF102137 Genomic DNA. Translation: AAF15544.1 .
AB030817 Genomic DNA. Translation: BAA94085.1 .
AB088477 mRNA. Translation: BAC06326.2 . Different initiation.
AK295410 mRNA. Translation: BAG58361.1 .
AC129492 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90090.1 .
CH471108 Genomic DNA. Translation: EAW90091.1 .
BC137346 mRNA. Translation: AAI37347.1 .
CCDSi CCDS11131.1. [O15534-1 ]
PIRi T00018.
RefSeqi NP_002607.2. NM_002616.2. [O15534-1 ]
XP_005256746.1. XM_005256689.1. [O15534-1 ]
UniGenei Hs.445534.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1UL6 model - A 830-845 [» ]
ProteinModelPortali O15534.
SMRi O15534. Positions 196-502, 1124-1205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111210. 29 interactions.
DIPi DIP-56603N.
IntActi O15534. 4 interactions.
STRINGi 9606.ENSP00000314420.

PTM databases

PhosphoSitei O15534.

Proteomic databases

MaxQBi O15534.
PaxDbi O15534.
PRIDEi O15534.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000317276 ; ENSP00000314420 ; ENSG00000179094 . [O15534-1 ]
ENST00000354903 ; ENSP00000346979 ; ENSG00000179094 . [O15534-4 ]
GeneIDi 5187.
KEGGi hsa:5187.
UCSCi uc002gkd.3. human. [O15534-1 ]

Organism-specific databases

CTDi 5187.
GeneCardsi GC17M008043.
H-InvDB HIX0039072.
HGNCi HGNC:8845. PER1.
MIMi 602260. gene.
neXtProti NX_O15534.
PharmGKBi PA33184.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG253593.
GeneTreei ENSGT00510000046467.
HOGENOMi HOG000231111.
HOVERGENi HBG008167.
InParanoidi O15534.
KOi K02633.
OMAi ELGAVHS.
PhylomeDBi O15534.
TreeFami TF318445.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSi PER1. human.
GeneWikii PER1.
GenomeRNAii 5187.
NextBioi 20060.
PROi O15534.
SOURCEi Search...

Gene expression databases

Bgeei O15534.
CleanExi HS_PER1.
ExpressionAtlasi O15534. baseline and differential.
Genevestigatori O15534.

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. "Rigui, a putative mammalian ortholog of the Drosophila period gene."
    Sun Z.S., Albrecht U., Zhuchenko O., Bailey J., Eichele G., Lee C.C.
    Cell 90:1003-1011(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, VARIANT PRO-962.
    Tissue: Heart.
  2. "Circadian oscillation of a mammalian homologue of the Drosophila period gene."
    Tei H., Okamura H., Shigeyoshi Y., Fukuhara C., Ozawa R., Hirose M., Sakaki Y.
    Nature 389:512-516(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, VARIANT PRO-962.
    Tissue: Brain.
  3. "The human Per1 gene: genomic organization and promoter analysis of the first human orthologue of the Drosophila period gene."
    Taruscio D., Zoraqi G.K., Falchi M., Iosi F., Paradisi S., Di Fiore B., Lavia P., Falbo V.
    Gene 253:161-170(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-962.
  4. "The human and mouse Period1 genes: five well-conserved E-boxes additively contribute to the enhancement of mPer1 transcription."
    Hida A., Koike N., Hirose M., Hattori M., Sakaki Y., Tei H.
    Genomics 65:224-233(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT PRO-962.
  5. "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."
    Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.
    DNA Res. 4:345-349(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-962.
    Tissue: Brain.
  6. Nagase T., Kikuno R., Ohara O.
    Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Corpus callosum.
  8. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-962.
  10. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT PRO-962.
  11. "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.
  12. "Phosphorylation and destabilization of human period I clock protein by human casein kinase I epsilon."
    Keesler G.A., Camacho F., Guo Y., Virshup D., Mondadori C., Yao Z.
    NeuroReport 11:951-955(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION BY CSNK1E.
  13. "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: PHOSPHORYLATION BY CSNK1D.
  14. "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: PHOSPHORYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INDUCTION.
  15. "SCFbeta-TRCP controls clock-dependent transcription via casein kinase 1-dependent degradation of the mammalian period-1 (Per1) protein."
    Shirogane T., Jin J., Ang X.L., Harper J.W.
    J. Biol. Chem. 280:26863-26872(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH BTRC AND FBXW11, PHOSPHORYLATION AT THR-121; SER-122 AND SER-126, UBIQUITINATION, MUTAGENESIS OF 210-SER--THR-213; 714-SER--SER-726 AND 794-PHE--PHE-798.
  16. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979 AND SER-980, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704 AND SER-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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].
  20. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  21. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  22. "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.
  23. "A meeting of two chronobiological systems: circadian proteins Period1 and BMAL1 modulate the human hair cycle clock."
    Al-Nuaimi Y., Hardman J.A., Biro T., Haslam I.S., Philpott M.P., Toth B.I., Farjo N., Farjo B., Baier G., Watson R.E., Grimaldi B., Kloepper J.E., Paus R.
    J. Invest. Dermatol. 134:610-619(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HAIR GROWTH, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  24. "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.
  25. Cited for: VARIANTS [LARGE SCALE ANALYSIS] GLN-696; SER-985 AND LEU-1060.

Entry informationi

Entry nameiPER1_HUMAN
AccessioniPrimary (citable) accession number: O15534
Secondary accession number(s): B2RPA8, B4DI49, D3DTR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: December 16, 2008
Last modified: October 29, 2014
This is version 141 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3