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O15534 (PER1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Period circadian protein homolog 1

Short name=hPER1
Alternative name(s):
Circadian clock protein PERIOD 1
Circadian pacemaker protein Rigui
Gene names
Name:PER1
Synonyms:KIAA0482, PER, RIGUI
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1290 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 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, NR1D2, RORA, RORB and RORG, 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. Ref.22

Subunit structure

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 and clock. Interacts with GPRASP1. Interacts (phosphorylated) with BTRC and FBXW11; the interactions trigger proteasomal degradation. Interacts with NONO and WDR5. Ref.14

Subcellular location

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. Ref.13 Ref.22

Tissue specificity

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. Ref.2 Ref.10 Ref.13 Ref.22

Induction

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. Ref.13

Post-translational modification

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. Ref.11 Ref.12 Ref.13 Ref.14

Ubiquitinated; requires phosphorylation by CSNK1E and interaction with BTRC and FBXW11. Ref.14

Sequence similarities

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

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

Sequence caution

The sequence BAC06326.2 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
   DomainRepeat
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcircadian regulation of gene expression

Inferred from direct assay Ref.22. Source: UniProtKB

circadian regulation of translation

Inferred from sequence or structural similarity. Source: UniProtKB

circadian rhythm

Inferred from expression pattern PubMed 14645221. Source: UniProtKB

entrainment of circadian clock

Traceable author statement Ref.1. Source: ProtInc

entrainment of circadian clock by photoperiod

Inferred from sequence or structural similarity. Source: UniProtKB

histone H3 acetylation

Inferred from direct assay PubMed 14645221. Source: UniProtKB

histone H3 deacetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4 acetylation

Inferred from direct assay PubMed 14645221. Source: UniProtKB

negative regulation of I-kappaB kinase/NF-kappaB signaling

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of JNK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of glucocorticoid receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

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

negative regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

posttranscriptional regulation of gene expression

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of circadian rhythm

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cytokine production involved in inflammatory response

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of hair cycle

Inferred from mutant phenotype Ref.22. Source: UniProtKB

regulation of p38MAPK cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of sodium ion transport

Inferred from sequence or structural similarity. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from direct assay Ref.22. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionE-box binding

Inferred from direct assay PubMed 18411297. Source: BHF-UCL

RNA polymerase II core promoter proximal region sequence-specific DNA binding

Inferred from direct assay PubMed 18411297. Source: BHF-UCL

chromatin DNA binding

Inferred from sequence or structural similarity. Source: UniProtKB

kinase binding

Inferred from physical interaction Ref.14. Source: UniProtKB

signal transducer activity

Inferred from electronic annotation. Source: InterPro

transcription factor binding transcription factor activity

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

ubiquitin protein ligase binding

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Select]

Note: Additional isoforms seem to exist.
Isoform Rigui 4.7 (identifier: O15534-1)

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 Rigui 3.0 (identifier: O15534-2)

The sequence of this isoform is not available.
Isoform Rigui 6.6 (identifier: O15534-3)

Also known as: Truncated;

The sequence of this isoform is not available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 12901290Period circadian protein homolog 1
PRO_0000162627

Regions

Domain208 – 27568PAS 1
Domain348 – 41467PAS 2
Domain422 – 46544PAC
Region1 – 151151Interaction with BTRC
Region596 – 815220Required for phosphorylation by CSNK1E By similarity
Region1149 – 1290142CRY binding domain By similarity
Motif138 – 14710Nuclear export signal 1 By similarity
Motif489 – 49810Nuclear export signal 3 By similarity
Motif827 – 84317Nuclear localization signal By similarity
Motif982 – 9898Nuclear export signal 2 By similarity
Motif1043 – 10475LXXLL
Compositional bias49 – 12981Ser-rich
Compositional bias653 – 6564Poly-Ser
Compositional bias848 – 1013166Pro-rich
Compositional bias1030 – 110475Ser-rich
Compositional bias1269 – 12735Poly-Glu
Compositional bias1276 – 12794Poly-Ser

Amino acid modifications

Modified residue1211Phosphothreonine; by CSNK1E Potential
Modified residue1221Phosphoserine; by CSNK1E Potential
Modified residue1261Phosphoserine; by CSNK1E Potential
Modified residue6611Phosphoserine By similarity
Modified residue6631Phosphoserine By similarity
Modified residue7041Phosphoserine Ref.17 Ref.20
Modified residue8151Phosphoserine Ref.17 Ref.19
Modified residue9791Phosphoserine Ref.15
Modified residue9801Phosphoserine Ref.15

Natural variations

Natural variant6961E → Q in a breast cancer sample; somatic mutation. Ref.24
VAR_036038
Natural variant9621A → P. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.8 Ref.9
Corresponds to variant rs2585405 [ dbSNP | Ensembl ].
VAR_047899
Natural variant9681R → H.
Corresponds to variant rs3027193 [ dbSNP | Ensembl ].
VAR_047900
Natural variant9851N → S in a breast cancer sample; somatic mutation. Ref.24
VAR_036039
Natural variant10601S → L in a colorectal cancer sample; somatic mutation. Ref.24
VAR_036040

Experimental info

Mutagenesis121 – 1266TSGCSS → AAGCSA: Strongly decreases interaction with BTRC and FBXW11 and inhibits degradation promoted by CSNK1E.
Mutagenesis210 – 2134SEYT → AEYA: No effect on interaction with BTRC and FBXW11.
Mutagenesis714 – 72613SVVSV…CSFSS → AVVAVTAQCAFAA: No effect on interaction with BTRC and FBXW11. Ref.14
Mutagenesis794 – 7985FLSRF → ALSRA: Strongly decreases interaction with BTRC and FBXW11. Ref.14

Sequences

Sequence LengthMass (Da)Tools
Isoform Rigui 4.7 [UniParc].

Last modified December 16, 2008. Version 2.
Checksum: 60B844468EEF4D1B

FASTA1,290136,212
        10         20         30         40         50         60 
MSGPLEGADG GGDPRPGESF CPGGVPSPGP PQHRPCPGPS LADDTDANSN GSSGNESNGH 

        70         80         90        100        110        120 
ESRGASQRSS HSSSSGNGKD SALLETTESS KSTNSQSPSP PSSSIAYSLL SASSEQDNPS 

       130        140        150        160        170        180 
TSGCSSEQSA RARTQKELMT ALRELKLRLP PERRGKGRSG TLATLQYALA CVKQVQANQE 

       190        200        210        220        230        240 
YYQQWSLEEG EPCSMDMSTY TLEELEHITS EYTLQNQDTF SVAVSFLTGR IVYISEQAAV 

       250        260        270        280        290        300 
LLRCKRDVFR GTRFSELLAP QDVGVFYGST APSRLPTWGT GASAGSGLRD FTQEKSVFCR 

       310        320        330        340        350        360 
IRGGPDRDPG PRYQPFRLTP YVTKIRVSDG APAQPCCLLI AERIHSGYEA PRIPPDKRIF 

       370        380        390        400        410        420 
TTRHTPSCLF QDVDERAAPL LGYLPQDLLG APVLLFLHPE DRPLMLAIHK KILQLAGQPF 

       430        440        450        460        470        480 
DHSPIRFCAR NGEYVTMDTS WAGFVHPWSR KVAFVLGRHK VRTAPLNEDV FTPPAPSPAP 

       490        500        510        520        530        540 
SLDTDIQELS EQIHRLLLQP VHSPSPTGLC GVGAVTSPGP LHSPGSSSDS NGGDAEGPGP 

       550        560        570        580        590        600 
PAPVTFQQIC KDVHLVKHQG QQLFIESRAR PQSRPRLPAT GTFKAKALPC QSPDPELEAG 

       610        620        630        640        650        660 
SAPVQAPLAL VPEEAERKEA SSCSYQQINC LDSILRYLES CNLPSTTKRK CASSSSYTTS 

       670        680        690        700        710        720 
SASDDDRQRT GPVSVGTKKD PPSAALSGEG ATPRKEPVVG GTLSPLALAN KAESVVSVTS 

       730        740        750        760        770        780 
QCSFSSTIVH VGDKKPPESD IIMMEDLPGL APGPAPSPAP SPTVAPDPAP DAYRPVGLTK 

       790        800        810        820        830        840 
AVLSLHTQKE EQAFLSRFRD LGRLRGLDSS STAPSALGER GCHHGPAPPS RRHHCRSKAK 

       850        860        870        880        890        900 
RSRHHQNPRA EAPCYVSHPS PVPPSTPWPT PPATTPFPAV VQPYPLPVFS PRGGPQPLPP 

       910        920        930        940        950        960 
APTSVPPAAF PAPLVTPMVA LVLPNYLFPT PSSYPYGALQ TPAEGPPTPA SHSPSPSLPA 

       970        980        990       1000       1010       1020 
LAPSPPHRPD SPLFNSRCSS PLQLNLLQLE ELPRAEGAAV AGGPGSSAGP PPPSAEAAEP 

      1030       1040       1050       1060       1070       1080 
EARLAEVTES SNQDALSGSS DLLELLLQED SRSGTGSAAS GSLGSGLGSG SGSGSHEGGS 

      1090       1100       1110       1120       1130       1140 
TSASITRSSQ SSHTSKYFGS IDSSEAEAGA ARGGAEPGDQ VIKYVLQDPI WLLMANADQR 

      1150       1160       1170       1180       1190       1200 
VMMTYQVPSR DMTSVLKQDR ERLRAMQKQQ PRFSEDQRRE LGAVHSWVRK GQLPRALDVM 

      1210       1220       1230       1240       1250       1260 
ACVDCGSSTQ DPGHPDDPLF SELDGLGLEP MEEGGGEQGS SGGGSGEGEG CEEAQGGAKA 

      1270       1280       1290 
SSSQDLAMEE EEEGRSSSSP ALPTAGNCTS 

« Hide

Isoform Rigui 3.0 (Sequence not available).
Isoform Rigui 6.6 (Truncated) (Sequence not available).

References

« Hide 'large scale' references
[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]"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. expand/collapse author list , 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].
[8]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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PRO-962.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704 AND SER-815, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"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].
[19]"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.
[20]"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.
[21]"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.
[22]"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.
[23]"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.
[24]"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: VARIANTS [LARGE SCALE ANALYSIS] GLN-696; SER-985 AND LEU-1060.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
AC129492 Genomic DNA. No translation available.
CH471108 Genomic DNA. Translation: EAW90090.1.
CH471108 Genomic DNA. Translation: EAW90091.1.
BC137346 mRNA. Translation: AAI37347.1.
CCDSCCDS11131.1. [O15534-1]
PIRT00018.
RefSeqNP_002607.2. NM_002616.2. [O15534-1]
XP_005256746.1. XM_005256689.1. [O15534-1]
UniGeneHs.445534.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UL6model-A830-845[»]
ProteinModelPortalO15534.
SMRO15534. Positions 196-502.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111210. 18 interactions.
DIPDIP-56603N.
IntActO15534. 4 interactions.
STRING9606.ENSP00000314420.

PTM databases

PhosphoSiteO15534.

Proteomic databases

MaxQBO15534.
PaxDbO15534.
PRIDEO15534.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000317276; ENSP00000314420; ENSG00000179094. [O15534-1]
GeneID5187.
KEGGhsa:5187.
UCSCuc002gkd.3. human. [O15534-1]

Organism-specific databases

CTD5187.
GeneCardsGC17M008043.
H-InvDBHIX0039072.
HGNCHGNC:8845. PER1.
MIM602260. gene.
neXtProtNX_O15534.
PharmGKBPA33184.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG253593.
HOGENOMHOG000231111.
HOVERGENHBG008167.
InParanoidO15534.
KOK02633.
OMAELGAVHS.
PhylomeDBO15534.
TreeFamTF318445.

Enzyme and pathway databases

ReactomeREACT_24941. Circadian Clock.

Gene expression databases

ArrayExpressO15534.
BgeeO15534.
CleanExHS_PER1.
GenevestigatorO15534.

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

ChiTaRSPER1. human.
GeneWikiPER1.
GenomeRNAi5187.
NextBio20060.
PROO15534.
SOURCESearch...

Entry information

Entry namePER1_HUMAN
AccessionPrimary (citable) accession number: O15534
Secondary accession number(s): B2RPA8, D3DTR3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: December 16, 2008
Last modified: July 9, 2014
This is version 138 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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 17

Human chromosome 17: entries, gene names and cross-references to MIM