[1]	NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING, AND VARIANT PRO-962. TISSUE=Heart; DOI=10.1016/S0092-8674(00)80366-9; PubMed=9323128 [NCBI, ExPASy, EBI, Israel, Japan] Sun Z.S., Albrecht U., Zhuchenko O., Bailey J., Eichele G., Lee C.C.; "Rigui, a putative mammalian ortholog of the Drosophila period gene."; Cell 90:1003-1011(1997).
[2]	NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND VARIANT PRO-962. TISSUE=Brain; DOI=10.1038/39086; PubMed=9333243 [NCBI, ExPASy, EBI, Israel, Japan] Tei H., Okamura H., Shigeyoshi Y., Fukuhara C., Ozawa R., Hirose M., Sakaki Y.; "Circadian oscillation of a mammalian homologue of the Drosophila period gene."; Nature 389:512-516(1997).
[3]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-962. DOI=10.1016/S0378-1119(00)00248-1; PubMed=10940553 [NCBI, ExPASy, EBI, Israel, Japan] Taruscio D., Zoraqi G.K., Falchi M., Iosi F., Paradisi S., Di Fiore B., Lavia P., Falbo V.; "The human Per1 gene: genomic organization and promoter analysis of the first human orthologue of the Drosophila period gene."; Gene 253:161-170(2000).
[4]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT PRO-962. DOI=10.1006/geno.2000.6166; PubMed=10857746 [NCBI, ExPASy, EBI, Israel, Japan] Hida A., Koike N., Hirose M., Hattori M., Sakaki Y., Tei H.; "The human and mouse Period1 genes: five well-conserved E-boxes additively contribute to the enhancement of mPer1 transcription."; Genomics 65:224-233(2000).
[5]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-962. TISSUE=Brain; DOI=10.1093/dnares/4.5.345; PubMed=9455484 [NCBI, ExPASy, EBI, Israel, Japan] Seki N., Ohira M., Nagase T., Ishikawa K., Miyajima N., Nakajima D., Nomura N., Ohara O.; "Characterization of cDNA clones in size-fractionated cDNA libraries from human brain."; DNA Res. 4:345-349(1997).
[6]	SEQUENCE REVISION. Nagase T., Kikuno R., Ohara O.; Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
[7]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. DOI=10.1038/nature04689; PubMed=16625196 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."; Nature 440:1045-1049(2006).
[8]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PRO-962. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.; Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[9]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PRO-962. DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[10]	TISSUE SPECIFICITY. DOI=10.1016/S0896-6273(00)80417-1; PubMed=9427249 [NCBI, ExPASy, EBI, Israel, Japan] Shearman L.P., Zylka M.J., Weaver D.R., Kolakowski L.F. Jr., Reppert S.M.; "Two period homologs: circadian expression and photic regulation in the suprachiasmatic nuclei."; Neuron 19:1261-1269(1997).
[11]	PHOSPHORYLATION, AND INTERACTION WITH CSNK1E. PubMed=10790862 [NCBI, ExPASy, EBI, Israel, Japan] Keesler G.A., Camacho F., Guo Y., Virshup D., Mondadori C., Yao Z.; "Phosphorylation and destabilization of human period I clock protein by human casein kinase I epsilon."; NeuroReport 11:951-955(2000).
[12]	PHOSPHORYLATION, AND INTERACTION WITH CSNK1D. DOI=10.1016/S0014-5793(00)02434-0; PubMed=11165242 [NCBI, ExPASy, EBI, Israel, Japan] Camacho F., Cilio M., Guo Y., Virshup D.M., Patel K., Khorkova O., Styren S., Morse B., Yao Z., Keesler G.A.; "Human casein kinase Idelta phosphorylation of human circadian clock proteins period 1 and 2."; FEBS Lett. 489:159-165(2001).
[13]	PHOSPHORYLATION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND INDUCTION. DOI=10.1042/BJ20031308; PubMed=14750904 [NCBI, ExPASy, EBI, Israel, Japan] Miyazaki K., Nagase T., Mesaki M., Narukawa J., Ohara O., Ishida N.; "Phosphorylation of clock protein PER1 regulates its circadian degradation in normal human fibroblasts."; Biochem. J. 380:95-103(2004).
[14]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-979; SER-980; SER-1100; SER-1103 AND SER-1104, AND MASS SPECTROMETRY. TISSUE=Epithelium; DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan] Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."; Cell 127:635-648(2006).
[15]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1262 AND SER-1263, AND MASS SPECTROMETRY. DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan] 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.; "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."; Science 316:1160-1166(2007).
[16]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-704 AND SER-815, AND MASS SPECTROMETRY. DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan] Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.; "A quantitative atlas of mitotic phosphorylation."; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]	VARIANTS [LARGE SCALE ANALYSIS] GLN-696; SER-985 AND LEU-1060. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.; "The consensus coding sequences of human breast and colorectal cancers."; Science 314:268-274(2006).

Comments

FUNCTION: Component of the circadian clock mechanism which is essential for generating circadian rhythms. Negative element in the circadian transcriptional loop. Influences clock function by interacting with other circadian regulatory proteins and transporting them to the nucleus. Negatively regulates CLOCK|NPAS2-BMAL1|BMAL2-induced transactivation (By similarity).
SUBUNIT: Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, BMAL1 or 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. Interaction with CSNK1D or CSNK1E promotes nuclear location of PER proteins. Interacts with GPRASP1 (By similarity).
SUBCELLULAR LOCATION: Nucleus (By similarity). Cytoplasm (By similarity). Note=Mainly nuclear. 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 or by interaction with CSNK1E and/or phosphorylation which appears to mask the PER1 nuclear localization signal. Also translocated to the nucleus by CRY1 or CRY2 (By similarity).

ALTERNATIVE PRODUCTS: 3 named isoforms [FASTA] produced by alternative splicing. Additional isoforms seem to exist.

Name	Rigui 4.7
Isoform ID	O15534-1
This is the isoform sequence displayed in this entry.

Name	Rigui 3.0
Isoform ID	O15534-2
The sequence of this isoform is not described.

Name	Rigui 6.6
Synonyms	Truncated
Isoform ID	O15534-3
The sequence of this isoform is not described.

TISSUE SPECIFICITY: Widely expressed. Found in heart, brain, placenta, lung, liver, skeletal muscle, pancreas, kidney, spleen, thymus, prostate, testis, ovary and small intestine. Highest level in skeletal muscle. Low level in kidney.
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.
PTM: Phosphorylated on serine residues by CSNK1E. Also can be phosphorylated by the delta isoform. Phosphorylation by CSNK1 retains PER1 in the cytoplasm and leads to its ubiquitination and subsequent degradation. Phosphorylated upon DNA damage, probably by ATM or ATR.
PTM: Ubiquitinated (By similarity).
SIMILARITY: Contains 1 PAC (PAS-associated C-terminal) domain.
SIMILARITY: Contains 2 PAS (PER-ARNT-SIM) domains.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF022991; AAC51765.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB002107; BAA22633.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF102137; AAF15544.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030817; BAA94085.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB088477; BAC06326.2; ALT_INIT; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AC129492; -; NOT_ANNOTATED_CDS; Genomic_DNA.	[EMBL / GenBank / DDBJ]
CH471108; EAW90090.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC137346; AAI37347.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI00440484; -.

T00018; T00018.

NP_002607.2; -.

3D structure databases

PDB

1UL6; Model; -; A=830-845.

[ExPASy / RCSB / EBI]

1UL6; -.

PTM databases

O15534; -.

Enzyme and pathway databases

Pathway_Interaction_DB

circadianpathway; Circadian rhythm pathway.

Organism-specific databases

GC17M007984; -.

HIX0019808; -.

HGNC:8845; PER1.

602260; gene. [NCBI / EBI]

PharmGKB

PA38438; -.

HUGE

KIAA0482.

Gene expression databases

O15534; -.

O15534; -.

HS_PER1; -.

ENSG00000179094; Homo sapiens.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005634;	Cellular component: nucleus (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004871;	Molecular function: signal transducer activity (inferred from electronic annotation from InterPro).
GO:0007623;	Biological process: circadian rhythm (traceable author statement from ProtInc).
GO:0009649;	Biological process: entrainment of circadian clock (traceable author statement from ProtInc).
GO:0016481;	Biological process: negative regulation of transcription (inferred from sequence or structural similarity from UniProtKB).
GO:0006355;	Biological process: regulation of transcription, DNA-dependent (inferred from electronic annotation from UniProtKB-KW).
GO:0007165;	Biological process: signal transduction (inferred from electronic annotation from InterPro).
GO:0006350;	Biological process: transcription (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR001610; PAC.
IPR000014; PAS.
IPR013655; PAS_fold_3.
Graphical view of domain structure.

Pfam

PF08447; PAS_3; 1.
Pfam graphical view of domain structure.

SMART

SM00086; PAC; 1.
SM00091; PAS; 2.
SMART graphical view of domain structure.

PROSITE

PS50113; PAC; FALSE_NEG.
PS50112; PAS; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

O15534; -.

Genome annotation databases

Ensembl

ENSG00000179094; Homo sapiens. [Contig view]

GeneID

5187; -.

KEGG

hsa:5187; -.

Phylogenomic databases

HOGENOM

O15534; -.

HOVERGEN

O15534; -.

OMA

O15534; RIFTTRH.

Other

20060; -.

PER1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; Biological rhythms; Cytoplasm; Nucleus; Phosphoprotein; Polymorphism; Repeat; Transcription; Transcription regulation; Ubl conjugation.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 1290`	`1290`	`Period circadian protein homolog 1.`	`PRO_0000162627`
`DOMAIN`	`208 275`	`68`	`PAS 1.`
`DOMAIN`	`348 414`	`67`	`PAS 2.`
`DOMAIN`	`422 465`	`44`	`PAC.`
`REGION`	`596 815`	`220`	`CSNK1E binding domain (By similarity).`
`REGION`	`1149 1290`	`142`	`CRY binding domain (By similarity).`
`MOTIF`	`486 498`	`13`	`Nuclear export signal (By similarity).`
`MOTIF`	`827 843`	`17`	`Nuclear localization signal (By similarity).`
`COMPBIAS`	`49 129`	`81`	`Ser-rich.`
`COMPBIAS`	`653 656`	`4`	`Poly-Ser.`
`COMPBIAS`	`848 1013`	`166`	`Pro-rich.`
`COMPBIAS`	`1030 1104`	`75`	`Ser-rich.`
`COMPBIAS`	`1269 1273`	`5`	`Poly-Glu.`
`COMPBIAS`	`1276 1279`	`4`	`Poly-Ser.`
`MOD_RES`	`704 704`		`Phosphoserine.`
`MOD_RES`	`815 815`		`Phosphoserine.`
`MOD_RES`	`979 979`		`Phosphoserine.`
`MOD_RES`	`980 980`		`Phosphoserine.`
`MOD_RES`	`1100 1100`		`Phosphoserine.`
`MOD_RES`	`1103 1103`		`Phosphoserine.`
`MOD_RES`	`1104 1104`		`Phosphoserine.`
`MOD_RES`	`1262 1262`		`Phosphoserine.`
`MOD_RES`	`1263 1263`		`Phosphoserine.`
`VARIANT`	`696 696`	`1`	`E -> Q (in a breast cancer sample; somatic mutation).`	`VAR_036038`
`VARIANT`	`962 962`	`1`	`A -> P (in dbSNP:rs2585405 [NCBI]).`	`VAR_047899`
`VARIANT`	`968 968`	`1`	`R -> H (in dbSNP:rs3027193 [NCBI]).`	`VAR_047900`
`VARIANT`	`985 985`	`1`	`N -> S (in a breast cancer sample; somatic mutation).`	`VAR_036039`
`VARIANT`	`1060 1060`	`1`	`S -> L (in a colorectal cancer sample; somatic mutation).`	`VAR_036040`

Sequence information

Length: 1290 AA [This is the length of the unprocessed precursor]

Molecular weight: 136212 Da [This is the MW of the unprocessed precursor]

CRC64: 60B844468EEF4D1B [This is a checksum on the sequence]

        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

O15534 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools