O15534 (PER1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1290 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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. Can bind heme By similarity.
Subunit structure	Homodimer By similarity. 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. Binding to CSNK1G2 triggers proteasomal degradation. Ref.11 Ref.12 Ref.14
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. Ref.13
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. Ref.2 Ref.10 Ref.13
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 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. Ref.11 Ref.12 Ref.13 Ubiquitinated By similarity.
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.

Ontologies

Keywords
Biological process	Biological rhythms Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	circadian regulation of gene expression Inferred from direct assay PubMed 18411297. Source: BHF-UCL entrainment of circadian clock Traceable author statement Ref.1. Source: ProtInc negative regulation of transcription from RNA polymerase II promoter Inferred from sequence or structural similarity. Source: BHF-UCL response to light stimulus Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	E-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 protein binding transcription factor activity Inferred from sequence or structural similarity. Source: BHF-UCL signal transducer activity Inferred from electronic annotation. Source: InterPro
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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1290	1290	Period circadian protein homolog 1		PRO_0000162627
Regions
	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
	Compositional bias	49 – 129	81	Ser-rich
	Compositional bias	653 – 656	4	Poly-Ser
	Compositional bias	848 – 1013	166	Pro-rich
	Compositional bias	1030 – 1104	75	Ser-rich
	Compositional bias	1269 – 1273	5	Poly-Glu
	Compositional bias	1276 – 1279	4	Poly-Ser
Amino acid modifications
	Modified residue	704	1	Phosphoserine Ref.17 Ref.19
	Modified residue	815	1	Phosphoserine Ref.17 Ref.18
	Modified residue	979	1	Phosphoserine Ref.15
	Modified residue	980	1	Phosphoserine Ref.15
Natural variations
	Natural variant	696	1	E → Q in a breast cancer sample; somatic mutation. Ref.20		VAR_036038
	Natural variant	962	1	A → P. Ref.1 Ref.2 Ref.3 Ref.4 Ref.5 Ref.8 Ref.9 Corresponds to variant rs2585405 [ dbSNP | Ensembl ].		VAR_047899
	Natural variant	968	1	R → H. Corresponds to variant rs3027193 [ dbSNP | Ensembl ].		VAR_047900
	Natural variant	985	1	N → S in a breast cancer sample; somatic mutation. Ref.20		VAR_036039
	Natural variant	1060	1	S → L in a colorectal cancer sample; somatic mutation. Ref.20		VAR_036040

Sequences

	Sequence		Length	Mass (Da)
	Isoform Rigui 4.7 [UniParc]. Last modified December 16, 2008. Version 2. Checksum: 60B844468EEF4D1B	FASTA	1,290	136,212
	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
	Isoform Rigui 3.0 (Sequence not available).		–	–
	Isoform Rigui 6.6 (Truncated) (Sequence not available).		–	–

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, INTERACTION WITH 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, INTERACTION WITH 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 CSNK1G2.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[18]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"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. , 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.

IPI

IPI00440484.

PIR

T00018.

RefSeq

NP_002607.2. NM_002616.2.

UniGene

Hs.445534.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1UL6	model	-	A	830-845	[»]

ProteinModelPortal

O15534.

ModBase

Search...

Protein-protein interaction databases

IntAct

O15534. 4 interactions.

STRING

9606.ENSP00000314420.

PTM databases

PhosphoSite

O15534.

Proteomic databases

PaxDb

O15534.

PRIDE

O15534.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000317276; ENSP00000314420; ENSG00000179094.

GeneID

5187.

KEGG

hsa:5187.

UCSC

uc002gkd.3. human.

Organism-specific databases

CTD

5187.

GeneCards

GC17M008043.

H-InvDB

HIX0039072.

HGNC

HGNC:8845. PER1.

MIM

602260. gene.

neXtProt

NX_O15534.

PharmGKB

PA33184.

HUGE

Search...

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG253593.

HOGENOM

HOG000231111.

HOVERGEN

HBG008167.

InParanoid

O15534.

KO

K02633.

OMA

ELGAVHS.

OrthoDB

EOG4HMJ8R.

PhylomeDB

O15534.

Enzyme and pathway databases

Pathway_Interaction_DB

circadianpathway. Circadian rhythm pathway.

Reactome

REACT_24941. Circadian Clock.

Gene expression databases

ArrayExpress

O15534.

Bgee

O15534.

CleanEx

HS_PER1.

Genevestigator

O15534.

GermOnline

ENSG00000179094. Homo sapiens.

Family and domain databases

InterPro

IPR001610. PAC.
IPR000014. PAS.
IPR013655. PAS_fold_3.
IPR022728. Period_circadian-like_C.
[Graphical view]

Pfam

PF08447. PAS_3. 1 hit.
PF12114. Period_C. 1 hit.
[Graphical view]

SMART

SM00086. PAC. 1 hit.
SM00091. PAS. 2 hits.
[Graphical view]

PROSITE

PS50113. PAC. False negative.
PS50112. PAS. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

PER1. human.

GenomeRNAi

5187.

NextBio

20060.

SOURCE

Search...

Entry information

Entry name

PER1_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 126 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.