Period circadian protein homolog 2 - Mus musculus (Mouse)

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Reviewed, UniProtKB/Swiss-Prot O54943 (PER2_MOUSE)

Last modified February 9, 2010. Version 78. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Period circadian protein homolog 2
      Short name=mPER2
Alternative name(s):
    Circadian clock protein PERIOD 2

Gene names

Name:

Per2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus

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Protein attributes

Sequence length	1257 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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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. Ref.5
Subunit structure	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 PER1 and PER3, and through a C-terminal domain, with CRY1 and CRY2. Interacts with NFIL3. Interaction with CSNK1D or CSNK1E promotes nuclear location of PER proteins. Interacts, via its second PAS domain, with TIMELESS in vitro By similarity. Ref.5 Ref.4 Ref.6 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
Subcellular location	Nucleus. Cytoplasm. 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 PER nuclear localization signal. Also translocated to the nucleus by CRY1 or CRY2. Ref.5 Ref.6 Ref.8 Ref.7
Tissue specificity	In the brain, high expression in SCN during the subjective day. Constitutive expression in the cornu ammonis and in the dentate gyrus of the hyppocampus. Also expressed in the piriform cortex and the glomeruli of the olfactory bulb, and at a lower extent in the cerebral cortex. Not expressed in the pars tuberalis and the Purkinje neurons. Also found in heart, skeletal muscle, spleen, lung and liver. Highest levels in skeletal muscle and liver. Low level in spleen. Not expressed in kidney nor testis. Ref.1 Ref.2
Developmental stage	Expressed in the SCN during late fetal and early neonatal life. Ref.2
Induction	Exhibits circadian rhythm patterns. Levels alter by light exposure during subjective night, but not during subjective day. Ref.1 Ref.2
Post-translational modification	Phosphorylated by CSNK1E and CSNK1D. Phosphorylation results in PER2 protein degradation. Ref.9 Ref.11 Ref.14
Sequence similarities	Contains 1 PAC (PAS-associated C-terminal) domain. Contains 2 PAS (PER-ARNT-SIM) domains.

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Ontologies

Keywords
Biological process	Biological rhythms Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Domain	Repeat
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	circadian rhythm Inferred from direct assay. Source: MGI negative regulation of gene-specific transcription from RNA polymerase II promoter Inferred from direct assay. Source: MGI signal transduction Inferred from electronic annotation. Source: InterPro transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from direct assay. Source: MGI nucleus Inferred from physical interaction. Source: MGI
Molecular function	protein binding Ref.4 Inferred from physical interaction. Source: UniProtKB signal transducer activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
Arntl	Q9WTL8	3	EBI-1266779,EBI-644534
Clock	O08785	3	EBI-1266779,EBI-79859
SIRT1	Q96EB6	1	EBI-1266779,EBI-1802965	From a different organism.

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1257

1257

Period circadian protein homolog 2

PRO_0000162631

Regions

Domain

179 – 246

PAS 1

Domain

319 – 385

PAS 2

Domain

393 – 436

PAC

Region

555 – 763

209

CSNK1E binding domain By similarity

Region

1157 – 1257

101

CRY binding domain By similarity

Motif

457 – 469

Nuclear export signal

Motif

778 – 794

Nuclear localization signal By similarity

Compositional bias

831 – 961

131

Pro-rich

Compositional bias

1061 – 1111

Ser-rich

Amino acid modifications

Modified residue

525

Phosphoserine Ref.11

Modified residue

528

Phosphoserine Ref.11

Modified residue

531

Phosphoserine Ref.11

Modified residue

538

Phosphoserine Ref.11

Modified residue

544

Phosphoserine Ref.11

Modified residue

554

Phosphothreonine Ref.11

Modified residue

693

Phosphoserine Ref.14

Modified residue

697

Phosphoserine Ref.14

Modified residue

706

Phosphoserine Ref.11

Modified residue

758

Phosphoserine Ref.11

Modified residue

763

Phosphoserine Ref.11

Modified residue

858

Phosphothreonine Ref.11

Modified residue

939

Phosphoserine Ref.11

Modified residue

964

Phosphothreonine Ref.11

Modified residue

971

Phosphoserine Ref.11

Modified residue

1126

Phosphoserine Ref.11

Experimental info

Sequence conflict

445

P → S in AAC53592. Ref.2

Sequence conflict

728

K → R in AAC53592. Ref.2

Secondary structure

1257

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

O54943-1 [UniParc].

Last modified July 15, 1999. Version 3.
Checksum: 554B8AFF036CF7FB
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FASTA

1,257

135,881

        10         20         30         40         50         60 
MNGYVDFSPS PTSPTKEPGA PQPTQAVLQE DVDMSSGSSG NENCSTGRDS QGSDCDDNGK 

        70         80         90        100        110        120 
ELRMLVESSN THPSPDDAFR LMMTEAEHNP STSGCSSEQS AKADAHKELI RTLKELKVHL 

       130        140        150        160        170        180 
PADKKAKGKA STLATLKYAL RSVKQVKANE EYYQLLMSSE SQPCSVDVPS YSMEQVEGIT 

       190        200        210        220        230        240 
SEYIVKNADM FAVAVSLVSG KILYISNQVA SIFHCKKDAF SDAKFVEFLA PHDVSVFHSY 

       250        260        270        280        290        300 
TTPYKLPPWS VCSGLDSFTQ ECMEEKSFFC RVSVGKHHEN EIRYQPFRMT PYLVKVQEQQ 

       310        320        330        340        350        360 
GAESQLCCLL LAERVHSGYE APRIPPEKRI FTTTHTPNCL FQAVDERAVP LLGYLPQDLI 

       370        380        390        400        410        420 
ETPVLVQLHP SDRPLMLAIH KKILQAGGQP FDYSPIRFRT RNGEYITLDT SWSSFINPWS 

       430        440        450        460        470        480 
RKISFIIGRH KVRVGPLNED VFAAPPCPEE KTPHPSVQEL TEQIHRLLMQ PVPHSGSSGY 

       490        500        510        520        530        540 
GSLGSNGSHE HLMSQTSSSD SNGQEESHRR RSGIFKTSGK IQTKSHVSHE SGGQKEASVA 

       550        560        570        580        590        600 
EMQSSPPAQV KAVTTIERDS SGASLPKASF PEELAYKNQP PCSYQQISCL DSVIRYLESC 

       610        620        630        640        650        660 
SEAATLKRKC EFPANIPSRK ATVSPGLHSG EAARPSKVTS HTEVSAHLSS LTLPGKAESV 

       670        680        690        700        710        720 
VSLTSQCSYS STIVHVGDKK PQPELETVED MASGPESLDG AAGGLSQEKG PLQKLGLTKE 

       730        740        750        760        770        780 
VLAAHTQKEE QGFLQRFREV SRLSALQAHC QNYLQERSRA QASDRGLRNT SGLESSWKKT 

       790        800        810        820        830        840 
GKNRKLKSKR VKTRDSSEST GSGGPVSHRP PLMGLNATAW SPSDTSQSSC PSAPFPTAVP 

       850        860        870        880        890        900 
AYPLPVFQAP GIVSTPGTVV APPAATHTGF TMPVVPMGTQ PEFAVQPLPF AAPLAPVMAF 

       910        920        930        940        950        960 
MLPSYPFPPA TPNLPQAFLP SQPHFPAHPT LASEITPASQ AEFPSRTSTL RQPCACPVTP 

       970        980        990       1000       1010       1020 
PAGTVALGRA SPPLFQSRGS SPLQLNLLQL EEAPEGSTGA AGTLGTTGTA ASGLDCTSGT 

      1030       1040       1050       1060       1070       1080 
SRDRQPKAPP TCNEPSDTQN SDAISTSSDL LNLLLGEDLC SATGSALSRS GASATSDSLG 

      1090       1100       1110       1120       1130       1140 
SSSLGFGTSQ SGAGSSDTSH TSKYFGSIDS SENNHKAKMI PDTEESEQFI KYVLQDPIWL 

      1150       1160       1170       1180       1190       1200 
LMANTDDSIM MTYQLPSRDL QAVLKEDQEK LKLLQRSQPR FTEGQRRELR EVHPWVHTGG 

      1210       1220       1230       1240       1250 
LPTAIDVTGC VYCESEEKGN ICLPYEEDSP SPGLCDTSEA KEEEGEQLTG PRIEAQT

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A differential response of two putative mammalian circadian regulators, mper1 and mper2, to light." Albrecht U., Sun Z.S., Eichele G., Lee C.C. Cell 91:1055-1064(1997) [PubMed: 9428527] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION. Tissue: Brain.
[2]	"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: 9427249] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION, DEVELOPMENTAL STAGE. Tissue: Brain.
[3]	Zylka M.J., Reppert S.M. Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 172 AND 501.
[4]	"Mammalian circadian autoregulatory loop: a timeless ortholog and mPer1 interact and negatively regulate CLOCK-BMAL1-induced transcription." Sangoram A.M., Saez L., Antoch M.P., Gekakis N., Staknis D., Whiteley A., Fruechte E.M., Vitaterna M.H., Shimomura K., King D.P., Young M.W., Weitz C.J., Takahashi J.S. Neuron 21:1101-1113(1998) [PubMed: 9856465] [Abstract] Cited for: INTERACTION WITH TIMELESS.
[5]	"mCRY1 and mCRY2 are essential components of the negative limb of the circadian clock feedback loop." Kume K., Zylka M.J., Sriram S., Shearman L.P., Weaver D.R., Jin X., Maywood E.S., Hastings M.H., Reppert S.M. Cell 98:193-205(1999) [PubMed: 10428031] [Abstract] Cited for: INTERACTION WITH PER3; CRY1 AND CRY2, FUNCTION, SUBCELLULAR LOCATION.
[6]	"Nuclear entry of the circadian regulator mPER1 is controlled by mammalian casein kinase I epsilon." Vielhaber E., Eide E., Rivers A., Gao Z.-H., Virshup D.M. Mol. Cell. Biol. 20:4888-4899(2000) [PubMed: 10848614] [Abstract] Cited for: INTERACTION WITH PER1; CKSN1D AND CKSN1E, SUBCELLULAR LOCATION.
[7]	"Nuclear export of mammalian PERIOD proteins." Vielhaber E.L., Duricka D., Ullman K.S., Virshup D.M. J. Biol. Chem. 276:45921-45927(2001) [PubMed: 11591712] [Abstract] Cited for: SUBCELLULAR LOCATION, NUCLEAR EXPORT SIGNAL.
[8]	"Nucleocytoplasmic shuttling and mCRY-dependent inhibition of ubiquitylation of the mPER2 clock protein." Yagita K., Tamanini F., Yasuda M., Hoeijmakers J.H., van der Horst G.T., Okamura H. EMBO J. 21:1301-1314(2002) [PubMed: 11889036] [Abstract] Cited for: INTERACTION WITH CRY1 AND CRY2, SUBCELLULAR LOCATION.
[9]	"Control of intracellular dynamics of mammalian period proteins by casein kinase I epsilon (CKIepsilon) and CKIdelta in cultured cells." Akashi M., Tsuchiya Y., Yoshino T., Nishida E. Mol. Cell. Biol. 22:1693-1703(2002) [PubMed: 11865049] [Abstract] Cited for: INTERACTION WITH CSNK1D AND CKSN1E, PHOSPHORYLATION.
[10]	"Direct association between mouse PERIOD and CKIepsilon is critical for a functioning circadian clock." Lee C., Weaver D.R., Reppert S.M. Mol. Cell. Biol. 24:584-594(2004) [PubMed: 14701732] [Abstract] Cited for: INTERACTION WITH CKSN1E; PER1; PER3; CRY1 AND CRY2.
[11]	"Mapping of phosphorylation sites by a multi-protease approach with specific phosphopeptide enrichment and NanoLC-MS/MS analysis." Schlosser A., Vanselow J.T., Kramer A. Anal. Chem. 77:5243-5250(2005) [PubMed: 16097765] [Abstract] Cited for: PHOSPHORYLATION AT SER-525; SER-528; SER-531; SER-538; SER-544; THR-554; SER-706; SER-758; SER-763; THR-858; SER-939; THR-964; SER-971 AND SER-1126.
[12]	"Functional evolution of the photolyase/cryptochrome protein family: importance of the C terminus of mammalian CRY1 for circadian core oscillator performance." Chaves I., Yagita K., Barnhoorn S., Okamura H., van der Horst G.T.J., Tamanini F. Mol. Cell. Biol. 26:1743-1753(2006) [PubMed: 16478995] [Abstract] Cited for: INTERACTION WITH CRY1 AND CRY2.
[13]	"The negative transcription factor E4BP4 is associated with circadian clock protein PERIOD2." Ohno T., Onishi Y., Ishida N. Biochem. Biophys. Res. Commun. 354:1010-1015(2007) [PubMed: 17274955] [Abstract] Cited for: INTERACTION WITH NFIL3.
[14]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-693 AND SER-697, MASS SPECTROMETRY. Tissue: Liver.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF036893 mRNA. Translation: AAC39942.1.
AF035830 mRNA. Translation: AAC53592.1.

IPI

IPI00469179.

PIR

T09493.

RefSeq

NP_035196.2.

UniGene

Mm.218141

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3GDI	X-ray	2.40	A/B	170-473	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O54943. 6 interactions.

STRING

O54943.

PTM databases

PhosphoSite

O54943.

Proteomic databases

PRIDE

O54943.

Genome annotation databases

Ensembl

ENSMUST00000069620; ENSMUSP00000066620; ENSMUSG00000055866; Mus musculus. [Genome view]

GeneID

18627.

KEGG

mmu:18627.

Organism-specific databases

CTD

18627.

MGI

MGI:1195265. Per2.

Phylogenomic databases

HOVERGEN

O54943.

InParanoid

O54943.

OrthoDB

EOG95XBF9.

Gene expression databases

ArrayExpress

O54943.

Bgee

O54943.

CleanEx

MM_PER2.

Genevestigator

O54943.

GermOnline

ENSMUSG00000055866. Mus musculus.

Family and domain databases

InterPro

IPR001610. PAC.
IPR000014. PAS.
IPR013655. PAS_fold_3.
[Graphical view]

Pfam

PF08447. PAS_3. 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 Resources

SOURCE

Search...

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Entry information

Entry name

PER2_MOUSE

Accession

Primary (citable) accession number: O54943
Secondary accession number(s): O54954

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	July 15, 1999
Last modified:	February 9, 2010
This is version 78 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents