Q9R194 (CRY2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Cryptochrome-2

Gene names

Name:	Cry2
Synonyms:	Kiaa0658

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Blue light-dependent regulator of the circadian feedback loop. Inhibits CLOCK|NPAS2-ARNTL E box-mediated transcription. Acts, in conjunction with CRY2, in maintaining period length and circadian rhythmicity. Has no photolyase activity. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. May inhibit CLOCK|NPAS2-ARNTL transcriptional activity through stabilizing the unphosphorylated form of ARNTL. Ref.1 Ref.10
Cofactor	Binds 1 FAD per subunit By similarity. Binds 1 5,10-methenyltetrahydrofolate non-covalently per subunit By similarity.
Subunit structure	Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1E, TIMELESS, and the PER proteins. Interacts directly with TIMELESS, PER1, PER2 and PER3. Interacts with NFIL3. Interaction with PER2 inhibits its ubiquitination and vice versa. Interacts with FBXL3 and FBXL21. Ref.1 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16
Subcellular location	Cytoplasm. Nucleus. Note: Translocated to the nucleus through interaction with other Clock proteins such as PER2 or ARNTL. Ref.1 Ref.5 Ref.8 Ref.9 Ref.13
Tissue specificity	Expressed in all tissues examined including heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Weak expression in spleen. Ref.5 Ref.6
Induction	Shows no clear circadian oscillation pattern in testis, cerebellum nor liver. In skeletal muscle, under constant darkness and 12 hours light:12 hours dark conditions, levels peak between ZT6 and ZT9. Ref.1 Ref.6
Post-translational modification	Phosphorylation on Ser-265 by MAPK is important for the inhibition of CLOCK-ARNTL-mediated transcriptional activity. Phosphorylation by CSKNE requires interaction with PER1 or PER2. Phosphorylated in a circadian manner at Ser-553 and Ser-557 in the suprachiasmatic nucleus (SCN) and liver. Phosphorylation at Ser-557 by DYRK1A promotes subsequent phosphorylation at Ser-553 by GSK3-beta: the two-step phosphorylation at the neighboring Ser residues leads to its proteasomal degradation. Ref.7 Ref.8 Ref.9 Ref.14 Ubiquitinated by the SCF(FBXL3) and SCF(FBXL21) complexes, regulating the balance between degradation and stabilization. The SCF(FBXL3) complex is mainly nuclear and mediates ubiquitination and subsequent degradation of CRY2. In contrast, cytoplasmic SCF(FBXL21) complex-mediated ubiquitination leads to stabilize CRY2 and counteract the activity of the SCF(FBXL3) complex. The SCF(FBXL3) and SCF(FBXL21) complexes probably mediate ubiquitination at different Lys residues. The SCF(FBXL3) complex recognizes and binds CRY2 phosphorylated at Ser-553 and Ser-557. Ref.7 Ref.8 Ref.9 Ref.14
Sequence similarities	Belongs to the DNA photolyase class-1 family. Contains 1 photolyase/cryptochrome alpha/beta domain.

Ontologies

Keywords
Biological process	Biological rhythms Sensory transduction Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	Chromophore FAD Flavoprotein Nucleotide-binding
Molecular function	Photoreceptor protein Receptor Repressor
PTM	Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA repair Inferred from electronic annotation. Source: InterPro circadian rhythm Inferred from mutant phenotype Ref.14. Source: UniProtKB negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara protein import into nucleus Inferred from physical interaction PubMed 15689618. Source: MGI protein-chromophore linkage Inferred from electronic annotation. Source: UniProtKB-KW regulation of circadian rhythm Inferred from mutant phenotype PubMed 10217146. Source: UniProtKB regulation of sodium-dependent phosphate transport Inferred from electronic annotation. Source: Compara transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	cytosol Traceable author statement. Source: Reactome extracellular region Inferred from electronic annotation. Source: Compara mitochondrion Inferred from direct assay Ref.5. Source: UniProtKB nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	DNA photolyase activity Inferred from electronic annotation. Source: InterPro damaged DNA binding Inferred from electronic annotation. Source: Compara nucleotide binding Inferred from electronic annotation. Source: UniProtKB-KW photoreceptor activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding transcription factor activity Inferred from electronic annotation. Source: Compara single-stranded DNA binding Inferred from electronic annotation. Source: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Arntl	Q9WTL8	6	EBI-1266619,EBI-644534
Fbxl3	Q8C4V4	3	EBI-1266619,EBI-1266589
Per2	O54943	3	EBI-1266619,EBI-1266779

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 592	592	Cryptochrome-2		PRO_0000261149
Regions
	Domain	21 – 150	130	Photolyase/cryptochrome alpha/beta
	Region	229 – 506	278	FAD-binding
	Region	389 – 488	100	Required for inhibition of CLOCK-ARNTL-mediated transcription By similarity
	Compositional bias	2 – 5	4	Poly-Ala
Amino acid modifications
	Modified residue	265	1	Phosphoserine; by MAPK Ref.7
	Modified residue	553	1	Phosphoserine; by GSK3-beta Ref.14
	Modified residue	557	1	Phosphoserine; by DYRK1A and MAPK Ref.7 Ref.9 Ref.14
	Cross-link	125		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16
	Cross-link	241		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16
	Cross-link	347		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16
	Cross-link	474		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16
	Cross-link	503		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.16
Experimental info
	Mutagenesis	265	1	S → A: Reduced in vitro MAPK-catalyzed phosphorylation. No effect on inhibition of CLOCK-ARNTL-mediated transcriptional activity. Very little in vitro MAPK-catalyzed phosphorylation; when associated with A-557. Ref.7
	Mutagenesis	265	1	S → D: Reduced inhibition of CLOCK-ARNTL-mediated transcriptional activity. No effect on nuclear localization nor on protein stability. Ref.7
	Mutagenesis	501	1	R → Q: Inhibits interaction with PER2. Does not suppress its nuclear localization. Inhibits its repression activity on CLOCK|NPAS2-ARNTL-driven transcription. Ref.13
	Mutagenesis	503	1	K → R: Inhibits interaction with PER2. Does not suppress its nuclear localization. Inhibits its repression activity on CLOCK|NPAS2-ARNTL-driven transcription. Ref.13
	Mutagenesis	553	1	S → A: Shorter circadian rhythm; when associated with A-557. Ref.14
	Mutagenesis	557	1	S → A: Reduced in vitro MAPK-catalyzed phosphorylation. No effect on inhibition of CLOCK-ARNTL-mediated transcriptional activity. Very little in vitro MAPK-catalyzed phosphorylation; when associated with A-265. Shorter circadian rhythm; when associated with A-553. Ref.7 Ref.14
	Mutagenesis	557	1	S → D: Reduced inhibition of CLOCK-ARNTL-mediated transcriptional activity. No effect on nuclear localization nor on protein stability. Ref.7 Ref.14
	Sequence conflict	191 – 192	2	QQ → SR in BAA19864. Ref.5
	Sequence conflict	202	1	E → K in BAA19864. Ref.5
	Sequence conflict	327	1	M → V in BAA19864. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q9R194 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 4D6E7B199C392CBB	FASTA	592	66,850
	10 20 30 40 50 60 MAAAAVVAAT VPAQSMGADG ASSVHWFRKG LRLHDNPALL AAVRGARCVR CVYILDPWFA 70 80 90 100 110 120 ASSSVGINRW RFLLQSLEDL DTSLRKLNSR LFVVRGQPAD VFPRLFKEWG VTRLTFEYDS 130 140 150 160 170 180 EPFGKERDAA IMKMAKEAGV EVVTENSHTL YDLDRIIELN GQKPPLTYKR FQALISRMEL 190 200 210 220 230 240 PKKPAVAVSS QQMESCRAEI QENHDDTYGV PSLEELGFPT EGLGPAVWQG GETEALARLD 250 260 270 280 290 300 KHLERKAWVA NYERPRMNAN SLLASPTGLS PYLRFGCLSC RLFYYRLWDL YKKVKRNSTP 310 320 330 340 350 360 PLSLFGQLLW REFFYTAATN NPRFDRMEGN PICIQIPWDR NPEALAKWAE GKTGFPWIDA 370 380 390 400 410 420 IMTQLRQEGW IHHLARHAVA CFLTRGDLWV SWESGVRVFD ELLLDADFSV NAGSWMWLSC 430 440 450 460 470 480 SAFFQQFFHC YCPVGFGRRT DPSGDYIRRY LPKLKGFPSR YIYEPWNAPE SVQKAAKCII 490 500 510 520 530 540 GVDYPRPIVN HAETSRLNIE RMKQIYQQLS RYRGLCLLAS VPSCVEDLSH PVAEPGSSQA 550 560 570 580 590 GSISNTGPRA LSSGPASPKR KLEAAEEPPG EELTKRARVT EMPTQEPASK DS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INDUCTION, INTERACTION WITH PER1; PER2; PER3 AND TIMELESS. Strain: C57BL/6.
[2]	"The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y. Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J. Tissue: Embryo, Fetal brain and Thymus.
[3]	"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]. Strain: C57BL/6 and CD-1. Tissue: Brain and Neural stem cell.
[4]	"Prediction of the coding sequences of mouse homologues of KIAA gene: IV. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries." Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H., Nagase T., Ohara O., Koga H. DNA Res. 11:205-218(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-592. Tissue: Fetal brain.
[5]	"Characterization of photolyase/blue-light receptor homologs in mouse and human cells." Kobayashi K., Kanno S., Smit B., van der Horst G.T.J., Takao M., Yasui A. Nucleic Acids Res. 26:5086-5092(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-592, TISSUE SPECIFICITY, SUBCELLULAR LOCATION. Tissue: Liver.
[6]	"Circadian regulation of cryptochrome genes in the mouse." Miyamoto Y., Sancar A. Brain Res. Mol. Brain Res. 71:238-243(1999) [PubMed] [Europe PMC] [Abstract] Cited for: TISSUE SPECIFICITY, INDUCTION.
[7]	"Serine phosphorylation of mCRY1 and mCRY2 by mitogen-activated protein kinase." Sanada K., Harada Y., Sakai M., Todo T., Fukada Y. Genes Cells 9:697-708(2004) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH MAPK, PHOSPHORYLATION AT SER-265 AND SER-557, MUTAGENESIS OF SER-265 AND SER-557.
[8]	"The circadian regulatory proteins BMAL1 and cryptochromes are substrates of casein kinase Iepsilon." Eide E.J., Vielhaber E.L., Hinz W.A., Virshup D.M. J. Biol. Chem. 277:17248-17254(2002) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH PER1 AND PER2, PHOSPHORYLATION, SUBCELLULAR LOCATION.
[9]	"Ser-557-phosphorylated mCRY2 is degraded upon synergistic phosphorylation by glycogen synthase kinase-3 beta." Harada Y., Sakai M., Kurabayashi N., Hirota T., Fukada Y. J. Biol. Chem. 280:31714-31721(2005) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-557, SUBCELLULAR LOCATION.
[10]	"Post-translational regulation of circadian transcriptional CLOCK(NPAS2)/BMAL1 complex by CRYPTOCHROMES." Kondratov R.V., Kondratova A.A., Lee C., Gorbacheva V.Y., Chernov M.V., Antoch M.P. Cell Cycle 5:890-895(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH CLOCK-ARNTL COMPLEX, FUNCTION.
[11]	"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] [Europe PMC] [Abstract] Cited for: INTERACTION WITH NFIL3.
[12]	"Circadian mutant Overtime reveals F-box protein FBXL3 regulation of cryptochrome and period gene expression." Siepka S.M., Yoo S.H., Park J., Song W., Kumar V., Hu Y., Lee C., Takahashi J.S. Cell 129:1011-1023(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FBXL3, UBIQUITINATION.
[13]	"Identification of two amino acids in the C-terminal domain of mouse CRY2 essential for PER2 interaction." Ozber N., Baris I., Tatlici G., Gur I., Kilinc S., Unal E.B., Kavakli I.H. BMC Mol. Biol. 11:69-69(2010) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARNTL AND PER2, SUBCELLULAR LOCATION, MUTAGENESIS OF ARG-501 AND LYS-503.
[14]	"DYRK1A and glycogen synthase kinase 3beta, a dual-kinase mechanism directing proteasomal degradation of CRY2 for circadian timekeeping." Kurabayashi N., Hirota T., Sakai M., Sanada K., Fukada Y. Mol. Cell. Biol. 30:1757-1768(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-553 AND SER-557, MUTAGENESIS OF SER-553 AND SER-557.
[15]	"Competing E3 ubiquitin ligases govern circadian periodicity by degradation of CRY in nucleus and cytoplasm." Yoo S.H., Mohawk J.A., Siepka S.M., Shan Y., Huh S.K., Hong H.K., Kornblum I., Kumar V., Koike N., Xu M., Nussbaum J., Liu X., Chen Z., Chen Z.J., Green C.B., Takahashi J.S. Cell 152:1091-1105(2013) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY THE SCF(FBXL3) AND SCF(FBXL21) COMPLEXES, INTERACTION WITH FBXL3 AND FBXL21.
[16]	"FBXL21 regulates oscillation of the circadian clock through ubiquitination and stabilization of cryptochromes." Hirano A., Yumimoto K., Tsunematsu R., Matsumoto M., Oyama M., Kozuka-Hata H., Nakagawa T., Lanjakornsiripan D., Nakayama K.I., Fukada Y. Cell 152:1106-1118(2013) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION BY THE SCF(FBXL3) AND SCF(FBXL21) COMPLEXES, UBIQUITINATION AT LYS-125; LYS-241; LYS-347; LYS-474 AND LYS-503, INTERACTION WITH FBXL3 AND FBXL21.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF156987 mRNA. Translation: AAD46561.1.
AK041696 mRNA. Translation: BAC31037.1.
AK133781 mRNA. Translation: BAE21836.1.
BC054794 mRNA. Translation: AAH54794.1.
BC066799 mRNA. Translation: AAH66799.1.
AK172994 mRNA. Translation: BAD32272.1.
AB003433 mRNA. Translation: BAA19864.1.

IPI

IPI00128234.

RefSeq

NP_001106804.1. NM_001113333.1.
NP_034093.1. NM_009963.4.

UniGene

Mm.254181.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4I6E	X-ray	2.70	A	1-512	[»]
4I6G	X-ray	2.20	A/B	1-512	[»]
4I6J	X-ray	2.70	A	1-544	[»]

ProteinModelPortal

Q9R194.

SMR

Q9R194. Positions 21-507.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-38517N.

IntAct

Q9R194. 12 interactions.

STRING

10090.ENSMUSP00000106909.

PTM databases

PhosphoSite

Q9R194.

Proteomic databases

PaxDb

Q9R194.

PRIDE

Q9R194.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000090559; ENSMUSP00000088047; ENSMUSG00000068742.
ENSMUST00000111278; ENSMUSP00000106909; ENSMUSG00000068742.

GeneID

12953.

KEGG

mmu:12953.

Organism-specific databases

CTD

1408.

MGI

MGI:1270859. Cry2.

Rouge

Search...

Phylogenomic databases

eggNOG

COG0415.

GeneTree

ENSGT00500000044813.

HOGENOM

HOG000245622.

HOVERGEN

HBG053470.

InParanoid

Q9R194.

KO

K02295.

OMA

LCKHLLI.

OrthoDB

EOG4VT5WZ.

Enzyme and pathway databases

Reactome

REACT_109335. Circadian Clock.
REACT_24972. Circadian Clock (mouse).

Gene expression databases

ArrayExpress

Q9R194.

Bgee

Q9R194.

CleanEx

MM_CRY2.

Genevestigator

Q9R194.

GermOnline

ENSMUSG00000068742. Mus musculus.

Family and domain databases

Gene3D

3.40.50.620. 1 hit.

InterPro

IPR006050. DNA_photolyase_N.
IPR005101. Photolyase_FAD-bd/Cryptochr_C.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]

Pfam

PF00875. DNA_photolyase. 1 hit.
PF03441. FAD_binding_7. 1 hit.
[Graphical view]

SUPFAM

SSF52425. DNA_photolyase_N. 1 hit.
SSF48173. Photolyase_FAD-bd/Cryptochr_C. 1 hit.

PROSITE

PS00394. DNA_PHOTOLYASES_1_1. False negative.
PS51645. PHR_CRY_ALPHA_BETA. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

282666.

SOURCE

Search...

Entry information

Entry name

CRY2_MOUSE

Accession

Primary (citable) accession number: Q9R194
Secondary accession number(s): O08706, Q6A024

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 28, 2006
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 95 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program