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Q9R194 (CRY2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cryptochrome-2
Gene names
Name:Cry2
Synonyms:Kiaa0658
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length592 AA.
Sequence statusComplete.
Protein existenceEvidence 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 CRY1, 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 Ref.13

Cofactor

Binds 1 FAD per subunit. Only a minority of the protein molecules contain bound FAD. Contrary to the situation in photolyases, the FAD is bound in a shallow, surface-exposed pocket. Ref.18

Binds 1 5,10-methenyltetrahydrofolate non-covalently per subunit By similarity. Ref.18

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. Interacts with FBXL3 and FBXL21. FBXL3, PER2 and the cofactor FAD compete for overlapping binding sites. FBXL3 cannot bind CRY2 that interacts already with PER2 or that contains bound FAD. Interaction with PER2 inhibits its ubiquitination and vice versa. Interacts with PPP5C (via TPR repeats); the interaction downregulates the PPP5C phosphatase activity on CSNK1E. Ref.1 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.16 Ref.17 Ref.18

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.14

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.15

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.15

Sequence similarities

Belongs to the DNA photolyase class-1 family.

Contains 1 photolyase/cryptochrome alpha/beta domain.

Ontologies

Keywords
   Biological processBiological rhythms
Sensory transduction
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandChromophore
FAD
Flavoprotein
Nucleotide-binding
   Molecular functionPhotoreceptor protein
Receptor
Repressor
   PTMIsopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA repair

Inferred from electronic annotation. Source: InterPro

circadian rhythm

Inferred from mutant phenotype Ref.15. Source: UniProtKB

negative regulation of phosphoprotein phosphatase activity

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12738229Ref.13PubMed 19605937. Source: UniProtKB

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: Ensembl

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular region

Inferred from electronic annotation. Source: Ensembl

mitochondrion

Inferred from direct assay Ref.5. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.14Ref.5. Source: UniProtKB

   Molecular_functionDNA photolyase activity

Inferred from electronic annotation. Source: InterPro

FAD binding

Inferred from direct assay Ref.18. Source: UniProtKB

damaged DNA binding

Inferred from electronic annotation. Source: Ensembl

photoreceptor activity

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

protein kinase binding

Inferred from physical interaction Ref.15. Source: UniProtKB

single-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 592592Cryptochrome-2
PRO_0000261149

Regions

Domain21 – 150130Photolyase/cryptochrome alpha/beta
Nucleotide binding405 – 4073FAD
Region389 – 488100Required for inhibition of CLOCK-ARNTL-mediated transcription By similarity
Compositional bias2 – 54Poly-Ala

Sites

Binding site2701FAD; via amide nitrogen
Binding site3071FAD By similarity
Binding site3731FAD

Amino acid modifications

Modified residue2651Phosphoserine; by MAPK Ref.7
Modified residue5531Phosphoserine; by GSK3-beta Ref.15
Modified residue5571Phosphoserine; by DYRK1A and MAPK Ref.7 Ref.9 Ref.15
Cross-link125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17
Cross-link241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17
Cross-link347Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17
Cross-link474Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17
Cross-link503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.17

Experimental info

Mutagenesis2651S → 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
Mutagenesis2651S → D: Reduced inhibition of CLOCK-ARNTL-mediated transcriptional activity. No effect on nuclear localization nor on protein stability. Ref.7
Mutagenesis3101W → A: Decreases FBXL3 binding. Strongly decreases CRY2 degradation. Ref.18
Mutagenesis3391D → R: Strongly reduces PER1 binding. Ref.18
Mutagenesis3761R → A: Impairs protein folding. Abolishes binding of ARNTL, PER1 and FBXL3. Strongly reduces SKP1 binding. Ref.18
Mutagenesis4281F → D: Abolishes binding of FBXL3 and SKP1. Strongly decreases CRY2 degradation. Ref.18
Mutagenesis4991I → D: Abolishes binding of FBXL3 and SKP1. Strongly decreases CRY2 degradation. Ref.18
Mutagenesis5011R → Q: Inhibits interaction with PER2. Does not suppress its nuclear localization. Inhibits its repression activity on CLOCK|NPAS2-ARNTL-driven transcription. Ref.14
Mutagenesis5031K → R: Inhibits interaction with PER2. Does not suppress its nuclear localization. Inhibits its repression activity on CLOCK|NPAS2-ARNTL-driven transcription. Ref.14
Mutagenesis5171L → D: Decreases FBXL3 binding. Strongly decreases CRY2 degradation. Ref.18
Mutagenesis5531S → A: Shorter circadian rhythm; when associated with A-557. Ref.15
Mutagenesis5571S → 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.15
Mutagenesis5571S → D: Reduced inhibition of CLOCK-ARNTL-mediated transcriptional activity. No effect on nuclear localization nor on protein stability. Ref.7 Ref.15
Sequence conflict191 – 1922QQ → SR in BAA19864. Ref.5
Sequence conflict2021E → K in BAA19864. Ref.5
Sequence conflict3271M → V in BAA19864. Ref.5

Secondary structure

.................................................................................... 592
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9R194 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 4D6E7B199C392CBB

FASTA59266,850
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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]"CIPC is a mammalian circadian clock protein without invertebrate homologues."
Zhao W.N., Malinin N., Yang F.C., Staknis D., Gekakis N., Maier B., Reischl S., Kramer A., Weitz C.J.
Nat. Cell Biol. 9:268-275(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"SCF(FBXL3) ubiquitin ligase targets cryptochromes at their cofactor pocket."
Xing W., Busino L., Hinds T.R., Marionni S.T., Saifee N.H., Bush M.F., Pagano M., Zheng N.
Nature 496:64-68(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-512 IN COMPLEXES WITH FAD; SKP1 AND FBXL3, IDENTIFICATION IN A COMPLEX WITH SKP1 AND FBXL3, COFACTOR, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TRP-310; ASP-339; ARG-376; PHE-428; ILE-499 AND LEU-517.
+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.
RefSeqNP_034093.1. NM_009963.4.
UniGeneMm.254181.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4I6EX-ray2.70A1-512[»]
4I6GX-ray2.20A/B1-512[»]
4I6JX-ray2.70A1-544[»]
4MLPX-ray1.94A/B/C/D1-512[»]
ProteinModelPortalQ9R194.
SMRQ9R194. Positions 21-512.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid198907. 15 interactions.
DIPDIP-38517N.
IntActQ9R194. 13 interactions.
STRING10090.ENSMUSP00000106909.

PTM databases

PhosphoSiteQ9R194.

Proteomic databases

PaxDbQ9R194.
PRIDEQ9R194.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000090559; ENSMUSP00000088047; ENSMUSG00000068742.
ENSMUST00000111278; ENSMUSP00000106909; ENSMUSG00000068742.
GeneID12953.
KEGGmmu:12953.
UCSCuc008kxy.2. mouse.

Organism-specific databases

CTD1408.
MGIMGI:1270859. Cry2.
RougeSearch...

Phylogenomic databases

eggNOGCOG0415.
GeneTreeENSGT00500000044813.
HOGENOMHOG000245622.
HOVERGENHBG053470.
InParanoidQ9R194.
KOK02295.
OMAKCIIGVD.
OrthoDBEOG7QG43M.
PhylomeDBQ9R194.
TreeFamTF323191.

Enzyme and pathway databases

ReactomeREACT_109335. Circadian Clock.
REACT_24972. Circadian Clock.

Gene expression databases

ArrayExpressQ9R194.
BgeeQ9R194.
CleanExMM_CRY2.
GenevestigatorQ9R194.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
InterProIPR006050. DNA_photolyase_N.
IPR005101. Photolyase_FAD-bd/Cryptochr_C.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF00875. DNA_photolyase. 1 hit.
PF03441. FAD_binding_7. 1 hit.
[Graphical view]
SUPFAMSSF48173. SSF48173. 1 hit.
SSF52425. SSF52425. 1 hit.
PROSITEPS51645. PHR_CRY_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio282666.
PROQ9R194.
SOURCESearch...

Entry information

Entry nameCRY2_MOUSE
AccessionPrimary (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: April 16, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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