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Protein

Cryptochrome-2

Gene

Cry2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Transcriptional repressor which forms a core component of the circadian clock. The circadian clock, an internal time-keeping system, regulates various physiological processes through the generation of approximately 24 hour circadian rhythms in gene expression, which are translated into rhythms in metabolism and behavior. It is derived from the Latin roots 'circa' (about) and 'diem' (day) and acts as an important regulator of a wide array of physiological functions including metabolism, sleep, body temperature, blood pressure, endocrine, immune, cardiovascular, and renal function. Consists of two major components: the central clock, residing in the suprachiasmatic nucleus (SCN) of the brain, and the peripheral clocks that are present in nearly every tissue and organ system. Both the central and peripheral clocks can be reset by environmental cues, also known as Zeitgebers (German for 'timegivers'). The predominant Zeitgeber for the central clock is light, which is sensed by retina and signals directly to the SCN. The central clock entrains the peripheral clocks through neuronal and hormonal signals, body temperature and feeding-related cues, aligning all clocks with the external light/dark cycle. Circadian rhythms allow an organism to achieve temporal homeostasis with its environment at the molecular level by regulating gene expression to create a peak of protein expression once every 24 hours to control when a particular physiological process is most active with respect to the solar day. Transcription and translation of core clock components (CLOCK, NPAS2, ARNTL/BMAL1, ARNTL2/BMAL2, PER1, PER2, PER3, CRY1 and CRY2) plays a critical role in rhythm generation, whereas delays imposed by post-translational modifications (PTMs) are important for determining the period (tau) of the rhythms (tau refers to the period of a rhythm and is the length, in time, of one complete cycle). A diurnal rhythm is synchronized with the day/night cycle, while the ultradian and infradian rhythms have a period shorter and longer than 24 hours, respectively. Disruptions in the circadian rhythms contribute to the pathology of cardiovascular diseases, cancer, metabolic syndromes and aging. A transcription/translation feedback loop (TTFL) forms the core of the molecular circadian clock mechanism. Transcription factors, CLOCK or NPAS2 and ARNTL/BMAL1 or ARNTL2/BMAL2, form the positive limb of the feedback loop, act in the form of a heterodimer and activate the transcription of core clock genes and clock-controlled genes (involved in key metabolic processes), harboring E-box elements (5'-CACGTG-3') within their promoters. The core clock genes: PER1/2/3 and CRY1/2 which are transcriptional repressors form the negative limb of the feedback loop and interact with the CLOCK|NPAS2-ARNTL/BMAL1|ARNTL2/BMAL2 heterodimer inhibiting its activity and thereby negatively regulating their own expression. This heterodimer also activates nuclear receptors NR1D1/2 and RORA/B/G, which form a second feedback loop and which activate and repress ARNTL/BMAL1 transcription, respectively. CRY1 and CRY2 have redundant functions but also differential and selective contributions at least in defining the pace of the SCN circadian clock and its circadian transcriptional outputs. Less potent transcriptional repressor in cerebellum and liver than CRY1, though less effective in lengthening the period of the SCN oscillator. Seems to play a critical role in tuning SCN circadian period by opposing the action of CRY1. With CRY1, dispensable for circadian rhythm generation but necessary for the development of intercellular networks for rhythm synchrony. May mediate circadian regulation of cAMP signaling and gluconeogenesis by blocking glucagon-mediated increases in intracellular cAMP concentrations and in CREB1 phosphorylation. Besides its role in the maintenance of the circadian clock, is also involved in the regulation of other processes. Plays a key role in glucose and lipid metabolism modulation, in part, through the transcriptional regulation of genes involved in these pathways, such as LEP or ACSL4. Represses glucocorticoid receptor NR3C1/GR-induced transcriptional activity by binding to glucocorticoid response elements (GREs). Represses the CLOCK-ARNTL/BMAL1 induced transcription of BHLHE40/DEC1 and NAMPT.10 Publications

Cofactori

Protein has several cofactor binding sites:
  • FAD1 PublicationNote: 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.1 Publication
  • 5,10-methylenetetrahydrofolateBy similarityNote: Binds 1 5,10-methenyltetrahydrofolate non-covalently per subunit.By similarity

Enzyme regulationi

KL001 (N-[3-(9H-carbazol-9-yl)-2-hydroxypropyl]-N-(2-furanylmethyl)-methanesulfonamide) binds to CRY1 and stabilizes it by inhibiting FBXL3- and ubiquitin-dependent degradation of CRY1 resulting in lengthening of the circadian periods. KL001-mediated CRY1 stabilization can inhibit glucagon-induced gluconeogenesis in primary hepatocytes.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei270 – 2701FAD; via amide nitrogen
Binding sitei307 – 3071FADBy similarity
Binding sitei373 – 3731FAD

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi405 – 4073FAD

GO - Molecular functioni

  • damaged DNA binding Source: MGI
  • DNA binding Source: MGI
  • FAD binding Source: UniProtKB
  • kinase binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • phosphatase binding Source: MGI
  • photoreceptor activity Source: UniProtKB-KW
  • protein kinase binding Source: UniProtKB
  • single-stranded DNA binding Source: MGI
  • transcription factor activity, transcription factor binding Source: MGI
  • transcription regulatory region sequence-specific DNA binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

GO - Biological processi

  • circadian regulation of gene expression Source: UniProtKB
  • circadian rhythm Source: UniProtKB
  • entrainment of circadian clock by photoperiod Source: UniProtKB
  • glucose homeostasis Source: UniProtKB
  • lipid storage Source: UniProtKB
  • negative regulation of circadian rhythm Source: UniProtKB
  • negative regulation of glucocorticoid receptor signaling pathway Source: UniProtKB
  • negative regulation of glucocorticoid secretion Source: UniProtKB
  • negative regulation of phosphoprotein phosphatase activity Source: MGI
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: MGI
  • protein-chromophore linkage Source: UniProtKB-KW
  • protein import into nucleus Source: MGI
  • regulation of circadian rhythm Source: UniProtKB
  • response to insulin Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Photoreceptor protein, Receptor, Repressor

Keywords - Biological processi

Biological rhythms, Sensory transduction, Transcription, Transcription regulation

Keywords - Ligandi

Chromophore, FAD, Flavoprotein, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-400253. Circadian Clock.
R-MMU-508751. Circadian Clock.

Names & Taxonomyi

Protein namesi
Recommended name:
Cryptochrome-2
Gene namesi
Name:Cry2
Synonyms:Kiaa0658
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1270859. Cry2.

Subcellular locationi

  • Cytoplasm
  • Nucleus

  • Note: Translocated to the nucleus through interaction with other Clock proteins such as PER2 or ARNTL.

GO - Cellular componenti

  • cytoplasm Source: MGI
  • cytosol Source: Reactome
  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Disruption phenotypei

Animals show longer circadian periods. Double knockouts of CRY1 and CRY2 show slightly decrease body weight and lose the cycling rhythmicity of feeding behavior, energy expenditure and glucocorticorids expression. Glucose homeostasis is severely disrupted and animals exhibit elevated blood glucose in response to acute feeding after an overnight fast as well as severely impaired glucose clearance in a glucose tolerance test. When challenged with high-fat diet, animals rapidly gain weight and surpass that of wild-type mice, despite displaying hypophagia. They exhibit hyperinsulinemia and selective insulin resistance in the liver and muscle but show high insulin sensitivity in adipose tissue and consequent increased lipid uptake. Mice display enlarged gonadal, subcutaneous and perirenal fat deposits with adipocyte hypertrophy and increased lipied accumulation in liver.4 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi265 – 2651S → 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. 1 Publication
Mutagenesisi265 – 2651S → D: Reduced inhibition of CLOCK-ARNTL-mediated transcriptional activity. No effect on nuclear localization nor on protein stability. 1 Publication
Mutagenesisi310 – 3101W → A: Decreases FBXL3 binding. Strongly decreases CRY2 degradation. 1 Publication
Mutagenesisi339 – 3391D → R: Strongly reduces PER1 binding. 1 Publication
Mutagenesisi376 – 3761R → A: Impairs protein folding. Abolishes binding of ARNTL, PER1 and FBXL3. Strongly reduces SKP1 binding. 1 Publication
Mutagenesisi428 – 4281F → D: Abolishes binding of FBXL3 and SKP1. Strongly decreases CRY2 degradation. 1 Publication
Mutagenesisi499 – 4991I → D: Abolishes binding of FBXL3 and SKP1. Strongly decreases CRY2 degradation. 1 Publication
Mutagenesisi501 – 5011R → Q: Inhibits interaction with PER2. Does not suppress its nuclear localization. Inhibits its repression activity on CLOCK|NPAS2-ARNTL-driven transcription. 1 Publication
Mutagenesisi503 – 5031K → R: Inhibits interaction with PER2. Does not suppress its nuclear localization. Inhibits its repression activity on CLOCK|NPAS2-ARNTL-driven transcription. 1 Publication
Mutagenesisi517 – 5171L → D: Decreases FBXL3 binding. Strongly decreases CRY2 degradation. 1 Publication
Mutagenesisi553 – 5531S → A: Shorter circadian rhythm; when associated with A-557. 1 Publication
Mutagenesisi557 – 5571S → 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. 2 Publications
Mutagenesisi557 – 5571S → D: Reduced inhibition of CLOCK-ARNTL-mediated transcriptional activity. No effect on nuclear localization nor on protein stability. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 592592Cryptochrome-2PRO_0000261149Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei89 – 891PhosphoserineBy similarity
Cross-linki125 – 125Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki241 – 241Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei265 – 2651Phosphoserine; by MAPK2 Publications
Modified residuei298 – 2981PhosphoserineBy similarity
Cross-linki347 – 347Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki474 – 474Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki503 – 503Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei553 – 5531Phosphoserine; by GSK3-beta2 Publications
Modified residuei557 – 5571Phosphoserine; by DYRK1A and MAPK4 Publications

Post-translational modificationi

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.4 Publications
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. Ubiquitination may be inhibited by PER2.6 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9R194.
PaxDbiQ9R194.
PeptideAtlasiQ9R194.
PRIDEiQ9R194.

PTM databases

iPTMnetiQ9R194.
PhosphoSiteiQ9R194.

Expressioni

Tissue specificityi

Expressed in all tissues examined including heart, brain, spleen, lung, liver, skeletal muscle, kidney and testis. Weak expression in spleen.3 Publications

Inductioni

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 ZT9.3 Publications

Gene expression databases

BgeeiENSMUSG00000068742.
CleanExiMM_CRY2.
GenevisibleiQ9R194. MM.

Interactioni

Subunit structurei

Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARNTL/BMAL1 or ARNTL2/BMAL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts directly with PER1 and PER2 C-terminal domains. Interaction with PER2 inhibits its ubiquitination and vice versa. 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. Interacts with PPP5C (via TPR repeats); the interaction downregulates the PPP5C phosphatase activity on CSNK1E. AR, NR1D1, NR3C1/GR, RORA and RORC; the interaction, at least, with NR3C1/GR is ligand dependent. Interacts with PRKDC and CIART.17 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ArntlQ9WTL86EBI-1266619,EBI-644534
Fbxl21Q8BFZ44EBI-1266619,EBI-6898235
Fbxl3Q8C4V46EBI-1266619,EBI-1266589
Per2O549434EBI-1266619,EBI-1266779

GO - Molecular functioni

  • kinase binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • phosphatase binding Source: MGI
  • protein kinase binding Source: UniProtKB
  • ubiquitin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi198907. 15 interactions.
DIPiDIP-38517N.
IntActiQ9R194. 13 interactions.
STRINGi10090.ENSMUSP00000088047.

Structurei

Secondary structure

1
592
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi22 – 265Combined sources
Beta strandi32 – 354Combined sources
Helixi37 – 437Combined sources
Beta strandi47 – 559Combined sources
Helixi59 – 613Combined sources
Helixi67 – 8519Combined sources
Turni86 – 883Combined sources
Beta strandi91 – 966Combined sources
Helixi98 – 10912Combined sources
Beta strandi113 – 1175Combined sources
Helixi122 – 13716Combined sources
Beta strandi141 – 1455Combined sources
Beta strandi148 – 1514Combined sources
Helixi153 – 1597Combined sources
Turni160 – 1623Combined sources
Helixi168 – 1769Combined sources
Helixi190 – 1945Combined sources
Helixi204 – 2085Combined sources
Turni213 – 2175Combined sources
Helixi232 – 24211Combined sources
Helixi245 – 2517Combined sources
Helixi259 – 2624Combined sources
Helixi270 – 2745Combined sources
Helixi280 – 29415Combined sources
Beta strandi295 – 2973Combined sources
Helixi302 – 3054Combined sources
Helixi306 – 31813Combined sources
Turni322 – 3254Combined sources
Helixi342 – 3509Combined sources
Helixi356 – 36813Combined sources
Helixi373 – 38311Combined sources
Turni384 – 3885Combined sources
Helixi392 – 40211Combined sources
Helixi408 – 41811Combined sources
Beta strandi421 – 4233Combined sources
Helixi435 – 4406Combined sources
Helixi445 – 4506Combined sources
Helixi452 – 4543Combined sources
Helixi459 – 4624Combined sources
Helixi465 – 4673Combined sources
Helixi470 – 4756Combined sources
Turni480 – 4823Combined sources
Helixi491 – 50717Combined sources
Beta strandi517 – 5215Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I6EX-ray2.70A1-512[»]
4I6GX-ray2.20A/B1-512[»]
4I6JX-ray2.70A1-544[»]
4MLPX-ray1.94A/B/C/D1-512[»]
4U8HX-ray2.80A/C1-510[»]
ProteinModelPortaliQ9R194.
SMRiQ9R194. Positions 21-512.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 150130Photolyase/cryptochrome alpha/betaAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni389 – 488100Required for inhibition of CLOCK-ARNTL-mediated transcriptionBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi2 – 54Poly-Ala

Sequence similaritiesi

Belongs to the DNA photolyase class-1 family.Curated

Phylogenomic databases

eggNOGiKOG0133. Eukaryota.
COG0415. LUCA.
GeneTreeiENSGT00500000044813.
HOGENOMiHOG000245622.
HOVERGENiHBG053470.
InParanoidiQ9R194.
KOiK02295.
OMAiFYYRLWE.
OrthoDBiEOG091G07M3.
PhylomeDBiQ9R194.
TreeFamiTF323191.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR005101. Cryptochr/Photolyase_FAD-bd.
IPR006050. DNA_photolyase_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00875. DNA_photolyase. 1 hit.
PF03441. FAD_binding_7. 1 hit.
[Graphical view]
SUPFAMiSSF48173. SSF48173. 1 hit.
SSF52425. SSF52425. 1 hit.
PROSITEiPS51645. PHR_CRY_ALPHA_BETA. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9R194-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAAVVAAT VPAQSMGADG ASSVHWFRKG LRLHDNPALL AAVRGARCVR
60 70 80 90 100
CVYILDPWFA ASSSVGINRW RFLLQSLEDL DTSLRKLNSR LFVVRGQPAD
110 120 130 140 150
VFPRLFKEWG VTRLTFEYDS EPFGKERDAA IMKMAKEAGV EVVTENSHTL
160 170 180 190 200
YDLDRIIELN GQKPPLTYKR FQALISRMEL PKKPAVAVSS QQMESCRAEI
210 220 230 240 250
QENHDDTYGV PSLEELGFPT EGLGPAVWQG GETEALARLD KHLERKAWVA
260 270 280 290 300
NYERPRMNAN SLLASPTGLS PYLRFGCLSC RLFYYRLWDL YKKVKRNSTP
310 320 330 340 350
PLSLFGQLLW REFFYTAATN NPRFDRMEGN PICIQIPWDR NPEALAKWAE
360 370 380 390 400
GKTGFPWIDA IMTQLRQEGW IHHLARHAVA CFLTRGDLWV SWESGVRVFD
410 420 430 440 450
ELLLDADFSV NAGSWMWLSC SAFFQQFFHC YCPVGFGRRT DPSGDYIRRY
460 470 480 490 500
LPKLKGFPSR YIYEPWNAPE SVQKAAKCII GVDYPRPIVN HAETSRLNIE
510 520 530 540 550
RMKQIYQQLS RYRGLCLLAS VPSCVEDLSH PVAEPGSSQA GSISNTGPRA
560 570 580 590
LSSGPASPKR KLEAAEEPPG EELTKRARVT EMPTQEPASK DS
Length:592
Mass (Da):66,850
Last modified:May 1, 2000 - v1
Checksum:i4D6E7B199C392CBB
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti191 – 1922QQ → SR in BAA19864 (PubMed:9801304).Curated
Sequence conflicti202 – 2021E → K in BAA19864 (PubMed:9801304).Curated
Sequence conflicti327 – 3271M → V in BAA19864 (PubMed:9801304).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16447.1.
RefSeqiNP_034093.1. NM_009963.4.
UniGeneiMm.254181.

Genome annotation databases

EnsembliENSMUST00000090559; ENSMUSP00000088047; ENSMUSG00000068742.
ENSMUST00000111278; ENSMUSP00000106909; ENSMUSG00000068742.
GeneIDi12953.
KEGGimmu:12953.
UCSCiuc008kxy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS16447.1.
RefSeqiNP_034093.1. NM_009963.4.
UniGeneiMm.254181.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I6EX-ray2.70A1-512[»]
4I6GX-ray2.20A/B1-512[»]
4I6JX-ray2.70A1-544[»]
4MLPX-ray1.94A/B/C/D1-512[»]
4U8HX-ray2.80A/C1-510[»]
ProteinModelPortaliQ9R194.
SMRiQ9R194. Positions 21-512.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198907. 15 interactions.
DIPiDIP-38517N.
IntActiQ9R194. 13 interactions.
STRINGi10090.ENSMUSP00000088047.

PTM databases

iPTMnetiQ9R194.
PhosphoSiteiQ9R194.

Proteomic databases

MaxQBiQ9R194.
PaxDbiQ9R194.
PeptideAtlasiQ9R194.
PRIDEiQ9R194.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000090559; ENSMUSP00000088047; ENSMUSG00000068742.
ENSMUST00000111278; ENSMUSP00000106909; ENSMUSG00000068742.
GeneIDi12953.
KEGGimmu:12953.
UCSCiuc008kxy.2. mouse.

Organism-specific databases

CTDi1408.
MGIiMGI:1270859. Cry2.
RougeiSearch...

Phylogenomic databases

eggNOGiKOG0133. Eukaryota.
COG0415. LUCA.
GeneTreeiENSGT00500000044813.
HOGENOMiHOG000245622.
HOVERGENiHBG053470.
InParanoidiQ9R194.
KOiK02295.
OMAiFYYRLWE.
OrthoDBiEOG091G07M3.
PhylomeDBiQ9R194.
TreeFamiTF323191.

Enzyme and pathway databases

ReactomeiR-MMU-1368108. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
R-MMU-1368110. Bmal1:Clock,Npas2 activates circadian gene expression.
R-MMU-400253. Circadian Clock.
R-MMU-508751. Circadian Clock.

Miscellaneous databases

PROiQ9R194.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000068742.
CleanExiMM_CRY2.
GenevisibleiQ9R194. MM.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
InterProiIPR005101. Cryptochr/Photolyase_FAD-bd.
IPR006050. DNA_photolyase_N.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF00875. DNA_photolyase. 1 hit.
PF03441. FAD_binding_7. 1 hit.
[Graphical view]
SUPFAMiSSF48173. SSF48173. 1 hit.
SSF52425. SSF52425. 1 hit.
PROSITEiPS51645. PHR_CRY_ALPHA_BETA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCRY2_MOUSE
AccessioniPrimary (citable) accession number: Q9R194
Secondary accession number(s): O08706, Q6A024
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 28, 2006
Last sequence update: May 1, 2000
Last modified: September 7, 2016
This is version 127 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.