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Q49AN0

- CRY2_HUMAN

UniProt

Q49AN0 - CRY2_HUMAN

Protein

Cryptochrome-2

Gene

CRY2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 2 (28 Nov 2006)
      Previous versions | rss
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    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, NR1D2, RORA, RORB and RORG, 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/DEC1.3 Publications

    Cofactori

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

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei271 – 2711FAD; via amide nitrogenBy similarity
    Binding sitei308 – 3081FADBy similarity
    Binding sitei374 – 3741FADBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi406 – 4083FADBy similarity

    GO - Molecular functioni

    1. blue light photoreceptor activity Source: UniProtKB
    2. damaged DNA binding Source: UniProtKB
    3. DNA binding Source: UniProtKB
    4. DNA photolyase activity Source: InterPro
    5. FAD binding Source: UniProtKB
    6. phosphatase binding Source: UniProtKB
    7. protein binding Source: UniProtKB
    8. single-stranded DNA binding Source: UniProtKB
    9. transcription factor binding transcription factor activity Source: BHF-UCL
    10. transcription regulatory region sequence-specific DNA binding Source: UniProtKB
    11. ubiquitin binding Source: UniProtKB

    GO - Biological processi

    1. blue light signaling pathway Source: UniProtKB
    2. circadian regulation of gene expression Source: UniProtKB
    3. circadian rhythm Source: UniProtKB
    4. DNA repair Source: InterPro
    5. entrainment of circadian clock by photoperiod Source: UniProtKB
    6. glucose homeostasis Source: UniProtKB
    7. negative regulation of circadian rhythm Source: UniProtKB
    8. negative regulation of glucocorticoid receptor signaling pathway Source: UniProtKB
    9. negative regulation of phosphoprotein phosphatase activity Source: UniProtKB
    10. negative regulation of transcription, DNA-templated Source: UniProtKB
    11. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    12. protein-chromophore linkage Source: UniProtKB-KW
    13. regulation of circadian rhythm Source: UniProtKB
    14. regulation of sodium-dependent phosphate transport Source: MGI
    15. transcription, DNA-templated Source: UniProtKB-KW

    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

    ReactomeiREACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_24941. Circadian Clock.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cryptochrome-2
    Gene namesi
    Name:CRY2
    Synonyms:KIAA0658
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:2385. CRY2.

    Subcellular locationi

    Cytoplasm 1 Publication. Nucleus 1 Publication
    Note: Translocated to the nucleus through interaction with other Clock proteins such as PER2 or ARNTL.

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular region Source: MGI
    3. nucleus Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA26905.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 593593Cryptochrome-2PRO_0000261148Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Cross-linki126 – 126Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki242 – 242Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei266 – 2661Phosphoserine; by MAPKBy similarity
    Cross-linki348 – 348Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki475 – 475Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Cross-linki504 – 504Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
    Modified residuei554 – 5541Phosphoserine; by GSK3-betaBy similarity
    Modified residuei558 – 5581Phosphoserine; by DYRK1A and MAPKBy similarity

    Post-translational modificationi

    Phosphorylation on Ser-266 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-554 and Ser-558 in the suprachiasmatic nucleus (SCN) and liver. Phosphorylation at Ser-558 by DYRK1A promotes subsequent phosphorylation at Ser-554 by GSK3-beta: the two-step phosphorylation at the neighboring Ser residues leads to its proteasomal degradation By similarity.By similarity
    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-554 and Ser-558. Ubiquitination may be inhibited by PER2.2 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ49AN0.
    PaxDbiQ49AN0.
    PRIDEiQ49AN0.

    Expressioni

    Tissue specificityi

    Expressed in all tissues examined including fetal brain, fibroblasts, heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and leukocytes. Highest levels in heart and skeletal muscle.2 Publications

    Gene expression databases

    ArrayExpressiQ49AN0.
    BgeeiQ49AN0.
    CleanExiHS_CRY2.
    GenevestigatoriQ49AN0.

    Organism-specific databases

    HPAiHPA037577.

    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.2 Publications

    Protein-protein interaction databases

    BioGridi107798. 15 interactions.
    IntActiQ49AN0. 3 interactions.
    STRINGi9606.ENSP00000406751.

    Structurei

    3D structure databases

    DisProtiDP00473.
    ProteinModelPortaliQ49AN0.
    SMRiQ49AN0. Positions 22-513.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini22 – 151130Photolyase/cryptochrome alpha/betaAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni390 – 489100Required for inhibition of CLOCK-ARNTL-mediated transcriptionBy similarityAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DNA photolyase class-1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0415.
    HOGENOMiHOG000245622.
    HOVERGENiHBG053470.
    InParanoidiQ49AN0.
    KOiK02295.
    PhylomeDBiQ49AN0.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    InterProiIPR006050. DNA_photolyase_N.
    IPR005101. Photolyase_FAD-bd/Cryptochr_C.
    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]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q49AN0-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MAATVATAAA VAPAPAPGTD SASSVHWFRK GLRLHDNPAL LAAVRGARCV    50
    RCVYILDPWF AASSSVGINR WRFLLQSLED LDTSLRKLNS RLFVVRGQPA 100
    DVFPRLFKEW GVTRLTFEYD SEPFGKERDA AIMKMAKEAG VEVVTENSHT 150
    LYDLDRIIEL NGQKPPLTYK RFQAIISRME LPKKPVGLVT SQQMESCRAE 200
    IQENHDETYG VPSLEELGFP TEGLGPAVWQ GGETEALARL DKHLERKAWV 250
    ANYERPRMNA NSLLASPTGL SPYLRFGCLS CRLFYYRLWD LYKKVKRNST 300
    PPLSLFGQLL WREFFYTAAT NNPRFDRMEG NPICIQIPWD RNPEALAKWA 350
    EGKTGFPWID AIMTQLRQEG WIHHLARHAV ACFLTRGDLW VSWESGVRVF 400
    DELLLDADFS VNAGSWMWLS CSAFFQQFFH CYCPVGFGRR TDPSGDYIRR 450
    YLPKLKAFPS RYIYEPWNAP ESIQKAAKCI IGVDYPRPIV NHAETSRLNI 500
    ERMKQIYQQL SRYRGLCLLA SVPSCVEDLS HPVAEPSSSQ AGSMSSAGPR 550
    PLPSGPASPK RKLEAAEEPP GEELSKRARV AELPTPELPS KDA 593
    Length:593
    Mass (Da):66,947
    Last modified:November 28, 2006 - v2
    Checksum:iBF380424092BEBFB
    GO
    Isoform 2 (identifier: Q49AN0-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-72: MAATVATAAA...SSSVGINRWR → MPAPPGRTHTW

    Note: No experimental confirmation available.Curated

    Show »
    Length:532
    Mass (Da):60,593
    Checksum:i07E1FCDFAC27731A
    GO

    Sequence cautioni

    The sequence AAH35161.1 differs from that shown. Reason: Probable cloning artifact. Aberrant splice sites.
    The sequence BAG57993.1 differs from that shown. Reason: Erroneous termination at position 110. Translated as Trp.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti422 – 4221S → G in AAH35161. (PubMed:15489334)Curated
    Isoform 2 (identifier: Q49AN0-2)
    Sequence conflicti9 – 91H → L in BAG57993. (PubMed:14702039)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7272MAATV…INRWR → MPAPPGRTHTW in isoform 2. 1 PublicationVSP_038970Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK294904 mRNA. Translation: BAG57993.1. Sequence problems.
    AC068385 Genomic DNA. No translation available.
    BC035161 mRNA. Translation: AAH35161.1. Sequence problems.
    BC041814 mRNA. Translation: AAH41814.1.
    AB014558 mRNA. Translation: BAA31633.1.
    CCDSiCCDS44576.1. [Q49AN0-2]
    RefSeqiNP_001120929.1. NM_001127457.2. [Q49AN0-2]
    NP_066940.2. NM_021117.3.
    UniGeneiHs.532491.

    Genome annotation databases

    EnsembliENST00000417225; ENSP00000397419; ENSG00000121671. [Q49AN0-2]
    GeneIDi1408.
    KEGGihsa:1408.
    UCSCiuc009ykw.3. human. [Q49AN0-2]
    uc010rgo.2. human. [Q49AN0-1]

    Polymorphism databases

    DMDMi118572252.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Wikipedia

    Cryptochrome entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK294904 mRNA. Translation: BAG57993.1 . Sequence problems.
    AC068385 Genomic DNA. No translation available.
    BC035161 mRNA. Translation: AAH35161.1 . Sequence problems.
    BC041814 mRNA. Translation: AAH41814.1 .
    AB014558 mRNA. Translation: BAA31633.1 .
    CCDSi CCDS44576.1. [Q49AN0-2 ]
    RefSeqi NP_001120929.1. NM_001127457.2. [Q49AN0-2 ]
    NP_066940.2. NM_021117.3.
    UniGenei Hs.532491.

    3D structure databases

    DisProti DP00473.
    ProteinModelPortali Q49AN0.
    SMRi Q49AN0. Positions 22-513.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107798. 15 interactions.
    IntActi Q49AN0. 3 interactions.
    STRINGi 9606.ENSP00000406751.

    Polymorphism databases

    DMDMi 118572252.

    Proteomic databases

    MaxQBi Q49AN0.
    PaxDbi Q49AN0.
    PRIDEi Q49AN0.

    Protocols and materials databases

    DNASUi 1408.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000417225 ; ENSP00000397419 ; ENSG00000121671 . [Q49AN0-2 ]
    GeneIDi 1408.
    KEGGi hsa:1408.
    UCSCi uc009ykw.3. human. [Q49AN0-2 ]
    uc010rgo.2. human. [Q49AN0-1 ]

    Organism-specific databases

    CTDi 1408.
    GeneCardsi GC11P045868.
    H-InvDB HIX0201587.
    HGNCi HGNC:2385. CRY2.
    HPAi HPA037577.
    MIMi 603732. gene.
    neXtProti NX_Q49AN0.
    PharmGKBi PA26905.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0415.
    HOGENOMi HOG000245622.
    HOVERGENi HBG053470.
    InParanoidi Q49AN0.
    KOi K02295.
    PhylomeDBi Q49AN0.

    Enzyme and pathway databases

    Reactomei REACT_111118. BMAL1:CLOCK,NPAS2 activates circadian gene expression.
    REACT_24941. Circadian Clock.

    Miscellaneous databases

    GenomeRNAii 1408.
    NextBioi 5757.
    PROi Q49AN0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q49AN0.
    Bgeei Q49AN0.
    CleanExi HS_CRY2.
    Genevestigatori Q49AN0.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    InterProi IPR006050. DNA_photolyase_N.
    IPR005101. Photolyase_FAD-bd/Cryptochr_C.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00875. DNA_photolyase. 1 hit.
    PF03441. FAD_binding_7. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48173. SSF48173. 1 hit.
    SSF52425. SSF52425. 1 hit.
    PROSITEi PS51645. PHR_CRY_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Putative human blue-light photoreceptors hCRY1 and hCRY2 are flavoproteins."
      Hsu D.S., Zhao X., Zhao S., Kazantsev A., Wang R.-P., Todo T., Wei Y.-F., Sancar A.
      Biochemistry 35:13871-13877(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION, TISSUE SPECIFICITY.
      Tissue: Fetal brain.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] (ISOFORM 1).
      Tissue: Testis.
    5. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 5-593 (ISOFORM 1).
      Tissue: Brain.
    6. "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: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    7. "Light-independent role of CRY1 and CRY2 in the mammalian circadian clock."
      Griffin E.A. Jr., Staknis D., Weitz C.J.
      Science 286:768-771(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    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] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION.
    9. Cited for: FUNCTION.
    10. "Posttranslational regulation of the mammalian circadian clock by cryptochrome and protein phosphatase 5."
      Partch C.L., Shields K.F., Thompson C.L., Selby C.P., Sancar A.
      Proc. Natl. Acad. Sci. U.S.A. 103:10467-10472(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH PPP5C.
    11. "SCFFbxl3 controls the oscillation of the circadian clock by directing the degradation of cryptochrome proteins."
      Busino L., Bassermann F., Maiolica A., Lee C., Nolan P.M., Godinho S.I., Draetta G.F., Pagano M.
      Science 316:900-904(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY, UBIQUITINATION BY FBXL3, INTERACTION WITH FBXL3.
    12. "Metabolism and the circadian clock converge."
      Eckel-Mahan K., Sassone-Corsi P.
      Physiol. Rev. 93:107-135(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    13. "Molecular architecture of the mammalian circadian clock."
      Partch C.L., Green C.B., Takahashi J.S.
      Trends Cell Biol. 24:90-99(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiCRY2_HUMAN
    AccessioniPrimary (citable) accession number: Q49AN0
    Secondary accession number(s): B4DH32, O75148, Q8IV71
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 28, 2006
    Last sequence update: November 28, 2006
    Last modified: October 1, 2014
    This is version 89 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny 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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3