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Q49AN0

- CRY2_HUMAN

UniProt

Q49AN0 - CRY2_HUMAN

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Protein
Cryptochrome-2
Gene
CRY2, KIAA0658
Organism
Homo sapiens (Human)
Status
Reviewed - 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, 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/DEC1.2 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.
Binds 1 5,10-methenyltetrahydrofolate non-covalently per subunit By similarity.

Sites

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

Regions

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

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. DNA photolyase activity Source: InterPro
  3. FAD binding Source: UniProtKB
  4. blue light photoreceptor activity Source: UniProtKB
  5. damaged DNA 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
Complete GO annotation...

GO - Biological processi

  1. DNA repair Source: InterPro
  2. blue light signaling pathway Source: UniProtKB
  3. circadian regulation of gene expression Source: UniProtKB
  4. circadian rhythm Source: UniProtKB
  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 from RNA polymerase II promoter Source: BHF-UCL
  11. negative regulation of transcription, DNA-templated Source: UniProtKB
  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
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

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

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA26905.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 593593Cryptochrome-2
PRO_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 MAPK By 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-beta By similarity
Modified residuei558 – 5581Phosphoserine; by DYRK1A and MAPK By 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.
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.

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.

Family & Domainsi

Domains and Repeats

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

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni390 – 489100Required for inhibition of CLOCK-ARNTL-mediated transcription By similarity
Add
BLAST

Sequence similaritiesi

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.

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.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7272MAATV…INRWR → MPAPPGRTHTW in isoform 2.
VSP_038970Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti422 – 4221S → G in AAH35161. 1 Publication
Isoform 2 (identifier: Q49AN0-2)
Sequence conflicti9 – 91H → L in BAG57993. 1 Publication

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...

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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 88 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

Similar proteinsi