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UniProtKB/Swiss-Prot entry Q16526


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CRY1_HUMAN
Primary accession number Q16526
Secondary accession numbers None
Integrated into Swiss-Prot on November 28, 2006
Sequence was last modified on November 1, 1996 (Sequence version 1)
Annotations were last modified on    March 18, 2008 (Entry version 50)
Name and origin of the protein
Protein name Cryptochrome-1
Synonyms None
Gene name
Name: CRY1
Synonyms: PHLL1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHARACTERIZATION.
TISSUE=Fibroblast;
DOI=10.1021/bi962209o; PubMed=8909283 [NCBI, ExPASy, EBI, Israel, Japan]
Hsu D.S., Zhao X., Zhao S., Kazantsev A., Wang R.-P., Todo T., Wei Y.-F., Sancar A.;
"Putative human blue-light photoreceptors hCRY1 and hCRY2 are flavoproteins.";
Biochemistry 35:13871-13877(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Testis;
DOI=10.1006/geno.1996.0539; PubMed=8921389 [NCBI, ExPASy, EBI, Israel, Japan]
van der Spek P.J., Kobayashi K., Bootsma D., Takao M., Eker A.P.M., Yasui A.;
"Cloning, tissue expression, and mapping of a human photolyase homolog with similarity to plant blue-light receptors.";
Genomics 37:177-182(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=8600518 [NCBI, ExPASy, EBI, Israel, Japan]
Todo T., Ryo H., Yamamoto K., Toh H., Inui T., Ayaki H., Nomura T., Ikenaga M.;
"Similarity among the Drosophila (6-4)photolyase, a human photolyase homolog, and the DNA photolyase-blue-light photoreceptor family.";
Science 272:109-112(1996).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
DOI=10.1126/science.286.5440.768; PubMed=10531061 [NCBI, ExPASy, EBI, Israel, Japan]
Griffin E.A. Jr., Staknis D., Weitz C.J.;
"Light-independent role of CRY1 and CRY2 in the mammalian circadian clock.";
Science 286:768-771(1999).
Comments
  • FUNCTION: Blue light-dependent regulator of the circadian feedback loop. Inhibits CLOCK|NPAS2-ARNTL E box-mediated transcription. Acts, in conjunction with CRY2, in maintaining period length and circadian rhythmicity. Has no photolyase activity. Capable of translocating circadian clock core proteins such as PER proteins to the nucleus. May inhibit CLOCK|NPAS2-ARNTL transcriptional activity through stabilizing the unphosphorylated form of ARNTL (By similarity).
  • COFACTOR: Binds 1 FAD per subunit.
  • COFACTOR: Binds 1 5,10-methenyltetrahydrofolate non-covalently per subunit.
  • SUBUNIT: Component of the circadian core oscillator, which includes the CRY proteins, CLOCK or NPAS2, ARNTL or ARNTL2, CSNK1D and/or CSNK1E, TIMELESS, and the PER proteins. Interacts directly with TIMELESS and the PER proteins. Interacts directly with PER1 and PER2 C-terminal domains. Interaction with PER2 inhibits its ubiquitination and vice versa. Binds MAPK (By similarity).
  • SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Translocated to the nucleus through interaction with other Clock proteins such as PER2 or ARNTL (By similarity).
  • INDUCTION: Expression is regulated by light and circadian rhythms. Peak expression in the suprachiasma nucleus (SCN) and eye at the day/night transition (CT12). Levels decrease with ARNTL-CLOCK inhibition as part of the autoregulatory feedback loop.
  • PTM: Phosphorylation on Ser-247 by MAPK is important for the inhibition of CLOCK-ARNTL-mediated transcriptional activity. Phosphorylation by CSNK1E requires interaction with PER1 or PER2 (By similarity).
  • SIMILARITY: Belongs to the DNA photolyase class-1 family.
  • SIMILARITY: Contains 1 DNA photolyase domain.
  • WEB RESOURCE: Name=Wikipedia; Note=Cryptochrome entry; URL="http://en.wikipedia.org/wiki/Cryptochrome";.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D84657; BAA12710.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D83702; BAA12068.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC030519; AAH30519.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_004066.1; -.
UniGene Hs.151573
3D structure databases
ModBase Q16526.
PTM databases
PhosphoSite Q16526; -.
Organism-specific databases
HGNC HGNC:2384; CRY1.
GeneLynx CRY1; Homo sapiens.
GenAtlas CRY1.
MIM 601933; gene. [NCBI / EBI]
PharmGKB PA26904; -.
GeneCards Q16526.
Gene expression databases
ArrayExpress Q16526; -.
CleanEx HS_CRY1; -.
GermOnline ENSG00000008405; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (traceable author statement from ProtInc).
GO:0003677; Molecular function: DNA binding (traceable author statement from ProtInc).
GO:0008020; Molecular function: G-protein coupled photoreceptor activity (traceable author statement from ProtInc).
GO:0007623; Biological process: circadian rhythm (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002081; Cryptochrome/DNA_photolyase_1.
IPR006050; DNA_photolyase_N.
IPR005101; Photolyase_FAD-bd/Cryptochr_C.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF00875; DNA_photolyase; 1.
PF03441; FAD_binding_7; 1.
Pfam graphical view of domain structure.
ProDom PD004390; FAD_binding_N; 1.
[Domain structure / List of seq. sharing at least 1 domain]
PROSITE PS00394; DNA_PHOTOLYASES_1_1; FALSE_NEG.
BLOCKS Q16526.
Genome annotation databases
Ensembl ENSG00000008405; Homo sapiens. [Contig view]
GeneID 1407; -.
KEGG hsa:1407; -.
Other
SOURCE CRY1; Homo sapiens.
ProtoNet Q16526.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Biological rhythms; Chromophore; Cytoplasm; FAD; Flavoprotein; Nucleotide-binding; Nucleus; Phosphoprotein; Photoreceptor protein; Receptor; Repressor; Sensory transduction; Transcription; Transcription regulation.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   586  586     Cryptochrome-1. PRO_0000261140
DOMAIN   3   178  176     DNA photolyase. 
REGION   211   488  278     FAD-binding. 
REGION   371   470  100     Required for inhibition of CLOCK-ARNTL-mediated transcription (By similarity). 
MOD_RES   247   247        Phosphoserine; by MAPK (By similarity). 
Sequence information
Length: 586 AA [This is the length of the unprocessed precursor] Molecular weight: 66395 Da [This is the MW of the unprocessed precursor] CRC64: 96A5B09A6364D3B9 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MGVNAVHWFR KGLRLHDNPA LKECIQGADT IRCVYILDPW FAGSSNVGIN RWRFLLQCLE 

        70         80         90        100        110        120 
DLDANLRKLN SRLFVIRGQP ADVFPRLFKE WNITKLSIEY DSEPFGKERD AAIKKLATEA 

       130        140        150        160        170        180 
GVEVIVRISH TLYDLDKIIE LNGGQPPLTY KRFQTLISKM EPLEIPVETI TSEVIEKCTT 

       190        200        210        220        230        240 
PLSDDHDEKY GVPSLEELGF DTDGLSSAVW PGGETEALTR LERHLERKAW VANFERPRMN 

       250        260        270        280        290        300 
ANSLLASPTG LSPYLRFGCL SCRLFYFKLT DLYKKVKKNS SPPLSLYGQL LWREFFYTAA 

       310        320        330        340        350        360 
TNNPRFDKME GNPICVQIPW DKNPEALAKW AEGRTGFPWI DAIMTQLRQE GWIHHLARHA 

       370        380        390        400        410        420 
VACFLTRGDL WISWEEGMKV FEELLLDADW SINAGSWMWL SCSSFFQQFF HCYCPVGFGR 

       430        440        450        460        470        480 
RTDPNGDYIR RYLPVLRGFP AKYIYDPWNA PEGIQKVAKC LIGVNYPKPM VNHAEASRLN 

       490        500        510        520        530        540 
IERMKQIYQQ LSRYRGLGLL ASVPSNPNGN GGFMGYSAEN IPGCSSSGSC SQGSGILHYA 

       550        560        570        580 
HGDSQQTHLL KQGRSSMGTG LSGGKRPSQE EDTQSIGPKV QRQSTN 

Q16526 in FASTA format

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