CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022762
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cryptochrome-2 
Protein Synonyms/Alias
  
Gene Name
 Cry2 
Gene Synonyms/Alias
 Kiaa0658 
Created Date
 July 27, 2013 
Organism
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
474NAPESVQKAAKCIIGubiquitination[1]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023] 
Functional Description
 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. 
Sequence Annotation
 DOMAIN 21 150 Photolyase/cryptochrome alpha/beta.
 REGION 229 506 FAD-binding.
 REGION 389 488 Required for inhibition of CLOCK-ARNTL-
 MOD_RES 265 265 Phosphoserine; by MAPK.
 MOD_RES 553 553 Phosphoserine; by GSK3-beta.
 MOD_RES 557 557 Phosphoserine; by DYRK1A and MAPK.
 CROSSLNK 125 125 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 241 241 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 347 347 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 474 474 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 503 503 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 3D-structure; Biological rhythms; Chromophore; Complete proteome; Cytoplasm; FAD; Flavoprotein; Isopeptide bond; Nucleotide-binding; Nucleus; Phosphoprotein; Photoreceptor protein; Receptor; Reference proteome; Repressor; Sensory transduction; Transcription; Transcription regulation; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 592 AA 
Protein Sequence
MAAAAVVAAT VPAQSMGADG ASSVHWFRKG LRLHDNPALL AAVRGARCVR CVYILDPWFA 60
ASSSVGINRW RFLLQSLEDL DTSLRKLNSR LFVVRGQPAD VFPRLFKEWG VTRLTFEYDS 120
EPFGKERDAA IMKMAKEAGV EVVTENSHTL YDLDRIIELN GQKPPLTYKR FQALISRMEL 180
PKKPAVAVSS QQMESCRAEI QENHDDTYGV PSLEELGFPT EGLGPAVWQG GETEALARLD 240
KHLERKAWVA NYERPRMNAN SLLASPTGLS PYLRFGCLSC RLFYYRLWDL YKKVKRNSTP 300
PLSLFGQLLW REFFYTAATN NPRFDRMEGN PICIQIPWDR NPEALAKWAE GKTGFPWIDA 360
IMTQLRQEGW IHHLARHAVA CFLTRGDLWV SWESGVRVFD ELLLDADFSV NAGSWMWLSC 420
SAFFQQFFHC YCPVGFGRRT DPSGDYIRRY LPKLKGFPSR YIYEPWNAPE SVQKAAKCII 480
GVDYPRPIVN HAETSRLNIE RMKQIYQQLS RYRGLCLLAS VPSCVEDLSH PVAEPGSSQA 540
GSISNTGPRA LSSGPASPKR KLEAAEEPPG EELTKRARVT EMPTQEPASK DS 592 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005576; C:extracellular region; IEA:Compara.
 GO:0005739; C:mitochondrion; IDA:UniProtKB.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003684; F:damaged DNA binding; IEA:Compara.
 GO:0003913; F:DNA photolyase activity; IEA:InterPro.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0009881; F:photoreceptor activity; IEA:UniProtKB-KW.
 GO:0000988; F:protein binding transcription factor activity; IEA:Compara.
 GO:0003697; F:single-stranded DNA binding; IEA:Compara.
 GO:0007623; P:circadian rhythm; IMP:UniProtKB.
 GO:0006281; P:DNA repair; IEA:InterPro.
 GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IEA:Compara.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Compara.
 GO:0006606; P:protein import into nucleus; IPI:MGI.
 GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
 GO:0042752; P:regulation of circadian rhythm; IMP:UniProtKB.
 GO:2000118; P:regulation of sodium-dependent phosphate transport; IEA:Compara.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR006050; DNA_photolyase_N.
 IPR005101; Photolyase_FAD-bd/Cryptochr_C.
 IPR014729; Rossmann-like_a/b/a_fold. 
Pfam
 PF00875; DNA_photolyase
 PF03441; FAD_binding_7 
SMART
  
PROSITE
 PS00394; DNA_PHOTOLYASES_1_1
 PS51645; PHR_CRY_ALPHA_BETA 
PRINTS