CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012676
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cryptochrome-1 
Protein Synonyms/Alias
  
Gene Name
 CRY1 
Gene Synonyms/Alias
 PHLL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
89DVFPRLFKEWNITKLubiquitination[1]
107YDSEPFGKERDAAIKubiquitination[1]
151GQPPLTYKRFQTLISacetylation[2]
159RFQTLISKMEPLEIPubiquitination[3]
228LERHLERKAWVANFEubiquitination[1, 4]
329KNPEALAKWAEGRTGubiquitination[5]
442VLRGFPAKYIYDPWNubiquitination[1, 3, 5, 6]
456NAPEGIQKVAKCLIGubiquitination[1]
459EGIQKVAKCLIGVNYubiquitination[1]
485RLNIERMKQIYQQLSubiquitination[1]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
 [5] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094] 
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 3 132 Photolyase/cryptochrome alpha/beta.
 REGION 211 488 FAD-binding.
 REGION 371 470 Required for inhibition of CLOCK-ARNTL-
 MOD_RES 71 71 Phosphoserine; by AMPK (By similarity).
 MOD_RES 247 247 Phosphoserine; by MAPK (By similarity).
 MOD_RES 280 280 Phosphoserine; by AMPK (By similarity).
 CROSSLNK 11 11 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 107 107 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 159 159 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 329 329 Glycyl lysine isopeptide (Lys-Gly)
 CROSSLNK 485 485 Glycyl lysine isopeptide (Lys-Gly)  
Keyword
 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
 586 AA 
Protein Sequence
MGVNAVHWFR KGLRLHDNPA LKECIQGADT IRCVYILDPW FAGSSNVGIN RWRFLLQCLE 60
DLDANLRKLN SRLFVIRGQP ADVFPRLFKE WNITKLSIEY DSEPFGKERD AAIKKLATEA 120
GVEVIVRISH TLYDLDKIIE LNGGQPPLTY KRFQTLISKM EPLEIPVETI TSEVIEKCTT 180
PLSDDHDEKY GVPSLEELGF DTDGLSSAVW PGGETEALTR LERHLERKAW VANFERPRMN 240
ANSLLASPTG LSPYLRFGCL SCRLFYFKLT DLYKKVKKNS SPPLSLYGQL LWREFFYTAA 300
TNNPRFDKME GNPICVQIPW DKNPEALAKW AEGRTGFPWI DAIMTQLRQE GWIHHLARHA 360
VACFLTRGDL WISWEEGMKV FEELLLDADW SINAGSWMWL SCSSFFQQFF HCYCPVGFGR 420
RTDPNGDYIR RYLPVLRGFP AKYIYDPWNA PEGIQKVAKC LIGVNYPKPM VNHAEASRLN 480
IERMKQIYQQ LSRYRGLGLL ASVPSNPNGN GGFMGYSAEN IPGCSSSGSC SQGSGILHYA 540
HGDSQQTHLL KQGRSSMGTG LSGGKRPSQE EDTQSIGPKV QRQSTN 586 
Gene Ontology
 GO:0005739; C:mitochondrion; IEA:Compara.
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 GO:0009882; F:blue light photoreceptor activity; NAS:UniProtKB.
 GO:0003913; F:DNA photolyase activity; IEA:InterPro.
 GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
 GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
 GO:0000988; F:protein binding transcription factor activity; IDA:BHF-UCL.
 GO:0007623; P:circadian rhythm; IEA:Compara.
 GO:0006281; P:DNA repair; IEA:InterPro.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
 GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
 GO:0042752; P:regulation of circadian rhythm; ISS:UniProtKB.
 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