CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-023203
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Fizzy-related protein homolog 
Protein Synonyms/Alias
 Fzr; CDC20-like protein 1; Cdh1/Hct1 homolog; hCDH1 
Gene Name
 FZR1 
Gene Synonyms/Alias
 CDH1; FYR; FZR; KIAA1242 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
96LAYSALLKNELLGAGubiquitination[1]
156SLSPVSNKSQKLLRSubiquitination[1]
173KPTRKISKIPFKVLDubiquitination[1]
262IWDAAAGKKLSMLEGubiquitination[1, 2, 3]
263WDAAAGKKLSMLEGHubiquitination[1]
320RQEVCGLKWSTDHQLubiquitination[4]
336ASGGNDNKLLVWNHSubiquitination[5]
429QNQILVWKYPSLTQVubiquitination[5]
475RFWNVFSKTRSTKVKubiquitination[5]
480FSKTRSTKVKWESVSubiquitination[1]
Reference
 [1] 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]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] 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]
 [5] 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] 
Functional Description
 Key regulator of ligase activity of the anaphase promoting complex/cyclosome (APC/C), which confers substrate specificity upon the complex. Associates with the APC/C in late mitosis, in replacement of CDC20, and activates the APC/C during anaphase and telophase. The APC/C remains active in degrading substrates to ensure that positive regulators of the cell cycle do not accumulate prematurely. At the G1/S transition FZR1 is phosphorylated, leading to its dissociation from the APC/C. Following DNA damage, it is required for the G2 DNA damage checkpoint: its dephosphorylation and reassociation with the APC/C leads to the ubiquitination of PLK1, preventing entry into mitosis. 
Sequence Annotation
 REPEAT 182 222 WD 1.
 REPEAT 227 266 WD 2.
 REPEAT 269 306 WD 3.
 REPEAT 311 350 WD 4.
 REPEAT 353 395 WD 5.
 REPEAT 397 438 WD 6.
 REPEAT 441 480 WD 7.
 MOD_RES 32 32 Phosphothreonine.
 MOD_RES 36 36 Phosphoserine.
 MOD_RES 138 138 Phosphoserine.
 MOD_RES 146 146 Phosphoserine.
 MOD_RES 151 151 Phosphoserine.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Complete proteome; Cytoplasm; DNA damage; DNA repair; Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation pathway; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 496 AA 
Protein Sequence
MDQDYERRLL RQIVIQNENT MPRVTEMRRT LTPASSPVSS PSKHGDRFIP SRAGANWSVN 60
FHRINENEKS PSQNRKAKDA TSDNGKDGLA YSALLKNELL GAGIEKVQDP QTEDRRLQPS 120
TPEKKGLFTY SLSTKRSSPD DGNDVSPYSL SPVSNKSQKL LRSPRKPTRK ISKIPFKVLD 180
APELQDDFYL NLVDWSSLNV LSVGLGTCVY LWSACTSQVT RLCDLSVEGD SVTSVGWSER 240
GNLVAVGTHK GFVQIWDAAA GKKLSMLEGH TARVGALAWN AEQLSSGSRD RMILQRDIRT 300
PPLQSERRLQ GHRQEVCGLK WSTDHQLLAS GGNDNKLLVW NHSSLSPVQQ YTEHLAAVKA 360
IAWSPHQHGL LASGGGTADR CIRFWNTLTG QPLQCIDTGS QVCNLAWSKH ANELVSTHGY 420
SQNQILVWKY PSLTQVAKLT GHSYRVLYLA MSPDGEAIVT GAGDETLRFW NVFSKTRSTK 480
VKWESVSVLN LFTRIR 496 
Gene Ontology
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0031965; C:nuclear membrane; IDA:HPA.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0051488; P:activation of anaphase-promoting complex activity; IDA:UniProtKB.
 GO:0031145; P:anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
 GO:0031572; P:G2 DNA damage checkpoint; IDA:UniProtKB.
 GO:0070306; P:lens fiber cell differentiation; IEA:Compara.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0090344; P:negative regulation of cell aging; IEA:Compara.
 GO:0051436; P:negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0045732; P:positive regulation of protein catabolic process; IGI:UniProtKB.
 GO:0051437; P:positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle; TAS:Reactome.
 GO:0070979; P:protein K11-linked ubiquitination; TAS:UniProtKB.
 GO:0040020; P:regulation of meiosis; IEA:Compara. 
Interpro
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS