CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015997
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein zer-1 homolog 
Protein Synonyms/Alias
 Hzyg; Zyg-11 homolog B-like protein 
Gene Name
 ZER1 
Gene Synonyms/Alias
 C9orf60; ZYG; ZYG11BL 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
31TLGYLLDKETLRLHPubiquitination[1, 2, 3, 4, 5, 6, 7, 8]
102QDLEAIRKQDLVELYubiquitination[5]
119NCEKLSAKSLQTLRSubiquitination[2, 5, 9]
263DRLSSYYKFKLTREVubiquitination[2]
313QTSIEPSKSSIIPFRubiquitination[2, 5, 6, 8]
323IIPFRALKRPLQFLGubiquitination[5]
351AYKVSGDKNEEQVLNubiquitination[5]
584CLKEFPEKQELHRNMubiquitination[8]
Reference
 [1] 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]
 [2] 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]
 [3] 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]
 [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
 [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]
 [6] 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]
 [7] 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]
 [8] 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]
 [9] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572
Functional Description
 Probably acts as target recruitment subunit in the E3 ubiquitin ligase complex ZER1-CUL2-Elongin BC. 
Sequence Annotation
 REPEAT 226 245 LRR 1.
 REPEAT 246 268 LRR 2.
 REPEAT 278 302 LRR 3.
 REPEAT 427 467 ARM 1.
 REPEAT 511 556 ARM 2.
 REPEAT 558 600 ARM 3.
 REPEAT 602 643 ARM 4.
 REPEAT 714 756 ARM 5.  
Keyword
 Complete proteome; Leucine-rich repeat; Polymorphism; Reference proteome; Repeat; Ubl conjugation pathway. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 766 AA 
Protein Sequence
MASDTPESLM ALCTDFCLRN LDGTLGYLLD KETLRLHPDI FLPSEICDRL VNEYVELVNA 60
ACNFEPHESF FSLFSDPRST RLTRIHLRED LVQDQDLEAI RKQDLVELYL TNCEKLSAKS 120
LQTLRSFSHT LVSLSLFGCT NIFYEEENPG GCEDEYLVNP TCQVLVKDFT FEGFSRLRFL 180
NLGRMIDWVP VESLLRPLNS LAALDLSGIQ TSDAAFLTQW KDSLVSLVLY NMDLSDDHIR 240
VIVQLHKLRH LDISRDRLSS YYKFKLTREV LSLFVQKLGN LMSLDISGHM ILENCSISKM 300
EEEAGQTSIE PSKSSIIPFR ALKRPLQFLG LFENSLCRLT HIPAYKVSGD KNEEQVLNAI 360
EAYTEHRPEI TSRAINLLFD IARIERCNQL LRALKLVITA LKCHKYDRNI QVTGSAALFY 420
LTNSEYRSEQ SVKLRRQVIQ VVLNGMESYQ EVTVQRNCCL TLCNFSIPEE LEFQYRRVNE 480
LLLSILNPTR QDESIQRIAV HLCNALVCQV DNDHKEAVGK MGFVVTMLKL IQKKLLDKTC 540
DQVMEFSWSA LWNITDETPD NCEMFLNFNG MKLFLDCLKE FPEKQELHRN MLGLLGNVAE 600
VKELRPQLMT SQFISVFSNL LESKADGIEV SYNACGVLSH IMFDGPEAWG VCEPQREEVE 660
ERMWAAIQSW DINSRRNINY RSFEPILRLL PQGISPVSQH WATWALYNLV SVYPDKYCPL 720
LIKEGGMPLL RDIIKMATAR QETKEMARKV IEHCSNFKEE NMDTSR 766 
Gene Ontology
 GO:0031462; C:Cul2-RING ubiquitin ligase complex; IDA:UniProtKB.
 GO:0004842; F:ubiquitin-protein ligase activity; IMP:UniProtKB.
 GO:0051438; P:regulation of ubiquitin-protein ligase activity; IMP:UniProtKB. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR004908; ATPase_V1-cplx_hsu. 
Pfam
 PF03224; V-ATPase_H_N 
SMART
  
PROSITE
 PS50176; ARM_REPEAT 
PRINTS