CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-031437
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Coatomer protein complex, subunit beta 2 (Beta prime), isoform CRA_b 
Protein Synonyms/Alias
 Coatomer subunit beta'; cDNA FLJ56271, highly similar to Coatomer subunit beta 
Gene Name
 COPB2 
Gene Synonyms/Alias
 hCG_17220 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
40AAKFVARKNWVVTGAubiquitination[1]
139ASLDRTIKVWQLGSSubiquitination[1, 2, 3]
170DYYSGGDKPYLISGAubiquitination[1]
183GADDRLVKIWDYQNKubiquitination[3]
289NGKIIWAKHSEVQQAacetylation[4]
289NGKIIWAKHSEVQQAubiquitination[1, 2, 3]
299EVQQANLKAMGDAEIubiquitination[2]
317ERLPLAVKDMGSCEIubiquitination[2, 3, 5]
357TAMALRNKSFGSAQEacetylation[6]
357TAMALRNKSFGSAQEubiquitination[2]
579RDFSMADKVLPTIPKubiquitination[1, 2, 3, 7]
598RVAHFLEKQGFKQQAacetylation[3]
598RVAHFLEKQGFKQQAubiquitination[1]
695EGAERDGKNNVAFMSubiquitination[1, 7]
742SQVSRVVKLWRENLSubiquitination[1]
754NLSKVNQKAAESLADubiquitination[1, 3, 7, 8]
793HADLWPAKQYPLVTPubiquitination[1, 3, 7, 9]
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] 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] 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]
 [4] Monoclonal antibody cocktail as an enrichment tool for acetylome analysis.
 Shaw PG, Chaerkady R, Zhang Z, Davidson NE, Pandey A.
 Anal Chem. 2011 May 15;83(10):3623-6. [PMID: 21466224]
 [5] 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]
 [6] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [7] 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]
 [8] 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]
 [9] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724] 
Functional Description
  
Sequence Annotation
  
Keyword
 Complete proteome; Reference proteome; Repeat; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 877 AA 
Protein Sequence
MLASLYNGSV CVWNHETQTL VKTFEVCDLP VRAAKFVARK NWVVTGADDM QIRVFNYNTL 60
ERVHMFEAHS DYIRCIAVHP TQPFILTSSD DMLIKLWDWD KKWSCSQVFE GHTHYVMQIV 120
INPKDNNQFA SASLDRTIKV WQLGSSSPNF TLEGHEKGVN CIDYYSGGDK PYLISGADDR 180
LVKIWDYQNK TCVQTLEGHA QNVSCASFHP ELPIIITGSE DGTVRIWHSS TYRLESTLNY 240
GMERVWCVAS LRGSNNVALG YDEGSIIVKL GREEPAMSMD ANGKIIWAKH SEVQQANLKA 300
MGDAEIKDGE RLPLAVKDMG SCEIYPQTIQ HNPNGRFVVV CGDGEYIIYT AMALRNKSFG 360
SAQEFAWAHD SSEYAIRESN SIVKIFKNFK EKKSFKPDFG AESIYGGFLL GVRSVNGLAF 420
YDWDNTELIR RIEIQPKHIF WSDSGELVCI ATEESFFILK YLSEKVLAAQ ETHEGVTEDG 480
IEDAFEVLGE IQEIVKTGLW VGDCFIYTSS VNRLNYYVGG EIVTIAHLDR TMYLLGYIPK 540
DNRLYLGDKE LNIISYSLLV SVLEYQTAVM RRDFSMADKV LPTIPKEQRT RVAHFLEKQG 600
FKQQALTVST DPEHRFELAL QLGELKIAYQ LAVEAESEQK WKQLAELAIS KCQFGLAQEC 660
LHHAQDYGGL LLLATASGNA NMVNKLAEGA ERDGKNNVAF MSYFLQGKVD ACLELLIRTG 720
RLPEAAFLAR TYLPSQVSRV VKLWRENLSK VNQKAAESLA DPTEYENLFP GLKEAFVVEE 780
WVKETHADLW PAKQYPLVTP NEERNVMEEG KDFQPSRSTA QQELDGKPAS PTPVIVASHT 840
ANKEEKSLLE LEVDLDNLEL EDIDTTDINL DEDILDD 877 
Gene Ontology
 GO:0015629; C:actin cytoskeleton; IDA:HPA.
 GO:0005794; C:Golgi apparatus; IDA:HPA.
 GO:0030117; C:membrane coat; IEA:InterPro.
 GO:0005198; F:structural molecule activity; IEA:InterPro.
 GO:0006886; P:intracellular protein transport; IEA:InterPro.
 GO:0016192; P:vesicle-mediated transport; IEA:InterPro. 
Interpro
 IPR006692; Coatomer_WD-assoc_reg.
 IPR016453; COPB2.
 IPR020472; G-protein_beta_WD-40_rep.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF04053; Coatomer_WDAD
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS
 PR00320; GPROTEINBRPT.