CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005954
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Coronin-1A 
Protein Synonyms/Alias
 Coronin-like protein A; Clipin-A; Coronin-like protein p57; Tryptophan aspartate-containing coat protein; TACO 
Gene Name
 CORO1A 
Gene Synonyms/Alias
 CORO1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
20HVFGQPAKADQCYEDubiquitination[1, 2, 3]
66FLVLPLGKTGRVDKNubiquitination[3]
233AVFVSEGKILTTGFSubiquitination[1, 2, 3, 4]
313YLSMFSSKESQRGMGubiquitination[1]
324RGMGYMPKRGLEVNKubiquitination[2, 3]
331KRGLEVNKCEIARFYubiquitination[2, 3]
339CEIARFYKLHERRCEacetylation[5]
339CEIARFYKLHERRCEubiquitination[3]
355IAMTVPRKSDLFQEDubiquitination[2, 3, 6]
393GPLLISLKDGYVPPKubiquitination[2, 3, 6]
400KDGYVPPKSRELRVNubiquitination[3, 6]
439RLEEEMRKLQATVQEubiquitination[3]
449ATVQELQKRLDRLEEacetylation[5]
449ATVQELQKRLDRLEEubiquitination[3]
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] 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]
 [3] 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]
 [4] 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]
 [5] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [6] 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] 
Functional Description
 May be a crucial component of the cytoskeleton of highly motile cells, functioning both in the invagination of large pieces of plasma membrane, as well as in forming protrusions of the plasma membrane involved in cell locomotion. In mycobacteria- infected cells, its retention on the phagosomal membrane prevents fusion between phagosomes and lysosomes. 
Sequence Annotation
 REPEAT 13 63 WD 1.
 REPEAT 73 110 WD 2.
 REPEAT 123 160 WD 3.
 REPEAT 164 204 WD 4.
 REPEAT 207 251 WD 5.
 REPEAT 258 296 WD 6.
 REPEAT 302 349 WD 7.
 MOD_RES 2 2 N-acetylserine.
 MOD_RES 2 2 Phosphoserine; by PKC.
 MOD_RES 412 412 Phosphothreonine; by PKC.
 MOD_RES 449 449 N6-acetyllysine.  
Keyword
 Acetylation; Actin-binding; Coiled coil; Complete proteome; Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; WD repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 461 AA 
Protein Sequence
MSRQVVRSSK FRHVFGQPAK ADQCYEDVRV SQTTWDSGFC AVNPKFVALI CEASGGGAFL 60
VLPLGKTGRV DKNAPTVCGH TAPVLDIAWC PHNDNVIASG SEDCTVMVWE IPDGGLMLPL 120
REPVVTLEGH TKRVGIVAWH TTAQNVLLSA GCDNVIMVWD VGTGAAMLTL GPEVHPDTIY 180
SVDWSRDGGL ICTSCRDKRV RIIEPRKGTV VAEKDRPHEG TRPVRAVFVS EGKILTTGFS 240
RMSERQVALW DTKHLEEPLS LQELDTSSGV LLPFFDPDTN IVYLCGKGDS SIRYFEITSE 300
APFLHYLSMF SSKESQRGMG YMPKRGLEVN KCEIARFYKL HERRCEPIAM TVPRKSDLFQ 360
EDLYPPTAGP DPALTAEEWL GGRDAGPLLI SLKDGYVPPK SRELRVNRGL DTGRRRAAPE 420
ASGTPSSDAV SRLEEEMRKL QATVQELQKR LDRLEETVQA K 461 
Gene Ontology
 GO:0005884; C:actin filament; IDA:UniProtKB.
 GO:0030864; C:cortical actin cytoskeleton; IDA:UniProtKB.
 GO:0001772; C:immunological synapse; IEA:Compara.
 GO:0030027; C:lamellipodium; IDA:UniProtKB.
 GO:0001891; C:phagocytic cup; IDA:UniProtKB.
 GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
 GO:0030670; C:phagocytic vesicle membrane; IEA:UniProtKB-SubCell.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0043548; F:phosphatidylinositol 3-kinase binding; IDA:UniProtKB.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0030036; P:actin cytoskeleton organization; IMP:UniProtKB.
 GO:0007015; P:actin filament organization; IEA:Compara.
 GO:0006816; P:calcium ion transport; IEA:Compara.
 GO:0031589; P:cell-substrate adhesion; IMP:UniProtKB.
 GO:0048873; P:homeostasis of number of cells within a tissue; IEA:Compara.
 GO:0045087; P:innate immune response; NAS:UniProtKB.
 GO:0030595; P:leukocyte chemotaxis; IBA:RefGenome.
 GO:0051126; P:negative regulation of actin nucleation; IDA:UniProtKB.
 GO:0001845; P:phagolysosome assembly; IMP:UniProtKB.
 GO:0050918; P:positive chemotaxis; IDA:UniProtKB.
 GO:0030335; P:positive regulation of cell migration; IEA:Compara.
 GO:0042102; P:positive regulation of T cell proliferation; IEA:Compara.
 GO:0030833; P:regulation of actin filament polymerization; IEA:Compara.
 GO:0008360; P:regulation of cell shape; IBA:RefGenome.
 GO:0034097; P:response to cytokine stimulus; IEA:Compara.
 GO:0043029; P:T cell homeostasis; IEA:Compara.
 GO:0032796; P:uropod organization; IBA:RefGenome. 
Interpro
 IPR027334; CORO1A.
 IPR015505; Coronin.
 IPR015048; DUF1899.
 IPR015049; DUF1900.
 IPR015943; WD40/YVTN_repeat-like_dom.
 IPR001680; WD40_repeat.
 IPR019775; WD40_repeat_CS.
 IPR017986; WD40_repeat_dom. 
Pfam
 PF08953; DUF1899
 PF08954; DUF1900
 PF00400; WD40 
SMART
 SM00320; WD40 
PROSITE
 PS00678; WD_REPEATS_1
 PS50082; WD_REPEATS_2
 PS50294; WD_REPEATS_REGION 
PRINTS