CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-006936
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Coilin 
Protein Synonyms/Alias
 p80 
Gene Name
 COIL 
Gene Synonyms/Alias
 CLN80 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
293TKNTTADKLAIKLGFacetylation[1]
405EENLFSWKGAKGRGMacetylation[2]
476AAPQVGEKIAFKLLEubiquitination[3]
496SPDVSDYKEGRILSHubiquitination[3, 4, 5]
555SKITVFWKELIDPRLubiquitination[6, 7]
Reference
 [1] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] 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]
 [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
Functional Description
 Is a component of the nuclear coiled bodies (CBS) which are involved in the function or assembly/disassembly of nucleoplasmic snRNPs. During mitosis, CBS disassemble, coinciding with a mitotic-specific phosphorylation of p80 coilin. 
Sequence Annotation
 REPEAT 223 226 1-1.
 REPEAT 268 271 1-2.
 REPEAT 386 389 2-1.
 REPEAT 413 414 3-1.
 REPEAT 415 416 3-2.
 REPEAT 417 418 3-3.
 REPEAT 419 420 3-4.
 DOMAIN 460 559 Tudor; atypical.
 REPEAT 517 520 2-2.
 REGION 223 271 2 X 4 AA repeats of A-R-N-S.
 REGION 386 520 2 X 4 AA repeats of S-L-P-A.
 REGION 413 420 4 X 2 AA tandem repeats of R-G.
 MOD_RES 105 105 Phosphoserine.
 MOD_RES 122 122 Phosphothreonine.
 MOD_RES 184 184 Phosphoserine; by VRK1 and VRK2.
 MOD_RES 271 271 Phosphoserine.
 MOD_RES 272 272 Phosphoserine.
 MOD_RES 290 290 Phosphothreonine.
 MOD_RES 301 301 Phosphoserine.
 MOD_RES 303 303 Phosphothreonine.
 MOD_RES 456 456 Phosphothreonine.
 MOD_RES 489 489 Phosphoserine.
 MOD_RES 566 566 Phosphoserine.  
Keyword
 Complete proteome; Methylation; Nucleus; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 576 AA 
Protein Sequence
MAASETVRLR LQFDYPPPAT PHCTAFWLLV DLNRCRVVTD LISLIRQRFG FSSGAFLGLY 60
LEGGLLPPAE SARLVRDNDC LRVKLEERGV AENSVVISNG DINLSLRKAK KRAFQLEEGE 120
ETEPDCKYSK KHWKSRENNN NNEKVLDLEP KAVTDQTVSK KNKRKNKATC GTVGDDNEEA 180
KRKSPKKKEK CEYKKKAKNP KSPKVQAVKD WANQRCSSPK GSARNSLVKA KRKGSVSVCS 240
KESPSSSSES ESCDESISDG PSKVTLEARN SSEKLPTELS KEEPSTKNTT ADKLAIKLGF 300
SLTPSKGKTS GTTSSSSDSS AESDDQCLMS SSTPECAAGF LKTVGLFAGR GRPGPGLSSQ 360
TAGAAGWRRS GSNGGGQAPG ASPSVSLPAS LGRGWGREEN LFSWKGAKGR GMRGRGRGRG 420
HPVSCVVNRS TDNQRQQQLN DVVKNSSTII QNPVETPKKD YSLLPLLAAA PQVGEKIAFK 480
LLELTSSYSP DVSDYKEGRI LSHNPETQQV DIEILSSLPA LREPGKFDLV YHNENGAEVV 540
EYAVTQESKI TVFWKELIDP RLIIESPSNT SSTEPA 576 
Gene Ontology
 GO:0015030; C:Cajal body; IDA:UniProtKB.
 GO:0001674; C:female germ cell nucleus; IEA:Compara.
 GO:0005730; C:nucleolus; IDA:UniProtKB.
 GO:0015036; F:disulfide oxidoreductase activity; IEA:Compara. 
Interpro
 IPR024822; Coilin. 
Pfam
  
SMART
  
PROSITE
 PS50304; TUDOR 
PRINTS