CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022530
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Protein RCC2 
Protein Synonyms/Alias
 RCC1-like protein TD-60; Telophase disk protein of 60 kDa 
Gene Name
 RCC2 
Gene Synonyms/Alias
 KIAA1470; TD60 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
5***MPRKKAAAAAWEubiquitination[1, 2]
77ARPATAGKAGGAAVVubiquitination[2]
92ITEPEHTKERVKLEGacetylation[2, 3, 4]
92ITEPEHTKERVKLEGubiquitination[1, 2, 5]
96EHTKERVKLEGSKCKacetylation[2]
120NWDLIGRKEVPKQQAubiquitination[1]
124IGRKEVPKQQAAYRNubiquitination[1, 2, 6]
293LGHNSDGKFIARAQRacetylation[2, 3, 4, 7]
293LGHNSDGKFIARAQRmethylation[8]
293LGHNSDGKFIARAQRubiquitination[1, 2, 9]
318RVAIFIEKTKDGQILubiquitination[1]
320AIFIEKTKDGQILPVacetylation[2]
320AIFIEKTKDGQILPVubiquitination[1, 2, 5, 9, 10, 11]
349TLVLDSQKRVFSWGFubiquitination[1, 2, 9, 12]
368RLGHAEQKDEMVPRLacetylation[2]
368RLGHAEQKDEMVPRLubiquitination[1, 2, 5]
377EMVPRLVKLFDFPGRacetylation[2, 3]
377EMVPRLVKLFDFPGRubiquitination[1, 2, 5, 6, 9, 10, 11, 13, 14]
422RESTMYPKAVQDLCGacetylation[2]
422RESTMYPKAVQDLCGubiquitination[1, 2]
510ESETEKEKIKKLPEYubiquitination[2]
513TEKEKIKKLPEYNPRacetylation[2]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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]
 [6] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [7] 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]
 [8] A general molecular affinity strategy for global detection and proteomic analysis of lysine methylation.
 Moore KE, Carlson SM, Camp ND, Cheung P, James RG, Chua KF, Wolf-Yadlin A, Gozani O.
 Mol Cell. 2013 May 9;50(3):444-56. [PMID: 23583077]
 [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]
 [10] 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]
 [11] 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]
 [12] 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]
 [13] Global analysis of lysine ubiquitination by ubiquitin remnant immunoaffinity profiling.
 Xu G, Paige JS, Jaffrey SR.
 Nat Biotechnol. 2010 Aug;28(8):868-73. [PMID: 20639865]
 [14] 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
Functional Description
 Required for completion of mitosis and cytokinesis. May function as a guanine nucleotide exchange factor for the small GTPase RAC1. 
Sequence Annotation
 REPEAT 103 165 RCC1 1.
 REPEAT 168 219 RCC1 2.
 REPEAT 221 271 RCC1 3.
 REPEAT 273 347 RCC1 4.
 REPEAT 348 401 RCC1 5.
 REPEAT 403 447 RCC1 6.
 REPEAT 448 501 RCC1 7.
 MOD_RES 16 16 Phosphoserine.
 MOD_RES 43 43 Phosphoserine.
 MOD_RES 44 44 Phosphoserine.
 MOD_RES 45 45 Phosphoserine.
 MOD_RES 46 46 Phosphoserine.
 MOD_RES 50 50 Phosphoserine.
 MOD_RES 51 51 Phosphoserine.
 MOD_RES 92 92 N6-acetyllysine.
 MOD_RES 293 293 N6-acetyllysine.
 MOD_RES 342 342 Phosphothreonine.
 MOD_RES 347 347 Phosphoserine.
 MOD_RES 377 377 N6-acetyllysine.  
Keyword
 Acetylation; Cell cycle; Cell division; Centromere; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 522 AA 
Protein Sequence
MPRKKAAAAA WEEPSSGNGT ARAGPRKRGG PAGRKRERPE RCSSSSGGGS SGDEDGLELD 60
GAPGGGKRAA RPATAGKAGG AAVVITEPEH TKERVKLEGS KCKGQLLIFG ATNWDLIGRK 120
EVPKQQAAYR NLGQNLWGPH RYGCLAGVRV RTVVSGSCAA HSLLITTEGK LWSWGRNEKG 180
QLGHGDTKRV EAPRLIEGLS HEVIVSAACG RNHTLALTET GSVFAFGENK MGQLGLGNQT 240
DAVPSPAQIM YNGQPITKMA CGAEFSMIMD CKGNLYSFGC PEYGQLGHNS DGKFIARAQR 300
IEYDCELVPR RVAIFIEKTK DGQILPVPNV VVRDVACGAN HTLVLDSQKR VFSWGFGGYG 360
RLGHAEQKDE MVPRLVKLFD FPGRGASQIY AGYTCSFAVS EVGGLFFWGA TNTSRESTMY 420
PKAVQDLCGW RIRSLACGKS SIIVAADEST ISWGPSPTFG ELGYGDHKPK SSTAAQEVKT 480
LDGIFSEQVA MGYSHSLVIA RDESETEKEK IKKLPEYNPR TL 522 
Gene Ontology
 GO:0000775; C:chromosome, centromeric region; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
 GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome. 
Interpro
 IPR009091; RCC1/BLIP-II.
 IPR000408; Reg_chr_condens. 
Pfam
 PF00415; RCC1 
SMART
  
PROSITE
 PS00625; RCC1_1
 PS00626; RCC1_2
 PS50012; RCC1_3 
PRINTS
 PR00633; RCCNDNSATION.