CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-036859
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
  
Protein Name
 Condensin complex subunit 1 
Protein Synonyms/Alias
  
Gene Name
 NCAPD2 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
35VQEVLSIKHLPPQLRubiquitination[1, 2, 3, 4, 5]
87NPTINHQKNRPTREAubiquitination[2, 3]
157IVREIGQKCPQELSRubiquitination[2, 3, 5]
170SRDPSGTKGFAAFLTubiquitination[1, 2, 3, 4, 6]
267FTRIVQQKALPLTRFubiquitination[1, 2, 3]
288AVGRLADKSVLVCKNubiquitination[3, 5]
324DLAGPLQKETQKLQEubiquitination[1, 2, 3, 5]
328PLQKETQKLQEMRAQubiquitination[3]
389TETTEDVKGRIYQLLubiquitination[1, 2, 4]
398RIYQLLAKASYKKAIubiquitination[2]
443NILGLIFKGPAASTQubiquitination[4]
452PAASTQEKNPRESTGubiquitination[1]
469VTGQTVCKNKPNMSDubiquitination[2]
471GQTVCKNKPNMSDPEubiquitination[2]
488RGNDELVKQEMLVQYubiquitination[1, 2, 6]
505DAYSFSRKITEAIGIubiquitination[3]
557MLPLIWSKEPGVREAubiquitination[2, 3, 5, 7]
577RQLYLNPKGDSARAKubiquitination[1, 2, 3, 4]
621FVQKDELKPAVTQLLubiquitination[1, 3, 7]
635LWERATEKVACCPLEubiquitination[2, 3, 5, 8]
657LGMMARGKPEIVGSNubiquitination[1, 2, 4]
676VSIGLDEKFPQDYRLubiquitination[1, 2, 4]
704RRKPSLGKRHPPFRLubiquitination[2]
727RLRETVTKGFVHPDPubiquitination[1, 2, 3, 7]
772CAKQALEKLEEKRTSubiquitination[3]
834LREEQEHKTKDPKEKubiquitination[1]
841KTKDPKEKNTSSETTubiquitination[1, 2]
880EMELLDGKQTLAAFVubiquitination[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] 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]
 [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] 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]
 [5] 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]
 [6] 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]
 [7] 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]
 [8] 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. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 919 AA 
Protein Sequence
MAPQMYEFHL PLSPEELLKS GGVNQYVVQE VLSIKHLPPQ LRAFQAAFRA QGPLAMLQHF 60
DTIYSILHLV TGCCYRLLEN PTINHQKNRP TREAITHLLG VALTRYNHML SATVKIIQML 120
QHFEHLAPVL VAAVSLWATD YGMKSIVGEI VREIGQKCPQ ELSRDPSGTK GFAAFLTELA 180
ERVPAILMSS MCILLDHLDG ENYMMRNAVL AAMAEMVLQV LSGDQLEAAA RDTRDQFLDT 240
LQAHGHDVNS FVRSRVLQLF TRIVQQKALP LTRFQAVVAL AVGRLADKSV LVCKNAIQLL 300
ASFLANNPFS CKLSDADLAG PLQKETQKLQ EMRAQRRTAA ASAVLDPEEE WEAMLPELKS 360
TLQQLLQLPQ GEEEIPEQIA NTETTEDVKG RIYQLLAKAS YKKAIILTRE ATGHFQESEP 420
FSHIDPEESE ETRLLNILGL IFKGPAASTQ EKNPRESTGN MVTGQTVCKN KPNMSDPEES 480
RGNDELVKQE MLVQYLQDAY SFSRKITEAI GIISKMMYEN TTTVVQEVIE FFVMVFQFGV 540
PQALFGVRRM LPLIWSKEPG VREAVLNAYR QLYLNPKGDS ARAKAQALIQ NLSLLLVDAS 600
VGTIQCLEEI LCEFVQKDEL KPAVTQLLWE RATEKVACCP LERCSSVMLL GMMARGKPEI 660
VGSNLDTLVS IGLDEKFPQD YRLAQQVCHA IANISDRRKP SLGKRHPPFR LPQEHRLFER 720
LRETVTKGFV HPDPLWIPFK EVAVTLIYQL AEGPEVICAQ ILQGCAKQAL EKLEEKRTSQ 780
EDPKESPAML PTFLLMNLLS LAGDVALQQL VHLEQAVSGE LCRRRVLREE QEHKTKDPKE 840
KNTSSETTME EELGLVGATA DDTEAELIRG ICEMELLDGK QTLAAFVPLL LKVCNNPGLY 900
SNPDLSAAAS LALGKFCMI 919 
Gene Ontology
 GO:0005737; C:cytoplasm; IDA:HPA.
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0007076; P:mitotic chromosome condensation; IEA:InterPro. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR026971; CND1/NCAPD3.
 IPR007673; Condensin_cplx_su1.
 IPR024324; Condensin_cplx_su1_N. 
Pfam
 PF12922; Cnd1_N 
SMART
  
PROSITE
  
PRINTS