CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012460
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Condensin complex subunit 1 
Protein Synonyms/Alias
 Chromosome condensation-related SMC-associated protein 1; Chromosome-associated protein D2; hCAP-D2; Non-SMC condensin I complex subunit D2; XCAP-D2 homolog 
Gene Name
 NCAPD2 
Gene Synonyms/Alias
 CAPD2; CNAP1; KIAA0159 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
35VQEVLSIKHLPPQLRubiquitination[1, 2, 3]
78RSIDPGLKEDTLQFLubiquitination[1]
118NAHLNALKMNCYALIubiquitination[2]
148VDLDLGGKGKKARTKubiquitination[1]
151DLGGKGKKARTKAAHubiquitination[2]
155KGKKARTKAAHGFDWubiquitination[1]
215NPTINHQKNRPTREAubiquitination[1, 2, 4]
285IVREIGQKCPQELSRubiquitination[2]
298SRDPSGTKGFAAFLTubiquitination[1, 2, 3, 5]
395FTRIVQQKALPLTRFubiquitination[1, 2, 4]
416AVGRLADKSVLVCKNubiquitination[2]
452DLAGPLQKETQKLQEubiquitination[1, 2]
456PLQKETQKLQEMRAQubiquitination[2]
517TETTEDVKGRIYQLLubiquitination[1, 3]
571NILGLIFKGPAASTQubiquitination[3]
580PAASTQEKNPRESTGubiquitination[1]
616RGNDELVKQEMLVQYubiquitination[1, 4, 5]
633DAYSFSRKITEAIGIubiquitination[2]
685MLPLIWSKEPGVREAubiquitination[2, 4, 6, 7]
705RQLYLNPKGDSARAKubiquitination[1, 2, 3, 4]
749FVQKDELKPAVTQLLubiquitination[1, 2, 6, 7]
763LWERATEKVACCPLEubiquitination[2, 4, 8]
785LGMMARGKPEIVGSNubiquitination[1, 3]
804VSIGLDEKFPQDYRLubiquitination[1, 3, 4]
855RLRETVTKGFVHPDPubiquitination[1, 2, 6, 7]
900CAKQALEKLEEKRTSubiquitination[2]
962LREEQEHKTKDPKEKubiquitination[1]
969KTKDPKEKNTSSETTubiquitination[1]
1008EMELLDGKQTLAAFVubiquitination[2, 4]
1065LLFTMLEKSPLPIVRubiquitination[1, 2, 4]
1110DPAQQVRKTAGLVMTubiquitination[2]
1201LSYITKDKQTESLVEubiquitination[1, 2]
1209QTESLVEKLCQRFRTubiquitination[2]
1288IIDEFEQKLRACHTRubiquitination[1, 2]
1301TRGLDGIKELEIGQAubiquitination[1, 2, 6, 7]
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] 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]
 [3] 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]
 [4] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [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]
 [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
 Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases. May target the condensin complex to DNA via its C-terminal domain. 
Sequence Annotation
 REGION 1 603 Interactions with SMC2 and SMC4.
 MOTIF 1342 1362 Bipartite nuclear localization signal.
 MOD_RES 20 20 Phosphoserine.
 MOD_RES 585 585 Phosphoserine.
 MOD_RES 1310 1310 Phosphoserine.
 MOD_RES 1330 1330 Phosphoserine.
 MOD_RES 1331 1331 Phosphothreonine.
 MOD_RES 1333 1333 Phosphoserine.
 MOD_RES 1339 1339 Phosphothreonine.
 MOD_RES 1366 1366 Phosphoserine.
 MOD_RES 1367 1367 Phosphoserine.
 MOD_RES 1370 1370 Phosphoserine.
 MOD_RES 1371 1371 Phosphoserine.
 MOD_RES 1376 1376 Phosphoserine.
 MOD_RES 1384 1384 Phosphothreonine; by CDK1 (By
 MOD_RES 1389 1389 Phosphothreonine; by CDK1 (By  
Keyword
 Cell cycle; Cell division; Chromosome; Complete proteome; Cytoplasm; Direct protein sequencing; DNA condensation; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1401 AA 
Protein Sequence
MAPQMYEFHL PLSPEELLKS GGVNQYVVQE VLSIKHLPPQ LRAFQAAFRA QGPLAMLQHF 60
DTIYSILHHF RSIDPGLKED TLQFLIKVVS RHSQELPAIL DDTTLSGSDR NAHLNALKMN 120
CYALIRLLES FETMASQTNL VDLDLGGKGK KARTKAAHGF DWEEERQPIL QLLTQLLQLD 180
IRHLWNHSII EEEFVSLVTG CCYRLLENPT INHQKNRPTR EAITHLLGVA LTRYNHMLSA 240
TVKIIQMLQH FEHLAPVLVA AVSLWATDYG MKSIVGEIVR EIGQKCPQEL SRDPSGTKGF 300
AAFLTELAER VPAILMSSMC ILLDHLDGEN YMMRNAVLAA MAEMVLQVLS GDQLEAAARD 360
TRDQFLDTLQ AHGHDVNSFV RSRVLQLFTR IVQQKALPLT RFQAVVALAV GRLADKSVLV 420
CKNAIQLLAS FLANNPFSCK LSDADLAGPL QKETQKLQEM RAQRRTAAAS AVLDPEEEWE 480
AMLPELKSTL QQLLQLPQGE EEIPEQIANT ETTEDVKGRI YQLLAKASYK KAIILTREAT 540
GHFQESEPFS HIDPEESEET RLLNILGLIF KGPAASTQEK NPRESTGNMV TGQTVCKNKP 600
NMSDPEESRG NDELVKQEML VQYLQDAYSF SRKITEAIGI ISKMMYENTT TVVQEVIEFF 660
VMVFQFGVPQ ALFGVRRMLP LIWSKEPGVR EAVLNAYRQL YLNPKGDSAR AKAQALIQNL 720
SLLLVDASVG TIQCLEEILC EFVQKDELKP AVTQLLWERA TEKVACCPLE RCSSVMLLGM 780
MARGKPEIVG SNLDTLVSIG LDEKFPQDYR LAQQVCHAIA NISDRRKPSL GKRHPPFRLP 840
QEHRLFERLR ETVTKGFVHP DPLWIPFKEV AVTLIYQLAE GPEVICAQIL QGCAKQALEK 900
LEEKRTSQED PKESPAMLPT FLLMNLLSLA GDVALQQLVH LEQAVSGELC RRRVLREEQE 960
HKTKDPKEKN TSSETTMEEE LGLVGATADD TEAELIRGIC EMELLDGKQT LAAFVPLLLK 1020
VCNNPGLYSN PDLSAAASLA LGKFCMISAT FCDSQLRLLF TMLEKSPLPI VRSNLMVATG 1080
DLAIRFPNLV DPWTPHLYAR LRDPAQQVRK TAGLVMTHLI LKDMVKVKGQ VSEMAVLLID 1140
PEPQIAALAK NFFNELSHKG NAIYNLLPDI ISRLSDPELG VEEEPFHTIM KQLLSYITKD 1200
KQTESLVEKL CQRFRTSRTE RQQRDLAYCV SQLPLTERGL RKMLDNFDCF GDKLSDESIF 1260
SAFLSVVGKL RRGAKPEGKA IIDEFEQKLR ACHTRGLDGI KELEIGQAGS QRAPSAKKPS 1320
TGSRYQPLAS TASDNDFVTP EPRRTTRRHP NTQQRASKKK PKVVFSSDES SEEDLSAEMT 1380
EDETPKKTTP ILRASARRHR S 1401 
Gene Ontology
 GO:0000797; C:condensin core heterodimer; NAS:UniProtKB.
 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005634; C:nucleus; NAS:UniProtKB.
 GO:0045120; C:pronucleus; IEA:Compara.
 GO:0042393; F:histone binding; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB. 
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