CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-016300
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Condensin-2 complex subunit G2 
Protein Synonyms/Alias
 Chromosome-associated protein G2; CAP-G2; hCAP-G2; Leucine zipper protein 5; Non-SMC condensin II complex subunit G2 
Gene Name
 NCAPG2 
Gene Synonyms/Alias
 LUZP5 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
45LLDELSRKQKEELWQubiquitination[1]
47DELSRKQKEELWQRLubiquitination[1]
139ALPESERKLQSSIQDubiquitination[1]
159WEKGLPAKEDTGKTAubiquitination[1]
164PAKEDTGKTAFVMLLubiquitination[1]
178LRRSLETKTGADVCRubiquitination[1]
317LSYFHHQKKVRQGVEubiquitination[1]
318SYFHHQKKVRQGVEEubiquitination[1]
332EMLYRLYKPILWRGLubiquitination[1, 2]
402TGILGVCKITSKYWEubiquitination[1]
406GVCKITSKYWEMMPPubiquitination[1]
422ILIDLLKKVTGELAFubiquitination[1]
442DVRCSVFKCLPMILDubiquitination[1]
451LPMILDNKLSHPLLEubiquitination[1]
474SLHDNSEKVRVAFVDubiquitination[1]
485AFVDMLLKIKAVRAAubiquitination[1]
496VRAAKFWKICPMEHIubiquitination[1]
569TACTNIAKLIHVIRHubiquitination[1]
644MENNKEAKLYTINKFubiquitination[1]
650AKLYTINKFASVLPEubiquitination[1, 2, 3, 4, 5]
660SVLPEYLKVFKDDRCubiquitination[1, 2]
784LLSAPRKKLNHLLKAubiquitination[1]
790KKLNHLLKALETSKAubiquitination[1]
796LKALETSKADLESLLubiquitination[1, 3, 5]
809LLQTPGGKPRGFSEAubiquitination[1, 3, 5]
871DQEEDYLKLHRVIYQubiquitination[1]
956MLLDTVQKVFQKMLEubiquitination[5]
960TVQKVFQKMLECIARubiquitination[1]
971CIARSFRKQPEEGLRubiquitination[1]
1025EISHQLRKVSDVEELubiquitination[1]
1054CLIGIIIKSSNVVRSubiquitination[1]
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] 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]
 [3] 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]
 [4] 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]
 [5] 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] 
Functional Description
 Regulatory subunit of the condensin-2 complex, a complex which establishes mitotic chromosome architecture and is involved in physical rigidity of the chromatid axis. 
Sequence Annotation
 REPEAT 460 498 HEAT.
 MOD_RES 30 30 Phosphoserine.
 MOD_RES 805 805 Phosphothreonine.
 MOD_RES 1119 1119 Phosphothreonine.  
Keyword
 Alternative splicing; Cell cycle; Cell division; Complete proteome; DNA condensation; Mitosis; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1143 AA 
Protein Sequence
MEKRETFVQA VSKELVGEFL QFVQLDKEAS DPFSLNELLD ELSRKQKEEL WQRLKNLLTD 60
VLLESPVDGW QVVEAQGEDN METEHGSKMR KSIEIIYAIT SVILASVSVI NESENYEALL 120
ECVIILNGIL YALPESERKL QSSIQDLCVT WWEKGLPAKE DTGKTAFVML LRRSLETKTG 180
ADVCRLWRIH QALYCFDYDL EESGEIKDML LECFININYI KKEEGRRFLS CLFNWNINFI 240
KMIHGTIKNQ LQGLQKSLMV YIAEIYFRAW KKASGKILEA IENDCIQDFM FHGIHLPRRS 300
PVHSKVREVL SYFHHQKKVR QGVEEMLYRL YKPILWRGLK ARNSEVRSNA ALLFVEAFPI 360
RDPNLHAIEM DSEIQKQFEE LYSLLEDPYP MVRSTGILGV CKITSKYWEM MPPTILIDLL 420
KKVTGELAFD TSSADVRCSV FKCLPMILDN KLSHPLLEQL LPALRYSLHD NSEKVRVAFV 480
DMLLKIKAVR AAKFWKICPM EHILVRLETD SRPVSRRLVS LIFNSFLPVN QPEEVWCERC 540
VTLVQMNHAA ARRFYQYAHE HTACTNIAKL IHVIRHCLNA CIQRAVREPP EDEEEEDGRE 600
KENVTVLDKT LSVNDVACMA GLLEIIVILW KSIDRSMENN KEAKLYTINK FASVLPEYLK 660
VFKDDRCKIP LFMLMSFMPA SAVPPFSCGV ISTLRSREEG AVDKSYCTLL DCLCSWGQVG 720
HILELVDNWL PTEHAQAKSN TASKGRVQIH DTRPVKPELA LVYIEYLLTH PKNRECLLSA 780
PRKKLNHLLK ALETSKADLE SLLQTPGGKP RGFSEAAAPR AFGLHCRLSI HLQHKFCSEG 840
KVYLSMLEDT GFWLESKILS FIQDQEEDYL KLHRVIYQQI IQTYLTVCKD VVMVGLGDHQ 900
FQMQLLQRSL GIMQTVKGFF YVSLLLDILK EITGSSLIQK TDSDEEVAML LDTVQKVFQK 960
MLECIARSFR KQPEEGLRLL YSVQRPLHEF ITAVQSRHTD TPVHRGVLST LIAGPVVEIS 1020
HQLRKVSDVE ELTPPEHLSD LPPFSRCLIG IIIKSSNVVR SFLDELKACV ASNDIEGIVC 1080
LTAAVHIILV INAGKHKSSK VREVAATVHR KLKTFMEITL EEDSIERYED LLCCPGWALT 1140
PGLLDSIYPS ASVPIG 1156 
Gene Ontology
 GO:0005634; C:nucleus; IDA:HPA.
 GO:0035064; F:methylated histone residue binding; IDA:UniProtKB.
 GO:0051301; P:cell division; IEA:UniProtKB-KW.
 GO:0030261; P:chromosome condensation; IEA:UniProtKB-KW.
 GO:0001833; P:inner cell mass cell proliferation; IEA:Compara.
 GO:0007067; P:mitosis; IEA:UniProtKB-KW. 
Interpro
 IPR011989; ARM-like.
 IPR016024; ARM-type_fold.
 IPR024741; Condensin2_G2. 
Pfam
 PF12422; Condensin2nSMC 
SMART
  
PROSITE
 PS50077; HEAT_REPEAT 
PRINTS