CNDG2_HUMAN - dbPTM
CNDG2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNDG2_HUMAN
UniProt AC Q86XI2
Protein Name Condensin-2 complex subunit G2
Gene Name NCAPG2
Organism Homo sapiens (Human).
Sequence Length 1143
Subcellular Localization Nucleus .
Protein 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..
Protein Sequence MEKRETFVQAVSKELVGEFLQFVQLDKEASDPFSLNELLDELSRKQKEELWQRLKNLLTDVLLESPVDGWQVVEAQGEDNMETEHGSKMRKSIEIIYAITSVILASVSVINESENYEALLECVIILNGILYALPESERKLQSSIQDLCVTWWEKGLPAKEDTGKTAFVMLLRRSLETKTGADVCRLWRIHQALYCFDYDLEESGEIKDMLLECFININYIKKEEGRRFLSCLFNWNINFIKMIHGTIKNQLQGLQKSLMVYIAEIYFRAWKKASGKILEAIENDCIQDFMFHGIHLPRRSPVHSKVREVLSYFHHQKKVRQGVEEMLYRLYKPILWRGLKARNSEVRSNAALLFVEAFPIRDPNLHAIEMDSEIQKQFEELYSLLEDPYPMVRSTGILGVCKITSKYWEMMPPTILIDLLKKVTGELAFDTSSADVRCSVFKCLPMILDNKLSHPLLEQLLPALRYSLHDNSEKVRVAFVDMLLKIKAVRAAKFWKICPMEHILVRLETDSRPVSRRLVSLIFNSFLPVNQPEEVWCERCVTLVQMNHAAARRFYQYAHEHTACTNIAKLIHVIRHCLNACIQRAVREPPEDEEEEDGREKENVTVLDKTLSVNDVACMAGLLEIIVILWKSIDRSMENNKEAKLYTINKFASVLPEYLKVFKDDRCKIPLFMLMSFMPASAVPPFSCGVISTLRSREEGAVDKSYCTLLDCLCSWGQVGHILELVDNWLPTEHAQAKSNTASKGRVQIHDTRPVKPELALVYIEYLLTHPKNRECLLSAPRKKLNHLLKALETSKADLESLLQTPGGKPRGFSEAAAPRAFGLHCRLSIHLQHKFCSEGKVYLSMLEDTGFWLESKILSFIQDQEEDYLKLHRVIYQQIIQTYLTVCKDVVMVGLGDHQFQMQLLQRSLGIMQTVKGFFYVSLLLDILKEITGSSLIQKTDSDEEVAMLLDTVQKVFQKMLECIARSFRKQPEEGLRLLYSVQRPLHEFITAVQSRHTDTPVHRGVLSTLIAGPVVEISHQLRKVSDVEELTPPEHLSDLPPFSRCLIGIIIKSSNVVRSFLDELKACVASNDIEGIVCLTAAVHIILVINAGKHKSSKVREVAATVHRKLKTFMEITLEEDSIERFLYESSSRTLGELLNS
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
3Ubiquitination-----MEKRETFVQA
-----CCHHHHHHHH		68.35-
6Phosphorylation--MEKRETFVQAVSK
--CCHHHHHHHHHHH		32.8925159151
30PhosphorylationVQLDKEASDPFSLNE
HCCCHHHCCCCCHHH		47.0825159151
34PhosphorylationKEASDPFSLNELLDE
HHHCCCCCHHHHHHH		35.3622199227
45UbiquitinationLLDELSRKQKEELWQ
HHHHHHHHHHHHHHH		63.45-
45 (in isoform 2)Ubiquitination-63.45-
47UbiquitinationDELSRKQKEELWQRL
HHHHHHHHHHHHHHH		57.08-
47 (in isoform 2)Ubiquitination-57.08-
83PhosphorylationQGEDNMETEHGSKMR
CCCCCCCCCCHHHHH		23.63-
106PhosphorylationITSVILASVSVINES
HHHHHHHHHHCCCCC		16.1022210691
108PhosphorylationSVILASVSVINESEN
HHHHHHHHCCCCCCC		18.1322210691
131PhosphorylationIILNGILYALPESER
HHHHHHHHHCCHHHH		12.2722210691
136PhosphorylationILYALPESERKLQSS
HHHHCCHHHHHHHHH		40.5422210691
139UbiquitinationALPESERKLQSSIQD
HCCHHHHHHHHHHHH		46.99-
139 (in isoform 2)Ubiquitination-46.99-
154UbiquitinationLCVTWWEKGLPAKED
HHHHHHHCCCCCCCC		52.61-
159UbiquitinationWEKGLPAKEDTGKTA
HHCCCCCCCCCCHHH		54.9321906983
159 (in isoform 1)Ubiquitination-54.9321890473
159 (in isoform 2)Ubiquitination-54.9321890473
164UbiquitinationPAKEDTGKTAFVMLL
CCCCCCCHHHHHHHH		38.4821906983
164 (in isoform 1)Ubiquitination-38.4821890473
164 (in isoform 2)Ubiquitination-38.4821890473
165PhosphorylationAKEDTGKTAFVMLLR
CCCCCCHHHHHHHHH		27.0329457462
178UbiquitinationLRRSLETKTGADVCR
HHHHHCCCCCHHHHH		35.27-
178 (in isoform 2)Ubiquitination-35.27-
248UbiquitinationKMIHGTIKNQLQGLQ
HHHHHHHHHHHHHHH		38.18-
257PhosphorylationQLQGLQKSLMVYIAE
HHHHHHHHHHHHHHH		14.56-
276UbiquitinationAWKKASGKILEAIEN
HHHHHHCHHHHHHHC		41.44-
305UbiquitinationRRSPVHSKVREVLSY
CCCCCHHHHHHHHHH		30.36-
317UbiquitinationLSYFHHQKKVRQGVE
HHHHHHHHHHHHHHH		49.21-
317 (in isoform 2)Ubiquitination-49.21-
318 (in isoform 2)Ubiquitination-35.76-
332AcetylationEMLYRLYKPILWRGL
HHHHHHHHHHHHHHH		30.1226051181
332UbiquitinationEMLYRLYKPILWRGL
HHHHHHHHHHHHHHH		30.1221890473
332 (in isoform 1)Ubiquitination-30.1221890473
332 (in isoform 2)Ubiquitination-30.1221890473
382PhosphorylationQKQFEELYSLLEDPY
HHHHHHHHHHHHCCC		10.6828450419
383PhosphorylationKQFEELYSLLEDPYP
HHHHHHHHHHHCCCC		38.8228450419
389PhosphorylationYSLLEDPYPMVRSTG
HHHHHCCCCCHHCCC		19.1128450419
402AcetylationTGILGVCKITSKYWE
CCCHHEEECCHHHHH		46.7625953088
402UbiquitinationTGILGVCKITSKYWE
CCCHHEEECCHHHHH		46.76-
402 (in isoform 2)Ubiquitination-46.76-
406UbiquitinationGVCKITSKYWEMMPP
HEEECCHHHHHHCCC		45.81-
406 (in isoform 2)Ubiquitination-45.81-
407PhosphorylationVCKITSKYWEMMPPT
EEECCHHHHHHCCCH		13.33-
414PhosphorylationYWEMMPPTILIDLLK
HHHHCCCHHHHHHHH		23.65-
422UbiquitinationILIDLLKKVTGELAF
HHHHHHHHHHCCCCC		45.0221906983
422 (in isoform 1)Ubiquitination-45.0221890473
422 (in isoform 2)Ubiquitination-45.0221890473
442UbiquitinationDVRCSVFKCLPMILD
HHCHHHHHHHHHHHC		32.48-
442 (in isoform 2)Ubiquitination-32.48-
451UbiquitinationLPMILDNKLSHPLLE
HHHHHCCCCCCHHHH		51.54-
451 (in isoform 2)Ubiquitination-51.54-
474UbiquitinationSLHDNSEKVRVAFVD
HCCCCCCHHHHHHHH		34.8521906983
474 (in isoform 1)Ubiquitination-34.8521890473
474 (in isoform 2)Ubiquitination-34.8521890473
485 (in isoform 2)Ubiquitination-37.89-
496AcetylationVRAAKFWKICPMEHI
HHHHHHHHHCCHHHE		37.2525953088
496UbiquitinationVRAAKFWKICPMEHI
HHHHHHHHHCCHHHE		37.25-
496 (in isoform 2)Ubiquitination-37.25-
509PhosphorylationHILVRLETDSRPVSR
HEEHHHHCCCCCCHH		43.8123090842
511PhosphorylationLVRLETDSRPVSRRL
EHHHHCCCCCCHHHH		46.0023090842
515PhosphorylationETDSRPVSRRLVSLI
HCCCCCCHHHHHHHH		17.8623090842
555PhosphorylationHAAARRFYQYAHEHT
HHHHHHHHHHHHHHC		9.9829496907
557PhosphorylationAARRFYQYAHEHTAC
HHHHHHHHHHHHCCH		9.8829496907
569UbiquitinationTACTNIAKLIHVIRH
CCHHHHHHHHHHHHH		44.15-
569 (in isoform 2)Ubiquitination-44.15-
601UbiquitinationEEEDGREKENVTVLD
CCCCCCCCCCEEEEE		53.9121906983
601 (in isoform 1)Ubiquitination-53.9121890473
601 (in isoform 2)Ubiquitination-53.9121890473
605PhosphorylationGREKENVTVLDKTLS
CCCCCCEEEEECCCC		27.2519691289
641UbiquitinationDRSMENNKEAKLYTI
HHHHHCCHHCEEHHH		71.3021906983
641 (in isoform 1)Ubiquitination-71.3021890473
641 (in isoform 2)Ubiquitination-71.3021890473
644UbiquitinationMENNKEAKLYTINKF
HHCCHHCEEHHHHHH		43.02-
644 (in isoform 2)Ubiquitination-43.02-
647PhosphorylationNKEAKLYTINKFASV
CHHCEEHHHHHHHHH		28.63-
650AcetylationAKLYTINKFASVLPE
CEEHHHHHHHHHCHH		38.1626051181
650SumoylationAKLYTINKFASVLPE
CEEHHHHHHHHHCHH		38.16-
650UbiquitinationAKLYTINKFASVLPE
CEEHHHHHHHHHCHH		38.1621890473
650 (in isoform 1)Ubiquitination-38.1621890473
650 (in isoform 2)Ubiquitination-38.1621890473
660UbiquitinationSVLPEYLKVFKDDRC
HHCHHHHHHHCCCCC		44.7321890473
660 (in isoform 1)Ubiquitination-44.7321890473
660 (in isoform 2)Ubiquitination-44.7321890473
663UbiquitinationPEYLKVFKDDRCKIP
HHHHHHHCCCCCCCC		62.80-
752PhosphorylationGRVQIHDTRPVKPEL
CCCEEECCCCCCHHH		23.7828102081
779PhosphorylationKNRECLLSAPRKKLN
CCCHHHHCCCHHHHH		24.2324719451
784UbiquitinationLLSAPRKKLNHLLKA
HHCCCHHHHHHHHHH		56.66-
784 (in isoform 2)Ubiquitination-56.66-
790UbiquitinationKKLNHLLKALETSKA
HHHHHHHHHHHCCHH		58.23-
790 (in isoform 2)Ubiquitination-58.23-
796UbiquitinationLKALETSKADLESLL
HHHHHCCHHHHHHHH		54.0321906983
796 (in isoform 1)Ubiquitination-54.0321890473
796 (in isoform 2)Ubiquitination-54.0321890473
801PhosphorylationTSKADLESLLQTPGG
CCHHHHHHHHCCCCC		41.5024732914
805PhosphorylationDLESLLQTPGGKPRG
HHHHHHCCCCCCCCC		24.7025159151
809UbiquitinationLLQTPGGKPRGFSEA
HHCCCCCCCCCCCCC		37.1421906983
809 (in isoform 1)Ubiquitination-37.1421890473
809 (in isoform 2)Ubiquitination-37.1421890473
814PhosphorylationGGKPRGFSEAAAPRA
CCCCCCCCCCHHCHH		29.2019691289
871UbiquitinationDQEEDYLKLHRVIYQ
CCCHHHHHHHHHHHH		35.7021906983
871 (in isoform 1)Ubiquitination-35.7021890473
871 (in isoform 2)Ubiquitination-35.7021890473
909PhosphorylationQMQLLQRSLGIMQTV
HHHHHHHHHCHHHHH		20.2720860994
915PhosphorylationRSLGIMQTVKGFFYV
HHHCHHHHHHHHHHH		13.55-
933PhosphorylationLDILKEITGSSLIQK
HHHHHHHHCCCCCCC		31.9120860994
935PhosphorylationILKEITGSSLIQKTD
HHHHHHCCCCCCCCC		17.2022067460
936PhosphorylationLKEITGSSLIQKTDS
HHHHHCCCCCCCCCC		30.7322067460
940UbiquitinationTGSSLIQKTDSDEEV
HCCCCCCCCCCHHHH		47.5121906983
940 (in isoform 1)Ubiquitination-47.5121890473
940 (in isoform 2)Ubiquitination-47.5121890473
956UbiquitinationMLLDTVQKVFQKMLE
HHHHHHHHHHHHHHH		40.45-
956 (in isoform 2)Ubiquitination-40.45-
960UbiquitinationTVQKVFQKMLECIAR
HHHHHHHHHHHHHHH		33.71-
960 (in isoform 2)Ubiquitination-33.71-
971UbiquitinationCIARSFRKQPEEGLR
HHHHHHHHCCHHHHH		69.10-
971 (in isoform 2)Ubiquitination-69.10-
1025UbiquitinationEISHQLRKVSDVEEL
HHHHHHCCCCCHHHC		55.472190698
1025 (in isoform 1)Ubiquitination-55.4721890473
1025 (in isoform 2)Ubiquitination-55.4721890473
1054UbiquitinationCLIGIIIKSSNVVRS
CHHHHHHCCCHHHHH		37.11-
1054 (in isoform 2)Ubiquitination-37.11-
1114PhosphorylationTVHRKLKTFMEITLE
HHHHHHHHHHEEECC		38.3519691289
1119PhosphorylationLKTFMEITLEEDSIE
HHHHHEEECCHHHHH		18.1416565220
1130PhosphorylationDSIERFLYESSSRTL
HHHHHHHHHHCCCCH		15.85-
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CNDG2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNDG2_HUMAN !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CNDG2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
ACTN4_HUMANACTN4physical
26344197
CLCB_HUMANCLTBphysical
26344197
CNDD3_HUMANNCAPD3physical
26344197
SSU72_HUMANSSU72physical
26344197
RAF1_HUMANRAF1physical
27173435
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNDG2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-30, AND MASSSPECTROMETRY.
"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-814, AND MASSSPECTROMETRY.
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1119, AND MASSSPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805 AND THR-1119, ANDMASS SPECTROMETRY.
"Phosphoproteome analysis of the human mitotic spindle.";
Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R.;
Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-805 AND THR-1119, ANDMASS SPECTROMETRY.

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