dbPTM

CND3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CND3_HUMAN
UniProt AC	Q9BPX3
Protein Name	Condensin complex subunit 3
Gene Name	NCAPG
Organism	Homo sapiens (Human).
Sequence Length	1015
Subcellular Localization	Nucleus. Cytoplasm. Chromosome. In interphase cells, the majority of the condensin complex is found in the cytoplasm, while a minority of the complex is associated with chromatin. A subpopulation of the complex however remains associated with chromos
Protein 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..
Protein Sequence	MGAERRLLSIKEAFRLAQQPHQNQAKLVVALSRTYRTMDDKTVFHEEFIHYLKYVMVVYKREPAVERVIEFAAKFVTSFHQSDMEDDEEEEDGGLLNYLFTFLLKSHEANSNAVRFRVCLLINKLLGSMPENAQIDDDVFDKINKAMLIRLKDKIPNVRIQAVLALSRLQDPKDDECPVVNAYATLIENDSNPEVRRAVLSCIAPSAKTLPKIVGRTKDVKEAVRKLAYQVLAEKVHMRAMSIAQRVMLLQQGLNDRSDAVKQAMQKHLLQGWLRFSEGNILELLHRLDVENSSEVAVSVLNALFSITPLSELVGLCKNNDGRKLIPVETLTPEIALYWCALCEYLKSKGDEGEEFLEQILPEPVVYADYLLSYIQSIPVVNEEHRGDFSYIGNLMTKEFIGQQLILIIKSLDTSEEGGRKKLLAVLQEILILPTIPISLVSFLVERLLHIIIDDNKRTQIVTEIISEIRAPIVTVGVNNDPADVRKKELKMAEIKVKLIEAKEALENCITLQDFNRASELKEEIKALEDARINLLKETEQLEIKEVHIEKNDAETLQKCLILCYELLKQMSISTGLSATMNGIIESLILPGIISIHPVVRNLAVLCLGCCGLQNQDFARKHFVLLLQVLQIDDVTIKISALKAIFDQLMTFGIEPFKTKKIKTLHCEGTEINSDDEQESKEVEETATAKNVLKLLSDFLDSEVSELRTGAAEGLAKLMFSGLLVSSRILSRLILLWYNPVTEEDVQLRHCLGVFFPVFAYASRTNQECFEEAFLPTLQTLANAPASSPLAEIDITNVAELLVDLTRPSGLNPQAKTSQDYQALTVHDNLAMKICNEILTSPCSPEIRVYTKALSSLELSSHLAKDLLVLLNEILEQVKDRTCLRALEKIKIQLEKGNKEFGDQAEAAQDATLTTTTFQNEDEKNKEVYMTPLRGVKATQASKSTQLKTNRGQRKVTVSARTNRRCQTAEADSESDHEVPEPESEMKMRLPRRAKTAALEKSKLNLAQFLNEDLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
9	Phosphorylation	GAERRLLSIKEAFRL CHHHHHHHHHHHHHH	35.88	24719451
11	Ubiquitination	ERRLLSIKEAFRLAQ HHHHHHHHHHHHHHC	39.35	29967540
26	Acetylation	QPHQNQAKLVVALSR CCCCCHHHHHHHHHC	31.86	25953088
26	Malonylation	QPHQNQAKLVVALSR CCCCCHHHHHHHHHC	31.86	26320211
26	Ubiquitination	QPHQNQAKLVVALSR CCCCCHHHHHHHHHC	31.86	29967540
32	Phosphorylation	AKLVVALSRTYRTMD HHHHHHHHCCEECCC	16.91	21406692
33	Ubiquitination	KLVVALSRTYRTMDD HHHHHHHCCEECCCC	36.30	23000965
38	Ubiquitination	LSRTYRTMDDKTVFH HHCCEECCCCCCEEH	4.67	23000965
142	Ubiquitination	IDDDVFDKINKAMLI CCHHHHHHCCHHHHH	36.39	21906983
145	Ubiquitination	DVFDKINKAMLIRLK HHHHHCCHHHHHHHH	38.35	27667366
152	Ubiquitination	KAMLIRLKDKIPNVR HHHHHHHHCCCCCHH	47.31	-
154	Ubiquitination	MLIRLKDKIPNVRIQ HHHHHHCCCCCHHHH	59.48	29967540
167	Phosphorylation	IQAVLALSRLQDPKD HHHHHHHHCCCCCCC	25.90	24719451
201	Phosphorylation	EVRRAVLSCIAPSAK HHHHHHHHHHCCCCC	9.25	20068231
206	Phosphorylation	VLSCIAPSAKTLPKI HHHHHCCCCCCHHHH	33.12	20068231
208	Acetylation	SCIAPSAKTLPKIVG HHHCCCCCCHHHHHC	55.73	25953088
208	Ubiquitination	SCIAPSAKTLPKIVG HHHCCCCCCHHHHHC	55.73	27667366
212	Ubiquitination	PSAKTLPKIVGRTKD CCCCCHHHHHCCCHH	53.81	29967540
226	Ubiquitination	DVKEAVRKLAYQVLA HHHHHHHHHHHHHHH	30.76	33845483
235	Ubiquitination	AYQVLAEKVHMRAMS HHHHHHHHHHHHHHH	31.65	-
248	Sulfoxidation	MSIAQRVMLLQQGLN HHHHHHHHHHHCCCC	3.17	21406390
257	Methylation	LQQGLNDRSDAVKQA HHCCCCCHHHHHHHH	35.05	115484547
262	2-Hydroxyisobutyrylation	NDRSDAVKQAMQKHL CCHHHHHHHHHHHHH	33.78	-
262	Ubiquitination	NDRSDAVKQAMQKHL CCHHHHHHHHHHHHH	33.78	23000965
267	Ubiquitination	AVKQAMQKHLLQGWL HHHHHHHHHHHHHHH	24.12	23000965
293	Ubiquitination	HRLDVENSSEVAVSV HHCCCCCCHHHHHHH	17.86	22817900
297	Ubiquitination	VENSSEVAVSVLNAL CCCCHHHHHHHHHHH	5.47	22817900
308	Phosphorylation	LNALFSITPLSELVG HHHHHHCCCHHHHHC	19.58	18977199
308	Ubiquitination	LNALFSITPLSELVG HHHHHHCCCHHHHHC	19.58	22817900
332	Phosphorylation	LIPVETLTPEIALYW EEEHHHCCHHHHHHH	26.71	18977199
390	Phosphorylation	EEHRGDFSYIGNLMT HHHCCCCCHHCCHHC	22.15	25159151
391	Phosphorylation	EHRGDFSYIGNLMTK HHCCCCCHHCCHHCH	16.91	24732914
397	Phosphorylation	SYIGNLMTKEFIGQQ CHHCCHHCHHHHCCC	30.50	24732914
410	Ubiquitination	QQLILIIKSLDTSEE CCEEEHHHCCCCCCC	37.66	-
411	Phosphorylation	QLILIIKSLDTSEEG CEEEHHHCCCCCCCC	22.52	20873877
414	Phosphorylation	LIIKSLDTSEEGGRK EHHHCCCCCCCCHHH	43.24	20873877
415	Phosphorylation	IIKSLDTSEEGGRKK HHHCCCCCCCCHHHH	33.06	20873877
459	Phosphorylation	IIDDNKRTQIVTEII HCCCCCCHHHHHHHH	25.02	20068231
461	Ubiquitination	DDNKRTQIVTEIISE CCCCCHHHHHHHHHH	4.02	22817900
463	Phosphorylation	NKRTQIVTEIISEIR CCCHHHHHHHHHHCC	24.09	20068231
463	Ubiquitination	NKRTQIVTEIISEIR CCCHHHHHHHHHHCC	24.09	22817900
465	Ubiquitination	RTQIVTEIISEIRAP CHHHHHHHHHHCCCC	2.83	22817900
467	Phosphorylation	QIVTEIISEIRAPIV HHHHHHHHHCCCCEE	32.41	20068231
467	Ubiquitination	QIVTEIISEIRAPIV HHHHHHHHHCCCCEE	32.41	22817900
491	Acetylation	DVRKKELKMAEIKVK HHHHHHHHHHHHHHH	36.84	25953088
496	Ubiquitination	ELKMAEIKVKLIEAK HHHHHHHHHHHHHHH	25.48	32015554
498	Ubiquitination	KMAEIKVKLIEAKEA HHHHHHHHHHHHHHH	38.45	29967540
503	Ubiquitination	KVKLIEAKEALENCI HHHHHHHHHHHHHCC	30.63	32015554
509	Glutathionylation	AKEALENCITLQDFN HHHHHHHCCCHHHHH	1.51	22555962
511	Phosphorylation	EALENCITLQDFNRA HHHHHCCCHHHHHHH	22.14	27174698
519	Phosphorylation	LQDFNRASELKEEIK HHHHHHHHHHHHHHH	39.98	27174698
522	Acetylation	FNRASELKEEIKALE HHHHHHHHHHHHHHH	49.61	25953088
522	Ubiquitination	FNRASELKEEIKALE HHHHHHHHHHHHHHH	49.61	21906983
526	Ubiquitination	SELKEEIKALEDARI HHHHHHHHHHHHHHH	50.64	29967540
537	Ubiquitination	DARINLLKETEQLEI HHHHHHHHHHHHCEE	66.80	21906983
545	Ubiquitination	ETEQLEIKEVHIEKN HHHHCEEEEEEECCC	44.29	33845483
551	Ubiquitination	IKEVHIEKNDAETLQ EEEEEECCCCHHHHH	60.57	29967540
623	Ubiquitination	QDFARKHFVLLLQVL HHHHHHHHHHHHHHH	4.67	21890473
625	Ubiquitination	FARKHFVLLLQVLQI HHHHHHHHHHHHHCC	3.74	21890473
664	Phosphorylation	FKTKKIKTLHCEGTE CCCCCCEEEEEECCC	25.80	23927012
667	Ubiquitination	KKIKTLHCEGTEINS CCCEEEEEECCCCCC	6.08	22817900
669	Ubiquitination	IKTLHCEGTEINSDD CEEEEEECCCCCCCC	33.76	22817900
670	Phosphorylation	KTLHCEGTEINSDDE EEEEEECCCCCCCCH	16.05	23927012
670	Ubiquitination	KTLHCEGTEINSDDE EEEEEECCCCCCCCH	16.05	22817900
672	Ubiquitination	LHCEGTEINSDDEQE EEEECCCCCCCCHHH	6.33	22817900
674	Phosphorylation	CEGTEINSDDEQESK EECCCCCCCCHHHHH	52.69	29255136
680	Phosphorylation	NSDDEQESKEVEETA CCCCHHHHHHHHHHH	33.53	30278072
686	Phosphorylation	ESKEVEETATAKNVL HHHHHHHHHHHHHHH	18.79	23927012
688	Phosphorylation	KEVEETATAKNVLKL HHHHHHHHHHHHHHH	45.65	23927012
690	Ubiquitination	VEETATAKNVLKLLS HHHHHHHHHHHHHHH	43.14	21906983
692	Ubiquitination	ETATAKNVLKLLSDF HHHHHHHHHHHHHHH	5.00	22817900
694	Ubiquitination	ATAKNVLKLLSDFLD HHHHHHHHHHHHHHC	43.00	22817900
696	Ubiquitination	AKNVLKLLSDFLDSE HHHHHHHHHHHHCHH	4.39	22817900
697	Phosphorylation	KNVLKLLSDFLDSEV HHHHHHHHHHHCHHH	36.43	-
702	Phosphorylation	LLSDFLDSEVSELRT HHHHHHCHHHHHHHH	41.88	23401153
705	Phosphorylation	DFLDSEVSELRTGAA HHHCHHHHHHHHCCH	27.19	21712546
717	Ubiquitination	GAAEGLAKLMFSGLL CCHHHHHHHHHHHHH	45.59	-
726	Phosphorylation	MFSGLLVSSRILSRL HHHHHHHHHHHHHHH	17.54	24719451
731	Phosphorylation	LVSSRILSRLILLWY HHHHHHHHHHHHHHH	23.75	24702127
817	Phosphorylation	GLNPQAKTSQDYQAL CCCCCCCCCCCCHHH	34.34	25159151
818	Phosphorylation	LNPQAKTSQDYQALT CCCCCCCCCCCHHHC	21.98	25159151
821	Phosphorylation	QAKTSQDYQALTVHD CCCCCCCCHHHCCCH	6.50	24732914
825	Phosphorylation	SQDYQALTVHDNLAM CCCCHHHCCCHHHHH	20.86	24732914
833	Ubiquitination	VHDNLAMKICNEILT CCHHHHHHHHHHHHC	38.20	29967540
840	Phosphorylation	KICNEILTSPCSPEI HHHHHHHCCCCCHHH	35.96	28555341
841	Phosphorylation	ICNEILTSPCSPEIR HHHHHHCCCCCHHHH	22.06	21815630
844	Phosphorylation	EILTSPCSPEIRVYT HHHCCCCCHHHHHHH	29.02	21815630
851	Phosphorylation	SPEIRVYTKALSSLE CHHHHHHHHHHHHHH	13.64	-
852	Ubiquitination	PEIRVYTKALSSLEL HHHHHHHHHHHHHHH	29.64	23000965
854	Ubiquitination	IRVYTKALSSLELSS HHHHHHHHHHHHHHH	3.68	21890473
891	Ubiquitination	LRALEKIKIQLEKGN HHHHHHHHHHHHCCC	35.15	29967540
896	Ubiquitination	KIKIQLEKGNKEFGD HHHHHHHCCCHHHHH	76.11	22817900
898	Ubiquitination	KIQLEKGNKEFGDQA HHHHHCCCHHHHHHH	52.32	22817900
899	Ubiquitination	IQLEKGNKEFGDQAE HHHHCCCHHHHHHHH	64.19	22817900
901	Ubiquitination	LEKGNKEFGDQAEAA HHCCCHHHHHHHHHH	16.25	22817900
912	Phosphorylation	AEAAQDATLTTTTFQ HHHHHHCCEEECCEE	32.69	20860994
914	Phosphorylation	AAQDATLTTTTFQNE HHHHCCEEECCEECC	20.10	29978859
915	Phosphorylation	AQDATLTTTTFQNED HHHCCEEECCEECCC	27.27	29978859
916	Phosphorylation	QDATLTTTTFQNEDE HHCCEEECCEECCCC	22.00	29978859
917	Phosphorylation	DATLTTTTFQNEDEK HCCEEECCEECCCCC	22.56	29978859
929	Phosphorylation	DEKNKEVYMTPLRGV CCCCCEEEEEECCCC	9.07	25159151
931	Phosphorylation	KNKEVYMTPLRGVKA CCCEEEEEECCCCCC	11.07	30266825
934	Methylation	EVYMTPLRGVKATQA EEEEEECCCCCCCCC	49.41	115484539
937	Ubiquitination	MTPLRGVKATQASKS EEECCCCCCCCCCCC	48.84	29967540
942	Phosphorylation	GVKATQASKSTQLKT CCCCCCCCCCCCCCC	19.81	24732914
943	2-Hydroxyisobutyrylation	VKATQASKSTQLKTN CCCCCCCCCCCCCCC	61.61	-
943	Ubiquitination	VKATQASKSTQLKTN CCCCCCCCCCCCCCC	61.61	29967540
944	Phosphorylation	KATQASKSTQLKTNR CCCCCCCCCCCCCCC	20.91	26055452
945	Phosphorylation	ATQASKSTQLKTNRG CCCCCCCCCCCCCCC	41.48	24732914
949	Phosphorylation	SKSTQLKTNRGQRKV CCCCCCCCCCCCCEE	38.45	26425664
957	Phosphorylation	NRGQRKVTVSARTNR CCCCCEEEEEECCCC	16.27	30266825
959	Phosphorylation	GQRKVTVSARTNRRC CCCEEEEEECCCCCC	11.58	30266825
962	Phosphorylation	KVTVSARTNRRCQTA EEEEEECCCCCCCCC	32.56	28985074
968	Phosphorylation	RTNRRCQTAEADSES CCCCCCCCCCCCCCC	30.05	23401153
973	Phosphorylation	CQTAEADSESDHEVP CCCCCCCCCCCCCCC	46.15	22167270
975	Phosphorylation	TAEADSESDHEVPEP CCCCCCCCCCCCCCC	48.49	22167270
984	Phosphorylation	HEVPEPESEMKMRLP CCCCCCHHHHHHHCC	54.42	22167270
996	Phosphorylation	RLPRRAKTAALEKSK HCCHHHHHHHHHHHH	19.04	18669648
1002	Phosphorylation	KTAALEKSKLNLAQF HHHHHHHHHCCHHHH	32.76	28176443
1003	Ubiquitination	TAALEKSKLNLAQFL HHHHHHHHCCHHHHH	53.08	29967540
1015	Phosphorylation	QFLNEDLS------- HHHCCCCC-------	50.96	25159151

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
308	T	Phosphorylation	Kinase	CDK1	P06493	PSP
332	T	Phosphorylation	Kinase	CDK1	P06493	PSP
931	T	Phosphorylation	Kinase	CDK1	P06493	PSP
973	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
975	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of CND3_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 CND3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DNM3B_HUMAN	DNMT3B	physical	15148359
PARP1_HUMAN	PARP1	physical	16543152
XRCC1_HUMAN	XRCC1	physical	16543152
FEN1_HUMAN	FEN1	physical	16543152
DNLI3_HUMAN	LIG3	physical	16543152
DPOD1_HUMAN	POLD1	physical	16543152
DPOLB_HUMAN	POLB	physical	16543152
CND2_HUMAN	NCAPH	physical	17268547
SMC4_HUMAN	SMC4	physical	11136719
CND1_HUMAN	NCAPD2	physical	11136719
SMC2_HUMAN	SMC2	physical	11136719
CND2_HUMAN	NCAPH	physical	11136719
SMC4_HUMAN	SMC4	physical	14532007
CND1_HUMAN	NCAPD2	physical	14532007
SMC2_HUMAN	SMC2	physical	14532007
CND2_HUMAN	NCAPH	physical	14532007
SMC2_HUMAN	SMC2	physical	22939629
SMC4_HUMAN	SMC4	physical	22939629
CND1_HUMAN	NCAPD2	physical	22863883
CND2_HUMAN	NCAPH	physical	22863883
PLEC_HUMAN	PLEC	physical	22863883
SMC2_HUMAN	SMC2	physical	22863883
SMC4_HUMAN	SMC4	physical	22863883
ARRD1_HUMAN	ARRDC1	physical	26186194
CND2_HUMAN	NCAPH	physical	26344197
SMC2_HUMAN	SMC2	physical	26344197
SMC4_HUMAN	SMC4	physical	26344197
ESR1_HUMAN	ESR1	physical	26166704
SMC2_HUMAN	SMC2	physical	26166704
SMC4_HUMAN	SMC4	physical	26166704
CND1_HUMAN	NCAPD2	physical	26166704
CND2_HUMAN	NCAPH	physical	26166704
UBC_HUMAN	UBC	physical	26166704
DTX3L_HUMAN	DTX3L	physical	26166704
HECD1_HUMAN	HECTD1	physical	26166704
CNDH2_HUMAN	NCAPH2	physical	26166704
ARRD1_HUMAN	ARRDC1	physical	28514442

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 CND3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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 SER-390; SER-674 ANDSER-1015, AND MASS SPECTROMETRY.	19690332 [Abstract]
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; THR-968; SER-973;SER-975 AND SER-1015, AND MASS SPECTROMETRY.	19413330 [Abstract]
"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 SER-674; SER-973; SER-975;SER-1002 AND SER-1015, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-674 AND SER-1015, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"Improved titanium dioxide enrichment of phosphopeptides from HeLacells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."; Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; J. Proteome Res. 6:4150-4162(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-463; SER-467; SER-944AND SER-959, AND MASS SPECTROMETRY.	17924679 [Abstract]
"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 SER-390 AND SER-674, ANDMASS SPECTROMETRY.	16565220 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-973; SER-975AND SER-1015, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-686, AND MASSSPECTROMETRY.	18088087 [Abstract]