SMC2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: SMC2_HUMAN
• UniProt AC: O95347
• Protein Name: Structural maintenance of chromosomes protein 2
• Gene Name: SMC2
• Organism: Homo sapiens (Human).
• Sequence Length: 1197
• 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 chro
• Protein Description: Central component 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: MHIKSIILEGFKSYAQRTEVNGFDPLFNAITGLNGSGKSNILDSICFLLGISNLSQVRASNLQDLVYKNGQAGITKASVSITFDNSDKKQSPLGFEVHDEITVTRQVVIGGRNKYLINGVNANNTRVQDLFCSVGLNVNNPHFLIMQGRITKVLNMKPPEILSMIEEAAGTRMYEYKKIAAQKTIEKKEAKLKEIKTILEEEITPTIQKLKEERSSYLEYQKVMREIEHLSRLYIAYQFLLAEDTKVRSAEELKEMQDKVIKLQEELSENDKKIKALNHEIEELEKRKDKETGGILRSLEDALAEAQRVNTKSQSAFDLKKKNLACEESKRKELEKNMVEDSKTLAAKEKEVKKITDGLHALQEASNKDAEALAAAQQHFNAVSAGLSSNEDGAEATLAGQMMACKNDISKAQTEAKQAQMKLKHAQQELKNKQAEVKKMDSGYRKDQEALEAVKRLKEKLEAEMKKLNYEENKEESLLEKRRQLSRDIGRLKETYEALLARFPNLRFAYKDPEKNWNRNCVKGLVASLISVKDTSATTALELVAGERLYNVVVDTEVTGKKLLERGELKRRYTIIPLNKISARCIAPETLRVAQNLVGPDNVHVALSLVEYKPELQKAMEFVFGTTFVCDNMDNAKKVAFDKRIMTRTVTLGGDVFDPHGTLSGGARSQAASILTKFQELKDVQDELRIKENELRALEEELAGLKNTAEKYRQLKQQWEMKTEEADLLQTKLQQSSYHKQQEELDALKKTIEESEETLKNTKEIQRKAEEKYEVLENKMKNAEAERERELKDAQKKLDCAKTKADASSKKMKEKQQEVEAITLELEELKREHTSYKQQLEAVNEAIKSYESQIEVMAAEVAKNKESVNKAQEEVTKQKEVITAQDTVIKAKYAEVAKHKEQNNDSQLKIKELDHNISKHKREAEDGAAKVSKMLKDYDWINAERHLFGQPNSAYDFKTNNPKEAGQRLQKLQEMKEKLGRNVNMRAMNVLTEAEERYNDLMKKKRIVENDKSKILTTIEDLDQKKNQALNIAWQKVNKDFGSIFSTLLPGANAMLAPPEGQTVLDGLEFKVALGNTWKENLTELSGGQRSLVALSLILSMLLFKPAPIYILDEVDAALDLSHTQNIGQMLRTHFTHSQFIVVSLKEGMFNNANVLFKTKFVDGVSTVARFTQCQNGKISKEAKSKAKPPKGAHVEV

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
4	Ubiquitination	----MHIKSIILEGF ----CCCCCHHHHHH	37.21	-
12	Ubiquitination	SIILEGFKSYAQRTE CHHHHHHHHHHHHHC	54.11	21890473
12 (in isoform 1)	Ubiquitination	-	54.11	21890473
12 (in isoform 2)	Ubiquitination	-	54.11	21890473
60	Phosphorylation	NLSQVRASNLQDLVY CHHHHHHHCHHHHHH	27.75	19691289
67	Phosphorylation	SNLQDLVYKNGQAGI HCHHHHHHHCCCCCC	13.16	21406692
68	Acetylation	NLQDLVYKNGQAGIT CHHHHHHHCCCCCCC	47.31	25953088
68	Ubiquitination	NLQDLVYKNGQAGIT CHHHHHHHCCCCCCC	47.31	21890473
68 (in isoform 1)	Ubiquitination	-	47.31	21890473
68 (in isoform 2)	Ubiquitination	-	47.31	21890473
80	Phosphorylation	GITKASVSITFDNSD CCCEEEEEEEECCCC	17.26	17929957
89	Ubiquitination	TFDNSDKKQSPLGFE EECCCCCCCCCCCEE	62.08	-
114	Acetylation	VVIGGRNKYLINGVN EEECCCCCEEEECCC	39.82	19608861
114	Ubiquitination	VVIGGRNKYLINGVN EEECCCCCEEEECCC	39.82	19608861
151	Phosphorylation	LIMQGRITKVLNMKP EEECCEEEHHHCCCC	17.46	20068231
152	Ubiquitination	IMQGRITKVLNMKPP EECCEEEHHHCCCCH	42.21	-
157	Ubiquitination	ITKVLNMKPPEILSM EEHHHCCCCHHHHHH	57.24	-
163	Phosphorylation	MKPPEILSMIEEAAG CCCHHHHHHHHHHHC	24.31	20068231
171	Phosphorylation	MIEEAAGTRMYEYKK HHHHHHCCCHHHHHH	13.92	20068231
177	Ubiquitination	GTRMYEYKKIAAQKT CCCHHHHHHHHHHHH	26.26	-
178	Ubiquitination	TRMYEYKKIAAQKTI CCHHHHHHHHHHHHH	36.35	-
183	2-Hydroxyisobutyrylation	YKKIAAQKTIEKKEA HHHHHHHHHHHHHHH	46.90	-
183	Acetylation	YKKIAAQKTIEKKEA HHHHHHHHHHHHHHH	46.90	25953088
183	Ubiquitination	YKKIAAQKTIEKKEA HHHHHHHHHHHHHHH	46.90	-
184	Phosphorylation	KKIAAQKTIEKKEAK HHHHHHHHHHHHHHH	23.45	30624053
196	Ubiquitination	EAKLKEIKTILEEEI HHHHHHHHHHHHHCC	30.51	-
209	Ubiquitination	EITPTIQKLKEERSS CCCHHHHHHHHHHHH	58.64	-
211	Ubiquitination	TPTIQKLKEERSSYL CHHHHHHHHHHHHHH	65.64	-
215	Phosphorylation	QKLKEERSSYLEYQK HHHHHHHHHHHHHHH	26.98	25627689
216	Phosphorylation	KLKEERSSYLEYQKV HHHHHHHHHHHHHHH	39.70	25627689
222	Acetylation	SSYLEYQKVMREIEH HHHHHHHHHHHHHHH	36.78	19608861
222	Ubiquitination	SSYLEYQKVMREIEH HHHHHHHHHHHHHHH	36.78	19608861
249	Phosphorylation	AEDTKVRSAEELKEM HCCCCCCCHHHHHHH	42.91	-
254	Acetylation	VRSAEELKEMQDKVI CCCHHHHHHHHHHHH	55.19	25953088
268	Phosphorylation	IKLQEELSENDKKIK HHHHHHHCCCHHHHH	37.32	-
272	Acetylation	EELSENDKKIKALNH HHHCCCHHHHHHHHH	68.90	25953088
272	Ubiquitination	EELSENDKKIKALNH HHHCCCHHHHHHHHH	68.90	-
275	Ubiquitination	SENDKKIKALNHEIE CCCHHHHHHHHHHHH	56.55	-
290	Ubiquitination	ELEKRKDKETGGILR HHHHHCCHHCCCHHH	61.28	-
292	Phosphorylation	EKRKDKETGGILRSL HHHCCHHCCCHHHHH	46.58	-
298	Phosphorylation	ETGGILRSLEDALAE HCCCHHHHHHHHHHH	32.44	24719451
312	Acetylation	EAQRVNTKSQSAFDL HHHHCCCCCCCHHHH	41.09	25953088
312	Ubiquitination	EAQRVNTKSQSAFDL HHHHCCCCCCCHHHH	41.09	-
315	Phosphorylation	RVNTKSQSAFDLKKK HCCCCCCCHHHHHHH	37.68	24719451
320	Acetylation	SQSAFDLKKKNLACE CCCHHHHHHHHHCCH	64.64	23749302
320	Succinylation	SQSAFDLKKKNLACE CCCHHHHHHHHHCCH	64.64	23954790
321	Acetylation	QSAFDLKKKNLACEE CCHHHHHHHHHCCHH	54.94	11923817
321	Ubiquitination	QSAFDLKKKNLACEE CCHHHHHHHHHCCHH	54.94	-
330	Acetylation	NLACEESKRKELEKN HHCCHHHHHHHHHHH	71.42	23749302
336	Acetylation	SKRKELEKNMVEDSK HHHHHHHHHHHHHHH	64.07	20167786
343	2-Hydroxyisobutyrylation	KNMVEDSKTLAAKEK HHHHHHHHHHHHHHH	60.94	-
343	Acetylation	KNMVEDSKTLAAKEK HHHHHHHHHHHHHHH	60.94	23236377
348	2-Hydroxyisobutyrylation	DSKTLAAKEKEVKKI HHHHHHHHHHHHHHH	64.81	-
348	Acetylation	DSKTLAAKEKEVKKI HHHHHHHHHHHHHHH	64.81	20167786
353	Acetylation	AAKEKEVKKITDGLH HHHHHHHHHHHHHHH	39.28	20167786
354	2-Hydroxyisobutyrylation	AKEKEVKKITDGLHA HHHHHHHHHHHHHHH	56.89	-
455	Acetylation	QEALEAVKRLKEKLE HHHHHHHHHHHHHHH	60.09	25953088
458	Acetylation	LEAVKRLKEKLEAEM HHHHHHHHHHHHHHH	57.76	25953088
460	Acetylation	AVKRLKEKLEAEMKK HHHHHHHHHHHHHHH	50.46	25953088
477	Phosphorylation	YEENKEESLLEKRRQ HHHHHHHHHHHHHHH	39.07	24719451
481	Ubiquitination	KEESLLEKRRQLSRD HHHHHHHHHHHHHHH	53.50	-
486	Phosphorylation	LEKRRQLSRDIGRLK HHHHHHHHHHHHHHH	21.40	-
493	Ubiquitination	SRDIGRLKETYEALL HHHHHHHHHHHHHHH	46.80	-
495	Phosphorylation	DIGRLKETYEALLAR HHHHHHHHHHHHHHH	25.69	28152594
496	Phosphorylation	IGRLKETYEALLARF HHHHHHHHHHHHHHC	10.57	28152594
511	Acetylation	PNLRFAYKDPEKNWN CCCCEEECCCCCCCC	64.48	25953088
511	Ubiquitination	PNLRFAYKDPEKNWN CCCCEEECCCCCCCC	64.48	-
515	Acetylation	FAYKDPEKNWNRNCV EEECCCCCCCCCCHH	73.06	25953088
515	Ubiquitination	FAYKDPEKNWNRNCV EEECCCCCCCCCCHH	73.06	-
523	Ubiquitination	NWNRNCVKGLVASLI CCCCCHHHHHHHHHC	49.04	-
531	Phosphorylation	GLVASLISVKDTSAT HHHHHHCCCCCCCCC	28.54	24719451
533	Ubiquitination	VASLISVKDTSATTA HHHHCCCCCCCCCHH	48.80	-
535	Phosphorylation	SLISVKDTSATTALE HHCCCCCCCCCHHHH	17.97	24719451
550	Phosphorylation	LVAGERLYNVVVDTE HHCCCCCEEEEEECC	16.48	27642862
561	Acetylation	VDTEVTGKKLLERGE EECCCCCHHHHHCCC	30.77	26051181
562	Ubiquitination	DTEVTGKKLLERGEL ECCCCCHHHHHCCCC	60.70	-
573	Phosphorylation	RGELKRRYTIIPLNK CCCCCCEEEEEEHHH	13.31	26657352
574	Phosphorylation	GELKRRYTIIPLNKI CCCCCEEEEEEHHHH	15.60	26657352
580	Acetylation	YTIIPLNKISARCIA EEEEEHHHHHCHHCC	45.80	25953088
580	Ubiquitination	YTIIPLNKISARCIA EEEEEHHHHHCHHCC	45.80	-
590	Phosphorylation	ARCIAPETLRVAQNL CHHCCHHHHHHHHHH	20.85	24719451
643	Acetylation	AKKVAFDKRIMTRTV HHHHHHCCCCCCCEE	37.05	26051181
669	Phosphorylation	TLSGGARSQAASILT CCCCCHHHHHHHHHH	24.52	21406692
673	Phosphorylation	GARSQAASILTKFQE CHHHHHHHHHHHHHH	22.58	24719451
676	Phosphorylation	SQAASILTKFQELKD HHHHHHHHHHHHHHH	28.30	21406692
677	2-Hydroxyisobutyrylation	QAASILTKFQELKDV HHHHHHHHHHHHHHH	41.42	-
677	Acetylation	QAASILTKFQELKDV HHHHHHHHHHHHHHH	41.42	19608861
677	Ubiquitination	QAASILTKFQELKDV HHHHHHHHHHHHHHH	41.42	21890473
677 (in isoform 1)	Ubiquitination	-	41.42	21890473
677 (in isoform 2)	Ubiquitination	-	41.42	21890473
682	Acetylation	LTKFQELKDVQDELR HHHHHHHHHHHHHHH	55.91	25953088
682	Ubiquitination	LTKFQELKDVQDELR HHHHHHHHHHHHHHH	55.91	-
691	Ubiquitination	VQDELRIKENELRAL HHHHHHHCHHHHHHH	48.31	-
706	Acetylation	EEELAGLKNTAEKYR HHHHHHCHHHHHHHH	51.87	25953088
706	Ubiquitination	EEELAGLKNTAEKYR HHHHHHCHHHHHHHH	51.87	-
711	2-Hydroxyisobutyrylation	GLKNTAEKYRQLKQQ HCHHHHHHHHHHHHH	43.18	-
711	Ubiquitination	GLKNTAEKYRQLKQQ HCHHHHHHHHHHHHH	43.18	-
732	2-Hydroxyisobutyrylation	EADLLQTKLQQSSYH HHHHHHHHHHHCHHH	31.19	-
732	Ubiquitination	EADLLQTKLQQSSYH HHHHHHHHHHHCHHH	31.19	-
749	Acetylation	QEELDALKKTIEESE HHHHHHHHHHHHHHH	49.98	25953088
760	Acetylation	EESEETLKNTKEIQR HHHHHHHHCHHHHHH	70.73	23236377
763	2-Hydroxyisobutyrylation	EETLKNTKEIQRKAE HHHHHCHHHHHHHHH	63.31	-
768	Acetylation	NTKEIQRKAEEKYEV CHHHHHHHHHHHHHH	43.72	133755
792	Acetylation	AERERELKDAQKKLD HHHHHHHHHHHHHHH	46.38	18530289
802	2-Hydroxyisobutyrylation	QKKLDCAKTKADASS HHHHHHHHHHHHHHH	57.81	-
809	Phosphorylation	KTKADASSKKMKEKQ HHHHHHHHHHHHHHH	37.71	22817901
813	Acetylation	DASSKKMKEKQQEVE HHHHHHHHHHHHHHH	71.31	18530299
815	Acetylation	SSKKMKEKQQEVEAI HHHHHHHHHHHHHHH	52.33	25953088
837	Acetylation	KREHTSYKQQLEAVN HHHCCCHHHHHHHHH	31.19	23749302
849	Phosphorylation	AVNEAIKSYESQIEV HHHHHHHHHHHHHHH	28.19	24719451
850	Phosphorylation	VNEAIKSYESQIEVM HHHHHHHHHHHHHHH	18.01	28102081
852	Phosphorylation	EAIKSYESQIEVMAA HHHHHHHHHHHHHHH	28.38	24719451
883	Phosphorylation	TKQKEVITAQDTVIK HHHHHHCCCHHHHHH	24.36	29514088
887	Phosphorylation	EVITAQDTVIKAKYA HHCCCHHHHHHHHHH	16.43	29514088
890	2-Hydroxyisobutyrylation	TAQDTVIKAKYAEVA CCHHHHHHHHHHHHH	34.19	-
890	Acetylation	TAQDTVIKAKYAEVA CCHHHHHHHHHHHHH	34.19	25953088
892	Acetylation	QDTVIKAKYAEVAKH HHHHHHHHHHHHHHH	39.74	25953088
909	2-Hydroxyisobutyrylation	QNNDSQLKIKELDHN HCCCCHHHHHHHHHC	44.06	-
911	Ubiquitination	NDSQLKIKELDHNIS CCCHHHHHHHHHCHH	51.11	-
918	Phosphorylation	KELDHNISKHKREAE HHHHHCHHHHHHHHH	33.74	28348404
930	Acetylation	EAEDGAAKVSKMLKD HHHHHHHHHHHHHHC	46.65	25953088
932	Phosphorylation	EDGAAKVSKMLKDYD HHHHHHHHHHHHCCC	16.19	21406692
936	Ubiquitination	AKVSKMLKDYDWINA HHHHHHHHCCCCHHC	51.23	-
938	Phosphorylation	VSKMLKDYDWINAER HHHHHHCCCCHHCHH	16.16	21406692
958	Acetylation	PNSAYDFKTNNPKEA CCCCCCCCCCCHHHH	47.66	25953088
958	Ubiquitination	PNSAYDFKTNNPKEA CCCCCCCCCCCHHHH	47.66	-
963	Acetylation	DFKTNNPKEAGQRLQ CCCCCCHHHHHHHHH	63.42	23749302
971	Acetylation	EAGQRLQKLQEMKEK HHHHHHHHHHHHHHH	57.65	23749302
971	Ubiquitination	EAGQRLQKLQEMKEK HHHHHHHHHHHHHHH	57.65	-
976	2-Hydroxyisobutyrylation	LQKLQEMKEKLGRNV HHHHHHHHHHHCCCH	51.44	-
976	Acetylation	LQKLQEMKEKLGRNV HHHHHHHHHHHCCCH	51.44	25953088
988	Sulfoxidation	RNVNMRAMNVLTEAE CCHHHHHHHHHHHHH	2.22	21406390
992	Phosphorylation	MRAMNVLTEAEERYN HHHHHHHHHHHHHHH	28.94	-
1003	Acetylation	ERYNDLMKKKRIVEN HHHHHHHHHHHHHHC	63.54	25953088
1003	Ubiquitination	ERYNDLMKKKRIVEN HHHHHHHHHHHHHHC	63.54	-
1004	Ubiquitination	RYNDLMKKKRIVEND HHHHHHHHHHHHHCC	33.06	-
1014	Ubiquitination	IVENDKSKILTTIED HHHCCCHHCCCCHHH	47.69	-
1017	Phosphorylation	NDKSKILTTIEDLDQ CCCHHCCCCHHHHHH	29.24	20068231
1018	Phosphorylation	DKSKILTTIEDLDQK CCHHCCCCHHHHHHH	20.94	20068231
1025	2-Hydroxyisobutyrylation	TIEDLDQKKNQALNI CHHHHHHHHHHHHHH	54.05	-
1025	Acetylation	TIEDLDQKKNQALNI CHHHHHHHHHHHHHH	54.05	25953088
1025	Ubiquitination	TIEDLDQKKNQALNI CHHHHHHHHHHHHHH	54.05	21906983
1025 (in isoform 1)	Ubiquitination	-	54.05	21890473
1025 (in isoform 2)	Ubiquitination	-	54.05	21890473
1026	Ubiquitination	IEDLDQKKNQALNIA HHHHHHHHHHHHHHH	48.97	-
1036	Ubiquitination	ALNIAWQKVNKDFGS HHHHHHHHHCCCHHH	36.75	-
1039	Ubiquitination	IAWQKVNKDFGSIFS HHHHHHCCCHHHHHH	58.38	-
1077	Phosphorylation	FKVALGNTWKENLTE EEEECCCHHHHHHHH	35.79	22199227
1079	Ubiquitination	VALGNTWKENLTELS EECCCHHHHHHHHHC	34.39	-
1158	Acetylation	NNANVLFKTKFVDGV CCCCEEEEEEECCCC	46.79	19608861
1158	Malonylation	NNANVLFKTKFVDGV CCCCEEEEEEECCCC	46.79	32601280
1158	Methylation	NNANVLFKTKFVDGV CCCCEEEEEEECCCC	46.79	19608861
1158	Ubiquitination	NNANVLFKTKFVDGV CCCCEEEEEEECCCC	46.79	19608861
1159	Phosphorylation	NANVLFKTKFVDGVS CCCEEEEEEECCCCH	23.52	-
1160	Acetylation	ANVLFKTKFVDGVST CCEEEEEEECCCCHH	43.94	19608861
1160	Malonylation	ANVLFKTKFVDGVST CCEEEEEEECCCCHH	43.94	26320211
1160	Methylation	ANVLFKTKFVDGVST CCEEEEEEECCCCHH	43.94	22634479
1160	Ubiquitination	ANVLFKTKFVDGVST CCEEEEEEECCCCHH	43.94	21890473
1160 (in isoform 1)	Ubiquitination	-	43.94	21890473
1166	Phosphorylation	TKFVDGVSTVARFTQ EEECCCCHHHHHHHC	23.77	21406692
1167	Phosphorylation	KFVDGVSTVARFTQC EECCCCHHHHHHHCC	18.77	21406692
1172	O-linked_Glycosylation	VSTVARFTQCQNGKI CHHHHHHHCCCCCCC	23.92	30379171
1178	Acetylation	FTQCQNGKISKEAKS HHCCCCCCCCHHHHH	51.89	25953088
1178	Ubiquitination	FTQCQNGKISKEAKS HHCCCCCCCCHHHHH	51.89	-
1188	Ubiquitination	KEAKSKAKPPKGAHV HHHHHCCCCCCCCCC	66.64	-
1191	Ubiquitination	KSKAKPPKGAHVEV- HHCCCCCCCCCCCC-	76.80	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of SMC2_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of SMC2_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of SMC2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
SMC4_HUMAN	SMC4	physical	17113138
H2AZ_HUMAN	H2AFZ	physical	21633354
H32_HUMAN	HIST2H3C	physical	21633354
H2B2E_HUMAN	HIST2H2BE	physical	21633354
H2A2C_HUMAN	HIST2H2AC	physical	21633354
DNLI4_HUMAN	LIG4	physical	12589063
SMC4_HUMAN	SMC4	physical	17268547
CND1_HUMAN	NCAPD2	physical	17268547
CND3_HUMAN	NCAPG	physical	17268547
CND2_HUMAN	NCAPH	physical	17268547
CNDD3_HUMAN	NCAPD3	physical	17268547
CNDG2_HUMAN	NCAPG2	physical	17268547
CNDH2_HUMAN	NCAPH2	physical	17268547
CND3_HUMAN	NCAPG	physical	14532007
SMC4_HUMAN	SMC4	physical	14532007
CND1_HUMAN	NCAPD2	physical	14532007
CND2_HUMAN	NCAPH	physical	14532007
CNDG2_HUMAN	NCAPG2	physical	14532007
CNDH2_HUMAN	NCAPH2	physical	14532007
CNDD3_HUMAN	NCAPD3	physical	14532007
SMC4_HUMAN	SMC4	physical	22939629
CCAR2_HUMAN	CCAR2	physical	22863883
CND1_HUMAN	NCAPD2	physical	22863883
CND2_HUMAN	NCAPH	physical	22863883
PLEC_HUMAN	PLEC	physical	22863883
SMC4_HUMAN	SMC4	physical	22863883
DSRAD_HUMAN	ADAR	physical	26344197
ESR1_HUMAN	ESR1	physical	26166704
CND3_HUMAN	NCAPG	physical	26166704
SMC4_HUMAN	SMC4	physical	26166704
CND1_HUMAN	NCAPD2	physical	26166704
CND2_HUMAN	NCAPH	physical	26166704
CNDD3_HUMAN	NCAPD3	physical	26166704
CNDH2_HUMAN	NCAPH2	physical	26166704
CNDG2_HUMAN	NCAPG2	physical	26166704
HECD1_HUMAN	HECTD1	physical	26166704

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-222; LYS-677;LYS-1158 AND LYS-1160, AND MASS SPECTROMETRY.
PubMed: 19608861