dbPTM

MCM7_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM7_HUMAN
UniProt AC	P33993
Protein Name	DNA replication licensing factor MCM7
Gene Name	MCM7
Organism	Homo sapiens (Human).
Sequence Length	719
Subcellular Localization	Nucleus.
Protein Description	Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for S-phase checkpoint activation upon UV-induced damage..
Protein Sequence	MALKDYALEKEKVKKFLQEFYQDDELGKKQFKYGNQLVRLAHREQVALYVDLDDVAEDDPELVDSICENARRYAKLFADAVQELLPQYKEREVVNKDVLDVYIEHRLMMEQRSRDPGMVRSPQNQYPAELMRRFELYFQGPSSNKPRVIREVRADSVGKLVTVRGIVTRVSEVKPKMVVATYTCDQCGAETYQPIQSPTFMPLIMCPSQECQTNRSGGRLYLQTRGSRFIKFQEMKMQEHSDQVPVGNIPRSITVLVEGENTRIAQPGDHVSVTGIFLPILRTGFRQVVQGLLSETYLEAHRIVKMNKSEDDESGAGELTREELRQIAEEDFYEKLAASIAPEIYGHEDVKKALLLLLVGGVDQSPRGMKIRGNINICLMGDPGVAKSQLLSYIDRLAPRSQYTTGRGSSGVGLTAAVLRDSVSGELTLEGGALVLADQGVCCIDEFDKMAEADRTAIHEVMEQQTISIAKAGILTTLNARCSILAAANPAYGRYNPRRSLEQNIQLPAALLSRFDLLWLIQDRPDRDNDLRLAQHITYVHQHSRQPPSQFEPLDMKLMRRYIAMCREKQPMVPESLADYITAAYVEMRREAWASKDATYTSARTLLAILRLSTALARLRMVDVVEKEDVNEAIRLMEMSKDSLLGDKGQTARTQRPADVIFATVRELVSGGRSVRFSEAEQRCVSRGFTPAQFQAALDEYEELNVWQVNASRTRITFV

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MALKDYALE ------CCHHHHHHH	24.26	22223895
4	Sumoylation	----MALKDYALEKE ----CCHHHHHHHHH	38.87	-
4	2-Hydroxyisobutyrylation	----MALKDYALEKE ----CCHHHHHHHHH	38.87	-
4	Acetylation	----MALKDYALEKE ----CCHHHHHHHHH	38.87	25953088
4	Succinylation	----MALKDYALEKE ----CCHHHHHHHHH	38.87	23954790
4	Sumoylation	----MALKDYALEKE ----CCHHHHHHHHH	38.87	-
4	Ubiquitination	----MALKDYALEKE ----CCHHHHHHHHH	38.87	-
6	Phosphorylation	--MALKDYALEKEKV --CCHHHHHHHHHHH	16.11	20068231
10	Sumoylation	LKDYALEKEKVKKFL HHHHHHHHHHHHHHH	64.78	-
10	Succinylation	LKDYALEKEKVKKFL HHHHHHHHHHHHHHH	64.78	23954790
10	Sumoylation	LKDYALEKEKVKKFL HHHHHHHHHHHHHHH	64.78	-
10	Ubiquitination	LKDYALEKEKVKKFL HHHHHHHHHHHHHHH	64.78	-
10 (in isoform 1)	Ubiquitination	-	64.78	21890473
10 (in isoform 2)	Ubiquitination	-	64.78	21890473
12	Ubiquitination	DYALEKEKVKKFLQE HHHHHHHHHHHHHHH	71.12	-
15	Ubiquitination	LEKEKVKKFLQEFYQ HHHHHHHHHHHHHHC	55.05	21890473
15	Sumoylation	LEKEKVKKFLQEFYQ HHHHHHHHHHHHHHC	55.05	-
15	Sumoylation	LEKEKVKKFLQEFYQ HHHHHHHHHHHHHHC	55.05	28112733
15	Ubiquitination	LEKEKVKKFLQEFYQ HHHHHHHHHHHHHHC	55.05	21890473
15 (in isoform 1)	Ubiquitination	-	55.05	21890473
15 (in isoform 2)	Ubiquitination	-	55.05	21890473
21	Nitration	KKFLQEFYQDDELGK HHHHHHHHCCCHHHH	15.41	-
21	Phosphorylation	KKFLQEFYQDDELGK HHHHHHHHCCCHHHH	15.41	28152594
28	Acetylation	YQDDELGKKQFKYGN HCCCHHHHHHHHHHH	56.90	23954790
28	Sumoylation	YQDDELGKKQFKYGN HCCCHHHHHHHHHHH	56.90	28112733
28	Ubiquitination	YQDDELGKKQFKYGN HCCCHHHHHHHHHHH	56.90	21890473
28 (in isoform 1)	Ubiquitination	-	56.90	21890473
28 (in isoform 2)	Ubiquitination	-	56.90	21890473
29	Ubiquitination	QDDELGKKQFKYGNQ CCCHHHHHHHHHHHH	60.20	21890473
29	Acetylation	QDDELGKKQFKYGNQ CCCHHHHHHHHHHHH	60.20	30590355
29	Ubiquitination	QDDELGKKQFKYGNQ CCCHHHHHHHHHHHH	60.20	22053931
29 (in isoform 1)	Ubiquitination	-	60.20	21890473
29 (in isoform 2)	Ubiquitination	-	60.20	21890473
32	Sumoylation	ELGKKQFKYGNQLVR HHHHHHHHHHHHHHH	50.16	-
32	Sumoylation	ELGKKQFKYGNQLVR HHHHHHHHHHHHHHH	50.16	-
32	Ubiquitination	ELGKKQFKYGNQLVR HHHHHHHHHHHHHHH	50.16	-
33	Phosphorylation	LGKKQFKYGNQLVRL HHHHHHHHHHHHHHH	23.69	28152594
55	Ubiquitination	LYVDLDDVAEDDPEL EEEEHHHHHCCCHHH	6.66	21890473
75	Ubiquitination	ENARRYAKLFADAVQ HHHHHHHHHHHHHHH	34.89	21890473
75	Ubiquitination	ENARRYAKLFADAVQ HHHHHHHHHHHHHHH	34.89	21890473
75 (in isoform 1)	Ubiquitination	-	34.89	21890473
75 (in isoform 2)	Ubiquitination	-	34.89	21890473
89	Ubiquitination	QELLPQYKEREVVNK HHHHHHHHHHHCCCH	45.08	890473
89 (in isoform 1)	Ubiquitination	-	45.08	21890473
89 (in isoform 2)	Ubiquitination	-	45.08	21890473
96	2-Hydroxyisobutyrylation	KEREVVNKDVLDVYI HHHHCCCHHHHHHHH	37.29	-
96	Acetylation	KEREVVNKDVLDVYI HHHHCCCHHHHHHHH	37.29	26822725
96	Ubiquitination	KEREVVNKDVLDVYI HHHHCCCHHHHHHHH	37.29	-
102	Phosphorylation	NKDVLDVYIEHRLMM CHHHHHHHHHHHHHH	10.56	27642862
113	Phosphorylation	RLMMEQRSRDPGMVR HHHHHHHCCCCCCCC	40.50	20068231
121	Phosphorylation	RDPGMVRSPQNQYPA CCCCCCCCCCCCCCH	21.30	22167270
126	Phosphorylation	VRSPQNQYPAELMRR CCCCCCCCCHHHHHH	16.38	28450419
137	Phosphorylation	LMRRFELYFQGPSSN HHHHHEEEECCCCCC	6.15	28152594
145	Ubiquitination	FQGPSSNKPRVIREV ECCCCCCCCCEEEEE	35.83	21890473
145	Ubiquitination	FQGPSSNKPRVIREV ECCCCCCCCCEEEEE	35.83	22053931
145 (in isoform 1)	Ubiquitination	-	35.83	21890473
145 (in isoform 2)	Ubiquitination	-	35.83	21890473
156	Phosphorylation	IREVRADSVGKLVTV EEEEECCCCCCEEEE	31.61	23401153
159	Sumoylation	VRADSVGKLVTVRGI EECCCCCCEEEEEEE	37.31	-
159	2-Hydroxyisobutyrylation	VRADSVGKLVTVRGI EECCCCCCEEEEEEE	37.31	-
159	Acetylation	VRADSVGKLVTVRGI EECCCCCCEEEEEEE	37.31	25953088
159	Sumoylation	VRADSVGKLVTVRGI EECCCCCCEEEEEEE	37.31	-
159	Ubiquitination	VRADSVGKLVTVRGI EECCCCCCEEEEEEE	37.31	21906983
159 (in isoform 1)	Ubiquitination	-	37.31	21890473
159 (in isoform 2)	Ubiquitination	-	37.31	21890473
168	Phosphorylation	VTVRGIVTRVSEVKP EEEEEEEEEHHHCCC	24.35	-
174	Sumoylation	VTRVSEVKPKMVVAT EEEHHHCCCCEEEEE	34.56	-
174	Sumoylation	VTRVSEVKPKMVVAT EEEHHHCCCCEEEEE	34.56	-
174	Ubiquitination	VTRVSEVKPKMVVAT EEEHHHCCCCEEEEE	34.56	-
219	Methylation	QTNRSGGRLYLQTRG CCCCCCCEEEEEECC	24.55	115483003
225	Methylation	GRLYLQTRGSRFIKF CEEEEEECCCCCEEH	28.29	115482987
231	Ubiquitination	TRGSRFIKFQEMKMQ ECCCCCEEHHHHHCH	37.98	21890473
231	Sumoylation	TRGSRFIKFQEMKMQ ECCCCCEEHHHHHCH	37.98	-
231	Sumoylation	TRGSRFIKFQEMKMQ ECCCCCEEHHHHHCH	37.98	-
231	Ubiquitination	TRGSRFIKFQEMKMQ ECCCCCEEHHHHHCH	37.98	21890473
231 (in isoform 1)	Ubiquitination	-	37.98	21890473
231 (in isoform 2)	Ubiquitination	-	37.98	21890473
236	Sumoylation	FIKFQEMKMQEHSDQ CEEHHHHHCHHCCCC	36.36	-
236	Acetylation	FIKFQEMKMQEHSDQ CEEHHHHHCHHCCCC	36.36	25953088
236	Sumoylation	FIKFQEMKMQEHSDQ CEEHHHHHCHHCCCC	36.36	-
236	Ubiquitination	FIKFQEMKMQEHSDQ CEEHHHHHCHHCCCC	36.36	21906983
236 (in isoform 1)	Ubiquitination	-	36.36	21890473
236 (in isoform 2)	Ubiquitination	-	36.36	21890473
237	Sulfoxidation	IKFQEMKMQEHSDQV EEHHHHHCHHCCCCC	5.65	28183972
272	Phosphorylation	AQPGDHVSVTGIFLP CCCCCEEEEEEEHHH	15.56	28450419
274	Phosphorylation	PGDHVSVTGIFLPIL CCCEEEEEEEHHHHH	19.63	28450419
294	Phosphorylation	QVVQGLLSETYLEAH HHHHHHHCHHHHHHH	32.70	28152594
296	Phosphorylation	VQGLLSETYLEAHRI HHHHHCHHHHHHHHH	29.99	28152594
297	Phosphorylation	QGLLSETYLEAHRIV HHHHCHHHHHHHHHE	9.86	28152594
305	Ubiquitination	LEAHRIVKMNKSEDD HHHHHHEECCCCCCC	34.09	21906983
305 (in isoform 1)	Ubiquitination	-	34.09	21890473
305 (in isoform 2)	Ubiquitination	-	34.09	21890473
306	Sulfoxidation	EAHRIVKMNKSEDDE HHHHHEECCCCCCCC	5.45	21406390
308	Sumoylation	HRIVKMNKSEDDESG HHHEECCCCCCCCCC	52.29	-
308	Acetylation	HRIVKMNKSEDDESG HHHEECCCCCCCCCC	52.29	26822725
308	Sumoylation	HRIVKMNKSEDDESG HHHEECCCCCCCCCC	52.29	-
308	Ubiquitination	HRIVKMNKSEDDESG HHHEECCCCCCCCCC	52.29	21906983
308 (in isoform 1)	Ubiquitination	-	52.29	21890473
308 (in isoform 2)	Ubiquitination	-	52.29	21890473
309	Phosphorylation	RIVKMNKSEDDESGA HHEECCCCCCCCCCC	41.05	20873877
314	Phosphorylation	NKSEDDESGAGELTR CCCCCCCCCCCCCCH	40.72	23401153
320	Phosphorylation	ESGAGELTREELRQI CCCCCCCCHHHHHHH	31.56	25159151
321	Methylation	SGAGELTREELRQIA CCCCCCCHHHHHHHH	48.28	29151839
325	Methylation	ELTREELRQIAEEDF CCCHHHHHHHHHHHH	29.19	115482955
333	Phosphorylation	QIAEEDFYEKLAASI HHHHHHHHHHHHHHH	25.19	29978859
335	Ubiquitination	AEEDFYEKLAASIAP HHHHHHHHHHHHHCH	31.85	21906983
335 (in isoform 1)	Ubiquitination	-	31.85	21890473
351	Acetylation	IYGHEDVKKALLLLL HHCCHHHHHHHHHHH	44.65	25953088
351	Succinylation	IYGHEDVKKALLLLL HHCCHHHHHHHHHHH	44.65	23954790
351	Sumoylation	IYGHEDVKKALLLLL HHCCHHHHHHHHHHH	44.65	-
351	Ubiquitination	IYGHEDVKKALLLLL HHCCHHHHHHHHHHH	44.65	-
351 (in isoform 1)	Ubiquitination	-	44.65	21890473
352	Ubiquitination	YGHEDVKKALLLLLV HCCHHHHHHHHHHHH	44.08	-
365	Phosphorylation	LVGGVDQSPRGMKIR HHCCCCCCCCCCEEC	16.46	19647517
378	Glutathionylation	IRGNINICLMGDPGV ECCCEEEEECCCCCC	1.53	22555962
381	Ubiquitination	NINICLMGDPGVAKS CEEEEECCCCCCCHH	25.64	21890473
387	Ubiquitination	MGDPGVAKSQLLSYI CCCCCCCHHHHHHHH	36.01	22053931
387 (in isoform 1)	Ubiquitination	-	36.01	21890473
388	Phosphorylation	GDPGVAKSQLLSYID CCCCCCHHHHHHHHH	19.14	21712546
392	Phosphorylation	VAKSQLLSYIDRLAP CCHHHHHHHHHHHCC	28.74	28152594
393	Phosphorylation	AKSQLLSYIDRLAPR CHHHHHHHHHHHCCH	13.55	28152594
396	Methylation	QLLSYIDRLAPRSQY HHHHHHHHHCCHHHC	24.16	115483011
407	Methylation	RSQYTTGRGSSGVGL HHHCCCCCCCCCCCC	39.46	115483019
409	Phosphorylation	QYTTGRGSSGVGLTA HCCCCCCCCCCCCCE	23.66	21406692
410	Phosphorylation	YTTGRGSSGVGLTAA CCCCCCCCCCCCCEE	40.08	21406692
415	Phosphorylation	GSSGVGLTAAVLRDS CCCCCCCCEEHHHCC	13.47	21406692
420	Ubiquitination	GLTAAVLRDSVSGEL CCCEEHHHCCCCCEE	27.79	21890473
449	"N6,N6-dimethyllysine"	CCIDEFDKMAEADRT EEEHHHHHHHHHHHH	45.38	-
449	Methylation	CCIDEFDKMAEADRT EEEHHHHHHHHHHHH	45.38	23583077
462	Sulfoxidation	RTAIHEVMEQQTISI HHHHHHHHHHHCHHH	3.33	28183972
471	Ubiquitination	QQTISIAKAGILTTL HHCHHHHHHCHHHHH	45.54	22053931
471 (in isoform 1)	Ubiquitination	-	45.54	21890473
472	Ubiquitination	QTISIAKAGILTTLN HCHHHHHHCHHHHHH	10.96	21890473
482	Glutathionylation	LTTLNARCSILAAAN HHHHHHHHHHHHHHC	2.49	22555962
482	S-nitrosylation	LTTLNARCSILAAAN HHHHHHHHHHHHHHC	2.49	24105792
483	Phosphorylation	TTLNARCSILAAANP HHHHHHHHHHHHHCC	18.32	27080861
492	Phosphorylation	LAAANPAYGRYNPRR HHHHCCCCCCCCCCC	11.91	28152594
500	Phosphorylation	GRYNPRRSLEQNIQL CCCCCCCCHHHHCCC	37.22	26055452
524	Methylation	LLWLIQDRPDRDNDL EEHHHCCCCCCCCHH	20.74	115482979
527	Methylation	LIQDRPDRDNDLRLA HHCCCCCCCCHHHHH	47.52	115482971
532	Methylation	PDRDNDLRLAQHITY CCCCCHHHHHHHHHH	30.73	115482947
538	Phosphorylation	LRLAQHITYVHQHSR HHHHHHHHHHHHCCC	19.84	28152594
539	Phosphorylation	RLAQHITYVHQHSRQ HHHHHHHHHHHCCCC	8.71	28152594
544	Phosphorylation	ITYVHQHSRQPPSQF HHHHHHCCCCCCHHC	26.49	28152594
549	Phosphorylation	QHSRQPPSQFEPLDM HCCCCCCHHCCCCCH	54.94	17525332
556	Sulfoxidation	SQFEPLDMKLMRRYI HHCCCCCHHHHHHHH	4.77	21406390
557	Ubiquitination	QFEPLDMKLMRRYIA HCCCCCHHHHHHHHH	38.51	21890473
557	Ubiquitination	QFEPLDMKLMRRYIA HCCCCCHHHHHHHHH	38.51	21890473
557 (in isoform 1)	Ubiquitination	-	38.51	21890473
569	Ubiquitination	YIAMCREKQPMVPES HHHHHHHCCCCCCHH	40.11	21906983
569 (in isoform 1)	Ubiquitination	-	40.11	21890473
576	Phosphorylation	KQPMVPESLADYITA CCCCCCHHHHHHHHH	23.84	20068231
580	Phosphorylation	VPESLADYITAAYVE CCHHHHHHHHHHHHH	8.45	20068231
582	Phosphorylation	ESLADYITAAYVEMR HHHHHHHHHHHHHHH	10.06	20068231
585	Phosphorylation	ADYITAAYVEMRREA HHHHHHHHHHHHHHH	8.42	20068231
596	Ubiquitination	RREAWASKDATYTSA HHHHHHCCCCCHHHH	43.57	21890473
596	2-Hydroxyisobutyrylation	RREAWASKDATYTSA HHHHHHCCCCCHHHH	43.57	-
596	Acetylation	RREAWASKDATYTSA HHHHHHCCCCCHHHH	43.57	26051181
596	Ubiquitination	RREAWASKDATYTSA HHHHHHCCCCCHHHH	43.57	21890473
596 (in isoform 1)	Ubiquitination	-	43.57	21890473
599	Phosphorylation	AWASKDATYTSARTL HHHCCCCCHHHHHHH	37.15	-
600	Phosphorylation	WASKDATYTSARTLL HHCCCCCHHHHHHHH	10.62	25884760
601	Phosphorylation	ASKDATYTSARTLLA HCCCCCHHHHHHHHH	16.14	28152594
605	Phosphorylation	ATYTSARTLLAILRL CCHHHHHHHHHHHHH	26.32	-
613	Phosphorylation	LLAILRLSTALARLR HHHHHHHHHHHHHCC	12.75	25367160
614	Phosphorylation	LAILRLSTALARLRM HHHHHHHHHHHHCCC	30.22	25367160
621	Sulfoxidation	TALARLRMVDVVEKE HHHHHCCCCCEECHH	3.41	21406390
627	2-Hydroxyisobutyrylation	RMVDVVEKEDVNEAI CCCCEECHHCHHHHH	47.83	-
627	Acetylation	RMVDVVEKEDVNEAI CCCCEECHHCHHHHH	47.83	26051181
627	Ubiquitination	RMVDVVEKEDVNEAI CCCCEECHHCHHHHH	47.83	21906983
627 (in isoform 1)	Ubiquitination	-	47.83	21890473
640	Phosphorylation	AIRLMEMSKDSLLGD HHHHHHHCHHHHCCC	21.72	26657352
641	2-Hydroxyisobutyrylation	IRLMEMSKDSLLGDK HHHHHHCHHHHCCCC	50.45	-
641	Ubiquitination	IRLMEMSKDSLLGDK HHHHHHCHHHHCCCC	50.45	21906983
641 (in isoform 1)	Ubiquitination	-	50.45	21890473
643	Phosphorylation	LMEMSKDSLLGDKGQ HHHHCHHHHCCCCCC	29.27	26657352
648	Ubiquitination	KDSLLGDKGQTARTQ HHHHCCCCCCCCCCC	51.63	21890473
648	Acetylation	KDSLLGDKGQTARTQ HHHHCCCCCCCCCCC	51.63	25953088
648	Ubiquitination	KDSLLGDKGQTARTQ HHHHCCCCCCCCCCC	51.63	22053931
648 (in isoform 1)	Ubiquitination	-	51.63	21890473
670	Phosphorylation	ATVRELVSGGRSVRF EEHHHHHHCCCCCCC	48.42	24719451
673	Methylation	RELVSGGRSVRFSEA HHHHHCCCCCCCCHH	35.19	115482963
674	Phosphorylation	ELVSGGRSVRFSEAE HHHHCCCCCCCCHHH	22.40	23312004
678	Phosphorylation	GGRSVRFSEAEQRCV CCCCCCCCHHHHHHH	25.90	23911959

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
121	S	Phosphorylation	Kinase	CDK1	P06493	PSP
121	S	Phosphorylation	Kinase	CDK2	P24941	PSP
365	S	Phosphorylation	Kinase	CDK1	P06493	PSP
365	S	Phosphorylation	Kinase	CDK2	P24941	PSP
600	Y	Phosphorylation	Kinase	LYN	P07948	PSP
-	K	Ubiquitination	E3 ubiquitin ligase	UBE3A	Q05086	PMID:9852095

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCM7_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 MCM7_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ORC1_HUMAN	ORC1	physical	12614612
RB_HUMAN	RB1	physical	9566894
DBF4A_HUMAN	DBF4	physical	12614612
CDC7_HUMAN	CDC7	physical	12614612
ORC3_HUMAN	ORC3	physical	12614612
RFA1_HUMAN	RPA1	physical	12614612
FHL2_HUMAN	FHL2	physical	10649446
ORC2_HUMAN	ORC2	physical	12614612
ORC5_HUMAN	ORC5	physical	12614612
RBM8A_HUMAN	RBM8A	physical	16189514
MBIP1_HUMAN	MBIP	physical	16189514
MCM7_HUMAN	MCM7	physical	12614612
ATR_HUMAN	ATR	physical	15210935
MCM8_HUMAN	MCM8	physical	12771218
MCM2_HUMAN	MCM2	physical	12694531
MCM7_HUMAN	MCM7	physical	12694531
MCM2_HUMAN	MCM2	physical	12614612
MCM3_HUMAN	MCM3	physical	12614612
MCM6_HUMAN	MCM6	physical	12614612
CDC6_HUMAN	CDC6	physical	12614612
CDC45_HUMAN	CDC45	physical	12614612
CDC45_HUMAN	CDC45	physical	10518787
CDC6_HUMAN	CDC6	physical	10464337
MCM3_HUMAN	MCM3	physical	10464337
UBE3A_HUMAN	UBE3A	physical	9852095
MCM4_HUMAN	MCM4	physical	9099751
MCM5_HUMAN	MCM5	physical	9099751
MCM6_HUMAN	MCM6	physical	9099751
MCM3_HUMAN	MCM3	physical	9099751
MCM2_HUMAN	MCM2	physical	9099751
MCM4_HUMAN	MCM4	physical	12207017
MCM2_HUMAN	MCM2	physical	12207017
CDC45_HUMAN	CDC45	physical	16912045
RB_HUMAN	RB1	physical	16912045
CCL2_HUMAN	CCL2	physical	21383955
HIF1A_HUMAN	HIF1A	physical	21658608
EPAS1_HUMAN	EPAS1	physical	21658608
RB_HUMAN	RB1	physical	12519773
INT6_HUMAN	INTS6	physical	17310990
A4_HUMAN	APP	physical	21832049
SMC1A_HUMAN	SMC1A	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
RBBP4_HUMAN	RBBP4	physical	22939629
RU2A_HUMAN	SNRPA1	physical	22939629
ORC4_HUMAN	ORC4	physical	15232106
MCM10_HUMAN	MCM10	physical	15232106
MCM2_HUMAN	MCM2	physical	15232106
ORC6_HUMAN	ORC6	physical	15232106
MCM4_HUMAN	MCM4	physical	15232106
SMC1A_HUMAN	SMC1A	physical	16438930
HS90B_HUMAN	HSP90AB1	physical	22863883
HYOU1_HUMAN	HYOU1	physical	22863883
CLU_HUMAN	CLUH	physical	22863883
MCM2_HUMAN	MCM2	physical	22863883
MCM4_HUMAN	MCM4	physical	22863883
ANM1_HUMAN	PRMT1	physical	22863883
TOM34_HUMAN	TOMM34	physical	22863883
NAB2_HUMAN	NAB2	physical	25416956
TRI27_HUMAN	TRIM27	physical	25416956
SP2_HUMAN	SP2	physical	25416956
PNMA1_HUMAN	PNMA1	physical	25416956
UBQL1_HUMAN	UBQLN1	physical	25416956
MBIP1_HUMAN	MBIP	physical	25416956
TRI54_HUMAN	TRIM54	physical	25416956
C102B_HUMAN	CCDC102B	physical	25416956
MCMBP_HUMAN	MCMBP	physical	25416956
USBP1_HUMAN	USHBP1	physical	25416956
CH034_HUMAN	C8orf34	physical	25416956
MIPO1_HUMAN	MIPOL1	physical	25416956
KAD8_HUMAN	AK8	physical	25416956
VPS29_HUMAN	VPS29	physical	26186194
VPS35_HUMAN	VPS35	physical	26186194
MCM2_HUMAN	MCM2	physical	26186194
TIM_HUMAN	TIMELESS	physical	26186194
DAPLE_HUMAN	CCDC88C	physical	26186194
VP26A_HUMAN	VPS26A	physical	26186194
HDAC6_HUMAN	HDAC6	physical	26186194
CE290_HUMAN	CEP290	physical	26186194
PSF2_HUMAN	GINS2	physical	26186194
SLD5_HUMAN	GINS4	physical	26186194
TCPD_HUMAN	CCT4	physical	26344197
MARE2_HUMAN	MAPRE2	physical	26344197
MCMBP_HUMAN	MCMBP	physical	26344197
PSMD2_HUMAN	PSMD2	physical	26344197
SF3B1_HUMAN	SF3B1	physical	26344197
KCTD5_HUMAN	KCTD5	physical	26188516
CUL3_HUMAN	CUL3	physical	26188516
DAPLE_HUMAN	CCDC88C	physical	28514442
VP26A_HUMAN	VPS26A	physical	28514442
TIM_HUMAN	TIMELESS	physical	28514442
PSF2_HUMAN	GINS2	physical	28514442
VPS35_HUMAN	VPS35	physical	28514442
HDAC6_HUMAN	HDAC6	physical	28514442
CE290_HUMAN	CEP290	physical	28514442
SLD5_HUMAN	GINS4	physical	28514442
VPS29_HUMAN	VPS29	physical	28514442
PSF1_HUMAN	GINS1	physical	28514442
UBP15_HUMAN	USP15	physical	27173435
MCM2_HUMAN	MCM2	physical	27173435
MCM4_HUMAN	MCM4	physical	27173435
MCM6_HUMAN	MCM6	physical	27173435
FANCA_HUMAN	FANCA	physical	28215707
CEP68_HUMAN	CEP68	physical	28578000
GRWD1_HUMAN	GRWD1	physical	25990725
CDT1_HUMAN	CDT1	physical	25990725
CDC6_HUMAN	CDC6	physical	25990725

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 MCM7_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-121 AND SER-500, ANDMASS SPECTROMETRY.	19690332 [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-121 AND SER-500, ANDMASS 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-121 AND SER-500, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-549, AND MASSSPECTROMETRY.	17525332 [Abstract]