dbPTM

MCM4_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM4_HUMAN
UniProt AC	P33991
Protein Name	DNA replication licensing factor MCM4
Gene Name	MCM4
Organism	Homo sapiens (Human).
Sequence Length	863
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..
Protein Sequence	MSSPASTPSRRGSRRGRATPAQTPRSEDARSSPSQRRRGEDSTSTGELQPMPTSPGVDLQSPAAQDVLFSSPPQMHSSAIPLDFDVSSPLTYGTPSSRVEGTPRSGVRGTPVRQRPDLGSAQKGLQVDLQSDGAAAEDIVASEQSLGQKLVIWGTDVNVAACKENFQRFLQRFIDPLAKEEENVGIDITEPLYMQRLGEINVIGEPFLNVNCEHIKSFDKNLYRQLISYPQEVIPTFDMAVNEIFFDRYPDSILEHQIQVRPFNALKTKNMRNLNPEDIDQLITISGMVIRTSQLIPEMQEAFFQCQVCAHTTRVEMDRGRIAEPSVCGRCHTTHSMALIHNRSLFSDKQMIKLQESPEDMPAGQTPHTVILFAHNDLVDKVQPGDRVNVTGIYRAVPIRVNPRVSNVKSVYKTHIDVIHYRKTDAKRLHGLDEEAEQKLFSEKRVELLKELSRKPDIYERLASALAPSIYEHEDIKKGILLQLFGGTRKDFSHTGRGKFRAEINILLCGDPGTSKSQLLQYVYNLVPRGQYTSGKGSSAVGLTAYVMKDPETRQLVLQTGALVLSDNGICCIDEFDKMNESTRSVLHEVMEQQTLSIAKAGIICQLNARTSVLAAANPIESQWNPKKTTIENIQLPHTLLSRFDLIFLLLDPQDEAYDRRLAHHLVALYYQSEEQAEEELLDMAVLKDYIAYAHSTIMPRLSEEASQALIEAYVDMRKIGSSRGMVSAYPRQLESLIRLAEAHAKVRLSNKVEAIDVEEAKRLHREALKQSATDPRTGIVDISILTTGMSATSRKRKEELAEALKKLILSKGKTPALKYQQLFEDIRGQSDIAITKDMFEEALRALADDDFLTVTGKTVRLL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSSPASTPS ------CCCCCCCCC	45.06	21406692
2	Phosphorylation	------MSSPASTPS ------CCCCCCCCC	45.06	23401153
3	Phosphorylation	-----MSSPASTPSR -----CCCCCCCCCC	24.16	23401153
6	Phosphorylation	--MSSPASTPSRRGS --CCCCCCCCCCCCC	44.21	29255136
7	Phosphorylation	-MSSPASTPSRRGSR -CCCCCCCCCCCCCC	27.65	29255136
9	Phosphorylation	SSPASTPSRRGSRRG CCCCCCCCCCCCCCC	34.40	29255136
10	Dimethylation	SPASTPSRRGSRRGR CCCCCCCCCCCCCCC	48.46	-
10	Methylation	SPASTPSRRGSRRGR CCCCCCCCCCCCCCC	48.46	115385265
11	Methylation	PASTPSRRGSRRGRA CCCCCCCCCCCCCCC	52.34	115385273
13	Phosphorylation	STPSRRGSRRGRATP CCCCCCCCCCCCCCC	19.59	21406692
14	Dimethylation	TPSRRGSRRGRATPA CCCCCCCCCCCCCCC	48.15	-
14	Methylation	TPSRRGSRRGRATPA CCCCCCCCCCCCCCC	48.15	115385281
15	Methylation	PSRRGSRRGRATPAQ CCCCCCCCCCCCCCC	40.42	115385289
17	Methylation	RRGSRRGRATPAQTP CCCCCCCCCCCCCCC	33.21	115385297
19	O-linked_Glycosylation	GSRRGRATPAQTPRS CCCCCCCCCCCCCCC	20.14	28510447
19	Phosphorylation	GSRRGRATPAQTPRS CCCCCCCCCCCCCCC	20.14	25159151
23	Phosphorylation	GRATPAQTPRSEDAR CCCCCCCCCCCCCCC	23.83	25159151
26	Phosphorylation	TPAQTPRSEDARSSP CCCCCCCCCCCCCCH	40.82	25159151
31	Phosphorylation	PRSEDARSSPSQRRR CCCCCCCCCHHHHHC	48.61	25159151
32	Phosphorylation	RSEDARSSPSQRRRG CCCCCCCCHHHHHCC	24.02	25159151
34	Phosphorylation	EDARSSPSQRRRGED CCCCCCHHHHHCCCC	37.96	22115753
42	Phosphorylation	QRRRGEDSTSTGELQ HHHCCCCCCCCCCCC	21.69	26074081
43	Phosphorylation	RRRGEDSTSTGELQP HHCCCCCCCCCCCCC	42.50	26074081
44	Phosphorylation	RRGEDSTSTGELQPM HCCCCCCCCCCCCCC	38.06	26074081
45	Phosphorylation	RGEDSTSTGELQPMP CCCCCCCCCCCCCCC	34.46	26074081
53	Phosphorylation	GELQPMPTSPGVDLQ CCCCCCCCCCCCCCC	41.10	26657352
54	Phosphorylation	ELQPMPTSPGVDLQS CCCCCCCCCCCCCCC	17.49	19276368
61	Phosphorylation	SPGVDLQSPAAQDVL CCCCCCCCHHHHHHH	24.65	30140170
70	Phosphorylation	AAQDVLFSSPPQMHS HHHHHHHCCCCCCCC	37.46	26074081
71	Phosphorylation	AQDVLFSSPPQMHSS HHHHHHCCCCCCCCC	33.01	28464451
77	Phosphorylation	SSPPQMHSSAIPLDF CCCCCCCCCCCCCCC	19.00	26074081
78	Phosphorylation	SPPQMHSSAIPLDFD CCCCCCCCCCCCCCC	18.62	28464451
87	Phosphorylation	IPLDFDVSSPLTYGT CCCCCCCCCCCCCCC	28.25	28464451
88	Phosphorylation	PLDFDVSSPLTYGTP CCCCCCCCCCCCCCC	24.63	26657352
91	Phosphorylation	FDVSSPLTYGTPSSR CCCCCCCCCCCCCHH	24.24	20068231
92	Phosphorylation	DVSSPLTYGTPSSRV CCCCCCCCCCCCHHC	27.04	26074081
94	Phosphorylation	SSPLTYGTPSSRVEG CCCCCCCCCCHHCCC	15.02	20068231
96	Phosphorylation	PLTYGTPSSRVEGTP CCCCCCCCHHCCCCC	30.52	26074081
97	Phosphorylation	LTYGTPSSRVEGTPR CCCCCCCHHCCCCCC	41.36	26074081
102	Phosphorylation	PSSRVEGTPRSGVRG CCHHCCCCCCCCCCC	11.30	21955146
105	Phosphorylation	RVEGTPRSGVRGTPV HCCCCCCCCCCCCCC	42.73	22167270
108	Methylation	GTPRSGVRGTPVRQR CCCCCCCCCCCCCCC	46.95	115482867
110	Phosphorylation	PRSGVRGTPVRQRPD CCCCCCCCCCCCCCC	14.19	22167270
120	Phosphorylation	RQRPDLGSAQKGLQV CCCCCCCCCCCCEEE	34.52	22167270
123	Acetylation	PDLGSAQKGLQVDLQ CCCCCCCCCEEEEEC	62.39	25953088
123	Ubiquitination	PDLGSAQKGLQVDLQ CCCCCCCCCEEEEEC	62.39	-
131	Phosphorylation	GLQVDLQSDGAAAED CEEEEECCCCCCHHH	45.36	25159151
142	Phosphorylation	AAEDIVASEQSLGQK CHHHHHHCCCHHCCC	25.85	30266825
145	Phosphorylation	DIVASEQSLGQKLVI HHHHCCCHHCCCEEE	30.34	30266825
163	Ubiquitination	DVNVAACKENFQRFL CCCHHHHHHHHHHHH	51.47	-
179	Ubiquitination	RFIDPLAKEEENVGI HHHHHHHHHHHCCCC	73.64	21906983
189	Phosphorylation	ENVGIDITEPLYMQR HCCCCCCCCCCHHHC	28.00	20068231
193	Phosphorylation	IDITEPLYMQRLGEI CCCCCCCHHHCCCCC	11.25	20068231
212	Glutathionylation	EPFLNVNCEHIKSFD CCCCCCCCHHHHHCC	3.33	22555962
216	Acetylation	NVNCEHIKSFDKNLY CCCCHHHHHCCHHHH	47.15	25953088
216	Methylation	NVNCEHIKSFDKNLY CCCCHHHHHCCHHHH	47.15	23583077
216	Ubiquitination	NVNCEHIKSFDKNLY CCCCHHHHHCCHHHH	47.15	21890473
217	Phosphorylation	VNCEHIKSFDKNLYR CCCHHHHHCCHHHHH	37.77	24719451
220	Acetylation	EHIKSFDKNLYRQLI HHHHHCCHHHHHHHH	47.01	19608861
220	Ubiquitination	EHIKSFDKNLYRQLI HHHHHCCHHHHHHHH	47.01	21906983
223	Phosphorylation	KSFDKNLYRQLISYP HHCCHHHHHHHHHCC	13.00	24719451
236	Phosphorylation	YPQEVIPTFDMAVNE CCHHHCCCCHHHHHH	22.57	24275569
267	Ubiquitination	VRPFNALKTKNMRNL CCCCCCCCCCCCCCC	55.85	-
326	Phosphorylation	RGRIAEPSVCGRCHT CCCCCCCCCCCCCCC	22.88	19664994
344	Phosphorylation	MALIHNRSLFSDKQM HHHEECCCCCCCHHH	38.80	21815630
349	2-Hydroxyisobutyrylation	NRSLFSDKQMIKLQE CCCCCCCHHHEECCC	40.33	-
349	Acetylation	NRSLFSDKQMIKLQE CCCCCCCHHHEECCC	40.33	25953088
349	Ubiquitination	NRSLFSDKQMIKLQE CCCCCCCHHHEECCC	40.33	-
357	Phosphorylation	QMIKLQESPEDMPAG HHEECCCCCCCCCCC	22.19	25159151
381	Ubiquitination	AHNDLVDKVQPGDRV EECCHHHCCCCCCCE	34.98	-
387	Methylation	DKVQPGDRVNVTGIY HCCCCCCCEEECEEE	28.02	115482875
391	Phosphorylation	PGDRVNVTGIYRAVP CCCCEEECEEEEEEE	16.80	20068231
394	Phosphorylation	RVNVTGIYRAVPIRV CEEECEEEEEEEEEC	8.21	20068231
406	Phosphorylation	IRVNPRVSNVKSVYK EECCCCCCCCCHHEE	36.87	20068231
409	2-Hydroxyisobutyrylation	NPRVSNVKSVYKTHI CCCCCCCCHHEEEEE	38.15	-
409	Acetylation	NPRVSNVKSVYKTHI CCCCCCCCHHEEEEE	38.15	25953088
409	Succinylation	NPRVSNVKSVYKTHI CCCCCCCCHHEEEEE	38.15	23954790
409	Ubiquitination	NPRVSNVKSVYKTHI CCCCCCCCHHEEEEE	38.15	-
412	Phosphorylation	VSNVKSVYKTHIDVI CCCCCHHEEEEEEEE	19.77	29496907
413	Acetylation	SNVKSVYKTHIDVIH CCCCHHEEEEEEEEE	31.32	25953088
413	Methylation	SNVKSVYKTHIDVIH CCCCHHEEEEEEEEE	31.32	82980083
413	Ubiquitination	SNVKSVYKTHIDVIH CCCCHHEEEEEEEEE	31.32	-
414	Phosphorylation	NVKSVYKTHIDVIHY CCCHHEEEEEEEEEE	13.33	20068231
421	Phosphorylation	THIDVIHYRKTDAKR EEEEEEEEECCCHHH	11.59	29496907
427	Ubiquitination	HYRKTDAKRLHGLDE EEECCCHHHHCCCCH	59.30	-
439	Sumoylation	LDEEAEQKLFSEKRV CCHHHHHHHHHHHHH	42.90	-
439	2-Hydroxyisobutyrylation	LDEEAEQKLFSEKRV CCHHHHHHHHHHHHH	42.90	-
439	Acetylation	LDEEAEQKLFSEKRV CCHHHHHHHHHHHHH	42.90	25953088
439	Sumoylation	LDEEAEQKLFSEKRV CCHHHHHHHHHHHHH	42.90	28112733
439	Ubiquitination	LDEEAEQKLFSEKRV CCHHHHHHHHHHHHH	42.90	21906983
444	Ubiquitination	EQKLFSEKRVELLKE HHHHHHHHHHHHHHH	61.62	-
450	2-Hydroxyisobutyrylation	EKRVELLKELSRKPD HHHHHHHHHHCCCCC	70.05	-
450	Acetylation	EKRVELLKELSRKPD HHHHHHHHHHCCCCC	70.05	19608861
450	Ubiquitination	EKRVELLKELSRKPD HHHHHHHHHHCCCCC	70.05	21906983
453	Phosphorylation	VELLKELSRKPDIYE HHHHHHHCCCCCHHH	39.07	22496350
455	Ubiquitination	LLKELSRKPDIYERL HHHHHCCCCCHHHHH	43.60	21906983
459	Phosphorylation	LSRKPDIYERLASAL HCCCCCHHHHHHHHH	11.46	29496907
464	Phosphorylation	DIYERLASALAPSIY CHHHHHHHHHCCHHH	28.54	-
469	Phosphorylation	LASALAPSIYEHEDI HHHHHCCHHHCCCCH	31.99	28152594
471	Phosphorylation	SALAPSIYEHEDIKK HHHCCHHHCCCCHHH	18.64	28152594
477	Sumoylation	IYEHEDIKKGILLQL HHCCCCHHHCHHHHH	58.21	-
477	Acetylation	IYEHEDIKKGILLQL HHCCCCHHHCHHHHH	58.21	25953088
477	Sumoylation	IYEHEDIKKGILLQL HHCCCCHHHCHHHHH	58.21	-
477	Ubiquitination	IYEHEDIKKGILLQL HHCCCCHHHCHHHHH	58.21	21906983
478	Ubiquitination	YEHEDIKKGILLQLF HCCCCHHHCHHHHHH	52.06	-
488	Phosphorylation	LLQLFGGTRKDFSHT HHHHHCCCCCCCCCC	34.62	-
490	Ubiquitination	QLFGGTRKDFSHTGR HHHCCCCCCCCCCCC	64.06	-
522	Phosphorylation	SKSQLLQYVYNLVPR CHHHHHHHHHHHCCC	12.60	-
524	Phosphorylation	SQLLQYVYNLVPRGQ HHHHHHHHHHCCCCC	9.61	-
536	Acetylation	RGQYTSGKGSSAVGL CCCCCCCCCCCCEEE	56.22	26051181
536	Ubiquitination	RGQYTSGKGSSAVGL CCCCCCCCCCCCEEE	56.22	21906983
538	Phosphorylation	QYTSGKGSSAVGLTA CCCCCCCCCCEEEEE	20.71	22210691
539	Phosphorylation	YTSGKGSSAVGLTAY CCCCCCCCCEEEEEE	35.33	22210691
544	Phosphorylation	GSSAVGLTAYVMKDP CCCCEEEEEEEECCH	15.26	26270265
546	Phosphorylation	SAVGLTAYVMKDPET CCEEEEEEEECCHHH	8.88	22210691
548	Sulfoxidation	VGLTAYVMKDPETRQ EEEEEEEECCHHHHH	2.37	28183972
549	Ubiquitination	GLTAYVMKDPETRQL EEEEEEECCHHHHHH	61.15	-
553	Phosphorylation	YVMKDPETRQLVLQT EEECCHHHHHHHHHC	29.15	26270265
560	Phosphorylation	TRQLVLQTGALVLSD HHHHHHHCCCEEECC	21.91	22210691
578	Ubiquitination	CCIDEFDKMNESTRS EEECCHHHCCHHHHH	49.28	21906983
600	Ubiquitination	QQTLSIAKAGIICQL HHHHHHHHHCEEEEC	45.54	21906983
605	Glutathionylation	IAKAGIICQLNARTS HHHHCEEEECCCCCH	3.39	22555962
627	Acetylation	IESQWNPKKTTIENI CCCCCCCCCCCCCCC	60.58	25953088
627	Ubiquitination	IESQWNPKKTTIENI CCCCCCCCCCCCCCC	60.58	21906983
628	Ubiquitination	ESQWNPKKTTIENIQ CCCCCCCCCCCCCCC	52.75	21906983
703	Phosphorylation	STIMPRLSEEASQAL HCHHHHCCHHHHHHH	34.37	26552605
707	Phosphorylation	PRLSEEASQALIEAY HHCCHHHHHHHHHHH	21.18	26552605
714	Phosphorylation	SQALIEAYVDMRKIG HHHHHHHHHHHHHHC	5.56	26552605
722	Phosphorylation	VDMRKIGSSRGMVSA HHHHHHCCCCCHHHC	21.97	22210691
723	Phosphorylation	DMRKIGSSRGMVSAY HHHHHCCCCCHHHCC	27.86	22210691
724	Methylation	MRKIGSSRGMVSAYP HHHHCCCCCHHHCCH	38.63	115482859
726	Sulfoxidation	KIGSSRGMVSAYPRQ HHCCCCCHHHCCHHH	1.77	28183972
728	Phosphorylation	GSSRGMVSAYPRQLE CCCCCHHHCCHHHHH	17.13	22210691
730	Phosphorylation	SRGMVSAYPRQLESL CCCHHHCCHHHHHHH	7.46	22210691
736	Phosphorylation	AYPRQLESLIRLAEA CCHHHHHHHHHHHHH	37.37	20068231
746	Ubiquitination	RLAEAHAKVRLSNKV HHHHHHHHHCCCCCC	20.30	21906983
752	2-Hydroxyisobutyrylation	AKVRLSNKVEAIDVE HHHCCCCCCEEECHH	37.77	-
752	Acetylation	AKVRLSNKVEAIDVE HHHCCCCCCEEECHH	37.77	25953088
752	Sumoylation	AKVRLSNKVEAIDVE HHHCCCCCCEEECHH	37.77	-
752	Ubiquitination	AKVRLSNKVEAIDVE HHHCCCCCCEEECHH	37.77	21906983
762	Acetylation	AIDVEEAKRLHREAL EECHHHHHHHHHHHH	59.79	25953088
762	Ubiquitination	AIDVEEAKRLHREAL EECHHHHHHHHHHHH	59.79	21906983
770	Acetylation	RLHREALKQSATDPR HHHHHHHHHHCCCCC	49.61	25953088
770	Ubiquitination	RLHREALKQSATDPR HHHHHHHHHHCCCCC	49.61	21906983
784	Phosphorylation	RTGIVDISILTTGMS CCCEEEEEHHHCCCC	13.69	-
788	Phosphorylation	VDISILTTGMSATSR EEEEHHHCCCCCCCH	27.69	-
798	Sumoylation	SATSRKRKEELAEAL CCCCHHHHHHHHHHH	59.58	28112733
798	Ubiquitination	SATSRKRKEELAEAL CCCCHHHHHHHHHHH	59.58	-
806	Trimethylation	EELAEALKKLILSKG HHHHHHHHHHHHCCC	53.21	-
806	2-Hydroxyisobutyrylation	EELAEALKKLILSKG HHHHHHHHHHHHCCC	53.21	-
806	Acetylation	EELAEALKKLILSKG HHHHHHHHHHHHCCC	53.21	25953088
806	Methylation	EELAEALKKLILSKG HHHHHHHHHHHHCCC	53.21	-
811	Phosphorylation	ALKKLILSKGKTPAL HHHHHHHCCCCCHHH	32.16	28060719
814	Acetylation	KLILSKGKTPALKYQ HHHHCCCCCHHHHHH	55.88	25953088
814	Ubiquitination	KLILSKGKTPALKYQ HHHHCCCCCHHHHHH	55.88	21906983
815	Phosphorylation	LILSKGKTPALKYQQ HHHCCCCCHHHHHHH	23.59	23312004
819	2-Hydroxyisobutyrylation	KGKTPALKYQQLFED CCCCHHHHHHHHHHH	43.02	-
819	Acetylation	KGKTPALKYQQLFED CCCCHHHHHHHHHHH	43.02	23954790
819	Ubiquitination	KGKTPALKYQQLFED CCCCHHHHHHHHHHH	43.02	21906983
820	Phosphorylation	GKTPALKYQQLFEDI CCCHHHHHHHHHHHH	11.44	28152594
828	Methylation	QQLFEDIRGQSDIAI HHHHHHHCCCCCEEE	49.79	115482883
837	Acetylation	QSDIAITKDMFEEAL CCCEEECHHHHHHHH	40.87	26051181
837	Ubiquitination	QSDIAITKDMFEEAL CCCEEECHHHHHHHH	40.87	21906983
839	Sulfoxidation	DIAITKDMFEEALRA CEEECHHHHHHHHHH	4.92	21406390
858	2-Hydroxyisobutyrylation	DFLTVTGKTVRLL-- CCEEECCCEEEEC--	34.19	-
858	Acetylation	DFLTVTGKTVRLL-- CCEEECCCEEEEC--	34.19	23954790
858	Ubiquitination	DFLTVTGKTVRLL-- CCEEECCCEEEEC--	34.19	21906983

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
32	S	Phosphorylation	Kinase	CDK2	P24941	PSP
54	S	Phosphorylation	Kinase	CDK2	P24941	PSP
54	S	Phosphorylation	Kinase	CHEK1	O14757	GPS
110	T	Phosphorylation	Kinase	CDK2	P24941	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCM4_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 MCM4_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
CDC7_HUMAN	CDC7	physical	12614612
MCM8_HUMAN	MCM8	physical	12771218
MCM2_HUMAN	MCM2	physical	12694531
MCM6_HUMAN	MCM6	physical	12694531
MCM7_HUMAN	MCM7	physical	12694531
MCM2_HUMAN	MCM2	physical	12614612
MCM4_HUMAN	MCM4	physical	12614612
MCM6_HUMAN	MCM6	physical	12614612
ORC1_HUMAN	ORC1	physical	12614612
ORC2_HUMAN	ORC2	physical	12614612
ORC3_HUMAN	ORC3	physical	12614612
ORC4_HUMAN	ORC4	physical	12614612
ORC5_HUMAN	ORC5	physical	12614612
ORC6_HUMAN	ORC6	physical	12614612
RFA1_HUMAN	RPA1	physical	12614612
MCM6_HUMAN	MCM6	physical	8798650
MCM7_HUMAN	MCM7	physical	8798650
MCM2_HUMAN	MCM2	physical	8798650
SSRP1_HUMAN	SSRP1	physical	16902406
SP16H_HUMAN	SUPT16H	physical	16902406
MCM2_HUMAN	MCM2	physical	16902406
CDC45_HUMAN	CDC45	physical	16902406
MCM7_HUMAN	MCM7	physical	22939629
MCM6_HUMAN	MCM6	physical	22939629
MCM5_HUMAN	MCM5	physical	22939629
SF3A1_HUMAN	SF3A1	physical	22939629
ORC6_HUMAN	ORC6	physical	15232106
EIF3B_HUMAN	EIF3B	physical	22863883
FKBP4_HUMAN	FKBP4	physical	22863883
CLU_HUMAN	CLUH	physical	22863883
IMA4_HUMAN	KPNA3	physical	22863883
MCM2_HUMAN	MCM2	physical	22863883
MCM6_HUMAN	MCM6	physical	22863883
NCKP1_HUMAN	NCKAP1	physical	22863883
ANM1_HUMAN	PRMT1	physical	22863883
SHIP2_HUMAN	INPPL1	physical	26344197
IMA3_HUMAN	KPNA4	physical	26344197
MARE2_HUMAN	MAPRE2	physical	26344197
MCM3_HUMAN	MCM3	physical	26344197
MCM6_HUMAN	MCM6	physical	26344197
MCM7_HUMAN	MCM7	physical	26344197
RAD21_HUMAN	RAD21	physical	26344197
SF3A1_HUMAN	SF3A1	physical	26344197
SF3A3_HUMAN	SF3A3	physical	26344197
SF3B1_HUMAN	SF3B1	physical	26344197
SF3B2_HUMAN	SF3B2	physical	26344197
NADAP_HUMAN	SLC4A1AP	physical	26344197
CIP4_HUMAN	TRIP10	physical	26344197
UBP15_HUMAN	USP15	physical	27173435
MCM2_HUMAN	MCM2	physical	27173435
NS1BP_HUMAN	IVNS1ABP	physical	27173435
SMC1A_HUMAN	SMC1A	physical	27173435
SMC3_HUMAN	SMC3	physical	27173435
GAPD1_HUMAN	GAPVD1	physical	27173435
ANK3_HUMAN	ANK3	physical	27173435
SBNO1_HUMAN	SBNO1	physical	27173435
SOX4_HUMAN	SOX4	physical	27173435
HSF1_HUMAN	HSF1	physical	27173435
K1468_HUMAN	KIAA1468	physical	27173435
PLK1_HUMAN	PLK1	physical	27173435
SF3A1_HUMAN	SF3A1	physical	27173435
P4R3A_HUMAN	SMEK1	physical	27173435

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609981	Natural killer cell and glucocorticoid deficiency with DNA repair defect (NKGCD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MCM4_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-220 AND LYS-450, AND MASSSPECTROMETRY.	19608861 [Abstract]
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-131, AND MASSSPECTROMETRY.	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-26; SER-31; SER-32;SER-34; THR-102; SER-105; THR-110; SER-131; SER-142 AND SER-145, 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-120, AND MASSSPECTROMETRY.	18691976 [Abstract]
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis."; Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III; J. Proteome Res. 7:1346-1351(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-54, AND MASSSPECTROMETRY.	18220336 [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 SER-105 AND THR-110, ANDMASS SPECTROMETRY.	17924679 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-26, AND MASSSPECTROMETRY.	16964243 [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-32; SER-120; SER-131;SER-142 AND SER-145, AND MASS SPECTROMETRY.	17081983 [Abstract]
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-326, AND MASSSPECTROMETRY.	15302935 [Abstract]