dbPTM

MCM5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MCM5_HUMAN
UniProt AC	P33992
Protein Name	DNA replication licensing factor MCM5
Gene Name	MCM5
Organism	Homo sapiens (Human).
Sequence Length	734
Subcellular Localization	Nucleus . Cytoplasm, cytosol .
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 (By similarity). Interacts with MCMBP..
Protein Sequence	MSGFDDPGIFYSDSFGGDAQADEGQARKSQLQRRFKEFLRQYRVGTDRTGFTFKYRDELKRHYNLGEYWIEVEMEDLASFDEDLADYLYKQPAEHLQLLEEAAKEVADEVTRPRPSGEEVLQDIQVMLKSDASPSSIRSLKSDMMSHLVKIPGIIIAASAVRAKATRISIQCRSCRNTLTNIAMRPGLEGYALPRKCNTDQAGRPKCPLDPYFIMPDKCKCVDFQTLKLQELPDAVPHGEMPRHMQLYCDRYLCDKVVPGNRVTIMGIYSIKKFGLTTSRGRDRVGVGIRSSYIRVLGIQVDTDGSGRSFAGAVSPQEEEEFRRLAALPNVYEVISKSIAPSIFGGTDMKKAIACLLFGGSRKRLPDGLTRRGDINLLMLGDPGTAKSQLLKFVEKCSPIGVYTSGKGSSAAGLTASVMRDPSSRNFIMEGGAMVLADGGVVCIDEFDKMREDDRVAIHEAMEQQTISIAKAGITTTLNSRCSVLAAANSVFGRWDETKGEDNIDFMPTILSRFDMIFIVKDEHNEERDVMLAKHVITLHVSALTQTQAVEGEIDLAKLKKFIAYCRVKCGPRLSAEAAEKLKNRYIIMRSGARQHERDSDRRSSIPITVRQLEAIVRIAEALSKMKLQPFATEADVEEALRLFQVSTLDAALSGTLSGVEGFTSQEDQEMLSRIEKQLKRRFAIGSQVSEHSIIKDFTKQKYPEHAIHKVLQLMLRRGEIQHRMQRKVLYRLK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSGFDDPGI ------CCCCCCCCC	48.44	18491316
2	Phosphorylation	------MSGFDDPGI ------CCCCCCCCC	48.44	26552605
11	Phosphorylation	FDDPGIFYSDSFGGD CCCCCCCCCCCCCCC	15.06	28450419
12	Phosphorylation	DDPGIFYSDSFGGDA CCCCCCCCCCCCCCC	18.94	28450419
14	Phosphorylation	PGIFYSDSFGGDAQA CCCCCCCCCCCCCCC	21.61	28450419
36	Ubiquitination	SQLQRRFKEFLRQYR HHHHHHHHHHHHHHC	45.83	-
54	Ubiquitination	DRTGFTFKYRDELKR CCCCCEEEEHHHHHH	36.00	-
55	Phosphorylation	RTGFTFKYRDELKRH CCCCEEEEHHHHHHH	21.07	28152594
60	Acetylation	FKYRDELKRHYNLGE EEEHHHHHHHCCCCC	34.77	25953088
129	Ubiquitination	QDIQVMLKSDASPSS HHHHHHHHCCCCHHH	28.35	-
130	Phosphorylation	DIQVMLKSDASPSSI HHHHHHHCCCCHHHH	34.15	20068231
133	Phosphorylation	VMLKSDASPSSIRSL HHHHCCCCHHHHHHH	30.24	30576142
135	Phosphorylation	LKSDASPSSIRSLKS HHCCCCHHHHHHHHH	35.58	25262027
136	Phosphorylation	KSDASPSSIRSLKSD HCCCCHHHHHHHHHH	25.96	25262027
139	Phosphorylation	ASPSSIRSLKSDMMS CCHHHHHHHHHHHHH	38.18	27251275
141	Acetylation	PSSIRSLKSDMMSHL HHHHHHHHHHHHHHH	45.73	25953088
141	Ubiquitination	PSSIRSLKSDMMSHL HHHHHHHHHHHHHHH	45.73	21890473
142	Phosphorylation	SSIRSLKSDMMSHLV HHHHHHHHHHHHHHH	35.71	21406692
146	Phosphorylation	SLKSDMMSHLVKIPG HHHHHHHHHHHCCCH	13.66	21406692
150	Ubiquitination	DMMSHLVKIPGIIIA HHHHHHHCCCHHHEE	49.93	-
159	Phosphorylation	PGIIIAASAVRAKAT CHHHEEHHHHHHHCC	20.48	20068231
178	Phosphorylation	QCRSCRNTLTNIAMR EEHHHCCHHHHHHHC	18.66	27080861
184	Sulfoxidation	NTLTNIAMRPGLEGY CHHHHHHHCCCCCCC	4.74	21406390
206	Ubiquitination	TDQAGRPKCPLDPYF CCCCCCCCCCCCCCE	47.31	-
212	Phosphorylation	PKCPLDPYFIMPDKC CCCCCCCCEECCCCC	12.85	-
218	Ubiquitination	PYFIMPDKCKCVDFQ CCEECCCCCEEEECC	29.71	-
220	Acetylation	FIMPDKCKCVDFQTL EECCCCCEEEECCEE	42.93	23749302
220	Ubiquitination	FIMPDKCKCVDFQTL EECCCCCEEEECCEE	42.93	-
228	Acetylation	CVDFQTLKLQELPDA EEECCEEEHHHCCCC	52.06	25953088
228	Ubiquitination	CVDFQTLKLQELPDA EEECCEEEHHHCCCC	52.06	-
241	Sulfoxidation	DAVPHGEMPRHMQLY CCCCCCCCCHHHHHH	4.12	21406390
248	Phosphorylation	MPRHMQLYCDRYLCD CCHHHHHHHHHHHCC	3.87	-
251	Methylation	HMQLYCDRYLCDKVV HHHHHHHHHHCCCCC	23.82	115482899
256	2-Hydroxyisobutyrylation	CDRYLCDKVVPGNRV HHHHHCCCCCCCCCE	44.10	-
256	Acetylation	CDRYLCDKVVPGNRV HHHHHCCCCCCCCCE	44.10	25953088
256	Ubiquitination	CDRYLCDKVVPGNRV HHHHHCCCCCCCCCE	44.10	-
269	Phosphorylation	RVTIMGIYSIKKFGL CEEEEEEEEEEECCC	9.90	-
270	Phosphorylation	VTIMGIYSIKKFGLT EEEEEEEEEEECCCC	26.47	24719451
272	Acetylation	IMGIYSIKKFGLTTS EEEEEEEEECCCCCC	35.79	25953088
273	Acetylation	MGIYSIKKFGLTTSR EEEEEEEECCCCCCC	42.89	25953088
273	Ubiquitination	MGIYSIKKFGLTTSR EEEEEEEECCCCCCC	42.89	-
277	Phosphorylation	SIKKFGLTTSRGRDR EEEECCCCCCCCCCC	24.09	28555341
278	Phosphorylation	IKKFGLTTSRGRDRV EEECCCCCCCCCCCC	22.82	23186163
279	Phosphorylation	KKFGLTTSRGRDRVG EECCCCCCCCCCCCC	27.74	23186163
280	Methylation	KFGLTTSRGRDRVGV ECCCCCCCCCCCCCC	41.91	82797193
303	Phosphorylation	VLGIQVDTDGSGRSF EEEEEEECCCCCCCC	43.32	-
309	Phosphorylation	DTDGSGRSFAGAVSP ECCCCCCCCCCCCCH	23.99	23186163
315	Phosphorylation	RSFAGAVSPQEEEEF CCCCCCCCHHHHHHH	21.97	23401153
332	Phosphorylation	LAALPNVYEVISKSI HHHCCCHHHHHHHHH	15.89	28152594
336	Phosphorylation	PNVYEVISKSIAPSI CCHHHHHHHHHCHHH	26.06	28152594
337	Ubiquitination	NVYEVISKSIAPSIF CHHHHHHHHHCHHHH	34.45	21890473
338	Phosphorylation	VYEVISKSIAPSIFG HHHHHHHHHCHHHHC	19.72	27362937
342	Phosphorylation	ISKSIAPSIFGGTDM HHHHHCHHHHCCCCH	22.87	27362937
350	Succinylation	IFGGTDMKKAIACLL HHCCCCHHHHHHHHH	41.69	23954790
350	Ubiquitination	IFGGTDMKKAIACLL HHCCCCHHHHHHHHH	41.69	-
351	Acetylation	FGGTDMKKAIACLLF HCCCCHHHHHHHHHH	38.09	26051181
351	Ubiquitination	FGGTDMKKAIACLLF HCCCCHHHHHHHHHH	38.09	-
361	Phosphorylation	ACLLFGGSRKRLPDG HHHHHCCCCCCCCCC	34.70	27362937
363	Ubiquitination	LLFGGSRKRLPDGLT HHHCCCCCCCCCCCC	61.04	-
379	Sulfoxidation	RGDINLLMLGDPGTA CCCEEEEEECCCCCH	4.41	21406390
385	Phosphorylation	LMLGDPGTAKSQLLK EEECCCCCHHHHHHH	35.98	-
387	Acetylation	LGDPGTAKSQLLKFV ECCCCCHHHHHHHHH	38.27	7833957
387	Ubiquitination	LGDPGTAKSQLLKFV ECCCCCHHHHHHHHH	38.27	-
392	2-Hydroxyisobutyrylation	TAKSQLLKFVEKCSP CHHHHHHHHHHHCCC	56.83	-
392	Acetylation	TAKSQLLKFVEKCSP CHHHHHHHHHHHCCC	56.83	19608861
392	Ubiquitination	TAKSQLLKFVEKCSP CHHHHHHHHHHHCCC	56.83	19608861
396	2-Hydroxyisobutyrylation	QLLKFVEKCSPIGVY HHHHHHHHCCCCEEE	34.41	-
396	Acetylation	QLLKFVEKCSPIGVY HHHHHHHHCCCCEEE	34.41	19608861
396	Malonylation	QLLKFVEKCSPIGVY HHHHHHHHCCCCEEE	34.41	26320211
396	Ubiquitination	QLLKFVEKCSPIGVY HHHHHHHHCCCCEEE	34.41	19608861
403	Phosphorylation	KCSPIGVYTSGKGSS HCCCCEEEECCCCCC	7.03	28152594
404	Phosphorylation	CSPIGVYTSGKGSSA CCCCEEEECCCCCCC	28.70	28152594
405	Phosphorylation	SPIGVYTSGKGSSAA CCCEEEECCCCCCCC	22.33	28152594
407	Ubiquitination	IGVYTSGKGSSAAGL CEEEECCCCCCCCCC	56.22	-
409	Phosphorylation	VYTSGKGSSAAGLTA EEECCCCCCCCCCCH	21.93	21406692
410	Phosphorylation	YTSGKGSSAAGLTAS EECCCCCCCCCCCHH	30.70	21406692
415	Phosphorylation	GSSAAGLTASVMRDP CCCCCCCCHHHCCCH	18.90	21406692
417	Phosphorylation	SAAGLTASVMRDPSS CCCCCCHHHCCCHHH	15.94	21406692
419	Sulfoxidation	AGLTASVMRDPSSRN CCCCHHHCCCHHHCC	3.59	21406390
423	Phosphorylation	ASVMRDPSSRNFIME HHHCCCHHHCCEEEE	46.34	-
424	Phosphorylation	SVMRDPSSRNFIMEG HHCCCHHHCCEEEEC	36.31	-
471	Ubiquitination	QQTISIAKAGITTTL HHCCEEECCCCCCCC	45.54	21890473
482	S-nitrosocysteine	TTTLNSRCSVLAAAN CCCCHHHHHHHHHHH	3.11	-
482	S-nitrosylation	TTTLNSRCSVLAAAN CCCCHHHHHHHHHHH	3.11	19483679
483	Phosphorylation	TTLNSRCSVLAAANS CCCHHHHHHHHHHHH	21.03	27080861
498	Phosphorylation	VFGRWDETKGEDNID HHCCCCCCCCCCCCC	41.71	28851738
499	Ubiquitination	FGRWDETKGEDNIDF HCCCCCCCCCCCCCC	59.25	21890473
509	Phosphorylation	DNIDFMPTILSRFDM CCCCCHHHHHHHCCE	23.82	28851738
512	Phosphorylation	DFMPTILSRFDMIFI CCHHHHHHHCCEEEE	27.35	28851738
528	Methylation	KDEHNEERDVMLAKH ECCCCCHHHHHHHHH	35.33	115482891
531	Sulfoxidation	HNEERDVMLAKHVIT CCCHHHHHHHHHHHE	3.36	21406390
561	Acetylation	IDLAKLKKFIAYCRV CCHHHHHHHHHHHHC	53.06	25953088
561	Ubiquitination	IDLAKLKKFIAYCRV CCHHHHHHHHHHHHC	53.06	-
565	Phosphorylation	KLKKFIAYCRVKCGP HHHHHHHHHHCCCCC	3.96	25367160
581	Acetylation	LSAEAAEKLKNRYII CCHHHHHHHHHCEEE	61.10	23749302
581	Ubiquitination	LSAEAAEKLKNRYII CCHHHHHHHHHCEEE	61.10	-
583	Ubiquitination	AEAAEKLKNRYIIMR HHHHHHHHHCEEEEC	50.91	-
586	Phosphorylation	AEKLKNRYIIMRSGA HHHHHHCEEEECCCC	12.28	20049867
604	Phosphorylation	ERDSDRRSSIPITVR CCCCCCCCCCCCHHH	33.25	28450419
605	Phosphorylation	RDSDRRSSIPITVRQ CCCCCCCCCCCHHHH	30.49	28450419
609	Phosphorylation	RRSSIPITVRQLEAI CCCCCCCHHHHHHHH	12.32	23186163
625	Ubiquitination	RIAEALSKMKLQPFA HHHHHHHCCCCCCCC	40.69	-
627	2-Hydroxyisobutyrylation	AEALSKMKLQPFATE HHHHHCCCCCCCCCC	47.94	-
627	Ubiquitination	AEALSKMKLQPFATE HHHHHCCCCCCCCCC	47.94	21890473
633	Phosphorylation	MKLQPFATEADVEEA CCCCCCCCCCCHHHH	31.89	-
690	Phosphorylation	FAIGSQVSEHSIIKD HCCCCCCCCHHHHHH	23.19	23186163
693	Phosphorylation	GSQVSEHSIIKDFTK CCCCCCHHHHHHHHC	23.20	23186163
696	Acetylation	VSEHSIIKDFTKQKY CCCHHHHHHHHCCCC	45.15	19608861
696	Ubiquitination	VSEHSIIKDFTKQKY CCCHHHHHHHHCCCC	45.15	21906983
702	Ubiquitination	IKDFTKQKYPEHAIH HHHHHCCCCCHHHHH	65.41	-

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
633	T	Phosphorylation	Kinase	CHEK1	O14757	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MCM5_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 MCM5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM2_HUMAN	MCM2	physical	12614612
CDC7_HUMAN	CDC7	physical	12614612
MDFI_HUMAN	MDFI	physical	16189514
MCM3_HUMAN	MCM3	physical	12614612
MCM7_HUMAN	MCM7	physical	12614612
ORC2_HUMAN	ORC2	physical	12614612
ORC6_HUMAN	ORC6	physical	12614612
STAT1_HUMAN	STAT1	physical	9843502
MCM3_HUMAN	MCM3	physical	11248027
MCM4_HUMAN	MCM4	physical	11248027
MCM6_HUMAN	MCM6	physical	11248027
MCM7_HUMAN	MCM7	physical	11248027
MCM2_HUMAN	MCM2	physical	11248027
LMBL1_HUMAN	L3MBTL1	physical	21149733
A4_HUMAN	APP	physical	21832049
MCM7_HUMAN	MCM7	physical	22939629
MCM6_HUMAN	MCM6	physical	22939629
U2AF1_HUMAN	U2AF1	physical	22939629
ORC1_HUMAN	ORC1	physical	15232106
MCM2_HUMAN	MCM2	physical	15232106
CDC5L_HUMAN	CDC5L	physical	15232106
MCM7_HUMAN	MCM7	physical	15232106
CDN2A_HUMAN	CDKN2A	physical	15232106
ARF_HUMAN	CDKN2A	physical	15232106
ORC5_HUMAN	ORC5	physical	15232106
CAP1_HUMAN	CAP1	physical	22863883
FKBP5_HUMAN	FKBP5	physical	22863883
HS90A_HUMAN	HSP90AA1	physical	22863883
HS90B_HUMAN	HSP90AB1	physical	22863883
MAGD2_HUMAN	MAGED2	physical	22863883
MCM3_HUMAN	MCM3	physical	22863883
NEK9_HUMAN	NEK9	physical	22863883
RBPMS_HUMAN	RBPMS	physical	25416956
KR107_HUMAN	KRTAP10-7	physical	25416956
ILF2_HUMAN	ILF2	physical	20808282
RAD50_HUMAN	RAD50	physical	20808282
ILF3_HUMAN	ILF3	physical	20808282
API5_HUMAN	API5	physical	26344197
SPF27_HUMAN	BCAS2	physical	26344197
COPE_HUMAN	COPE	physical	26344197
DDB1_HUMAN	DDB1	physical	26344197
SLD5_HUMAN	GINS4	physical	26344197
ERF3A_HUMAN	GSPT1	physical	26344197
LAGE3_HUMAN	LAGE3	physical	26344197
MCM3_HUMAN	MCM3	physical	26344197
MCM4_HUMAN	MCM4	physical	26344197
MCM7_HUMAN	MCM7	physical	26344197
MCMBP_HUMAN	MCMBP	physical	26344197
ORC2_HUMAN	ORC2	physical	26344197
ANM5_HUMAN	PRMT5	physical	26344197
PSA3_HUMAN	PSMA3	physical	26344197
PSMD4_HUMAN	PSMD4	physical	26344197
SF3A3_HUMAN	SF3A3	physical	26344197
SF3B1_HUMAN	SF3B1	physical	26344197
SPTB2_HUMAN	SPTBN1	physical	26344197
MCM3_HUMAN	MCM3	physical	25963833
ROA2_HUMAN	HNRNPA2B1	physical	25963833
DREB_HUMAN	DBN1	physical	25963833
HNRPC_HUMAN	HNRNPC	physical	25963833
H12_HUMAN	HIST1H1C	physical	25963833
ROA3_HUMAN	HNRNPA3	physical	25963833
HSP7C_HUMAN	HSPA8	physical	25963833
H2B3B_HUMAN	HIST3H2BB	physical	25963833
MYO1C_HUMAN	MYO1C	physical	25963833
MATR3_HUMAN	MATR3	physical	25963833
HNRPU_HUMAN	HNRNPU	physical	25963833
ILF2_HUMAN	ILF2	physical	25963833
DDX21_HUMAN	DDX21	physical	25963833
FBRL_HUMAN	FBL	physical	25963833
DDX5_HUMAN	DDX5	physical	25963833
ILF3_HUMAN	ILF3	physical	25963833
ROA1_HUMAN	HNRNPA1	physical	25963833
PRP8_HUMAN	PRPF8	physical	25963833
SFPQ_HUMAN	SFPQ	physical	25963833
RBMX_HUMAN	RBMX	physical	25963833
PELP1_HUMAN	PELP1	physical	25963833
DHX9_HUMAN	DHX9	physical	25963833
H2A1J_HUMAN	HIST1H2AJ	physical	25963833
TOP2A_HUMAN	TOP2A	physical	25963833
HNRL2_HUMAN	HNRNPUL2	physical	25963833
U520_HUMAN	SNRNP200	physical	25963833
TR150_HUMAN	THRAP3	physical	25963833
LMNA_HUMAN	LMNA	physical	25963833
MCM6_HUMAN	MCM6	physical	25963833
SF3B1_HUMAN	SF3B1	physical	25963833
ACTN1_HUMAN	ACTN1	physical	25963833
DHX15_HUMAN	DHX15	physical	25963833
NOP2_HUMAN	NOP2	physical	25963833
SF3B3_HUMAN	SF3B3	physical	25963833
DDX27_HUMAN	DDX27	physical	25963833
K1C18_HUMAN	KRT18	physical	25963833
NEST_HUMAN	NES	physical	25963833
NUCL_HUMAN	NCL	physical	25963833
NAT10_HUMAN	NAT10	physical	25963833
VIME_HUMAN	VIM	physical	25963833
HS90A_HUMAN	HSP90AA1	physical	25963833
HNRPQ_HUMAN	SYNCRIP	physical	25963833
TOP1_HUMAN	TOP1	physical	25963833
COF1_HUMAN	CFL1	physical	25963833
PRDX1_HUMAN	PRDX1	physical	25963833
ANXA2_HUMAN	ANXA2	physical	25963833
UBB_HUMAN	UBB	physical	25963833
MYH9_HUMAN	MYH9	physical	25963833
CALL5_HUMAN	CALML5	physical	25963833
DSC1_HUMAN	DSC1	physical	25963833
TGM3_HUMAN	TGM3	physical	25963833
ZA2G_HUMAN	AZGP1	physical	25963833
S10A8_HUMAN	S100A8	physical	25963833
DESP_HUMAN	DSP	physical	25963833
KPRP_HUMAN	KPRP	physical	25963833
DSG1_HUMAN	DSG1	physical	25963833
PLAK_HUMAN	JUP	physical	25963833
S10A9_HUMAN	S100A9	physical	25963833
PIP_HUMAN	PIP	physical	25963833
K22E_HUMAN	KRT2	physical	25963833
DCD_HUMAN	DCD	physical	25963833
PYGL_HUMAN	PYGL	physical	25963833
LANC1_HUMAN	LANCL1	physical	25963833
PYGB_HUMAN	PYGB	physical	25963833
LEG1_HUMAN	LGALS1	physical	25963833
GRP75_HUMAN	HSPA9	physical	25963833
ERP44_HUMAN	ERP44	physical	25963833
TBB4B_HUMAN	TUBB4B	physical	25963833
TBB5_HUMAN	TUBB	physical	25963833
ATPA_HUMAN	ATP5A1	physical	25963833
KPYM_HUMAN	PKM	physical	25963833
ADT2_HUMAN	SLC25A5	physical	25963833
HS90B_HUMAN	HSP90AB1	physical	25963833
MLEC_HUMAN	MLEC	physical	25963833
FLNC_HUMAN	FLNC	physical	25963833
G3P_HUMAN	GAPDH	physical	25963833
RS18_HUMAN	RPS18	physical	25963833
ENOA_HUMAN	ENO1	physical	25963833
PHB2_HUMAN	PHB2	physical	25963833
WDR36_HUMAN	WDR36	physical	25963833
SBSN_HUMAN	SBSN	physical	25963833
MCM2_HUMAN	MCM2	physical	25963833
H2A1A_HUMAN	HIST1H2AA	physical	25963833
HS71L_HUMAN	HSPA1L	physical	25963833
K1C19_HUMAN	KRT19	physical	25963833
ACTBL_HUMAN	ACTBL2	physical	25963833
TBB2B_HUMAN	TUBB2B	physical	25963833
H2B2E_HUMAN	HIST2H2BE	physical	25963833
H2B1B_HUMAN	HIST1H2BB	physical	25963833
H2B1O_HUMAN	HIST1H2BO	physical	25963833
H2B1J_HUMAN	HIST1H2BJ	physical	25963833
H2B1L_HUMAN	HIST1H2BL	physical	25963833
H2B1M_HUMAN	HIST1H2BM	physical	25963833
H2B1N_HUMAN	HIST1H2BN	physical	25963833
H2B1H_HUMAN	HIST1H2BH	physical	25963833
H2B2F_HUMAN	HIST2H2BF	physical	25963833
H2B1D_HUMAN	HIST1H2BD	physical	25963833
H2B1C_HUMAN	HIST1H2BD	physical	25963833
H2B1K_HUMAN	HIST1H2BK	physical	25963833
H2B1A_HUMAN	HIST1H2BA	physical	25963833
H2A2A_HUMAN	HIST2H2AA3	physical	25963833
H2A1D_HUMAN	HIST1H2AD	physical	25963833
H2AV_HUMAN	H2AFV	physical	25963833
H2AZ_HUMAN	H2AFZ	physical	25963833
COF2_HUMAN	CFL2	physical	25963833
DDX17_HUMAN	DDX17	physical	25963833
EF1A1_HUMAN	EEF1A1	physical	25963833
FLNA_HUMAN	FLNA	physical	25963833
H2AX_HUMAN	H2AFX	physical	25963833
H33_HUMAN	H3F3A	physical	25963833
H14_HUMAN	HIST1H1E	physical	25963833
H2A1H_HUMAN	HIST1H2AH	physical	25963833
RA1L2_HUMAN	HNRNPA1L2	physical	25963833
HNRC1_HUMAN	HNRNPCL1	physical	25963833
HNRPR_HUMAN	HNRNPR	physical	25963833
HSP72_HUMAN	HSPA2	physical	25963833
HSP76_HUMAN	HSPA6	physical	25963833
RMXL1_HUMAN	RBMXL1	physical	25963833
RS27A_HUMAN	RPS27A	physical	25963833
TOP1M_HUMAN	TOP1MT	physical	25963833
TBB2A_HUMAN	TUBB2A	physical	25963833
TBB3_HUMAN	TUBB3	physical	25963833
TBB4A_HUMAN	TUBB4A	physical	25963833
EF1A2_HUMAN	EEF1A2	physical	25963833
FLNB_HUMAN	FLNB	physical	25963833
H2AJ_HUMAN	H2AFJ	physical	25963833
H13_HUMAN	HIST1H1D	physical	25963833
H2A2B_HUMAN	HIST2H2AB	physical	25963833
RMXL2_HUMAN	RBMXL2	physical	25963833
UBC_HUMAN	UBC	physical	25963833
H2A2C_HUMAN	HIST2H2AC	physical	25963833
H31T_HUMAN	HIST3H3	physical	25963833
RMXL3_HUMAN	RBMXL3	physical	25963833
RL40_HUMAN	UBA52	physical	25963833
H2A1C_HUMAN	HIST1H2AC	physical	25963833
H31_HUMAN	HIST1H3A	physical	25963833
H3C_HUMAN	H3F3C	physical	25963833
H2A3_HUMAN	HIST3H2A	physical	25963833
MCM2_HUMAN	MCM2	physical	24207054
MCM3_HUMAN	MCM3	physical	25843623
FANCI_HUMAN	FANCI	physical	25843623
FANCA_HUMAN	FANCA	physical	28215707
FACD2_HUMAN	FANCD2	physical	23993743
MCM2_HUMAN	MCM2	physical	23993743
MCM3_HUMAN	MCM3	physical	23993743
MCM7_HUMAN	MCM7	physical	23993743

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 MCM5_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-392; LYS-396 AND LYS-696,AND MASS SPECTROMETRY.	19608861 [Abstract]