MCM6_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MCM6_MOUSE
• UniProt AC: P97311
• Protein Name: DNA replication licensing factor MCM6
• Gene Name: Mcm6
• Organism: Mus musculus (Mouse).
• Sequence Length: 821
• Subcellular Localization: Nucleus. Binds to chromatin during G1 and detach from it during S phase..
• 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: MDLAAAAEPGAGSQHPEVRDEVAEKCQKLFLDFLEEFQGSDGEIKYLQFAEELIRPERNTLVVSFADLEQFNQQLSTTIQEEFYRVYPYLCRALKTFVKDRKEIPFAKDFYVAFQDLPTRHKIRELTSSRIGLLTRISGQVVRTHPVHPELVSGTFLCLDCQTVIKDVEQQFKYTQPNICRNPVCANRKRFLLDTNKSRFVDFQKVRIQETQAELPRGSIPRSLEVILRAEAVESAQAGDRCDFTGALIVVPDVSKLSTPGARAETNSRVSGADGYETEGIRGLRALGVRDLSYRLVFLACHVAPTNPRFGGKELRDEEQTAESIKNQMTVKEWEKVFEMSQDKNLYHNLCTSLFPTIHGNDEVKRGVLLMLFGGVPKTTGEGTSLRGDINVCIVGDPSTAKSQFLKHVDEFSPRAVYTSGKASSAAGLTAAVVRDEESHEFVIEAGALMLADNGVCCIDEFDKMDMRDQVAIHEAMEQQTISITKAGVKATLNARTSILAAANPVSGHYDRSKSLKQNINLSAPIMSRFDLFFILVDECNEVTDYAIARRIVDLHSRIEESIDRVYSLDDIRRYLLFARQFKPKISKESEDFIVEQYKRLRQRDGSGVTKSSWRITVRQLESMIRLSESMARMHCCDEVQPKHVKEAFRLLNKSIIRVETPDVNLDQEEEIQMETDEGQGGVNGHADSPAPVNRFNGSSEDASQETVSKPSLRLGFAEYCRISNLIVLHLRKMEEEEDESALKRSELVNWYLKEIESEIDSEEELINKKTIIEKVVHRLTHYDHVLIELTQAGLKGSSEGSESYEEDPYLVVNPNYLLED

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
1	Acetylation	-------MDLAAAAE -------CCHHHHCC	9.57	-
13	Phosphorylation	AAEPGAGSQHPEVRD HCCCCCCCCCHHHHH	25.45	26824392
173	Acetylation	KDVEQQFKYTQPNIC HHHHHHHCCCCCCCC	42.95	22826441
197	Ubiquitination	RFLLDTNKSRFVDFQ EEEEECCHHHCCCEE	45.13	-
211	Phosphorylation	QKVRIQETQAELPRG EEEEEEEHHHCCCCC	19.39	24759943
219	Phosphorylation	QAELPRGSIPRSLEV HHCCCCCCCCCHHHH	30.60	28507225
223	Phosphorylation	PRGSIPRSLEVILRA CCCCCCCHHHHHHHH	24.43	18779572
258	Phosphorylation	VPDVSKLSTPGARAE ECCHHHCCCCCCCHH	35.97	-
259	Phosphorylation	PDVSKLSTPGARAET CCHHHCCCCCCCHHC	35.86	27149854
266	Phosphorylation	TPGARAETNSRVSGA CCCCCHHCCCCCCCC	37.19	25168779
268	Phosphorylation	GARAETNSRVSGADG CCCHHCCCCCCCCCC	41.29	26525534
271	Phosphorylation	AETNSRVSGADGYET HHCCCCCCCCCCCCC	27.44	26824392
276	Phosphorylation	RVSGADGYETEGIRG CCCCCCCCCCCCCCC	21.89	21659605
278	Phosphorylation	SGADGYETEGIRGLR CCCCCCCCCCCCCHH	30.91	26525534
301	S-nitrosocysteine	YRLVFLACHVAPTNP HHHHHHHHHCCCCCC	2.63	-
301	S-nitrosylation	YRLVFLACHVAPTNP HHHHHHHHHCCCCCC	2.63	20925432
407	Ubiquitination	TAKSQFLKHVDEFSP HHHHHHHHHHHHCCC	42.76	-
413	Phosphorylation	LKHVDEFSPRAVYTS HHHHHHCCCCEEEEC	16.07	27600695
418	Phosphorylation	EFSPRAVYTSGKASS HCCCCEEEECCCCCC	8.33	20415495
419	Phosphorylation	FSPRAVYTSGKASSA CCCCEEEECCCCCCC	25.14	20415495
420	Phosphorylation	SPRAVYTSGKASSAA CCCEEEECCCCCCCC	22.17	20415495
424	Phosphorylation	VYTSGKASSAAGLTA EEECCCCCCCCCCEE	24.81	20415495
425	Phosphorylation	YTSGKASSAAGLTAA EECCCCCCCCCCEEE	27.31	20415495
430	Phosphorylation	ASSAAGLTAAVVRDE CCCCCCCEEEEECCC	16.20	20415495
490	Ubiquitination	SITKAGVKATLNART EEEHHHHHHHHHHHH	34.43	-
567	Phosphorylation	EESIDRVYSLDDIRR HHHHHHCCCHHHHHH	12.38	28066266
568	Phosphorylation	ESIDRVYSLDDIRRY HHHHHCCCHHHHHHH	23.59	22817900
607	Phosphorylation	RLRQRDGSGVTKSSW HHHHCCCCCCCHHHH	34.09	29109428
611	Acetylation	RDGSGVTKSSWRITV CCCCCCCHHHHEEEH	39.83	23806337
643	Acetylation	CCDEVQPKHVKEAFR CCCCCCHHHHHHHHH	43.89	23806337
655	Phosphorylation	AFRLLNKSIIRVETP HHHHHHCCCEEEECC	23.36	27087446
661	Phosphorylation	KSIIRVETPDVNLDQ CCCEEEECCCCCCCH	23.18	25619855
676	Phosphorylation	EEEIQMETDEGQGGV HHHEECCCCCCCCCC	33.73	26239621
689	Phosphorylation	GVNGHADSPAPVNRF CCCCCCCCCCCCCCC	24.60	27087446
699	Phosphorylation	PVNRFNGSSEDASQE CCCCCCCCCCCCCHH	31.49	26824392
700	Phosphorylation	VNRFNGSSEDASQET CCCCCCCCCCCCHHH	40.68	22942356
704	Phosphorylation	NGSSEDASQETVSKP CCCCCCCCHHHCCCC	40.65	27087446
707	Phosphorylation	SEDASQETVSKPSLR CCCCCHHHCCCCHHH	23.57	25168779
709	Phosphorylation	DASQETVSKPSLRLG CCCHHHCCCCHHHHC	46.39	25619855
710	Ubiquitination	ASQETVSKPSLRLGF CCHHHCCCCHHHHCH	34.00	-
712	Phosphorylation	QETVSKPSLRLGFAE HHHCCCCHHHHCHHH	29.83	25619855
741	Phosphorylation	MEEEEDESALKRSEL CCHHHCHHHHHHHHH	51.74	26824392
758	Phosphorylation	WYLKEIESEIDSEEE HHHHHHHHCCCCHHH	45.58	25168779
762	Phosphorylation	EIESEIDSEEELINK HHHHCCCCHHHHHCH	53.20	26824392
791	Phosphorylation	DHVLIELTQAGLKGS HHHHHHHHHHCCCCC	12.00	17525332
798	Phosphorylation	TQAGLKGSSEGSESY HHHCCCCCCCCCCCC	24.51	26643407
799	Phosphorylation	QAGLKGSSEGSESYE HHCCCCCCCCCCCCC	55.43	25293948
802	Phosphorylation	LKGSSEGSESYEEDP CCCCCCCCCCCCCCC	21.22	26643407
804	Phosphorylation	GSSEGSESYEEDPYL CCCCCCCCCCCCCEE	39.27	26643407
805	Phosphorylation	SSEGSESYEEDPYLV CCCCCCCCCCCCEEE	21.20	23984901
810	Phosphorylation	ESYEEDPYLVVNPNY CCCCCCCEEEECCCC	25.17	23984901

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

Oops, there are no upstream regulatory protein records of MCM6_MOUSE !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MCM6_MOUSE !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MCM6_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
MCM10_HUMAN	MCM10	physical	11095689
DMRTD_MOUSE	Dmrtc2	physical	20211142
GMEB2_MOUSE	Gmeb2	physical	20211142

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

Phosphorylation

"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 THR-791, AND MASSSPECTROMETRY.
PubMed: 17525332