MCM2_SCHPO - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: MCM2_SCHPO
• UniProt AC: P40377
• Protein Name: DNA replication licensing factor mcm2
• Gene Name: mcm2
• Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
• Sequence Length: 830
• 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 (By similarity). Plays an important role in DNA replication..
• Protein Sequence: MDSFRKRGRRDSESLPFESENSSLGATPLSLPPSSPPPEFSDEAAEALVEEDIEDLDGEALDVEDEEGEDLFGEGMERDYQQNLELDRYDIEELDDDNDLEELDIGARRAVDARLRRRDIELDAAAGRTKPAAFLQDEDDDLDSNLGTGFTRHRHRIYDEYSPNVGALDESGELPLESIADVKADSIAEWVTLDPVRRTIAREFKNFLLEYTDENGTSVYGNRIRTLGEVNAESLMVNYAHLGESKPILAYFLANAPAPIFRIFDRVALEATLLHYPDYERIHSDIHVRITNLPTCFTLRDLRQSHLNCLVRVSGVVTRRTGLFPQLKYIRFTCTKCGATLGPFFQDSSVEVKISFCHNCSSRGPFVINSERTVYNNYQRITLQESPGTVPSGRLPRHREVILLADLVDVAKPGEEIDVTGIYRNNFDASLNTKNGFPVFATIIEANHISQLDGSGNTDDDFSLSRLTDDEEREIRALAKSPDIHNRIIASMAPSIYGHRSIKTAIAAALFGGVPKNINGKHKIRGDINVLLLGDPGTAKSQFLKYVEKTAHRAVFATGQGASAVGLTASVRKDPITNEWTLEGGALVLADKGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTTLQARCTIIAAANPIGGRYNTTIPFNQNVELTEPILSRFDILQVVKDTVNPEIDEQLANFVVSSHIRSHPAFDPNMDVLKKVPTETGIDAKPIPQDLLRKYIHFAREKVFPRLQQMDEEKISRLYSDMRRESLATGSYPITVRHLESAIRLSEAFAKMQLSEFVRPSHIDKAIQVIIDSFVNAQKMSVKRSLSRTFAKYLI

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
129	Phosphorylation	LDAAAGRTKPAAFLQ HHHHCCCCCCCHHCC	40.23	29996109
144	Phosphorylation	DEDDDLDSNLGTGFT CCCCCCCCCCCCCCH	41.05	28889911
158	Phosphorylation	TRHRHRIYDEYSPNV HHHHHHCCCCCCCCC	11.59	27738172
162	Phosphorylation	HRIYDEYSPNVGALD HHCCCCCCCCCCCCC	14.14	29996109
764	Phosphorylation	MRRESLATGSYPITV HHHHHHCCCCCCCCH	31.77	29996109
766	Phosphorylation	RESLATGSYPITVRH HHHHCCCCCCCCHHH	24.31	29996109

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

Oops, there are no upstream regulatory protein records of MCM2_SCHPO !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of MCM2_SCHPO !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of MCM2_SCHPO !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
DED1_SCHPO	sum3	genetic	10725227
CG22_SCHPO	cig2	genetic	10725227
CHK1_SCHPO	chk1	genetic	9914167
CDS1_SCHPO	cds1	genetic	9914167
RUM1_SCHPO	rum1	genetic	15194812
CDC18_SCHPO	cdc18	genetic	9383050
DPOD2_SCHPO	cdc1	genetic	9383050
DPOD_SCHPO	cdc6	genetic	9383050
MCM2_SCHPO	mcm2	genetic	10588642
CDC45_SCHPO	cdc45	genetic	9619628
MCM6_SCHPO	mcm6	physical	9658174
MCM6_SCHPO	mcm6	physical	10770926
MCM7_SCHPO	mcm7	physical	10770926
MCM3_SCHPO	mcm3	physical	10770926
CDC45_SCHPO	cdc45	physical	15338237
SWI1_SCHPO	swi1	physical	16263721
MCM6_SCHPO	mcm6	physical	21813639
MCM7_SCHPO	mcm7	physical	21813639
MCM3_SCHPO	mcm3	physical	21813639
CG22_SCHPO	cig2	genetic	15194812
MCM6_SCHPO	mcm6	genetic	9383050
MCM6_SCHPO	mcm6	physical	9366552
MCM7_SCHPO	mcm7	physical	9366552
MCM3_SCHPO	mcm3	physical	9366552
XPO1_SCHPO	crm1	genetic	10588642
SPT16_YEAST	SPT16	physical	23499444
POB3_YEAST	POB3	physical	23499444
H2B1_YEAST	HTB1	physical	23499444
H2B2_YEAST	HTB2	physical	23499444
H3_YEAST	HHT1	physical	23499444

Drug and Disease Associations

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