MCM6_SCHPO - dbPTM
MCM6_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCM6_SCHPO
UniProt AC P49731
Protein Name DNA replication licensing factor mcm6
Gene Name mcm6
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 892
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)..
Protein Sequence MSSLASQGNNASTPAYRYGFQTSEVGDRPTVSMPSQPESSAMLEDDGMVKRKPFAAIGEAIPKVIDTTGESVREAFEEFLLSFSDDRVAGGDALPSASQEKYYVQQIHGLAMYEIHTVYVDYKHLTSYNDVLALAIVEQYYRFSPFLLRALQKLIEKFEPEYYRSSLSRENASLSPNFKASDKTFALAFYNLPFRSTIRDLRTDRIGRLTTITGTVTRTSEVRPELAQGTFICEECHTVVSNVEQAFRYTEPTQCPNELCANKRSWRLNISQSSFQDWQKVRIQENSNEIPTGSMPRTLDVILRGDIVERAKAGDKCAFTGILIAVPDVSQLGIPGVKPEAYRDSRNFGGRDADGVTGLKSLGVRDLTYKLSFLACMVQPDDANDKSGADVRGDGSQGIEEQDEFLQSLSQEEIDDLRAMVHSDHIYSRLTNSLAPSVYGHEIIKKGILLQLMGGVHKLTPEGINLRGDLNICIVGDPSTSKSQFLKYVCNFLPRAIYTSGKASSAAGLTAAVVKDEETGDFTIEAGALMLADNGICAIDEFDKMDLSDQVAIHEAMEQQTISIAKAGIQATLNARTSILAAANPIGGRYNRKTTLRNNINMSAPIMSRFDLFFVVLDECNESVDRHLAKHIVDIHRLRDDAMQPEFSTEQLQRYIRYARTFKPKLNTESCAEIVKKYKQLRMDDAQGAGKNSYRITVRQLESMIRLSEAIARANCVDDITPAFVNEAYSLLRQSIIHVERDDIEVEEDDAEAQELENDNTNTTNGNDNVSSEEALQKPKVKITYDKYVSIMNGILQVLRQRSTEGVDGVPAGDLVQSYLELREDQFHTEEDIIYEVGLVRKVLTRLVHESIIMEIQNLTDSAVRLPFEERVFSIHPNCDIDALLSNGDVPN
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 Orthologous
Protein Cluster
39PhosphorylationSMPSQPESSAMLEDD
CCCCCCCCCCCCCCC
30.0427738172
96PhosphorylationAGGDALPSASQEKYY
CCCCCCCCHHHHHHH
41.2128889911
98PhosphorylationGDALPSASQEKYYVQ
CCCCCCHHHHHHHHH
43.1228889911

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

Oops, there are no upstream regulatory protein records of MCM6_SCHPO !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCM6_SCHPO !!

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 MCM6_SCHPO !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CUT1_SCHPOcut1genetic
15507118
DIS1_SCHPOdis1genetic
15507118
ALP14_SCHPOalp14genetic
15507118
MCM2_SCHPOmcm2physical
9658174
MCM7_SCHPOmcm7physical
11136247
CDC45_SCHPOcdc45physical
15338237
CDT1_SCHPOcdt1genetic
21971174
CDC18_SCHPOcdc18genetic
21971174
CDT1_SCHPOcdt1physical
21971174
CG22_SCHPOcig2genetic
21971174
CDC45_SCHPOcdc45physical
12006645
CG22_SCHPOcig2genetic
15194812
RUM1_SCHPOrum1genetic
15194812
SLD3_SCHPOsld3physical
15194812
MCM2_SCHPOmcm2genetic
15507118
BIR1_SCHPObir1genetic
15507118
H31_SCHPOhht3genetic
15507118
H4_SCHPOhhf3genetic
15507118
MCM7_SCHPOmcm7physical
23444842
MCM6_SCHPOmcm6physical
23444842
HAP2_SCHPOphp2physical
26771498
MCM3_SCHPOmcm3physical
26771498

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCM6_SCHPO

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of fission yeast.";
Wilson-Grady J.T., Villen J., Gygi S.P.;
J. Proteome Res. 7:1088-1097(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-96 AND SER-98, AND MASSSPECTROMETRY.

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