MCM10_SCHPO - dbPTM
MCM10_SCHPO - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCM10_SCHPO
UniProt AC O42709
Protein Name DNA replication licensing factor mcm10
Gene Name mcm10
Organism Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Sequence Length 593
Subcellular Localization Nucleus . Associates with chromatin.
Protein Description Required for DNA synthesis. Required for entry into or completion of S phase. Involved in DNA replication and seems to participate in the activation of the pre-replication complex (pre-RC) and in transcription elongation. May play a role as key coordinator in assembling the replication fork. Proposed to function at replication origins following the binding of the mcm2-7 complex prior to the recruitment of sna41. Probably is required to stimulate phosphorylation of the mcm2-7 complex by the dfp1-hsk1 kinase complex. May recruit the DNA polymerase alpha:primase complex to replication origins and is required to maintain it on chromatin independently of sna41. May have primase activity. Binds to single-stranded DNA..
Protein Sequence MHDPFIAEENDLDLEEKRLQRQLNEIQEKKRLRSAQKEASSENAEVIQVPRSPPQQVRVLTVSSPSKLKSPKRLILGIDKGKTGKDVSLGKGPRGPLPKPFHERLAEARNQERKRSDKLKTMKKNRKQSFQRKRNILEDGKSEEEKFPMKCDEIDPYSRQAIVIRYISDEVAKENIGGNQVYLIHQLLKLVRAPKFEAPEVDNYVVMGIVASNSGTRETVNGNKYCMLTLTDLKWQLECFLFGKAFERYWKIQSGTVIALLNPEVLKPKNPDIGRFSLKLDSEYDVLLEIGRSKHLGYCSSRRKSGELCKHWLDKRAGDVCEYHVDLAVQRSMSTRTEFASSMATMHEPRARREKRFRGQGFQGYFAGEKYSAIPNAVAGLYDAEDAVQTERERKERYKKQRAQAEREREILVRLSKRCCASSSSSSNSNNLSTGMSMRTLGHQYLNLQGSGVKNLHDKGNPTALSKDSEIDSSTKKPSVLASFNASIMNPKSSLPSFSNSAILGTNDAASGTPVPQDTTSTKVSPAVVFTSSPRIFSPQSLRKIGFDPTHSADASTTHSTATGLSRSGSLKNIKFRYEFTESDDEDDLEIVP
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
41PhosphorylationSAQKEASSENAEVIQ
HHHHHHHHCCCEEEE		41.7521712547
52PhosphorylationEVIQVPRSPPQQVRV
EEEECCCCCCCCEEE		34.5625720772
61PhosphorylationPQQVRVLTVSSPSKL
CCCEEEEEECCHHHC		18.5825720772
63PhosphorylationQVRVLTVSSPSKLKS
CEEEEEECCHHHCCC		31.1525720772
64PhosphorylationVRVLTVSSPSKLKSP
EEEEEECCHHHCCCC		28.9328889911
66PhosphorylationVLTVSSPSKLKSPKR
EEEECCHHHCCCCCE		53.2029996109
70PhosphorylationSSPSKLKSPKRLILG
CCHHHCCCCCEEEEE		46.2025720772
532PhosphorylationSPAVVFTSSPRIFSP
CCEEEEECCCCCCCH		27.2124763107
533PhosphorylationPAVVFTSSPRIFSPQ
CEEEEECCCCCCCHH		18.3624763107
538PhosphorylationTSSPRIFSPQSLRKI
ECCCCCCCHHHHHHC		21.4725720772
541PhosphorylationPRIFSPQSLRKIGFD
CCCCCHHHHHHCCCC		33.2621712547
560PhosphorylationADASTTHSTATGLSR
CCCCCCCCCCCCCCC		20.0421712547
561PhosphorylationDASTTHSTATGLSRS
CCCCCCCCCCCCCCC		22.1921712547
566PhosphorylationHSTATGLSRSGSLKN
CCCCCCCCCCCCCCC		26.2421712547
568PhosphorylationTATGLSRSGSLKNIK
CCCCCCCCCCCCCEE		29.3821712547
570PhosphorylationTGLSRSGSLKNIKFR
CCCCCCCCCCCEEEE		37.1021712547
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 MCM10_SCHPO !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCM10_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 MCM10_SCHPO !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RAD3_SCHPOrad3genetic
11606526
HSK1_SCHPOhsk1genetic
11606526
RAD4_SCHPOrad4genetic
11606526
MCM2_SCHPOmcm2genetic
12185500
MCM6_SCHPOmcm6genetic
12185500
CBH2_SCHPOcbh2genetic
17112379
CBH1_SCHPOcbh1genetic
17112379
ABP1_SCHPOcbp1genetic
17112379
HSK1_SCHPOhsk1physical
12604790
MCM3_SCHPOmcm3physical
12604790
MCM2_SCHPOmcm2physical
12604790
MCM6_SCHPOmcm6physical
12185500
ORC1_SCHPOorc1physical
12185500
ORC2_SCHPOorc2physical
12185500
ORC5_SCHPOorc5physical
12185500
ORC6_SCHPOorc6physical
12185500
ABP1_SCHPOcbp1physical
17112379
HIM1_SCHPOdfp1physical
12604790
MMS22_SCHPOmus7genetic
17660542
RAD4_SCHPOrad4physical
21945095
PSF1_SCHPOpsf1physical
22433840
CDC45_SCHPOcdc45physical
22433840
DPOA_SCHPOpol1physical
22433840
DPOD_SCHPOcdc6physical
22433840
MCM2_SCHPOmcm2physical
22433840
MCM6_SCHPOmcm6physical
22433840
SLD5_SCHPOsld5physical
22433840
PSF2_SCHPOpsf2physical
22433840
RAD4_SCHPOrad4physical
22433840
MCM10_SCHPOcdc23physical
22433840
PSF3_SCHPOpsf3physical
22433840
DPOE_SCHPOcdc20physical
22433840
SLD2_SCHPOdrc1physical
22433840
DPB2_SCHPOdpb2physical
22433840
HUS2_SCHPOrqh1genetic
9891047
MCM10_SCHPOcdc23physical
23583778
MCM6_SCHPOmcm6physical
23695164
NU211_SCHPOnup211physical
23695164
CBH2_SCHPOcbh2physical
26771498
YH7G_SCHPOSPBC16G5.16physical
26771498
MCM6_SCHPOmcm6physical
26771498
YGNB_SCHPOnap2physical
26771498
CSK2C_SCHPOckb2physical
26771498
TAS3_SCHPOtas3physical
26771498
YHI5_SCHPOabo2physical
26771498
SEC6_SCHPOsec6physical
26771498
NU211_SCHPOnup211physical
26771498
YQO1_SCHPOSPCC569.01cphysical
26771498
PIL1_SCHPOpil1physical
26771498
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCM10_SCHPO

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Related Literatures of Post-Translational Modification

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