MCM1_YEAST - dbPTM
MCM1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MCM1_YEAST
UniProt AC P11746
Protein Name Pheromone receptor transcription factor
Gene Name MCM1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 286
Subcellular Localization Nucleus.
Protein Description Transcription factor required for the efficient replication of minichromosomes and the transcriptional regulation of early cell cycle genes. Activates transcription of ECB-dependent genes during the G1/M phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. Interacts with the alpha-2 repressor or with the alpha-1 activator thereby regulating the expression of mating-type-specific genes. With ARG80, ARG81 and ARG82, coordinates the expression of arginine anabolic and catabolic genes in response to arginine..
Protein Sequence MSDIEEGTPTNNGQQKERRKIEIKFIENKTRRHVTFSKRKHGIMKKAFELSVLTGTQVLLLVVSETGLVYTFSTPKFEPIVTQQEGRNLIQACLNAPDDEEEDEEEDGDDDDDDDDDGNDMQRQQPQQQQPQQQQQVLNAHANSLGHLNQDQVPAGALKQEVKSQLLGGANPNQNSMIQQQQHHTQNSQPQQQQQQQPQQQMSQQQMSQHPRPQQGIPHPQQSQPQQQQQQQQQLQQQQQQQQQQPLTGIHQPHQQAFANAASPYLNAEQNAAYQQYFQEPQQGQY
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
2Acetylation------MSDIEEGTP
------CCCCCCCCC
47.5022814378
2Phosphorylation------MSDIEEGTP
------CCCCCCCCC
47.5022369663
8PhosphorylationMSDIEEGTPTNNGQQ
CCCCCCCCCCCCCCC
30.1622369663
10PhosphorylationDIEEGTPTNNGQQKE
CCCCCCCCCCCCCCC
40.9522369663
35PhosphorylationNKTRRHVTFSKRKHG
CCCCCCEEECHHHCC
18.9621177495
82PhosphorylationPKFEPIVTQQEGRNL
CCCCCCCCHHHHHHH
25.8427214570
144PhosphorylationVLNAHANSLGHLNQD
HHHHHHHHHHCCCCC
36.1923810556

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 MCM1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MCM1_YEAST !!

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 MCM1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MCM7_YEASTMCM7physical
12738768
FKH2_YEASTFKH2physical
10959837
FKH2_YEASTFKH2physical
10899128
FKH2_YEASTFKH2physical
10894549
STE12_YEASTSTE12physical
1756728
MTAL1_YEASTHMLALPHA1physical
8139556
HMAL1_YEASTHMLALPHA1physical
8139556
STE12_YEASTSTE12physical
8139556
ARGR1_YEASTARG80physical
10632874
ARGR2_YEASTARG81physical
10632874
IPMK_YEASTARG82physical
10632874
MCM1_YEASTMCM1physical
10632874
YOX1_YEASTYOX1physical
12464633
YHP1_YEASTYHP1physical
12464633
MTAL2_YEASTHMLALPHA2physical
9490409
HMAL2_YEASTHMLALPHA2physical
9490409
PGM1_YEASTPGM1genetic
7623855
H4_YEASTHHF1physical
16554755
BOP3_YEASTBOP3physical
16554755
SNF5_YEASTSNF5physical
19233144
SNF6_YEASTSNF6physical
19233144
NDD1_YEASTNDD1genetic
10207056
YOX1_YEASTYOX1physical
20385087
FKH2_YEASTFKH2physical
20385087
MCM7_YEASTMCM7genetic
12738768

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MCM1_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2; THR-8 AND SER-144,AND MASS SPECTROMETRY.

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