CDC31_YEAST - dbPTM
CDC31_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CDC31_YEAST
UniProt AC P06704
Protein Name Cell division control protein 31
Gene Name CDC31
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 161
Subcellular Localization Nucleus, nuclear pore complex. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Spindle pole body, SPB half- bridge.
Protein Description Functions as a component of the nuclear pore complex (NPC) and the spindle pole body (SPB) half-bridge. At the SPB, it is recruited by KAR1 and MPS3 to the SPB half-bridge and involved in the initial steps of SPB duplication. It probably plays a similar role in de novo assembly of NPCs at the nuclear envelope. Also involved in connection with the protein kinase KIC1 in the maintenance of cell morphology and integrity..
Protein Sequence MSKNRSSLQSGPLNSELLEEQKQEIYEAFSLFDMNNDGFLDYHELKVAMKALGFELPKREILDLIDEYDSEGRHLMKYDDFYIVMGEKILKRDPLDEIKRAFQLFDDDHTGKISIKNLRRVAKELGETLTDEELRAMIEEFDLDGDGEINENEFIAICTDS
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
6Phosphorylation--MSKNRSSLQSGPL
--CCCCHHHHHCCCC
44.8122369663
7Phosphorylation-MSKNRSSLQSGPLN
-CCCCHHHHHCCCCC
27.4722369663
10PhosphorylationKNRSSLQSGPLNSEL
CCHHHHHCCCCCHHH
47.9022369663
15PhosphorylationLQSGPLNSELLEEQK
HHCCCCCHHHHHHHH
36.9921700874
70PhosphorylationDLIDEYDSEGRHLMK
HHHHHCCCCCCCCCC
40.8419779198
110PhosphorylationQLFDDDHTGKISIKN
HHHCCCCCCCEEHHH
47.3628889911
128PhosphorylationVAKELGETLTDEELR
HHHHHHCCCCHHHHH
32.9122369663
130PhosphorylationKELGETLTDEELRAM
HHHHCCCCHHHHHHH
49.1122369663
161PhosphorylationFIAICTDS-------
EEEEEECC-------
24.7821700874

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 CDC31_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CDC31_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 CDC31_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HEMH_YEASTHEM15physical
14504268
SFI1_YEASTSFI1physical
14504268
THP1_YEASTTHP1physical
14504268
KAR1_YEASTKAR1physical
8910460
KAR1_YEASTKAR1physical
7876310
SAC3_YEASTSAC3physical
15311284
THP1_YEASTTHP1physical
15311284
SUS1_YEASTSUS1physical
15311284
KIC1_YEASTKIC1physical
9813095
VPS13_YEASTVPS13physical
14504268
KPC1_YEASTPKC1genetic
10924456
SLG1_YEASTSLG1genetic
10924456
KAR1_YEASTKAR1genetic
11156974
MPS1_YEASTMPS1genetic
8567717
KAR1_YEASTKAR1genetic
8070654
KIC1_YEASTKIC1genetic
9813095
SAC3_YEASTSAC3physical
16554755
SEM1_YEASTSEM1physical
16554755
STM1_YEASTSTM1physical
16554755
NBP1_YEASTNBP1genetic
16436507
RAD4_YEASTRAD4physical
18160718
RAD23_YEASTRAD23physical
18160718
PRS7_YEASTRPT1physical
18160718
PSB5_YEASTPRE2physical
18160718
RPN12_YEASTRPN12physical
18160718
PRS10_YEASTRPT4physical
18160718
PRS8_YEASTRPT6physical
18160718
SAC3_YEASTSAC3physical
19269973
SUS1_YEASTSUS1physical
19269973
KAR1_YEASTKAR1genetic
20368617
KAR1_YEASTKAR1physical
21714500
SFI1_YEASTSFI1physical
21714500
SAC3_YEASTSAC3physical
21714500
VPS13_YEASTVPS13physical
28122955

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CDC31_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 THR-130, AND MASSSPECTROMETRY.

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