HUA1_YEAST - dbPTM
HUA1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID HUA1_YEAST
UniProt AC P40325
Protein Name Proline-rich protein HUA1
Gene Name HUA1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 198
Subcellular Localization Cytoplasm .
Protein Description May be involved in assembly and disassembly of the actin cytoskeleton..
Protein Sequence MSKDTHDDELPSYEDVIKEEERLQSQPPRPPRPAANLAQGHQSRPHQRPSTMPATSSSQTYAHSHSYTPTSSQPRPPPRPQQNPSLPWTYPPRFYCSKCGNTGYKLKNGRSCKSCWRRFAPQNNVVSAPTYYTNYTMPVYTNAWQGNRPLYVQPGDPRLGGVLCGECRGSGRTRFLLDEDICPLCHGVGRIITQPQRY
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------MSKDTHDDE
------CCCCCCCCC
38.9622814378
3Ubiquitination-----MSKDTHDDEL
-----CCCCCCCCCC
66.4024961812
18UbiquitinationPSYEDVIKEEERLQS
CCHHHHHHHHHHHHC
59.9412872131

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 HUA1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of HUA1_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 HUA1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RUP1_YEASTRUP1physical
17079730
RSP5_YEASTRSP5physical
17079730
HSE1_YEASTHSE1physical
17079730
UBP2_YEASTUBP2physical
17079730
RSP5_YEASTRSP5physical
11283351
RSP5_YEASTRSP5physical
18719252
DIG1_YEASTDIG1physical
18719252
HUA1_YEASTHUA1physical
18719252
CUE5_YEASTCUE5physical
18719252
UBX5_YEASTUBX5physical
18719252
ENT2_YEASTENT2physical
18719252
POP7_YEASTPOP7genetic
27708008
LCB2_YEASTLCB2genetic
27708008
CDC1_YEASTCDC1genetic
27708008
TSC11_YEASTTSC11genetic
27708008
ACT_YEASTACT1genetic
27708008
CDC12_YEASTCDC12genetic
27708008
VTI1_YEASTVTI1genetic
27708008
RNA1_YEASTRNA1genetic
27708008
NOG2_YEASTNOG2genetic
27708008
SGT1_YEASTSGT1genetic
27708008
BUR1_YEASTSGV1genetic
27708008
RABX5_HUMANRABGEF1physical
27107014
MED4_HUMANMED4physical
27107014
BIRC2_HUMANBIRC2physical
27107014
TNIP1_HUMANTNIP1physical
27107014
UBQL1_HUMANUBQLN1physical
27107014
CACO2_HUMANCALCOCO2physical
27107014
STAM2_HUMANSTAM2physical
27107014
OPTN_HUMANOPTNphysical
27107014
UBXN1_HUMANUBXN1physical
27107014
UBC_HUMANUBCphysical
27107014
WWP2_HUMANWWP2physical
27107014
DVL2_HUMANDVL2physical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of HUA1_YEAST

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Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"A proteomics approach to understanding protein ubiquitination.";
Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D.,Marsischky G., Roelofs J., Finley D., Gygi S.P.;
Nat. Biotechnol. 21:921-926(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-3 AND LYS-18, AND MASSSPECTROMETRY.

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