UniProt ID | HMF1_YEAST | |
---|---|---|
UniProt AC | P40037 | |
Protein Name | Protein HMF1 | |
Gene Name | HMF1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 129 | |
Subcellular Localization | Cytoplasm. Nucleus. Mitochondrion intermembrane space . | |
Protein Description | ||
Protein Sequence | MVTTLTPVICESAPAAAASYSHAMKVNNLIFLSGQIPVTPDNKLVEGSIADKAEQVIQNIKNVLEASNSSLDRVVKVNIFLADINHFAEFNSVYAKYFNTHKPARSCVAVAALPLGVDMEMEAIAAERD | |
Overview of Protein Modification Sites with Functional and Structural Information | ||
* ASA = Accessible Surface Area
Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
---|---|---|---|---|---|
3 | Phosphorylation | -----MVTTLTPVIC -----CCCCCCCEEE | 18.13 | 28889911 | |
4 | Phosphorylation | ----MVTTLTPVICE ----CCCCCCCEEEC | 19.75 | 28889911 | |
6 | Phosphorylation | --MVTTLTPVICESA --CCCCCCCEEECCC | 17.26 | 21082442 | |
12 | Phosphorylation | LTPVICESAPAAAAS CCCEEECCCHHHHHH | 34.83 | 30377154 | |
19 | Phosphorylation | SAPAAAASYSHAMKV CCHHHHHHCCHHHHC | 23.57 | 30377154 | |
20 | Phosphorylation | APAAAASYSHAMKVN CHHHHHHCCHHHHCC | 10.35 | 28132839 | |
21 | Phosphorylation | PAAAASYSHAMKVNN HHHHHHCCHHHHCCC | 11.41 | 30377154 | |
52 | Ubiquitination | VEGSIADKAEQVIQN CCCCHHHHHHHHHHH | 44.81 | 23749301 | |
52 | Acetylation | VEGSIADKAEQVIQN CCCCHHHHHHHHHHH | 44.81 | 24489116 | |
61 | Ubiquitination | EQVIQNIKNVLEASN HHHHHHHHHHHHHCC | 48.86 | 24961812 | |
61 | Acetylation | EQVIQNIKNVLEASN HHHHHHHHHHHHHCC | 48.86 | 24489116 | |
102 | Ubiquitination | AKYFNTHKPARSCVA HHHHCCCCCHHHEEE | 38.03 | 23749301 | |
102 | Acetylation | AKYFNTHKPARSCVA HHHHCCCCCHHHEEE | 38.03 | 22865919 |
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 HMF1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of HMF1_YEAST !! |
* 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 HMF1_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
RPA34_YEAST | RPA34 | physical | 18467557 | |
RU2A_YEAST | LEA1 | genetic | 27708008 | |
KPYK1_YEAST | CDC19 | genetic | 27708008 | |
CALM_YEAST | CMD1 | genetic | 27708008 | |
MAK5_YEAST | MAK5 | genetic | 27708008 | |
DBF4_YEAST | DBF4 | genetic | 27708008 | |
LCB2_YEAST | LCB2 | genetic | 27708008 | |
CDC37_YEAST | CDC37 | genetic | 27708008 | |
TFB1_YEAST | TFB1 | genetic | 27708008 | |
PSF2_YEAST | PSF2 | genetic | 27708008 | |
CDC11_YEAST | CDC11 | genetic | 27708008 | |
MED14_YEAST | RGR1 | genetic | 27708008 | |
NEP1_YEAST | EMG1 | genetic | 27708008 | |
SMC6_YEAST | SMC6 | genetic | 27708008 | |
BET5_YEAST | BET5 | genetic | 27708008 | |
UTP15_YEAST | UTP15 | genetic | 27708008 | |
CBF3B_YEAST | CEP3 | genetic | 27708008 | |
AIM3_YEAST | AIM3 | genetic | 27708008 | |
RS6A_YEAST | RPS6B | genetic | 27708008 | |
RS6B_YEAST | RPS6B | genetic | 27708008 | |
STE50_YEAST | STE50 | genetic | 27708008 | |
MTU1_YEAST | SLM3 | genetic | 27708008 | |
YD056_YEAST | YDR056C | genetic | 27708008 | |
FMP16_YEAST | FMP16 | genetic | 27708008 | |
SAC7_YEAST | SAC7 | genetic | 27708008 | |
SNF6_YEAST | SNF6 | genetic | 27708008 | |
ACA2_YEAST | CST6 | genetic | 27708008 | |
YIQ5_YEAST | YIL165C | genetic | 27708008 | |
DHOM_YEAST | HOM6 | genetic | 27708008 | |
SRL3_YEAST | SRL3 | genetic | 27708008 |
Kegg Drug | ||||||
---|---|---|---|---|---|---|
DrugBank | ||||||
There are no disease associations of PTM sites. |
loading...
Phosphorylation | |
Reference | PubMed |
"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-3, AND MASSSPECTROMETRY. |