UniProt ID | YCT1_YEAST | |
---|---|---|
UniProt AC | Q12235 | |
Protein Name | High affinity cysteine transporter | |
Gene Name | YCT1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 531 | |
Subcellular Localization |
Cell membrane Multi-pass membrane protein. Endoplasmic reticulum membrane Multi-pass membrane protein. |
|
Protein Description | High affinity cysteine-specific transporter. Major contributor to cysteine transport when cysteine, at low concentrations, is provided as the sole sulfur source.. | |
Protein Sequence | MSKVDVKIGADSISSSDEILVPSRLADVTLAFMEENDAAVPEITPEQEKKLKRKLFLTIFTFVSAINLLLYMDKATLSYDSILGFFEDTGLTQNTYNTVNTLFYVGFAIGQFPGQYLAQKLPLGKFLGGLLATWTILIFLSCTAYNFSGVVALRFFLGLTESVVIPILITTMGMFFDASERAAAQPFFFAACMGSPIPTGFIAYGVLHITNPSISLWKIFTIIIGGLTFIMTVVVILWFPNNPADVKFFSIQERVWIIRRVQASTGSSIEQKVFKKSQFREAMKDYITWLFGLFFLLQQLANNLPYQQNLLFEGMGGVDALGSTLVSVAGAGFAVVCAFIATLMLAKWKNISALTAIFWTLPALVGSIAAAALPWDNKIGILANICMAGQIFGIPFIIALSWASSSASGYTKKLTRSSVSLFAMGIANIISPQIWREKDSPRFLPAWIVQIVLSFSLAPAILLLIHFILKRRNNQRLKNYDENLQNYLDRIQLIESENPSSIEEGKVVTHENNLAVFDLTDLENETFIYPL | |
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 |
---|---|---|---|---|---|
12 | Phosphorylation | DVKIGADSISSSDEI CEEECCCCCCCCCCE | 24.68 | 25005228 | |
14 | Phosphorylation | KIGADSISSSDEILV EECCCCCCCCCCEEC | 27.95 | 25005228 | |
15 | Phosphorylation | IGADSISSSDEILVP ECCCCCCCCCCEECC | 39.89 | 25005228 | |
16 | Phosphorylation | GADSISSSDEILVPS CCCCCCCCCCEECCH | 32.26 | 25005228 | |
146 | N-linked_Glycosylation | FLSCTAYNFSGVVAL HHHCCCCCCCHHHHH | 23.34 | - | |
265 | Phosphorylation | IRRVQASTGSSIEQK EEHHHHCCCCCHHHH | 44.06 | 28889911 | |
267 | Phosphorylation | RVQASTGSSIEQKVF HHHHCCCCCHHHHHH | 28.38 | 28889911 | |
286 | Phosphorylation | FREAMKDYITWLFGL HHHHHHHHHHHHHHH | 8.50 | 28889911 | |
288 | Phosphorylation | EAMKDYITWLFGLFF HHHHHHHHHHHHHHH | 15.19 | 28889911 | |
323 | Phosphorylation | GGVDALGSTLVSVAG CHHHCCHHHHHHHHH | 21.30 | 28889911 | |
324 | Phosphorylation | GVDALGSTLVSVAGA HHHCCHHHHHHHHHH | 29.40 | 28889911 | |
342 | Phosphorylation | VVCAFIATLMLAKWK HHHHHHHHHHHHHHC | 14.10 | 28889911 | |
496 | Phosphorylation | DRIQLIESENPSSIE HHHHHHHCCCCCCCC | 35.36 | 28889911 | |
500 | Phosphorylation | LIESENPSSIEEGKV HHHCCCCCCCCCCCE | 56.37 | 28152593 | |
501 | Phosphorylation | IESENPSSIEEGKVV HHCCCCCCCCCCCEE | 34.96 | 25005228 |
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 YCT1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of YCT1_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 YCT1_YEAST !! |
Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
---|---|---|---|---|
TPO1_YEAST | TPO1 | genetic | 16269340 | |
CYPD_YEAST | CPR5 | genetic | 16269340 | |
TLG2_YEAST | TLG2 | genetic | 16269340 | |
PLMT_YEAST | OPI3 | genetic | 16269340 | |
HLJ1_YEAST | HLJ1 | genetic | 16269340 | |
CND2_YEAST | BRN1 | genetic | 27708008 | |
CDC10_YEAST | CDC10 | genetic | 27708008 | |
TFB1_YEAST | TFB1 | genetic | 27708008 | |
UTP5_YEAST | UTP5 | genetic | 27708008 | |
CDC12_YEAST | CDC12 | genetic | 27708008 | |
MET30_YEAST | MET30 | genetic | 27708008 | |
KTHY_YEAST | CDC8 | genetic | 27708008 | |
CDC11_YEAST | CDC11 | genetic | 27708008 | |
SEC65_YEAST | SEC65 | genetic | 27708008 | |
PROF_YEAST | PFY1 | genetic | 27708008 |
Kegg Drug | ||||||
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DrugBank | ||||||
There are no disease associations of PTM sites. |
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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 SER-496 AND SER-500, ANDMASS SPECTROMETRY. |