YCT1_YEAST - dbPTM
YCT1_YEAST - PTM Information in dbPTM
Basic Information of Protein
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
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure
ASA (%) Reference Orthologous
Protein Cluster
12PhosphorylationDVKIGADSISSSDEI
CEEECCCCCCCCCCE
24.6825005228
14PhosphorylationKIGADSISSSDEILV
EECCCCCCCCCCEEC
27.9525005228
15PhosphorylationIGADSISSSDEILVP
ECCCCCCCCCCEECC
39.8925005228
16PhosphorylationGADSISSSDEILVPS
CCCCCCCCCCEECCH
32.2625005228
146N-linked_GlycosylationFLSCTAYNFSGVVAL
HHHCCCCCCCHHHHH
23.34-
265PhosphorylationIRRVQASTGSSIEQK
EEHHHHCCCCCHHHH
44.0628889911
267PhosphorylationRVQASTGSSIEQKVF
HHHHCCCCCHHHHHH
28.3828889911
286PhosphorylationFREAMKDYITWLFGL
HHHHHHHHHHHHHHH
8.5028889911
288PhosphorylationEAMKDYITWLFGLFF
HHHHHHHHHHHHHHH
15.1928889911
323PhosphorylationGGVDALGSTLVSVAG
CHHHCCHHHHHHHHH
21.3028889911
324PhosphorylationGVDALGSTLVSVAGA
HHHCCHHHHHHHHHH
29.4028889911
342PhosphorylationVVCAFIATLMLAKWK
HHHHHHHHHHHHHHC
14.1028889911
496PhosphorylationDRIQLIESENPSSIE
HHHHHHHCCCCCCCC
35.3628889911
500PhosphorylationLIESENPSSIEEGKV
HHHCCCCCCCCCCCE
56.3728152593
501PhosphorylationIESENPSSIEEGKVV
HHCCCCCCCCCCCEE
34.9625005228

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 YCT1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of YCT1_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 YCT1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPO1_YEASTTPO1genetic
16269340
CYPD_YEASTCPR5genetic
16269340
TLG2_YEASTTLG2genetic
16269340
PLMT_YEASTOPI3genetic
16269340
HLJ1_YEASTHLJ1genetic
16269340
CND2_YEASTBRN1genetic
27708008
CDC10_YEASTCDC10genetic
27708008
TFB1_YEASTTFB1genetic
27708008
UTP5_YEASTUTP5genetic
27708008
CDC12_YEASTCDC12genetic
27708008
MET30_YEASTMET30genetic
27708008
KTHY_YEASTCDC8genetic
27708008
CDC11_YEASTCDC11genetic
27708008
SEC65_YEASTSEC65genetic
27708008
PROF_YEASTPFY1genetic
27708008

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of YCT1_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-496 AND SER-500, ANDMASS SPECTROMETRY.

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