UniProt ID | GNP1_YEAST | |
---|---|---|
UniProt AC | P48813 | |
Protein Name | High-affinity glutamine permease | |
Gene Name | GNP1 | |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). | |
Sequence Length | 663 | |
Subcellular Localization |
Mitochondrion membrane Multi-pass membrane protein . |
|
Protein Description | High affinity transport of glutamine. Also transport Leu, Ser, Thr, Cys, Met and Asn.. | |
Protein Sequence | MTLGNRRHGRNNEGSSNMNMNRNDLDDVSHYEMKEIQPKEKQIGSIEPENEVEYFEKTVEKTIENMEYEGEHHASYLRRFIDSFRRAEGSHANSPDSSNSNGTTPISTKDSSSQLDNELNRKSSYITVDGIKQSPQEQEQKQENLKKSIKPRHTVMMSLGTGIGTGLLVGNSKVLNNAGPGGLIIGYAIMGSCVYCIIQACGELAVIYSDLIGGFNTYPLFLVDPALGFSVAWLFCLQWLCVCPLELVTASMTIKYWTTSVNPDVFVVIFYVLIVVINVFGAKGYAEADFFFNCCKILMIVGFFILAIIIDCGGAGTDGYIGSKYWRDPGAFRGDTPIQRFKGVVATFVTAAFAFGMSEQLAMTASEQSNPRKAIPSAAKKMIYRILFVFLASLTLVGFLVPYTSDQLLGAAGSATKASPYVIAVSSHGVRVVPHFINAVILLSVLSVANGAFYTSSRILMSLAKQGNAPKCFDYIDREGRPAAAMLVSALFGVIAFCASSKKEEDVFTWLLAISGLSQLFTWITICLSHIRFRRAMKVQGRSLGEVGYKSQVGVWGSAYAVLMMVLALIAQFWVAIAPIGGGGKLSAQSFFENYLAMPIWIALYIFYKVWKKDWSLFIPADKVDLVSHRNIFDEELLKQEDEEYKERLRNGPYWKRVLDFWC | |
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 |
---|---|---|---|---|---|
2 | Phosphorylation | ------MTLGNRRHG ------CCCCCCCCC | 43.29 | 21551504 | |
15 | Phosphorylation | HGRNNEGSSNMNMNR CCCCCCCCCCCCCCC | 16.62 | 24909858 | |
16 | Phosphorylation | GRNNEGSSNMNMNRN CCCCCCCCCCCCCCC | 51.45 | 25704821 | |
29 | Phosphorylation | RNDLDDVSHYEMKEI CCCCCCCCHHHHHHC | 27.61 | 22369663 | |
31 | Phosphorylation | DLDDVSHYEMKEIQP CCCCCCHHHHHHCCC | 15.37 | 22890988 | |
34 | Acetylation | DVSHYEMKEIQPKEK CCCHHHHHHCCCCCC | 39.46 | 24489116 | |
34 | Ubiquitination | DVSHYEMKEIQPKEK CCCHHHHHHCCCCCC | 39.46 | 23749301 | |
39 | Ubiquitination | EMKEIQPKEKQIGSI HHHHCCCCCCCCCCC | 62.26 | 24961812 | |
41 | Ubiquitination | KEIQPKEKQIGSIEP HHCCCCCCCCCCCCC | 54.03 | 23749301 | |
41 | Acetylation | KEIQPKEKQIGSIEP HHCCCCCCCCCCCCC | 54.03 | 24489116 | |
45 | Phosphorylation | PKEKQIGSIEPENEV CCCCCCCCCCCCCHH | 25.96 | 21440633 | |
57 | Ubiquitination | NEVEYFEKTVEKTIE CHHHHHHHHHHHHHH | 48.23 | 23749301 | |
57 | Acetylation | NEVEYFEKTVEKTIE CHHHHHHHHHHHHHH | 48.23 | 24489116 | |
61 | Ubiquitination | YFEKTVEKTIENMEY HHHHHHHHHHHCCCC | 50.93 | 23749301 | |
61 | Acetylation | YFEKTVEKTIENMEY HHHHHHHHHHHCCCC | 50.93 | 24489116 | |
94 | Phosphorylation | AEGSHANSPDSSNSN HCCCCCCCCCCCCCC | 30.76 | 23749301 | |
97 | Phosphorylation | SHANSPDSSNSNGTT CCCCCCCCCCCCCCC | 34.50 | 19779198 | |
100 | Phosphorylation | NSPDSSNSNGTTPIS CCCCCCCCCCCCCCC | 38.29 | 22369663 | |
103 | Phosphorylation | DSSNSNGTTPISTKD CCCCCCCCCCCCCCC | 33.38 | 22369663 | |
104 | Phosphorylation | SSNSNGTTPISTKDS CCCCCCCCCCCCCCC | 21.74 | 22369663 | |
107 | Phosphorylation | SNGTTPISTKDSSSQ CCCCCCCCCCCCHHH | 30.52 | 22369663 | |
108 | Phosphorylation | NGTTPISTKDSSSQL CCCCCCCCCCCHHHH | 39.32 | 24909858 | |
109 | Ubiquitination | GTTPISTKDSSSQLD CCCCCCCCCCHHHHC | 49.15 | 23749301 | |
111 | Phosphorylation | TPISTKDSSSQLDNE CCCCCCCCHHHHCHH | 33.18 | 22369663 | |
112 | Phosphorylation | PISTKDSSSQLDNEL CCCCCCCHHHHCHHH | 32.03 | 25521595 | |
113 | Phosphorylation | ISTKDSSSQLDNELN CCCCCCHHHHCHHHH | 38.42 | 22369663 | |
122 | Ubiquitination | LDNELNRKSSYITVD HCHHHHHCCCCEEEC | 42.55 | 23749301 | |
123 | Phosphorylation | DNELNRKSSYITVDG CHHHHHCCCCEEECC | 25.74 | 22369663 | |
124 | Phosphorylation | NELNRKSSYITVDGI HHHHHCCCCEEECCC | 24.48 | 22369663 | |
125 | Phosphorylation | ELNRKSSYITVDGIK HHHHCCCCEEECCCC | 14.01 | 22890988 | |
127 | Phosphorylation | NRKSSYITVDGIKQS HHCCCCEEECCCCCC | 12.33 | 22369663 | |
132 | Ubiquitination | YITVDGIKQSPQEQE CEEECCCCCCHHHHH | 50.70 | 23749301 | |
134 | Phosphorylation | TVDGIKQSPQEQEQK EECCCCCCHHHHHHH | 24.45 | 28889911 | |
141 | Ubiquitination | SPQEQEQKQENLKKS CHHHHHHHHHHHHHH | 59.85 | 23749301 | |
146 | Ubiquitination | EQKQENLKKSIKPRH HHHHHHHHHHCCHHH | 56.93 | 22817900 | |
373 | Ubiquitination | SEQSNPRKAIPSAAK HHCCCHHHCCCHHHH | 52.50 | 23749301 | |
465 | Ubiquitination | RILMSLAKQGNAPKC HHHHHHHHCCCCCCH | 65.12 | 23749301 | |
471 | Ubiquitination | AKQGNAPKCFDYIDR HHCCCCCCHHHHHCC | 45.16 | 23749301 | |
639 | Acetylation | IFDEELLKQEDEEYK CCCHHHHHHCCHHHH | 65.35 | 24489116 | |
646 | Acetylation | KQEDEEYKERLRNGP HHCCHHHHHHHHHCH | 39.37 | 24489116 | |
646 | Ubiquitination | KQEDEEYKERLRNGP HHCCHHHHHHHHHCH | 39.37 | 24961812 | |
663 | S-palmitoylation | KRVLDFWC------- HHHHHHCC------- | 3.95 | 16751107 |
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 GNP1_YEAST !! |
Modified Location | Modified Residue | Modification | Function | Reference | ||
---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of GNP1_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 GNP1_YEAST !! |
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-29; SER-124 AND THR-127,AND MASS SPECTROMETRY. | |
"Proteome-wide identification of in vivo targets of DNA damagecheckpoint kinases."; Smolka M.B., Albuquerque C.P., Chen S.H., Zhou H.; Proc. Natl. Acad. Sci. U.S.A. 104:10364-10369(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123 AND SER-124, ANDMASS SPECTROMETRY. | |
"Large-scale phosphorylation analysis of alpha-factor-arrestedSaccharomyces cerevisiae."; Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,Elias J.E., Gygi S.P.; J. Proteome Res. 6:1190-1197(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND THR-127, ANDMASS SPECTROMETRY. | |
"Phosphoproteome analysis by mass spectrometry and its application toSaccharomyces cerevisiae."; Ficarro S.B., McCleland M.L., Stukenberg P.T., Burke D.J., Ross M.M.,Shabanowitz J., Hunt D.F., White F.M.; Nat. Biotechnol. 20:301-305(2002). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-124 AND THR-127, ANDMASS SPECTROMETRY. | |
Ubiquitylation | |
Reference | PubMed |
"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-34; LYS-41 AND LYS-132,AND MASS SPECTROMETRY. |