GAP1_YEAST - dbPTM
GAP1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GAP1_YEAST
UniProt AC P19145
Protein Name General amino-acid permease GAP1 {ECO:0000303|PubMed:5474888}
Gene Name GAP1 {ECO:0000303|PubMed:5474888}
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 602
Subcellular Localization Cell membrane
Multi-pass membrane protein . Endoplasmic reticulum membrane
Multi-pass membrane protein . Depending on nitrogen source, GAP1 is transported to the plasma membrane, where it functions for amino acid uptake, or to the vacuole, where
Protein Description General amino-acid permease involved in the uptake of all the naturally occurring L-amino-acids, related compounds such as ornithine and citrulline, some D-amino acids, toxic amino acid analogs such as azetidine-2-carboxylate, and the polyamines putrescine and spermidine. [PubMed: 5474888]
Protein Sequence MSNTSSYEKNNPDNLKHNGITIDSEFLTQEPITIPSNGSAVSIDETGSGSKWQDFKDSFKRVKPIEVDPNLSEAEKVAIITAQTPLKHHLKNRHLQMIAIGGAIGTGLLVGSGTALRTGGPASLLIGWGSTGTMIYAMVMALGELAVIFPISGGFTTYATRFIDESFGYANNFNYMLQWLVVLPLEIVSASITVNFWGTDPKYRDGFVALFWLAIVIINMFGVKGYGEAEFVFSFIKVITVVGFIILGIILNCGGGPTGGYIGGKYWHDPGAFAGDTPGAKFKGVCSVFVTAAFSFAGSELVGLAASESVEPRKSVPKAAKQVFWRITLFYILSLLMIGLLVPYNDKSLIGASSVDAAASPFVIAIKTHGIKGLPSVVNVVILIAVLSVGNSAIYACSRTMVALAEQRFLPEIFSYVDRKGRPLVGIAVTSAFGLIAFVAASKKEGEVFNWLLALSGLSSLFTWGGICICHIRFRKALAAQGRGLDELSFKSPTGVWGSYWGLFMVIIMFIAQFYVAVFPVGDSPSAEGFFEAYLSFPLVMVMYIGHKIYKRNWKLFIPAEKMDIDTGRREVDLDLLKQEIAEEKAIMATKPRWYRIWNFWC
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
4Phosphorylation----MSNTSSYEKNN
----CCCCCCCCCCC		16.2527717283
5Phosphorylation---MSNTSSYEKNNP
---CCCCCCCCCCCC		34.8630377154
6Phosphorylation--MSNTSSYEKNNPD
--CCCCCCCCCCCCC		34.9627717283
7Phosphorylation-MSNTSSYEKNNPDN
-CCCCCCCCCCCCCC		30.5930377154
16UbiquitinationKNNPDNLKHNGITID
CCCCCCCCCCCEEEC		41.0824961812
42PhosphorylationPSNGSAVSIDETGSG
CCCCCEEEEECCCCC		24.8427214570
51UbiquitinationDETGSGSKWQDFKDS
ECCCCCCCCCHHHHH		53.0217644757
56UbiquitinationGSKWQDFKDSFKRVK
CCCCCHHHHHHHCCC		61.8317644757
60UbiquitinationQDFKDSFKRVKPIEV
CHHHHHHHCCCCEEC		61.3017644757
63UbiquitinationKDSFKRVKPIEVDPN
HHHHHCCCCEECCCC		44.2923793018
72PhosphorylationIEVDPNLSEAEKVAI
EECCCCCCHHHEEEE		41.2128889911
76UbiquitinationPNLSEAEKVAIITAQ
CCCCHHHEEEEEEEC		43.9723749301
87UbiquitinationITAQTPLKHHLKNRH
EEECCCCHHHHCCCC		30.1317644757
265UbiquitinationTGGYIGGKYWHDPGA
CCCCCCCCCCCCCCC		39.7017644757
281UbiquitinationAGDTPGAKFKGVCSV
CCCCCCCCCCHHHHH		54.2317644757
420UbiquitinationIFSYVDRKGRPLVGI
HHHHHCCCCCCCCEE		55.6017644757
491UbiquitinationGLDELSFKSPTGVWG
CCCCCCCCCCCCCHH		52.7517644757
578UbiquitinationEVDLDLLKQEIAEEK
EECHHHHHHHHHHHH		53.8617644757
585UbiquitinationKQEIAEEKAIMATKP
HHHHHHHHCHHHCCC		34.4217644757
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
-KUbiquitinationE3 ubiquitin ligaseRSP5P39940
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GAP1_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 GAP1_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GAS1_YEASTGAS1physical
12885760
SHR3_YEASTSHR3physical
15623581
PTR3_YEASTPTR3genetic
11489133
SSY5_YEASTSSY5genetic
11489133
AGP1_YEASTAGP1genetic
9891035
SSY1_YEASTSSY1genetic
9891035
SSY1_YEASTSSY1genetic
11489133
SAC3_YEASTSAC3genetic
10517330
ATC1_YEASTPMR1physical
17095607
SSY1_YEASTSSY1genetic
11356187
GRR1_YEASTGRR1genetic
11356187
YPT6_YEASTYPT6genetic
19398763
PMA1_YEASTPMA1physical
19398763
PMA1_YEASTPMA1physical
19748353
LYP1_YEASTLYP1genetic
16941010
LYS1_YEASTLYS1genetic
16941010
LYS2_YEASTLYS2genetic
16941010
LYS9_YEASTLYS9genetic
16941010
P5CR_YEASTPRO3genetic
16941010
PUT4_YEASTPUT4genetic
16941010
LYS12_YEASTLYS12genetic
16941010
HOSC_YEASTLYS20genetic
16941010
LYS4_YEASTLYS4genetic
16941010
PROB_YEASTPRO1genetic
16941010
KMO_YEASTBNA4genetic
16941010
I23O_YEASTBNA2genetic
16941010
KYNU_YEASTBNA5genetic
16941010
LST4_YEASTLST4genetic
18434603
AGP1_YEASTAGP1genetic
19906648
STP1_YEASTSTP1genetic
19906648
STP2_YEASTSTP2genetic
19906648
DAL81_YEASTDAL81genetic
19906648
STP1_YEASTSTP1genetic
15126393
SSY1_YEASTSSY1genetic
15126393
AGP1_YEASTAGP1genetic
15126393
DAL81_YEASTDAL81genetic
15126393
BUL2_YEASTBUL2genetic
11352928
BUL1_YEASTBUL1genetic
11352928
SHR3_YEASTSHR3physical
16093310
PHO88_YEASTPHO88physical
16093310
MKAR_YEASTIFA38physical
16093310
MST27_YEASTMST27physical
16093310
DIP5_YEASTDIP5genetic
20956561
CACM_YEASTYAT1genetic
21623372
PGM1_YEASTPGM1genetic
21623372
FOLE_YEASTMET7genetic
21623372
GSH1_YEASTGSH1genetic
21623372
ARE2_YEASTARE2genetic
21623372
AMDY_YEASTAMD2genetic
21623372
FABD_YEASTMCT1genetic
21623372
POS5_YEASTPOS5genetic
21623372
GLYC_YEASTSHM2genetic
21623372
GAS3_YEASTGAS3genetic
21623372
GRE3_YEASTGRE3genetic
21623372
INV2_YEASTSUC2genetic
21623372
DPM1_YEASTDPM1physical
21912684
BSC6_YEASTBSC6physical
21912684
NACA_YEASTEGD2physical
21912684
EFM6_YEASTYNL024Cphysical
21912684
YIT4_YEASTYIR014Wphysical
21912684
TED1_YEASTTED1physical
21912684
SRPB_YEASTSRP102physical
21912684
SPC2_YEASTSPC2physical
21912684
TPIS_YEASTTPI1physical
21912684
LIP1_YEASTLIP1physical
21912684
PIS_YEASTPIS1physical
21912684
SC61G_YEASTSSS1physical
21912684
NHX1_YEASTNHX1physical
21912684
CWP2_YEASTCWP2physical
21912684
PMP3_YEASTPMP3physical
21912684
FMP46_YEASTFMP46physical
21912684
FKS1_YEASTFKS1physical
21912684
HACD_YEASTPHS1physical
21912684
HXT2_YEASTHXT2physical
21912684
CBF5_YEASTCBF5physical
21912684
VATE_YEASTVMA4physical
21912684
GUP1_YEASTGUP1physical
21912684
PMT1_YEASTPMT1physical
21912684
VTC1_YEASTVTC1physical
21912684
VTC4_YEASTVTC4physical
21912684
PEP12_YEASTPEP12physical
21575114
PMA1_YEASTPMA1physical
21575114
GAS1_YEASTGAS1physical
21575114
BGL2_YEASTBGL2physical
21575114
AGP1_YEASTAGP1genetic
24701347
AGP1_YEASTAGP1genetic
27708008
DAL81_YEASTDAL81genetic
27708008
ATC3_YEASTDRS2genetic
27708008
REI1_YEASTREI1genetic
27708008
PEF1_YEASTPEF1genetic
27708008
ASK10_YEASTASK10genetic
27708008
ERG3_YEASTERG3genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
CSF1_YEASTCSF1genetic
27708008
ACE2_YEASTACE2genetic
27708008
VRP1_YEASTVRP1genetic
27708008
ERG6_YEASTERG6genetic
27708008
SIN3_YEASTSIN3genetic
27708008
NCBP2_YEASTCBC2genetic
27708008
SRO7_YEASTSRO7genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GAP1_YEAST

loading...

Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"A subset of membrane-associated proteins is ubiquitinated in responseto mutations in the endoplasmic reticulum degradation machinery.";
Hitchcock A.L., Auld K., Gygi S.P., Silver P.A.;
Proc. Natl. Acad. Sci. U.S.A. 100:12735-12740(2003).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-76, AND MASSSPECTROMETRY.
"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-76, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory