GLNA_YEAST - dbPTM
GLNA_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GLNA_YEAST
UniProt AC P32288
Protein Name Glutamine synthetase
Gene Name GLN1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 370
Subcellular Localization Cytoplasm .
Protein Description
Protein Sequence MAEASIEKTQILQKYLELDQRGRIIAEYVWIDGTGNLRSKGRTLKKRITSIDQLPEWNFDGSSTNQAPGHDSDIYLKPVAYYPDPFRRGDNIVVLAACYNNDGTPNKFNHRHEAAKLFAAHKDEEIWFGLEQEYTLFDMYDDVYGWPKGGYPAPQGPYYCGVGAGKVYARDMIEAHYRACLYAGLEISGINAEVMPSQWEFQVGPCTGIDMGDQLWMARYFLHRVAEEFGIKISFHPKPLKGDWNGAGCHTNVSTKEMRQPGGMKYIEQAIEKLSKRHAEHIKLYGSDNDMRLTGRHETASMTAFSSGVANRGSSIRIPRSVAKEGYGYFEDRRPASNIDPYLVTGIMCETVCGAIDNADMTKEFERESS
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
2Acetylation------MAEASIEKT
------CCCHHHHHH		22.519298649
5Phosphorylation---MAEASIEKTQIL
---CCCHHHHHHHHH		23.8415665377
8UbiquitinationMAEASIEKTQILQKY
CCCHHHHHHHHHHHH		44.0224961812
82-HydroxyisobutyrylationMAEASIEKTQILQKY
CCCHHHHHHHHHHHH		44.02-
8AcetylationMAEASIEKTQILQKY
CCCHHHHHHHHHHHH		44.0222865919
9PhosphorylationAEASIEKTQILQKYL
CCHHHHHHHHHHHHH		14.1928152593
14UbiquitinationEKTQILQKYLELDQR
HHHHHHHHHHHHHHC		48.6423749301
14AcetylationEKTQILQKYLELDQR
HHHHHHHHHHHHHHC		48.6424489116
46UbiquitinationSKGRTLKKRITSIDQ
CCCCCHHHHCCCHHH		52.7417644757
49PhosphorylationRTLKKRITSIDQLPE
CCHHHHCCCHHHCCC		24.5419779198
50PhosphorylationTLKKRITSIDQLPEW
CHHHHCCCHHHCCCC		23.0721551504
75PhosphorylationPGHDSDIYLKPVAYY
CCCCCCEEEEEEEEC		17.4228132839
77UbiquitinationHDSDIYLKPVAYYPD
CCCCEEEEEEEECCC		22.0723749301
107UbiquitinationNNDGTPNKFNHRHEA
CCCCCCCCCCHHHHH		49.0717644757
116AcetylationNHRHEAAKLFAAHKD
CHHHHHHHHHHHCCC		51.7022865919
116UbiquitinationNHRHEAAKLFAAHKD
CHHHHHHHHHHHCCC		51.7017644757
122UbiquitinationAKLFAAHKDEEIWFG
HHHHHHCCCCCEEEE		63.2117644757
148UbiquitinationDDVYGWPKGGYPAPQ
CCCCCCCCCCCCCCC		59.4617644757
166UbiquitinationYCGVGAGKVYARDMI
CCCCCCCCCHHHHHH		31.3823749301
232UbiquitinationVAEEFGIKISFHPKP
HHHHHCCEEEEECCC		32.4517644757
238AcetylationIKISFHPKPLKGDWN
CEEEEECCCCCCCCC		55.1822865919
265UbiquitinationMRQPGGMKYIEQAIE
CCCCCHHHHHHHHHH		46.4817644757
273UbiquitinationYIEQAIEKLSKRHAE
HHHHHHHHHHHHHHH		52.5323749301
273AcetylationYIEQAIEKLSKRHAE
HHHHHHHHHHHHHHH		52.5324489116
275PhosphorylationEQAIEKLSKRHAEHI
HHHHHHHHHHHHHHH		38.4228889911
276UbiquitinationQAIEKLSKRHAEHIK
HHHHHHHHHHHHHHE		59.6524961812
283UbiquitinationKRHAEHIKLYGSDND
HHHHHHHEEECCCCC		37.2523749301
283AcetylationKRHAEHIKLYGSDND
HHHHHHHEEECCCCC		37.2524489116
285PhosphorylationHAEHIKLYGSDNDMR
HHHHHEEECCCCCCC		15.0222369663
287PhosphorylationEHIKLYGSDNDMRLT
HHHEEECCCCCCCCC		21.4922369663
299PhosphorylationRLTGRHETASMTAFS
CCCCCCCCCCHHHCC		20.2222369663
301PhosphorylationTGRHETASMTAFSSG
CCCCCCCCHHHCCCC		24.8822369663
303PhosphorylationRHETASMTAFSSGVA
CCCCCCHHHCCCCCC		23.2722369663
306PhosphorylationTASMTAFSSGVANRG
CCCHHHCCCCCCCCC		24.5828889911
314PhosphorylationSGVANRGSSIRIPRS
CCCCCCCCCCCCCHH		21.2525533186
315PhosphorylationGVANRGSSIRIPRSV
CCCCCCCCCCCCHHH		20.7927017623
324UbiquitinationRIPRSVAKEGYGYFE
CCCHHHHHCCCCCCC		49.9023749301
324SuccinylationRIPRSVAKEGYGYFE
CCCHHHHHCCCCCCC		49.9023954790
324AcetylationRIPRSVAKEGYGYFE
CCCHHHHHCCCCCCC		49.9024489116
3242-HydroxyisobutyrylationRIPRSVAKEGYGYFE
CCCHHHHHCCCCCCC		49.90-
337PhosphorylationFEDRRPASNIDPYLV
CCCCCCCCCCCHHHH		36.6827017623
351PhosphorylationVTGIMCETVCGAIDN
HHHHHHHHHHHHHHC		19.0327017623
363UbiquitinationIDNADMTKEFERESS
HHCHHHHHHHHHHCC		54.4923749301
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 GLNA_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GLNA_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 GLNA_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GPX3_YEASTHYR1physical
17707771
GLNA_YEASTGLN1physical
19322816
SYSM_YEASTDIA4genetic
21623372
AATC_YEASTAAT2genetic
21623372
ELO3_YEASTELO3genetic
21623372
POS5_YEASTPOS5genetic
21623372
DCOR_YEASTSPE1genetic
21623372
ADH3_YEASTADH3genetic
21623372
6PGD1_YEASTGND1genetic
21623372
ATP14_YEASTATP14genetic
21623372
ATPO_YEASTATP5genetic
21623372
UBR1_YEASTUBR1genetic
22670231
GLNA_YEASTGLN1physical
24771766
HIR1_YEASTHIR1genetic
27708008
CHK1_YEASTCHK1genetic
27708008
TDA1_YEASTTDA1genetic
27708008
CDC37_YEASTCDC37genetic
27708008
SNU56_YEASTSNU56genetic
27708008
RSP5_YEASTRSP5genetic
27708008
MOB2_YEASTMOB2genetic
27708008
YJ9I_YEASTYJR141Wgenetic
27708008
CWC16_YEASTYJU2genetic
27708008
MED14_YEASTRGR1genetic
27708008
ORC1_YEASTORC1genetic
27708008
GPI12_YEASTGPI12genetic
27708008
APC5_YEASTAPC5genetic
27708008
SCC1_YEASTMCD1genetic
27708008
GLE1_YEASTGLE1genetic
27708008
PRP38_YEASTPRP38genetic
27708008
PRP31_YEASTPRP31genetic
27708008
DBF2_YEASTDBF2genetic
27708008
SYV_YEASTVAS1genetic
27708008
ESP1_YEASTESP1genetic
27708008
TEL2_YEASTTEL2genetic
27708008
PESC_YEASTNOP7genetic
27708008
DAM1_YEASTDAM1genetic
27708008
NUP57_YEASTNUP57genetic
27708008
COG2_YEASTCOG2genetic
27708008
CBF3A_YEASTCBF2genetic
27708008
PTI1_YEASTPTI1genetic
27708008
SEC22_YEASTSEC22genetic
27708008
RS6A_YEASTRPS6Bgenetic
27708008
RS6B_YEASTRPS6Bgenetic
27708008
AIM4_YEASTAIM4genetic
27708008
BRE1_YEASTBRE1genetic
27708008
RL13A_YEASTRPL13Agenetic
27708008
CYK3_YEASTCYK3genetic
27708008
INO2_YEASTINO2genetic
27708008
SWF1_YEASTSWF1genetic
27708008
STP1_YEASTSTP1genetic
27708008
URC2_YEASTURC2genetic
27708008
CGR1_YEASTCGR1genetic
27708008
PEF1_YEASTPEF1genetic
27708008
RSSA1_YEASTRPS0Agenetic
27708008
NPR3_YEASTNPR3genetic
27708008
STB5_YEASTSTB5genetic
27708008
SDS3_YEASTSDS3genetic
27708008
DAL81_YEASTDAL81genetic
27708008
RPE_YEASTRPE1genetic
27708008
RS21B_YEASTRPS21Bgenetic
27708008
BFA1_YEASTBFA1genetic
27708008
IXR1_YEASTIXR1genetic
27708008
EF1G2_YEASTTEF4genetic
27708008
EMC6_YEASTEMC6genetic
27708008
ARV1_YEASTARV1genetic
27708008
SEI1_YEASTFLD1genetic
27708008
RS3A1_YEASTRPS1Agenetic
27708008
GBLP_YEASTASC1genetic
27708008
IPA3_YEASTPAI3genetic
27708008
BUL1_YEASTBUL1genetic
27708008
GAS1_YEASTGAS1genetic
27708008
PET8_YEASTPET8genetic
27708008
HRB1_YEASTHRB1genetic
27708008
YNB0_YEASTYNL010Wgenetic
27708008
TPM1_YEASTTPM1genetic
27708008
MIC27_YEASTMIC27genetic
27708008
PDAT_YEASTLRO1genetic
27708008
PDE2_YEASTPDE2genetic
27708008
HSP71_YEASTSSA1genetic
27708008
DEP1_YEASTDEP1genetic
27708008
RXT2_YEASTRXT2genetic
27708008
RV161_YEASTRVS161genetic
27708008
VAM6_YEASTVAM6genetic
27708008
TRS85_YEASTTRS85genetic
27708008
ARO1_YEASTARO1genetic
27708008
YD132_YEASTYDR132Cgenetic
27708008
H2A1_YEASTHTA1genetic
27708008
MNN10_YEASTMNN10genetic
27708008
AIM11_YEASTAIM11genetic
27708008
MON1_YEASTMON1genetic
27708008
DOHH_YEASTLIA1genetic
27708008
RL22A_YEASTRPL22Agenetic
27708008
SUB1_YEASTSUB1genetic
27708008
YNO0_YEASTYNL140Cgenetic
27708008
SIN3_YEASTSIN3genetic
27708008
INO4_YEASTINO4genetic
27708008
VAM3_YEASTVAM3genetic
27708008
LDB19_YEASTLDB19genetic
27708008
ATG41_YEASTICY2genetic
27708008
PMP1_YEASTPMP1physical
26404137
HSP82_YEASTHSP82physical
24488121
HSC82_YEASTHSC82physical
24488121
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GLNA_YEAST

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Proteome studies of Saccharomyces cerevisiae: identification andcharacterization of abundant proteins.";
Garrels J.I., McLaughlin C.S., Warner J.R., Futcher B., Latter G.I.,Kobayashi R., Schwender B., Volpe T., Anderson D.S.,Mesquita-Fuentes R., Payne W.E.;
Electrophoresis 18:1347-1360(1997).
Cited for: ACETYLATION AT ALA-2.
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-324, 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-324, AND MASSSPECTROMETRY.

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