GPA1_ARATH - dbPTM
GPA1_ARATH - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GPA1_ARATH
UniProt AC P18064
Protein Name Guanine nucleotide-binding protein alpha-1 subunit {ECO:0000303|PubMed:2111018}
Gene Name GPA1 {ECO:0000303|PubMed:2111018}
Organism Arabidopsis thaliana (Mouse-ear cress).
Sequence Length 383
Subcellular Localization Cell membrane .
Protein Description Exhibits a fast rate of basal nucleotide exchange. Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Together with GCR1, may regulate the cell cycle via a signaling cascade that uses phosphatidylinositol-specific phospholipase C (PI-PLC) as an effector and inositol 1,4,5-trisphosphate (IP(3)) as a second messenger. Promotes abscisic acid (ABA) responses in guard cells. But, together with GCR1 and GB1, acts as a negative regulator of ABA during seed germination and early seedling development. Involved in the blue light (BL) signaling. Together with GCR1 and ADT3, required for BL-mediated synthesis of phenylpyruvate and subsequently of phenylalanine (Phe), in etiolated seedlings. Modulates root architecture (e.g. lateral root formation). Negatively regulated by RGS1..
Protein Sequence MGLLCSRSRHHTEDTDENTQAAEIERRIEQEAKAEKHIRKLLLLGAGESGKSTIFKQIKLLFQTGFDEGELKSYVPVIHANVYQTIKLLHDGTKEFAQNETDSAKYMLSSESIAIGEKLSEIGGRLDYPRLTKDIAEGIETLWKDPAIQETCARGNELQVPDCTKYLMENLKRLSDINYIPTKEDVLYARVRTTGVVEIQFSPVGENKKSGEVYRLFDVGGQRNERRKWIHLFEGVTAVIFCAAISEYDQTLFEDEQKNRMMETKELFDWVLKQPCFEKTSFMLFLNKFDIFEKKVLDVPLNVCEWFRDYQPVSSGKQEIEHAYEFVKKKFEELYYQNTAPDRVDRVFKIYRTTALDQKLVKKTFKLVDETLRRRNLLEAGLL
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
2N-myristoyl glycine------MGLLCSRSR
------CCCCCCCCC
27.62-
2Myristoylation------MGLLCSRSR
------CCCCCCCCC
27.6212912986
5S-palmitoylation---MGLLCSRSRHHT
---CCCCCCCCCCCC
3.6917158913
12PhosphorylationCSRSRHHTEDTDENT
CCCCCCCCCCCCCHH
29.4519880383
15PhosphorylationSRHHTEDTDENTQAA
CCCCCCCCCCHHHHH
38.6919880383
19PhosphorylationTEDTDENTQAAEIER
CCCCCCHHHHHHHHH
19.9620374526
49PhosphorylationLLLGAGESGKSTIFK
HHHCCCCCCCCHHHH
51.0719880383
166PhosphorylationQVPDCTKYLMENLKR
CCCHHHHHHHHHHHH
7.9820374526

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 GPA1_ARATH !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GPA1_ARATH !!

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 GPA1_ARATH !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCR1_ARATHGCR1physical
15155892
PRN1_ARATHPRNphysical
12837948
GTG2_ARATHGTG2physical
19135895
GTG1_ARATHGTG1physical
19135895
PLDA1_ARATHPLDALPHA1physical
14594812
AROD3_ARATHPD1physical
16415218
THF1_ARATHPSB29physical
16582010
MTND4_ARATHARD4physical
21952135
TCP7_ARATHAT5G23280physical
21952135
CAS_ARATHCaSphysical
21952135
SPX1_ARATHSPX1physical
21952135
Y5659_ARATHLRR1physical
21952135
DEF1B_ARATHPDF1Bphysical
21952135
KN14A_ARATHKAC1physical
21952135
MYB32_ARATHMYB32physical
21952135
CPY57_ARATHAT4G33060physical
21952135
SODF1_ARATHFSD1physical
21952135
SYP23_ARATHSYP23physical
21952135
EIF3A_ARATHEIF3Aphysical
21952135
PRN1_ARATHPRNphysical
21952135
TCP16_ARATHTCP16physical
21952135
RGS1_ARATHRGS1physical
21952135
AGP16_ARATHAGP16physical
21952135
BAG6_ARATHBAG6physical
21952135
TCP9_ARATHAT2G45680physical
21952135
VOZ2_ARATHVOZ2physical
21952135
RS252_ARATHAT2G21580physical
21952135
THF1_ARATHPSB29physical
21952135
XTH4_ARATHXTH4physical
21952135
TCP3_ARATHTCP3physical
21952135
VOZ1_ARATHVOZ1physical
21952135
CSN5A_ARATHCSN5Aphysical
21952135
AROD1_ARATHADT1physical
21952135
CDPK1_ARATHCPK1physical
22737156
GDU2_ARATHGDU2physical
22737156
CAAT9_ARATHCAT9physical
22737156
PLDA1_ARATHPLDALPHA1physical
25187041
RGS1_ARATHRGS1physical
15313574
CERK1_ARATHCERK1physical
26414709
Y5838_ARATHBIR1physical
26414709
BAK1_ARATHBAK1physical
26414709

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GPA1_ARATH

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Related Literatures of Post-Translational Modification
Myristoylation
ReferencePubMed
"Unexpected protein families including cell defense components featurein the N-myristoylome of a higher eukaryote.";
Boisson B., Giglione C., Meinnel T.;
J. Biol. Chem. 278:43418-43429(2003).
Cited for: N-MYRISTOYLATION.

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