dbPTM

EIF3A_ARATH - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF3A_ARATH
UniProt AC	Q9LD55
Protein Name	Eukaryotic translation initiation factor 3 subunit A {ECO:0000255\|HAMAP-Rule:MF_03000}
Gene Name	TIF3A1
Organism	Arabidopsis thaliana (Mouse-ear cress).
Sequence Length	987
Subcellular Localization	Cytoplasm .
Protein Description	RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation..
Protein Sequence	MANFAKPENALKRADELINVGQKQDALQALHDLITSKRYRAWQKPLEKIMFKYLDLCVDLKRGRFAKDGLIQYRIVCQQVNVSSLEEVIKHFLHLATDKAEQARSQADALEEALDVDDLEADRKPEDLQLSIVSGEKGKDRSDRELVTPWFKFLWETYRTVLEILRNNSKLEALYAMTAHKAFQFCKQYKRTTEFRRLCEIIRNHLANLNKYRDQRDRPDLSAPESLQLYLDTRFDQLKVATELGLWQEAFRSVEDIYGLMCMVKKTPKSSLLMVYYSKLTEIFWISSSHLYHAYAWFKLFSLQKNFNKNLSQKDLQLIASSVVLAALSIPPFDRAQSASHMELENEKERNLRMANLIGFNLEPKFEGKDMLSRSALLSELVSKGVLSCASQEVKDLFHVLEHEFHPLDLGSKIQPLLEKISKSGGKLSSAPSLPEVQLSQYVPSLEKLATLRLLQQVSKIYQTIRIESLSQLVPFFQFSEVEKISVDAVKNNFVAMKVDHMKGVVIFGNLGIESDGLRDHLAVFAESLSKVRAMLYPVPSKASKLAGVIPNLADTVEKEHKRLLARKSIIEKRKEDQERQQLEMEREEEQKRLKLQKLTEEAEQKRLAAELAERRKQRILREIEEKELEEAQALLEETEKRMKKGKKKPLLDGEKVTKQSVKERALTEQLKERQEMEKKLQKLAKTMDYLERAKREEAAPLIEAAYQRRLVEEREFYEREQQREVELSKERHESDLKEKNRLSRMLGNKEIFQAQVISRRQAEFDRIRTEREERISKIIREKKQERDIKRKQIYYLKIEEERIRKLQEEEEARKQEEAERLKKVEAERKANLDKAFEKQRQREIELEEKSRREREELLRGTNAPPARLAEPTVTPVGTTAPAAAAAAAGAPAAPYVPKWKRQTTEVSGPSAPTSSETDRRSNRGPPPGDDHWGSNRGAAQNTDRWTSNRERSGPPAEGGDRWGSGPRGSDDRRSTFGSSRPRPTQR

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
61	Ubiquitination	LDLCVDLKRGRFAKD HHHHHHHCCCCCCCC	48.63	17272265
459	Phosphorylation	LRLLQQVSKIYQTIR HHHHHHHHHHHHHHC	14.70	22074104
486	Phosphorylation	FSEVEKISVDAVKNN CCCEEEEEHHHHHCC	25.64	19880383
873	Phosphorylation	PARLAEPTVTPVGTT CHHHCCCEEECCCCC	28.63	27288362
875	Phosphorylation	RLAEPTVTPVGTTAP HHCCCEEECCCCCHH	18.09	29654922
879	Phosphorylation	PTVTPVGTTAPAAAA CEEECCCCCHHHHHH	21.73	19880383
880	Phosphorylation	TVTPVGTTAPAAAAA EEECCCCCHHHHHHH	25.39	19880383
896	Phosphorylation	AGAPAAPYVPKWKRQ CCCCCCCCCCCCCCC	25.34	29654922
905	Phosphorylation	PKWKRQTTEVSGPSA CCCCCCCCCCCCCCC	26.50	25561503
953	Phosphorylation	WTSNRERSGPPAEGG CCCCCCCCCCCCCCC	51.39	25561503
965	Phosphorylation	EGGDRWGSGPRGSDD CCCCCCCCCCCCCCC	38.37	29654922
975	Phosphorylation	RGSDDRRSTFGSSRP CCCCCCCCCCCCCCC	29.05	25561503
976	Phosphorylation	GSDDRRSTFGSSRPR CCCCCCCCCCCCCCC	30.15	25561503
979	Phosphorylation	DRRSTFGSSRPRPTQ CCCCCCCCCCCCCCC	20.98	25561503
980	Phosphorylation	RRSTFGSSRPRPTQR CCCCCCCCCCCCCCC	46.84	25561503

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
-	K	Ubiquitination	E3 ubiquitin ligase	TaMAB2	-	PMID:31824527

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF3A_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 EIF3A_ARATH !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
EIF3H_ARATH	TIF3H1	physical	15548739

Drug and Disease Associations

Kegg Drug
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of EIF3A_ARATH

Related Literatures of Post-Translational Modification

Ubiquitylation
Reference	PubMed
"Multidimensional protein identification technology (MudPIT) analysisof ubiquitinated proteins in plants."; Maor R., Jones A., Nuehse T.S., Studholme D.J., Peck S.C., Shirasu K.; Mol. Cell. Proteomics 6:601-610(2007). Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-61, AND MASSSPECTROMETRY.	17272265 [Abstract]