EIF3A_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3A_RAT
• UniProt AC: Q1JU68
• Protein Name: Eukaryotic translation initiation factor 3 subunit A {ECO:0000255|HAMAP-Rule:MF_03000}
• Gene Name: Eif3a
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 1354
• Subcellular Localization: Cytoplasm .
• Protein Description: RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. The eIF-3 complex associates with the 40S ribosome and facilitates the recruitment of eIF-1, eIF-1A, eIF-2:GTP:methionyl-tRNAi and eIF-5 to form the 43S pre-initiation complex (43S PIC). The eIF-3 complex stimulates mRNA recruitment to the 43S PIC and scanning of the mRNA for AUG recognition. The eIF-3 complex is also required for disassembly and recycling of post-termination ribosomal complexes and subsequently prevents premature joining of the 40S and 60S ribosomal subunits prior to initiation. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation, including cell cycling, differentiation and apoptosis, and uses different modes of RNA stem-loop binding to exert either translational activation or repression..
• Protein Sequence: MPAYFQRPENALKRANEFLEVGKKQPALDVLYDVMKSKKHRTWQKIHEPIMLKYLELCVDLRKSHLAKEGLYQYKNICQQVNIKSLEDVVRAYLKLAEEKTEAAKEESQQMVLDIEDLDNIQTPESVLLSAVSGEDTQDRTDRLLLTPWVKFLWESYRQCLDLLRNNSRVERLYHDIAQQAFKFCLQYTRKAEFRKLCDNLRMHLSQIQRHHNQSTAINLNNPESQSMHLETRLVQLDSAISMELWQEAFKAVEDIHGLFSLSKKPPKPQLMANYYNKVSTVFWKSGNALFHASTLHRLYHLSREMRKNLTQDEMQRMSTRVLLATLSIPITPERTDIARLLDMDGIIVEKQRRLATLLGLQAPPTRIGLINDMVRFNVLQYVVPEVKDLYNWLEVEFNPLKLCERVTKVLNWVREQPEKEPELQQYVPQLQNNTILRLLQQVAQIYQSIEFSRLTSLVPFVDAFQLERAIVDAARHCDLQVRIDHTSRTLSFGSDLNYATREDAPIGPHLQSMPSEQIRNQLTAMSSVLAKALEVIKPAHILQEKEEQHQLAVTAYIKNSRKEHQRILARRQTIEERKERLESLNIQREKEELEQREAELQKVRKAEEERLRQEAKEREKERILQEHEQIKKKTVRERLEQIKKTELGAKAFKDIDIEDLEELDPDFIMAKQVEQLEKEKKELQERLKNQEKKIDYFERAKRLEEIPLIKSAYEEQRVKDMDLWEQQEEERITTMQLEREKALEHKNRMSRMLEDRDLFVMRLKAARQSVYEEKLKQFEERLAEERHNRLEERKRQRKEERKITYYREKEEEEQRRAEEQMLKEREERERAERAKREEELREYQERVKKLEEVERKKRQRELEIEERERRREEERRLGEDPLSRKDSRWGDRDSEGTWRKGPEADSEWRRGPPEKEWRRETRDDERPHRRDEDRLRRLGGDDEERESSLRPDDDRIPRRGLDDDRGPRRGPDEDRFSRRGTDDDRPSWRNADDDRPPRRIGDDDRGSWRHTDDDRPPRRGLDDDRPPRRGLDDERGSWRTAEEDRGPRRGMDDDRGPRRGGADDERSSWRNADDDRGPRRGMDDDRGPRRGLDDDRGPWRNAAEDRISRRGADDDRGPWRNMDDDRVPRRGDDARPGPWRPFVKPGGWREKEKAREESWGPPRESRPPEEREWDRDKEKDRDNQDREENDKDLERDRDRERDGDREDRFRRPRDEGGWRRGPAEESSSWRDSSRRDDRDRDDRRRDRDDRRDLRDLRDRRDLRDDRDRRGPPLRSEREEASSWRRTDDRKDDRTEERDPPRRVPPPTLSRERERERDREGEKEKASWRAEKDRESLRRTKNETDEDGWTTVRR

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
68	Acetylation	LRKSHLAKEGLYQYK HHHHHHHHHHHHHHH	59.69	22902405
206	Phosphorylation	DNLRMHLSQIQRHHN HHHHHHHHHHHHHHC	15.57	23984901
261	Phosphorylation	EDIHGLFSLSKKPPK HHHHHHHHCCCCCCC	36.45	23984901
263	Phosphorylation	IHGLFSLSKKPPKPQ HHHHHHCCCCCCCCC	37.12	23984901
382	Phosphorylation	VRFNVLQYVVPEVKD HHHCHHHHHCHHHHH	10.15	-
420	Ubiquitination	WVREQPEKEPELQQY HHHHCCCCCHHHHHH	82.39	-
490	Phosphorylation	RIDHTSRTLSFGSDL EEECCCCCEECCCCC	26.90	28432305
492	Phosphorylation	DHTSRTLSFGSDLNY ECCCCCEECCCCCCC	27.27	28432305
495	Phosphorylation	SRTLSFGSDLNYATR CCCEECCCCCCCCCC	36.59	27097102
524	Phosphorylation	EQIRNQLTAMSSVLA HHHHHHHHHHHHHHH	15.56	27097102
527	Phosphorylation	RNQLTAMSSVLAKAL HHHHHHHHHHHHHHH	18.16	27097102
528	Phosphorylation	NQLTAMSSVLAKALE HHHHHHHHHHHHHHH	14.20	27097102
574	Phosphorylation	RILARRQTIEERKER HHHHHHHHHHHHHHH	28.66	29779826
584	Phosphorylation	ERKERLESLNIQREK HHHHHHHHCCHHHHH	31.16	27097102
644	Acetylation	RERLEQIKKTELGAK HHHHHHHHHCHHHHH	54.02	22902405
645	Acetylation	ERLEQIKKTELGAKA HHHHHHHHCHHHHHH	49.19	22902405
694	Acetylation	RLKNQEKKIDYFERA HHHHHHHHHHHHHHH	39.80	22902405
775	Ubiquitination	RQSVYEEKLKQFEER HHHHHHHHHHHHHHH	49.39	-
895	Phosphorylation	SRWGDRDSEGTWRKG CCCCCCCCCCCCCCC	38.53	-
948	Phosphorylation	GDDEERESSLRPDDD CCHHHHHHHCCCCCC	40.68	27097102
949	Phosphorylation	DDEERESSLRPDDDR CHHHHHHHCCCCCCC	24.52	27097102
978	Phosphorylation	GPDEDRFSRRGTDDD CCCCCCCCCCCCCCC	23.20	25575281
982	Phosphorylation	DRFSRRGTDDDRPSW CCCCCCCCCCCCCCC	34.15	28432305
988	Phosphorylation	GTDDDRPSWRNADDD CCCCCCCCCCCCCCC	39.29	25575281
1008	Phosphorylation	IGDDDRGSWRHTDDD CCCCCCCCCCCCCCC	23.10	28432305
1038	Phosphorylation	GLDDERGSWRTAEED CCCCCCCCCCCCCHH	21.43	-
1159	Phosphorylation	KEKAREESWGPPRES HHHHHHHHCCCCCCC	32.36	27097102
1227	Phosphorylation	RRGPAEESSSWRDSS CCCCCCCCCCCCCCC	22.60	27097102
1228	Phosphorylation	RGPAEESSSWRDSSR CCCCCCCCCCCCCCC	36.88	27097102
1229	Phosphorylation	GPAEESSSWRDSSRR CCCCCCCCCCCCCCC	35.10	27097102
1233	Phosphorylation	ESSSWRDSSRRDDRD CCCCCCCCCCCCCCC	19.71	27097102
1234	Phosphorylation	SSSWRDSSRRDDRDR CCCCCCCCCCCCCCH	35.31	27097102
1308	Phosphorylation	PRRVPPPTLSRERER CCCCCCCCCCHHHHH	43.04	28432305
1310	Phosphorylation	RVPPPTLSRERERER CCCCCCCCHHHHHHH	34.28	27097102
1336	Phosphorylation	RAEKDRESLRRTKNE HHHHHHHHHHHHCCC	28.24	29779826

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of EIF3A_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3A_RAT !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of EIF3A_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of EIF3A_RAT !!

Drug and Disease Associations

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