EIF3B_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3B_RAT
• UniProt AC: Q4G061
• Protein Name: Eukaryotic translation initiation factor 3 subunit B {ECO:0000255|HAMAP-Rule:MF_03001}
• Gene Name: Eif3b
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 797
• 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: MQDAENVAAPEAAEERAEPARQQPVSESPPTDEAAGSGGSEVGRTEDAEEDAEARPEPEVRAKPAAQSEEETAASPAASPTPQSAQEPSAPGKAEAGGEQARHPSARAEEEGGSDGSAAEAEPRALENGEADEPSFSDPEDFVDDVSEEELLGDVLKDRPQEADGIDSVIVVDNVPQVGPDRLEKLKNVIHKIFSKFGKIINDYYPEEDGKTKGYIFLEYASPAHAVDAVKNADGYKLDKQHTFRVNLFTDFDKYMTISDEWDIPEKQPFKDLGNLRYWLEEAECRDQYSVIFESGDRTSIFWNDVKDPVSIEERARWTETYVRWSPKGTYLATFHQRGIALWGGDKFKQIQRFSHQGVQLIDFSPCERYLVTFSPLMDTQDDPQAIIIWDILTGHKKRGFHCESSAHWPIFKWSHDGKFFARMTLDTLSIYETPSMGLLDKKSLKISGIKDFSWSPGGNIIAFWVPEDKDIPARVTLMQLPTRQEIRVRNLFNVVDCKLHWQKNGDYLCVKVDRTPKGTQGVVTNFEIFRMREKQVPVDVVEMKETIIAFAWEPNGSKFAVLHGEAPRISVSFYHVKSNGKIELIKMFDKQQANTIFWSPQGQFVVLAGLRSMNGALAFVDTSDCTVMNIAEHYMASDVEWDPTGRYVVTSVSWWSHKVDNAYWLWTFQGRLLQKNNKDRFCQLLWRPRPPTLLSQDQIKQIKKDLKKYSKIFEQKDRLSQSKASKELVERRRTMMEDFRQYRKMAQELYMKQKNERLELRGGVDTDELDSNVDDWEEETIEFFVTEEVIPLGSQE

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
1	Acetylation	-------MQDAENVA -------CCHHHHCC	8.00	-
26	Phosphorylation	PARQQPVSESPPTDE HHHCCCCCCCCCCCC	38.75	27097102
28	Phosphorylation	RQQPVSESPPTDEAA HCCCCCCCCCCCCCC	28.77	28689409
31	Phosphorylation	PVSESPPTDEAAGSG CCCCCCCCCCCCCCC	50.27	27097102
37	Phosphorylation	PTDEAAGSGGSEVGR CCCCCCCCCCCCCCC	34.94	27097102
40	Phosphorylation	EAAGSGGSEVGRTED CCCCCCCCCCCCCCC	32.41	27097102
45	Phosphorylation	GGSEVGRTEDAEEDA CCCCCCCCCCHHHHH	32.08	28432305
68	Phosphorylation	RAKPAAQSEEETAAS CCCCCCCCHHHHCCC	42.10	23712012
72	Phosphorylation	AAQSEEETAASPAAS CCCCHHHHCCCCCCC	30.70	23712012
75	Phosphorylation	SEEETAASPAASPTP CHHHHCCCCCCCCCC	16.77	23712012
79	Phosphorylation	TAASPAASPTPQSAQ HCCCCCCCCCCCCCC	31.26	23712012
81	Phosphorylation	ASPAASPTPQSAQEP CCCCCCCCCCCCCCC	31.31	28825834
84	Phosphorylation	AASPTPQSAQEPSAP CCCCCCCCCCCCCCC	32.87	27097102
89	Phosphorylation	PQSAQEPSAPGKAEA CCCCCCCCCCCCCCC	46.47	27097102
105	Phosphorylation	GEQARHPSARAEEEG CCCCCCCCHHHHHCC	25.02	28689409
114	Phosphorylation	RAEEEGGSDGSAAEA HHHHCCCCCCCCCCC	50.05	19700791
117	Phosphorylation	EEGGSDGSAAEAEPR HCCCCCCCCCCCCCH	29.33	19700791
135	Phosphorylation	NGEADEPSFSDPEDF CCCCCCCCCCCHHHH	35.02	21630457
137	Phosphorylation	EADEPSFSDPEDFVD CCCCCCCCCHHHHCC	57.50	29779826
147	Phosphorylation	EDFVDDVSEEELLGD HHHCCCCCHHHHHHH	46.41	21630457
192	Acetylation	KLKNVIHKIFSKFGK HHHHHHHHHHHHHHH	34.03	22902405
199	Acetylation	KIFSKFGKIINDYYP HHHHHHHHHHHHCCC	43.47	22902405
211	Acetylation	YYPEEDGKTKGYIFL CCCCCCCCEEEEEEE	60.43	22902405
222	Phosphorylation	YIFLEYASPAHAVDA EEEEEECCHHHHHHH	23.01	-
237	Acetylation	VKNADGYKLDKQHTF HHCCCCCCCCCCCEE	56.59	22902405
271	Acetylation	IPEKQPFKDLGNLRY CCCCCCCCCCCCHHH	59.74	-
347	Acetylation	IALWGGDKFKQIQRF EEEECCHHHHCHHHH	58.71	-
349	Acetylation	LWGGDKFKQIQRFSH EECCHHHHCHHHHCC	52.83	22902405
419	Acetylation	FKWSHDGKFFARMTL EEECCCCCEEEEEEE	43.28	22902405
442	Acetylation	PSMGLLDKKSLKISG CCCCCCCCCCCEECC	44.20	22902405
573	Phosphorylation	EAPRISVSFYHVKSN CCCEEEEEEEEEEEC	17.19	23984901
726	Phosphorylation	RLSQSKASKELVERR HHCHHHHHHHHHHHH	30.33	25403869

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

Oops, there are no upstream regulatory protein records of EIF3B_RAT !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3B_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 EIF3B_RAT !!

Protein-Protein Interaction

Oops, there are no PPI records of EIF3B_RAT !!

Drug and Disease Associations

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

Related Literatures of Post-Translational Modification

Phosphorylation

"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:regulation of aquaporin-2 phosphorylation at two sites.";
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-117, ANDMASS SPECTROMETRY.
PubMed: 16641100