dbPTM

EIF3D_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EIF3D_HUMAN
UniProt AC	O15371
Protein Name	Eukaryotic translation initiation factor 3 subunit D {ECO:0000255\|HAMAP-Rule:MF_03003}
Gene Name	EIF3D {ECO:0000255\|HAMAP-Rule:MF_03003}
Organism	Homo sapiens (Human).
Sequence Length	548
Subcellular Localization	Cytoplasm .
Protein Description	mRNA cap-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, a complex required for several steps in the initiation of protein synthesis of a specialized repertoire of mRNAs. [PubMed: 27462815 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]
Protein Sequence	MAKFMTPVIQDNPSGWGPCAVPEQFRDMPYQPFSKGDRLGKVADWTGATYQDKRYTNKYSSQFGGGSQYAYFHEEDESSFQLVDTARTQKTAYQRNRMRFAQRNLRRDKDRRNMLQFNLQILPKSAKQKERERIRLQKKFQKQFGVRQKWDQKSQKPRDSSVEVRSDWEVKEEMDFPQLMKMRYLEVSEPQDIECCGALEYYDKAFDRITTRSEKPLRSIKRIFHTVTTTDDPVIRKLAKTQGNVFATDAILATLMSCTRSVYSWDIVVQRVGSKLFFDKRDNSDFDLLTVSETANEPPQDEGNSFNSPRNLAMEATYINHNFSQQCLRMGKERYNFPNPNPFVEDDMDKNEIASVAYRYRRWKLGDDIDLIVRCEHDGVMTGANGEVSFINIKTLNEWDSRHCNGVDWRQKLDSQRGAVIATELKNNSYKLARWTCCALLAGSEYLKLGYVSRYHVKDSSRHVILGTQQFKPNEFASQINLSVENAWGILRCVIDICMKLEEGKYLILKDPNKQVIRVYSLPDGTFSSDEDEEEEEEEEEEEEEEET

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
3	Acetylation	-----MAKFMTPVIQ -----CCCCCCCEEC	34.08	25953088
19	Glutathionylation	NPSGWGPCAVPEQFR CCCCCCCCCCCHHHC	5.41	22555962
28	Sulfoxidation	VPEQFRDMPYQPFSK CCHHHCCCCCCCCCC	2.65	30846556
30	Phosphorylation	EQFRDMPYQPFSKGD HHHCCCCCCCCCCCC	23.37	-
34	Phosphorylation	DMPYQPFSKGDRLGK CCCCCCCCCCCCCCC	42.27	23917254
35	Ubiquitination	MPYQPFSKGDRLGKV CCCCCCCCCCCCCCC	66.27	23000965
35	Ubiquitination	MPYQPFSKGDRLGKV CCCCCCCCCCCCCCC	66.27	21890473
35	Ubiquitination	MPYQPFSKGDRLGKV CCCCCCCCCCCCCCC	66.27	21890473
35	Acetylation	MPYQPFSKGDRLGKV CCCCCCCCCCCCCCC	66.27	26051181
41	Sumoylation	SKGDRLGKVADWTGA CCCCCCCCCCCCCCC	38.55	-
41	Ubiquitination	SKGDRLGKVADWTGA CCCCCCCCCCCCCCC	38.55	23000965
41	Sumoylation	SKGDRLGKVADWTGA CCCCCCCCCCCCCCC	38.55	-
41	Ubiquitination	SKGDRLGKVADWTGA CCCCCCCCCCCCCCC	38.55	21890473
41	Acetylation	SKGDRLGKVADWTGA CCCCCCCCCCCCCCC	38.55	23236377
46	Phosphorylation	LGKVADWTGATYQDK CCCCCCCCCCCCCCH	19.93	28152594
49	Phosphorylation	VADWTGATYQDKRYT CCCCCCCCCCCHHCC	24.06	28152594
50	Phosphorylation	ADWTGATYQDKRYTN CCCCCCCCCCHHCCC	17.74	28152594
53	Acetylation	TGATYQDKRYTNKYS CCCCCCCHHCCCCCC	31.60	23236377
53	Ubiquitination	TGATYQDKRYTNKYS CCCCCCCHHCCCCCC	31.60	27667366
53	2-Hydroxyisobutyrylation	TGATYQDKRYTNKYS CCCCCCCHHCCCCCC	31.60	-
53	Ubiquitination	TGATYQDKRYTNKYS CCCCCCCHHCCCCCC	31.60	21890473
53	Ubiquitination	TGATYQDKRYTNKYS CCCCCCCHHCCCCCC	31.60	21890473
55	Phosphorylation	ATYQDKRYTNKYSSQ CCCCCHHCCCCCCCC	22.02	-
58	Ubiquitination	QDKRYTNKYSSQFGG CCHHCCCCCCCCCCC	38.41	33845483
67	Phosphorylation	SSQFGGGSQYAYFHE CCCCCCCCCCEEEEC	24.24	17525332
69	Phosphorylation	QFGGGSQYAYFHEED CCCCCCCCEEEECCC	12.64	-
78	Phosphorylation	YFHEEDESSFQLVDT EEECCCCCCEEEECC	49.10	24275569
79	O-linked_Glycosylation	FHEEDESSFQLVDTA EECCCCCCEEEECCH	18.24	30379171
88	Phosphorylation	QLVDTARTQKTAYQR EEECCHHHHHHHHHH	31.77	20068231
90	Ubiquitination	VDTARTQKTAYQRNR ECCHHHHHHHHHHHH	34.21	27667366
91	Phosphorylation	DTARTQKTAYQRNRM CCHHHHHHHHHHHHH	22.30	19664994
93	Phosphorylation	ARTQKTAYQRNRMRF HHHHHHHHHHHHHHH	17.15	20068231
114	Sulfoxidation	RDKDRRNMLQFNLQI CCHHHHHHHHHHHHH	2.70	28465586
124	Ubiquitination	FNLQILPKSAKQKER HHHHHCCCCCHHHHH	60.65	23503661
127	Ubiquitination	QILPKSAKQKERERI HHCCCCCHHHHHHHH	69.83	23503661
129	Ubiquitination	LPKSAKQKERERIRL CCCCCHHHHHHHHHH	59.02	23503661
138	Ubiquitination	RERIRLQKKFQKQFG HHHHHHHHHHHHHHC	61.21	22817900
139	Ubiquitination	ERIRLQKKFQKQFGV HHHHHHHHHHHHHCC	39.81	22817900
142	Ubiquitination	RLQKKFQKQFGVRQK HHHHHHHHHHCCCCC	51.21	21906983
142	Ubiquitination	RLQKKFQKQFGVRQK HHHHHHHHHHCCCCC	51.21	21890473
149	Ubiquitination	KQFGVRQKWDQKSQK HHHCCCCCCCCCCCC	42.02	24816145
160	Phosphorylation	KSQKPRDSSVEVRSD CCCCCCCCCCCCCCC	37.25	30576142
161	Phosphorylation	SQKPRDSSVEVRSDW CCCCCCCCCCCCCCC	26.96	30278072
166	Phosphorylation	DSSVEVRSDWEVKEE CCCCCCCCCCHHCCC	52.86	20873877
171	Sumoylation	VRSDWEVKEEMDFPQ CCCCCHHCCCCCHHH	36.12	-
171	Sumoylation	VRSDWEVKEEMDFPQ CCCCCHHCCCCCHHH	36.12	-
171	Ubiquitination	VRSDWEVKEEMDFPQ CCCCCHHCCCCCHHH	36.12	-
181	Ubiquitination	MDFPQLMKMRYLEVS CCHHHHHHCCEECCC	28.90	21963094
196	Glutathionylation	EPQDIECCGALEYYD CCCCCCCCCHHHHHH	2.01	22555962
204	Ubiquitination	GALEYYDKAFDRITT CHHHHHHHHHHHHCC	34.53	21963094
208	Methylation	YYDKAFDRITTRSEK HHHHHHHHHCCCCCC	23.00	-
226	Ubiquitination	SIKRIFHTVTTTDDP HHHHHEEECCCCCCH	14.59	-
228	Phosphorylation	KRIFHTVTTTDDPVI HHHEEECCCCCCHHH	25.74	20068231
229	Phosphorylation	RIFHTVTTTDDPVIR HHEEECCCCCCHHHH	24.72	20068231
230	Phosphorylation	IFHTVTTTDDPVIRK HEEECCCCCCHHHHH	29.10	20068231
231	Ubiquitination	FHTVTTTDDPVIRKL EEECCCCCCHHHHHH	57.00	-
241	Phosphorylation	VIRKLAKTQGNVFAT HHHHHHHHCCCHHHH	35.78	22210691
248	Phosphorylation	TQGNVFATDAILATL HCCCHHHHHHHHHHH	17.94	22210691
258	Glutathionylation	ILATLMSCTRSVYSW HHHHHHHCCCCCCCH	1.98	22555962
261	Phosphorylation	TLMSCTRSVYSWDIV HHHHCCCCCCCHHHH	13.78	28152594
263	Phosphorylation	MSCTRSVYSWDIVVQ HHCCCCCCCHHHHEE	12.80	28152594
264	Phosphorylation	SCTRSVYSWDIVVQR HCCCCCCCHHHHEEE	19.00	28152594
265	Ubiquitination	CTRSVYSWDIVVQRV CCCCCCCHHHHEEEE	5.01	21890473
274	Phosphorylation	IVVQRVGSKLFFDKR HHEEEECCCCEEECC	24.27	27134283
275	Ubiquitination	VVQRVGSKLFFDKRD HEEEECCCCEEECCC	43.30	33845483
275	Acetylation	VVQRVGSKLFFDKRD HEEEECCCCEEECCC	43.30	25953088
280	Ubiquitination	GSKLFFDKRDNSDFD CCCCEEECCCCCCCE	57.40	21906983
280	Acetylation	GSKLFFDKRDNSDFD CCCCEEECCCCCCCE	57.40	26051181
284	Phosphorylation	FFDKRDNSDFDLLTV EEECCCCCCCEEEEE	43.90	25693802
301	Ubiquitination	TANEPPQDEGNSFNS CCCCCCCCCCCCCCC	72.10	21890473
308	Phosphorylation	DEGNSFNSPRNLAME CCCCCCCCHHHHHHH	24.19	18669648
315	Ubiquitination	SPRNLAMEATYINHN CHHHHHHHHHEECCC	32.05	21890473
317	Phosphorylation	RNLAMEATYINHNFS HHHHHHHHEECCCHH	16.19	23663014
318	Phosphorylation	NLAMEATYINHNFSQ HHHHHHHEECCCHHH	13.53	27155012
324	Phosphorylation	TYINHNFSQQCLRMG HEECCCHHHHHHHCC	25.34	23663014
327	Glutathionylation	NHNFSQQCLRMGKER CCCHHHHHHHCCHHH	1.70	22555962
335	Ubiquitination	LRMGKERYNFPNPNP HHCCHHHHCCCCCCC	23.42	21890473
349	Ubiquitination	PFVEDDMDKNEIASV CCCCCCCCHHHHHHH	58.59	21890473
350	Ubiquitination	FVEDDMDKNEIASVA CCCCCCCHHHHHHHH	50.25	21906983
350	Acetylation	FVEDDMDKNEIASVA CCCCCCCHHHHHHHH	50.25	26051181
355	Phosphorylation	MDKNEIASVAYRYRR CCHHHHHHHHHHHHH	16.97	30108239
358	Phosphorylation	NEIASVAYRYRRWKL HHHHHHHHHHHHHHC	13.16	30108239
360	Phosphorylation	IASVAYRYRRWKLGD HHHHHHHHHHHHCCC	7.58	30108239
364	Ubiquitination	AYRYRRWKLGDDIDL HHHHHHHHCCCCEEE	40.56	21906983
364	Acetylation	AYRYRRWKLGDDIDL HHHHHHHHCCCCEEE	40.56	26051181
377	Ubiquitination	DLIVRCEHDGVMTGA EEEEEEECCCEECCC	40.53	21890473
381	Sulfoxidation	RCEHDGVMTGANGEV EEECCCEECCCCCEE	3.32	30846556
411	Ubiquitination	CNGVDWRQKLDSQRG CCCCCHHHHHHHCCC	46.54	21890473
412	Ubiquitination	NGVDWRQKLDSQRGA CCCCHHHHHHHCCCE	45.76	24816145
423	O-linked_Glycosylation	QRGAVIATELKNNSY CCCEEEEEECCCCHH	30.63	30379171
426	Methylation	AVIATELKNNSYKLA EEEEEECCCCHHHHH	48.10	-
426	Ubiquitination	AVIATELKNNSYKLA EEEEEECCCCHHHHH	48.10	29967540
426	2-Hydroxyisobutyrylation	AVIATELKNNSYKLA EEEEEECCCCHHHHH	48.10	-
426	Malonylation	AVIATELKNNSYKLA EEEEEECCCCHHHHH	48.10	26320211
426	Acetylation	AVIATELKNNSYKLA EEEEEECCCCHHHHH	48.10	25953088
431	Ubiquitination	ELKNNSYKLARWTCC ECCCCHHHHHHHHHH	35.18	-
431	Acetylation	ELKNNSYKLARWTCC ECCCCHHHHHHHHHH	35.18	26051181
444	Phosphorylation	CCALLAGSEYLKLGY HHHHHHCCCHHHHCC	19.91	28152594
446	Phosphorylation	ALLAGSEYLKLGYVS HHHHCCCHHHHCCEE	15.72	28152594
458	Ubiquitination	YVSRYHVKDSSRHVI CEEEEEECCCCCEEE	38.28	24816145
490	Ubiquitination	SVENAWGILRCVIDI CHHHHHHHHHHHHHH	1.21	21890473
499	Ubiquitination	RCVIDICMKLEEGKY HHHHHHHHHHHCCCE	5.92	21890473
505	Ubiquitination	CMKLEEGKYLILKDP HHHHHCCCEEEEECC	39.91	21906983
505	2-Hydroxyisobutyrylation	CMKLEEGKYLILKDP HHHHHCCCEEEEECC	39.91	-
505	Acetylation	CMKLEEGKYLILKDP HHHHHCCCEEEEECC	39.91	26822725
510	Ubiquitination	EGKYLILKDPNKQVI CCCEEEEECCCCCEE	65.23	32015554
510	Acetylation	EGKYLILKDPNKQVI CCCEEEEECCCCCEE	65.23	26051181
514	Ubiquitination	LILKDPNKQVIRVYS EEEECCCCCEEEEEE	51.86	33845483
514	2-Hydroxyisobutyrylation	LILKDPNKQVIRVYS EEEECCCCCEEEEEE	51.86	-
520	Phosphorylation	NKQVIRVYSLPDGTF CCCEEEEEECCCCCC	8.47	30576142
521	Phosphorylation	KQVIRVYSLPDGTFS CCEEEEEECCCCCCC	30.48	28176443
526	Phosphorylation	VYSLPDGTFSSDEDE EEECCCCCCCCCCCH	27.94	28176443
528	Phosphorylation	SLPDGTFSSDEDEEE ECCCCCCCCCCCHHH	36.40	26503892
529	Phosphorylation	LPDGTFSSDEDEEEE CCCCCCCCCCCHHHH	40.61	26503892
548	Phosphorylation	EEEEEEET------- HHHHHHCC-------	47.38	25137130

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 EIF3D_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EIF3D_HUMAN !!

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 EIF3D_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF3G_HUMAN	EIF3G	physical	9822659
EIF3E_HUMAN	EIF3E	physical	22939629
EIF3H_HUMAN	EIF3H	physical	22939629
EIF3F_HUMAN	EIF3F	physical	22939629
EIF3G_HUMAN	EIF3G	physical	22939629
EIF3K_HUMAN	EIF3K	physical	22939629
EIF3L_HUMAN	EIF3L	physical	22939629
EIF3I_HUMAN	EIF3I	physical	22939629
EIF3M_HUMAN	EIF3M	physical	22939629
NUCL_HUMAN	NCL	physical	22939629
EIF3A_HUMAN	EIF3A	physical	22190034
EIF3B_HUMAN	EIF3B	physical	22190034
EIF3C_HUMAN	EIF3C	physical	22190034
EIF3E_HUMAN	EIF3E	physical	22190034
EIF3F_HUMAN	EIF3F	physical	22190034
EIF3G_HUMAN	EIF3G	physical	22190034
EIF3H_HUMAN	EIF3H	physical	22190034
EIF3I_HUMAN	EIF3I	physical	22190034
EIF3J_HUMAN	EIF3J	physical	22190034
EIF3K_HUMAN	EIF3K	physical	22190034
EIF3L_HUMAN	EIF3L	physical	22190034
EIF3M_HUMAN	EIF3M	physical	22190034
DDX3X_HUMAN	DDX3X	physical	22863883
EIF3A_HUMAN	EIF3A	physical	22863883
EIF3C_HUMAN	EIF3C	physical	22863883
EIF3K_HUMAN	EIF3K	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
RL23A_HUMAN	RPL23A	physical	22863883
RL35_HUMAN	RPL35	physical	22863883
RS11_HUMAN	RPS11	physical	22863883
RS12_HUMAN	RPS12	physical	22863883
RS18_HUMAN	RPS18	physical	22863883
RS20_HUMAN	RPS20	physical	22863883
RS27_HUMAN	RPS27	physical	22863883
RS28_HUMAN	RPS28	physical	22863883
RS4X_HUMAN	RPS4X	physical	22863883
RS9_HUMAN	RPS9	physical	22863883
HOME3_HUMAN	HOMER3	physical	25416956
BEND5_HUMAN	BEND5	physical	25416956
LZTS2_HUMAN	LZTS2	physical	25416956
SRSF5_HUMAN	SRSF5	physical	26344197
SPT4H_HUMAN	SUPT4H1	physical	26344197
RAF1_HUMAN	RAF1	physical	27173435

Drug and Disease Associations

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

Regulatory Network of EIF3D_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions."; Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.; Sci. Signal. 2:RA46-RA46(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-529, ANDMASS SPECTROMETRY.	19690332 [Abstract]
"Phosphoproteome of resting human platelets."; Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.; J. Proteome Res. 7:526-534(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-528 AND SER-529, ANDMASS SPECTROMETRY.	18088087 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-67, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells."; Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.; Nat. Biotechnol. 23:94-101(2005). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-318, AND MASSSPECTROMETRY.	15592455 [Abstract]