EIF3C_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: EIF3C_HUMAN
• UniProt AC: Q99613
• Protein Name: Eukaryotic translation initiation factor 3 subunit C {ECO:0000255|HAMAP-Rule:MF_03002}
• Gene Name: EIF3C {ECO:0000255|HAMAP-Rule:MF_03002}
• Organism: Homo sapiens (Human).
• Sequence Length: 913
• Subcellular Localization: Cytoplasm .
• Protein Description: Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is required for several steps in the initiation of protein synthesis. [PubMed: 17581632]
• Protein Sequence: MSRFFTTGSDSESESSLSGEELVTKPVGGNYGKQPLLLSEDEEDTKRVVRSAKDKRFEELTNLIRTIRNAMKIRDVTKCLEEFELLGKAYGKAKSIVDKEGVPRFYIRILADLEDYLNELWEDKEGKKKMNKNNAKALSTLRQKIRKYNRDFESHITSYKQNPEQSADEDAEKNEEDSEGSSDEDEDEDGVSAATFLKKKSEAPSGESRKFLKKMDDEDEDSEDSEDDEDWDTGSTSSDSDSEEEEGKQTALASRFLKKAPTTDEDKKAAEKKREDKAKKKHDRKSKRLDEEEEDNEGGEWERVRGGVPLVKEKPKMFAKGTEITHAVVIKKLNEILQARGKKGTDRAAQIELLQLLVQIAAENNLGEGVIVKIKFNIIASLYDYNPNLATYMKPEMWGKCLDCINELMDILFANPNIFVGENILEESENLHNADQPLRVRGCILTLVERMDEEFTKIMQNTDPHSQEYVEHLKDEAQVCAIIERVQRYLEEKGTTEEVCRIYLLRILHTYYKFDYKAHQRQLTPPEGSSKSEQDQAENEGEDSAVLMERLCKYIYAKDRTDRIRTCAILCHIYHHALHSRWYQARDLMLMSHLQDNIQHADPPVQILYNRTMVQLGICAFRQGLTKDAHNALLDIQSSGRAKELLGQGLLLRSLQERNQEQEKVERRRQVPFHLHINLELLECVYLVSAMLLEIPYMAAHESDARRRMISKQFHHQLRVGERQPLLGPPESMREHVVAASKAMKMGDWKTCHSFIINEKMNGKVWDLFPEADKVRTMLVRKIQEESLRTYLFTYSSVYDSISMETLSDMFELDLPTVHSIISKMIINEELMASLDQPTQTVVMHRTEPTAQQNLALQLAEKLGSLVENNERVFDHKQGTYGGYFRDQKDGYRKNEGYMRRGGYRQQQSQTAY

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
2	Phosphorylation	------MSRFFTTGS ------CCCCCCCCC	37.48	29514088
6	Phosphorylation	--MSRFFTTGSDSES --CCCCCCCCCCCCC	27.77	23927012
7	Phosphorylation	-MSRFFTTGSDSESE -CCCCCCCCCCCCCC	29.54	30278072
9	Phosphorylation	SRFFTTGSDSESESS CCCCCCCCCCCCCCC	35.55	23927012
11	Phosphorylation	FFTTGSDSESESSLS CCCCCCCCCCCCCCC	44.73	23927012
13	Phosphorylation	TTGSDSESESSLSGE CCCCCCCCCCCCCCC	46.89	25159151
15	Phosphorylation	GSDSESESSLSGEEL CCCCCCCCCCCCCCE	45.95	25159151
16	Phosphorylation	SDSESESSLSGEELV CCCCCCCCCCCCCEE	23.62	23927012
18	Phosphorylation	SESESSLSGEELVTK CCCCCCCCCCCEEEC	46.21	23927012
24	Phosphorylation	LSGEELVTKPVGGNY CCCCCEEECCCCCCC	42.11	23927012
31	Phosphorylation	TKPVGGNYGKQPLLL ECCCCCCCCCCCCCC	29.04	23927012
39	Phosphorylation	GKQPLLLSEDEEDTK CCCCCCCCCCHHHHH	42.86	19664994
45	Phosphorylation	LSEDEEDTKRVVRSA CCCCHHHHHHHHHHH	24.83	22167270
61	Phosphorylation	DKRFEELTNLIRTIR HHHHHHHHHHHHHHH	31.12	-
66	Phosphorylation	ELTNLIRTIRNAMKI HHHHHHHHHHHHHHH	19.79	-
78	Acetylation	MKIRDVTKCLEEFEL HHHHHHHHHHHHHHH	36.35	26051181
78	Ubiquitination	MKIRDVTKCLEEFEL HHHHHHHHHHHHHHH	36.35	-
79	Glutathionylation	KIRDVTKCLEEFELL HHHHHHHHHHHHHHH	4.17	22555962
88	Ubiquitination	EEFELLGKAYGKAKS HHHHHHHHHHCCHHH	38.10	-
92	Ubiquitination	LLGKAYGKAKSIVDK HHHHHHCCHHHCCCC	39.71	-
94	Ubiquitination	GKAYGKAKSIVDKEG HHHHCCHHHCCCCCC	44.17	-
95	Phosphorylation	KAYGKAKSIVDKEGV HHHCCHHHCCCCCCC	32.48	22817900
99	Acetylation	KAKSIVDKEGVPRFY CHHHCCCCCCCCHHH	45.53	23236377
99	Ubiquitination	KAKSIVDKEGVPRFY CHHHCCCCCCCCHHH	45.53	-
104	Methylation	VDKEGVPRFYIRILA CCCCCCCHHHHHHHH	34.30	-
124	Ubiquitination	LNELWEDKEGKKKMN HHHHHCCHHHHHHCC	57.77	-
127	Acetylation	LWEDKEGKKKMNKNN HHCCHHHHHHCCHHH	50.76	24431599
128	Acetylation	WEDKEGKKKMNKNNA HCCHHHHHHCCHHHH	69.02	156801
136	Acetylation	KMNKNNAKALSTLRQ HCCHHHHHHHHHHHH	52.57	26051181
136	Malonylation	KMNKNNAKALSTLRQ HCCHHHHHHHHHHHH	52.57	26320211
136	Ubiquitination	KMNKNNAKALSTLRQ HCCHHHHHHHHHHHH	52.57	-
140	Phosphorylation	NNAKALSTLRQKIRK HHHHHHHHHHHHHHH	27.15	-
148	Phosphorylation	LRQKIRKYNRDFESH HHHHHHHHHHHHHHH	12.94	21406692
154	Phosphorylation	KYNRDFESHITSYKQ HHHHHHHHHHHHCCC	21.86	21406692
157	Phosphorylation	RDFESHITSYKQNPE HHHHHHHHHCCCCCC	22.15	21406692
158	Phosphorylation	DFESHITSYKQNPEQ HHHHHHHHCCCCCCC	29.72	21406692
159	Phosphorylation	FESHITSYKQNPEQS HHHHHHHCCCCCCCC	14.14	21406692
160	Ubiquitination	ESHITSYKQNPEQSA HHHHHHCCCCCCCCC	43.28	-
166	Phosphorylation	YKQNPEQSADEDAEK CCCCCCCCCCHHHHH	35.71	29255136
178	Phosphorylation	AEKNEEDSEGSSDED HHHCHHCCCCCCCCC	47.33	26503892
181	Phosphorylation	NEEDSEGSSDEDEDE CHHCCCCCCCCCCCC	30.48	26503892
182	Phosphorylation	EEDSEGSSDEDEDED HHCCCCCCCCCCCCC	56.74	26503892
192	Phosphorylation	DEDEDGVSAATFLKK CCCCCCCCHHHHHHH	20.09	25850435
195	Phosphorylation	EDGVSAATFLKKKSE CCCCCHHHHHHHHCC	29.26	25850435
201	Phosphorylation	ATFLKKKSEAPSGES HHHHHHHCCCCCHHH	48.12	28674151
205	Phosphorylation	KKKSEAPSGESRKFL HHHCCCCCHHHHHHH	63.34	30576142
208	Phosphorylation	SEAPSGESRKFLKKM CCCCCHHHHHHHHHC	44.27	28102081
222	Phosphorylation	MDDEDEDSEDSEDDE CCCCCCCCCCCCCCC	41.05	22210691
225	Phosphorylation	EDEDSEDSEDDEDWD CCCCCCCCCCCCCCC	38.58	25137130
233	Phosphorylation	EDDEDWDTGSTSSDS CCCCCCCCCCCCCCC	28.86	25137130
235	Phosphorylation	DEDWDTGSTSSDSDS CCCCCCCCCCCCCCC	27.49	25137130
236	Phosphorylation	EDWDTGSTSSDSDSE CCCCCCCCCCCCCCH	33.33	22210691
237	Phosphorylation	DWDTGSTSSDSDSEE CCCCCCCCCCCCCHH	33.57	25137130
238	Phosphorylation	WDTGSTSSDSDSEEE CCCCCCCCCCCCHHH	41.02	25137130
240	Phosphorylation	TGSTSSDSDSEEEEG CCCCCCCCCCHHHHH	45.01	22210691
242	Phosphorylation	STSSDSDSEEEEGKQ CCCCCCCCHHHHHHH	51.35	26657352
250	Phosphorylation	EEEEGKQTALASRFL HHHHHHHHHHHHHHH	27.42	24719451
262	Phosphorylation	RFLKKAPTTDEDKKA HHHHHCCCCHHHHHH	52.30	30576142
263	Phosphorylation	FLKKAPTTDEDKKAA HHHHCCCCHHHHHHH	36.01	26657352
277	Acetylation	AEKKREDKAKKKHDR HHHHHHHHHHHHHHH	58.30	-
286	Phosphorylation	KKKHDRKSKRLDEEE HHHHHHHHHCCCHHH	24.73	30624053
287	Acetylation	KKHDRKSKRLDEEEE HHHHHHHHCCCHHHC	61.08	23236377
288	Methylation	KHDRKSKRLDEEEED HHHHHHHCCCHHHCC	55.23	-
303	Methylation	NEGGEWERVRGGVPL CCCCCCEECCCCCCC	25.22	-
304	Methylation	EGGEWERVRGGVPLV CCCCCEECCCCCCCC	4.52	-
305	Methylation	GGEWERVRGGVPLVK CCCCEECCCCCCCCC	42.23	-
306	Methylation	GEWERVRGGVPLVKE CCCEECCCCCCCCCC	38.30	-
312	Ubiquitination	RGGVPLVKEKPKMFA CCCCCCCCCCCCCCC	68.64	-
313	Ubiquitination	GGVPLVKEKPKMFAK CCCCCCCCCCCCCCC	68.09	-
320	Acetylation	EKPKMFAKGTEITHA CCCCCCCCCCCCCHH	55.91	26051181
321	Ubiquitination	KPKMFAKGTEITHAV CCCCCCCCCCCCHHH	25.75	-
331	Acetylation	ITHAVVIKKLNEILQ CCHHHHHHHHHHHHH	39.33	26051181
331	Ubiquitination	ITHAVVIKKLNEILQ CCHHHHHHHHHHHHH	39.33	21906983
332	Ubiquitination	THAVVIKKLNEILQA CHHHHHHHHHHHHHH	45.48	-
333	Ubiquitination	HAVVIKKLNEILQAR HHHHHHHHHHHHHHC	6.21	-
446	Phosphorylation	RVRGCILTLVERMDE HHHHHHHHHHHHCHH	14.62	20068231
447	Phosphorylation	VRGCILTLVERMDEE HHHHHHHHHHHCHHH	3.18	20068231
462	Phosphorylation	FTKIMQNTDPHSQEY HHHHHHCCCCCCHHH	33.73	28851738
466	Phosphorylation	MQNTDPHSQEYVEHL HHCCCCCCHHHHHHH	30.05	28851738
469	Phosphorylation	TDPHSQEYVEHLKDE CCCCCHHHHHHHHHH	11.96	-
470	Phosphorylation	DPHSQEYVEHLKDEA CCCCHHHHHHHHHHH	3.53	-
474	Acetylation	QEYVEHLKDEAQVCA HHHHHHHHHHHHHHH	56.27	26051181
475	Ubiquitination	EYVEHLKDEAQVCAI HHHHHHHHHHHHHHH	63.92	-
493	Acetylation	VQRYLEEKGTTEEVC HHHHHHHCCCHHHHH	52.78	26051181
493	Ubiquitination	VQRYLEEKGTTEEVC HHHHHHHCCCHHHHH	52.78	-
494	Ubiquitination	QRYLEEKGTTEEVCR HHHHHHCCCHHHHHH	40.94	-
513	Acetylation	RILHTYYKFDYKAHQ HHHHHHHHCCHHHHH	22.73	26051181
513	Ubiquitination	RILHTYYKFDYKAHQ HHHHHHHHCCHHHHH	22.73	-
514	Ubiquitination	ILHTYYKFDYKAHQR HHHHHHHCCHHHHHC	7.78	-
517	Acetylation	TYYKFDYKAHQRQLT HHHHCCHHHHHCCCC	41.03	27452117
517	Ubiquitination	TYYKFDYKAHQRQLT HHHHCCHHHHHCCCC	41.03	-
518	Ubiquitination	YYKFDYKAHQRQLTP HHHCCHHHHHCCCCC	9.60	-
524	Phosphorylation	KAHQRQLTPPEGSSK HHHHCCCCCCCCCCH	28.58	25159151
525	Phosphorylation	AHQRQLTPPEGSSKS HHHCCCCCCCCCCHH	33.27	15302935
529	Phosphorylation	QLTPPEGSSKSEQDQ CCCCCCCCCHHHHHH	32.69	30266825
530	Phosphorylation	LTPPEGSSKSEQDQA CCCCCCCCHHHHHHH	51.57	30266825
531	Ubiquitination	TPPEGSSKSEQDQAE CCCCCCCHHHHHHHH	60.76	21890473
532	Phosphorylation	PPEGSSKSEQDQAEN CCCCCCHHHHHHHHH	42.30	25159151
532	Ubiquitination	PPEGSSKSEQDQAEN CCCCCCHHHHHHHHH	42.30	-
533	Phosphorylation	PEGSSKSEQDQAENE CCCCCHHHHHHHHHC	63.01	-
544	Phosphorylation	AENEGEDSAVLMERL HHHCCCHHHHHHHHH	18.90	23322592
548	Acetylation	GEDSAVLMERLCKYI CCHHHHHHHHHHHHH	1.95	19608861
550	Methylation	DSAVLMERLCKYIYA HHHHHHHHHHHHHHH	31.27	-
551	Methylation	SAVLMERLCKYIYAK HHHHHHHHHHHHHHC	1.56	-
553	Acetylation	VLMERLCKYIYAKDR HHHHHHHHHHHHCCC	39.00	26051181
553	Ubiquitination	VLMERLCKYIYAKDR HHHHHHHHHHHHCCC	39.00	-
554	Ubiquitination	LMERLCKYIYAKDRT HHHHHHHHHHHCCCC	9.73	-
558	Acetylation	LCKYIYAKDRTDRIR HHHHHHHCCCCHHHH	30.67	19608861
559	Acetylation	CKYIYAKDRTDRIRT HHHHHHCCCCHHHHH	51.01	19608861
559	Ubiquitination	CKYIYAKDRTDRIRT HHHHHHCCCCHHHHH	51.01	19608861
612	Phosphorylation	VQILYNRTMVQLGIC HHHEECCHHHHHHHH	20.32	-
627	Acetylation	AFRQGLTKDAHNALL HHHCCCCCHHHHHHH	58.94	26051181
627	Ubiquitination	AFRQGLTKDAHNALL HHHCCCCCHHHHHHH	58.94	21906983
628	Ubiquitination	FRQGLTKDAHNALLD HHCCCCCHHHHHHHH	48.07	-
638	Phosphorylation	NALLDIQSSGRAKEL HHHHHHHCCCHHHHH	34.78	20873877
639	Phosphorylation	ALLDIQSSGRAKELL HHHHHHCCCHHHHHH	18.87	20873877
643	Ubiquitination	IQSSGRAKELLGQGL HHCCCHHHHHHHHHH	47.75	21890473
643	Acetylation	IQSSGRAKELLGQGL HHCCCHHHHHHHHHH	47.75	26051181
643	Malonylation	IQSSGRAKELLGQGL HHCCCHHHHHHHHHH	47.75	26320211
643	Ubiquitination	IQSSGRAKELLGQGL HHCCCHHHHHHHHHH	47.75	21890473
644	Ubiquitination	QSSGRAKELLGQGLL HCCCHHHHHHHHHHH	48.52	-
653	Methylation	LGQGLLLRSLQERNQ HHHHHHHHHHHHHHH	34.98	-
654	Methylation	GQGLLLRSLQERNQE HHHHHHHHHHHHHHH	34.08	-
664	Acetylation	ERNQEQEKVERRRQV HHHHHHHHHHHHHHC	49.44	23749302
664	Ubiquitination	ERNQEQEKVERRRQV HHHHHHHHHHHHHHC	49.44	21906983
665	Acetylation	RNQEQEKVERRRQVP HHHHHHHHHHHHHCC	7.33	-
665	Ubiquitination	RNQEQEKVERRRQVP HHHHHHHHHHHHHCC	7.33	-
712	Ubiquitination	ARRRMISKQFHHQLR HHHHHHHHHHHHHCC	46.16	21890473
712	Acetylation	ARRRMISKQFHHQLR HHHHHHHHHHHHHCC	46.16	23749302
712	Ubiquitination	ARRRMISKQFHHQLR HHHHHHHHHHHHHCC	46.16	21906983
713	Acetylation	RRRMISKQFHHQLRV HHHHHHHHHHHHCCC	35.79	-
713	Ubiquitination	RRRMISKQFHHQLRV HHHHHHHHHHHHCCC	35.79	-
719	Methylation	KQFHHQLRVGERQPL HHHHHHCCCCCCCCC	28.02	-
720	Methylation	QFHHQLRVGERQPLL HHHHHCCCCCCCCCC	14.71	-
732	Phosphorylation	PLLGPPESMREHVVA CCCCCCHHHHHHHHH	28.99	22985185
733	Phosphorylation	LLGPPESMREHVVAA CCCCCHHHHHHHHHH	5.78	-
742	Ubiquitination	EHVVAASKAMKMGDW HHHHHHHHHHHCCCC	48.01	-
743	Ubiquitination	HVVAASKAMKMGDWK HHHHHHHHHHCCCCC	10.59	-
745	Acetylation	VAASKAMKMGDWKTC HHHHHHHHCCCCCCC	44.59	25953088
746	Ubiquitination	AASKAMKMGDWKTCH HHHHHHHCCCCCCCE	3.65	-
750	Acetylation	AMKMGDWKTCHSFII HHHCCCCCCCEEEEE	46.12	26051181
751	Phosphorylation	MKMGDWKTCHSFIIN HHCCCCCCCEEEEEE	15.93	21406692
751	Ubiquitination	MKMGDWKTCHSFIIN HHCCCCCCCEEEEEE	15.93	-
752	Glutathionylation	KMGDWKTCHSFIINE HCCCCCCCEEEEEEH	1.94	22555962
754	Phosphorylation	GDWKTCHSFIINEKM CCCCCCEEEEEEHHH	21.93	21406692
755	Phosphorylation	DWKTCHSFIINEKMN CCCCCEEEEEEHHHC	2.64	-
760	Ubiquitination	HSFIINEKMNGKVWD EEEEEEHHHCCCHHH	32.93	-
761	Ubiquitination	SFIINEKMNGKVWDL EEEEEHHHCCCHHHC	6.97	-
764	Acetylation	INEKMNGKVWDLFPE EEHHHCCCHHHCCCC	34.84	26051181
764	Ubiquitination	INEKMNGKVWDLFPE EEHHHCCCHHHCCCC	34.84	-
765	Ubiquitination	NEKMNGKVWDLFPEA EHHHCCCHHHCCCCH	5.22	-
774	Acetylation	DLFPEADKVRTMLVR HCCCCHHHHHHHHHH	40.44	26051181
775	Ubiquitination	LFPEADKVRTMLVRK CCCCHHHHHHHHHHH	6.75	-
787	Phosphorylation	VRKIQEESLRTYLFT HHHHCHHHHHHHHHC	23.54	21406692
788	Phosphorylation	RKIQEESLRTYLFTY HHHCHHHHHHHHHCC	5.54	-
820	Phosphorylation	LDLPTVHSIISKMII CCHHHHHHHHHHHHC	19.79	24719451
839	Phosphorylation	MASLDQPTQTVVMHR HHCCCCCCCEEEEEC	31.10	20860994
841	Phosphorylation	SLDQPTQTVVMHRTE CCCCCCCEEEEECCC	19.97	21601212
847	Phosphorylation	QTVVMHRTEPTAQQN CEEEEECCCCHHHHH	31.47	20860994
862	Ubiquitination	LALQLAEKLGSLVEN HHHHHHHHHHHHHHC	53.17	21890473
862	Ubiquitination	LALQLAEKLGSLVEN HHHHHHHHHHHHHHC	53.17	21906983
863	Ubiquitination	ALQLAEKLGSLVENN HHHHHHHHHHHHHCC	4.19	-
865	Phosphorylation	QLAEKLGSLVENNER HHHHHHHHHHHCCCC	39.41	21815630
866	Phosphorylation	LAEKLGSLVENNERV HHHHHHHHHHCCCCE	5.48	-
877	Ubiquitination	NERVFDHKQGTYGGY CCCEECCCCCCCCCC	52.87	21890473
877	Acetylation	NERVFDHKQGTYGGY CCCEECCCCCCCCCC	52.87	27452117
877	Ubiquitination	NERVFDHKQGTYGGY CCCEECCCCCCCCCC	52.87	21906983
878	Ubiquitination	ERVFDHKQGTYGGYF CCEECCCCCCCCCCC	46.14	-
880	Phosphorylation	VFDHKQGTYGGYFRD EECCCCCCCCCCCCC	19.25	28152594
881	Phosphorylation	FDHKQGTYGGYFRDQ ECCCCCCCCCCCCCC	18.51	28152594
882	Phosphorylation	DHKQGTYGGYFRDQK CCCCCCCCCCCCCCC	24.94	-
884	Phosphorylation	KQGTYGGYFRDQKDG CCCCCCCCCCCCCCC	7.35	28152594
885	Phosphorylation	QGTYGGYFRDQKDGY CCCCCCCCCCCCCCC	8.63	-
889	Ubiquitination	GGYFRDQKDGYRKNE CCCCCCCCCCCCCCC	58.36	21890473
889	Ubiquitination	GGYFRDQKDGYRKNE CCCCCCCCCCCCCCC	58.36	21906983
890	Ubiquitination	GYFRDQKDGYRKNEG CCCCCCCCCCCCCCC	54.44	-
892	Phosphorylation	FRDQKDGYRKNEGYM CCCCCCCCCCCCCCC	28.66	29759185
894	Ubiquitination	DQKDGYRKNEGYMRR CCCCCCCCCCCCCCC	51.36	21906983
895	Ubiquitination	QKDGYRKNEGYMRRG CCCCCCCCCCCCCCC	38.64	-
898	Phosphorylation	GYRKNEGYMRRGGYR CCCCCCCCCCCCCCC	4.93	-
901	Methylation	KNEGYMRRGGYRQQQ CCCCCCCCCCCCCCC	26.76	-
902	Methylation	NEGYMRRGGYRQQQS CCCCCCCCCCCCCCC	27.41	-
904	Phosphorylation	GYMRRGGYRQQQSQT CCCCCCCCCCCCCCC	14.20	26074081
909	Phosphorylation	GGYRQQQSQTAY--- CCCCCCCCCCCC---	25.76	25159151
910	Phosphorylation	GYRQQQSQTAY---- CCCCCCCCCCC----	26.30	16964243
911	Phosphorylation	YRQQQSQTAY----- CCCCCCCCCC-----	32.92	22617229
913	Phosphorylation	QQQSQTAY------- CCCCCCCC-------	23.60	22199227
914	Phosphorylation	QQSQTAY-------- CCCCCCC--------		-

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

Oops, there are no upstream regulatory protein records of EIF3C_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of EIF3C_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of EIF3C_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
EIF3G_HUMAN	EIF3G	physical	16189514
MTOR_HUMAN	MTOR	physical	16286006
KS6B1_HUMAN	RPS6KB1	physical	16286006
EIF3J_HUMAN	EIF3J	physical	15946946
RPTOR_HUMAN	RPTOR	physical	16286006
EIF3G_HUMAN	EIF3G	physical	9822659
EIF3E_HUMAN	EIF3E	physical	22939629
EIF3K_HUMAN	EIF3K	physical	22939629
EIF3G_HUMAN	EIF3G	physical	22939629
EIF3F_HUMAN	EIF3F	physical	22939629
EIF3H_HUMAN	EIF3H	physical	22939629
EIF3D_HUMAN	EIF3D	physical	22939629
EIF3I_HUMAN	EIF3I	physical	22939629
EIF3L_HUMAN	EIF3L	physical	22939629
EIF3M_HUMAN	EIF3M	physical	22939629
RL8_HUMAN	RPL8	physical	22939629
RS24_HUMAN	RPS24	physical	22939629
IF2P_HUMAN	EIF5B	physical	22939629
RS4X_HUMAN	RPS4X	physical	22939629
RS3A_HUMAN	RPS3A	physical	22939629
NUCL_HUMAN	NCL	physical	22939629
MRP1_HUMAN	ABCC1	physical	22939629
ODPX_HUMAN	PDHX	physical	22939629
TIM16_HUMAN	PAM16	physical	22939629
RT35_HUMAN	MRPS35	physical	22939629
RM15_HUMAN	MRPL15	physical	22939629
G45IP_HUMAN	GADD45GIP1	physical	22939629
RM02_HUMAN	MRPL2	physical	22939629
TMEDA_HUMAN	TMED10	physical	22939629
MYH9_HUMAN	MYH9	physical	22939629
NP1L4_HUMAN	NAP1L4	physical	22939629
NP1L1_HUMAN	NAP1L1	physical	22939629
NELFB_HUMAN	NELFB	physical	22863883
EI2BG_HUMAN	EIF2B3	physical	22863883
EIF3A_HUMAN	EIF3A	physical	22863883
EIF3K_HUMAN	EIF3K	physical	22863883
HNRPU_HUMAN	HNRNPU	physical	22863883
LARP1_HUMAN	LARP1	physical	22863883
MTAP2_HUMAN	MAP2	physical	22863883
EIF3B_HUMAN	EIF3B	physical	26344197
EIF3D_HUMAN	EIF3D	physical	26344197
EIF3I_HUMAN	EIF3I	physical	26344197

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.

Related Literatures of Post-Translational Modification

Acetylation

"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-558, AND MASS SPECTROMETRY.
PubMed: 19608861

Phosphorylation

"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-9 AND SER-39, AND MASSSPECTROMETRY.
PubMed: 19690332

"Large-scale proteomics analysis of the human kinome.";
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,Mann M., Daub H.;
Mol. Cell. Proteomics 8:1751-1764(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.
PubMed: 19369195

"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-166, AND MASSSPECTROMETRY.
PubMed: 19413330

"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-6; SER-9; SER-11;SER-13; SER-15; SER-16; SER-18; SER-39; SER-166; SER-178; SER-181 ANDSER-182, AND MASS SPECTROMETRY.
PubMed: 18669648

"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.
PubMed: 18187866

"Evaluation of the low-specificity protease elastase for large-scalephosphoproteome analysis.";
Wang B., Malik R., Nigg E.A., Korner R.;
Anal. Chem. 80:9526-9533(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-166, AND MASSSPECTROMETRY.
PubMed: 19007248

"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry.";
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39 AND SER-166, AND MASSSPECTROMETRY.
PubMed: 17287340

"Structural characterization of the human eukaryotic initiation factor3 protein complex by mass spectrometry.";
Damoc E., Fraser C.S., Zhou M., Videler H., Mayeur G.L.,Hershey J.W.B., Doudna J.A., Robinson C.V., Leary J.A.;
Mol. Cell. Proteomics 6:1135-1146(2007).
Cited for: IDENTIFICATION IN THE EIF-3 COMPLEX, CHARACTERIZATION OF THE EIF-3COMPLEX, PHOSPHORYLATION AT SER-9; SER-11; SER-13; SER-15; SER-16;SER-18; SER-39; SER-166; THR-524 AND SER-909, AND MASS SPECTROMETRY.
PubMed: 17322308

"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-166 AND SER-909,AND MASS SPECTROMETRY.
PubMed: 16964243

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39; SER-95; SER-166;SER-178; SER-181 AND SER-182, AND MASS SPECTROMETRY.
PubMed: 17081983

"Global phosphoproteome analysis on human HepG2 hepatocytes usingreversed-phase diagonal LC.";
Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K.,Demol H., Martens L., Goethals M., Vandekerckhove J.;
Proteomics 5:3589-3599(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, AND MASSSPECTROMETRY.
PubMed: 16097034

"Global phosphoproteome of HT-29 human colon adenocarcinoma cells.";
Kim J.-E., Tannenbaum S.R., White F.M.;
J. Proteome Res. 4:1339-1346(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-909, AND MASSSPECTROMETRY.
PubMed: 16083285

"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-166 AND THR-524, ANDMASS SPECTROMETRY.
PubMed: 15302935