dbPTM

IF5_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF5_HUMAN
UniProt AC	P55010
Protein Name	Eukaryotic translation initiation factor 5
Gene Name	EIF5
Organism	Homo sapiens (Human).
Sequence Length	431
Subcellular Localization
Protein Description	Catalyzes the hydrolysis of GTP bound to the 40S ribosomal initiation complex (40S.mRNA.Met-tRNA[F].eIF-2.GTP) with the subsequent joining of a 60S ribosomal subunit resulting in the release of eIF-2 and the guanine nucleotide. The subsequent joining of a 60S ribosomal subunit results in the formation of a functional 80S initiation complex (80S.mRNA.Met-tRNA[F])..
Protein Sequence	MSVNVNRSVSDQFYRYKMPRLIAKVEGKGNGIKTVIVNMVDVAKALNRPPTYPTKYFGCELGAQTQFDVKNDRYIVNGSHEANKLQDMLDGFIKKFVLCPECENPETDLHVNPKKQTIGNSCKACGYRGMLDTHHKLCTFILKNPPENSDSGTGKKEKEKKNRKGKDKENGSVSSSETPPPPPPPNEINPPPHTMEEEEDDDWGEDTTEEAQRRRMDEISDHAKVLTLSDDLERTIEERVNILFDFVKKKKEEGVIDSSDKEIVAEAERLDVKAMGPLVLTEVLFNEKIREQIKKYRRHFLRFCHNNKKAQRYLLHGLECVVAMHQAQLISKIPHILKEMYDADLLEEEVIISWSEKASKKYVSKELAKEIRVKAEPFIKWLKEAEEESSGGEEEDEDENIEVVYSKAASVPKVETVKSDNKDDDIDIDAI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MSVNVNRSV ------CCCCCCCHH	23.54	19413330
2	Phosphorylation	------MSVNVNRSV ------CCCCCCCHH	23.54	22199227
8	Phosphorylation	MSVNVNRSVSDQFYR CCCCCCCHHHHHHHH	22.29	25159151
10	Phosphorylation	VNVNRSVSDQFYRYK CCCCCHHHHHHHHHC	27.26	25159151
14	Phosphorylation	RSVSDQFYRYKMPRL CHHHHHHHHHCCCCE	13.85	29396449
16	Phosphorylation	VSDQFYRYKMPRLIA HHHHHHHHCCCCEEE	10.56	20068231
24	Malonylation	KMPRLIAKVEGKGNG CCCCEEEEEECCCCC	33.55	26320211
24	Acetylation	KMPRLIAKVEGKGNG CCCCEEEEEECCCCC	33.55	23749302
24	Ubiquitination	KMPRLIAKVEGKGNG CCCCEEEEEECCCCC	33.55	-
28	Acetylation	LIAKVEGKGNGIKTV EEEEEECCCCCEEEE	35.38	21466224
33	Acetylation	EGKGNGIKTVIVNMV ECCCCCEEEEEEEHH	37.83	21466224
51	Phosphorylation	KALNRPPTYPTKYFG HHHCCCCCCCCCCCC	44.83	28152594
52	Phosphorylation	ALNRPPTYPTKYFGC HHCCCCCCCCCCCCC	18.06	28152594
54	Phosphorylation	NRPPTYPTKYFGCEL CCCCCCCCCCCCCCC	28.15	28152594
55	Ubiquitination	RPPTYPTKYFGCELG CCCCCCCCCCCCCCC	33.79	21890473
55	Malonylation	RPPTYPTKYFGCELG CCCCCCCCCCCCCCC	33.79	26320211
55	Ubiquitination	RPPTYPTKYFGCELG CCCCCCCCCCCCCCC	33.79	21890473
55	Acetylation	RPPTYPTKYFGCELG CCCCCCCCCCCCCCC	33.79	25953088
59	Glutathionylation	YPTKYFGCELGAQTQ CCCCCCCCCCCCEEE	2.53	22555962
70	Ubiquitination	AQTQFDVKNDRYIVN CEEEEEECCCEEEEC	55.78	-
94	2-Hydroxyisobutyrylation	DMLDGFIKKFVLCPE HHHHHHHHHHCCCCC	37.59	-
95	Ubiquitination	MLDGFIKKFVLCPEC HHHHHHHHHCCCCCC	35.57	-
95	Malonylation	MLDGFIKKFVLCPEC HHHHHHHHHCCCCCC	35.57	26320211
95	Acetylation	MLDGFIKKFVLCPEC HHHHHHHHHCCCCCC	35.57	25953088
114	Malonylation	TDLHVNPKKQTIGNS CCCCCCCCCCCCCCC	52.92	26320211
114	Acetylation	TDLHVNPKKQTIGNS CCCCCCCCCCCCCCC	52.92	25953088
114	Ubiquitination	TDLHVNPKKQTIGNS CCCCCCCCCCCCCCC	52.92	-
115	Ubiquitination	DLHVNPKKQTIGNSC CCCCCCCCCCCCCCC	54.66	-
117	Phosphorylation	HVNPKKQTIGNSCKA CCCCCCCCCCCCCCC	39.47	30257219
121	Phosphorylation	KKQTIGNSCKACGYR CCCCCCCCCCCCCCC	16.28	27251275
136	Acetylation	GMLDTHHKLCTFILK CHHHHCCCCEEHHHC	37.34	25953088
138	Glutathionylation	LDTHHKLCTFILKNP HHHCCCCEEHHHCCC	3.30	22555962
139	Phosphorylation	DTHHKLCTFILKNPP HHCCCCEEHHHCCCC	24.93	28857561
143	Malonylation	KLCTFILKNPPENSD CCEEHHHCCCCCCCC	63.69	26320211
143	Acetylation	KLCTFILKNPPENSD CCEEHHHCCCCCCCC	63.69	26051181
149	Phosphorylation	LKNPPENSDSGTGKK HCCCCCCCCCCCCHH	31.34	22817900
151	Phosphorylation	NPPENSDSGTGKKEK CCCCCCCCCCCHHHH	37.77	30576142
153	Phosphorylation	PENSDSGTGKKEKEK CCCCCCCCCHHHHHH	50.18	30576142
155	Acetylation	NSDSGTGKKEKEKKN CCCCCCCHHHHHHCC	58.56	26051181
172	Phosphorylation	GKDKENGSVSSSETP CCCCCCCCCCCCCCC	30.33	28985074
174	Phosphorylation	DKENGSVSSSETPPP CCCCCCCCCCCCCCC	29.82	11861906
175	Phosphorylation	KENGSVSSSETPPPP CCCCCCCCCCCCCCC	30.00	-
176	Phosphorylation	ENGSVSSSETPPPPP CCCCCCCCCCCCCCC	37.67	-
178	Phosphorylation	GSVSSSETPPPPPPP CCCCCCCCCCCCCCC	42.94	28348404
194	Phosphorylation	EINPPPHTMEEEEDD CCCCCCCCCCCCCCC	31.86	30576142
207	Phosphorylation	DDDWGEDTTEEAQRR CCCCCCCCHHHHHHH	31.63	22817900
208	Phosphorylation	DDWGEDTTEEAQRRR CCCCCCCHHHHHHHH	44.12	22817900
220	Phosphorylation	RRRMDEISDHAKVLT HHHHHHHHHHHEEEE	22.69	26074081
224	2-Hydroxyisobutyrylation	DEISDHAKVLTLSDD HHHHHHHEEEECCHH	34.06	-
227	Phosphorylation	SDHAKVLTLSDDLER HHHHEEEECCHHHHH	27.48	30266825
229	Phosphorylation	HAKVLTLSDDLERTI HHEEEECCHHHHHHH	24.68	29255136
235	Phosphorylation	LSDDLERTIEERVNI CCHHHHHHHHHHHHH	24.30	26074081
248	2-Hydroxyisobutyrylation	NILFDFVKKKKEEGV HHHHHHHHHHHHCCC	59.89	-
249	Ubiquitination	ILFDFVKKKKEEGVI HHHHHHHHHHHCCCC	64.87	-
261	Ubiquitination	GVIDSSDKEIVAEAE CCCCCCCHHHHHHHH	51.82	-
275	Sulfoxidation	ERLDVKAMGPLVLTE HHCCCHHCCHHHHHH	4.75	28465586
288	Ubiquitination	TEVLFNEKIREQIKK HHHHCCHHHHHHHHH	48.44	21890473
308	2-Hydroxyisobutyrylation	LRFCHNNKKAQRYLL HHHHCCCHHHHHHHH	55.60	-
324	Sulfoxidation	GLECVVAMHQAQLIS HHHHHHHHHHHHHHH	1.30	30846556
331	Phosphorylation	MHQAQLISKIPHILK HHHHHHHHHCHHHHH	32.88	24719451
353	Phosphorylation	LEEEVIISWSEKASK CCCCEEEECCHHHCH	17.27	25332170
362	Phosphorylation	SEKASKKYVSKELAK CHHHCHHHCCHHHHH	17.43	22817900
369	Malonylation	YVSKELAKEIRVKAE HCCHHHHHHHHHHHH	67.32	26320211
369	Acetylation	YVSKELAKEIRVKAE HCCHHHHHHHHHHHH	67.32	25953088
374	Malonylation	LAKEIRVKAEPFIKW HHHHHHHHHHHHHHH	36.86	26320211
374	2-Hydroxyisobutyrylation	LAKEIRVKAEPFIKW HHHHHHHHHHHHHHH	36.86	-
389	Phosphorylation	LKEAEEESSGGEEED HHHHHHHHCCCCCCC	37.25	23927012
390	Phosphorylation	KEAEEESSGGEEEDE HHHHHHHCCCCCCCC	54.84	23927012
405	Phosphorylation	DENIEVVYSKAASVP CCCEEEEEEECCCCC	15.05	28176443
406	Phosphorylation	ENIEVVYSKAASVPK CCEEEEEEECCCCCC	12.28	23403867
410	Phosphorylation	VVYSKAASVPKVETV EEEEECCCCCCEEEE	43.76	23911959
413	Sumoylation	SKAASVPKVETVKSD EECCCCCCEEEECCC	51.01	28112733
416	Phosphorylation	ASVPKVETVKSDNKD CCCCCEEEECCCCCC	35.90	30266825
418	Sumoylation	VPKVETVKSDNKDDD CCCEEEECCCCCCCC	60.56	28112733
419	Phosphorylation	PKVETVKSDNKDDDI CCEEEECCCCCCCCC	41.92	30266825
422	Acetylation	ETVKSDNKDDDIDID EEECCCCCCCCCCCC	68.47	26051181

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
207	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
208	T	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
389	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS
390	S	Phosphorylation	Kinase	CSNK2A1	P68400	GPS

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF5_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 IF5_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
IF2B_HUMAN	EIF2S2	physical	10805737
A4_HUMAN	APP	physical	21832049
RL29_HUMAN	RPL29	physical	22939629
PUM1_HUMAN	PUM1	physical	21988832
NEUG_HUMAN	NRGN	physical	21988832
CPNS1_HUMAN	CAPNS1	physical	22863883
DFFA_HUMAN	DFFA	physical	22863883
IF4H_HUMAN	EIF4H	physical	22863883
AGAL_HUMAN	GLA	physical	22863883
HNRPK_HUMAN	HNRNPK	physical	22863883
GRP75_HUMAN	HSPA9	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
MAT2B_HUMAN	MAT2B	physical	22863883
LIS1_HUMAN	PAFAH1B1	physical	22863883
PCY2_HUMAN	PCYT2	physical	22863883
ODPB_HUMAN	PDHB	physical	22863883
SCLY_HUMAN	SCLY	physical	22863883
SMD1_HUMAN	SNRPD1	physical	22863883
TBCB_HUMAN	TBCB	physical	22863883
TBB5_HUMAN	TUBB	physical	22863883
UBFD1_HUMAN	UBFD1	physical	22863883
1433E_HUMAN	YWHAE	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
1433T_HUMAN	YWHAQ	physical	22863883
1433Z_HUMAN	YWHAZ	physical	22863883
DUS12_HUMAN	DUSP12	physical	25416956
RS6_HUMAN	RPS6	physical	21745818
BZW2_HUMAN	BZW2	physical	26344197
CHD4_HUMAN	CHD4	physical	26344197
CHD5_HUMAN	CHD5	physical	26344197
EIF1_HUMAN	EIF1	physical	26344197
IF2A_HUMAN	EIF2S1	physical	26344197
IF2B_HUMAN	EIF2S2	physical	26344197
EIF3B_HUMAN	EIF3B	physical	26344197
EIF3I_HUMAN	EIF3I	physical	26344197
SRSF2_HUMAN	SRSF2	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.

Regulatory Network of IF5_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-10; SER-229; SER-389 ANDSER-390, AND MASS SPECTROMETRY.	19690332 [Abstract]
"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-389 AND SER-390, ANDMASS SPECTROMETRY.	19413330 [Abstract]
"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 SER-10; SER-229; SER-389;SER-390 AND SER-419, AND MASS SPECTROMETRY.	18669648 [Abstract]
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle."; Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.; Mol. Cell 31:438-448(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389 AND SER-390, ANDMASS SPECTROMETRY.	18691976 [Abstract]
"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-149; SER-389; SER-390;TYR-405 AND SER-410, AND MASS SPECTROMETRY.	17287340 [Abstract]
"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-389 AND SER-390, ANDMASS SPECTROMETRY.	17081983 [Abstract]