dbPTM

IF5A2_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	IF5A2_HUMAN
UniProt AC	Q9GZV4
Protein Name	Eukaryotic translation initiation factor 5A-2
Gene Name	EIF5A2
Organism	Homo sapiens (Human).
Sequence Length	153
Subcellular Localization	Cytoplasm. Nucleus. Endoplasmic reticulum membrane Peripheral membrane protein Cytoplasmic side. Nucleus, nuclear pore complex. Hypusine modification promotes the nuclear export and cytoplasmic localization and there was a dynamic shift in the loca
Protein Description	mRNA-binding protein involved in translation elongation. Has an important function at the level of mRNA turnover, probably acting downstream of decapping. Involved in actin dynamics and cell cycle progression, mRNA decay and probably in a pathway involved in stress response and maintenance of cell wall integrity. Functions as a regulator of apoptosis. Mediates effects of polyamines on neuronal process extension and survival. May play an important role in brain development and function, and in skeletal muscle stem cell differentiation (By similarity)..
Protein Sequence	MADEIDFTTGDAGASSTYPMQCSALRKNGFVVLKGRPCKIVEMSTSKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDYQLICIQDGYLSLLTETGEVREDLKLPEGELGKEIEGKYNAGEDVQVSVMCAMSEEYAVAIKPCK

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Acetylation	------MADEIDFTT ------CCCCCEECC	24.12	22814378
8	Phosphorylation	MADEIDFTTGDAGAS CCCCCEECCCCCCCC	26.56	25072903
9	Phosphorylation	ADEIDFTTGDAGASS CCCCEECCCCCCCCC	32.81	25072903
15	Phosphorylation	TTGDAGASSTYPMQC CCCCCCCCCCCCCCC	23.46	25072903
16	Phosphorylation	TGDAGASSTYPMQCS CCCCCCCCCCCCCCH	31.27	25072903
17	Phosphorylation	GDAGASSTYPMQCSA CCCCCCCCCCCCCHH	29.20	25072903
18	Phosphorylation	DAGASSTYPMQCSAL CCCCCCCCCCCCHHE	9.92	25072903
23	Phosphorylation	STYPMQCSALRKNGF CCCCCCCHHEECCCE	17.28	25072903
27	Acetylation	MQCSALRKNGFVVLK CCCHHEECCCEEEEC	63.37	42347641
27	Sumoylation	MQCSALRKNGFVVLK CCCHHEECCCEEEEC	63.37	-
27	Sumoylation	MQCSALRKNGFVVLK CCCHHEECCCEEEEC	63.37	-
27	Ubiquitination	MQCSALRKNGFVVLK CCCHHEECCCEEEEC	63.37	22817900
34	Neddylation	KNGFVVLKGRPCKIV CCCEEEECCCEEEEE	41.06	32015554
34	Sumoylation	KNGFVVLKGRPCKIV CCCEEEECCCEEEEE	41.06	-
34	Ubiquitination	KNGFVVLKGRPCKIV CCCEEEECCCEEEEE	41.06	21906983
34	Sumoylation	KNGFVVLKGRPCKIV CCCEEEECCCEEEEE	41.06	-
39	Sumoylation	VLKGRPCKIVEMSTS EECCCEEEEEEEECC	53.09	-
39	Acetylation	VLKGRPCKIVEMSTS EECCCEEEEEEEECC	53.09	42347625
39	Sumoylation	VLKGRPCKIVEMSTS EECCCEEEEEEEECC	53.09	-
39	Ubiquitination	VLKGRPCKIVEMSTS EECCCEEEEEEEECC	53.09	21906983
44	Phosphorylation	PCKIVEMSTSKTGKH EEEEEEEECCCCCCC	18.94	29255136
45	Phosphorylation	CKIVEMSTSKTGKHG EEEEEEECCCCCCCC	32.69	29255136
46	Phosphorylation	KIVEMSTSKTGKHGH EEEEEECCCCCCCCC	22.40	29255136
47	Acetylation	IVEMSTSKTGKHGHA EEEEECCCCCCCCCE	62.48	37092633
47	Ubiquitination	IVEMSTSKTGKHGHA EEEEECCCCCCCCCE	62.48	29967540
50	Other	MSTSKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	14622290
50	Ubiquitination	MSTSKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	22817900
50	Hypusine	MSTSKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	-
55	Ubiquitination	TGKHGHAKVHLVGID CCCCCCEEEEEEEEE	25.23	22817900
65	Phosphorylation	LVGIDIFTGKKYEDI EEEEECCCCCCHHHC	48.72	21712546
67	Sumoylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	-
67	Ubiquitination	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	23000965
67	Sumoylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	-
67	Acetylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	42347637
67	Neddylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	32015554
68	Ubiquitination	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	23000965
68	Sumoylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	Acetylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	42347645
68	Sumoylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	Methylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
69	Phosphorylation	DIFTGKKYEDICPST ECCCCCCHHHCCCCC	23.48	28796482
73	S-nitrosylation	GKKYEDICPSTHNMD CCCHHHCCCCCCCCC	3.17	22126794
73	S-nitrosocysteine	GKKYEDICPSTHNMD CCCHHHCCCCCCCCC	3.17	-
75	Phosphorylation	KYEDICPSTHNMDVP CHHHCCCCCCCCCCC	37.58	25849741
76	Phosphorylation	YEDICPSTHNMDVPN HHHCCCCCCCCCCCC	11.47	25849741
85	Sumoylation	NMDVPNIKRNDYQLI CCCCCCCCCCCEEEE	52.36	-
85	Ubiquitination	NMDVPNIKRNDYQLI CCCCCCCCCCCEEEE	52.36	21906983
85	Sumoylation	NMDVPNIKRNDYQLI CCCCCCCCCCCEEEE	52.36	-
89	Phosphorylation	PNIKRNDYQLICIQD CCCCCCCEEEEEEEC	14.57	24719451
113	Ubiquitination	GEVREDLKLPEGELG CCCCCCCCCCCCCHH	74.45	29967540
121	Ubiquitination	LPEGELGKEIEGKYN CCCCCHHCEEECCCC	69.05	29967540

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 IF5A2_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of IF5A2_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 IF5A2_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
RAB30_HUMAN	RAB30	physical	21988832
PTBP2_HUMAN	PTBP2	physical	21988832
NIF3L_HUMAN	NIF3L1	physical	25416956
MYCBP_HUMAN	MYCBP	physical	26344197
TAGL2_HUMAN	TAGLN2	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 IF5A2_HUMAN

Related Literatures of Post-Translational Modification

Acetylation
Reference	PubMed
"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-47, AND MASS SPECTROMETRY.	19608861 [Abstract]
"Substrate and functional diversity of lysine acetylation revealed bya proteomics survey."; Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.; Mol. Cell 23:607-618(2006). Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-68, AND MASS SPECTROMETRY.	16916647 [Abstract]