IF5AL_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: IF5AL_HUMAN
• UniProt AC: Q6IS14
• Protein Name: Eukaryotic translation initiation factor 5A-1-like
• Gene Name: EIF5AL1
• Organism: Homo sapiens (Human).
• Sequence Length: 154
• 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: MADDLDFETGDAGASATFPMQCSALRKNGFVVLKGWPCKIVEMSASKTGKHGHAKVHLVGIDIFTGKKYEDICPSTHNMDVPNIKRNDFQLIGIQDGYLSLLQDSGEVPEDLRLPEGDLGKEIEQKYDCGEEILITVLSAMTEEAAVAIKAMAK

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
9	Phosphorylation	ADDLDFETGDAGASA CCCCCCCCCCCCCCC	40.11	28355574
15	Phosphorylation	ETGDAGASATFPMQC CCCCCCCCCCCCCCC	27.24	25159151
17	Phosphorylation	GDAGASATFPMQCSA CCCCCCCCCCCCCHH	26.27	24275569
22	S-palmitoylation	SATFPMQCSALRKNG CCCCCCCCHHHHHCC	1.77	26865113
23	Phosphorylation	ATFPMQCSALRKNGF CCCCCCCHHHHHCCE	17.28	27251275
27	Sumoylation	MQCSALRKNGFVVLK CCCHHHHHCCEEEEC	63.37	-
27	Acetylation	MQCSALRKNGFVVLK CCCHHHHHCCEEEEC	63.37	42347661
27	Sumoylation	MQCSALRKNGFVVLK CCCHHHHHCCEEEEC	63.37	-
27	Ubiquitination	MQCSALRKNGFVVLK CCCHHHHHCCEEEEC	63.37	22817900
44	O-linked_Glycosylation	PCKIVEMSASKTGKH EEEEEEEECCCCCCC	18.84	30379171
47	Ubiquitination	IVEMSASKTGKHGHA EEEEECCCCCCCCCE	62.10	29967540
50	Hypusine	MSASKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	-
50	Other	MSASKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	-
50	Ubiquitination	MSASKTGKHGHAKVH EECCCCCCCCCEEEE	52.20	22817900
55	Ubiquitination	TGKHGHAKVHLVGID CCCCCCEEEEEEEEE	25.23	22817900
65	Phosphorylation	LVGIDIFTGKKYEDI EEEEECCCCCCHHHC	48.72	21712546
67	Acetylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	-
67	Sumoylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	-
67	Neddylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	32015554
67	Ubiquitination	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	23000965
67	Sumoylation	GIDIFTGKKYEDICP EEECCCCCCHHHCCC	49.47	-
68	Acetylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	Methylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	Sumoylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	Sumoylation	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	-
68	Ubiquitination	IDIFTGKKYEDICPS EECCCCCCHHHCCCC	56.04	23000965
69	Phosphorylation	DIFTGKKYEDICPST ECCCCCCHHHCCCCC	23.48	28796482
73	Glutathionylation	GKKYEDICPSTHNMD CCCHHHCCCCCCCCC	3.17	22555962
75	Phosphorylation	KYEDICPSTHNMDVP CHHHCCCCCCCCCCC	37.58	25849741
76	Phosphorylation	YEDICPSTHNMDVPN HHHCCCCCCCCCCCC	11.47	25849741
85	Sumoylation	NMDVPNIKRNDFQLI CCCCCCCCCCCCEEE	52.36	-
85	Sumoylation	NMDVPNIKRNDFQLI CCCCCCCCCCCCEEE	52.36	-
85	Ubiquitination	NMDVPNIKRNDFQLI CCCCCCCCCCCCEEE	52.36	23000965
98	Phosphorylation	LIGIQDGYLSLLQDS EEEEECCHHHHHHCC	11.04	-
100	Phosphorylation	GIQDGYLSLLQDSGE EEECCHHHHHHCCCC	20.67	-
113	Methylation	GEVPEDLRLPEGDLG CCCCCCCCCCCCCHH	61.59	-
121	Neddylation	LPEGDLGKEIEQKYD CCCCCHHHHHHHHHC	63.92	32015554
121	Acetylation	LPEGDLGKEIEQKYD CCCCCHHHHHHHHHC	63.92	42347649
121	Ubiquitination	LPEGDLGKEIEQKYD CCCCCHHHHHHHHHC	63.92	27667366
126	Ubiquitination	LGKEIEQKYDCGEEI HHHHHHHHHCCCCHH	30.21	33845483
126	Sumoylation	LGKEIEQKYDCGEEI HHHHHHHHHCCCCHH	30.21	-
126	Sumoylation	LGKEIEQKYDCGEEI HHHHHHHHHCCCCHH	30.21	-
127	Phosphorylation	GKEIEQKYDCGEEIL HHHHHHHHCCCCHHH	19.03	-
129	Glutathionylation	EIEQKYDCGEEILIT HHHHHHCCCCHHHHH	7.20	22555962
150	Ubiquitination	EEAAVAIKAMAK--- HHHHHHHHHHHC---	23.52	33845483

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

Oops, there are no upstream regulatory protein records of IF5AL_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of IF5AL_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 IF5AL_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
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.

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-27, AND MASS SPECTROMETRY.
PubMed: 19608861