AIF1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: AIF1_HUMAN
• UniProt AC: P55008
• Protein Name: Allograft inflammatory factor 1
• Gene Name: AIF1
• Organism: Homo sapiens (Human).
• Sequence Length: 147
• Subcellular Localization: Cytoplasm, cytoskeleton . Cell projection, ruffle membrane ; Peripheral membrane protein ; Cytoplasmic side . Cell projection, phagocytic cup . Associated with the actin cytoskeleton at membrane ruffles and at sites of phagocytosis.
• Protein Description: Actin-binding protein that enhances membrane ruffling and RAC activation. Enhances the actin-bundling activity of LCP1. Binds calcium. Plays a role in RAC signaling and in phagocytosis. May play a role in macrophage activation and function. Promotes the proliferation of vascular smooth muscle cells and of T-lymphocytes. Enhances lymphocyte migration. Plays a role in vascular inflammation..
• Protein Sequence: MSQTRDLQGGKAFGLLKAQQEERLDEINKQFLDDPKYSSDEDLPSKLEGFKEKYMEFDLNGNGDIDIMSLKRMLEKLGVPKTHLELKKLIGEVSSGSGETFSYPDFLRMMLGKRSAILKMILMYEEKAREKEKPTGPPAKKAISELP

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	------MSQTRDLQG ------CCCCCCCCC	40.01	28450419
2	Acetylation	------MSQTRDLQG ------CCCCCCCCC	40.01	-
4	Phosphorylation	----MSQTRDLQGGK ----CCCCCCCCCCH	20.88	27486199
11	Acetylation	TRDLQGGKAFGLLKA CCCCCCCHHHHHHHH	47.57	19608861
11	Ubiquitination	TRDLQGGKAFGLLKA CCCCCCCHHHHHHHH	47.57	21890473
22	Ubiquitination	LLKAQQEERLDEINK HHHHHHHHHHHHHHH	54.96	21890473
37	Phosphorylation	QFLDDPKYSSDEDLP HHHCCCCCCCCCCCC	20.85	28450419
38	Phosphorylation	FLDDPKYSSDEDLPS HHCCCCCCCCCCCCH	37.12	23401153
39	Phosphorylation	LDDPKYSSDEDLPSK HCCCCCCCCCCCCHH	41.76	28355574
45	Phosphorylation	SSDEDLPSKLEGFKE CCCCCCCHHCCCHHH	58.11	28450419
54	Phosphorylation	LEGFKEKYMEFDLNG CCCHHHHHHHCCCCC	11.72	2010525
66 (in isoform 3)	Phosphorylation	-	34.97	-
69	Phosphorylation	NGDIDIMSLKRMLEK CCCCCHHHHHHHHHH	30.95	68735927
69 (in isoform 3)	Phosphorylation	-	30.95	-
76	Ubiquitination	SLKRMLEKLGVPKTH HHHHHHHHHCCCHHH	46.72	21890473
81	Ubiquitination	LEKLGVPKTHLELKK HHHHCCCHHHHHHHH	46.28	-
88	Ubiquitination	KTHLELKKLIGEVSS HHHHHHHHHHCCCCC	58.94	21890473
113	Methylation	FLRMMLGKRSAILKM HHHHHHCCHHHHHHH	38.94	-
124	Phosphorylation	ILKMILMYEEKAREK HHHHHHHHHHHHHHH	19.93	29759185

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
-	K	Ubiquitination	E3 ubiquitin ligase	XIAP	P98170	PMID:22199232

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of AIF1_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 AIF1_HUMAN !!

Protein-Protein Interaction

Oops, there are no PPI records of AIF1_HUMAN !!

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-11, AND MASS SPECTROMETRY.
PubMed: 19608861