UniProt Accession

 AIF1_HUMAN; P55008; A8K406; O43904; Q9UIV4; Q9UKS9 

Genbank Protein ID

 U49392; U95213; U19713; Y14768; Y14768; Y14768; D86438; AF299327; EF070982; AK290771; CR542153; AF129756; BA000025; AL662847; AL805934; AL662801; AL805934; CR753892; CR759761; BX248305; CH471081; CH471081; BC009474 

Genbank Nucleotide ID

 AAA92457.1; AAC24422.1; AAB05003.1; CAA75060.1; CAA75061.1; CAA75062.1; BAA13088.1; AAG39110.1; ABK35646.1; BAF83460.1; CAG46950.1; AAD18087.1; BAB63392.1; CAI17694.1; CAI18495.1; CAI18308.1; CAO03652.1; CAQ06958.1; CAQ10844.1; CAM26281.1; EAX03442.1; EAX03446.1; AAH09474.1 

Protein Name

 Allograft inflammatory factor 1 

Protein Synonyms/Alias

 AIF-1; Ionized calcium-binding adapter molecule 1; Protein G1 

Gene Name

 AIF1 

Gene Synonyms/Alias

 G1; IBA1 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
11	TRDLQGGKAFGLLKA	acetylation	[1]
11	TRDLQGGKAFGLLKA	ubiquitination	[2, 3]
76	SLKRMLEKLGVPKTH	ubiquitination	[2, 3, 4, 5, 6]

Reference

 [1] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [2] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [3] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [4] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [5] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [6] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 

Functional 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. 

Sequence Annotation

 DOMAIN 45 80 EF-hand 1.
 DOMAIN 81 115 EF-hand 2; degenerate.
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 11 11 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Actin-binding; Alternative splicing; Calcium; Cell membrane; Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 147 AA 

Protein Sequence

Gene Ontology

 GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0030027; C:lamellipodium; ISS:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0001891; C:phagocytic cup; ISS:UniProtKB.
 GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
 GO:0051015; F:actin filament binding; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; ISS:UniProtKB.
 GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
 GO:0030041; P:actin filament polymerization; IDA:UniProtKB.
 GO:0071346; P:cellular response to interferon-gamma; IEP:UniProtKB.
 GO:0006954; P:inflammatory response; ISS:UniProtKB.
 GO:0001774; P:microglial cell activation; NAS:UniProtKB.
 GO:0071672; P:negative regulation of smooth muscle cell chemotaxis; IDA:UniProtKB.
 GO:0048662; P:negative regulation of smooth muscle cell proliferation; IDA:UniProtKB.
 GO:0006911; P:phagocytosis, engulfment; ISS:UniProtKB.
 GO:1900087; P:positive regulation of G1/S transition of mitotic cell cycle; IDA:UniProtKB.
 GO:0090026; P:positive regulation of monocyte chemotaxis; IDA:UniProtKB.
 GO:0071673; P:positive regulation of smooth muscle cell chemotaxis; IDA:UniProtKB.
 GO:0048661; P:positive regulation of smooth muscle cell proliferation; IDA:UniProtKB.
 GO:2000406; P:positive regulation of T cell migration; IDA:UniProtKB.
 GO:0042102; P:positive regulation of T cell proliferation; IDA:UniProtKB.
 GO:0016601; P:Rac protein signal transduction; ISS:UniProtKB.
 GO:0097178; P:ruffle assembly; ISS:UniProtKB. 

Interpro

 IPR011992; EF-hand-like_dom.
 IPR002048; EF_hand_dom. 

Pfam

  

SMART

  

PROSITE

 PS00018; EF_HAND_1
 PS50222; EF_HAND_2 

PRINTS