P55008 (AIF1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Allograft inflammatory factor 1
Short name=AIF-1

Alternative name(s):
Ionized calcium-binding adapter molecule 1
Protein G1

Gene names

Name:	AIF1
Synonyms:	G1, IBA1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	147 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.17 Ref.18 Ref.19
Subunit structure	Homodimer Potential. Monomer. Interacts with LCP1. Ref.18 Ref.19
Subcellular location	Cytoplasm › cytoskeleton. Cell projection › ruffle membrane; Peripheral membrane protein; Cytoplasmic side. Note: Associated with the actin cytoskeleton at membrane ruffles and at sites of phagocytosis.
Tissue specificity	Detected in T-lymphocytes and peripheral blood mononuclear cells. Ref.18
Post-translational modification	Phosphorylated on serine residues.
Sequence similarities	Contains 2 EF-hand domains.

Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Actin-binding Calcium Metal-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Rac protein signal transduction Inferred from sequence or structural similarity. Source: UniProtKB actin filament bundle assembly Inferred from direct assay Ref.19. Source: UniProtKB actin filament polymerization Inferred from direct assay Ref.18. Source: UniProtKB cellular response to interferon-gamma Inferred from expression pattern PubMed 9614071. Source: UniProtKB inflammatory response Inferred from sequence or structural similarity. Source: UniProtKB microglial cell activation Non-traceable author statement Ref.21. Source: UniProtKB negative regulation of smooth muscle cell chemotaxis Inferred from direct assay PubMed 22116621. Source: UniProtKB negative regulation of smooth muscle cell proliferation Inferred from direct assay PubMed 22116621PubMed 9614071. Source: UniProtKB phagocytosis, engulfment Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of G1/S transition of mitotic cell cycle Inferred from direct assay PubMed 11557666Ref.17. Source: UniProtKB positive regulation of T cell migration Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of T cell proliferation Inferred from direct assay Ref.18. Source: UniProtKB positive regulation of monocyte chemotaxis Inferred from direct assay Ref.17. Source: UniProtKB positive regulation of smooth muscle cell chemotaxis Inferred from direct assay PubMed 22116621. Source: UniProtKB positive regulation of smooth muscle cell proliferation Inferred from direct assay Ref.17PubMed 22116621. Source: UniProtKB ruffle assembly Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from direct assay PubMed 22116621. Source: UniProtKB lamellipodium Inferred from sequence or structural similarity. Source: UniProtKB nucleus Inferred from direct assay PubMed 22116621. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay PubMed 9614071. Source: UniProtKB phagocytic cup Inferred from sequence or structural similarity. Source: UniProtKB ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	actin filament binding Inferred from direct assay Ref.18Ref.19. Source: UniProtKB calcium ion binding Inferred from sequence or structural similarity Ref.21. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P55008-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P55008-2)

Also known as: G1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-54: Missing.

Isoform 3 (identifier: P55008-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-65: MSQTRDLQGG...EFDLNGNGDI → MEFDLNGNGD...PSPHPHPLPP
     121-147: Missing.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed By similarity

Chain

2 – 147

146

Allograft inflammatory factor 1

PRO_0000073865

Regions

Domain

45 – 80

36

EF-hand 1

Domain

81 – 115

35

EF-hand 2; degenerate

Calcium binding

58 – 69

12

1 Potential

Calcium binding

94 – 105

12

2 By similarity

Amino acid modifications

Modified residue

2

1

N-acetylserine By similarity

Modified residue

11

1

N6-acetyllysine Ref.20

Natural variations

Alternative sequence

1 – 65

65

MSQTR…GNGDI → MEFDLNGNGDIGEKRVICGG RVVCRPKKTEVSPTCSIPHD LGGGPPTTVGGRRMGMRKWE RRERVSPPSPHPHPLPP in isoform 3.

VSP_043837

Alternative sequence

1 – 54

54

Missing in isoform 2.

VSP_043838

Alternative sequence

121 – 147

27

Missing in isoform 3.

VSP_043839

Natural variant

14

1

G → R. Ref.10 Ref.12
Corresponds to variant rs2736182 [ dbSNP | Ensembl ].

VAR_048665

Experimental info

Sequence conflict

33

1

D → H in AAA92457. Ref.1

Sequence conflict

131 – 147

17

KEKPT…ISELP → RKTNTPPSQESPI in AAA92457. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

147

Helix Strand Turn

Details...

Beta strand

10 – 13

4

Helix

20 – 32

13

Helix

35 – 37

3

Helix

43 – 54

12

Helix

67 – 76

10

Helix

83 – 93

11

Beta strand

95 – 101

7

Helix

103 – 110

8

Beta strand

111 – 114

4

Helix

117 – 122

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified October 1, 1996. Version 1. Checksum: 0104CCF092074E8F	FASTA	147	16,703
	10 20 30 40 50 60 MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF KEKYMEFDLN 70 80 90 100 110 120 GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET FSYPDFLRMM LGKRSAILKM 130 140 ILMYEEKARE KEKPTGPPAK KAISELP
	Isoform 2 (G1) [UniParc]. Checksum: 4365FCB38F2B7329	FASTA	93	10,455
	10 20 30 40 50 60 MEFDLNGNGD IDIMSLKRML EKLGVPKTHL ELKKLIGEVS SGSGETFSYP DFLRMMLGKR 70 80 90 SAILKMILMY EEKAREKEKP TGPPAKKAIS ELP
	Isoform 3 [UniParc]. Checksum: FC69F38ECC92A697	FASTA	132	14,617
	10 20 30 40 50 60 MEFDLNGNGD IGEKRVICGG RVVCRPKKTE VSPTCSIPHD LGGGPPTTVG GRRMGMRKWE 70 80 90 100 110 120 RRERVSPPSP HPHPLPPDIM SLKRMLEKLG VPKTHLELKK LIGEVSSGSG ETFSYPDFLR 130 MMLGKRSAIL KM

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of a novel gene in the human major histocompatibility complex that encodes a potential new member of the I kappa B family of proteins." Albertella M.R., Campbell D.R. Hum. Mol. Genet. 3:793-799(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3).
[2]	"Cloning and genomic characterization of LST1: a new gene in the human TNF region." Holzinger I., de Baey A., Messer G., Kick G., Zwierzina H., Weiss E.H. Immunogenetics 42:315-322(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[3]	"cDNA cloning of human allograft inflammatory factor-1: tissue distribution, cytokine induction, and mRNA expression in injured rat carotid arteries." Autieri M.V. Biochem. Biophys. Res. Commun. 228:29-37(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3). Tissue: Lymphocyte.
[4]	"Allograft inflammatory factory-1. A cytokine-responsive macrophage molecule expressed in transplanted human hearts." Utans U., Quist W.C., McManus B.M., Wilson J.E., Arceci R.J., Wallace A.F., Russell M.E. Transplantation 61:1387-1392(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[5]	"Complex expression pattern of the TNF region gene LST1 through differential regulation, initiation, and alternative splicing." de Baey A., Fellerhoff B., Maier S., Martinozzi S., Weidle U., Weiss E.H. Genomics 45:591-600(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING.
[6]	"A new member of the Ig superfamily and a V-ATPase G subunit are among the predicted products of novel genes close to the TNF locus in the human MHC." Neville M.J., Campbell R.D. J. Immunol. 162:4745-4754(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 1; 2 AND 3).
[7]	"Novel calcium binding protein, Iba1 (ionized calcium binding adapter molecule 1), which is phosphorylated on serine." Imai Y., Ohsawa K., Kohsaka S. Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
[8]	"Upregulation of Allograft inflammatory factor (AIF) is induced by Ab-stimulation in vitro and in human Alzheimer's disease brain." Deininger M.H., Trautmann K. Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Glial tumor.
[9]	Del Galdo F., Artlett C., Jimenez S.A. Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[10]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ARG-14.
[11]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[12]	"Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse." Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L. Genome Res. 13:2621-2636(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT ARG-14.
[13]	"Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region." Shiina S., Tamiya G., Oka A., Inoko H. Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[14]	"The DNA sequence and analysis of human chromosome 6." Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S. Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[16]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Prostate.
[17]	"AIF-1 expression modulates proliferation of human vascular smooth muscle cells by autocrine expression of G-CSF." Chen X., Kelemen S.E., Autieri M.V. Arterioscler. Thromb. Vasc. Biol. 24:1217-1222(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[18]	"Expression of allograft inflammatory factor-1 in T lymphocytes: a role in T-lymphocyte activation and proliferative arteriopathies." Kelemen S.E., Autieri M.V. Am. J. Pathol. 167:619-626(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH ACTIN, TISSUE SPECIFICITY.
[19]	"Structural and functional characterization of human Iba proteins." Schulze J.O., Quedenau C., Roske Y., Adam T., Schueler H., Behlke J., Turnbull A.P., Sievert V., Scheich C., Mueller U., Heinemann U., Buessow K. FEBS J. 275:4627-4640(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBUNIT.
[20]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-11, MASS SPECTROMETRY.
[21]	"X-ray structures of the microglia/macrophage-specific protein Iba1 from human and mouse demonstrate novel molecular conformation change induced by calcium binding." Yamada M., Ohsawa K., Imai Y., Kohsaka S., Kamitori S. J. Mol. Biol. 364:449-457(2006) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 17-123 OF APOPROTEIN.
[22]	"NMR structure of the human allograft inflammatory factor 1." Center for eukaryotic structural genomics (CESG) Submitted (FEB-2009) to the PDB data bank Cited for: STRUCTURE BY NMR OF 2-147.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U49392 mRNA. Translation: AAA92457.1.
U95213 mRNA. Translation: AAC24422.1.
U19713 mRNA. Translation: AAB05003.1.
Y14768 Genomic DNA. Translation: CAA75060.1.
Y14768 Genomic DNA. Translation: CAA75061.1.
Y14768 Genomic DNA. Translation: CAA75062.1.
D86438 mRNA. Translation: BAA13088.1.
AF299327 mRNA. Translation: AAG39110.1.
EF070982 mRNA. Translation: ABK35646.1.
AK290771 mRNA. Translation: BAF83460.1.
CR542153 mRNA. Translation: CAG46950.1.
AF129756 Genomic DNA. Translation: AAD18087.1.
BA000025 Genomic DNA. Translation: BAB63392.1.
AL662847 Genomic DNA. Translation: CAI17694.1.
AL805934 Genomic DNA. Translation: CAI18495.1.
AL662801 Genomic DNA. Translation: CAI18308.1.
AL805934 Genomic DNA. Translation: CAO03652.1.
CR753892 Genomic DNA. Translation: CAQ06958.1.
CR759761 Genomic DNA. Translation: CAQ10844.1.
BX248305 Genomic DNA. Translation: CAM26281.1.
CH471081 Genomic DNA. Translation: EAX03442.1.
CH471081 Genomic DNA. Translation: EAX03446.1.
BC009474 mRNA. Translation: AAH09474.1.

IPI

IPI00022630.

PIR

JC5246.

RefSeq

NP_001614.3. NM_001623.3.
NP_004838.1. NM_004847.3.
NP_116573.1. NM_032955.1.

UniGene

Hs.76364.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D58	X-ray	1.90	A	17-123	[»]
2G2B	NMR	-	A	2-147	[»]

ProteinModelPortal

P55008.

ModBase

Search...

Protein-protein interaction databases

STRING

9606.ENSP00000393996.

PTM databases

PhosphoSite

P55008.

Polymorphism databases

DMDM

1703217.

Proteomic databases

PaxDb

P55008.

PRIDE

P55008.

Protocols and materials databases

DNASU

199.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376049; ENSP00000365217; ENSG00000204472.
ENST00000376059; ENSP00000365227; ENSG00000204472.
ENST00000383473; ENSP00000372965; ENSG00000206428.
ENST00000383474; ENSP00000372966; ENSG00000206428.
ENST00000413349; ENSP00000416061; ENSG00000235985.
ENST00000414149; ENSP00000391720; ENSG00000237727.
ENST00000415830; ENSP00000413709; ENSG00000235985.
ENST00000416422; ENSP00000399901; ENSG00000234836.
ENST00000419376; ENSP00000401433; ENSG00000237727.
ENST00000424944; ENSP00000399621; ENSG00000235588.
ENST00000425748; ENSP00000398013; ENSG00000234836.
ENST00000440907; ENSP00000397842; ENSG00000235588.
ENST00000549432; ENSP00000447578; ENSG00000235588.

GeneID

199.

KEGG

hsa:199.

UCSC

uc003nuy.3. human.
uc010jsy.3. human.

Organism-specific databases

CTD

199.

GeneCards

GC06P031582.

HGNC

HGNC:352. AIF1.

HPA

HPA049234.

MIM

601833. gene.

neXtProt

NX_P55008.

PharmGKB

PA24646.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG262998.

HOGENOM

HOG000231928.

HOVERGEN

HBG004002.

InParanoid

P55008.

OrthoDB

EOG41C6XK.

PhylomeDB

P55008.

Gene expression databases

ArrayExpress

P55008.

Bgee

P55008.

CleanEx

HS_AIF1.

Genevestigator

P55008.

GermOnline

ENSG00000204472. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 1 hit.

InterPro

IPR011992. EF-hand-like_dom.
IPR002048. EF_hand_dom.
[Graphical view]

PROSITE

PS00018. EF_HAND_1. False negative.
PS50222. EF_HAND_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

AIF1. human.

EvolutionaryTrace

P55008.

GenomeRNAi

199.

NextBio

796.

SOURCE

Search...

Entry information

Entry name

AIF1_HUMAN

Accession

Primary (citable) accession number: P55008
Secondary accession number(s): A8K406 , O43904, Q9UIV4, Q9UKS9

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	October 1, 1996
Last modified:	May 29, 2013
This is version 121 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.