Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Allograft inflammatory factor 1

Gene

AIF1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi58 – 69121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi94 – 105122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • calcium ion binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Allograft inflammatory factor 1
Short name:
AIF-1
Alternative name(s):
Ionized calcium-binding adapter molecule 1
Protein G1
Gene namesi
Name:AIF1
Synonyms:G1, IBA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:352. AIF1.

Subcellular locationi

GO - Cellular componenti

  • actin filament Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • lamellipodium Source: UniProtKB
  • nucleus Source: UniProtKB
  • perikaryon Source: Ensembl
  • perinuclear region of cytoplasm Source: UniProtKB
  • phagocytic cup Source: UniProtKB
  • ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA24646.

Polymorphism and mutation databases

BioMutaiAIF1.
DMDMi1703217.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 147146Allograft inflammatory factor 1PRO_0000073865Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei11 – 111N6-acetyllysine1 Publication
Modified residuei39 – 391Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine residues.

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP55008.
PaxDbiP55008.
PRIDEiP55008.

PTM databases

PhosphoSiteiP55008.

Expressioni

Tissue specificityi

Detected in T-lymphocytes and peripheral blood mononuclear cells.1 Publication

Gene expression databases

BgeeiP55008.
CleanExiHS_AIF1.
ExpressionAtlasiP55008. baseline and differential.
GenevisibleiP55008. HS.

Organism-specific databases

HPAiHPA049234.

Interactioni

Subunit structurei

Homodimer (Potential). Monomer. Interacts with LCP1.Curated2 Publications

Protein-protein interaction databases

BioGridi106702. 1 interaction.
IntActiP55008. 2 interactions.
STRINGi9606.ENSP00000365227.

Structurei

Secondary structure

1
147
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi10 – 134Combined sources
Helixi20 – 3213Combined sources
Helixi35 – 373Combined sources
Helixi43 – 5412Combined sources
Helixi67 – 7610Combined sources
Helixi83 – 9311Combined sources
Beta strandi95 – 1017Combined sources
Helixi103 – 1108Combined sources
Beta strandi111 – 1144Combined sources
Helixi117 – 1226Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D58X-ray1.90A17-123[»]
2G2BNMR-A2-147[»]
ProteinModelPortaliP55008.
SMRiP55008. Positions 2-147.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55008.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini45 – 8036EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini81 – 11535EF-hand 2; degeneratePROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG262998.
GeneTreeiENSGT00390000013846.
HOGENOMiHOG000231928.
HOVERGENiHBG004002.
InParanoidiP55008.
KOiK18617.
OrthoDBiEOG73FQPC.
PhylomeDBiP55008.
TreeFamiTF320736.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55008-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MSQTRDLQGG KAFGLLKAQQ EERLDEINKQ FLDDPKYSSD EDLPSKLEGF
60 70 80 90 100
KEKYMEFDLN GNGDIDIMSL KRMLEKLGVP KTHLELKKLI GEVSSGSGET
110 120 130 140
FSYPDFLRMM LGKRSAILKM ILMYEEKARE KEKPTGPPAK KAISELP
Length:147
Mass (Da):16,703
Last modified:October 1, 1996 - v1
Checksum:i0104CCF092074E8F
GO
Isoform 2 (identifier: P55008-2) [UniParc]FASTAAdd to basket

Also known as: G1

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

Show »
Length:93
Mass (Da):10,455
Checksum:i4365FCB38F2B7329
GO
Isoform 3 (identifier: P55008-3) [UniParc]FASTAAdd to basket

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

Show »
Length:132
Mass (Da):14,617
Checksum:iFC69F38ECC92A697
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti33 – 331D → H in AAA92457 (PubMed:8081366).Curated
Sequence conflicti131 – 14717KEKPT…ISELP → RKTNTPPSQESPI in AAA92457 (PubMed:8081366).CuratedAdd
BLAST

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti14 – 141G → R.2 Publications
Corresponds to variant rs2736182 [ dbSNP | Ensembl ].
VAR_048665

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6565MSQTR…GNGDI → MEFDLNGNGDIGEKRVICGG RVVCRPKKTEVSPTCSIPHD LGGGPPTTVGGRRMGMRKWE RRERVSPPSPHPHPLPP in isoform 3. 2 PublicationsVSP_043837Add
BLAST
Alternative sequencei1 – 5454Missing in isoform 2. 3 PublicationsVSP_043838Add
BLAST
Alternative sequencei121 – 14727Missing in isoform 3. 2 PublicationsVSP_043839Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34398.1. [P55008-2]
CCDS4706.1. [P55008-1]
PIRiJC5246.
RefSeqiNP_001614.3. NM_001623.3. [P55008-1]
NP_004838.1. NM_004847.3. [P55008-3]
NP_116573.1. NM_032955.1. [P55008-2]
UniGeneiHs.76364.

Genome annotation databases

EnsembliENST00000376059; ENSP00000365227; ENSG00000204472.
ENST00000383474; ENSP00000372966; ENSG00000206428.
ENST00000413349; ENSP00000416061; ENSG00000235985.
ENST00000414149; ENSP00000391720; ENSG00000237727.
ENST00000425748; ENSP00000398013; ENSG00000234836.
ENST00000440907; ENSP00000397842; ENSG00000235588.
GeneIDi199.
KEGGihsa:199.
UCSCiuc003nuy.3. human. [P55008-1]
uc010jsy.3. human. [P55008-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS34398.1. [P55008-2]
CCDS4706.1. [P55008-1]
PIRiJC5246.
RefSeqiNP_001614.3. NM_001623.3. [P55008-1]
NP_004838.1. NM_004847.3. [P55008-3]
NP_116573.1. NM_032955.1. [P55008-2]
UniGeneiHs.76364.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D58X-ray1.90A17-123[»]
2G2BNMR-A2-147[»]
ProteinModelPortaliP55008.
SMRiP55008. Positions 2-147.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106702. 1 interaction.
IntActiP55008. 2 interactions.
STRINGi9606.ENSP00000365227.

PTM databases

PhosphoSiteiP55008.

Polymorphism and mutation databases

BioMutaiAIF1.
DMDMi1703217.

Proteomic databases

MaxQBiP55008.
PaxDbiP55008.
PRIDEiP55008.

Protocols and materials databases

DNASUi199.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376059; ENSP00000365227; ENSG00000204472.
ENST00000383474; ENSP00000372966; ENSG00000206428.
ENST00000413349; ENSP00000416061; ENSG00000235985.
ENST00000414149; ENSP00000391720; ENSG00000237727.
ENST00000425748; ENSP00000398013; ENSG00000234836.
ENST00000440907; ENSP00000397842; ENSG00000235588.
GeneIDi199.
KEGGihsa:199.
UCSCiuc003nuy.3. human. [P55008-1]
uc010jsy.3. human. [P55008-3]

Organism-specific databases

CTDi199.
GeneCardsiGC06P031582.
GC06Pj31570.
GC06Pk31565.
GC06Pm31659.
GC06Pn31573.
GC06Po31572.
HGNCiHGNC:352. AIF1.
HPAiHPA049234.
MIMi601833. gene.
neXtProtiNX_P55008.
PharmGKBiPA24646.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG262998.
GeneTreeiENSGT00390000013846.
HOGENOMiHOG000231928.
HOVERGENiHBG004002.
InParanoidiP55008.
KOiK18617.
OrthoDBiEOG73FQPC.
PhylomeDBiP55008.
TreeFamiTF320736.

Miscellaneous databases

ChiTaRSiAIF1. human.
EvolutionaryTraceiP55008.
GeneWikiiAIF1.
GenomeRNAii199.
NextBioi796.
PROiP55008.
SOURCEiSearch...

Gene expression databases

BgeeiP55008.
CleanExiHS_AIF1.
ExpressionAtlasiP55008. baseline and differential.
GenevisibleiP55008. HS.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PROSITEiPS50222. EF_HAND_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-39, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  22. "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.
  23. "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.

Entry informationi

Entry nameiAIF1_HUMAN
AccessioniPrimary (citable) accession number: P55008
Secondary accession number(s): A8K406
, O43904, Q9UIV4, Q9UKS9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 22, 2015
This is version 142 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.