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P13164 (IFM1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon-induced transmembrane protein 1
Alternative name(s):
Dispanin subfamily A member 2a
Short name=DSPA2a
Interferon-induced protein 17
Interferon-inducible protein 9-27
Leu-13 antigen
CD_antigen=CD225
Gene names
Name:IFITM1
Synonyms:CD225, IFI17
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length125 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and hepatitis C virus (HCV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and SARS-CoV S protein-mediated viral entry. Also implicated in cell adhesion and control of cell growth and migration. Plays a key role in the antiproliferative action of IFN-gamma either by inhibiting the ERK activation or by arresting cell growth in G1 phase in a p53-dependent manner. Acts as a positive regulator of osteoblast differentiation. Ref.9 Ref.11 Ref.13 Ref.14 Ref.16 Ref.17 Ref.18 Ref.19

Subunit structure

Interacts with CAV1; this interaction enhances the ability of CAV1 in inhibiting ERK activation. Interacts with CD81. Ref.8 Ref.10

Subcellular location

Cell membrane; Multi-pass membrane protein Ref.10.

Tissue specificity

Bone (at protein level). Levels greatly elevated in colon cancer, cervical cancer, esophageal cancer and ovarian cancer. Expressed in glioma cell lines. Ref.13 Ref.18

Induction

By IFN-alpha and IFNG/IFN-gamma.

Post-translational modification

Palmitoylation on membrane-proximal cysteines controls clustering in membrane compartments and antiviral activity against influenza virus By similarity.

Sequence similarities

Belongs to the CD225/Dispanin family.

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
Osteogenesis
   Cellular componentCell membrane
Membrane
   Coding sequence diversityPolymorphism
   DomainTransmembrane
Transmembrane helix
   PTMLipoprotein
Palmitate
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell surface receptor signaling pathway

Traceable author statement Ref.2. Source: ProtInc

cytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

intracellular signal transduction

Traceable author statement Ref.2. Source: GOC

negative regulation of cell migration

Inferred from mutant phenotype Ref.13. Source: UniProtKB

negative regulation of cell proliferation

Inferred from mutant phenotype Ref.13. Source: UniProtKB

negative regulation of viral entry into host cell

Inferred from direct assay Ref.17. Source: UniProtKB

negative regulation of viral genome replication

Inferred from direct assay Ref.17. Source: UniProtKB

ossification

Inferred from electronic annotation. Source: UniProtKB-KW

positive regulation of osteoblast differentiation

Inferred from mutant phenotype Ref.18. Source: UniProtKB

regulation of immune response

Traceable author statement. Source: Reactome

response to interferon-alpha

Inferred from direct assay Ref.19. Source: UniProtKB

response to interferon-beta

Inferred from direct assay Ref.17. Source: UniProtKB

response to interferon-gamma

Inferred from direct assay Ref.17. Source: UniProtKB

response to virus

Inferred from direct assay Ref.17Ref.19. Source: UniProtKB

type I interferon signaling pathway

Traceable author statement. Source: Reactome

   Cellular_componentintegral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionprotein binding

Inferred from physical interaction Ref.8. Source: UniProtKB

receptor signaling protein activity

Traceable author statement Ref.2. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 125125Interferon-induced transmembrane protein 1
PRO_0000153727

Regions

Topological domain1 – 3636Extracellular Potential
Transmembrane37 – 5721Helical; Potential
Topological domain58 – 8629Cytoplasmic Potential
Transmembrane87 – 10721Helical; Potential
Topological domain108 – 12518Extracellular Potential
Region84 – 12542Interaction with CAV1

Amino acid modifications

Lipidation501S-palmitoyl cysteine By similarity
Lipidation511S-palmitoyl cysteine By similarity
Lipidation841S-palmitoyl cysteine By similarity

Natural variations

Natural variant131P → A. Ref.1 Ref.2 Ref.3 Ref.4 Ref.6 Ref.7 Ref.21
Corresponds to variant rs9667990 [ dbSNP | Ensembl ].
VAR_047422

Experimental info

Sequence conflict1031L → S in AAA35494. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P13164 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 10EE5B64894838ED

FASTA12513,964
        10         20         30         40         50         60 
MHKEEHEVAV LGPPPSTILP RSTVINIHSE TSVPDHVVWS LFNTLFLNWC CLGFIAFAYS 

        70         80         90        100        110        120 
VKSRDRKMVG DVTGAQAYAS TAKCLNIWAL ILGILMTIGF ILLLVFGSVT VYHIMLQIIQ 


EKRGY 

« Hide

References

« Hide 'large scale' references
[1]"A single DNA response element can confer inducibility by both alpha- and gamma-interferons."
Reid L.E., Brasnett A.H., Gilbert C.S., Porter A.C.G., Gewert D.R., Stark G.R., Kerr I.M.
Proc. Natl. Acad. Sci. U.S.A. 86:840-844(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-13.
[2]"Expression cloning of an interferon-inducible 17-kDa membrane protein implicated in the control of cell growth."
Deblandre G.A., Marinx O.P., Evans S.S., Majjaj S., Leo O., Caput D., Huez G.A., Wathelet M.G.
J. Biol. Chem. 270:23860-23866(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANT ALA-13.
[3]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT ALA-13.
[4]"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. expand/collapse author list , 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], VARIANT ALA-13.
Tissue: Brain.
[5]"Human chromosome 11 DNA sequence and analysis including novel gene identification."
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K., Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F., Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E., FitzGerald M.G. expand/collapse author list , Jaffe D.B., LaButti K., Nicol R., Park H.-S., Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W., Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S., Sakaki Y.
Nature 440:497-500(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]Mural R.J., Istrail S., Sutton 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. expand/collapse author list , 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], VARIANT ALA-13.
[7]"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], VARIANT ALA-13.
Tissue: Cervix.
[8]"TAPA-1, the target of an antiproliferative antibody, is associated on the cell surface with the Leu-13 antigen."
Takahashi S., Doss C., Levy S., Levy R.
J. Immunol. 145:2207-2213(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CD81.
[9]"IFITM1 plays an essential role in the antiproliferative action of interferon-gamma."
Yang G., Xu Y., Chen X., Hu G.
Oncogene 26:594-603(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Binding of IFITM1 enhances the inhibiting effect of caveolin-1 on ERK activation."
Xu Y., Yang G., Hu G.
Acta Biochim. Biophys. Sin. 41:488-494(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, INTERACTION WITH CAV1.
[11]"The IFITM proteins mediate cellular resistance to influenza A H1N1 virus, West Nile virus, and dengue virus."
Brass A.L., Huang I.C., Benita Y., John S.P., Krishnan M.N., Feeley E.M., Ryan B.J., Weyer J.L., van der Weyden L., Fikrig E., Adams D.J., Xavier R.J., Farzan M., Elledge S.J.
Cell 139:1243-1254(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN VIRAL RESISTANCE.
[12]"The small interferon-induced transmembrane genes and proteins."
Siegrist F., Ebeling M., Certa U.
J. Interferon Cytokine Res. 31:183-197(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.
[13]"Knockdown of interferon-induced transmembrane protein 1 (IFITM1) inhibits proliferation, migration, and invasion of glioma cells."
Yu F., Ng S.S., Chow B.K., Sze J., Lu G., Poon W.S., Kung H.F., Lin M.C.
J. Neurooncol. 103:187-195(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[14]"The IFITM proteins inhibit HIV-1 infection."
Lu J., Pan Q., Rong L., He W., Liu S.L., Liang C.
J. Virol. 85:2126-2137(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[15]Erratum
Lu J., Pan Q., Rong L., He W., Liu S.L., Liang C.
J. Virol. 85:4043-4043(2011)
[16]"ISG56 and IFITM1 proteins inhibit hepatitis C virus replication."
Raychoudhuri A., Shrivastava S., Steele R., Kim H., Ray R., Ray R.B.
J. Virol. 85:12881-12889(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[17]"Distinct patterns of IFITM-mediated restriction of filoviruses, SARS coronavirus, and influenza A virus."
Huang I.C., Bailey C.C., Weyer J.L., Radoshitzky S.R., Becker M.M., Chiang J.J., Brass A.L., Ahmed A.A., Chi X., Dong L., Longobardi L.E., Boltz D., Kuhn J.H., Elledge S.J., Bavari S., Denison M.R., Choe H., Farzan M.
PLoS Pathog. 7:E1001258-E1001258(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[18]"IFITM1 increases osteogenesis through Runx2 in human alveolar-derived bone marrow stromal cells."
Kim B.S., Kim H.J., Kim J.S., You Y.O., Zadeh H., Shin H.I., Lee S.J., Park Y.J., Takata T., Pi S.H., Lee J., You H.K.
Bone 51:506-514(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, TISSUE SPECIFICITY.
[19]"IFITM proteins restrict antibody-dependent enhancement of dengue virus infection."
Chan Y.K., Huang I.C., Farzan M.
PLoS ONE 7:E34508-E34508(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[20]"The dispanins: a novel gene family of ancient origin that contains 14 human members."
Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.
PLoS ONE 7:E31961-E31961(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENE FAMILY.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] ALA-13, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
J04164 mRNA. Translation: AAA35494.1.
X84958 mRNA. Translation: CAA59337.1.
BT007173 mRNA. Translation: AAP35837.1.
AK290480 mRNA. Translation: BAF83169.1.
AC136475 Genomic DNA. No translation available.
CH471278 Genomic DNA. Translation: EAW61218.1.
BC000897 mRNA. Translation: AAH00897.1.
CCDSCCDS41584.1.
PIRA31454.
RefSeqNP_003632.3. NM_003641.3.
UniGeneHs.458414.

3D structure databases

ProteinModelPortalP13164.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114091. 5 interactions.
DIPDIP-32672N.
IntActP13164. 3 interactions.
MINTMINT-1036538.
STRING9606.ENSP00000386187.

PTM databases

PhosphoSiteP13164.

Polymorphism databases

DMDM215274118.

Proteomic databases

MaxQBP13164.
PaxDbP13164.
PeptideAtlasP13164.
PRIDEP13164.

Protocols and materials databases

DNASU8519.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000328221; ENSP00000330825; ENSG00000185885.
ENST00000408968; ENSP00000386187; ENSG00000185885.
ENST00000528780; ENSP00000437057; ENSG00000185885.
GeneID8519.
KEGGhsa:8519.
UCSCuc001loy.4. human.

Organism-specific databases

CTD8519.
GeneCardsGC11P000313.
HGNCHGNC:5412. IFITM1.
HPACAB017615.
HPA004810.
MIM604456. gene.
neXtProtNX_P13164.
PharmGKBPA29653.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG268489.
HOGENOMHOG000115781.
HOVERGENHBG001182.
InParanoidP13164.
KOK06566.
OMAWCCLGFI.
OrthoDBEOG7288T5.
PhylomeDBP13164.
TreeFamTF334894.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

BgeeP13164.
CleanExHS_IFITM1.
GenevestigatorP13164.

Family and domain databases

InterProIPR007593. CD225/Dispanin_fam.
[Graphical view]
PfamPF04505. Dispanin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSIFITM1. human.
GeneWikiIFITM1.
GenomeRNAi8519.
NextBio31894.
PROP13164.
SOURCESearch...

Entry information

Entry nameIFM1_HUMAN
AccessionPrimary (citable) accession number: P13164
Secondary accession number(s): Q15322, Q53XZ0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 128 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 11

Human chromosome 11: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries