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Q01628 (IFM3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Interferon-induced transmembrane protein 3
Alternative name(s):
Dispanin subfamily A member 2b
Short name=DSPA2b
Interferon-inducible protein 1-8U
Gene names
Name:IFITM3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length133 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

IFN-induced antiviral protein which disrupts intracellular cholesterol homeostasis. Inhibits the entry of viruses to the host cell cytoplasm by preventing viral fusion with cholesterol depleted endosomes. May inactivate new enveloped viruses which buds out of the infected cell, by letting them go out with a cholesterol depleted membrane. Active against multiple viruses, including influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus (MARV) and Ebola virus (EBOV), Dengue virus (DNV), West Nile virus (WNV), human immunodeficiency virus type 1 (HIV-1) and vesicular stomatitis virus (VSV). Can inhibit: influenza virus hemagglutinin protein-mediated viral entry, MARV and EBOV GP1,2-mediated viral entry, SARS-CoV S protein-mediated viral entry and VSV G protein-mediated viral entry. Plays a critical role in the structural stability and function of vacuolar ATPase (v-ATPase). Establishes physical contact with the v-ATPase of endosomes which is critical for proper clathrin localization and is also required for the function of the v-ATPase to lower the pH in phagocytic endosomes thus establishing an antiviral state. Ref.8 Ref.9 Ref.10 Ref.14 Ref.16 Ref.17 Ref.19 Ref.21

Subunit structure

Interacts with ATP6V0B and CD81 By similarity. Interacts with SPP1; the interaction reduces OPN expression. Interacts with VAPA. Ref.11 Ref.21

Subcellular location

Cell membrane; Single-pass type II membrane protein. Late endosome membrane; Single-pass type II membrane protein. Lysosome membrane; Single-pass type II membrane protein Ref.10 Ref.16 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. Ref.12 Ref.18

Not glycosylated. Ref.18

Polyubiquitinated with both 'Lys-48' and 'Lys-63' linkages. Ubiqutination negatively regulates antiviral activity. Lys-24 is the most prevalent ubiquitination site.

Polymorphism

Genetic variations in IFITM3 are responsible for susceptibility to severe influenza virus infection [MIM:614680].

Sequence similarities

Belongs to the CD225/Dispanin family.

Ontologies

Keywords
   Biological processAntiviral defense
Immunity
Innate immunity
   Cellular componentCell membrane
Endosome
Lysosome
Membrane
   Coding sequence diversityPolymorphism
   DomainSignal-anchor
Transmembrane
Transmembrane helix
   PTMIsopeptide bond
Lipoprotein
Palmitate
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcytokine-mediated signaling pathway

Traceable author statement. Source: Reactome

defense response to virus

Inferred from electronic annotation. Source: UniProtKB-KW

immune response

Traceable author statement Ref.1. Source: ProtInc

negative regulation of viral entry into host cell

Inferred from direct assay Ref.10Ref.17. Source: UniProtKB

negative regulation of viral genome replication

Inferred from direct assay Ref.10Ref.17. Source: UniProtKB

negative regulation of viral transcription

Inferred from direct assay Ref.10. Source: UniProtKB

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.10Ref.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

late endosome membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

lysosomal membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.10. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 18486613. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

NAMPTP434903EBI-7932862,EBI-2829310

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 133133Interferon-induced transmembrane protein 3
PRO_0000153729

Regions

Topological domain1 – 5757Cytoplasmic Potential
Intramembrane58 – 7821Helical; Potential
Topological domain79 – 10729Cytoplasmic Potential
Transmembrane108 – 12821Helical; Potential
Topological domain129 – 1335Extracellular Potential
Region60 – 9334Interaction with SPP1
Region108 – 13326Interaction with VAPA

Amino acid modifications

Lipidation711S-palmitoyl cysteine Ref.12 Ref.18
Lipidation721S-palmitoyl cysteine Ref.12 Ref.18
Lipidation1051S-palmitoyl cysteine Ref.12 Ref.18
Cross-link24Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.18
Cross-link83Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.18
Cross-link88Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.18
Cross-link104Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.18

Natural variations

Natural variant31H → Q. Ref.7
Corresponds to variant rs1136853 [ dbSNP | Ensembl ].
VAR_053810

Experimental info

Sequence conflict21N → S in CAA40626. Ref.1
Sequence conflict341A → G in CAA40626. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q01628 [UniParc].

Last modified April 16, 2002. Version 2.
Checksum: 9FFB2E4623F7A1DD

FASTA13314,632
        10         20         30         40         50         60 
MNHTVQTFFS PVNSGQPPNY EMLKEEHEVA VLGAPHNPAP PTSTVIHIRS ETSVPDHVVW 

        70         80         90        100        110        120 
SLFNTLFMNP CCLGFIAFAY SVKSRDRKMV GDVTGAQAYA STAKCLNIWA LILGILMTIL 

       130 
LIVIPVLIFQ AYG 

« Hide

References

« Hide 'large scale' references
[1]"Molecular analysis of a human interferon-inducible gene family."
Lewin A.R., Reid L.E., McMahon M., Stark G.R., Kerr I.M.
Eur. J. Biochem. 199:417-423(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"IFITM3 restricts the morbidity and mortality associated with influenza."
Everitt A.R., Clare S., Pertel T., John S.P., Wash R.S., Smith S.E., Chin C.R., Feeley E.M., Sims J.S., Adams D.J., Wise H.M., Kane L., Goulding D., Digard P., Anttila V., Baillie J.K., Walsh T.S., Hume D.A. expand/collapse author list , Palotie A., Xue Y., Colonna V., Tyler-Smith C., Dunning J., Gordon S.B., Smyth R.L., Openshaw P.J., Dougan G., Brass A.L., Kellam P.
Nature 484:519-523(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INVOLVEMENT IN SUSCEPTIBILITY TO SEVERE INFLUENZA INFECTION.
[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].
[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].
[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].
[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 GLN-3.
Tissue: Brain, Cervix and Vascular endothelial cell.
[8]"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.
[9]"Identification of five interferon-induced cellular proteins that inhibit west nile virus and dengue virus infections."
Jiang D., Weidner J.M., Qing M., Pan X.B., Guo H., Xu C., Zhang X., Birk A., Chang J., Shi P.Y., Block T.M., Guo J.T.
J. Virol. 84:8332-8341(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Interferon-induced cell membrane proteins, IFITM3 and tetherin, inhibit vesicular stomatitis virus infection via distinct mechanisms."
Weidner J.M., Jiang D., Pan X.B., Chang J., Block T.M., Guo J.T.
J. Virol. 84:12646-12657(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[11]"Interferon-induced transmembrane 3 binds osteopontin in vitro: expressed in vivo IFITM3 reduced OPN expression."
El-Tanani M.K., Jin D., Campbell F.C., Johnston P.G.
Oncogene 29:752-762(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SPP1.
[12]"Palmitoylome profiling reveals S-palmitoylation-dependent antiviral activity of IFITM3."
Yount J.S., Moltedo B., Yang Y.Y., Charron G., Moran T.M., Lopez C.B., Hang H.C.
Nat. Chem. Biol. 6:610-614(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PALMITOYLATION AT CYS-71; CYS-72 AND CYS-105.
[13]"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.
[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]"IFITM3 inhibits influenza A virus infection by preventing cytosolic entry."
Feeley E.M., Sims J.S., John S.P., Chin C.R., Pertel T., Chen L.M., Gaiha G.D., Ryan B.J., Donis R.O., Elledge S.J., Brass A.L.
PLoS Pathog. 7:E1002337-E1002337(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[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]"S-palmitoylation and ubiquitination differentially regulate interferon-induced transmembrane protein 3 (IFITM3)-mediated resistance to influenza virus."
Yount J.S., Karssemeijer R.A., Hang H.C.
J. Biol. Chem. 287:19631-19641(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION AT LYS-24; LYS-83; LYS-88 AND LYS-104, PALMITOYLATION, TOPOLOGY, ABSENCE OF GLYCOSYLATION, SUBCELLULAR LOCATION.
[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]"The antiviral effector IFITM3 disrupts intracellular cholesterol homeostasis to block viral entry."
Amini-Bavil-Olyaee S., Choi Y.J., Lee J.H., Shi M., Huang I.C., Farzan M., Jung J.U.
Cell Host Microbe 13:452-464(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH VAPA.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X57352 mRNA. Translation: CAA40626.1.
JQ610571 Genomic DNA. Translation: AFF60305.1.
JQ610572 Genomic DNA. Translation: AFF60306.1.
JQ610573 Genomic DNA. Translation: AFF60307.1.
JQ610574 Genomic DNA. Translation: AFF60308.1.
JQ610575 Genomic DNA. Translation: AFF60309.1.
JQ610576 Genomic DNA. Translation: AFF60310.1.
JQ610577 Genomic DNA. Translation: AFF60311.1.
JQ610578 Genomic DNA. Translation: AFF60312.1.
JQ610579 Genomic DNA. Translation: AFF60313.1.
JQ610580 Genomic DNA. Translation: AFF60314.1.
JQ610581 Genomic DNA. Translation: AFF60315.1.
JQ610582 Genomic DNA. Translation: AFF60316.1.
JQ610583 Genomic DNA. Translation: AFF60317.1.
JQ610585 Genomic DNA. Translation: AFF60319.1.
JQ610586 Genomic DNA. Translation: AFF60320.1.
JQ610587 Genomic DNA. Translation: AFF60321.1.
JQ610588 Genomic DNA. Translation: AFF60322.1.
JQ610589 Genomic DNA. Translation: AFF60323.1.
JQ610590 Genomic DNA. Translation: AFF60324.1.
JQ610591 Genomic DNA. Translation: AFF60325.1.
JQ610592 Genomic DNA. Translation: AFF60326.1.
JQ610593 Genomic DNA. Translation: AFF60327.1.
JQ610594 Genomic DNA. Translation: AFF60328.1.
JQ610595 Genomic DNA. Translation: AFF60329.1.
JQ610596 Genomic DNA. Translation: AFF60330.1.
JQ610597 Genomic DNA. Translation: AFF60331.1.
JQ610598 Genomic DNA. Translation: AFF60332.1.
JQ610599 Genomic DNA. Translation: AFF60333.1.
JQ610600 Genomic DNA. Translation: AFF60334.1.
JQ610601 Genomic DNA. Translation: AFF60335.1.
JQ610602 Genomic DNA. Translation: AFF60336.1.
JQ610603 Genomic DNA. Translation: AFF60337.1.
JQ610604 Genomic DNA. Translation: AFF60338.1.
JQ610605 Genomic DNA. Translation: AFF60339.1.
JQ610606 Genomic DNA. Translation: AFF60340.1.
JQ610607 Genomic DNA. Translation: AFF60341.1.
JQ610608 Genomic DNA. Translation: AFF60342.1.
JQ610609 Genomic DNA. Translation: AFF60343.1.
JQ610610 Genomic DNA. Translation: AFF60344.1.
JQ610611 Genomic DNA. Translation: AFF60345.1.
JQ610613 Genomic DNA. Translation: AFF60347.1.
JQ610614 Genomic DNA. Translation: AFF60348.1.
JQ610615 Genomic DNA. Translation: AFF60349.1.
JQ610616 Genomic DNA. Translation: AFF60350.1.
JQ610617 Genomic DNA. Translation: AFF60351.1.
JQ610618 Genomic DNA. Translation: AFF60352.1.
JQ610620 Genomic DNA. Translation: AFF60354.1.
JQ610621 Genomic DNA. Translation: AFF60355.1.
BT006892 mRNA. Translation: AAP35538.1.
AK292173 mRNA. Translation: BAF84862.1.
AC136475 Genomic DNA. No translation available.
CH891444 Genomic DNA. Translation: EAW50866.1.
BC006794 mRNA. Translation: AAH06794.1.
BC008417 mRNA. Translation: AAH08417.1.
BC022439 mRNA. Translation: AAH22439.1.
BC070243 mRNA. Translation: AAH70243.1.
CCDSCCDS41585.1.
PIRS17182.
RefSeqNP_066362.2. NM_021034.2.
UniGeneHs.374650.

3D structure databases

ProteinModelPortalQ01628.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115681. 4 interactions.
IntActQ01628. 1 interaction.
MINTMINT-2805186.
STRING9606.ENSP00000382707.

PTM databases

PhosphoSiteQ01628.

Polymorphism databases

DMDM20178301.

Proteomic databases

MaxQBQ01628.
PaxDbQ01628.
PRIDEQ01628.

Protocols and materials databases

DNASU10410.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000399808; ENSP00000382707; ENSG00000142089.
GeneID10410.
KEGGhsa:10410.
UCSCuc001lpa.2. human.

Organism-specific databases

CTD10410.
GeneCardsGC11M000319.
HGNCHGNC:5414. IFITM3.
HPAHPA004337.
MIM605579. gene.
614680. phenotype.
neXtProtNX_Q01628.
PharmGKBPA29655.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG26698.
HOGENOMHOG000115781.
HOVERGENHBG001182.
KOK06566.
OMAVLIFQAY.
OrthoDBEOG7288T5.
PhylomeDBQ01628.
TreeFamTF334894.

Enzyme and pathway databases

ReactomeREACT_6900. Immune System.

Gene expression databases

ArrayExpressQ01628.
BgeeQ01628.
CleanExHS_IFITM3.
GenevestigatorQ01628.

Family and domain databases

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

Other

GeneWikiIFITM3.
GenomeRNAi10410.
NextBio39457.
PROQ01628.
SOURCESearch...

Entry information

Entry nameIFM3_HUMAN
AccessionPrimary (citable) accession number: Q01628
Secondary accession number(s): Q53Y76, Q96HK8, Q96J15
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: April 16, 2002
Last modified: July 9, 2014
This is version 120 of the entry and version 2 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