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Entry version 164 (13 Feb 2019)
Sequence version 1 (01 Nov 1996)
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Protein

Interferon-induced protein with tetratricopeptide repeats 5

Gene

IFIT5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Interferon-induced RNA-binding protein involved in the human innate immune response. Has a broad and adaptable RNA structure recognition important for RNA recognition specificity in antiviral defense. Binds precursor and processed tRNAs as well as poly-U-tailed tRNA fragments (PubMed:25092312, PubMed:23317505, PubMed:23774268). Specifically binds single-stranded RNA bearing a 5'-triphosphate group (PPP-RNA), thereby acting as a sensor of viral single-stranded RNAs. Single-stranded PPP-RNAs, which lack 2'-O-methylation of the 5' cap and bear a 5'-triphosphate group instead, are specific from viruses, providing a molecular signature to distinguish between self and non-self mRNAs by the host during viral infection. Directly binds PPP-RNA in a non-sequence-specific manner (PubMed:23334420). Also recognizes and selectively binds AT-rich dsDNA (PubMed:23774268). Additionally, as a mediator in innate immunity, regulates positively IKK-NFKB signaling by sinergizing the recruitment of IKK to MAP3K7 (PubMed:26334375).5 Publications

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionRNA-binding, tRNA-binding
Biological processAntiviral defense, Immunity, Innate immunity

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Interferon-induced protein with tetratricopeptide repeats 5
Short name:
IFIT-5
Alternative name(s):
Interferon-induced 58 kDa protein
Retinoic acid- and interferon-inducible 58 kDa protein
Short name:
P58
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:IFIT5
Synonyms:ISG58, RI58
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...
EuPathDBi
HostDB:ENSG00000152778.8

Human Gene Nomenclature Database

More...
HGNCi
HGNC:13328 IFIT5

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
616135 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q13325

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell membrane, Cell projection, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi33E → A: No effect on RNA-binding but changes size profile of RNA bound. Reduces PPP-RNA-binding. 2 Publications1
Mutagenesisi37T → A or V: No effect on RNA-binding but changes size profile of RNA bound. 1 Publication1
Mutagenesisi37T → V: Abolishes PPP-RNA-binding. 1
Mutagenesisi41Q → E: No effect on RNA-binding but changes size profile of RNA bound. Abolishes PPP-RNA-binding. 2 Publications1
Mutagenesisi48K → A or E: Inhibits RNA-binding. 1 Publication1
Mutagenesisi150K → M: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi150K → N or E: Inhibits RNA-binding. 1 Publication1
Mutagenesisi150K → R: Reduces RNA-binding. 1 Publication1
Mutagenesisi156Y → F or A: No effect on RNA-binding. Reduces PPP-RNA-binding. 2 Publications1
Mutagenesisi185 – 186YR → AE: Reduces binding to RNA and DNA. 1 Publication2
Mutagenesisi186R → H or A: Abolishes RNA-binding. 2 Publications1
Mutagenesisi250Y → F: No effect on RNA-binding but changes size profile of RNA bound. Abolishes PPP-RNA-binding. 2 Publications1
Mutagenesisi253 – 254RY → EA: Reduces binding to RNA and DNA. 1 Publication2
Mutagenesisi253R → M: Abolishes RNA-binding. 2 Publications1
Mutagenesisi254Y → F: Abolishes RNA-binding. 2 Publications1
Mutagenesisi257K → E: Reduces binding to RNA and DNA. 1 Publication1
Mutagenesisi260R → E: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi284F → A: Strongly reduces binding to dsDNA. No effect on ssRNA binding. 1 Publication1
Mutagenesisi287H → A: Reduces PPP-RNA-binding. 1 Publication1
Mutagenesisi288Q → E: Abolishes RNA-binding. 2 Publications1
Mutagenesisi291L → A: No effect RNA-binding. 2 Publications1
Mutagenesisi294R → E: Strongly reduces binding to dsDNA. No effect on ssRNA binding. 1 Publication1
Mutagenesisi302K → A: Reduces RNA-binding. 1 Publication1
Mutagenesisi307R → A: Reduces RNA-binding. 25 fold reduction in tRNA-binding. 2 Publications1
Mutagenesisi309K → A: Reduces RNA-binding. 1 Publication1
Mutagenesisi334D → A: No effect on RNA-binding but changes size profile of RNA bound. 1 Publication1
Mutagenesisi337 – 339FAF → AAA: Reduces binding to RNA and DNA. 1 Publication3
Mutagenesisi337F → A: Abolishes PPP-RNA-binding. 1 Publication1
Mutagenesisi339F → A: Reduces RNA-binding. 1 Publication1
Mutagenesisi384R → E: Reduces binding to RNA and DNA and impairs antiviral activity; when associated with E-415. 1 Publication1
Mutagenesisi388 – 389FH → AA: Reduces RNA-binding. 1 Publication2
Mutagenesisi415K → A: Reduces RNA-binding. 25 fold reduction in tRNA-binding. 2 Publications1
Mutagenesisi415K → E: Reduces binding to RNA and DNA and impairs antiviral activity; when associated with E-384. 1 Publication1
Mutagenesisi422 – 426KLSTK → ELSTE: Reduces binding to RNA and DNA. 1 Publication5
Mutagenesisi422K → A: Reduced RNA-binding. 2 Publications1
Mutagenesisi426K → A: Reduces RNA-binding. 5 fold reduction in tRNA-binding. 1 Publication1

Organism-specific databases

DisGeNET

More...
DisGeNETi
24138

Open Targets

More...
OpenTargetsi
ENSG00000152778

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA134988392

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
IFIT5

Domain mapping of disease mutations (DMDM)

More...
DMDMi
6831571

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00001063511 – 482Interferon-induced protein with tetratricopeptide repeats 5Add BLAST482

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q13325

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q13325

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q13325

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q13325

PeptideAtlas

More...
PeptideAtlasi
Q13325

PRoteomics IDEntifications database

More...
PRIDEi
Q13325

ProteomicsDB human proteome resource

More...
ProteomicsDBi
59315

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
Q13325-1 [Q13325-1]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q13325

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q13325

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By interferons (IFNs).

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000152778 Expressed in 221 organ(s), highest expression level in palpebral conjunctiva

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q13325 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
HPA037957
HPA062180

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Monomer (PubMed:23317505, PubMed:23334420, PubMed:23774268). Interacts with MAP3K7 and the components of the IKK core complex CHUK, IKBKB and IKBKG; the interaction synergizes the recruitment of IKK to MAP3K7 and enhances IKK phosphorylation (PubMed:26334375).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei33Interaction with PPP-RNA1
Sitei37Interaction with PPP-RNA1
Sitei41Interaction with PPP-RNA1
Sitei150Interaction with PPP-RNA1
Sitei186Interaction with PPP-RNA1
Sitei250Interaction with PPP-RNA1
Sitei288Interaction with the 5'-triphosphate group of PPP-RNA1

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
117289, 29 interactors

Protein interaction database and analysis system

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IntActi
Q13325, 13 interactors

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000360860

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1482
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZGQX-ray2.20A1-482[»]
4HOQX-ray2.07A1-482[»]
4HORX-ray1.86A1-482[»]
4HOSX-ray2.00A1-482[»]
4HOTX-ray2.50A1-482[»]
4J0UX-ray1.97A1-482[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
Q13325

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q13325

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati51 – 84TPR 1Add BLAST34
Repeati94 – 127TPR 2Add BLAST34
Repeati138 – 173TPR 3Add BLAST36
Repeati181 – 214TPR 4Add BLAST34
Repeati249 – 282TPR 5Add BLAST34
Repeati338 – 371TPR 6Add BLAST34
Repeati376 – 410TPR 7Add BLAST35
Repeati435 – 468TPR 8Add BLAST34

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni254 – 260Interaction with the 5'-triphosphate group of PPP-RNA7

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

RNA recognition is mediated by a convoluted intramolecular fold of the TPR repeats (TPR eddy), which scaffolds unique additional helices that form an RNA binding cleft (PubMed:23317505 and PubMed:23334420). Undergoes a conformational change upon RNA-binding: unliganded exists in a more open conformation, facilitating RNA entry (PubMed:23334420).1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the IFIT family.Curated

Keywords - Domaini

Repeat, TPR repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG1124 Eukaryota
COG0457 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000013876

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000001558

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG066330

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q13325

Identification of Orthologs from Complete Genome Data

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OMAi
NSWDKAL

Database of Orthologous Groups

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OrthoDBi
460948at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q13325

TreeFam database of animal gene trees

More...
TreeFami
TF342671

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.25.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR024125 Interferon_induced_IFIT5
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR013105 TPR_2
IPR019734 TPR_repeat

The PANTHER Classification System

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PANTHERi
PTHR10271:SF24 PTHR10271:SF24, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF07719 TPR_2, 1 hit
PF13181 TPR_8, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00028 TPR, 5 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF48452 SSF48452, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS50005 TPR, 5 hits
PS50293 TPR_REGION, 3 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket
Isoform 1 (identifier: Q13325-1) [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
MSEIRKDTLK AILLELECHF TWNLLKEDID LFEVEDTIGQ QLEFLTTKSR
60 70 80 90 100
LALYNLLAYV KHLKGQNKDA LECLEQAEEI IQQEHSDKEE VRSLVTWGNY
110 120 130 140 150
AWVYYHMDQL EEAQKYTGKI GNVCKKLSSP SNYKLECPET DCEKGWALLK
160 170 180 190 200
FGGKYYQKAK AAFEKALEVE PDNPEFNIGY AITVYRLDDS DREGSVKSFS
210 220 230 240 250
LGPLRKAVTL NPDNSYIKVF LALKLQDVHA EAEGEKYIEE ILDQISSQPY
260 270 280 290 300
VLRYAAKFYR RKNSWNKALE LLKKALEVTP TSSFLHHQMG LCYRAQMIQI
310 320 330 340 350
KKATHNRPKG KDKLKVDELI SSAIFHFKAA MERDSMFAFA YTDLANMYAE
360 370 380 390 400
GGQYSNAEDI FRKALRLENI TDDHKHQIHY HYGRFQEFHR KSENTAIHHY
410 420 430 440 450
LEALKVKDRS PLRTKLTSAL KKLSTKRLCH NALDVQSLSA LGFVYKLEGE
460 470 480
KRQAAEYYEK AQKIDPENAE FLTALCELRL SI
Length:482
Mass (Da):55,847
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i8045BC100384BE05
GO
Isoform 2 (identifier: Q13325-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     158-205: Missing.

Note: No experimental confirmation available.
Show »
Length:434
Mass (Da):50,520
Checksum:i6CA739D6614569C8
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti215S → N in CAG33312 (Ref. 3) Curated1
Sequence conflicti449G → R in BAG35276 (PubMed:14702039).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_056412158 – 205Missing in isoform 2. 1 PublicationAdd BLAST48

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
U34605 mRNA Translation: AAA84934.1
AK293346 mRNA Translation: BAG56862.1
AK312358 mRNA Translation: BAG35276.1
CR457031 mRNA Translation: CAG33312.1
AL353146 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW50135.1
BC025786 mRNA Translation: AAH25786.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS7403.1 [Q13325-1]

Protein sequence database of the Protein Information Resource

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PIRi
G02058

NCBI Reference Sequences

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RefSeqi
NP_036552.1, NM_012420.2 [Q13325-1]

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.252839

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000371795; ENSP00000360860; ENSG00000152778 [Q13325-1]

Database of genes from NCBI RefSeq genomes

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GeneIDi
24138

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:24138

UCSC genome browser

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UCSCi
uc010qnh.3 human [Q13325-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U34605 mRNA Translation: AAA84934.1
AK293346 mRNA Translation: BAG56862.1
AK312358 mRNA Translation: BAG35276.1
CR457031 mRNA Translation: CAG33312.1
AL353146 Genomic DNA No translation available.
CH471066 Genomic DNA Translation: EAW50135.1
BC025786 mRNA Translation: AAH25786.1
CCDSiCCDS7403.1 [Q13325-1]
PIRiG02058
RefSeqiNP_036552.1, NM_012420.2 [Q13325-1]
UniGeneiHs.252839

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3ZGQX-ray2.20A1-482[»]
4HOQX-ray2.07A1-482[»]
4HORX-ray1.86A1-482[»]
4HOSX-ray2.00A1-482[»]
4HOTX-ray2.50A1-482[»]
4J0UX-ray1.97A1-482[»]
ProteinModelPortaliQ13325
SMRiQ13325
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117289, 29 interactors
IntActiQ13325, 13 interactors
STRINGi9606.ENSP00000360860

PTM databases

iPTMnetiQ13325
PhosphoSitePlusiQ13325

Polymorphism and mutation databases

BioMutaiIFIT5
DMDMi6831571

Proteomic databases

EPDiQ13325
jPOSTiQ13325
MaxQBiQ13325
PaxDbiQ13325
PeptideAtlasiQ13325
PRIDEiQ13325
ProteomicsDBi59315
TopDownProteomicsiQ13325-1 [Q13325-1]

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371795; ENSP00000360860; ENSG00000152778 [Q13325-1]
GeneIDi24138
KEGGihsa:24138
UCSCiuc010qnh.3 human [Q13325-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
24138
DisGeNETi24138
EuPathDBiHostDB:ENSG00000152778.8

GeneCards: human genes, protein and diseases

More...
GeneCardsi
IFIT5
HGNCiHGNC:13328 IFIT5
HPAiHPA037957
HPA062180
MIMi616135 gene
neXtProtiNX_Q13325
OpenTargetsiENSG00000152778
PharmGKBiPA134988392

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG1124 Eukaryota
COG0457 LUCA
GeneTreeiENSGT00390000013876
HOGENOMiHOG000001558
HOVERGENiHBG066330
InParanoidiQ13325
OMAiNSWDKAL
OrthoDBi460948at2759
PhylomeDBiQ13325
TreeFamiTF342671

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
IFIT5 human

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
24138

Protein Ontology

More...
PROi
PR:Q13325

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000152778 Expressed in 221 organ(s), highest expression level in palpebral conjunctiva
GenevisibleiQ13325 HS

Family and domain databases

Gene3Di1.25.40.10, 3 hits
InterProiView protein in InterPro
IPR024125 Interferon_induced_IFIT5
IPR013026 TPR-contain_dom
IPR011990 TPR-like_helical_dom_sf
IPR013105 TPR_2
IPR019734 TPR_repeat
PANTHERiPTHR10271:SF24 PTHR10271:SF24, 1 hit
PfamiView protein in Pfam
PF07719 TPR_2, 1 hit
PF13181 TPR_8, 1 hit
SMARTiView protein in SMART
SM00028 TPR, 5 hits
SUPFAMiSSF48452 SSF48452, 1 hit
PROSITEiView protein in PROSITE
PS50005 TPR, 5 hits
PS50293 TPR_REGION, 3 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIFIT5_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q13325
Secondary accession number(s): B2R5X9
, B4DDV1, Q5T7I9, Q6IAX3
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1996
Last modified: February 13, 2019
This is version 164 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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