Q9BYX4 (IFIH1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Interferon-induced helicase C domain-containing protein 1
EC=3.6.4.13

Alternative name(s):
Clinically amyopathic dermatomyositis autoantigen 140 kDa
Short name=CADM-140 autoantigen
Helicase with 2 CARD domains
Short name=Helicard
Interferon-induced with helicase C domain protein 1
Melanoma differentiation-associated protein 5
Short name=MDA-5
Murabutide down-regulated protein
RNA helicase-DEAD box protein 116

Gene names

Name:	IFIH1
Synonyms:	MDA5, RH116

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1025 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	RNA helicase that, through its ATP-dependent unwinding of RNA, may function to promote message degradation by specific RNases. Seems to have growth suppressive properties. Involved in innate immune defense against viruses. Upon interaction with intracellular dsRNA produced during viral replication, triggers a transduction cascade involving MAVS/IPS1, which results in the activation of NF-kappa-B, IRF3 and IRF7 and the induction of the expression of antiviral cytokines such as IFN-beta and RANTES (CCL5). ATPase activity is specifically induced by dsRNA. Essential for the production of interferons in response to picornaviruses. Ref.2
Catalytic activity	ATP + H2O = ADP + phosphate.
Cofactor	Zinc.
Subunit structure	Interacts with MAVS. Interacts with V protein of Simian virus 5, Human parainfluenza virus 2, Mumps virus, Sendai virus and Hendra virus. Binding to paramyxoviruses V proteins prevents IFN-beta induction, and the further establishment of an antiviral state. Interacts with PCBP2. Interacts with NLRC5. Ref.7 Ref.8 Ref.9 Ref.11 Ref.12
Subcellular location	Cytoplasm. Nucleus Potential. Note: May be found in the nucleus, during apoptosis. Ref.1 Ref.2
Tissue specificity	Widely expressed, at a low level. Expression is detected at slightly highest levels in placenta, pancreas and spleen and at barely levels in detectable brain, testis and lung. Ref.1 Ref.2 Ref.5
Induction	By IFNB1/IFN-beta and TNF. Ref.1
Post-translational modification	During apoptosis, processed into 3 cleavage products. The helicase-containing fragment, once liberated from the CARD domains, translocate from the cytoplasm to the nucleus. The processed protein significantly sensitizes cells to DNA degradation By similarity.
Involvement in disease	Genetic variation in IFIH1 is associated with diabetes mellitus insulin-dependent type 19 (IDDM19) [MIM:610155]. A multifactorial disorder of glucose homeostasis that is characterized by susceptibility to ketoacidosis in the absence of insulin therapy. Clinical fetaures are polydipsia, polyphagia and polyuria which result from hyperglycemia-induced osmotic diuresis and secondary thirst. These derangements result in long-term complications that affect the eyes, kidneys, nerves, and blood vessels. Ref.15 Note=IFIH1 is the CADM-140 autoantigen, involved in clinically amyopathic dermatomyositis (CADM). This is a chronic inflammatory disorder that shows typical skin manifestations of dermatomyositis but has no or little evidence of clinical myositis. Anti-CADM-140 antibodies appear to be specific to dermatomyositis, especially CADM. Patients with anti-CADM-140 antibodies frequently develop life-threatening acute progressive interstitial lung disease (ILD). Ref.10 Ref.13
Miscellaneous	In HIV-1 infected HeLa-CD4 cells, overexpression of IFIH1 results in a great increase in the level of secreted viral p24 protein.
Sequence similarities	Belongs to the helicase family. Contains 2 CARD domains. Contains 1 helicase ATP-binding domain. Contains 1 helicase C-terminal domain.
Sequence caution	The sequence AAH78180.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence. The sequence BAB71141.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Antiviral defense Host-virus interaction Immunity Innate immunity
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Diabetes mellitus
Domain	Repeat
Ligand	ATP-binding Metal-binding Nucleotide-binding RNA-binding Zinc
Molecular function	Helicase Hydrolase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	detection of virus Traceable author statement. Source: BHF-UCL innate immune response Traceable author statement. Source: Reactome interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of type I interferon production Traceable author statement. Source: Reactome positive regulation of interferon-alpha production Traceable author statement. Source: BHF-UCL positive regulation of interferon-beta production Traceable author statement. Source: BHF-UCL regulation of apoptotic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA binding Inferred from electronic annotation. Source: InterPro double-stranded RNA binding Traceable author statement. Source: BHF-UCL helicase activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction Ref.12. Source: UniProtKB ribonucleoprotein complex binding Inferred from physical interaction Ref.11. Source: UniProtKB zinc ion binding Inferred from direct assay Ref.17Ref.16. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9BYX4-1)

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

Isoform 2 (identifier: Q9BYX4-2)

The sequence of this isoform differs from the canonical sequence as follows:
     208-221: EIENLSQVDGPQVE → GICNFTEEDSSNSA
     222-1025: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1025

1025

Interferon-induced helicase C domain-containing protein 1

PRO_0000102012

Regions

Domain

7 – 97

91

CARD 1

Domain

110 – 190

81

CARD 2

Domain

316 – 509

194

Helicase ATP-binding

Domain

700 – 882

183

Helicase C-terminal

Sites

Metal binding

907

1

Zinc

Metal binding

910

1

Zinc

Metal binding

962

1

Zinc

Metal binding

964

1

Zinc

Site

208 – 209

2

Cleavage By similarity

Site

216 – 217

2

Cleavage By similarity

Site

251 – 252

2

Cleavage By similarity

Amino acid modifications

Modified residue

289

1

Phosphoserine By similarity

Modified residue

301

1

Phosphoserine By similarity

Modified residue

645

1

Phosphoserine By similarity

Natural variations

Alternative sequence

208 – 221

14

EIENL…GPQVE → GICNFTEEDSSNSA in isoform 2.

VSP_013337

Alternative sequence

222 – 1025

804

Missing in isoform 2.

VSP_013338

Natural variant

460

1

H → R.
Corresponds to variant rs10930046 [ dbSNP | Ensembl ].

VAR_031226

Natural variant

843

1

H → R. Ref.2 Ref.3 Ref.4
Corresponds to variant rs3747517 [ dbSNP | Ensembl ].

VAR_021594

Natural variant

946

1

A → T Associated with susceptibility to IDDM19. Ref.3 Ref.4 Ref.15
Corresponds to variant rs1990760 [ dbSNP | Ensembl ].

VAR_021595

Experimental info

Mutagenesis

251

1

D → A: No cleavage and no acceleration of DNA degradation. Ref.5

Mutagenesis

444

1

E → A: No acceleration of DNA degradation, no binding to ATP, and no helicase activity. Ref.5

Sequence conflict

439

1

L → F in AAG54076. Ref.2

Sequence conflict

475

1

N → H in BAB71141. Ref.4

Sequence conflict

592

1

E → K in AAG34368. Ref.1

Sequence conflict

598

1

R → S in AAG54076. Ref.2

Sequence conflict

609

1

E → K in AAG54076. Ref.2

Sequence conflict

782

1

K → R in BAB71141. Ref.4

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

1025

Helix Strand Turn

Details...

Helix

293 – 299

7

Helix

310 – 320

11

Beta strand

325 – 328

4

Helix

332 – 352

21

Beta strand

359 – 365

7

Helix

366 – 375

10

Helix

377 – 381

5

Turn

382 – 384

3

Beta strand

387 – 389

3

Helix

400 – 406

7

Beta strand

408 – 413

6

Helix

414 – 422

9

Helix

434 – 436

3

Beta strand

438 – 442

5

Helix

454 – 473

20

Beta strand

483 – 488

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 20, 2007. Version 3. Checksum: 789CFB4824B92DC9	FASTA	1,025	116,689
	10 20 30 40 50 60 MSNGYSTDEN FRYLISCFRA RVKMYIQVEP VLDYLTFLPA EVKEQIQRTV ATSGNMQAVE 70 80 90 100 110 120 LLLSTLEKGV WHLGWTREFV EALRRTGSPL AARYMNPELT DLPSPSFENA HDEYLQLLNL 130 140 150 160 170 180 LQPTLVDKLL VRDVLDKCME EELLTIEDRN RIAAAENNGN ESGVRELLKR IVQKENWFSA 190 200 210 220 230 240 FLNVLRQTGN NELVQELTGS DCSESNAEIE NLSQVDGPQV EEQLLSTTVQ PNLEKEVWGM 250 260 270 280 290 300 ENNSSESSFA DSSVVSESDT SLAEGSVSCL DESLGHNSNM GSDSGTMGSD SDEENVAARA 310 320 330 340 350 360 SPEPELQLRP YQMEVAQPAL EGKNIIICLP TGSGKTRVAV YIAKDHLDKK KKASEPGKVI 370 380 390 400 410 420 VLVNKVLLVE QLFRKEFQPF LKKWYRVIGL SGDTQLKISF PEVVKSCDII ISTAQILENS 430 440 450 460 470 480 LLNLENGEDA GVQLSDFSLI IIDECHHTNK EAVYNNIMRH YLMQKLKNNR LKKENKPVIP 490 500 510 520 530 540 LPQILGLTAS PGVGGATKQA KAEEHILKLC ANLDAFTIKT VKENLDQLKN QIQEPCKKFA 550 560 570 580 590 600 IADATREDPF KEKLLEIMTR IQTYCQMSPM SDFGTQPYEQ WAIQMEKKAA KEGNRKERVC 610 620 630 640 650 660 AEHLRKYNEA LQINDTIRMI DAYTHLETFY NEEKDKKFAV IEDDSDEGGD DEYCDGDEDE 670 680 690 700 710 720 DDLKKPLKLD ETDRFLMTLF FENNKMLKRL AENPEYENEK LTKLRNTIME QYTRTEESAR 730 740 750 760 770 780 GIIFTKTRQS AYALSQWITE NEKFAEVGVK AHHLIGAGHS SEFKPMTQNE QKEVISKFRT 790 800 810 820 830 840 GKINLLIATT VAEEGLDIKE CNIVIRYGLV TNEIAMVQAR GRARADESTY VLVAHSGSGV 850 860 870 880 890 900 IEHETVNDFR EKMMYKAIHC VQNMKPEEYA HKILELQMQS IMEKKMKTKR NIAKHYKNNP 910 920 930 940 950 960 SLITFLCKNC SVLACSGEDI HVIEKMHHVN MTPEFKELYI VRENKALQKK CADYQINGEI 970 980 990 1000 1010 1020 ICKCGQAWGT MMVHKGLDLP CLKIRNFVVV FKNNSTKKQY KKWVELPITF PNLDYSECCL FSDED
	Isoform 2 [UniParc]. Checksum: 3C7139ECAC564BB5	FASTA	221	25,129
	10 20 30 40 50 60 MSNGYSTDEN FRYLISCFRA RVKMYIQVEP VLDYLTFLPA EVKEQIQRTV ATSGNMQAVE 70 80 90 100 110 120 LLLSTLEKGV WHLGWTREFV EALRRTGSPL AARYMNPELT DLPSPSFENA HDEYLQLLNL 130 140 150 160 170 180 LQPTLVDKLL VRDVLDKCME EELLTIEDRN RIAAAENNGN ESGVRELLKR IVQKENWFSA 190 200 210 220 FLNVLRQTGN NELVQELTGS DCSESNAGIC NFTEEDSSNS A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"mda-5: an interferon-inducible putative RNA helicase with double-stranded RNA-dependent ATPase activity and melanoma growth-suppressive properties." Kang D.-C., Gopalkrishnan R.V., Wu Q., Jankowsky E., Pyle A.M., Fisher P.B. Proc. Natl. Acad. Sci. U.S.A. 99:637-642(2002) [PubMed: 11805321] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INDUCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY. Tissue: Melanoma.
[2]	"A novel cellular RNA helicase, RH116, differentially regulates cell growth, programmed cell death and human immunodeficiency virus type 1 replication." Cocude C., Truong M.-J., Billaut-Mulot O., Delsart V., Darcissac E., Capron A., Mouton Y., Bahr G.M. J. Gen. Virol. 84:3215-3225(2003) [PubMed: 14645903] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, VARIANT ARG-843. Tissue: Spleen.
[3]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANTS ARG-843 AND THR-946. Tissue: Uterus.
[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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 475-1025 (ISOFORM 1), VARIANTS ARG-843 AND THR-946.
[5]	"Overexpression of Helicard, a CARD-containing helicase cleaved during apoptosis, accelerates DNA degradation." Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K., Tschopp J. Curr. Biol. 12:838-843(2002) [PubMed: 12015121] [Abstract] Cited for: MUTAGENESIS OF ASP-251 AND GLU-444, TISSUE SPECIFICITY.
[6]	Erratum Kovacsovics M., Martinon F., Micheau O., Bodmer J.-L., Hofmann K., Tschopp J. Curr. Biol. 12:1633-1633(2002)
[7]	"The V proteins of paramyxoviruses bind the IFN-inducible RNA helicase, mda-5, and inhibit its activation of the IFN-beta promoter." Andrejeva J., Childs K.S., Young D.F., Carlos T.S., Stock N., Goodbourn S., Randall R.E. Proc. Natl. Acad. Sci. U.S.A. 101:17264-17269(2004) [PubMed: 15563593] [Abstract] Cited for: INTERACTION WITH PARAMYXOVIRUSES V PROTEIN.
[8]	"IPS-1, an adaptor triggering RIG-I- and Mda5-mediated type I interferon induction." Kawai T., Takahashi K., Sato S., Coban C., Kumar H., Kato H., Ishii K.J., Takeuchi O., Akira S. Nat. Immunol. 6:981-988(2005) [PubMed: 16127453] [Abstract] Cited for: INTERACTION WITH MAVS.
[9]	"Cardif is an adaptor protein in the RIG-I antiviral pathway and is targeted by hepatitis C virus." Meylan E., Curran J., Hofmann K., Moradpour D., Binder M., Bartenschlager R., Tschopp J. Nature 437:1167-1172(2005) [PubMed: 16177806] [Abstract] Cited for: INTERACTION WITH MAVS.
[10]	"RNA helicase encoded by melanoma differentiation-associated gene 5 is a major autoantigen in patients with clinically amyopathic dermatomyositis: Association with rapidly progressive interstitial lung disease." Sato S., Hoshino K., Satoh T., Fujita T., Kawakami Y., Fujita T., Kuwana M. Arthritis Rheum. 60:2193-2200(2009) [PubMed: 19565506] [Abstract] Cited for: INVOLVEMENT IN CLINICALLY AMYOPATHIC DERMATOMYOSITIS, IDENTIFICATION AS CADM-140 AUTOANTIGEN.
[11]	"PCBP2 mediates degradation of the adaptor MAVS via the HECT ubiquitin ligase AIP4." You F., Sun H., Zhou X., Sun W., Liang S., Zhai Z., Jiang Z. Nat. Immunol. 10:1300-1308(2009) [PubMed: 19881509] [Abstract] Cited for: INTERACTION WITH PCBP2.
[12]	"NLRC5 negatively regulates the NF-kappaB and type I interferon signaling pathways." Cui J., Zhu L., Xia X., Wang H.Y., Legras X., Hong J., Ji J., Shen P., Zheng S., Chen Z.J., Wang R.F. Cell 141:483-496(2010) [PubMed: 20434986] [Abstract] Cited for: INTERACTION WITH NLRC5.
[13]	"The RIG-I-like receptor IFIH1/MDA5 is a dermatomyositis-specific autoantigen identified by the anti-CADM-140 antibody." Nakashima R., Imura Y., Kobayashi S., Yukawa N., Yoshifuji H., Nojima T., Kawabata D., Ohmura K., Usui T., Fujii T., Okawa K., Mimori T. Rheumatology 49:433-440(2010) [PubMed: 20015976] [Abstract] Cited for: INVOLVEMENT IN CLINICALLY AMYOPATHIC DERMATOMYOSITIS, IDENTIFICATION AS CADM-140 AUTOANTIGEN, MASS SPECTROMETRY.
[14]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"A genome-wide association study of nonsynonymous SNPs identifies a type 1 diabetes locus in the interferon-induced helicase (IFIH1) region." Smyth D.J., Cooper J.D., Bailey R., Field S., Burren O., Smink L.J., Guja C., Ionescu-Tirgoviste C., Widmer B., Dunger D.B., Savage D.A., Walker N.M., Clayton D.G., Todd J.A. Nat. Genet. 38:617-619(2006) [PubMed: 16699517] [Abstract] Cited for: VARIANT THR-946, ASSOCIATION WITH IDDM19.
[16]	"Structural basis of double-stranded RNA recognition by the RIG-I like receptor MDA5." Li X., Lu C., Stewart M., Xu H., Strong R.K., Igumenova T., Li P. Arch. Biochem. Biophys. 488:23-33(2009) [PubMed: 19531363] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS) OF 893-1017 IN COMPLEX WITH ZINC IONS.
[17]	"Solution structures of cytosolic RNA sensor MDA5 and LGP2 C-terminal domains: identification of the RNA recognition loop in RIG-I-like receptors." Takahasi K., Kumeta H., Tsuduki N., Narita R., Shigemoto T., Hirai R., Yoneyama M., Horiuchi M., Ogura K., Fujita T., Inagaki F. J. Biol. Chem. 284:17465-17474(2009) [PubMed: 19380577] [Abstract] Cited for: STRUCTURE BY NMR OF 896-1025 IN COMPLEX WITH ZINC IONS.
[18]	"Human dech-box RNA helicase mda5 (melanoma differentiation-associated protein 5), dech-domain." Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bank Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 277-490.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF095844 mRNA. Translation: AAG34368.1.
AY017378 mRNA. Translation: AAG54076.1.
BC046208 mRNA. Translation: AAH46208.1.
BC078180 mRNA. Translation: AAH78180.1. Sequence problems.
BC111750 mRNA. Translation: AAI11751.1.
AK056293 mRNA. Translation: BAB71141.1. Different initiation.

IPI

IPI00005577.
IPI00556546.

RefSeq

NP_071451.2. NM_022168.2.

UniGene

Hs.163173.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2RQB	NMR	-	A	896-1025	[»]
3B6E	X-ray	1.60	A	277-490	[»]
3GA3	X-ray	1.45	A	893-1017	[»]

ProteinModelPortal

Q9BYX4.

SMR

Q9BYX4. Positions 112-200, 292-1025.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42607N.

MINT

MINT-3381993.

STRING

Q9BYX4.

PTM databases

PhosphoSite

Q9BYX4.

Polymorphism databases

DMDM

134047802.

Proteomic databases

PRIDE

Q9BYX4.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000263642; ENSP00000263642; ENSG00000115267.

GeneID

64135.

KEGG

hsa:64135.

UCSC

uc002uce.1. human.
uc002ucf.2. human.

Organism-specific databases

CTD

64135.

GeneCards

GC02M163123.

H-InvDB

HIX0200280.

HGNC

HGNC:18873. IFIH1.

HPA

HPA002656.

MIM

606951. gene.
610155. phenotype.

neXtProt

NX_Q9BYX4.

PharmGKB

PA134889215.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG07506.

GeneTree

ENSGT00510000046789.

HOGENOM

HBG715302.

HOVERGEN

HBG106019.

InParanoid

Q9BYX4.

OMA

EKFAEVG.

OrthoDB

EOG48KR9P.

PhylomeDB

Q9BYX4.

Enzyme and pathway databases

Reactome

REACT_25177. RNF125 mediated ubiquitination of RIG-I, MDA5 and IPS-1.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

Q9BYX4.

Bgee

Q9BYX4.

CleanEx

HS_IFIH1.

Genevestigator

Q9BYX4.

GermOnline

ENSG00000115267. Homo sapiens.

Family and domain databases

InterPro

IPR001315. CARD.
IPR014001. DEAD-like_helicase.
IPR011029. DEATH-like.
IPR006935. Helicase/UvrB_dom.
IPR001650. Helicase_C.
IPR021673. RIG-I_C-RD.
[Graphical view]

Gene3D

G3DSA:1.10.533.10. DEATH_like. 1 hit.

KO

K12647.

Pfam

PF00619. CARD. 1 hit.
PF00271. Helicase_C. 1 hit.
PF04851. ResIII. 1 hit.
PF11648. RIG-I_C-RD. 1 hit.
[Graphical view]

SMART

SM00487. DEXDc. 1 hit.
SM00490. HELICc. 1 hit.
[Graphical view]

SUPFAM

SSF47986. DEATH_like. 1 hit.

PROSITE

PS50209. CARD. False negative.
PS51192. HELICASE_ATP_BIND_1. 1 hit.
PS51194. HELICASE_CTER. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

NextBio

66034.

SOURCE

Search...

Entry information

Entry name

IFIH1_HUMAN

Accession

Primary (citable) accession number: Q9BYX4
Secondary accession number(s): Q2NKL6 , Q6DC96, Q86X56, Q96MX8, Q9H3G6

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 12, 2005
Last sequence update:	March 20, 2007
Last modified:	January 25, 2012
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

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