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Protein

FAD-dependent oxidoreductase domain-containing protein 2

Gene

FOXRED2

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

Functioni

Probable flavoprotein which may function in endoplasmic reticulum associated degradation (ERAD). May bind non-native proteins in the endoplasmic reticulum and target them to the ubiquitination machinery for subsequent degradation.1 Publication

Cofactori

FAD1 Publication

GO - Molecular functioni

  1. flavin adenine dinucleotide binding Source: UniProtKB
  2. glycoprotein binding Source: UniProtKB
  3. oxidoreductase activity Source: UniProtKB-KW

GO - Biological processi

  1. ER-associated ubiquitin-dependent protein catabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

FAD, Flavoprotein

Names & Taxonomyi

Protein namesi
Recommended name:
FAD-dependent oxidoreductase domain-containing protein 2
Alternative name(s):
Endoplasmic reticulum flavoprotein associated with degradation
Gene namesi
Name:FOXRED2
Synonyms:ERFAD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:26264. FOXRED2.

Subcellular locationi

  1. Endoplasmic reticulum lumen PROSITE-ProRule annotation1 Publication

GO - Cellular componenti

  1. endoplasmic reticulum lumen Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA145148808.

Polymorphism and mutation databases

BioMutaiFOXRED2.
DMDMi74759632.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2626Sequence AnalysisAdd
BLAST
Chaini27 – 684658FAD-dependent oxidoreductase domain-containing protein 2PRO_0000337692Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi143 – 1431N-linked (GlcNAc...)1 Publication

Post-translational modificationi

N-glycosylated.2 Publications

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiQ8IWF2.
PaxDbiQ8IWF2.
PRIDEiQ8IWF2.

PTM databases

PhosphoSiteiQ8IWF2.

Expressioni

Gene expression databases

BgeeiQ8IWF2.
CleanExiHS_FOXRED2.
ExpressionAtlasiQ8IWF2. baseline and differential.
GenevestigatoriQ8IWF2.

Organism-specific databases

HPAiHPA031611.
HPA031612.

Interactioni

Subunit structurei

Interacts with SEL1L. May interact with OS9 and DNAJC10.1 Publication

Protein-protein interaction databases

BioGridi123074. 30 interactions.
DIPiDIP-48946N.
STRINGi9606.ENSP00000216187.

Structurei

3D structure databases

ProteinModelPortaliQ8IWF2.
SMRiQ8IWF2. Positions 28-232.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi681 – 6844Prevents secretion from ERPROSITE-ProRule annotation

Sequence similaritiesi

Belongs to the FOXRED2 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG303889.
GeneTreeiENSGT00640000091519.
HOGENOMiHOG000031485.
HOVERGENiHBG100868.
InParanoidiQ8IWF2.
OMAiQAWNGHY.
OrthoDBiEOG7M6D70.
PhylomeDBiQ8IWF2.
TreeFamiTF324712.

Family and domain databases

PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8IWF2-1) [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
MGLSAAAPLW GPPGLLLAIA LHPALSVPPR RDYCVLGAGP AGLQMAYFLQ
60 70 80 90 100
RAGRDYAVFE RAPRPGSFFT RYPRHRKLIS INKRYTGKAN AEFNLRHDWN
110 120 130 140 150
SLLSHDPRLL FRHYSRAYFP DARDMVRYLG DFADTLGLRV QYNTTIAHVT
160 170 180 190 200
LDKDRQAWNG HYFILTDQKG QVHQCSVLFV ATGLSVPNQV DFPGSEYAEG
210 220 230 240 250
YESVSVDPED FVGQNVLILG RGNSAFETAE NILGVTNFIH MLSRSRVRLS
260 270 280 290 300
WATHYVGDLR AINNGLLDTY QLKSLDGLLE SDLTDLAILK DSKGKFHVTP
310 320 330 340 350
KFFLEEANTN QSADSITLPQ DDNDNFAMRV PYDRVIRCLG WNFDFSIFNK
360 370 380 390 400
SLRLNSGNAF GKKYPLIRAS YESKGSRGLF ILGTASHSVD YRKSAGGFIH
410 420 430 440 450
GFRYTVRAVH RLLEHRHHSV TWPATELPIT QLTSSIVRRV NEASGLYQMF
460 470 480 490 500
GVLADVILLK ENSTAFEYLE EFPIQMLAQL ETLTGRKAKH GLFVINMEYG
510 520 530 540 550
RNFSGPDKDV FFDDRSVGHT EDAWQSNFLH PVIYYYRYLP TEQEVRFRPA
560 570 580 590 600
HWPLPRPTAI HHIVEDFLTD WTAPIGHILP LRRFLENCLD TDLRSFYAES
610 620 630 640 650
CFLFALTRQK LPPFCQQGYL RMQGLVSTES LWQHRVESRL LRDYAPTGRR
660 670 680
LEDSSQQLGD QEPLGSPLAP GPLAQSVDSN KEEL
Length:684
Mass (Da):77,791
Last modified:March 1, 2003 - v1
Checksum:i8209FFAF6289DDAF
GO
Isoform 2 (identifier: Q8IWF2-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-327: Missing.

Note: No experimental confirmation available.

Show »
Length:357
Mass (Da):41,157
Checksum:i14C82B1E14D54A0A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti345 – 3451F → S in BAB15610 (PubMed:14702039).Curated
Sequence conflicti607 – 6071T → A in BAB15227 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti71 – 711R → C.
Corresponds to variant rs56767103 [ dbSNP | Ensembl ].
VAR_062247
Natural varianti179 – 1791F → L.2 Publications
Corresponds to variant rs760718 [ dbSNP | Ensembl ].
VAR_043704
Natural varianti308 – 3081N → S.3 Publications
Corresponds to variant rs2277841 [ dbSNP | Ensembl ].
VAR_043705
Natural varianti374 – 3741K → R.
Corresponds to variant rs35813894 [ dbSNP | Ensembl ].
VAR_043706
Natural varianti637 – 6371E → D.
Corresponds to variant rs35748020 [ dbSNP | Ensembl ].
VAR_043707

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 327327Missing in isoform 2. 1 PublicationVSP_033997Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR456444 mRNA. Translation: CAG30330.1.
AK025714 mRNA. Translation: BAB15227.1.
AK026975 mRNA. Translation: BAB15610.1.
AK315555 mRNA. Translation: BAG37931.1.
AL022313 Genomic DNA. Translation: CAI19228.1.
CH471095 Genomic DNA. Translation: EAW60106.1.
BC015726 mRNA. Translation: AAH15726.1.
BC027716 mRNA. Translation: AAH27716.1.
BC040351 mRNA. Translation: AAH40351.1.
CCDSiCCDS13929.1. [Q8IWF2-1]
RefSeqiNP_001095841.1. NM_001102371.1. [Q8IWF2-1]
NP_079231.4. NM_024955.5. [Q8IWF2-1]
UniGeneiHs.387601.

Genome annotation databases

EnsembliENST00000216187; ENSP00000216187; ENSG00000100350. [Q8IWF2-1]
ENST00000397223; ENSP00000380400; ENSG00000100350. [Q8IWF2-1]
ENST00000397224; ENSP00000380401; ENSG00000100350. [Q8IWF2-1]
GeneIDi80020.
KEGGihsa:80020.
UCSCiuc003apn.4. human. [Q8IWF2-1]

Polymorphism and mutation databases

BioMutaiFOXRED2.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CR456444 mRNA. Translation: CAG30330.1.
AK025714 mRNA. Translation: BAB15227.1.
AK026975 mRNA. Translation: BAB15610.1.
AK315555 mRNA. Translation: BAG37931.1.
AL022313 Genomic DNA. Translation: CAI19228.1.
CH471095 Genomic DNA. Translation: EAW60106.1.
BC015726 mRNA. Translation: AAH15726.1.
BC027716 mRNA. Translation: AAH27716.1.
BC040351 mRNA. Translation: AAH40351.1.
CCDSiCCDS13929.1. [Q8IWF2-1]
RefSeqiNP_001095841.1. NM_001102371.1. [Q8IWF2-1]
NP_079231.4. NM_024955.5. [Q8IWF2-1]
UniGeneiHs.387601.

3D structure databases

ProteinModelPortaliQ8IWF2.
SMRiQ8IWF2. Positions 28-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi123074. 30 interactions.
DIPiDIP-48946N.
STRINGi9606.ENSP00000216187.

PTM databases

PhosphoSiteiQ8IWF2.

Polymorphism and mutation databases

BioMutaiFOXRED2.
DMDMi74759632.

Proteomic databases

MaxQBiQ8IWF2.
PaxDbiQ8IWF2.
PRIDEiQ8IWF2.

Protocols and materials databases

DNASUi80020.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216187; ENSP00000216187; ENSG00000100350. [Q8IWF2-1]
ENST00000397223; ENSP00000380400; ENSG00000100350. [Q8IWF2-1]
ENST00000397224; ENSP00000380401; ENSG00000100350. [Q8IWF2-1]
GeneIDi80020.
KEGGihsa:80020.
UCSCiuc003apn.4. human. [Q8IWF2-1]

Organism-specific databases

CTDi80020.
GeneCardsiGC22M036883.
H-InvDBHIX0203159.
HGNCiHGNC:26264. FOXRED2.
HPAiHPA031611.
HPA031612.
MIMi613777. gene.
neXtProtiNX_Q8IWF2.
PharmGKBiPA145148808.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG303889.
GeneTreeiENSGT00640000091519.
HOGENOMiHOG000031485.
HOVERGENiHBG100868.
InParanoidiQ8IWF2.
OMAiQAWNGHY.
OrthoDBiEOG7M6D70.
PhylomeDBiQ8IWF2.
TreeFamiTF324712.

Miscellaneous databases

ChiTaRSiFOXRED2. human.
GenomeRNAii80020.
NextBioi70142.
PROiQ8IWF2.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IWF2.
CleanExiHS_FOXRED2.
ExpressionAtlasiQ8IWF2. baseline and differential.
GenevestigatoriQ8IWF2.

Family and domain databases

PROSITEiPS00014. ER_TARGET. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS LEU-179 AND SER-308.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Placenta.
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT SER-308.
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANTS LEU-179 AND SER-308.
    Tissue: Brain, Colon and Eye.
  6. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-143.
    Tissue: Liver.
  7. Cited for: FUNCTION, FAD-BINDING, GLYCOSYLATION, SUBCELLULAR LOCATION, INTERACTION WITH DNAJC10; OS9 AND SEL1L.

Entry informationi

Entry nameiFXRD2_HUMAN
AccessioniPrimary (citable) accession number: Q8IWF2
Secondary accession number(s): B2RDI4
, Q8N378, Q96BD1, Q9H5L5, Q9H6M8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: March 1, 2003
Last modified: April 29, 2015
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

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