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P55789

- ALR_HUMAN

UniProt

P55789 - ALR_HUMAN

Protein

FAD-linked sulfhydryl oxidase ALR

Gene

GFER

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 2 (16 Dec 2008)
      Previous versions | rss
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    Functioni

    Isoform 1: FAD-dependent sulfhydryl oxidase that regenerates the redox-active disulfide bonds in CHCHD4/MIA40, a chaperone essential for disulfide bond formation and protein folding in the mitochondrial intermembrane space. The reduced form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with GFER/ERV1, resulting in regeneration of the essential disulfide bonds in CHCHD4/MIA40, while GFER/ERV1 becomes re-oxidized by donating electrons to cytochrome c or molecular oxygen.
    Isoform 2: May act as an autocrine hepatotrophic growth factor promoting liver regeneration.

    Catalytic activityi

    2 R'C(R)SH + O2 = R'C(R)S-S(R)CR' + H2O2.2 Publications

    Cofactori

    FAD.2 PublicationsPROSITE-ProRule annotation

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei111 – 1111FAD1 Publication
    Binding sitei140 – 1401FAD1 Publication

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi99 – 1079FAD1 Publication
    Nucleotide bindingi171 – 18313FAD1 PublicationAdd
    BLAST
    Nucleotide bindingi194 – 1952FAD1 Publication

    GO - Molecular functioni

    1. flavin adenine dinucleotide binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein disulfide oxidoreductase activity Source: UniProtKB
    4. thiol oxidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. cellular protein metabolic process Source: Reactome
    2. protein targeting to mitochondrion Source: Reactome

    Keywords - Molecular functioni

    Growth factor, Oxidoreductase

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_118595. Mitochondrial protein import.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FAD-linked sulfhydryl oxidase ALR (EC:1.8.3.2)
    Alternative name(s):
    Augmenter of liver regeneration
    Short name:
    hERV1
    Hepatopoietin
    Gene namesi
    Name:GFER
    Synonyms:ALR, HERV1, HPO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:4236. GFER.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. extracellular region Source: UniProtKB-SubCell
    3. mitochondrial intermembrane space Source: UniProtKB-SubCell
    4. mitochondrion Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Myopathy, mitochondrial progressive, with congenital cataract, hearing loss and developmental delay (MPMCHD) [MIM:613076]: A disease characterized by progressive myopathy and partial combined respiratory-chain deficiency, congenital cataract, sensorineural hearing loss, and developmental delay.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti194 – 1941R → H in MPMCHD; less stable than the wild-type protein within the mitochondria, increased rate of dissociation of FAD by about 45-fold. 1 Publication
    Corresponds to variant rs121908192 [ dbSNP | Ensembl ].
    VAR_063435

    Keywords - Diseasei

    Cataract, Disease mutation

    Organism-specific databases

    MIMi613076. phenotype.
    Orphaneti330054. Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay.
    PharmGKBiPA28648.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 205205FAD-linked sulfhydryl oxidase ALRPRO_0000208548Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591Phosphoserine1 Publication
    Disulfide bondi95 – 95Interchain (with C-204)
    Disulfide bondi142 ↔ 145Redox-active
    Disulfide bondi171 ↔ 188
    Disulfide bondi204 – 204Interchain (with C-95)

    Keywords - PTMi

    Disulfide bond, Phosphoprotein

    Proteomic databases

    MaxQBiP55789.
    PaxDbiP55789.
    PRIDEiP55789.

    PTM databases

    PhosphoSiteiP55789.

    Expressioni

    Tissue specificityi

    Ubiquitously expressed. Highest expression in the testis and liver and low expression in the muscle.1 Publication

    Gene expression databases

    ArrayExpressiP55789.
    BgeeiP55789.
    CleanExiHS_GFER.
    GenevestigatoriP55789.

    Organism-specific databases

    HPAiHPA041227.

    Interactioni

    Subunit structurei

    Homodimer; disulfide-linked. May form heterodimers of isoform 1 and isoform 2.4 Publications

    Protein-protein interaction databases

    BioGridi108939. 9 interactions.
    IntActiP55789. 3 interactions.
    MINTiMINT-263560.
    STRINGi9606.ENSP00000248114.

    Structurei

    Secondary structure

    1
    205
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi86 – 883
    Beta strandi93 – 953
    Helixi99 – 11517
    Helixi123 – 13917
    Helixi143 – 15513
    Helixi163 – 18018
    Helixi188 – 1903
    Helixi191 – 1955

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3MBGX-ray1.85A/B/C81-205[»]
    3O55X-ray1.90A81-205[»]
    3TK0X-ray1.61A81-205[»]
    3U2LX-ray1.95A91-205[»]
    3U2MX-ray2.00A91-205[»]
    3U5SX-ray1.50A82-203[»]
    ProteinModelPortaliP55789.
    SMRiP55789. Positions 63-205.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP55789.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini95 – 195101ERV/ALR sulfhydryl oxidasePROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 ERV/ALR sulfhydryl oxidase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG5054.
    HOGENOMiHOG000195924.
    HOVERGENiHBG000235.
    InParanoidiP55789.
    KOiK17783.
    OMAiQKRDSKF.
    PhylomeDBiP55789.
    TreeFamiTF105271.

    Family and domain databases

    Gene3Di1.20.120.310. 1 hit.
    InterProiIPR017905. ERV/ALR_sulphydryl_oxidase.
    [Graphical view]
    PfamiPF04777. Evr1_Alr. 1 hit.
    [Graphical view]
    SUPFAMiSSF69000. SSF69000. 1 hit.
    PROSITEiPS51324. ERV_ALR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P55789-1) [UniParc]FASTAAdd to Basket

    Also known as: HPO-205, lfALR

    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

    MAAPGERGRF HGGNLFFLPG GARSEMMDDL ATDARGRGAG RRDAAASAST    50
    PAQAPTSDSP VAEDASRRRP CRACVDFKTW MRTQQKRDTK FREDCPPDRE 100
    ELGRHSWAVL HTLAAYYPDL PTPEQQQDMA QFIHLFSKFY PCEECAEDLR 150
    KRLCRNHPDT RTRACFTQWL CHLHNEVNRK LGKPDFDCSK VDERWRDGWK 200
    DGSCD 205
    Length:205
    Mass (Da):23,449
    Last modified:December 16, 2008 - v2
    Checksum:i43CBF8CCB5BA91C8
    GO
    Isoform 2 (identifier: P55789-2) [UniParc]FASTAAdd to Basket

    Also known as: HPO-125, sfALR

    The sequence of this isoform differs from the canonical sequence as follows:
         1-80: Missing.

    Show »
    Length:125
    Mass (Da):15,029
    Checksum:i3F0B927DC64EF606
    GO

    Sequence cautioni

    The sequence AAA96390.2 differs from that shown. Reason: Frameshift at position 70.
    The sequence AAD36986.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAD56538.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH02429.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAH28348.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti30 – 301L → S in AAA96390. (PubMed:10712775)Curated
    Sequence conflicti127 – 1271Q → R in AAG38105. 1 PublicationCurated
    Sequence conflicti180 – 1801K → E in AAG38105. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti166 – 1661F → L.
    Corresponds to variant rs36041021 [ dbSNP | Ensembl ].
    VAR_061994
    Natural varianti194 – 1941R → H in MPMCHD; less stable than the wild-type protein within the mitochondria, increased rate of dissociation of FAD by about 45-fold. 1 Publication
    Corresponds to variant rs121908192 [ dbSNP | Ensembl ].
    VAR_063435

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8080Missing in isoform 2. 2 PublicationsVSP_040393Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF183892 Genomic DNA. Translation: AAD56538.1. Different initiation.
    AF124604 mRNA. Translation: AAD17328.1.
    AF306863 mRNA. Translation: AAG38105.1.
    AY550027 mRNA. Translation: AAS55642.1.
    AC005606 Genomic DNA. No translation available.
    BC002429 mRNA. Translation: AAH02429.1. Different initiation.
    BC028348 mRNA. Translation: AAH28348.2. Different initiation.
    AF146394 Genomic DNA. Translation: AAD36986.1. Different initiation.
    U31176 mRNA. Translation: AAA96390.2. Frameshift.
    CCDSiCCDS32368.1. [P55789-1]
    RefSeqiNP_005253.3. NM_005262.2. [P55789-1]
    UniGeneiHs.27184.

    Genome annotation databases

    EnsembliENST00000248114; ENSP00000248114; ENSG00000127554. [P55789-1]
    GeneIDi2671.
    KEGGihsa:2671.
    UCSCiuc002cob.3. human. [P55789-1]

    Polymorphism databases

    DMDMi218511915.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF183892 Genomic DNA. Translation: AAD56538.1 . Different initiation.
    AF124604 mRNA. Translation: AAD17328.1 .
    AF306863 mRNA. Translation: AAG38105.1 .
    AY550027 mRNA. Translation: AAS55642.1 .
    AC005606 Genomic DNA. No translation available.
    BC002429 mRNA. Translation: AAH02429.1 . Different initiation.
    BC028348 mRNA. Translation: AAH28348.2 . Different initiation.
    AF146394 Genomic DNA. Translation: AAD36986.1 . Different initiation.
    U31176 mRNA. Translation: AAA96390.2 . Frameshift.
    CCDSi CCDS32368.1. [P55789-1 ]
    RefSeqi NP_005253.3. NM_005262.2. [P55789-1 ]
    UniGenei Hs.27184.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3MBG X-ray 1.85 A/B/C 81-205 [» ]
    3O55 X-ray 1.90 A 81-205 [» ]
    3TK0 X-ray 1.61 A 81-205 [» ]
    3U2L X-ray 1.95 A 91-205 [» ]
    3U2M X-ray 2.00 A 91-205 [» ]
    3U5S X-ray 1.50 A 82-203 [» ]
    ProteinModelPortali P55789.
    SMRi P55789. Positions 63-205.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108939. 9 interactions.
    IntActi P55789. 3 interactions.
    MINTi MINT-263560.
    STRINGi 9606.ENSP00000248114.

    Chemistry

    ChEMBLi CHEMBL1741189.
    DrugBanki DB03147. Flavin adenine dinucleotide.

    PTM databases

    PhosphoSitei P55789.

    Polymorphism databases

    DMDMi 218511915.

    Proteomic databases

    MaxQBi P55789.
    PaxDbi P55789.
    PRIDEi P55789.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000248114 ; ENSP00000248114 ; ENSG00000127554 . [P55789-1 ]
    GeneIDi 2671.
    KEGGi hsa:2671.
    UCSCi uc002cob.3. human. [P55789-1 ]

    Organism-specific databases

    CTDi 2671.
    GeneCardsi GC16P002095.
    H-InvDB HIX0012707.
    HGNCi HGNC:4236. GFER.
    HPAi HPA041227.
    MIMi 600924. gene.
    613076. phenotype.
    neXtProti NX_P55789.
    Orphaneti 330054. Congenital cataract - progressive muscular hypotonia - hearing loss - developmental delay.
    PharmGKBi PA28648.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5054.
    HOGENOMi HOG000195924.
    HOVERGENi HBG000235.
    InParanoidi P55789.
    KOi K17783.
    OMAi QKRDSKF.
    PhylomeDBi P55789.
    TreeFami TF105271.

    Enzyme and pathway databases

    Reactomei REACT_118595. Mitochondrial protein import.

    Miscellaneous databases

    EvolutionaryTracei P55789.
    GeneWikii GFER.
    GenomeRNAii 2671.
    NextBioi 10542.
    PROi P55789.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P55789.
    Bgeei P55789.
    CleanExi HS_GFER.
    Genevestigatori P55789.

    Family and domain databases

    Gene3Di 1.20.120.310. 1 hit.
    InterProi IPR017905. ERV/ALR_sulphydryl_oxidase.
    [Graphical view ]
    Pfami PF04777. Evr1_Alr. 1 hit.
    [Graphical view ]
    SUPFAMi SSF69000. SSF69000. 1 hit.
    PROSITEi PS51324. ERV_ALR. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Genomic structure, chromosomal localization, and characterization of a functional promoter for human hepatopoietin (HPO) gene."
      Liu M.-M., He F.-C., Wei H.-D., Zhou W.-Q.
      Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "HERV different transcription sequence."
      Li Y., Xing G.-C., He F.-C., Wei H.-D., Zhang C.-G., Zhu L., Yu Y.-T.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
      Tissue: Liver.
    3. "Isolation of human HPO cDNA from human liver tissue."
      Jun L., Wangxiang X., Xiaoming Y.
      Submitted (SEP-2000) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal liver.
    4. "Human augmenter of liver regeneration/hepatopoietin gene open reading frame sequence."
      Dai W.-J., Jiang H.-C.
      Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    5. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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] OF 2-205.
      Tissue: Placenta and Skin.
    7. "Cloning and sequence analysis of human genomic DNA of augmenter of liver regeneration hepatitis."
      Cheng J., Zhong Y.
      Zhonghua Gan Zang Bing Za Zhi 8:12-14(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 29-205.
    8. "A new human gene located in the PKD1 region of chromosome 16 is a functional homologue to ERV1 of yeast."
      Lisowsky T., Weinstat-Saslow D.L., Barton N., Reeders S.T., Schneider M.C.
      Genomics 29:690-697(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 30-205.
      Tissue: Renal cyst lining cell.
    9. "Identification of hepatopoietin dimerization, its interacting regions and alternative splicing of its transcription."
      Li Y., Wei K., Lu C., Li Y., Li M., Xing G., Wei H., Wang Q., Chen J., Wu C., Chen H., Yang S., He F.
      Eur. J. Biochem. 269:3888-3893(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING, SUBUNIT.
    10. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-59, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "Augmenter of liver regeneration: substrate specificity of a flavin-dependent oxidoreductase from the mitochondrial intermembrane space."
      Daithankar V.N., Farrell S.R., Thorpe C.
      Biochemistry 48:4828-4837(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    14. "Disulfide bond formation: sulfhydryl oxidase ALR controls mitochondrial biogenesis of human MIA40."
      Sztolsztener M.E., Brewinska A., Guiard B., Chacinska A.
      Traffic 14:309-320(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    15. "Structure of the human sulfhydryl oxidase augmenter of liver regeneration and characterization of a human mutation causing an autosomal recessive myopathy."
      Daithankar V.N., Schaefer S.A., Dong M., Bahnson B.J., Thorpe C.
      Biochemistry 49:6737-6745(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 81-205, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, DISULFIDE BONDS, FAD-BINDING SITES, CHARACTERIZATION OF VARIANT MPMCHD HIS-194.
    16. "Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR."
      Banci L., Bertini I., Calderone V., Cefaro C., Ciofi-Baffoni S., Gallo A., Kallergi E., Lionaki E., Pozidis C., Tokatlidis K.
      Proc. Natl. Acad. Sci. U.S.A. 108:4811-4816(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 81-205 IN COMPLEX WITH FAD, FUNCTION, COFACTOR, SUBUNIT, DISULFIDE BONDS, INTERACTION WITH CHCHD4.
    17. "An electron-transfer path through an extended disulfide relay system: the case of the redox protein ALR."
      Banci L., Bertini I., Calderone V., Cefaro C., Ciofi-Baffoni S., Gallo A., Tokatlidis K.
      J. Am. Chem. Soc. 134:1442-1445(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 91-205, FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BONDS, SUBUNIT.
    18. "The mitochondrial disulfide relay system protein GFER is mutated in autosomal-recessive myopathy with cataract and combined respiratory-chain deficiency."
      Di Fonzo A., Ronchi D., Lodi T., Fassone E., Tigano M., Lamperti C., Corti S., Bordoni A., Fortunato F., Nizzardo M., Napoli L., Donadoni C., Salani S., Saladino F., Moggio M., Bresolin N., Ferrero I., Comi G.P.
      Am. J. Hum. Genet. 84:594-604(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT MPMCHD HIS-194, CHARACTERIZATION OF VARIANT MPMCHD HIS-194, TISSUE SPECIFICITY.

    Entry informationi

    Entry nameiALR_HUMAN
    AccessioniPrimary (citable) accession number: P55789
    Secondary accession number(s): Q53YM6
    , Q8TAH6, Q9H290, Q9UK40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: December 16, 2008
    Last modified: October 1, 2014
    This is version 126 of the entry and version 2 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3