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P55789

- ALR_HUMAN

UniProt

P55789 - ALR_HUMAN

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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

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 disulfide oxidoreductase activity Source: UniProtKB
  3. thiol oxidase activity Source: UniProtKB-EC

GO - Biological processi

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

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-KW
  3. mitochondrion Source: HPA
Complete GO annotation...

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

BgeeiP55789.
CleanExiHS_GFER.
ExpressionAtlasiP55789. baseline.
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. 16 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 – 883Combined sources
Beta strandi93 – 953Combined sources
Helixi99 – 11517Combined sources
Helixi123 – 13917Combined sources
Helixi143 – 15513Combined sources
Helixi163 – 18018Combined sources
Helixi188 – 1903Combined sources
Helixi191 – 1955Combined sources

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[»]
4LDKX-ray2.04A81-205[»]
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.
GeneTreeiENSGT00390000001979.
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

        10         20         30         40         50
MAAPGERGRF HGGNLFFLPG GARSEMMDDL ATDARGRGAG RRDAAASAST
60 70 80 90 100
PAQAPTSDSP VAEDASRRRP CRACVDFKTW MRTQQKRDTK FREDCPPDRE
110 120 130 140 150
ELGRHSWAVL HTLAAYYPDL PTPEQQQDMA QFIHLFSKFY PCEECAEDLR
160 170 180 190 200
KRLCRNHPDT RTRACFTQWL CHLHNEVNRK LGKPDFDCSK VDERWRDGWK

DGSCD
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 [» ]
4LDK X-ray 2.04 A 81-205 [» ]
ProteinModelPortali P55789.
SMRi P55789. Positions 63-205.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108939. 16 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 GC16P002116.
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.
GeneTreei ENSGT00390000001979.
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

Bgeei P55789.
CleanExi HS_GFER.
ExpressionAtlasi P55789. baseline.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 127 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