SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O75306

- NDUS2_HUMAN

UniProt

O75306 - NDUS2_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial

Gene
NDUFS2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone By similarity.UniRule annotation

Catalytic activityi

NADH + ubiquinone + 5 H+(In) = NAD+ + ubiquinol + 4 H+(Out).UniRule annotation
NADH + acceptor = NAD+ + reduced acceptor.UniRule annotation

Cofactori

Binds 1 4Fe-4S cluster.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi326 – 3261Iron-sulfur (4Fe-4S) Reviewed prediction
Metal bindingi332 – 3321Iron-sulfur (4Fe-4S) Reviewed prediction
Metal bindingi347 – 3471Iron-sulfur (4Fe-4S) Reviewed prediction

GO - Molecular functioni

  1. 4 iron, 4 sulfur cluster binding Source: UniProtKB-KW
  2. electron carrier activity Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. NAD binding Source: InterPro
  5. NADH dehydrogenase (ubiquinone) activity Source: UniProtKB
  6. protein binding Source: UniProtKB
  7. quinone binding Source: InterPro

GO - Biological processi

  1. cellular metabolic process Source: Reactome
  2. mitochondrial electron transport, NADH to ubiquinone Source: UniProtKB
  3. respiratory electron transport chain Source: Reactome
  4. response to oxidative stress Source: UniProtKB
  5. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

4Fe-4S, Iron, Iron-sulfur, Metal-binding, NAD, Ubiquinone

Enzyme and pathway databases

ReactomeiREACT_22393. Respiratory electron transport.

Names & Taxonomyi

Protein namesi
Recommended name:
NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Alternative name(s):
Complex I-49kD
Short name:
CI-49kD
NADH-ubiquinone oxidoreductase 49 kDa subunit
Gene namesi
Name:NDUFS2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:7708. NDUFS2.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. mitochondrial respiratory chain complex I Source: UniProtKB
  3. mitochondrion Source: UniProtKB
  4. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Membrane, Mitochondrion, Mitochondrion inner membrane

Pathology & Biotechi

Involvement in diseasei

Mitochondrial complex I deficiency (MT-C1D) [MIM:252010]: A disorder of the mitochondrial respiratory chain that causes a wide range of clinical manifestations from lethal neonatal disease to adult-onset neurodegenerative disorders. Phenotypes include macrocephaly with progressive leukodystrophy, non-specific encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh syndrome, Leber hereditary optic neuropathy, and some forms of Parkinson disease.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti228 – 2281R → Q in MT-C1D. 1 Publication
VAR_019535
Natural varianti229 – 2291P → Q in MT-C1D. 1 Publication
VAR_019536
Natural varianti413 – 4131S → P in MT-C1D. 1 Publication
VAR_019537

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi252010. phenotype.
Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBiPA31519.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3333Mitochondrion By similarityAdd
BLAST
Chaini34 – 463430NADH dehydrogenase [ubiquinone] iron-sulfur protein 2, mitochondrialUniRule annotationPRO_0000019981Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei62 – 621N6-acetyllysine By similarity
Modified residuei118 – 1181Symmetric dimethylarginine By similarity

Keywords - PTMi

Acetylation, Methylation

Proteomic databases

MaxQBiO75306.
PaxDbiO75306.
PeptideAtlasiO75306.
PRIDEiO75306.

PTM databases

PhosphoSiteiO75306.

Expressioni

Gene expression databases

ArrayExpressiO75306.
BgeeiO75306.
CleanExiHS_NDUFS2.
GenevestigatoriO75306.

Organism-specific databases

HPAiHPA055140.

Interactioni

Subunit structurei

Complex I is composed of 45 different subunits. Component of the iron-sulfur (IP) fragment of the enzyme. Interacts with NDUFAF3 and NDUFAF7.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NDUFS3O754895EBI-1224806,EBI-1224896

Protein-protein interaction databases

BioGridi110800. 27 interactions.
IntActiO75306. 16 interactions.
STRINGi9606.ENSP00000356972.

Structurei

3D structure databases

ProteinModelPortaliO75306.
SMRiO75306. Positions 80-463.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0649.
HOGENOMiHOG000228264.
HOVERGENiHBG000760.
InParanoidiO75306.
KOiK03935.
OMAiQCFALAV.
OrthoDBiEOG7WT411.
PhylomeDBiO75306.
TreeFamiTF300370.

Family and domain databases

Gene3Di1.10.645.10. 1 hit.
HAMAPiMF_01358. NDH1_NuoD.
InterProiIPR001135. NADH_Q_OxRdtase_suD.
IPR014029. NADH_UbQ_OxRdtase_49kDa_CS.
IPR022885. NDH1_su_D/H.
IPR029014. NiFe_Hase-like.
[Graphical view]
PfamiPF00346. Complex1_49kDa. 1 hit.
[Graphical view]
SUPFAMiSSF56762. SSF56762. 1 hit.
TIGRFAMsiTIGR01962. NuoD. 1 hit.
PROSITEiPS00535. COMPLEX1_49K. 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. Align

Isoform 1 (identifier: O75306-1) [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

MAALRALCGF RGVAAQVLRP GAGVRLPIQP SRGVRQWQPD VEWAQQFGGA    50
VMYPSKETAH WKPPPWNDVD PPKDTIVKNI TLNFGPQHPA AHGVLRLVME 100
LSGEMVRKCD PHIGLLHRGT EKLIEYKTYL QALPYFDRLD YVSMMCNEQA 150
YSLAVEKLLN IRPPPRAQWI RVLFGEITRL LNHIMAVTTH ALDLGAMTPF 200
FWLFEEREKM FEFYERVSGA RMHAAYIRPG GVHQDLPLGL MDDIYQFSKN 250
FSLRLDELEE LLTNNRIWRN RTIDIGVVTA EEALNYGFSG VMLRGSGIQW 300
DLRKTQPYDV YDQVEFDVPV GSRGDCYDRY LCRVEEMRQS LRIIAQCLNK 350
MPPGEIKVDD AKVSPPKRAE MKTSMESLIH HFKLYTEGYQ VPPGATYTAI 400
EAPKGEFGVY LVSDGSSRPY RCKIKAPGFA HLAGLDKMSK GHMLADVVAI 450
IGTQDIVFGE VDR 463
Length:463
Mass (Da):52,546
Last modified:April 16, 2002 - v2
Checksum:iA2BF56F008B6312C
GO
Isoform 2 (identifier: O75306-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     454-463: QDIVFGEVDR → RPIV

Note: No experimental confirmation available.

Show »
Length:457
Mass (Da):51,852
Checksum:i312C97A91028FF66
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti20 – 201P → T.
Corresponds to variant rs11538340 [ dbSNP | Ensembl ].
VAR_034150
Natural varianti228 – 2281R → Q in MT-C1D. 1 Publication
VAR_019535
Natural varianti229 – 2291P → A.
Corresponds to variant rs16827493 [ dbSNP | Ensembl ].
VAR_034151
Natural varianti229 – 2291P → Q in MT-C1D. 1 Publication
VAR_019536
Natural varianti352 – 3521P → A.
Corresponds to variant rs11576415 [ dbSNP | Ensembl ].
VAR_034152
Natural varianti413 – 4131S → P in MT-C1D. 1 Publication
VAR_019537

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei454 – 46310QDIVFGEVDR → RPIV in isoform 2. VSP_046466

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241V → G in AAC34362. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF050640 mRNA. Translation: AAC27453.1.
AF013160 mRNA. Translation: AAC34362.1.
AK314807 mRNA. No translation available.
AL590714 Genomic DNA. Translation: CAH72148.1.
CH471121 Genomic DNA. Translation: EAW52625.1.
CH471121 Genomic DNA. Translation: EAW52626.1.
BC000170 mRNA. Translation: AAH00170.1.
BC001456 mRNA. Translation: AAH01456.1.
BC008868 mRNA. Translation: AAH08868.1.
CCDSiCCDS1224.1. [O75306-1]
CCDS53404.1. [O75306-2]
PIRiJE0193.
RefSeqiNP_001159631.1. NM_001166159.1. [O75306-2]
NP_004541.1. NM_004550.4. [O75306-1]
XP_005245265.1. XM_005245208.1. [O75306-1]
UniGeneiHs.173611.

Genome annotation databases

EnsembliENST00000367993; ENSP00000356972; ENSG00000158864. [O75306-1]
ENST00000392179; ENSP00000376018; ENSG00000158864. [O75306-2]
GeneIDi4720.
KEGGihsa:4720.
UCSCiuc001fyv.3. human. [O75306-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF050640 mRNA. Translation: AAC27453.1 .
AF013160 mRNA. Translation: AAC34362.1 .
AK314807 mRNA. No translation available.
AL590714 Genomic DNA. Translation: CAH72148.1 .
CH471121 Genomic DNA. Translation: EAW52625.1 .
CH471121 Genomic DNA. Translation: EAW52626.1 .
BC000170 mRNA. Translation: AAH00170.1 .
BC001456 mRNA. Translation: AAH01456.1 .
BC008868 mRNA. Translation: AAH08868.1 .
CCDSi CCDS1224.1. [O75306-1 ]
CCDS53404.1. [O75306-2 ]
PIRi JE0193.
RefSeqi NP_001159631.1. NM_001166159.1. [O75306-2 ]
NP_004541.1. NM_004550.4. [O75306-1 ]
XP_005245265.1. XM_005245208.1. [O75306-1 ]
UniGenei Hs.173611.

3D structure databases

ProteinModelPortali O75306.
SMRi O75306. Positions 80-463.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110800. 27 interactions.
IntActi O75306. 16 interactions.
STRINGi 9606.ENSP00000356972.

Chemistry

BindingDBi O75306.
ChEMBLi CHEMBL2363065.
DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei O75306.

Proteomic databases

MaxQBi O75306.
PaxDbi O75306.
PeptideAtlasi O75306.
PRIDEi O75306.

Protocols and materials databases

DNASUi 4720.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000367993 ; ENSP00000356972 ; ENSG00000158864 . [O75306-1 ]
ENST00000392179 ; ENSP00000376018 ; ENSG00000158864 . [O75306-2 ]
GeneIDi 4720.
KEGGi hsa:4720.
UCSCi uc001fyv.3. human. [O75306-1 ]

Organism-specific databases

CTDi 4720.
GeneCardsi GC01P161166.
HGNCi HGNC:7708. NDUFS2.
HPAi HPA055140.
MIMi 252010. phenotype.
602985. gene.
neXtProti NX_O75306.
Orphaneti 2609. Isolated NADH-CoQ reductase deficiency.
PharmGKBi PA31519.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0649.
HOGENOMi HOG000228264.
HOVERGENi HBG000760.
InParanoidi O75306.
KOi K03935.
OMAi QCFALAV.
OrthoDBi EOG7WT411.
PhylomeDBi O75306.
TreeFami TF300370.

Enzyme and pathway databases

Reactomei REACT_22393. Respiratory electron transport.

Miscellaneous databases

ChiTaRSi NDUFS2. human.
GeneWikii NDUFS2.
GenomeRNAii 4720.
NextBioi 18206.
PROi O75306.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75306.
Bgeei O75306.
CleanExi HS_NDUFS2.
Genevestigatori O75306.

Family and domain databases

Gene3Di 1.10.645.10. 1 hit.
HAMAPi MF_01358. NDH1_NuoD.
InterProi IPR001135. NADH_Q_OxRdtase_suD.
IPR014029. NADH_UbQ_OxRdtase_49kDa_CS.
IPR022885. NDH1_su_D/H.
IPR029014. NiFe_Hase-like.
[Graphical view ]
Pfami PF00346. Complex1_49kDa. 1 hit.
[Graphical view ]
SUPFAMi SSF56762. SSF56762. 1 hit.
TIGRFAMsi TIGR01962. NuoD. 1 hit.
PROSITEi PS00535. COMPLEX1_49K. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA sequence and chromosomal localization of the remaining three human nuclear encoded iron sulphur protein (IP) subunits of complex I: the human IP fraction is completed."
    Loeffen J., van den Heuvel L., Smeets R., Triepels R., Sengers R., Trijbels F., Smeitink J.
    Biochem. Biophys. Res. Commun. 247:751-758(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Mapping to 1q23 of the human gene (NDUFS2) encoding the 49-kDa subunit of the mitochondrial respiratory complex I and immunodetection of the mature protein in mitochondria."
    Procaccio V., de Sury R., Martinez P., Depetris D., Rabilloud T., Soularue P., Lunardi J., Issartel J.-P.
    Mamm. Genome 9:482-484(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. 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].
    Tissue: Muscle and Placenta.
  7. "The subunit composition of the human NADH dehydrogenase obtained by rapid one-step immunopurification."
    Murray J., Zhang B., Taylor S.W., Oglesbee D., Fahy E., Marusich M.F., Ghosh S.S., Capaldi R.A.
    J. Biol. Chem. 278:13619-13622(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Mutations in NDUFAF3 (C3ORF60), encoding an NDUFAF4 (C6ORF66)-interacting complex I assembly protein, cause fatal neonatal mitochondrial disease."
    Saada A., Vogel R.O., Hoefs S.J., van den Brand M.A., Wessels H.J., Willems P.H., Venselaar H., Shaag A., Barghuti F., Reish O., Shohat M., Huynen M.A., Smeitink J.A.M., van den Heuvel L.P., Nijtmans L.G.
    Am. J. Hum. Genet. 84:718-727(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NDUFAF3.
  9. Cited for: INTERACTION WITH NDUFAF7.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Mutations in the complex I NDUFS2 gene of patients with cardiomyopathy and encephalomyopathy."
    Loeffen J., Elpeleg O., Smeitink J., Smeets R., Stoeckler-Ipsiroglu S., Mandel H., Sengers R., Trijbels F., van den Heuvel L.
    Ann. Neurol. 49:195-201(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MT-C1D GLN-228; GLN-229 AND PRO-413.

Entry informationi

Entry nameiNDUS2_HUMAN
AccessioniPrimary (citable) accession number: O75306
Secondary accession number(s): D3DVG7
, J3KPM7, Q5VTW0, Q969P3, Q9UEV3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: April 16, 2002
Last modified: September 3, 2014
This is version 149 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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