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P28331

- NDUS1_HUMAN

UniProt

P28331 - NDUS1_HUMAN

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Protein
NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
Gene
NDUFS1
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. This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.

Catalytic activityi

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

Cofactori

Binds 1 2Fe-2S cluster per subunit By similarity.
Binds 2 4Fe-4S clusters per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi64 – 641Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi75 – 751Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi78 – 781Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi92 – 921Iron-sulfur 1 (2Fe-2S) By similarity
Metal bindingi124 – 1241Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
Metal bindingi128 – 1281Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi131 – 1311Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi137 – 1371Iron-sulfur 2 (4Fe-4S) By similarity
Metal bindingi176 – 1761Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi179 – 1791Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi182 – 1821Iron-sulfur 3 (4Fe-4S) By similarity
Metal bindingi226 – 2261Iron-sulfur 3 (4Fe-4S) By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. ATP metabolic process Source: UniProtKB
  2. apoptotic mitochondrial changes Source: UniProtKB
  3. cellular metabolic process Source: Reactome
  4. cellular respiration Source: UniProtKB
  5. mitochondrial electron transport, NADH to ubiquinone Source: UniProtKB
  6. reactive oxygen species metabolic process Source: UniProtKB
  7. regulation of mitochondrial membrane potential Source: UniProtKB
  8. respiratory electron transport chain Source: Reactome
  9. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Respiratory chain, Transport

Keywords - Ligandi

2Fe-2S, 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-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial (EC:1.6.5.3, EC:1.6.99.3)
Alternative name(s):
Complex I-75kD
Short name:
CI-75kD
Gene namesi
Name:NDUFS1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:7707. NDUFS1.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. mitochondrial intermembrane space Source: UniProtKB
  3. mitochondrial respiratory chain complex I Source: UniProtKB
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 varianti241 – 2411R → W in MT-C1D. 1 Publication
VAR_019532
Natural varianti252 – 2521D → G in MT-C1D. 1 Publication
VAR_019533

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi252010. phenotype.
Orphaneti2609. Isolated NADH-CoQ reductase deficiency.
255241. Leigh syndrome with leukodystrophy.
PharmGKBiPA31518.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2323Mitochondrion By similarity
Add
BLAST
Chaini24 – 727704NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
PRO_0000019968Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei84 – 841N6-acetyllysine By similarity
Modified residuei467 – 4671N6-acetyllysine By similarity
Modified residuei499 – 4991N6-acetyllysine By similarity
Modified residuei709 – 7091N6-acetyllysine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP28331.
PaxDbiP28331.
PeptideAtlasiP28331.
PRIDEiP28331.

2D gel databases

REPRODUCTION-2DPAGEIPI00604664.
P28331.
UCD-2DPAGEP28331.

PTM databases

PhosphoSiteiP28331.

Miscellaneous databases

PMAP-CutDBP28331.

Expressioni

Gene expression databases

ArrayExpressiP28331.
BgeeiP28331.
CleanExiHS_NDUFS1.
GenevestigatoriP28331.

Interactioni

Subunit structurei

Complex I is composed of 45 different subunits.1 Publication

Protein-protein interaction databases

BioGridi110799. 38 interactions.
IntActiP28331. 12 interactions.
MINTiMINT-3011123.
STRINGi9606.ENSP00000233190.

Structurei

3D structure databases

ProteinModelPortaliP28331.
SMRiP28331. Positions 31-636.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 108792Fe-2S ferredoxin-type
Add
BLAST
Domaini245 – 301574Fe-4S Mo/W bis-MGD-type
Add
BLAST

Sequence similaritiesi

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG1034.
HOGENOMiHOG000031442.
HOVERGENiHBG003482.
InParanoidiP28331.
KOiK03934.
OMAiKEDWVII.
OrthoDBiEOG783MTP.
PhylomeDBiP28331.
TreeFamiTF105756.

Family and domain databases

Gene3Di3.10.20.30. 1 hit.
InterProiIPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view]
PfamiPF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SMARTiSM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view]
SUPFAMiSSF54292. SSF54292. 1 hit.
TIGRFAMsiTIGR01973. NuoG. 1 hit.
PROSITEiPS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

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

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P28331-1) [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

MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL    50
QACEKVGMQI PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW 100
NILTNSEKSK KAREGVMEFL LANHPLDCPI CDQGGECDLQ DQSMMFGNDR 150
SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT RCIRFASEIA GVDDLGTTGR 200
GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA RPWETRKTES 250
IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 300
RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA 350
LVALKDLLNR VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV 400
LLVGTNPRFE APLFNARIRK SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK 450
ILQDIASGSH PFSQVLKEAK KPMVVLGSSA LQRNDGAAIL AAVSSIAQKI 500
RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN PPKVLFLLGA 550
DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 600
GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS 650
PNLVRYDDIE GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI 700
SRASQTMAKC VKAVTEGAQA VEEPSIC 727
Length:727
Mass (Da):79,468
Last modified:March 7, 2006 - v3
Checksum:i9C35F4B8294771FB
GO
Isoform 2 (identifier: P28331-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRIRGSSGTLSRINM

Note: No experimental confirmation available.

Show »
Length:741
Mass (Da):80,997
Checksum:iEB7CA8F41E3DF6E2
GO
Isoform 3 (identifier: P28331-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: ML → MW
     3-113: Missing.

Note: No experimental confirmation available.

Show »
Length:616
Mass (Da):67,524
Checksum:i16CA2EF571877D03
GO
Isoform 4 (identifier: P28331-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.

Note: No experimental confirmation available.

Show »
Length:670
Mass (Da):73,527
Checksum:iC8B37BF8C954187F
GO
Isoform 5 (identifier: P28331-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     52-87: Missing.

Note: No experimental confirmation available.

Show »
Length:691
Mass (Da):75,375
Checksum:i522872E0D6EB9E09
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti241 – 2411R → Q.1 Publication
Corresponds to variant rs17856901 [ dbSNP | Ensembl ].
VAR_025511
Natural varianti241 – 2411R → W in MT-C1D. 1 Publication
VAR_019532
Natural varianti252 – 2521D → G in MT-C1D. 1 Publication
VAR_019533
Natural varianti253 – 2531V → G.1 Publication
VAR_069506
Natural varianti649 – 6491V → F.1 Publication
Corresponds to variant rs1044049 [ dbSNP | Ensembl ].
VAR_018463

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5757Missing in isoform 4.
VSP_043727Add
BLAST
Alternative sequencei1 – 22ML → MW in isoform 3.
VSP_043728
Alternative sequencei1 – 11M → MRIRGSSGTLSRINM in isoform 2.
VSP_042682
Alternative sequencei3 – 113111Missing in isoform 3.
VSP_043729Add
BLAST
Alternative sequencei52 – 8736Missing in isoform 5.
VSP_045864Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81K → R in CAA43412. 1 Publication
Sequence conflicti417 – 4171R → W in CAA43412. 1 Publication
Sequence conflicti572 – 5721H → L in BAG58551. 1 Publication
Sequence conflicti691 – 6911I → L in CAA43412. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61100 mRNA. Translation: CAA43412.1.
AK295705 mRNA. Translation: BAG58551.1.
AK295987 mRNA. Translation: BAG58762.1.
AK298320 mRNA. Translation: BAG60573.1.
AK300585 mRNA. Translation: BAG62283.1.
AC007383 Genomic DNA. Translation: AAY15061.1.
CH471063 Genomic DNA. Translation: EAW70379.1.
BC022368 mRNA. Translation: AAH22368.1.
BC030833 mRNA. Translation: AAH30833.1.
CCDSiCCDS2366.1. [P28331-1]
CCDS56162.1. [P28331-4]
CCDS56163.1. [P28331-3]
CCDS56164.1. [P28331-5]
CCDS56165.1. [P28331-2]
PIRiS17854.
RefSeqiNP_001186910.1. NM_001199981.1. [P28331-5]
NP_001186911.1. NM_001199982.1. [P28331-3]
NP_001186912.1. NM_001199983.1. [P28331-4]
NP_001186913.1. NM_001199984.1. [P28331-2]
NP_004997.4. NM_005006.6. [P28331-1]
UniGeneiHs.471207.
Hs.598436.

Genome annotation databases

EnsembliENST00000233190; ENSP00000233190; ENSG00000023228. [P28331-1]
ENST00000423725; ENSP00000397760; ENSG00000023228. [P28331-4]
ENST00000432169; ENSP00000409689; ENSG00000023228. [P28331-3]
ENST00000440274; ENSP00000409766; ENSG00000023228. [P28331-5]
ENST00000449699; ENSP00000399912; ENSG00000023228. [P28331-1]
ENST00000455934; ENSP00000392709; ENSG00000023228. [P28331-2]
GeneIDi4719.
KEGGihsa:4719.
UCSCiuc002vbe.3. human. [P28331-1]
uc010ziq.2. human. [P28331-2]
uc010zit.2. human. [P28331-3]

Polymorphism databases

DMDMi92090799.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X61100 mRNA. Translation: CAA43412.1 .
AK295705 mRNA. Translation: BAG58551.1 .
AK295987 mRNA. Translation: BAG58762.1 .
AK298320 mRNA. Translation: BAG60573.1 .
AK300585 mRNA. Translation: BAG62283.1 .
AC007383 Genomic DNA. Translation: AAY15061.1 .
CH471063 Genomic DNA. Translation: EAW70379.1 .
BC022368 mRNA. Translation: AAH22368.1 .
BC030833 mRNA. Translation: AAH30833.1 .
CCDSi CCDS2366.1. [P28331-1 ]
CCDS56162.1. [P28331-4 ]
CCDS56163.1. [P28331-3 ]
CCDS56164.1. [P28331-5 ]
CCDS56165.1. [P28331-2 ]
PIRi S17854.
RefSeqi NP_001186910.1. NM_001199981.1. [P28331-5 ]
NP_001186911.1. NM_001199982.1. [P28331-3 ]
NP_001186912.1. NM_001199983.1. [P28331-4 ]
NP_001186913.1. NM_001199984.1. [P28331-2 ]
NP_004997.4. NM_005006.6. [P28331-1 ]
UniGenei Hs.471207.
Hs.598436.

3D structure databases

ProteinModelPortali P28331.
SMRi P28331. Positions 31-636.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110799. 38 interactions.
IntActi P28331. 12 interactions.
MINTi MINT-3011123.
STRINGi 9606.ENSP00000233190.

Chemistry

ChEMBLi CHEMBL2363065.
DrugBanki DB00157. NADH.

PTM databases

PhosphoSitei P28331.

Polymorphism databases

DMDMi 92090799.

2D gel databases

REPRODUCTION-2DPAGE IPI00604664.
P28331.
UCD-2DPAGE P28331.

Proteomic databases

MaxQBi P28331.
PaxDbi P28331.
PeptideAtlasi P28331.
PRIDEi P28331.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000233190 ; ENSP00000233190 ; ENSG00000023228 . [P28331-1 ]
ENST00000423725 ; ENSP00000397760 ; ENSG00000023228 . [P28331-4 ]
ENST00000432169 ; ENSP00000409689 ; ENSG00000023228 . [P28331-3 ]
ENST00000440274 ; ENSP00000409766 ; ENSG00000023228 . [P28331-5 ]
ENST00000449699 ; ENSP00000399912 ; ENSG00000023228 . [P28331-1 ]
ENST00000455934 ; ENSP00000392709 ; ENSG00000023228 . [P28331-2 ]
GeneIDi 4719.
KEGGi hsa:4719.
UCSCi uc002vbe.3. human. [P28331-1 ]
uc010ziq.2. human. [P28331-2 ]
uc010zit.2. human. [P28331-3 ]

Organism-specific databases

CTDi 4719.
GeneCardsi GC02M206986.
HGNCi HGNC:7707. NDUFS1.
MIMi 157655. gene.
252010. phenotype.
neXtProti NX_P28331.
Orphaneti 2609. Isolated NADH-CoQ reductase deficiency.
255241. Leigh syndrome with leukodystrophy.
PharmGKBi PA31518.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1034.
HOGENOMi HOG000031442.
HOVERGENi HBG003482.
InParanoidi P28331.
KOi K03934.
OMAi KEDWVII.
OrthoDBi EOG783MTP.
PhylomeDBi P28331.
TreeFami TF105756.

Enzyme and pathway databases

Reactomei REACT_22393. Respiratory electron transport.

Miscellaneous databases

ChiTaRSi NDUFS1. human.
GeneWikii NDUFS1.
GenomeRNAii 4719.
NextBioi 18202.
PMAP-CutDB P28331.
PROi P28331.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28331.
Bgeei P28331.
CleanExi HS_NDUFS1.
Genevestigatori P28331.

Family and domain databases

Gene3Di 3.10.20.30. 1 hit.
InterProi IPR001041. 2Fe-2S_ferredoxin-type.
IPR012675. Beta-grasp_dom.
IPR006656. Mopterin_OxRdtase.
IPR006963. Mopterin_OxRdtase_4Fe-4S_dom.
IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS.
IPR010228. NADH_UbQ_OxRdtase_Gsu.
IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
IPR015405. NuoG_C.
[Graphical view ]
Pfami PF09326. DUF1982. 1 hit.
PF00384. Molybdopterin. 1 hit.
PF10588. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view ]
SMARTi SM00929. NADH-G_4Fe-4S_3. 1 hit.
[Graphical view ]
SUPFAMi SSF54292. SSF54292. 1 hit.
TIGRFAMsi TIGR01973. NuoG. 1 hit.
PROSITEi PS51085. 2FE2S_FER_2. 1 hit.
PS51669. 4FE4S_MOW_BIS_MGD. 1 hit.
PS00641. COMPLEX1_75K_1. 1 hit.
PS00642. COMPLEX1_75K_2. 1 hit.
PS00643. COMPLEX1_75K_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Determination of the cDNA sequence for the human mitochondrial 75-kDa Fe-S protein of NADH-coenzyme Q reductase."
    Chow W., Ragan I., Robinson B.H.
    Eur. J. Biochem. 201:547-550(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT PHE-649.
  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; 3; 4 AND 5).
    Tissue: Hippocampus, Kidney and Substantia nigra.
  3. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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), VARIANT GLN-241.
    Tissue: Brain and Liver.
  6. Lubec G., Vishwanath V., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 185-200; 247-266; 277-289; 312-325; 361-382; 451-467; 471-499; 519-538; 544-557 AND 625-655, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain, Cajal-Retzius cell and Fetal brain cortex.
  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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Large-scale deletion and point mutations of the nuclear NDUFV1 and NDUFS1 genes in mitochondrial complex I deficiency."
    Benit P., Chretien D., Kadhom N., de Lonlay-Debeney P., Cormier-Daire V., Cabral A., Peudenier S., Rustin P., Munnich A., Roetig A.
    Am. J. Hum. Genet. 68:1344-1352(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MT-C1D TRP-241 AND GLY-252.
  10. "Genomic analysis of mitochondrial diseases in a consanguineous population reveals novel candidate disease genes."
    Shamseldin H.E., Alshammari M., Al-Sheddi T., Salih M.A., Alkhalidi H., Kentab A., Repetto G.M., Hashem M., Alkuraya F.S.
    J. Med. Genet. 49:234-241(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT GLY-253.

Entry informationi

Entry nameiNDUS1_HUMAN
AccessioniPrimary (citable) accession number: P28331
Secondary accession number(s): B4DIN9
, B4DJA0, B4DPG1, B4DUC1, E7ENF3, Q53TR8, Q8N1C4, Q8TCC9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: March 7, 2006
Last modified: September 3, 2014
This is version 161 of the entry and version 3 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: 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

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