P28331 (NDUS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:

NDUFS1

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	727 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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 activity	NADH + ubiquinone = NAD+ + ubiquinol. NADH + acceptor = NAD+ + reduced acceptor.
Cofactor	Binds 1 2Fe-2S cluster per subunit By similarity. Binds 2 4Fe-4S clusters per subunit By similarity.
Subunit structure	Complex I is composed of 45 different subunits. Ref.7
Subcellular location	Mitochondrion inner membrane.
Involvement in disease	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. Ref.9
Sequence similarities	Belongs to the complex I 75 kDa subunit family. Contains 1 2Fe-2S ferredoxin-type domain.

Ontologies

Keywords
Biological process	Electron transport Respiratory chain Transport
Cellular component	Membrane Mitochondrion Mitochondrion inner membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation
Domain	Transit peptide
Ligand	2Fe-2S 4Fe-4S Iron Iron-sulfur Metal-binding NAD Ubiquinone
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP metabolic process Inferred from mutant phenotype PubMed 15186778. Source: UniProtKB apoptotic process Inferred from direct assay PubMed 15186778. Source: UniProtKB mitochondrial electron transport, NADH to ubiquinone Non-traceable author statement PubMed 9878551. Source: UniProtKB reactive oxygen species metabolic process Inferred from mutant phenotype PubMed 15186778PubMed 16478720PubMed 16870178. Source: UniProtKB regulation of mitochondrial membrane potential Inferred from mutant phenotype PubMed 15186778PubMed 16478720. Source: UniProtKB
Cellular_component	mitochondrial intermembrane space Inferred from direct assay PubMed 15186778. Source: UniProtKB mitochondrial respiratory chain complex I Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	2 iron, 2 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW NADH dehydrogenase (ubiquinone) activity Non-traceable author statement PubMed 9878551. Source: UniProtKB electron carrier activity Non-traceable author statement Ref.1. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P28331-1)

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.

Isoform 2 (identifier: P28331-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: P28331-3)

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

Note: No experimental confirmation available.

Isoform 4 (identifier: P28331-4)

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

Note: No experimental confirmation available.

Isoform 5 (identifier: P28331-5)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Transit peptide	1 – 23	23	Mitochondrion By similarity
	Chain	24 – 727	704	NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial		PRO_0000019968
Regions
	Domain	30 – 108	79	2Fe-2S ferredoxin-type
Sites
	Metal binding	64	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	75	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	78	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	92	1	Iron-sulfur 1 (2Fe-2S) By similarity
	Metal binding	124	1	Iron-sulfur 2 (4Fe-4S); via pros nitrogen By similarity
	Metal binding	128	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	131	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	137	1	Iron-sulfur 2 (4Fe-4S) By similarity
	Metal binding	176	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	179	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	182	1	Iron-sulfur 3 (4Fe-4S) By similarity
	Metal binding	226	1	Iron-sulfur 3 (4Fe-4S) By similarity
Amino acid modifications
	Modified residue	84	1	N6-acetyllysine By similarity
Natural variations
	Alternative sequence	1 – 57	57	Missing in isoform 4.		VSP_043727
	Alternative sequence	1 – 2	2	ML → MW in isoform 3.		VSP_043728
	Alternative sequence	1	1	M → MRIRGSSGTLSRINM in isoform 2.		VSP_042682
	Alternative sequence	3 – 113	111	Missing in isoform 3.		VSP_043729
	Alternative sequence	52 – 87	36	Missing in isoform 5.		VSP_045864
	Natural variant	241	1	R → Q. Ref.5 Corresponds to variant rs17856901 [ dbSNP | Ensembl ].		VAR_025511
	Natural variant	241	1	R → W in MT-C1D. Ref.9		VAR_019532
	Natural variant	252	1	D → G in MT-C1D. Ref.9		VAR_019533
	Natural variant	649	1	V → F. Ref.1 Corresponds to variant rs1044049 [ dbSNP | Ensembl ].		VAR_018463
Experimental info
	Sequence conflict	8	1	K → R in CAA43412. Ref.1
	Sequence conflict	417	1	R → W in CAA43412. Ref.1
	Sequence conflict	572	1	H → L in BAG58551. Ref.2
	Sequence conflict	691	1	I → L in CAA43412. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 7, 2006. Version 3. Checksum: 9C35F4B8294771FB	FASTA	727	79,468
	10 20 30 40 50 60 MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QACEKVGMQI 70 80 90 100 110 120 PRFCYHERLS VAGNCRMCLV EIEKAPKVVA ACAMPVMKGW NILTNSEKSK KAREGVMEFL 130 140 150 160 170 180 LANHPLDCPI CDQGGECDLQ DQSMMFGNDR SRFLEGKRAV EDKNIGPLVK TIMTRCIQCT 190 200 210 220 230 240 RCIRFASEIA GVDDLGTTGR GNDMQVGTYI EKMFMSELSG NIIDICPVGA LTSKPYAFTA 250 260 270 280 290 300 RPWETRKTES IDVMDAVGSN IVVSTRTGEV MRILPRMHED INEEWISDKT RFAYDGLKRQ 310 320 330 340 350 360 RLTEPMVRNE KGLLTYTSWE DALSRVAGML QSFQGKDVAA IAGGLVDAEA LVALKDLLNR 370 380 390 400 410 420 VDSDTLCTEE VFPTAGAGTD LRSNYLLNTT IAGVEEADVV LLVGTNPRFE APLFNARIRK 430 440 450 460 470 480 SWLHNDLKVA LIGSPVDLTY TYDHLGDSPK ILQDIASGSH PFSQVLKEAK KPMVVLGSSA 490 500 510 520 530 540 LQRNDGAAIL AAVSSIAQKI RMTSGVTGDW KVMNILHRIA SQVAALDLGY KPGVEAIRKN 550 560 570 580 590 600 PPKVLFLLGA DGGCITRQDL PKDCFIIYQG HHGDVGAPIA DVILPGAAYT EKSATYVNTE 610 620 630 640 650 660 GRAQQTKVAV TPPGLAREDW KIIRALSEIA GMTLPYDTLD QVRNRLEEVS PNLVRYDDIE 670 680 690 700 710 720 GANYFQQANE LSKLVNQQLL ADPLVPPQLT IKDFYMTDSI SRASQTMAKC VKAVTEGAQA VEEPSIC
	Isoform 2 [UniParc]. Checksum: EB7CA8F41E3DF6E2	FASTA	741	80,997
	10 20 30 40 50 60 MRIRGSSGTL SRINMLRIPV RKALVGLSKS PKGCVRTTAT AASNLIEVFV DGQSVMVEPG 70 80 90 100 110 120 TTVLQACEKV GMQIPRFCYH ERLSVAGNCR MCLVEIEKAP KVVAACAMPV MKGWNILTNS 130 140 150 160 170 180 EKSKKAREGV MEFLLANHPL DCPICDQGGE CDLQDQSMMF GNDRSRFLEG KRAVEDKNIG 190 200 210 220 230 240 PLVKTIMTRC IQCTRCIRFA SEIAGVDDLG TTGRGNDMQV GTYIEKMFMS ELSGNIIDIC 250 260 270 280 290 300 PVGALTSKPY AFTARPWETR KTESIDVMDA VGSNIVVSTR TGEVMRILPR MHEDINEEWI 310 320 330 340 350 360 SDKTRFAYDG LKRQRLTEPM VRNEKGLLTY TSWEDALSRV AGMLQSFQGK DVAAIAGGLV 370 380 390 400 410 420 DAEALVALKD LLNRVDSDTL CTEEVFPTAG AGTDLRSNYL LNTTIAGVEE ADVVLLVGTN 430 440 450 460 470 480 PRFEAPLFNA RIRKSWLHND LKVALIGSPV DLTYTYDHLG DSPKILQDIA SGSHPFSQVL 490 500 510 520 530 540 KEAKKPMVVL GSSALQRNDG AAILAAVSSI AQKIRMTSGV TGDWKVMNIL HRIASQVAAL 550 560 570 580 590 600 DLGYKPGVEA IRKNPPKVLF LLGADGGCIT RQDLPKDCFI IYQGHHGDVG APIADVILPG 610 620 630 640 650 660 AAYTEKSATY VNTEGRAQQT KVAVTPPGLA REDWKIIRAL SEIAGMTLPY DTLDQVRNRL 670 680 690 700 710 720 EEVSPNLVRY DDIEGANYFQ QANELSKLVN QQLLADPLVP PQLTIKDFYM TDSISRASQT 730 740 MAKCVKAVTE GAQAVEEPSI C
	Isoform 3 [UniParc]. Checksum: 16CA2EF571877D03	FASTA	616	67,524
	10 20 30 40 50 60 MWEGVMEFLL ANHPLDCPIC DQGGECDLQD QSMMFGNDRS RFLEGKRAVE DKNIGPLVKT 70 80 90 100 110 120 IMTRCIQCTR CIRFASEIAG VDDLGTTGRG NDMQVGTYIE KMFMSELSGN IIDICPVGAL 130 140 150 160 170 180 TSKPYAFTAR PWETRKTESI DVMDAVGSNI VVSTRTGEVM RILPRMHEDI NEEWISDKTR 190 200 210 220 230 240 FAYDGLKRQR LTEPMVRNEK GLLTYTSWED ALSRVAGMLQ SFQGKDVAAI AGGLVDAEAL 250 260 270 280 290 300 VALKDLLNRV DSDTLCTEEV FPTAGAGTDL RSNYLLNTTI AGVEEADVVL LVGTNPRFEA 310 320 330 340 350 360 PLFNARIRKS WLHNDLKVAL IGSPVDLTYT YDHLGDSPKI LQDIASGSHP FSQVLKEAKK 370 380 390 400 410 420 PMVVLGSSAL QRNDGAAILA AVSSIAQKIR MTSGVTGDWK VMNILHRIAS QVAALDLGYK 430 440 450 460 470 480 PGVEAIRKNP PKVLFLLGAD GGCITRQDLP KDCFIIYQGH HGDVGAPIAD VILPGAAYTE 490 500 510 520 530 540 KSATYVNTEG RAQQTKVAVT PPGLAREDWK IIRALSEIAG MTLPYDTLDQ VRNRLEEVSP 550 560 570 580 590 600 NLVRYDDIEG ANYFQQANEL SKLVNQQLLA DPLVPPQLTI KDFYMTDSIS RASQTMAKCV 610 KAVTEGAQAV EEPSIC
	Isoform 4 [UniParc]. Checksum: C8B37BF8C954187F	FASTA	670	73,527
	10 20 30 40 50 60 MQIPRFCYHE RLSVAGNCRM CLVEIEKAPK VVAACAMPVM KGWNILTNSE KSKKAREGVM 70 80 90 100 110 120 EFLLANHPLD CPICDQGGEC DLQDQSMMFG NDRSRFLEGK RAVEDKNIGP LVKTIMTRCI 130 140 150 160 170 180 QCTRCIRFAS EIAGVDDLGT TGRGNDMQVG TYIEKMFMSE LSGNIIDICP VGALTSKPYA 190 200 210 220 230 240 FTARPWETRK TESIDVMDAV GSNIVVSTRT GEVMRILPRM HEDINEEWIS DKTRFAYDGL 250 260 270 280 290 300 KRQRLTEPMV RNEKGLLTYT SWEDALSRVA GMLQSFQGKD VAAIAGGLVD AEALVALKDL 310 320 330 340 350 360 LNRVDSDTLC TEEVFPTAGA GTDLRSNYLL NTTIAGVEEA DVVLLVGTNP RFEAPLFNAR 370 380 390 400 410 420 IRKSWLHNDL KVALIGSPVD LTYTYDHLGD SPKILQDIAS GSHPFSQVLK EAKKPMVVLG 430 440 450 460 470 480 SSALQRNDGA AILAAVSSIA QKIRMTSGVT GDWKVMNILH RIASQVAALD LGYKPGVEAI 490 500 510 520 530 540 RKNPPKVLFL LGADGGCITR QDLPKDCFII YQGHHGDVGA PIADVILPGA AYTEKSATYV 550 560 570 580 590 600 NTEGRAQQTK VAVTPPGLAR EDWKIIRALS EIAGMTLPYD TLDQVRNRLE EVSPNLVRYD 610 620 630 640 650 660 DIEGANYFQQ ANELSKLVNQ QLLADPLVPP QLTIKDFYMT DSISRASQTM AKCVKAVTEG 670 AQAVEEPSIC
	Isoform 5 [UniParc]. Checksum: 522872E0D6EB9E09	FASTA	691	75,375
	10 20 30 40 50 60 MLRIPVRKAL VGLSKSPKGC VRTTATAASN LIEVFVDGQS VMVEPGTTVL QVVAACAMPV 70 80 90 100 110 120 MKGWNILTNS EKSKKAREGV MEFLLANHPL DCPICDQGGE CDLQDQSMMF GNDRSRFLEG 130 140 150 160 170 180 KRAVEDKNIG PLVKTIMTRC IQCTRCIRFA SEIAGVDDLG TTGRGNDMQV GTYIEKMFMS 190 200 210 220 230 240 ELSGNIIDIC PVGALTSKPY AFTARPWETR KTESIDVMDA VGSNIVVSTR TGEVMRILPR 250 260 270 280 290 300 MHEDINEEWI SDKTRFAYDG LKRQRLTEPM VRNEKGLLTY TSWEDALSRV AGMLQSFQGK 310 320 330 340 350 360 DVAAIAGGLV DAEALVALKD LLNRVDSDTL CTEEVFPTAG AGTDLRSNYL LNTTIAGVEE 370 380 390 400 410 420 ADVVLLVGTN PRFEAPLFNA RIRKSWLHND LKVALIGSPV DLTYTYDHLG DSPKILQDIA 430 440 450 460 470 480 SGSHPFSQVL KEAKKPMVVL GSSALQRNDG AAILAAVSSI AQKIRMTSGV TGDWKVMNIL 490 500 510 520 530 540 HRIASQVAAL DLGYKPGVEA IRKNPPKVLF LLGADGGCIT RQDLPKDCFI IYQGHHGDVG 550 560 570 580 590 600 APIADVILPG AAYTEKSATY VNTEGRAQQT KVAVTPPGLA REDWKIIRAL SEIAGMTLPY 610 620 630 640 650 660 DTLDQVRNRL EEVSPNLVRY DDIEGANYFQ QANELSKLVN QQLLADPLVP PQLTIKDFYM 670 680 690 TDSISRASQT MAKCVKAVTE GAQAVEEPSI C

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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, 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: MASS SPECTROMETRY, IDENTIFICATION IN THE NADH-UBIQUINONE OXIDOREDUCTASE COMPLEX.
[8]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00925023. IPI00927225. IPI00927308. IPI00940744.
PIR	S17854.
RefSeq	NP_001186910.1. NM_001199981.1. NP_001186911.1. NM_001199982.1. NP_001186912.1. NM_001199983.1. NP_001186913.1. NM_001199984.1. NP_004997.4. NM_005006.6.
UniGene	Hs.471207. Hs.598436.
3D structure databases
ProteinModelPortal	P28331.
ModBase	Search...
Protein-protein interaction databases
IntAct	P28331. 8 interactions.
STRING	9606.ENSP00000233190.
PTM databases
PhosphoSite	P28331.
Polymorphism databases
DMDM	92090799.
2D gel databases
REPRODUCTION-2DPAGE	IPI00604664. P28331.
UCD-2DPAGE	P28331.
Proteomic databases
PaxDb	P28331.
PeptideAtlas	P28331.
PRIDE	P28331.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000233190; ENSP00000233190; ENSG00000023228. ENST00000423725; ENSP00000397760; ENSG00000023228. ENST00000432169; ENSP00000409689; ENSG00000023228. ENST00000440274; ENSP00000409766; ENSG00000023228. ENST00000449699; ENSP00000399912; ENSG00000023228. ENST00000455934; ENSP00000392709; ENSG00000023228.
GeneID	4719.
KEGG	hsa:4719.
UCSC	uc002vbe.3. human.
Organism-specific databases
CTD	4719.
GeneCards	GC02M206986.
HGNC	HGNC:7707. NDUFS1.
MIM	157655. gene. 252010. phenotype.
neXtProt	NX_P28331.
Orphanet	2609. Isolated NADH-CoQ reductase deficiency. 255241. Leigh syndrome with leukodystrophy.
PharmGKB	PA31518.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1034.
HOGENOM	HOG000031442.
HOVERGEN	HBG003482.
InParanoid	P28331.
KO	K03934.
OMA	LNTKIAG.
OrthoDB	EOG4D26PC.
PhylomeDB	P28331.
Enzyme and pathway databases
Reactome	REACT_111217. Metabolism.
Gene expression databases
ArrayExpress	P28331.
Bgee	P28331.
CleanEx	HS_NDUFS1.
Genevestigator	P28331.
GermOnline	ENSG00000023228. Homo sapiens.
Family and domain databases
Gene3D	3.10.20.30. 1 hit.
InterPro	IPR001041. 2Fe-2S_ferredoxin-type. IPR012675. Beta-grasp_dom. IPR006656. Mopterin_OxRdtase. IPR000283. NADH_UbQ_OxRdtase_75kDa_su_CS. IPR010228. NADH_UbQ_OxRdtase_Gsu. IPR019574. NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd. IPR015405. NuoG_C. [Graphical view]
Pfam	PF09326. DUF1982. 1 hit. PF00384. Molybdopterin. 1 hit. PF10588. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SMART	SM00929. NADH-G_4Fe-4S_3. 1 hit. [Graphical view]
SUPFAM	SSF54292. Ferredoxin. 1 hit.
TIGRFAMs	TIGR01973. NuoG. 1 hit.
PROSITE	PS00197. 2FE2S_FER_1. False negative. PS51085. 2FE2S_FER_2. 1 hit. PS00641. COMPLEX1_75K_1. 1 hit. PS00642. COMPLEX1_75K_2. 1 hit. PS00643. COMPLEX1_75K_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	NDUFS1. human.
DrugBank	DB00157. NADH.
GenomeRNAi	4719.
NextBio	18202.
PMAP-CutDB	P28331.
SOURCE	Search...

Entry information

Entry name

NDUS1_HUMAN

Accession

Primary (citable) accession number: P28331
Secondary accession number(s): B4DIN9 , B4DJA0, B4DPG1, B4DUC1, E7ENF3, Q53TR8, Q8N1C4, Q8TCC9

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 1992
Last sequence update:	March 7, 2006
Last modified:	May 1, 2013
This is version 146 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.