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Protein

Cysteine desulfurase, mitochondrial

Gene

NFS1

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

Functioni

Catalyzes the removal of elemental sulfur from cysteine to produce alanine. It supplies the inorganic sulfur for iron-sulfur (Fe-S) clusters. May be involved in the biosynthesis of molybdenum cofactor.1 Publication

Catalytic activityi

L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.

Cofactori

pyridoxal 5'-phosphateBy similarity

Kineticsi

Kinetic parameter was determined for the protein lacking the 55 N-terminal amino acids and in a complex with LYRM4.

  1. KM=434.75 µM for L-cysteine1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei207 – 2071Pyridoxal phosphateBy similarity
    Binding sitei235 – 2351Pyridoxal phosphateBy similarity
    Binding sitei295 – 2951Pyridoxal phosphateBy similarity
    Active sitei381 – 3811Cysteine persulfide intermediateBy similarity
    Metal bindingi381 – 3811Iron-sulfur (2Fe-2S); via persulfide group; shared with ISCUBy similarity

    GO - Molecular functioni

    • cysteine desulfurase activity Source: HGNC
    • iron-sulfur cluster binding Source: UniProtKB-KW
    • metal ion binding Source: UniProtKB-KW
    • protein homodimerization activity Source: HGNC
    • pyridoxal phosphate binding Source: InterPro

    GO - Biological processi

    • [2Fe-2S] cluster assembly Source: InterPro
    • iron incorporation into metallo-sulfur cluster Source: HGNC
    • molybdopterin cofactor biosynthetic process Source: Reactome
    • Mo-molybdopterin cofactor biosynthetic process Source: UniProtKB-KW
    • protein complex assembly Source: ProtInc
    • small molecule metabolic process Source: Reactome
    • sulfur amino acid metabolic process Source: ProtInc
    Complete GO annotation...

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

    Molybdenum cofactor biosynthesis

    Keywords - Ligandi

    Iron, Iron-sulfur, Metal-binding, Pyridoxal phosphate

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01304-MONOMER.
    ReactomeiR-HSA-1362409. Mitochondrial iron-sulfur cluster biogenesis.
    R-HSA-947581. Molybdenum cofactor biosynthesis.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Cysteine desulfurase, mitochondrial (EC:2.8.1.7)
    Gene namesi
    Name:NFS1
    Synonyms:NIFS
    ORF Names:HUSSY-08
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 20

    Organism-specific databases

    HGNCiHGNC:15910. NFS1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: HPA
    • cytosol Source: HGNC
    • intracellular membrane-bounded organelle Source: HPA
    • mitochondrial matrix Source: HGNC
    • mitochondrion Source: ProtInc
    • nucleolus Source: HPA
    • nucleoplasm Source: HPA
    • nucleus Source: HGNC
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    MalaCardsiNFS1.
    Orphaneti397593. Severe neonatal lactic acidosis due to NFS1-ISD11 complex deficiency.
    PharmGKBiPA31607.

    Chemistry

    DrugBankiDB00160. L-Alanine.
    DB00151. L-Cysteine.

    Polymorphism and mutation databases

    BioMutaiNFS1.
    DMDMi62512153.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 457Cysteine desulfurase, mitochondrialPRO_0000001292
    Transit peptidei1 – ?MitochondrionSequence analysis

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei258 – 2581N6-(pyridoxal phosphate)lysineBy similarity

    Proteomic databases

    EPDiQ9Y697.
    MaxQBiQ9Y697.
    PaxDbiQ9Y697.
    PeptideAtlasiQ9Y697.
    PRIDEiQ9Y697.

    PTM databases

    iPTMnetiQ9Y697.
    PhosphoSiteiQ9Y697.
    SwissPalmiQ9Y697.

    Expressioni

    Tissue specificityi

    Predominantly expressed in heart and skeletal muscle. Also found in brain, liver and pancreas.

    Gene expression databases

    BgeeiQ9Y697.
    CleanExiHS_NFS1.
    ExpressionAtlasiQ9Y697. baseline and differential.
    GenevisibleiQ9Y697. HS.

    Organism-specific databases

    HPAiCAB034314.
    HPA051801.
    HPA054755.

    Interactioni

    Subunit structurei

    Binds ISCU/NIFUN. Forms a complex with LYRM4.

    GO - Molecular functioni

    • protein homodimerization activity Source: HGNC

    Protein-protein interaction databases

    BioGridi114516. 29 interactions.
    IntActiQ9Y697. 9 interactions.
    STRINGi9606.ENSP00000363205.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y697.
    SMRiQ9Y697. Positions 58-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni127 – 1282Pyridoxal phosphate bindingBy similarity
    Regioni255 – 2573Pyridoxal phosphate bindingBy similarity

    Sequence similaritiesi

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiKOG1549. Eukaryota.
    COG1104. LUCA.
    GeneTreeiENSGT00530000063513.
    HOGENOMiHOG000017510.
    HOVERGENiHBG003708.
    InParanoidiQ9Y697.
    KOiK04487.
    OMAiEPIQSGG.
    PhylomeDBiQ9Y697.
    TreeFamiTF105658.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_00331. Cys_desulf_IscS.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR020578. Aminotrans_V_PyrdxlP_BS.
    IPR010240. Cys_deSase_IscS.
    IPR016454. Cysteine_dSase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005572. NifS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR02006. IscS. 1 hit.
    PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

    Note: Individual cells may vary AUG utilization in accordance with changes in metabolic status, the cytosolic pH being a strong determinant of this modulation.

    Isoform Mitochondrial (identifier: Q9Y697-1) [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

            10         20         30         40         50
    MLLRAAWRRA AVAVTAAPGP KPAAPTRGLR LRVGDRAPQS AVPADTAAAP
    60 70 80 90 100
    EVGPVLRPLY MDVQATTPLD PRVLDAMLPY LINYYGNPHS RTHAYGWESE
    110 120 130 140 150
    AAMERARQQV ASLIGADPRE IIFTSGATES NNIAIKGVAR FYRSRKKHLI
    160 170 180 190 200
    TTQTEHKCVL DSCRSLEAEG FQVTYLPVQK SGIIDLKELE AAIQPDTSLV
    210 220 230 240 250
    SVMTVNNEIG VKQPIAEIGR ICSSRKVYFH TDAAQAVGKI PLDVNDMKID
    260 270 280 290 300
    LMSISGHKIY GPKGVGAIYI RRRPRVRVEA LQSGGGQERG MRSGTVPTPL
    310 320 330 340 350
    VVGLGAACEV AQQEMEYDHK RISKLSERLI QNIMKSLPDV VMNGDPKHHY
    360 370 380 390 400
    PGCINLSFAY VEGESLLMAL KDVALSSGSA CTSASLEPSY VLRAIGTDED
    410 420 430 440 450
    LAHSSIRFGI GRFTTEEEVD YTVEKCIQHV KRLREMSPLW EMVQDGIDLK

    SIKWTQH
    Length:457
    Mass (Da):50,196
    Last modified:April 12, 2005 - v3
    Checksum:iFDE76177DB6E751B
    GO
    Isoform Cytoplasmic (identifier: Q9Y697-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-60: Missing.

    Show »
    Length:397
    Mass (Da):44,017
    Checksum:i61DF3AD65D5CDD3C
    GO
    Isoform 3 (identifier: Q9Y697-3) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         136-186: Missing.

    Show »
    Length:406
    Mass (Da):44,362
    Checksum:i422B10BDBCD0FAB2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti5 – 51A → V in AAD09187 (PubMed:9885568).Curated
    Sequence conflicti47 – 471A → T in AAD09187 (PubMed:9885568).Curated
    Sequence conflicti197 – 1971T → A in BAG63421 (PubMed:14702039).Curated
    Sequence conflicti412 – 4121R → A in AAD09187 (PubMed:9885568).Curated
    Sequence conflicti431 – 4311K → N in AAD09187 (PubMed:9885568).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 6060Missing in isoform Cytoplasmic. 4 PublicationsVSP_018646Add
    BLAST
    Alternative sequencei136 – 18651Missing in isoform 3. 1 PublicationVSP_045860Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097025 mRNA. Translation: AAD09187.2.
    AK001470 mRNA. Translation: BAG50917.1.
    AK302023 mRNA. Translation: BAG63421.1.
    AL109827, AL357374 Genomic DNA. Translation: CAB87612.2.
    AL109827, AL357374 Genomic DNA. Translation: CAI20116.1.
    CH471077 Genomic DNA. Translation: EAW76170.1.
    CH471077 Genomic DNA. Translation: EAW76172.1.
    BC065560 mRNA. Translation: AAH65560.1.
    AJ010952 mRNA. Translation: CAA09424.1.
    CCDSiCCDS13262.1. [Q9Y697-1]
    CCDS56185.1. [Q9Y697-3]
    RefSeqiNP_001185918.1. NM_001198989.1. [Q9Y697-3]
    NP_066923.3. NM_021100.4. [Q9Y697-1]
    UniGeneiHs.194692.

    Genome annotation databases

    EnsembliENST00000374085; ENSP00000363198; ENSG00000244005. [Q9Y697-2]
    ENST00000374092; ENSP00000363205; ENSG00000244005. [Q9Y697-1]
    ENST00000397425; ENSP00000380570; ENSG00000244005. [Q9Y697-2]
    ENST00000541387; ENSP00000440897; ENSG00000244005. [Q9Y697-3]
    GeneIDi9054.
    KEGGihsa:9054.
    UCSCiuc002xdt.3. human. [Q9Y697-1]

    Keywords - Coding sequence diversityi

    Alternative initiation, Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF097025 mRNA. Translation: AAD09187.2.
    AK001470 mRNA. Translation: BAG50917.1.
    AK302023 mRNA. Translation: BAG63421.1.
    AL109827, AL357374 Genomic DNA. Translation: CAB87612.2.
    AL109827, AL357374 Genomic DNA. Translation: CAI20116.1.
    CH471077 Genomic DNA. Translation: EAW76170.1.
    CH471077 Genomic DNA. Translation: EAW76172.1.
    BC065560 mRNA. Translation: AAH65560.1.
    AJ010952 mRNA. Translation: CAA09424.1.
    CCDSiCCDS13262.1. [Q9Y697-1]
    CCDS56185.1. [Q9Y697-3]
    RefSeqiNP_001185918.1. NM_001198989.1. [Q9Y697-3]
    NP_066923.3. NM_021100.4. [Q9Y697-1]
    UniGeneiHs.194692.

    3D structure databases

    ProteinModelPortaliQ9Y697.
    SMRiQ9Y697. Positions 58-444.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi114516. 29 interactions.
    IntActiQ9Y697. 9 interactions.
    STRINGi9606.ENSP00000363205.

    Chemistry

    DrugBankiDB00160. L-Alanine.
    DB00151. L-Cysteine.

    PTM databases

    iPTMnetiQ9Y697.
    PhosphoSiteiQ9Y697.
    SwissPalmiQ9Y697.

    Polymorphism and mutation databases

    BioMutaiNFS1.
    DMDMi62512153.

    Proteomic databases

    EPDiQ9Y697.
    MaxQBiQ9Y697.
    PaxDbiQ9Y697.
    PeptideAtlasiQ9Y697.
    PRIDEiQ9Y697.

    Protocols and materials databases

    DNASUi9054.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000374085; ENSP00000363198; ENSG00000244005. [Q9Y697-2]
    ENST00000374092; ENSP00000363205; ENSG00000244005. [Q9Y697-1]
    ENST00000397425; ENSP00000380570; ENSG00000244005. [Q9Y697-2]
    ENST00000541387; ENSP00000440897; ENSG00000244005. [Q9Y697-3]
    GeneIDi9054.
    KEGGihsa:9054.
    UCSCiuc002xdt.3. human. [Q9Y697-1]

    Organism-specific databases

    CTDi9054.
    GeneCardsiNFS1.
    HGNCiHGNC:15910. NFS1.
    HPAiCAB034314.
    HPA051801.
    HPA054755.
    MalaCardsiNFS1.
    MIMi603485. gene.
    neXtProtiNX_Q9Y697.
    Orphaneti397593. Severe neonatal lactic acidosis due to NFS1-ISD11 complex deficiency.
    PharmGKBiPA31607.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG1549. Eukaryota.
    COG1104. LUCA.
    GeneTreeiENSGT00530000063513.
    HOGENOMiHOG000017510.
    HOVERGENiHBG003708.
    InParanoidiQ9Y697.
    KOiK04487.
    OMAiEPIQSGG.
    PhylomeDBiQ9Y697.
    TreeFamiTF105658.

    Enzyme and pathway databases

    BioCyciMetaCyc:HS01304-MONOMER.
    ReactomeiR-HSA-1362409. Mitochondrial iron-sulfur cluster biogenesis.
    R-HSA-947581. Molybdenum cofactor biosynthesis.

    Miscellaneous databases

    ChiTaRSiNFS1. human.
    GeneWikiiNFS1.
    GenomeRNAii9054.
    PROiQ9Y697.
    SOURCEiSearch...

    Gene expression databases

    BgeeiQ9Y697.
    CleanExiHS_NFS1.
    ExpressionAtlasiQ9Y697. baseline and differential.
    GenevisibleiQ9Y697. HS.

    Family and domain databases

    Gene3Di3.40.640.10. 1 hit.
    3.90.1150.10. 1 hit.
    HAMAPiMF_00331. Cys_desulf_IscS.
    InterProiIPR000192. Aminotrans_V_dom.
    IPR020578. Aminotrans_V_PyrdxlP_BS.
    IPR010240. Cys_deSase_IscS.
    IPR016454. Cysteine_dSase.
    IPR015424. PyrdxlP-dep_Trfase.
    IPR015421. PyrdxlP-dep_Trfase_major_sub1.
    IPR015422. PyrdxlP-dep_Trfase_major_sub2.
    [Graphical view]
    PfamiPF00266. Aminotran_5. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005572. NifS. 1 hit.
    SUPFAMiSSF53383. SSF53383. 1 hit.
    TIGRFAMsiTIGR02006. IscS. 1 hit.
    PROSITEiPS00595. AA_TRANSFER_CLASS_5. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Targeting of a human iron-sulfur cluster assembly enzyme, nifs, to different subcellular compartments is regulated through alternative AUG utilization."
      Land T., Rouault T.A.
      Mol. Cell 2:807-815(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM CYTOPLASMIC), ALTERNATIVE INITIATION, SUBCELLULAR LOCATION.
    2. Land T., Rouault T.A.
      Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 380-402.
    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] (ISOFORMS CYTOPLASMIC AND 3).
      Tissue: Testis.
    4. "The DNA sequence and comparative analysis of human chromosome 20."
      Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
      , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
      Nature 414:865-871(2001) [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] (ISOFORM CYTOPLASMIC).
      Tissue: Pancreas.
    7. "Characterization of 16 novel human genes showing high similarity to yeast sequences."
      Stanchi F., Bertocco E., Toppo S., Dioguardi R., Simionati B., Cannata N., Zimbello R., Lanfranchi G., Valle G.
      Yeast 18:69-80(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 140-457 (ISOFORM CYTOPLASMIC).
    8. "Distinct iron-sulfur cluster assembly complexes exist in the cytosol and mitochondria of human cells."
      Tong W.-H., Rouault T.
      EMBO J. 19:5692-5700(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ISCU.
    9. "A novel role for human Nfs1 in the cytoplasm: Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis."
      Marelja Z., Stoecklein W., Nimtz M., Leimkuehler S.
      J. Biol. Chem. 283:25178-25185(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH LYRM4.
    10. "Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis."
      Shi Y., Ghosh M.C., Tong W.H., Rouault T.A.
      Hum. Mol. Genet. 18:3014-3025(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LYRM4, SUBCELLULAR LOCATION.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiNFS1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y697
    Secondary accession number(s): B3KMA5
    , B4DXK9, E1P5R8, F5GYK5, Q6P0L8, Q9NTZ5, Q9Y481
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 27, 2001
    Last sequence update: April 12, 2005
    Last modified: July 6, 2016
    This is version 159 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, Reference proteome

    Documents

    1. Human chromosome 20
      Human chromosome 20: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.