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Q9H1K1

- ISCU_HUMAN

UniProt

Q9H1K1 - ISCU_HUMAN

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Protein

Iron-sulfur cluster assembly enzyme ISCU, mitochondrial

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

Functioni

Involved in the assembly or repair of the [Fe-S] clusters present in iron-sulfur proteins. Binds iron.1 Publication

GO - Molecular functioni

  1. iron ion binding Source: UniProtKB
  2. iron-sulfur cluster binding Source: InterPro
  3. protein binding Source: UniProtKB
  4. protein complex scaffold Source: HGNC

GO - Biological processi

  1. iron-sulfur cluster assembly Source: UniProtKB
  2. nitrogen fixation Source: UniProtKB
  3. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Ligandi

Iron, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_150353. Mitochondrial iron-sulfur cluster biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Iron-sulfur cluster assembly enzyme ISCU, mitochondrial
Alternative name(s):
NifU-like N-terminal domain-containing protein
NifU-like protein
Gene namesi
Name:ISCU
Synonyms:NIFUN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:29882. ISCU.

Subcellular locationi

Isoform 1 : Mitochondrion 1 Publication
Isoform 2 : Cytoplasm. Nucleus 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: HGNC
  3. mitochondrial matrix Source: Reactome
  4. mitochondrion Source: UniProtKB
  5. nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Myopathy with exercise intolerance Swedish type (MEIS) [MIM:255125]: Autosomal recessive metabolic disease characterized by lifelong severe exercise intolerance, in which minor exertion causes fatigue of active muscles, shortness of breath, and cardiac palpitations in association with lactic acidosis. The biochemical phenotype is characterized by a deficiency in mitochondrial iron-sulfur proteins and impaired muscle oxidative metabolism.
Note: The disease is caused by mutations affecting the gene represented in this entry.1 Publication

Organism-specific databases

MIMi255125. phenotype.
Orphaneti43115. Hereditary myopathy with lactic acidosis due to ISCU deficiency.
PharmGKBiPA162392328.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 3434Mitochondrion Reviewed predictionAdd
BLAST
Chaini35 – 167133Iron-sulfur cluster assembly enzyme ISCU, mitochondrialPRO_0000019692Add
BLAST

Proteomic databases

MaxQBiQ9H1K1.
PaxDbiQ9H1K1.
PRIDEiQ9H1K1.

PTM databases

PhosphoSiteiQ9H1K1.

Expressioni

Tissue specificityi

Detected in heart, liver, skeletal muscle, brain, pancreas, kidney, lung and placenta.2 Publications

Gene expression databases

ArrayExpressiQ9H1K1.
BgeeiQ9H1K1.
CleanExiHS_ISCU.
GenevestigatoriQ9H1K1.

Organism-specific databases

HPAiCAB006329.
HPA038602.

Interactioni

Subunit structurei

Binds NFS1. Interacts with HSCB.2 Publications

Protein-protein interaction databases

BioGridi117038. 2 interactions.
IntActiQ9H1K1. 3 interactions.
MINTiMINT-3066312.
STRINGi9606.ENSP00000310623.

Structurei

3D structure databases

ProteinModelPortaliQ9H1K1.
SMRiQ9H1K1. Positions 44-162.

Family & Domainsi

Sequence similaritiesi

Belongs to the NifU family.

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0822.
HOGENOMiHOG000069228.
HOVERGENiHBG052621.
InParanoidiQ9H1K1.
OMAiRAGNDIC.
OrthoDBiEOG7JMGGC.
PhylomeDBiQ9H1K1.
TreeFamiTF105422.

Family and domain databases

InterProiIPR011339. ISC_FeS_clus_asmbl_IscU.
IPR002871. NIF_FeS_clus_asmbl_NifU_N.
[Graphical view]
PfamiPF01592. NifU_N. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01999. iscU. 1 hit.

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: Q9H1K1-1) [UniParc]FASTAAdd to Basket

Also known as: ISCU2

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

MAAAGAFRLR RAASALLLRS PRLPARELSA PARLYHKKVV DHYENPRNVG    50
SLDKTSKNVG TGLVGAPACG DVMKLQIQVD EKGKIVDARF KTFGCGSAIA 100
SSSLATEWVK GKTVEEALTI KNTDIAKELC LPPVKLHCSM LAEDAIKAAL 150
ADYKLKQEPK KGEAEKK 167
Length:167
Mass (Da):17,999
Last modified:November 30, 2010 - v2
Checksum:i0166D3EC9F1EEB47
GO
Isoform 2 (identifier: Q9H1K1-2) [UniParc]FASTAAdd to Basket

Also known as: ISCU1

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MAAAGAFRLRRAASALLLRSPRLPARELSAPARLYHKK → MVLIDMSVDLSTQ

Show »
Length:142
Mass (Da):15,263
Checksum:iEE72CEDC86CD6FF0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121A → V.5 Publications
Corresponds to variant rs2287555 [ dbSNP | Ensembl ].
VAR_060728

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 3838MAAAG…LYHKK → MVLIDMSVDLSTQ in isoform 2. VSP_013492Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71F → G in AAG37428. 1 Publication
Sequence conflicti7 – 71F → G in AAH11906. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY009127 mRNA. Translation: AAG37427.1.
AY009128 mRNA. Translation: AAG37428.1.
AC008119 Genomic DNA. No translation available.
BC011906 mRNA. Translation: AAH11906.1.
BC061903 mRNA. Translation: AAH61903.1.
U47101 mRNA. Translation: AAC50885.1.
CCDSiCCDS44966.1. [Q9H1K1-1]
CCDS9118.1. [Q9H1K1-2]
RefSeqiNP_055116.1. NM_014301.3. [Q9H1K1-2]
NP_998760.1. NM_213595.2. [Q9H1K1-1]
XP_006719378.1. XM_006719315.1. [Q9H1K1-2]
UniGeneiHs.615131.

Genome annotation databases

EnsembliENST00000311893; ENSP00000310623; ENSG00000136003. [Q9H1K1-1]
ENST00000392807; ENSP00000376554; ENSG00000136003. [Q9H1K1-2]
GeneIDi23479.
KEGGihsa:23479.
UCSCiuc001tnc.4. human. [Q9H1K1-2]
uc010sxc.2. human. [Q9H1K1-1]

Polymorphism databases

DMDMi313104118.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY009127 mRNA. Translation: AAG37427.1 .
AY009128 mRNA. Translation: AAG37428.1 .
AC008119 Genomic DNA. No translation available.
BC011906 mRNA. Translation: AAH11906.1 .
BC061903 mRNA. Translation: AAH61903.1 .
U47101 mRNA. Translation: AAC50885.1 .
CCDSi CCDS44966.1. [Q9H1K1-1 ]
CCDS9118.1. [Q9H1K1-2 ]
RefSeqi NP_055116.1. NM_014301.3. [Q9H1K1-2 ]
NP_998760.1. NM_213595.2. [Q9H1K1-1 ]
XP_006719378.1. XM_006719315.1. [Q9H1K1-2 ]
UniGenei Hs.615131.

3D structure databases

ProteinModelPortali Q9H1K1.
SMRi Q9H1K1. Positions 44-162.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 117038. 2 interactions.
IntActi Q9H1K1. 3 interactions.
MINTi MINT-3066312.
STRINGi 9606.ENSP00000310623.

PTM databases

PhosphoSitei Q9H1K1.

Polymorphism databases

DMDMi 313104118.

Proteomic databases

MaxQBi Q9H1K1.
PaxDbi Q9H1K1.
PRIDEi Q9H1K1.

Protocols and materials databases

DNASUi 23479.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000311893 ; ENSP00000310623 ; ENSG00000136003 . [Q9H1K1-1 ]
ENST00000392807 ; ENSP00000376554 ; ENSG00000136003 . [Q9H1K1-2 ]
GeneIDi 23479.
KEGGi hsa:23479.
UCSCi uc001tnc.4. human. [Q9H1K1-2 ]
uc010sxc.2. human. [Q9H1K1-1 ]

Organism-specific databases

CTDi 23479.
GeneCardsi GC12P108956.
GeneReviewsi ISCU.
HGNCi HGNC:29882. ISCU.
HPAi CAB006329.
HPA038602.
MIMi 255125. phenotype.
611911. gene.
neXtProti NX_Q9H1K1.
Orphaneti 43115. Hereditary myopathy with lactic acidosis due to ISCU deficiency.
PharmGKBi PA162392328.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0822.
HOGENOMi HOG000069228.
HOVERGENi HBG052621.
InParanoidi Q9H1K1.
OMAi RAGNDIC.
OrthoDBi EOG7JMGGC.
PhylomeDBi Q9H1K1.
TreeFami TF105422.

Enzyme and pathway databases

Reactomei REACT_150353. Mitochondrial iron-sulfur cluster biogenesis.

Miscellaneous databases

ChiTaRSi ISCU. human.
GeneWikii ISCU.
GenomeRNAii 23479.
NextBioi 45827.
PROi Q9H1K1.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q9H1K1.
Bgeei Q9H1K1.
CleanExi HS_ISCU.
Genevestigatori Q9H1K1.

Family and domain databases

InterProi IPR011339. ISC_FeS_clus_asmbl_IscU.
IPR002871. NIF_FeS_clus_asmbl_NifU_N.
[Graphical view ]
Pfami PF01592. NifU_N. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01999. iscU. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH NFS1, TISSUE SPECIFICITY, VARIANT VAL-12.
  2. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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 VAL-12.
    Tissue: Brain.
  4. "A modular domain of NifU, a nitrogen fixation cluster protein, is highly conserved in evolution."
    Hwang D.M., Dempsey A., Tan K.-T., Liew C.-C.
    J. Mol. Evol. 43:536-540(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 47-167, TISSUE SPECIFICITY.
    Tissue: Heart.
  5. "Splice mutation in the iron-sulfur cluster scaffold protein ISCU causes myopathy with exercise intolerance."
    Mochel F., Knight M.A., Tong W.-H., Hernandez D., Ayyad K., Taivassalo T., Andersen P.M., Singleton A., Rouault T.A., Fischbeck K.H., Haller R.G.
    Am. J. Hum. Genet. 82:652-660(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN MEIS.
  6. "Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis."
    Uhrigshardt H., Singh A., Kovtunovych G., Ghosh M., Rouault T.A.
    Hum. Mol. Genet. 19:3816-3834(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HSCB.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT [LARGE SCALE ANALYSIS] VAL-12, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.

Entry informationi

Entry nameiISCU_HUMAN
AccessioniPrimary (citable) accession number: Q9H1K1
Secondary accession number(s): Q6P713, Q99617, Q9H1K2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 30, 2010
Last modified: September 3, 2014
This is version 114 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 12
    Human chromosome 12: 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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