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Q9H1K1 (ISCU_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 110. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Iron-sulfur cluster assembly enzyme ISCU, mitochondrial
Alternative name(s):
NifU-like N-terminal domain-containing protein
NifU-like protein
Gene names
Name:ISCU
Synonyms:NIFUN
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length167 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Binds NFS1. Interacts with HSCB. Ref.1 Ref.6

Subcellular location

Isoform 1: Mitochondrion Ref.1.

Isoform 2: Cytoplasm. Nucleus Ref.1.

Tissue specificity

Detected in heart, liver, skeletal muscle, brain, pancreas, kidney, lung and placenta. Ref.1 Ref.4

Involvement in disease

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. Ref.5

Sequence similarities

Belongs to the NifU family.

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9H1K1-1)

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.
Isoform 2 (identifier: Q9H1K1-2)

Also known as: ISCU1;

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 3434Mitochondrion Potential
Chain35 – 167133Iron-sulfur cluster assembly enzyme ISCU, mitochondrial
PRO_0000019692

Natural variations

Alternative sequence1 – 3838MAAAG…LYHKK → MVLIDMSVDLSTQ in isoform 2.
VSP_013492
Natural variant121A → V. Ref.1 Ref.3 Ref.8 Ref.9 Ref.10
Corresponds to variant rs2287555 [ dbSNP | Ensembl ].
VAR_060728

Experimental info

Sequence conflict71F → G in AAG37428. Ref.1
Sequence conflict71F → G in AAH11906. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (ISCU2) [UniParc].

Last modified November 30, 2010. Version 2.
Checksum: 0166D3EC9F1EEB47

FASTA16717,999
        10         20         30         40         50         60 
MAAAGAFRLR RAASALLLRS PRLPARELSA PARLYHKKVV DHYENPRNVG SLDKTSKNVG 

        70         80         90        100        110        120 
TGLVGAPACG DVMKLQIQVD EKGKIVDARF KTFGCGSAIA SSSLATEWVK GKTVEEALTI 

       130        140        150        160 
KNTDIAKELC LPPVKLHCSM LAEDAIKAAL ADYKLKQEPK KGEAEKK 

« Hide

Isoform 2 (ISCU1) [UniParc].

Checksum: EE72CEDC86CD6FF0
Show »

FASTA14215,263

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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].
[8]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_055116.1. NM_014301.3.
NP_998760.1. NM_213595.2.
UniGeneHs.615131.

3D structure databases

ProteinModelPortalQ9H1K1.
SMRQ9H1K1. Positions 44-162.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117038. 2 interactions.
IntActQ9H1K1. 3 interactions.
MINTMINT-3066312.
STRING9606.ENSP00000310623.

PTM databases

PhosphoSiteQ9H1K1.

Polymorphism databases

DMDM313104118.

Proteomic databases

PaxDbQ9H1K1.
PRIDEQ9H1K1.

Protocols and materials databases

DNASU23479.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000311893; ENSP00000310623; ENSG00000136003. [Q9H1K1-1]
ENST00000392807; ENSP00000376554; ENSG00000136003. [Q9H1K1-2]
GeneID23479.
KEGGhsa:23479.
UCSCuc001tnc.4. human. [Q9H1K1-2]
uc010sxc.2. human. [Q9H1K1-1]

Organism-specific databases

CTD23479.
GeneCardsGC12P108956.
HGNCHGNC:29882. ISCU.
HPACAB006329.
HPA038602.
MIM255125. phenotype.
611911. gene.
neXtProtNX_Q9H1K1.
Orphanet43115. Hereditary myopathy with lactic acidosis due to ISCU deficiency.
PharmGKBPA162392328.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0822.
HOGENOMHOG000069228.
HOVERGENHBG052621.
InParanoidQ9H1K1.
OMATSSMVTE.
OrthoDBEOG7JMGGC.
PhylomeDBQ9H1K1.
TreeFamTF105422.

Enzyme and pathway databases

ReactomeREACT_111217. Metabolism.

Gene expression databases

ArrayExpressQ9H1K1.
BgeeQ9H1K1.
CleanExHS_ISCU.
GenevestigatorQ9H1K1.

Family and domain databases

InterProIPR011339. ISC_FeS_clus_asmbl_IscU.
IPR002871. NIF_FeS_clus_asmbl_NifU_N.
[Graphical view]
PfamPF01592. NifU_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01999. iscU. 1 hit.
ProtoNetSearch...

Other

ChiTaRSISCU. human.
GeneWikiISCU.
GenomeRNAi23479.
NextBio45827.
PROQ9H1K1.
SOURCESearch...

Entry information

Entry nameISCU_HUMAN
AccessionPrimary (citable) accession number: Q9H1K1
Secondary accession number(s): Q6P713, Q99617, Q9H1K2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: November 30, 2010
Last modified: April 16, 2014
This is version 110 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM