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Protein

Iron-sulfur cluster co-chaperone protein HscB, mitochondrial

Gene

HSCB

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

Functioni

Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria.1 Publication

Pathwayi: iron-sulfur cluster biosynthesis

This protein is involved in the pathway iron-sulfur cluster biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway iron-sulfur cluster biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi41 – 411Divalent metal cation
Metal bindingi44 – 441Divalent metal cation
Metal bindingi58 – 581Divalent metal cation
Metal bindingi61 – 611Divalent metal cation

GO - Molecular functioni

GO - Biological processi

  • iron-sulfur cluster assembly Source: UniProtKB
  • protein folding Source: InterPro
  • protein oligomerization Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Ligandi

Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-1268020. Mitochondrial protein import.
UniPathwayiUPA00266.

Names & Taxonomyi

Protein namesi
Recommended name:
Iron-sulfur cluster co-chaperone protein HscB, mitochondrial
Alternative name(s):
DnaJ homolog subfamily C member 20
Hsc20
Gene namesi
Name:HSCB
Synonyms:DNAJC20, HSC20
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:28913. HSCB.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi41 – 411C → S: Does not alter subcellular localization; when associated with A-44, A-58 and A-61.
Mutagenesisi44 – 441C → S: Does not alter subcellular localization; when associated with A-41, A-58 and A-61.
Mutagenesisi58 – 581C → S: Does not alter subcellular localization; when associated with A-41, A-44 and A-61.
Mutagenesisi61 – 611C → S: Does not alter subcellular localization; when associated with A-41, A-44 and A-58.
Mutagenesisi102 – 1043HPD → AAA: Does not interact with HSPA9. Does not inhibit interaction with ISCU. 1 Publication

Organism-specific databases

PharmGKBiPA162391621.

Polymorphism and mutation databases

BioMutaiHSCB.
DMDMi60416441.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 2929MitochondrionSequence analysisAdd
BLAST
Chaini30 – 235206Iron-sulfur cluster co-chaperone protein HscB, mitochondrialPRO_0000007262Add
BLAST

Proteomic databases

EPDiQ8IWL3.
MaxQBiQ8IWL3.
PaxDbiQ8IWL3.
PRIDEiQ8IWL3.

PTM databases

iPTMnetiQ8IWL3.
PhosphoSiteiQ8IWL3.

Expressioni

Tissue specificityi

Expressed in lung, brain, stomach, spleen, ovary, testis, liver, muscle and heart.2 Publications

Gene expression databases

BgeeiQ8IWL3.
CleanExiHS_HSCB.
ExpressionAtlasiQ8IWL3. baseline and differential.
GenevisibleiQ8IWL3. HS.

Organism-specific databases

HPAiHPA018447.

Interactioni

Subunit structurei

Interacts with ISCU and HSPA9.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
AGTRAPQ6RW133EBI-1805738,EBI-741181

GO - Molecular functioni

Protein-protein interaction databases

BioGridi127276. 6 interactions.
IntActiQ8IWL3. 5 interactions.
STRINGi9606.ENSP00000216027.

Structurei

Secondary structure

1
235
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi42 – 443Combined sources
Turni59 – 613Combined sources
Helixi73 – 764Combined sources
Helixi87 – 10115Combined sources
Helixi103 – 1064Combined sources
Helixi111 – 13222Combined sources
Helixi134 – 14411Combined sources
Beta strandi154 – 1574Combined sources
Helixi159 – 17416Combined sources
Helixi178 – 20427Combined sources
Helixi208 – 23124Combined sources
Turni232 – 2343Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BVOX-ray3.00A/B30-235[»]
ProteinModelPortaliQ8IWL3.
SMRiQ8IWL3. Positions 39-235.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8IWL3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini72 – 14473JAdd
BLAST

Sequence similaritiesi

Belongs to the HscB family.Curated
Contains 1 J domain.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG3192. Eukaryota.
COG1076. LUCA.
GeneTreeiENSGT00390000008206.
HOGENOMiHOG000006786.
HOVERGENiHBG051931.
InParanoidiQ8IWL3.
KOiK04082.
OMAiFWPTGVP.
OrthoDBiEOG7B8S5Q.
PhylomeDBiQ8IWL3.
TreeFamiTF319992.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
1.20.1280.20. 1 hit.
HAMAPiMF_00682. HscB.
InterProiIPR001623. DnaJ_domain.
IPR004640. HscB.
IPR009073. HscB_oligo_C.
[Graphical view]
PANTHERiPTHR14021. PTHR14021. 1 hit.
PfamiPF07743. HSCB_C. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF47144. SSF47144. 1 hit.
TIGRFAMsiTIGR00714. hscB. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q8IWL3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MWRGRAGALL RVWGFWPTGV PRRRPLSCDA ASQAGSNYPR CWNCGGPWGP
60 70 80 90 100
GREDRFFCPQ CRALQAPDPT RDYFSLMDCN RSFRVDTAKL QHRYQQLQRL
110 120 130 140 150
VHPDFFSQRS QTEKDFSEKH STLVNDAYKT LLAPLSRGLY LLKLHGIEIP
160 170 180 190 200
ERTDYEMDRQ FLIEIMEINE KLAEAESEAA MKEIESIVKA KQKEFTDNVS
210 220 230
SAFEQDDFEE AKEILTKMRY FSNIEEKIKL KKIPL
Length:235
Mass (Da):27,422
Last modified:March 1, 2005 - v3
Checksum:i70CF499E58FFD1C2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti43 – 431N → S in AAN85282 (PubMed:12938016).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti73 – 731Y → C.
Corresponds to variant rs17886090 [ dbSNP | Ensembl ].
VAR_048916
Natural varianti163 – 1631I → M.
Corresponds to variant rs17884212 [ dbSNP | Ensembl ].
VAR_048917

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY191719 mRNA. Translation: AAN85282.1.
CR456462 mRNA. Translation: CAG30348.1.
AL023494, AL117330 Genomic DNA. Translation: CAI20339.1.
AL117330, AL023494 Genomic DNA. Translation: CAH73876.1.
BC065569 mRNA. Translation: AAH65569.1.
CCDSiCCDS13845.1.
RefSeqiNP_741999.3. NM_172002.4.
UniGeneiHs.632780.

Genome annotation databases

EnsembliENST00000216027; ENSP00000216027; ENSG00000100209.
GeneIDi150274.
KEGGihsa:150274.
UCSCiuc003aea.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY191719 mRNA. Translation: AAN85282.1.
CR456462 mRNA. Translation: CAG30348.1.
AL023494, AL117330 Genomic DNA. Translation: CAI20339.1.
AL117330, AL023494 Genomic DNA. Translation: CAH73876.1.
BC065569 mRNA. Translation: AAH65569.1.
CCDSiCCDS13845.1.
RefSeqiNP_741999.3. NM_172002.4.
UniGeneiHs.632780.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3BVOX-ray3.00A/B30-235[»]
ProteinModelPortaliQ8IWL3.
SMRiQ8IWL3. Positions 39-235.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi127276. 6 interactions.
IntActiQ8IWL3. 5 interactions.
STRINGi9606.ENSP00000216027.

PTM databases

iPTMnetiQ8IWL3.
PhosphoSiteiQ8IWL3.

Polymorphism and mutation databases

BioMutaiHSCB.
DMDMi60416441.

Proteomic databases

EPDiQ8IWL3.
MaxQBiQ8IWL3.
PaxDbiQ8IWL3.
PRIDEiQ8IWL3.

Protocols and materials databases

DNASUi150274.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000216027; ENSP00000216027; ENSG00000100209.
GeneIDi150274.
KEGGihsa:150274.
UCSCiuc003aea.4. human.

Organism-specific databases

CTDi150274.
GeneCardsiHSCB.
HGNCiHGNC:28913. HSCB.
HPAiHPA018447.
MIMi608142. gene.
neXtProtiNX_Q8IWL3.
PharmGKBiPA162391621.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3192. Eukaryota.
COG1076. LUCA.
GeneTreeiENSGT00390000008206.
HOGENOMiHOG000006786.
HOVERGENiHBG051931.
InParanoidiQ8IWL3.
KOiK04082.
OMAiFWPTGVP.
OrthoDBiEOG7B8S5Q.
PhylomeDBiQ8IWL3.
TreeFamiTF319992.

Enzyme and pathway databases

UniPathwayiUPA00266.
ReactomeiR-HSA-1268020. Mitochondrial protein import.

Miscellaneous databases

ChiTaRSiHSCB. human.
EvolutionaryTraceiQ8IWL3.
GenomeRNAii150274.
PROiQ8IWL3.
SOURCEiSearch...

Gene expression databases

BgeeiQ8IWL3.
CleanExiHS_HSCB.
ExpressionAtlasiQ8IWL3. baseline and differential.
GenevisibleiQ8IWL3. HS.

Family and domain databases

Gene3Di1.10.287.110. 1 hit.
1.20.1280.20. 1 hit.
HAMAPiMF_00682. HscB.
InterProiIPR001623. DnaJ_domain.
IPR004640. HscB.
IPR009073. HscB_oligo_C.
[Graphical view]
PANTHERiPTHR14021. PTHR14021. 1 hit.
PfamiPF07743. HSCB_C. 1 hit.
[Graphical view]
SUPFAMiSSF46565. SSF46565. 1 hit.
SSF47144. SSF47144. 1 hit.
TIGRFAMsiTIGR00714. hscB. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-chaperone."
    Sun G., Gargus J.J., Ta D.T., Vickery L.E.
    J. Hum. Genet. 48:415-419(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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].
    Tissue: Eye.
  5. "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: FUNCTION, INTERACTION WITH ISCU AND HSPA9, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 102-HIS--ASP-104.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-binding domain."
    Bitto E., Bingman C.A., Bittova L., Kondrashov D.A., Bannen R.M., Fox B.G., Markley J.L., Phillips G.N. Jr.
    J. Biol. Chem. 283:30184-30192(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-235, METAL-BINDING SITES.

Entry informationi

Entry nameiHSC20_HUMAN
AccessioniPrimary (citable) accession number: Q8IWL3
Secondary accession number(s): Q9BWS7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 1, 2005
Last modified: June 8, 2016
This is version 123 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 22
    Human chromosome 22: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. 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.