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Reviewed, UniProtKB/Swiss-Prot Q8IWL3 (HSC20_HUMAN)

Last modified February 9, 2010. Version 64. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Iron-sulfur cluster co-chaperone protein HscB, mitochondrial
Alternative name(s):
    DnaJ homolog subfamily C member 20
    Hsc20
Gene names
Name: HSCB
Synonyms: DNAJC20, HSC20
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

May act as a co-chaperone in iron-sulfur cluster assembly in mitochondria.

Pathway

Cofactor biosynthesis; iron-sulfur cluster biosynthesis.

Subcellular location

Mitochondrion Potential.

Tissue specificity

Liver, muscle and heart. Ref.1

Sequence similarities

Belongs to the hscB family.

Contains 1 J domain.

Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   LigandMetal-binding
   Molecular functionChaperone
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processprotein folding

Inferred from electronic annotation. Source: InterPro

   Cellular componentmitochondrion Ref.1

Inferred from expression pattern. Source: HGNC

   Molecular functionchaperone binding

Inferred from electronic annotation. Source: InterPro

heat shock protein binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2929Mitochondrion Potential
Chain30 – 235206Iron-sulfur cluster co-chaperone protein HscB, mitochondrial
PRO_0000007262

Regions

Domain72 – 14473J

Sites

Metal binding411Divalent metal cation
Metal binding441Divalent metal cation
Metal binding581Divalent metal cation
Metal binding611Divalent metal cation

Natural variations

Natural variant731Y → C: dbSNP rs17886090.
VAR_048916
Natural variant1631I → M: dbSNP rs17884212.
VAR_048917

Experimental info

Sequence conflict431N → S in AAN85282. Ref.1

Secondary structure

........................ 235
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q8IWL3-1 [UniParc].

Last modified March 1, 2005. Version 3.
Checksum: 70CF499E58FFD1C2

FASTA23527,422
        10         20         30         40         50         60 
MWRGRAGALL RVWGFWPTGV PRRRPLSCDA ASQAGSNYPR CWNCGGPWGP GREDRFFCPQ 

        70         80         90        100        110        120 
CRALQAPDPT RDYFSLMDCN RSFRVDTAKL QHRYQQLQRL VHPDFFSQRS QTEKDFSEKH 

       130        140        150        160        170        180 
STLVNDAYKT LLAPLSRGLY LLKLHGIEIP ERTDYEMDRQ FLIEIMEINE KLAEAESEAA 

       190        200        210        220        230 
MKEIESIVKA KQKEFTDNVS SAFEQDDFEE AKEILTKMRY FSNIEEKIKL KKIPL 

« Hide

References

« Hide 'large scale' references
[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: 12938016] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]"A genome annotation-driven approach to cloning the human ORFeome."
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., Beare D.M., Dunham I.
Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract]
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. expand/collapse author list , 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: 10591208] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Eye.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]"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: 18713742] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-235, METAL-BINDING SITES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
IPIIPI00217313.
RefSeqNP_741999.3.
UniGeneHs.632780

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3BVOX-ray3.00A/B30-235[»]
ModBaseSearch...

Protein-protein interaction databases

IntActQ8IWL3. 3 interactions.
STRINGQ8IWL3.

Proteomic databases

PRIDEQ8IWL3.

Genome annotation databases

EnsemblENST00000216027; ENSP00000216027; ENSG00000100209; Homo sapiens. [Genome view]
GeneID150274.
KEGGhsa:150274.
NMPDRfig|9606.3.peg.21472.
UCSCuc003aea.1. human.

Organism-specific databases

CTD150274.
GeneCardsGC22P027468.
HGNCHGNC:28913. HSCB.
HPAHPA018447.
MIM608142. gene.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG12582.
HOGENOMHBG751004.
HOVERGENQ8IWL3.
InParanoidQ8IWL3.
OMALMRRMQF.
OrthoDBEOG9N5ZGC.
PhylomeDBQ8IWL3.

Gene expression databases

ArrayExpressQ8IWL3.
BgeeQ8IWL3.
CleanExHS_HSCB.
GenevestigatorQ8IWL3.
GermOnlineENSG00000100209. Homo sapiens.

Family and domain databases

InterProIPR001623. DnaJ_N.
IPR009073. Heat_shock_cognate_B_oligo_C.
IPR004640. HscB.
[Graphical view]
Gene3DG3DSA:1.10.287.110. DnaJ_N. 1 hit.
G3DSA:1.20.1280.20. Heat_shock_cognate_B_oligo_C. 1 hit.
PfamPF00226. DnaJ. 1 hit.
PF07743. HSCB_C. 1 hit.
[Graphical view]
SMARTSM00271. DnaJ. 1 hit.
[Graphical view]
TIGRFAMsTIGR00714. hscB. 1 hit.
PROSITEPS00636. DNAJ_1. False negative.
PS50076. DNAJ_2. False negative.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio86381.
SOURCESearch...

Entry information

Entry nameHSC20_HUMAN
AccessionPrimary (citable) accession number: Q8IWL3
Secondary accession number(s): Q9BWS7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: March 1, 2005
Last modified: February 9, 2010
This is version 64 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents