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Reviewed, UniProtKB/Swiss-Prot Q8IWL3 (HSC20_HUMAN)

Last modified June 16, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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

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Names and origin

Protein namesRecommended name:
    Co-chaperone protein HscB, mitochondrial
Alternative name(s):
    DnaJ homolog subfamily C member 20
      Short name=Hsc20
Gene names
Name: HSCB
Synonyms: DNAJC20, HSC20
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

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

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General annotation (Comments)

Function

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

Subcellular location

Mitochondrion Potential.

Tissue specificity

Liver, muscle and heart. Ref.1

Sequence similarities

Belongs to the hscB family.

Contains 1 J domain.

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Ontologies

Keywords
   Cellular componentMitochondrion
   Coding sequence diversityPolymorphism
   DomainTransit peptide
   Molecular functionChaperone
   Technical term3D-structure
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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 7171Mitochondrion Potential
Chain72 – 235164Co-chaperone protein HscB, mitochondrial
PRO_0000007262

Regions

Domain72 – 14473J

Natural variations

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

Experimental info

Sequence conflict431N → S Ref.1
Sequence conflict431N → S Ref.3

Secondary structure

1 ........................ 235
Helix Strand Turn

Details...

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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

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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:RESEARCH84.1-RESEARCH84.11(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 and Placenta.
[5]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

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Cross-references

Sequence databases

AY191719 mRNA. Translation: AAN85282.1.
CR456462 mRNA. Translation: CAG30348.1.
AL023494, AL117330 Genomic DNA. Translation: CAI20339.1.
AL117330, AL023494 Genomic DNA. Translation: CAH73876.1.
BC000004 mRNA. Translation: AAH00004.2.
BC065569 mRNA. Translation: AAH65569.1.
IPIIPI00217313.
RefSeqNP_741999.3.
UniGeneHs.291363
Hs.632780

3D structure databases

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

Protein-protein interaction databases

IntActQ8IWL3. 3 interactions.

Proteomic databases

PRIDEQ8IWL3.

Genome annotation databases

EnsemblENSG00000100209. Homo sapiens. [Contig view]
GeneID150274.
KEGGhsa:150274.
NMPDRfig|9606.3.peg.21472.

Organism-specific databases

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

Phylogenomic databases

HOGENOMQ8IWL3.
HOVERGENQ8IWL3.
OMAQ8IWL3. LMRRMQF.

Gene expression databases

ArrayExpressQ8IWL3.
BgeeQ8IWL3.
CleanExHS_HSCB.
GermOnlineENSG00000100209. Homo sapiens.

Family and domain databases

InterProIPR001623. DnaJ_N.
IPR009073. Heat_shock_cognate_B_oligo_C.
IPR018253. Heat_shock_DnaJ_CS.
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...

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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: June 16, 2009
This is version 55 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

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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

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