ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q8IWL3


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name HSC20_HUMAN
Primary accession number Q8IWL3
Secondary accession number Q9BWS7
Integrated into Swiss-Prot on March 29, 2004
Sequence was last modified on March 1, 2005 (Sequence version 3)
Annotations were last modified on    June 16, 2009 (Entry version 55)
Name and origin of the protein
Protein name Co-chaperone protein HscB, mitochondrial [Precursor]
Synonyms DnaJ homolog subfamily C member 20
Hsc20
Gene name
Name: HSCB
Synonyms: DNAJC20, HSC20
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
DOI=10.1007/s10038-003-0048-9; PubMed=12938016 [NCBI, ExPASy, EBI, Israel, Japan]
Sun G., Gargus J.J., Ta D.T., Vickery L.E.;
"Identification of a novel candidate gene in the iron-sulfur pathway implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-chaperone.";
J. Hum. Genet. 48:415-419(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1186/gb-2004-5-10-r84; PubMed=15461802 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/990031; PubMed=10591208 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Eye, and Placenta;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY.
Colinge J., Superti-Furga G., Bennett K.L.;
Submitted (OCT-2008) to UniProtKB.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AY191719; AAN85282.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456462; CAG30348.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL023494; CAI20339.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL117330; CAI20339.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL117330; CAH73876.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL023494; CAH73876.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000004; AAH00004.2; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC065569; AAH65569.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00217313; -.
RefSeq NP_741999.3; -.
UniGene Hs.291363
3D structure databases
PDB
3BVO; X-ray; 3.00 A; A/B=30-235.[ExPASy / RCSB / EBI]
PDBsum 3BVO; -.
ModBase Q8IWL3.
Protein-protein interaction databases
IntAct Q8IWL3; 3.
Organism-specific databases
GeneCards GC22P027468; -.
HGNC HGNC:28913; HSCB.
GenAtlas HSCB.
MIM 608142; gene. [NCBI / EBI]
Gene expression databases
ArrayExpress Q8IWL3; -.
Bgee Q8IWL3; -.
CleanEx HS_HSCB; -.
GermOnline ENSG00000100209; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from expression pattern from HGNC).
GO:0051087; Molecular function: chaperone binding (inferred from electronic annotation from InterPro).
GO:0031072; Molecular function: heat shock protein binding (inferred from electronic annotation from InterPro).
GO:0006457; Biological process: protein folding (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR001623; DnaJ_N.
IPR009073; Heat_shock_cognate_B_oligo_C.
IPR018253; Heat_shock_DnaJ_CS.
IPR004640; HscB.
Graphical view of domain structure.
Gene3D G3DSA:1.10.287.110; DnaJ_N; 1.
G3DSA:1.20.1280.20; Heat_shock_cognate_B_oligo_C; 1.
Pfam PF00226; DnaJ; 1.
PF07743; HSCB_C; 1.
Pfam graphical view of domain structure.
SMART SM00271; DnaJ; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00714; hscB; 1.
PROSITE PS00636; DNAJ_1; FALSE_NEG.
PS50076; DNAJ_2; FALSE_NEG.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q8IWL3; -.
Genome annotation databases
Ensembl ENSG00000100209; Homo sapiens. [Contig view]
GeneID 150274; -.
KEGG hsa:150274; -.
NMPDR fig|9606.3.peg.21472; -.
Phylogenomic databases
HOGENOM Q8IWL3; -.
HOVERGEN Q8IWL3; -.
OMA Q8IWL3; LMRRMQF.
Other
NextBio 86381; -.
SOURCE HSCB; Homo sapiens.
ProtoNet Q8IWL3.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Chaperone; Mitochondrion; Polymorphism; Transit peptide.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
TRANSIT   1    71  71     Mitochondrion (Potential). 
CHAIN   72   235  164     Co-chaperone protein HscB, mitochondrial. PRO_0000007262
DOMAIN   72   144  73     J. 
VARIANT   73    73  1     Y -> C (in dbSNP:rs17886090 [NCBI]). VAR_048916 
VARIANT   163   163  1     I -> M (in dbSNP:rs17884212 [NCBI]). VAR_048917 
CONFLICT   43    43        N -> S (in Ref. 1 and 3). 
STRAND   42    44  3      
TURN   59    61  3      
HELIX   73    76  4      
HELIX   87   101  15      
HELIX   103   106  4      
HELIX   111   132  22      
HELIX   134   144  11      
STRAND   154   157  4      
HELIX   159   174  16      
HELIX   178   204  27      
HELIX   208   231  24      
TURN   232   234  3      
Sequence information
Length: 235 AA [This is the length of the unprocessed precursor] Molecular weight: 27422 Da [This is the MW of the unprocessed precursor] CRC64: 70CF499E58FFD1C2 [This is a checksum on the sequence]
        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 

Q8IWL3 in FASTA format

View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!