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Iron-sulfur cluster co-chaperone protein HscB, mitochondrial (DnaJ homolog subfamily C member 20) (Hsc20)

 HSC20_HUMAN             Reviewed;         235 AA.
Q8IWL3; Q9BWS7;
29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
01-MAR-2005, sequence version 3.
22-NOV-2017, entry version 134.
RecName: Full=Iron-sulfur cluster co-chaperone protein HscB, mitochondrial;
AltName: Full=DnaJ homolog subfamily C member 20;
AltName: Full=Hsc20;
Flags: Precursor;
Name=HSCB; Synonyms=DNAJC20, HSC20;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
PubMed=12938016; DOI=10.1007/s10038-003-0048-9;
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].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
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:R84.1-R84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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]
FUNCTION, INTERACTION WITH ISCU AND HSPA9, SUBCELLULAR LOCATION,
TISSUE SPECIFICITY, AND MUTAGENESIS OF 102-HIS--ASP-104.
PubMed=20668094; DOI=10.1093/hmg/ddq301;
Uhrigshardt H., Singh A., Kovtunovych G., Ghosh M., Rouault T.A.;
"Characterization of the human HSC20, an unusual DnaJ type III
protein, involved in iron-sulfur cluster biogenesis.";
Hum. Mol. Genet. 19:3816-3834(2010).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[7]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-235, AND METAL-BINDING
SITES.
PubMed=18713742; DOI=10.1074/jbc.M804746200;
Bitto E., Bingman C.A., Bittova L., Kondrashov D.A., Bannen R.M.,
Fox B.G., Markley J.L., Phillips G.N. Jr.;
"Structure of human J-type co-chaperone HscB reveals a tetracysteine
metal-binding domain.";
J. Biol. Chem. 283:30184-30192(2008).
-!- FUNCTION: Acts as a co-chaperone in iron-sulfur cluster assembly
in mitochondria. {ECO:0000269|PubMed:20668094}.
-!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
-!- SUBUNIT: Interacts with ISCU and HSPA9.
{ECO:0000269|PubMed:20668094}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1805738, EBI-1805738;
Q6RW13:AGTRAP; NbExp=3; IntAct=EBI-1805738, EBI-741181;
P07814:EPRS; NbExp=4; IntAct=EBI-1805738, EBI-355315;
P13804:ETFA; NbExp=3; IntAct=EBI-1805738, EBI-1052886;
Q86SX6:GLRX5; NbExp=3; IntAct=EBI-1805738, EBI-1049910;
P42694:HELZ; NbExp=4; IntAct=EBI-1805738, EBI-1210654;
P38646:HSPA9; NbExp=15; IntAct=EBI-1805738, EBI-354932;
Q5U5X0:LYRM7; NbExp=7; IntAct=EBI-1805738, EBI-13943106;
P19404:NDUFV2; NbExp=6; IntAct=EBI-1805738, EBI-713665;
P16083:NQO2; NbExp=4; IntAct=EBI-1805738, EBI-358466;
A6NFY7:SDHAF1; NbExp=5; IntAct=EBI-1805738, EBI-12011488;
P21912:SDHB; NbExp=21; IntAct=EBI-1805738, EBI-1056481;
Q96I99:SUCLG2; NbExp=4; IntAct=EBI-1805738, EBI-2511878;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:20668094}.
Mitochondrion {ECO:0000269|PubMed:20668094}.
-!- TISSUE SPECIFICITY: Expressed in lung, brain, stomach, spleen,
ovary, testis, liver, muscle and heart.
{ECO:0000269|PubMed:12938016, ECO:0000269|PubMed:20668094}.
-!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
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EMBL; AY191719; AAN85282.1; -; mRNA.
EMBL; CR456462; CAG30348.1; -; mRNA.
EMBL; AL023494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL117330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC065569; AAH65569.1; -; mRNA.
CCDS; CCDS13845.1; -.
RefSeq; NP_741999.3; NM_172002.4.
UniGene; Hs.632780; -.
PDB; 3BVO; X-ray; 3.00 A; A/B=30-235.
PDBsum; 3BVO; -.
ProteinModelPortal; Q8IWL3; -.
SMR; Q8IWL3; -.
BioGrid; 127276; 6.
DIP; DIP-46570N; -.
IntAct; Q8IWL3; 738.
STRING; 9606.ENSP00000216027; -.
iPTMnet; Q8IWL3; -.
PhosphoSitePlus; Q8IWL3; -.
BioMuta; HSCB; -.
DMDM; 60416441; -.
EPD; Q8IWL3; -.
MaxQB; Q8IWL3; -.
PaxDb; Q8IWL3; -.
PeptideAtlas; Q8IWL3; -.
PRIDE; Q8IWL3; -.
DNASU; 150274; -.
Ensembl; ENST00000216027; ENSP00000216027; ENSG00000100209.
GeneID; 150274; -.
KEGG; hsa:150274; -.
UCSC; uc003aea.4; human.
CTD; 150274; -.
EuPathDB; HostDB:ENSG00000100209.9; -.
GeneCards; HSCB; -.
HGNC; HGNC:28913; HSCB.
HPA; HPA018447; -.
HPA; HPA031518; -.
MIM; 608142; gene.
neXtProt; NX_Q8IWL3; -.
OpenTargets; ENSG00000100209; -.
PharmGKB; PA162391621; -.
eggNOG; KOG3192; Eukaryota.
eggNOG; COG1076; LUCA.
GeneTree; ENSGT00390000008206; -.
HOGENOM; HOG000006786; -.
HOVERGEN; HBG051931; -.
InParanoid; Q8IWL3; -.
KO; K04082; -.
OMA; LRVWGFW; -.
OrthoDB; EOG091G0O5A; -.
PhylomeDB; Q8IWL3; -.
TreeFam; TF319992; -.
Reactome; R-HSA-1268020; Mitochondrial protein import.
Reactome; R-HSA-1362409; Mitochondrial iron-sulfur cluster biogenesis.
UniPathway; UPA00266; -.
ChiTaRS; HSCB; human.
EvolutionaryTrace; Q8IWL3; -.
GenomeRNAi; 150274; -.
PRO; PR:Q8IWL3; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100209; -.
CleanEx; HS_HSCB; -.
ExpressionAtlas; Q8IWL3; baseline and differential.
Genevisible; Q8IWL3; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:HPA.
GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
GO; GO:0051087; F:chaperone binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
GO; GO:0097428; P:protein maturation by iron-sulfur cluster transfer; IEA:InterPro.
GO; GO:0051259; P:protein oligomerization; IEA:InterPro.
CDD; cd06257; DnaJ; 1.
Gene3D; 1.10.287.110; -; 1.
Gene3D; 1.20.1280.20; -; 1.
HAMAP; MF_00682; HscB; 1.
InterPro; IPR036869; DnaJ_dom_sf.
InterPro; IPR001623; DnaJ_domain.
InterPro; IPR004640; HscB.
InterPro; IPR036386; HscB_C_sf.
InterPro; IPR009073; HscB_oligo_C.
PANTHER; PTHR14021; PTHR14021; 1.
Pfam; PF07743; HSCB_C; 1.
SUPFAM; SSF46565; SSF46565; 1.
SUPFAM; SSF47144; SSF47144; 1.
TIGRFAMs; TIGR00714; hscB; 1.
1: Evidence at protein level;
3D-structure; Chaperone; Complete proteome; Cytoplasm; Metal-binding;
Mitochondrion; Polymorphism; Reference proteome; Transit peptide.
TRANSIT 1 29 Mitochondrion. {ECO:0000255}.
CHAIN 30 235 Iron-sulfur cluster co-chaperone protein
HscB, mitochondrial.
/FTId=PRO_0000007262.
DOMAIN 72 144 J.
METAL 41 41 Divalent metal cation.
METAL 44 44 Divalent metal cation.
METAL 58 58 Divalent metal cation.
METAL 61 61 Divalent metal cation.
VARIANT 73 73 Y -> C (in dbSNP:rs17886090).
/FTId=VAR_048916.
VARIANT 163 163 I -> M (in dbSNP:rs17884212).
/FTId=VAR_048917.
MUTAGEN 41 41 C->S: Does not alter subcellular
localization; when associated with A-44,
A-58 and A-61.
MUTAGEN 44 44 C->S: Does not alter subcellular
localization; when associated with A-41,
A-58 and A-61.
MUTAGEN 58 58 C->S: Does not alter subcellular
localization; when associated with A-41,
A-44 and A-61.
MUTAGEN 61 61 C->S: Does not alter subcellular
localization; when associated with A-41,
A-44 and A-58.
MUTAGEN 102 104 HPD->AAA: Does not interact with HSPA9.
Does not inhibit interaction with ISCU.
{ECO:0000269|PubMed:20668094}.
CONFLICT 43 43 N -> S (in Ref. 1; AAN85282).
{ECO:0000305}.
STRAND 42 44 {ECO:0000244|PDB:3BVO}.
TURN 59 61 {ECO:0000244|PDB:3BVO}.
HELIX 73 76 {ECO:0000244|PDB:3BVO}.
HELIX 87 101 {ECO:0000244|PDB:3BVO}.
HELIX 103 106 {ECO:0000244|PDB:3BVO}.
HELIX 111 132 {ECO:0000244|PDB:3BVO}.
HELIX 134 144 {ECO:0000244|PDB:3BVO}.
STRAND 154 157 {ECO:0000244|PDB:3BVO}.
HELIX 159 174 {ECO:0000244|PDB:3BVO}.
HELIX 178 204 {ECO:0000244|PDB:3BVO}.
HELIX 208 231 {ECO:0000244|PDB:3BVO}.
TURN 232 234 {ECO:0000244|PDB:3BVO}.
SEQUENCE 235 AA; 27422 MW; 70CF499E58FFD1C2 CRC64;
MWRGRAGALL RVWGFWPTGV PRRRPLSCDA ASQAGSNYPR CWNCGGPWGP GREDRFFCPQ
CRALQAPDPT RDYFSLMDCN RSFRVDTAKL QHRYQQLQRL VHPDFFSQRS QTEKDFSEKH
STLVNDAYKT LLAPLSRGLY LLKLHGIEIP ERTDYEMDRQ FLIEIMEINE KLAEAESEAA
MKEIESIVKA KQKEFTDNVS SAFEQDDFEE AKEILTKMRY FSNIEEKIKL KKIPL


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