ID HSC20_HUMAN Reviewed; 235 AA.
AC Q8IWL3; Q9BWS7;
DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 3.
DT 27-MAR-2024, entry version 168.
DE RecName: Full=Iron-sulfur cluster co-chaperone protein HscB {ECO:0000305};
DE AltName: Full=DnaJ homolog subfamily C member 20;
DE Contains:
DE RecName: Full=Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic;
DE Short=C-HSC20 {ECO:0000303|PubMed:29309586};
DE Contains:
DE RecName: Full=Iron-sulfur cluster co-chaperone protein HscB, mitochondrial;
GN Name=HSCB {ECO:0000312|HGNC:HGNC:28913}; Synonyms=DNAJC20, HSC20;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RX PubMed=12938016; DOI=10.1007/s10038-003-0048-9;
RA Sun G., Gargus J.J., Ta D.T., Vickery L.E.;
RT "Identification of a novel candidate gene in the iron-sulfur pathway
RT implicated in ataxia-susceptibility: human gene encoding HscB, a J-type co-
RT chaperone.";
RL J. Hum. Genet. 48:415-419(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, INTERACTION WITH ISCU AND HSPA9, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF CYS-41; CYS-44; CYS-58; CYS-61 AND
RP 102-HIS--ASP-104.
RX PubMed=20668094; DOI=10.1093/hmg/ddq301;
RA Uhrigshardt H., Singh A., Kovtunovych G., Ghosh M., Rouault T.A.;
RT "Characterization of the human HSC20, an unusual DnaJ type III protein,
RT involved in iron-sulfur cluster biogenesis.";
RL Hum. Mol. Genet. 19:3816-3834(2010).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP FUNCTION, AND INTERACTION WITH SDHAF1.
RX PubMed=26749241; DOI=10.1016/j.cmet.2015.12.005;
RA Maio N., Ghezzi D., Verrigni D., Rizza T., Bertini E., Martinelli D.,
RA Zeviani M., Singh A., Carrozzo R., Rouault T.A.;
RT "Disease-causing SDHAF1 mutations impair transfer of Fe-S clusters to
RT SDHB.";
RL Cell Metab. 23:292-302(2016).
RN [8]
RP FUNCTION, SUBUNIT, INTERACTION WITH CIAO1 AND ISCU, SUBCELLULAR LOCATION,
RP MUTAGENESIS OF CYS-41; CYS-44; CYS-58 AND CYS-61, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=29309586; DOI=10.1093/hmg/ddy004;
RA Kim K.S., Maio N., Singh A., Rouault T.A.;
RT "Cytosolic HSC20 integrates de novo iron-sulfur cluster biogenesis with the
RT CIAO1-mediated transfer to recipients.";
RL Hum. Mol. Genet. 27:837-852(2018).
RN [9]
RP INVOLVEMENT IN SIDBA5.
RX PubMed=32634119; DOI=10.1172/jci135479;
RA Crispin A., Guo C., Chen C., Campagna D.R., Schmidt P.J., Lichtenstein D.,
RA Cao C., Sendamarai A.K., Hildick-Smith G.J., Huston N.C., Boudreaux J.,
RA Bottomley S.S., Heeney M.M., Paw B.H., Fleming M.D., Ducamp S.;
RT "Mutations in the iron-sulfur cluster biogenesis protein HSCB cause
RT congenital sideroblastic anemia.";
RL J. Clin. Invest. 130:5245-5256(2020).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 30-235, AND METAL-BINDING SITES.
RX PubMed=18713742; DOI=10.1074/jbc.m804746200;
RA Bitto E., Bingman C.A., Bittova L., Kondrashov D.A., Bannen R.M., Fox B.G.,
RA Markley J.L., Phillips G.N. Jr.;
RT "Structure of human J-type co-chaperone HscB reveals a tetracysteine metal-
RT binding domain.";
RL J. Biol. Chem. 283:30184-30192(2008).
CC -!- FUNCTION: [Iron-sulfur cluster co-chaperone protein HscB,
CC mitochondrial]: Acts as a co-chaperone in iron-sulfur cluster assembly
CC in mitochondria (PubMed:20668094). Required for incorporation of iron-
CC sulfur clusters into SDHB, the iron-sulfur protein subunit of succinate
CC dehydrogenase that is involved in complex II of the mitochondrial
CC electron transport chain (PubMed:26749241). Recruited to SDHB by
CC interaction with SDHAF1 which first binds SDHB and then recruits the
CC iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through
CC direct binding to HSC20 (PubMed:26749241). Plays an essential role in
CC hematopoiesis (By similarity). {ECO:0000250|UniProtKB:Q8K3A0,
CC ECO:0000269|PubMed:20668094, ECO:0000269|PubMed:26749241}.
CC -!- FUNCTION: [Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]:
CC Acts as a co-chaperone in iron-sulfur cluster assembly in the cytoplasm
CC (PubMed:29309586). Also mediates complex formation between components
CC of the cytosolic iron-sulfur biogenesis pathway and the CIA targeting
CC complex composed of CIAO1, DIPK1B/FAM69B and MMS19 by binding directly
CC to the scaffold protein ISCU and to CIAO1 (PubMed:29309586). This
CC facilitates iron-sulfur cluster insertion into a number of cytoplasmic
CC and nuclear proteins including POLD1, ELP3, DPYD and PPAT
CC (PubMed:29309586). {ECO:0000269|PubMed:29309586}.
CC -!- PATHWAY: Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
CC -!- SUBUNIT: [Iron-sulfur cluster co-chaperone protein HscB,
CC mitochondrial]: Interacts with ISCU and HSPA9 to form an iron-sulfur
CC transfer complex (PubMed:20668094). Interacts with SDHAF1 (via the
CC first LYR motif); the interaction recruits the iron-sulfur transfer
CC complex composed of HSC20, HSPA9 and ISCU and mediates the
CC incorporation of iron-sulfur clusters into SDHB which also interacts
CC with HSC20 (PubMed:26749241). Interacts with the cytoplasmic form of
CC ISCU and with CIA complex member CIAO1 (via LYR motif)
CC (PubMed:29309586). {ECO:0000269|PubMed:20668094,
CC ECO:0000269|PubMed:26749241}.
CC -!- SUBUNIT: [Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic]:
CC Homodimer (PubMed:29309586). Interacts with ISCU (cytoplasmic form);
CC this interaction stabilzes the (Fe-S) clusters on ISCU
CC (PubMed:29309586). Interacts with the CIA complex member CIAO1 (via LYR
CC motif) (PubMed:29309586). {ECO:0000269|PubMed:29309586}.
CC -!- INTERACTION:
CC Q8IWL3; Q6RW13: AGTRAP; NbExp=4; IntAct=EBI-1805738, EBI-741181;
CC Q8IWL3; P07814: EPRS1; NbExp=4; IntAct=EBI-1805738, EBI-355315;
CC Q8IWL3; P13804: ETFA; NbExp=3; IntAct=EBI-1805738, EBI-1052886;
CC Q8IWL3; Q86SX6: GLRX5; NbExp=3; IntAct=EBI-1805738, EBI-1049910;
CC Q8IWL3; P42694: HELZ; NbExp=4; IntAct=EBI-1805738, EBI-1210654;
CC Q8IWL3; Q8IWL3: HSCB; NbExp=3; IntAct=EBI-1805738, EBI-1805738;
CC Q8IWL3; P38646: HSPA9; NbExp=14; IntAct=EBI-1805738, EBI-354932;
CC Q8IWL3; Q5U5X0: LYRM7; NbExp=7; IntAct=EBI-1805738, EBI-13943106;
CC Q8IWL3; P19404: NDUFV2; NbExp=6; IntAct=EBI-1805738, EBI-713665;
CC Q8IWL3; P16083: NQO2; NbExp=4; IntAct=EBI-1805738, EBI-358466;
CC Q8IWL3; A6NFY7: SDHAF1; NbExp=5; IntAct=EBI-1805738, EBI-12011488;
CC Q8IWL3; P21912: SDHB; NbExp=22; IntAct=EBI-1805738, EBI-1056481;
CC Q8IWL3; Q96I99: SUCLG2; NbExp=4; IntAct=EBI-1805738, EBI-2511878;
CC -!- SUBCELLULAR LOCATION: [Iron-sulfur cluster co-chaperone protein HscB,
CC cytoplasmic]: Cytoplasm {ECO:0000269|PubMed:20668094,
CC ECO:0000269|PubMed:29309586}.
CC -!- SUBCELLULAR LOCATION: [Iron-sulfur cluster co-chaperone protein HscB,
CC mitochondrial]: Mitochondrion {ECO:0000269|PubMed:20668094}.
CC -!- TISSUE SPECIFICITY: Expressed in lung, brain, stomach, spleen, ovary,
CC testis, liver, muscle and heart. {ECO:0000269|PubMed:12938016,
CC ECO:0000269|PubMed:20668094}.
CC -!- DISEASE: Anemia, sideroblastic, 5 (SIDBA5) [MIM:619523]: A form of
CC sideroblastic anemia, a bone marrow disorder defined by the presence of
CC pathologic iron deposits in erythroblast mitochondria. Sideroblastic
CC anemia is characterized by anemia of varying severity, hypochromic
CC peripheral erythrocytes, systemic iron overload secondary to chronic
CC ineffective erythropoiesis, and the presence of bone marrow ringed
CC sideroblasts. Sideroblasts are characterized by iron-loaded
CC mitochondria clustered around the nucleus. SIDBA5 inheritance is
CC autosomal recessive. {ECO:0000269|PubMed:32634119}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the HscB family. {ECO:0000305}.
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DR EMBL; AY191719; AAN85282.1; -; mRNA.
DR EMBL; CR456462; CAG30348.1; -; mRNA.
DR EMBL; AL023494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL117330; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC065569; AAH65569.1; -; mRNA.
DR CCDS; CCDS13845.1; -.
DR RefSeq; NP_741999.3; NM_172002.4.
DR PDB; 3BVO; X-ray; 3.00 A; A/B=30-235.
DR PDBsum; 3BVO; -.
DR AlphaFoldDB; Q8IWL3; -.
DR SASBDB; Q8IWL3; -.
DR SMR; Q8IWL3; -.
DR BioGRID; 127276; 818.
DR DIP; DIP-46570N; -.
DR IntAct; Q8IWL3; 736.
DR STRING; 9606.ENSP00000216027; -.
DR iPTMnet; Q8IWL3; -.
DR PhosphoSitePlus; Q8IWL3; -.
DR BioMuta; HSCB; -.
DR DMDM; 60416441; -.
DR EPD; Q8IWL3; -.
DR jPOST; Q8IWL3; -.
DR MassIVE; Q8IWL3; -.
DR MaxQB; Q8IWL3; -.
DR PaxDb; 9606-ENSP00000216027; -.
DR PeptideAtlas; Q8IWL3; -.
DR ProteomicsDB; 70870; -.
DR Pumba; Q8IWL3; -.
DR Antibodypedia; 10209; 175 antibodies from 21 providers.
DR DNASU; 150274; -.
DR Ensembl; ENST00000216027.8; ENSP00000216027.3; ENSG00000100209.11.
DR GeneID; 150274; -.
DR KEGG; hsa:150274; -.
DR MANE-Select; ENST00000216027.8; ENSP00000216027.3; NM_172002.5; NP_741999.3.
DR UCSC; uc003aea.4; human.
DR AGR; HGNC:28913; -.
DR CTD; 150274; -.
DR DisGeNET; 150274; -.
DR GeneCards; HSCB; -.
DR HGNC; HGNC:28913; HSCB.
DR HPA; ENSG00000100209; Low tissue specificity.
DR MalaCards; HSCB; -.
DR MIM; 608142; gene.
DR MIM; 619523; phenotype.
DR neXtProt; NX_Q8IWL3; -.
DR OpenTargets; ENSG00000100209; -.
DR PharmGKB; PA162391621; -.
DR VEuPathDB; HostDB:ENSG00000100209; -.
DR eggNOG; KOG3192; Eukaryota.
DR GeneTree; ENSGT00390000008206; -.
DR HOGENOM; CLU_068529_0_2_1; -.
DR InParanoid; Q8IWL3; -.
DR OMA; LMFIERF; -.
DR OrthoDB; 5473494at2759; -.
DR PhylomeDB; Q8IWL3; -.
DR TreeFam; TF319992; -.
DR PathwayCommons; Q8IWL3; -.
DR Reactome; R-HSA-1268020; Mitochondrial protein import.
DR Reactome; R-HSA-1362409; Mitochondrial iron-sulfur cluster biogenesis.
DR SignaLink; Q8IWL3; -.
DR SIGNOR; Q8IWL3; -.
DR UniPathway; UPA00266; -.
DR BioGRID-ORCS; 150274; 602 hits in 1177 CRISPR screens.
DR ChiTaRS; HSCB; human.
DR EvolutionaryTrace; Q8IWL3; -.
DR GenomeRNAi; 150274; -.
DR Pharos; Q8IWL3; Tbio.
DR PRO; PR:Q8IWL3; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q8IWL3; Protein.
DR Bgee; ENSG00000100209; Expressed in parotid gland and 187 other cell types or tissues.
DR ExpressionAtlas; Q8IWL3; baseline and differential.
DR Genevisible; Q8IWL3; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001671; F:ATPase activator activity; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0051087; F:protein-folding chaperone binding; IEA:InterPro.
DR GO; GO:0044571; P:[2Fe-2S] cluster assembly; IBA:GO_Central.
DR GO; GO:0016226; P:iron-sulfur cluster assembly; IMP:UniProtKB.
DR GO; GO:0060319; P:primitive erythrocyte differentiation; ISS:UniProtKB.
DR GO; GO:0060215; P:primitive hemopoiesis; ISS:UniProtKB.
DR GO; GO:0051259; P:protein complex oligomerization; IEA:InterPro.
DR Gene3D; 1.10.287.110; DnaJ domain; 1.
DR Gene3D; 1.20.1280.20; HscB, C-terminal domain; 1.
DR HAMAP; MF_00682; HscB; 1.
DR InterPro; IPR004640; HscB.
DR InterPro; IPR040682; HscB_4_cys.
DR InterPro; IPR036386; HscB_C_sf.
DR InterPro; IPR009073; HscB_oligo_C.
DR InterPro; IPR036869; J_dom_sf.
DR NCBIfam; TIGR00714; hscB; 1.
DR PANTHER; PTHR14021; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR PANTHER; PTHR14021:SF15; IRON-SULFUR CLUSTER CO-CHAPERONE PROTEIN HSCB; 1.
DR Pfam; PF18256; HscB_4_cys; 1.
DR Pfam; PF07743; HSCB_C; 1.
DR SUPFAM; SSF46565; Chaperone J-domain; 1.
DR SUPFAM; SSF47144; HSC20 (HSCB), C-terminal oligomerisation domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chaperone; Cytoplasm; Metal-binding; Mitochondrion;
KW Reference proteome.
FT CHAIN 1..235
FT /note="Iron-sulfur cluster co-chaperone protein HscB,
FT cytoplasmic"
FT /evidence="ECO:0000305|PubMed:29309586"
FT /id="PRO_0000446242"
FT CHAIN 30..235
FT /note="Iron-sulfur cluster co-chaperone protein HscB,
FT mitochondrial"
FT /evidence="ECO:0000255"
FT /id="PRO_0000007262"
FT DOMAIN 72..144
FT /note="J"
FT BINDING 41
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:18713742,
FT ECO:0007744|PDB:3BVO"
FT BINDING 44
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:18713742,
FT ECO:0007744|PDB:3BVO"
FT BINDING 58
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:18713742,
FT ECO:0007744|PDB:3BVO"
FT BINDING 61
FT /ligand="a divalent metal cation"
FT /ligand_id="ChEBI:CHEBI:60240"
FT /evidence="ECO:0000269|PubMed:18713742,
FT ECO:0007744|PDB:3BVO"
FT VARIANT 73
FT /note="Y -> C (in dbSNP:rs17886090)"
FT /id="VAR_048916"
FT VARIANT 163
FT /note="I -> M (in dbSNP:rs17884212)"
FT /id="VAR_048917"
FT MUTAGEN 41
FT /note="C->S: Abolishes self-interaction and interaction
FT with HSPA9 and the CIA complex but does not alter
FT subcellular localization; when associated with S-44; S-58
FT and S-61."
FT /evidence="ECO:0000269|PubMed:20668094,
FT ECO:0000269|PubMed:29309586"
FT MUTAGEN 44
FT /note="C->S: Abolishes self-interaction and interaction
FT with HSPA9 and the CIA complex but does not alter
FT subcellular localization; when associated with S-41; S-58
FT and S-61."
FT /evidence="ECO:0000269|PubMed:20668094,
FT ECO:0000269|PubMed:29309586"
FT MUTAGEN 58
FT /note="C->S: Abolishes self-interaction and interaction
FT with HSPA9 and the CIA complex but does not alter
FT subcellular localization; when associated with S-41; S-44
FT and S-61."
FT /evidence="ECO:0000269|PubMed:20668094,
FT ECO:0000269|PubMed:29309586"
FT MUTAGEN 61
FT /note="C->S: Abolishes self-interaction and interaction
FT with HSPA9 and the CIA complex but does not alter
FT subcellular localization; when associated with S-41; S-44
FT and S-58."
FT /evidence="ECO:0000269|PubMed:20668094,
FT ECO:0000269|PubMed:29309586"
FT MUTAGEN 102..104
FT /note="HPD->AAA: Does not interact with HSPA9. Does not
FT inhibit interaction with ISCU."
FT /evidence="ECO:0000269|PubMed:20668094"
FT CONFLICT 43
FT /note="N -> S (in Ref. 1; AAN85282)"
FT /evidence="ECO:0000305"
FT STRAND 42..44
FT /evidence="ECO:0007829|PDB:3BVO"
FT TURN 59..61
FT /evidence="ECO:0007829|PDB:3BVO"
FT HELIX 73..76
FT /evidence="ECO:0007829|PDB:3BVO"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:3BVO"
FT HELIX 103..106
FT /evidence="ECO:0007829|PDB:3BVO"
FT HELIX 111..132
FT /evidence="ECO:0007829|PDB:3BVO"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:3BVO"
FT STRAND 154..157
FT /evidence="ECO:0007829|PDB:3BVO"
FT HELIX 159..174
FT /evidence="ECO:0007829|PDB:3BVO"
FT HELIX 178..204
FT /evidence="ECO:0007829|PDB:3BVO"
FT HELIX 208..231
FT /evidence="ECO:0007829|PDB:3BVO"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3BVO"
SQ 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
//
