Q8IWL3 (HSC20_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	235 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria. Ref.5
Pathway	Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subunit structure	Interacts with ISCU and HSPA9. Ref.5
Subcellular location	Cytoplasm. Mitochondrion Ref.5.
Tissue specificity	Expressed in lung, brain, stomach, spleen, ovary, testis, liver, muscle and heart. Ref.1 Ref.5
Sequence similarities	Belongs to the hscB family. Contains 1 J domain.

Ontologies

Keywords
Cellular component	Cytoplasm Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Metal-binding
Molecular function	Chaperone
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	iron-sulfur cluster assembly Inferred from mutant phenotype Ref.5. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from direct assay Ref.5. Source: UniProtKB
Molecular function	chaperone binding Inferred from electronic annotation. Source: InterPro heat shock protein binding Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Transit peptide

1 – 29

29

Mitochondrion Potential

Chain

30 – 235

206

Iron-sulfur cluster co-chaperone protein HscB, mitochondrial

PRO_0000007262

Regions

Domain

72 – 144

73

J

Sites

Metal binding

41

1

Divalent metal cation

Metal binding

44

1

Divalent metal cation

Metal binding

58

1

Divalent metal cation

Metal binding

61

1

Divalent metal cation

Natural variations

Natural variant

73

1

Y → C.
Corresponds to variant rs17886090 [ dbSNP | Ensembl ].

VAR_048916

Natural variant

163

1

I → M.
Corresponds to variant rs17884212 [ dbSNP | Ensembl ].

VAR_048917

Experimental info

Mutagenesis

41

1

C → S: Does not alter subcellular localization; when associated with A-44, A-58 and A-61.

Mutagenesis

44

1

C → S: Does not alter subcellular localization; when associated with A-41, A-58 and A-61.

Mutagenesis

58

1

C → S: Does not alter subcellular localization; when associated with A-41, A-44 and A-61.

Mutagenesis

61

1

C → S: Does not alter subcellular localization; when associated with A-41, A-44 and A-58.

Mutagenesis

102 – 104

3

HPD → AAA: Does not interact with HSPA9. Does not inhibit interaction with ISCU. Ref.5

Sequence conflict

43

1

N → S in AAN85282. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

235

Helix Strand Turn

Details...

Beta 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

Beta strand

154 – 157

4

Helix

159 – 174

16

Helix

178 – 204

27

Helix

208 – 231

24

Turn

232 – 234

3

Sequences

	Sequence		Length	Mass (Da)
	Q8IWL3 [UniParc]. Last modified March 1, 2005. Version 3. Checksum: 70CF499E58FFD1C2	FASTA	235	27,422
	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

References

	« Hide 'large scale' referencesShow '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. , 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]	"Characterization of the human HSC20, an unusual DnaJ type III protein, involved in iron-sulfur cluster biogenesis." Uhrigshardt H., Singh A., Kovtunovych G., Ghosh M., Rouault T.A. Hum. Mol. Genet. 19:3816-3834(2010) [PubMed: 20668094] [Abstract] Cited for: FUNCTION, INTERACTION WITH ISCU AND HSPA9, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF 102-HIS--ASP-104.
[6]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[7]	"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.
+	Additional computationally mapped references.

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.

IPI

IPI00217313.

RefSeq

NP_741999.3. NM_172002.3.

UniGene

Hs.632780.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3BVO	X-ray	3.00	A/B	30-235	[»]

ProteinModelPortal

Q8IWL3.

SMR

Q8IWL3. Positions 39-235.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8IWL3. 3 interactions.

STRING

Q8IWL3.

Polymorphism databases

DMDM

60416441.

Proteomic databases

PRIDE

Q8IWL3.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000216027; ENSP00000216027; ENSG00000100209.

GeneID

150274.

KEGG

hsa:150274.

NMPDR

fig|9606.3.peg.21472.

UCSC

uc003aea.1. human.

Organism-specific databases

CTD

150274.

GeneCards

GC22P029138.

H-InvDB

HIX0016342.

HGNC

HGNC:28913. HSCB.

HPA

HPA018447.

MIM

608142. gene.

neXtProt

NX_Q8IWL3.

PharmGKB

PA162391621.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12582.

GeneTree

ENSGT00390000008206.

HOGENOM

HBG751004.

HOVERGEN

HBG051931.

InParanoid

Q8IWL3.

OMA

LNDAYQT.

OrthoDB

EOG4894NF.

PhylomeDB

Q8IWL3.

Gene expression databases

ArrayExpress

Q8IWL3.

Bgee

Q8IWL3.

CleanEx

HS_HSCB.

Genevestigator

Q8IWL3.

GermOnline

ENSG00000100209. Homo sapiens.

Family and domain databases

InterPro

IPR001623. DnaJ_N.
IPR009073. Heat_shock_cognate_B_oligo_C.
IPR004640. HscB.
[Graphical view]

Gene3D

G3DSA:1.10.287.110. DnaJ_N. 1 hit.
G3DSA:1.20.1280.20. Heat_shock_cognate_B_oligo_C. 1 hit.

KO

K04082.

PANTHER

PTHR14021. PTHR14021. 1 hit.

Pfam

PF00226. DnaJ. 1 hit.
PF07743. HSCB_C. 1 hit.
[Graphical view]

SMART

SM00271. DnaJ. 1 hit.
[Graphical view]

SUPFAM

SSF46565. DnaJ_N. 1 hit.
SSF47144. HSC20_C. 1 hit.

TIGRFAMs

TIGR00714. HscB. 1 hit.

PROSITE

PS00636. DNAJ_1. False negative.
PS50076. DNAJ_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

NextBio

86381.

SOURCE

Search...

Entry information

Entry name

HSC20_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 82 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.