Reviewed, UniProtKB/Swiss-Prot Q8IWL3 (HSC20_HUMAN)

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) [Complete proteome]

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	May act as a co-chaperone in iron-sulfur cluster assembly in mitochondria.
Pathway	Cofactor biosynthesis; iron-sulfur cluster biosynthesis.
Subcellular location	Mitochondrion Potential.
Tissue specificity	Liver, muscle and heart. Ref.1
Sequence similarities	Belongs to the hscB family. Contains 1 J domain.

Ontologies

Keywords
Cellular component	Mitochondrion
Coding sequence diversity	Polymorphism
Domain	Transit peptide
Ligand	Metal-binding
Molecular function	Chaperone
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	protein folding Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Ref.1 Inferred from expression pattern. Source: HGNC
Molecular function	chaperone binding Inferred from electronic annotation. Source: InterPro heat shock protein binding Inferred from electronic annotation. Source: InterPro
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: dbSNP rs17886090.

VAR_048916

Natural variant

163

1

I → M: dbSNP rs17884212.

VAR_048917

Experimental info

Sequence conflict

43

1

N → S in AAN85282. Ref.1

Secondary structure

1

.

.

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.

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.

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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)
	Q8IWL3-1 [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]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[6]	"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.

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.

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	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

Q8IWL3. 3 interactions.

STRING

Q8IWL3.

Proteomic databases

PRIDE

Q8IWL3.

Genome annotation databases

Ensembl

ENST00000216027; ENSP00000216027; ENSG00000100209; Homo sapiens. [Genome view]

GeneID

150274.

KEGG

hsa:150274.

NMPDR

fig|9606.3.peg.21472.

UCSC

uc003aea.1. human.

Organism-specific databases

CTD

150274.

GeneCards

GC22P027468.

HGNC

HGNC:28913. HSCB.

HPA

HPA018447.

MIM

608142. gene.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG12582.

HOGENOM

HBG751004.

HOVERGEN

Q8IWL3.

InParanoid

Q8IWL3.

OMA

LMRRMQF.

OrthoDB

EOG9N5ZGC.

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.

Pfam

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

SMART

SM00271. DnaJ. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00714. hscB. 1 hit.

PROSITE

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

ProtoNet

Search...

Other Resources

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:	February 9, 2010
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.