Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Y276 (BCS1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 118. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Mitochondrial chaperone BCS1

Short name=h-BCS1
Alternative name(s):
BCS1-like protein
Gene names
Name:BCS1L
Synonyms:BCS1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length419 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Chaperone necessary for the assembly of mitochondrial respiratory chain complex III. Plays an important role in the maintenance of mitochondrial tubular networks, respiratory chain assembly and formation of the LETM1 complex. Ref.9

Subunit structure

Interacts with LETM1. Ref.9

Subcellular location

Mitochondrion inner membrane; Single-pass membrane protein Ref.1 Ref.9.

Tissue specificity

Ubiquitous. Ref.1

Involvement in disease

GRACILE syndrome (GRACILE) [MIM:603358]: GRACILE stands for 'growth retardation, aminoaciduria, cholestasis, iron overload, lactic acidosis, and early death'. It is a recessively inherited lethal disease characterized by fetal growth retardation, lactic acidosis, aminoaciduria, cholestasis, and abnormalities in iron metabolism.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.3 Ref.13

Mitochondrial complex III deficiency, nuclear 1 (MC3DN1) [MIM:124000]: A disorder of the mitochondrial respiratory chain resulting in a highly variable phenotype depending on which tissues are affected. Clinical features include mitochondrial encephalopathy, psychomotor retardation, ataxia, severe failure to thrive, liver dysfunction, renal tubulopathy, muscle weakness and exercise intolerance.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.2 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14

Bjoernstad syndrome (BJS) [MIM:262000]: An autosomal recessive disease characterized by congenital sensorineural hearing loss and twisted hairs (pili torti). Pili torti is a condition in which the hair shafts are flattened at irregular intervals and twisted 180 degrees from the normal axis, making the hair extremely brittle.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.13

Sequence similarities

Belongs to the AAA ATPase family. BCS1 subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 419419Mitochondrial chaperone BCS1
PRO_0000084772

Regions

Topological domain1 – 1515Mitochondrial intermembrane Potential
Transmembrane16 – 3217Helical; Potential
Topological domain33 – 419387Mitochondrial matrix Potential
Nucleotide binding230 – 2378ATP Potential

Natural variations

Natural variant351G → R in BJS; with mild mitochondrial complex III deficiency. Ref.13
VAR_032086
Natural variant451R → C in MC3DN1. Ref.11
VAR_032087
Natural variant501T → A in MC3DN1. Ref.14
VAR_064615
Natural variant731R → C in MC3DN1. Ref.12
VAR_064616
Natural variant781S → G in GRACILE. Ref.3 Ref.13
Corresponds to variant rs28937590 [ dbSNP | Ensembl ].
VAR_018149
Natural variant991P → L in MC3DN1. Ref.2 Ref.13
VAR_018159
Natural variant1141R → W in BJS. Ref.13
VAR_032088
Natural variant1441R → Q in GRACILE. Ref.3 Ref.13
VAR_018160
Natural variant1551R → P in MC3DN1; abolishes interaction with LETM1. Ref.2 Ref.9 Ref.13
VAR_018161
Natural variant1831R → C in MC3DN1; causes a decreased incorporation of the Rieske iron-sulfur protein UQCRFS1 into complex III. Ref.12
VAR_064617
Natural variant1831R → H in BJS. Ref.13
VAR_032089
Natural variant1841R → C in MC3DN1 and BJS; with mild mitochondrial complex III deficiency; causes a decreased incorporation of the Rieske iron-sulfur protein UQCRFS1 into complex III. Ref.12 Ref.13
VAR_032090
Natural variant2771S → N in MC3DN1. Ref.2 Ref.13
VAR_018162
Natural variant3021Q → E in BJS. Ref.13
VAR_032091
Natural variant3061R → H in BJS. Ref.13
VAR_032092
Natural variant3271V → A in GRACILE. Ref.3 Ref.13
VAR_018163
Natural variant3531V → M in MC3DN1. Ref.2 Ref.13
VAR_018164
Natural variant3681F → I in MC3DN1. Ref.12
VAR_064618

Experimental info

Sequence conflict3941A → T in CAE11877. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Q9Y276 [UniParc].

Last modified November 1, 1999. Version 1.
Checksum: 7F0F98BA62F2CBB8

FASTA41947,534
        10         20         30         40         50         60 
MPLSDFILAL KDNPYFGAGF GLVGVGTALA LARKGVQLGL VAFRRHYMIT LEVPARDRSY 

        70         80         90        100        110        120 
AWLLSWLTRH STRTQHLSVE TSYLQHESGR ISTKFEFVPS PGNHFIWYRG KWIRVERSRE 

       130        140        150        160        170        180 
MQMIDLQTGT PWESVTFTAL GTDRKVFFNI LEEARELALQ QEEGKTVMYT AVGSEWRPFG 

       190        200        210        220        230        240 
YPRRRRPLNS VVLQQGLADR IVRDVQEFID NPKWYTDRGI PYRRGYLLYG PPGCGKSSFI 

       250        260        270        280        290        300 
TALAGELEHS ICLLSLTDSS LSDDRLNHLL SVAPQQSLVL LEDVDAAFLS RDLAVENPVK 

       310        320        330        340        350        360 
YQGLGRLTFS GLLNALDGVA STEARIVFMT TNHVDRLDPA LIRPGRVDLK EYVGYCSHWQ 

       370        380        390        400        410 
LTQMFQRFYP GQAPSLAENF AEHVLRATNQ ISPAQVQGYF MLYKNDPVGA IHNAESLRR 

« Hide

References

« Hide 'large scale' references
[1]"Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain."
Petruzzella V., Tiranti V., Fernandez P., Ianna P., Carrozzo R., Zeviani M.
Genomics 54:494-504(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"A mutant mitochondrial respiratory chain assembly protein causes complex III deficiency in patients with tubulopathy, encephalopathy and liver failure."
de Lonlay P., Valnot I., Barrientos A., Gorbatyuk M., Tzagoloff A., Taanman J.-W., Benayoun E., Chretien D., Kadhom N., Lombes A., Ogier de Baulny H., Niaudet P., Munnich A., Rustin P., Roetig A.
Nat. Genet. 29:57-60(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS MC3DN1 LEU-99; PRO-155; ASN-277 AND MET-353.
[3]"GRACILE syndrome, a lethal metabolic disorder with iron overload, is caused by a point mutation in BCS1L."
Visapaeae I., Fellman V., Vesa J., Dasvarma A., Hutton J.L., Kumar V., Payne G.S., Makarow M., Van Coster R., Taylor R.W., Turnbull D.M., Suomalainen A., Peltonen L.
Am. J. Hum. Genet. 71:863-876(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], VARIANTS GRACILE GLY-78; GLN-144 AND ALA-327.
[4]"Large-scale concatenation cDNA sequencing."
Yu W., Andersson B., Worley K.C., Muzny D.M., Ding Y., Liu W., Ricafrente J.Y., Wentland M.A., Lennon G., Gibbs R.A.
Genome Res. 7:353-358(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Small intestine.
[7]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Muscle.
[9]"Characterization of the mitochondrial protein LETM1, which maintains the mitochondrial tubular shapes and interacts with the AAA-ATPase BCS1L."
Tamai S., Iida H., Yokota S., Sayano T., Kiguchiya S., Ishihara N., Hayashi J., Mihara K., Oka T.
J. Cell Sci. 121:2588-2600(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LETM1, FUNCTION, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANT MC3DN1 PRO-155.
[10]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Clinical and diagnostic characteristics of complex III deficiency due to mutations in the BCS1L gene."
De Meirleir L., Seneca S., Damis E., Sepulchre B., Hoorens A., Gerlo E., Garcia Silva M.T., Hernandez E.M., Lissens W., Van Coster R.
Am. J. Med. Genet. A 121:126-131(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MC3DN1 CYS-45.
[12]"Impaired complex III assembly associated with BCS1L gene mutations in isolated mitochondrial encephalopathy."
Fernandez-Vizarra E., Bugiani M., Goffrini P., Carrara F., Farina L., Procopio E., Donati A., Uziel G., Ferrero I., Zeviani M.
Hum. Mol. Genet. 16:1241-1252(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS MC3DN1 CYS-73; CYS-183; CYS-184 AND ILE-368.
[13]"Missense mutations in the BCS1L gene as a cause of the Bjoernstad syndrome."
Hinson J.T., Fantin V.R., Schoenberger J., Breivik N., Siem G., McDonough B., Sharma P., Keogh I., Godinho R., Santos F., Esparza A., Nicolau Y., Selvaag E., Cohen B.H., Hoppel C.L., Tranebjaerg L., Eavey R.D., Seidman J.G., Seidman C.E.
N. Engl. J. Med. 356:809-819(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BJS ARG-35; TRP-114; HIS-183; CYS-184; GLU-302 AND HIS-306, VARIANTS MC3DN1 LEU-99; PRO-155; ASN-277 AND MET-353, VARIANTS GRACILE GLY-78; GLN-144 AND ALA-327.
[14]"Infantile mitochondrial encephalomyopathy with unusual phenotype caused by a novel BCS1L mutation in an isolated complex III-deficient patient."
Blazquez A., Gil-Borlado M.C., Moran M., Verdu A., Cazorla-Calleja M.R., Martin M.A., Arenas J., Ugalde C.
Neuromuscul. Disord. 19:143-146(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT MC3DN1 ALA-50.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF026849 mRNA. Translation: AAD08638.1.
AF346835 Genomic DNA. Translation: AAK29417.1.
AF516670 Genomic DNA. Translation: AAN05490.1.
AF038195 mRNA. Translation: AAB97365.1.
AK096210 mRNA. Translation: BAG53231.1.
BX571752 mRNA. Translation: CAE11877.1.
CH471063 Genomic DNA. Translation: EAW70634.1.
BC000416 mRNA. Translation: AAH00416.1.
BC007500 mRNA. Translation: AAH07500.1.
RefSeqNP_001073335.1. NM_001079866.1.
NP_001244271.1. NM_001257342.1.
NP_001244272.1. NM_001257343.1.
NP_001244273.1. NM_001257344.1.
NP_004319.1. NM_004328.4.
XP_005246804.1. XM_005246747.2.
UniGeneHs.471401.

3D structure databases

ProteinModelPortalQ9Y276.
SMRQ9Y276. Positions 153-398.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107087. 6 interactions.
IntActQ9Y276. 3 interactions.
MINTMINT-1433080.
STRING9606.ENSP00000352219.

PTM databases

PhosphoSiteQ9Y276.

Polymorphism databases

DMDM46397351.

Proteomic databases

PaxDbQ9Y276.
PeptideAtlasQ9Y276.
PRIDEQ9Y276.

Protocols and materials databases

DNASU617.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000359273; ENSP00000352219; ENSG00000074582.
ENST00000392109; ENSP00000375957; ENSG00000074582.
ENST00000392110; ENSP00000375958; ENSG00000074582.
ENST00000392111; ENSP00000375959; ENSG00000074582.
ENST00000412366; ENSP00000406494; ENSG00000074582.
ENST00000431802; ENSP00000413908; ENSG00000074582.
ENST00000439945; ENSP00000404999; ENSG00000074582.
GeneID617.
KEGGhsa:617.
UCSCuc002vip.3. human.

Organism-specific databases

CTD617.
GeneCardsGC02P219523.
HGNCHGNC:1020. BCS1L.
HPAHPA037700.
HPA037701.
MIM124000. phenotype.
262000. phenotype.
603358. phenotype.
603647. gene.
neXtProtNX_Q9Y276.
Orphanet123. Bjornstad syndrome.
53693. GRACILE syndrome.
1460. Isolated CoQ-cytochrome C reductase deficiency.
255249. Leigh syndrome with nephrotic syndrome.
254902. Renal tubulopathy - encephalopathy - liver failure.
PharmGKBPA25327.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0465.
HOGENOMHOG000198799.
HOVERGENHBG048759.
InParanoidQ9Y276.
KOK08900.
OMAFMTTNHP.
PhylomeDBQ9Y276.
TreeFamTF315009.

Enzyme and pathway databases

ReactomeREACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ9Y276.
BgeeQ9Y276.
CleanExHS_BCS1L.
GenevestigatorQ9Y276.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027243. BCS1.
IPR014851. BCS1_N.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23070:SF2. PTHR23070:SF2. 1 hit.
PfamPF00004. AAA. 1 hit.
PF08740. BCS1_N. 1 hit.
[Graphical view]
SMARTSM00382. AAA. 1 hit.
SM01024. BCS1_N. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
PROSITEPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiBCS1L.
GenomeRNAi617.
NextBio2497.
PROQ9Y276.
SOURCESearch...

Entry information

Entry nameBCS1_HUMAN
AccessionPrimary (citable) accession number: Q9Y276
Secondary accession number(s): B3KTW9, Q7Z2V7
Entry history
Integrated into UniProtKB/Swiss-Prot: March 29, 2004
Last sequence update: November 1, 1999
Last modified: April 16, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM