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Q9CZP5

- BCS1_MOUSE

UniProt

Q9CZP5 - BCS1_MOUSE

Protein

Mitochondrial chaperone BCS1

Gene

Bcs1l

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 101 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    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 By similarity.By similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi230 – 2378ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. nucleoside-triphosphatase activity Source: InterPro

    GO - Biological processi

    1. mitochondrial respiratory chain complex I assembly Source: Ensembl
    2. mitochondrial respiratory chain complex III assembly Source: MGI
    3. mitochondrial respiratory chain complex IV assembly Source: Ensembl

    Keywords - Molecular functioni

    Chaperone

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Mitochondrial chaperone BCS1
    Alternative name(s):
    BCS1-like protein
    Gene namesi
    Name:Bcs1l
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:1914071. Bcs1l.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. mitochondrial inner membrane Source: UniProtKB-SubCell
    3. mitochondrion Source: MGI

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Mitochondrion inner membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 418418Mitochondrial chaperone BCS1PRO_0000084773Add
    BLAST

    Proteomic databases

    MaxQBiQ9CZP5.
    PaxDbiQ9CZP5.
    PRIDEiQ9CZP5.

    PTM databases

    PhosphoSiteiQ9CZP5.

    Expressioni

    Gene expression databases

    BgeeiQ9CZP5.
    CleanExiMM_BCS1L.
    GenevestigatoriQ9CZP5.

    Interactioni

    Subunit structurei

    Interacts with LETM1.By similarity

    Protein-protein interaction databases

    STRINGi10090.ENSMUSP00000109362.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9CZP5.
    SMRiQ9CZP5. Positions 153-398.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 1515Mitochondrial intermembraneSequence AnalysisAdd
    BLAST
    Topological domaini33 – 418386Mitochondrial matrixSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei16 – 3217HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AAA ATPase family. BCS1 subfamily.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0465.
    GeneTreeiENSGT00390000005415.
    HOGENOMiHOG000198799.
    HOVERGENiHBG048759.
    InParanoidiQ9CZP5.
    KOiK08900.
    OMAiAENPVKY.
    OrthoDBiEOG7P2XS1.
    PhylomeDBiQ9CZP5.
    TreeFamiTF315009.

    Family and domain databases

    Gene3Di3.40.50.300. 1 hit.
    InterProiIPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR027243. BCS1.
    IPR014851. BCS1_N.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PANTHERiPTHR23070:SF17. PTHR23070:SF17. 1 hit.
    PfamiPF00004. AAA. 1 hit.
    PF08740. BCS1_N. 1 hit.
    [Graphical view]
    SMARTiSM00382. AAA. 1 hit.
    SM01024. BCS1_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF52540. SSF52540. 1 hit.
    PROSITEiPS00674. AAA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9CZP5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPFSDFVLAL KDNPYFGAGF GLVGVGTALA MARKGAQLGL VAFRRHYMIT    50
    LEVPARDRSY AWLLSWLTRH STRTQHLSVE TSYLQHESGR ISTKFEFIPS 100
    PGNHFIWYQG KWIRVERNRD MQMVDLQTGT PWESVTFTAL GTDRKVFFNI 150
    LEEARALALQ QEEGKTVMYT AVGSEWRTFG YPRRRRPLDS VVLQQGLADR 200
    IVKDIREFID NPKWYIDRGI PYRRGYLLYG PPGCGKSSFI TALAGELEHS 250
    ICLLSLTDSS LSDDRLNHLL SVAPQQSLVL LEDVDAAFLS RDLAVENPIK 300
    YQGLGRLTFS GLLNALDGVA STEARIVFMT TNYIDRLDPA LIRPGRVDLK 350
    EYVGYCSHWQ LTQMFQRFYP GQAPSLAENF AEHVLKATSE ISPAQVQGYF 400
    MLYKNDPMGA VHNIESLR 418
    Length:418
    Mass (Da):47,406
    Last modified:June 1, 2001 - v1
    Checksum:i94905BA9B097F0DE
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012324 mRNA. Translation: BAB28162.1.
    AK078925 mRNA. Translation: BAC37464.1.
    AK079385 mRNA. Translation: BAC37629.1.
    BC019781 mRNA. Translation: AAH19781.1.
    CCDSiCCDS15051.1.
    RefSeqiNP_080060.1. NM_025784.4.
    XP_006496259.1. XM_006496196.1.
    UniGeneiMm.358700.

    Genome annotation databases

    EnsembliENSMUST00000027358; ENSMUSP00000027358; ENSMUSG00000026172.
    ENSMUST00000113732; ENSMUSP00000109361; ENSMUSG00000026172.
    ENSMUST00000113733; ENSMUSP00000109362; ENSMUSG00000026172.
    GeneIDi66821.
    KEGGimmu:66821.
    UCSCiuc007bmq.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK012324 mRNA. Translation: BAB28162.1 .
    AK078925 mRNA. Translation: BAC37464.1 .
    AK079385 mRNA. Translation: BAC37629.1 .
    BC019781 mRNA. Translation: AAH19781.1 .
    CCDSi CCDS15051.1.
    RefSeqi NP_080060.1. NM_025784.4.
    XP_006496259.1. XM_006496196.1.
    UniGenei Mm.358700.

    3D structure databases

    ProteinModelPortali Q9CZP5.
    SMRi Q9CZP5. Positions 153-398.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 10090.ENSMUSP00000109362.

    PTM databases

    PhosphoSitei Q9CZP5.

    Proteomic databases

    MaxQBi Q9CZP5.
    PaxDbi Q9CZP5.
    PRIDEi Q9CZP5.

    Protocols and materials databases

    DNASUi 66821.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000027358 ; ENSMUSP00000027358 ; ENSMUSG00000026172 .
    ENSMUST00000113732 ; ENSMUSP00000109361 ; ENSMUSG00000026172 .
    ENSMUST00000113733 ; ENSMUSP00000109362 ; ENSMUSG00000026172 .
    GeneIDi 66821.
    KEGGi mmu:66821.
    UCSCi uc007bmq.1. mouse.

    Organism-specific databases

    CTDi 617.
    MGIi MGI:1914071. Bcs1l.

    Phylogenomic databases

    eggNOGi COG0465.
    GeneTreei ENSGT00390000005415.
    HOGENOMi HOG000198799.
    HOVERGENi HBG048759.
    InParanoidi Q9CZP5.
    KOi K08900.
    OMAi AENPVKY.
    OrthoDBi EOG7P2XS1.
    PhylomeDBi Q9CZP5.
    TreeFami TF315009.

    Miscellaneous databases

    NextBioi 322735.
    PROi Q9CZP5.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9CZP5.
    CleanExi MM_BCS1L.
    Genevestigatori Q9CZP5.

    Family and domain databases

    Gene3Di 3.40.50.300. 1 hit.
    InterProi IPR003593. AAA+_ATPase.
    IPR003959. ATPase_AAA_core.
    IPR003960. ATPase_AAA_CS.
    IPR027243. BCS1.
    IPR014851. BCS1_N.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    PANTHERi PTHR23070:SF17. PTHR23070:SF17. 1 hit.
    Pfami PF00004. AAA. 1 hit.
    PF08740. BCS1_N. 1 hit.
    [Graphical view ]
    SMARTi SM00382. AAA. 1 hit.
    SM01024. BCS1_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52540. SSF52540. 1 hit.
    PROSITEi PS00674. AAA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Cecum and Cerebellum.
    2. "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: Mammary tumor.
    3. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 2-11, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.

    Entry informationi

    Entry nameiBCS1_MOUSE
    AccessioniPrimary (citable) accession number: Q9CZP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 101 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3