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Q8BK64

- AHSA1_MOUSE

UniProt

Q8BK64 - AHSA1_MOUSE

Protein

Activator of 90 kDa heat shock protein ATPase homolog 1

Gene

Ahsa1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 93 (01 Oct 2014)
      Sequence version 2 (30 Apr 2003)
      Previous versions | rss
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    Functioni

    Co-chaperone that stimulates HSP90 ATPase activity. May affect a step in the endoplasmic reticulum to Golgi trafficking By similarity.By similarity

    GO - Molecular functioni

    1. ATPase activator activity Source: UniProtKB

    GO - Biological processi

    1. positive regulation of ATPase activity Source: GOC
    2. protein folding Source: UniProtKB
    3. response to stress Source: UniProtKB

    Keywords - Molecular functioni

    Chaperone

    Keywords - Biological processi

    Stress response

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Activator of 90 kDa heat shock protein ATPase homolog 1
    Short name:
    AHA1
    Gene namesi
    Name:Ahsa1
    OrganismiMus musculus (Mouse)Imported
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 12

    Organism-specific databases

    MGIiMGI:2387603. Ahsa1.

    Subcellular locationi

    Cytoplasmcytosol By similarity. Endoplasmic reticulum By similarity
    Note: May transiently interact with the endoplasmic reticulum.By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. cytosol Source: UniProtKB-SubCell
    3. endoplasmic reticulum Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 338337Activator of 90 kDa heat shock protein ATPase homolog 1PRO_0000215821Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei3 – 31N6-acetyllysineBy similarity
    Modified residuei193 – 1931PhosphoserineBy similarity
    Modified residuei212 – 2121N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ8BK64.
    PaxDbiQ8BK64.
    PRIDEiQ8BK64.

    2D gel databases

    REPRODUCTION-2DPAGEQ8BK64.

    PTM databases

    PhosphoSiteiQ8BK64.

    Expressioni

    Inductioni

    By heat shock and treatment with the HSP90 inhibitor 17-demethoxygeldanamycin (17AAG).

    Gene expression databases

    BgeeiQ8BK64.
    GenevestigatoriQ8BK64.

    Interactioni

    Subunit structurei

    Interacts with HSPCA/HSP90. Interacts with GCH1 By similarity. Interacts with SRPK1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi229959. 2 interactions.
    IntActiQ8BK64. 3 interactions.
    MINTiMINT-4087362.
    STRINGi10090.ENSMUSP00000021425.

    Structurei

    3D structure databases

    ProteinModelPortaliQ8BK64.
    SMRiQ8BK64. Positions 25-126, 204-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the AHA1 family.Curated

    Phylogenomic databases

    eggNOGiCOG5580.
    GeneTreeiENSGT00390000006429.
    HOGENOMiHOG000242852.
    HOVERGENiHBG065806.
    InParanoidiQ8BK64.
    OMAiMRVEWTG.
    OrthoDBiEOG77DJ64.
    PhylomeDBiQ8BK64.
    TreeFamiTF313680.

    Family and domain databases

    Gene3Di3.30.530.20. 1 hit.
    InterProiIPR013538. Activator_of_Hsp90_ATPase.
    IPR015310. AHSA1_N.
    IPR023393. START-like_dom.
    [Graphical view]
    PfamiPF09229. Aha1_N. 1 hit.
    PF08327. AHSA1. 1 hit.
    [Graphical view]
    SMARTiSM01000. Aha1_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF103111. SSF103111. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q8BK64-1 [UniParc]FASTAAdd to Basket

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    MAKWGEGDPR WIVEERADAT NVNNWHWTER DASNWSTEKL KTLFLAVRVE    50
    NEEGKCEVTE VNKLDGEASI NNRKGKLIFF YEWTIKLNWT GTSKSGVQYK 100
    GHVEIPNLSD ENSVDEVEIS VSLAKDEPDT NLVALMKEDG VKLLREAVGI 150
    YISTLKTEFT QGMILPTVNG ESVDPVGQPA LKTETCKAKS APSKSQAKPV 200
    GVKIPTCKIT LKETFLTSPE ELYRVFTTQE LVQAFTHAPA ALEADRGGKF 250
    HMVDGNVTGE FTDLVPEKHI AMKWRFKSWP EGHFATITLT FIDKNGETEL 300
    CMEGRGIPAP EEERTRQGWQ RYYFEGIKQT FGYGARLF 338
    Length:338
    Mass (Da):38,117
    Last modified:April 30, 2003 - v2
    Checksum:iC4F0F94FF44F9FB3
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti192 – 1921P → L in BAC36160. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK076069 mRNA. Translation: BAC36160.1.
    BC023857 mRNA. Translation: AAH23857.1.
    BC025552 mRNA. Translation: AAH25552.1.
    CCDSiCCDS26075.1.
    RefSeqiNP_666148.1. NM_146036.1.
    UniGeneiMm.22626.

    Genome annotation databases

    EnsembliENSMUST00000021425; ENSMUSP00000021425; ENSMUSG00000021037.
    GeneIDi217737.
    KEGGimmu:217737.
    UCSCiuc007oit.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK076069 mRNA. Translation: BAC36160.1 .
    BC023857 mRNA. Translation: AAH23857.1 .
    BC025552 mRNA. Translation: AAH25552.1 .
    CCDSi CCDS26075.1.
    RefSeqi NP_666148.1. NM_146036.1.
    UniGenei Mm.22626.

    3D structure databases

    ProteinModelPortali Q8BK64.
    SMRi Q8BK64. Positions 25-126, 204-335.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 229959. 2 interactions.
    IntActi Q8BK64. 3 interactions.
    MINTi MINT-4087362.
    STRINGi 10090.ENSMUSP00000021425.

    PTM databases

    PhosphoSitei Q8BK64.

    2D gel databases

    REPRODUCTION-2DPAGE Q8BK64.

    Proteomic databases

    MaxQBi Q8BK64.
    PaxDbi Q8BK64.
    PRIDEi Q8BK64.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000021425 ; ENSMUSP00000021425 ; ENSMUSG00000021037 .
    GeneIDi 217737.
    KEGGi mmu:217737.
    UCSCi uc007oit.1. mouse.

    Organism-specific databases

    CTDi 10598.
    MGIi MGI:2387603. Ahsa1.

    Phylogenomic databases

    eggNOGi COG5580.
    GeneTreei ENSGT00390000006429.
    HOGENOMi HOG000242852.
    HOVERGENi HBG065806.
    InParanoidi Q8BK64.
    OMAi MRVEWTG.
    OrthoDBi EOG77DJ64.
    PhylomeDBi Q8BK64.
    TreeFami TF313680.

    Miscellaneous databases

    ChiTaRSi AHSA1. mouse.
    NextBioi 376016.
    PROi Q8BK64.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q8BK64.
    Genevestigatori Q8BK64.

    Family and domain databases

    Gene3Di 3.30.530.20. 1 hit.
    InterProi IPR013538. Activator_of_Hsp90_ATPase.
    IPR015310. AHSA1_N.
    IPR023393. START-like_dom.
    [Graphical view ]
    Pfami PF09229. Aha1_N. 1 hit.
    PF08327. AHSA1. 1 hit.
    [Graphical view ]
    SMARTi SM01000. Aha1_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF103111. SSF103111. 1 hit.
    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.
    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].
      Strain: FVB/N.
      Tissue: Mammary gland.

    Entry informationi

    Entry nameiAHSA1_MOUSE
    AccessioniPrimary (citable) accession number: Q8BK64
    Secondary accession number(s): Q8R3E6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 30, 2003
    Last sequence update: April 30, 2003
    Last modified: October 1, 2014
    This is version 93 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, 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