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Q9Y2T2

- AP3M1_HUMAN

UniProt

Q9Y2T2 - AP3M1_HUMAN

Protein

AP-3 complex subunit mu-1

Gene

AP3M1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 Nov 1999)
      Previous versions | rss
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    Functioni

    Part of the AP-3 complex, an adaptor-related complex which is not clathrin-associated. The complex is associated with the Golgi region as well as more peripheral structures. It facilitates the budding of vesicles from the Golgi membrane and may be directly involved in trafficking to lysosomes. In concert with the BLOC-1 complex, AP-3 is required to target cargos into vesicles assembled at cell bodies for delivery into neurites and nerve terminals.

    GO - Molecular functioni

    1. protein binding Source: UniProtKB
    2. Rab GTPase binding Source: BHF-UCL

    GO - Biological processi

    1. anterograde axon cargo transport Source: UniProtKB
    2. anterograde synaptic vesicle transport Source: UniProtKB
    3. protein targeting to lysosome Source: ProtInc

    Keywords - Biological processi

    Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
    SignaLinkiQ9Y2T2.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AP-3 complex subunit mu-1
    Alternative name(s):
    AP-3 adaptor complex mu3A subunit
    Adaptor-related protein complex 3 subunit mu-1
    Mu-adaptin 3A
    Mu3A-adaptin
    Gene namesi
    Name:AP3M1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:569. AP3M1.

    Subcellular locationi

    Golgi apparatus. Cytoplasmic vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: Component of the coat surrounding the cytoplasmic face of coated vesicles located at the Golgi complex.By similarity

    GO - Cellular componenti

    1. clathrin adaptor complex Source: InterPro
    2. cytoplasmic vesicle membrane Source: UniProtKB-SubCell
    3. Golgi apparatus Source: UniProtKB-SubCell
    4. lysosomal membrane Source: UniProtKB
    5. lysosome Source: ProtInc

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Golgi apparatus, Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24860.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 418418AP-3 complex subunit mu-1PRO_0000193781Add
    BLAST

    Proteomic databases

    MaxQBiQ9Y2T2.
    PaxDbiQ9Y2T2.
    PeptideAtlasiQ9Y2T2.
    PRIDEiQ9Y2T2.

    PTM databases

    PhosphoSiteiQ9Y2T2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9Y2T2.
    BgeeiQ9Y2T2.
    CleanExiHS_AP3M1.
    GenevestigatoriQ9Y2T2.

    Interactioni

    Subunit structurei

    Adaptor protein complex 3 (AP-3) is a heterotetramer composed of two large adaptins (delta-type subunit AP3D1 and beta-type subunit AP3B1 or AP3B2), a medium adaptin (mu-type subunit AP3M1 or AP3M2) and a small adaptin (sigma-type subunit APS1 or AP3S2). Interacts with AGAP1. AP-3 associates with the BLOC-1 complex By similarity.By similarity

    Protein-protein interaction databases

    BioGridi117938. 20 interactions.
    IntActiQ9Y2T2. 4 interactions.
    STRINGi9606.ENSP00000347408.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9Y2T2.
    SMRiQ9Y2T2. Positions 4-418.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini176 – 417242MHDPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 MHD (mu homology) domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG298719.
    HOGENOMiHOG000234366.
    HOVERGENiHBG104910.
    InParanoidiQ9Y2T2.
    KOiK12398.
    OMAiHMPKAVL.
    OrthoDBiEOG79KPF6.
    PhylomeDBiQ9Y2T2.
    TreeFamiTF315187.

    Family and domain databases

    InterProiIPR022775. AP_mu_sigma_su.
    IPR001392. Clathrin_mu.
    IPR008968. Clathrin_mu_C.
    IPR018240. Clathrin_mu_CS.
    IPR011012. Longin-like_dom.
    IPR028565. MHD.
    [Graphical view]
    PfamiPF00928. Adap_comp_sub. 1 hit.
    PF01217. Clat_adaptor_s. 1 hit.
    [Graphical view]
    PIRSFiPIRSF005992. Clathrin_mu. 1 hit.
    PRINTSiPR00314. CLATHRINADPT.
    SUPFAMiSSF49447. SSF49447. 1 hit.
    SSF64356. SSF64356. 1 hit.
    PROSITEiPS00990. CLAT_ADAPTOR_M_1. 1 hit.
    PS00991. CLAT_ADAPTOR_M_2. 1 hit.
    PS51072. MHD. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q9Y2T2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MIHSLFLINC SGDIFLEKHW KSVVSQSVCD YFFEAQEKAA DVENVPPVIS    50
    TPHHYLISIY RDKLFFVSVI QTEVPPLFVI EFLHRVADTF QDYFGECSEA 100
    AIKDNVVIVY ELLEEMLDNG FPLATESNIL KELIKPPTIL RSVVNSITGS 150
    SNVGDTLPTG QLSNIPWRRA GVKYTNNEAY FDVVEEIDAI IDKSGSTVFA 200
    EIQGVIDACI KLSGMPDLSL SFMNPRLLDD VSFHPCIRFK RWESERVLSF 250
    IPPDGNFRLI SYRVSSQNLV AIPVYVKHSI SFKENSSCGR FDITIGPKQN 300
    MGKTIEGITV TVHMPKVVLN MNLTPTQGSY TFDPVTKVLT WDVGKITPQK 350
    LPSLKGLVNL QSGAPKPEEN PSLNIQFKIQ QLAISGLKVN RLDMYGEKYK 400
    PFKGVKYVTK AGKFQVRT 418
    Length:418
    Mass (Da):46,939
    Last modified:November 1, 1999 - v1
    Checksum:i533E189C320C4C48
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti160 – 1601G → V in BAB15614. (PubMed:14702039)Curated
    Sequence conflicti285 – 2851N → D in BAB15614. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF092092 mRNA. Translation: AAD20446.1.
    AK026983 mRNA. Translation: BAB15614.1.
    AL731576 Genomic DNA. Translation: CAI39670.1.
    BC026232 mRNA. Translation: AAH26232.1.
    BC067127 mRNA. Translation: AAH67127.1.
    CCDSiCCDS7342.1.
    RefSeqiNP_036227.1. NM_012095.4.
    NP_996895.1. NM_207012.2.
    XP_006717826.1. XM_006717763.1.
    XP_006717827.1. XM_006717764.1.
    UniGeneiHs.500104.

    Genome annotation databases

    EnsembliENST00000355264; ENSP00000347408; ENSG00000185009.
    ENST00000372745; ENSP00000361831; ENSG00000185009.
    GeneIDi26985.
    KEGGihsa:26985.
    UCSCiuc001jwf.3. human.

    Polymorphism databases

    DMDMi13123952.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF092092 mRNA. Translation: AAD20446.1 .
    AK026983 mRNA. Translation: BAB15614.1 .
    AL731576 Genomic DNA. Translation: CAI39670.1 .
    BC026232 mRNA. Translation: AAH26232.1 .
    BC067127 mRNA. Translation: AAH67127.1 .
    CCDSi CCDS7342.1.
    RefSeqi NP_036227.1. NM_012095.4.
    NP_996895.1. NM_207012.2.
    XP_006717826.1. XM_006717763.1.
    XP_006717827.1. XM_006717764.1.
    UniGenei Hs.500104.

    3D structure databases

    ProteinModelPortali Q9Y2T2.
    SMRi Q9Y2T2. Positions 4-418.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117938. 20 interactions.
    IntActi Q9Y2T2. 4 interactions.
    STRINGi 9606.ENSP00000347408.

    PTM databases

    PhosphoSitei Q9Y2T2.

    Polymorphism databases

    DMDMi 13123952.

    Proteomic databases

    MaxQBi Q9Y2T2.
    PaxDbi Q9Y2T2.
    PeptideAtlasi Q9Y2T2.
    PRIDEi Q9Y2T2.

    Protocols and materials databases

    DNASUi 26985.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000355264 ; ENSP00000347408 ; ENSG00000185009 .
    ENST00000372745 ; ENSP00000361831 ; ENSG00000185009 .
    GeneIDi 26985.
    KEGGi hsa:26985.
    UCSCi uc001jwf.3. human.

    Organism-specific databases

    CTDi 26985.
    GeneCardsi GC10M075880.
    HGNCi HGNC:569. AP3M1.
    MIMi 610366. gene.
    neXtProti NX_Q9Y2T2.
    PharmGKBi PA24860.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG298719.
    HOGENOMi HOG000234366.
    HOVERGENi HBG104910.
    InParanoidi Q9Y2T2.
    KOi K12398.
    OMAi HMPKAVL.
    OrthoDBi EOG79KPF6.
    PhylomeDBi Q9Y2T2.
    TreeFami TF315187.

    Enzyme and pathway databases

    Reactomei REACT_16907. Association of TriC/CCT with target proteins during biosynthesis.
    SignaLinki Q9Y2T2.

    Miscellaneous databases

    ChiTaRSi AP3M1. human.
    GeneWikii AP3M1.
    GenomeRNAii 26985.
    NextBioi 49448.
    PROi Q9Y2T2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9Y2T2.
    Bgeei Q9Y2T2.
    CleanExi HS_AP3M1.
    Genevestigatori Q9Y2T2.

    Family and domain databases

    InterProi IPR022775. AP_mu_sigma_su.
    IPR001392. Clathrin_mu.
    IPR008968. Clathrin_mu_C.
    IPR018240. Clathrin_mu_CS.
    IPR011012. Longin-like_dom.
    IPR028565. MHD.
    [Graphical view ]
    Pfami PF00928. Adap_comp_sub. 1 hit.
    PF01217. Clat_adaptor_s. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF005992. Clathrin_mu. 1 hit.
    PRINTSi PR00314. CLATHRINADPT.
    SUPFAMi SSF49447. SSF49447. 1 hit.
    SSF64356. SSF64356. 1 hit.
    PROSITEi PS00990. CLAT_ADAPTOR_M_1. 1 hit.
    PS00991. CLAT_ADAPTOR_M_2. 1 hit.
    PS51072. MHD. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Altered trafficking of lysosomal proteins in Hermansky-Pudlak syndrome due to mutations in the beta 3A subunit of the AP-3 adaptor."
      Dell'Angelica E.C., Shotelersuk V., Aguilar R.C., Gahl W.A., Bonifacino J.S.
      Mol. Cell 3:11-21(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Peripheral blood and Skin fibroblast.
    2. "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.
      , 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].
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Eye and Prostate.
    5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiAP3M1_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y2T2
    Secondary accession number(s): Q5JQ12, Q9H5L2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2001
    Last sequence update: November 1, 1999
    Last modified: October 1, 2014
    This is version 120 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3