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Q9JME5

- AP3B2_MOUSE

UniProt

Q9JME5 - AP3B2_MOUSE

Protein

AP-3 complex subunit beta-2

Gene

Ap3b2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 2 (25 Oct 2004)
      Previous versions | rss
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    Functioni

    Subunit of non-clathrin- and clathrin-associated adaptor protein complex 3 (AP-3) that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. AP-3 appears to be involved in the sorting of a subset of transmembrane proteins targeted to lysosomes and lysosome-related organelles. 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.1 Publication

    GO - Biological processi

    1. anterograde axon cargo transport Source: UniProtKB
    2. anterograde synaptic vesicle transport Source: UniProtKB
    3. intracellular protein transport Source: MGI
    4. vesicle-mediated transport Source: MGI

    Keywords - Biological processi

    Protein transport, Transport

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AP-3 complex subunit beta-2
    Alternative name(s):
    Adaptor protein complex AP-3 subunit beta-2
    Adaptor-related protein complex 3 subunit beta-2
    Beta-3B-adaptin
    Clathrin assembly protein complex 3 beta-2 large chain
    Gene namesi
    Name:Ap3b2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:1100869. Ap3b2.

    Subcellular locationi

    Cytoplasmic vesicleclathrin-coated vesicle membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity. Golgi apparatus 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. AP-3 adaptor complex Source: InterPro
    2. clathrin-coated vesicle membrane Source: UniProtKB-SubCell
    3. nucleus Source: Ensembl
    4. trans-Golgi network Source: MGI

    Keywords - Cellular componenti

    Cytoplasmic vesicle, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 10821082AP-3 complex subunit beta-2PRO_0000193749Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei272 – 2721PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ9JME5.
    PaxDbiQ9JME5.
    PRIDEiQ9JME5.

    PTM databases

    PhosphoSiteiQ9JME5.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9JME5.
    BgeeiQ9JME5.
    CleanExiMM_AP3B2.
    GenevestigatoriQ9JME5.

    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) By similarity. AP-3 associates with the BLOC-1 complex.By similarity

    Protein-protein interaction databases

    BioGridi198133. 1 interaction.
    IntActiQ9JME5. 2 interactions.
    MINTiMINT-4087974.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JME5.
    SMRiQ9JME5. Positions 41-628.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi646 – 798153Glu/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5096.
    GeneTreeiENSGT00530000063546.
    HOGENOMiHOG000033978.
    HOVERGENiHBG050519.
    InParanoidiQ3UYP8.
    KOiK12397.
    OMAiWRKKTPP.
    OrthoDBiEOG74R1QG.
    PhylomeDBiQ9JME5.
    TreeFamiTF314605.

    Family and domain databases

    Gene3Di1.25.10.10. 2 hits.
    InterProiIPR026740. AP3_beta.
    IPR029390. AP3B_C.
    IPR026739. AP_beta.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR002553. Clathrin/coatomer_adapt-like_N.
    IPR013041. Coatomer/clathrin_app_Ig-like.
    [Graphical view]
    PANTHERiPTHR11134. PTHR11134. 1 hit.
    PfamiPF01602. Adaptin_N. 1 hit.
    PF14796. AP3B1_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037096. AP3_complex_beta. 1 hit.
    SUPFAMiSSF48371. SSF48371. 2 hits.
    SSF49348. SSF49348. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    Q9JME5-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSAAPAYSED KGGSAGPGEP EYGHDPASGG IFSSDYKRHD DLKEMLDTNK     50
    DSLKLEAMKR IVAMIARGKN ASDLFPAVVK NVACKNIEVK KLVYVYLVRY 100
    AEEQQDLALL SISTFQRGLK DPNQLIRASA LRVLSSIRVP IIVPIMMLAI 150
    KEAASDMSPY VRKTAAHAIP KLYSLDSDQK DQLIEVIEKL LADKTTLVAG 200
    SVVMAFEEVC PERIDLIHKN YRKLCNLLID VEEWGQVVII SMLTRYARTQ 250
    FLSPTQNESL LEENPEKAFY GSEEDEAKGP GSEEAATAAL PARKPYVMDP 300
    DHRLLLRNTK PLLQSRSAAV VMAVAQLYFH LAPKAEVGVI AKALVRLLRS 350
    HSEVQYVVLQ NVATMSIKRR GMFEPYLKSF YIRSTDPTQI KILKLEVLTN 400
    LANETNIPTV LREFQTYIRS MDKDFVAATI QAIGRCATNI GRVRDTCLNG 450
    LVQLLSNRDE LVVAESVVVI KKLLQMQPAQ HGEIIKHLAK LTDNIQVPMA 500
    RASILWLIGE YCEHVPKIAP DVLRKMAKSF TAEEDIVKLQ VINLAAKLYL 550
    TNSKQTKLLT QYVLSLAKYD QNYDIRDRAR FTRQLIVPSE QGGALSRHAK 600
    KLFLAPKPAP ILESSFKDRD HFQLGSLSHL LNAKATGYQE LPDWPEEAPD 650
    PSVRNVEVPE WTKCSNREKR KEKEKPFYSD SEGESGPTES ADSEPESESE 700
    SESKSSSGSG SGESSSESDN EEEDEEKGGG SESEQSEEED EKKKKTKKKK 750
    ASEGHREGSS SEEGSDSSSS SESEVTSESE EEQVEPASWR KKTPPGSKSA 800
    PVAKEISLLD LEDFTPPSVQ PVSPPMVVST SLAADLEGLT LTDSSLVPSL 850
    LSPVSSIGRQ ELLHRVAGEG LSVDYAFSRQ PFSGDPHMVS LHIYFSNNSE 900
    TPIKGLHVGT PKLPAGISIQ EFPEIESLAP GESTTTVMGI NFCDSTQAAN 950
    FQLCTQTRQF YVSIQPPVGE LMAPVFMSEN EFKKEQGKLT GMNEITEKLT 1000
    LPDTCRSDHM VVQKVTATAN LGRVPCGTSD EYRFAGRTLT SGSLVLLTLD 1050
    ARAAGAAQLT VNSEKMVIGT MLVKDVIQAL TQ 1082
    Length:1,082
    Mass (Da):119,193
    Last modified:October 25, 2004 - v2
    Checksum:iA2FEB20E83E16A52
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti734 – 7341E → D in BAA92765. (PubMed:10679242)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY528675 mRNA. Translation: AAS18679.1.
    BC139378 mRNA. Translation: AAI39379.1.
    BC139379 mRNA. Translation: AAI39380.1.
    AK134504 mRNA. Translation: BAE22164.1.
    AB030202 mRNA. Translation: BAA92765.1.
    CCDSiCCDS21403.1.
    RefSeqiNP_067467.2. NM_021492.3.
    UniGeneiMm.322894.

    Genome annotation databases

    EnsembliENSMUST00000082090; ENSMUSP00000080739; ENSMUSG00000062444.
    GeneIDi11775.
    KEGGimmu:11775.
    UCSCiuc009iby.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY528675 mRNA. Translation: AAS18679.1 .
    BC139378 mRNA. Translation: AAI39379.1 .
    BC139379 mRNA. Translation: AAI39380.1 .
    AK134504 mRNA. Translation: BAE22164.1 .
    AB030202 mRNA. Translation: BAA92765.1 .
    CCDSi CCDS21403.1.
    RefSeqi NP_067467.2. NM_021492.3.
    UniGenei Mm.322894.

    3D structure databases

    ProteinModelPortali Q9JME5.
    SMRi Q9JME5. Positions 41-628.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198133. 1 interaction.
    IntActi Q9JME5. 2 interactions.
    MINTi MINT-4087974.

    PTM databases

    PhosphoSitei Q9JME5.

    Proteomic databases

    MaxQBi Q9JME5.
    PaxDbi Q9JME5.
    PRIDEi Q9JME5.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000082090 ; ENSMUSP00000080739 ; ENSMUSG00000062444 .
    GeneIDi 11775.
    KEGGi mmu:11775.
    UCSCi uc009iby.1. mouse.

    Organism-specific databases

    CTDi 8120.
    MGIi MGI:1100869. Ap3b2.

    Phylogenomic databases

    eggNOGi COG5096.
    GeneTreei ENSGT00530000063546.
    HOGENOMi HOG000033978.
    HOVERGENi HBG050519.
    InParanoidi Q3UYP8.
    KOi K12397.
    OMAi WRKKTPP.
    OrthoDBi EOG74R1QG.
    PhylomeDBi Q9JME5.
    TreeFami TF314605.

    Miscellaneous databases

    NextBioi 279567.
    PROi Q9JME5.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JME5.
    Bgeei Q9JME5.
    CleanExi MM_AP3B2.
    Genevestigatori Q9JME5.

    Family and domain databases

    Gene3Di 1.25.10.10. 2 hits.
    InterProi IPR026740. AP3_beta.
    IPR029390. AP3B_C.
    IPR026739. AP_beta.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR002553. Clathrin/coatomer_adapt-like_N.
    IPR013041. Coatomer/clathrin_app_Ig-like.
    [Graphical view ]
    PANTHERi PTHR11134. PTHR11134. 1 hit.
    Pfami PF01602. Adaptin_N. 1 hit.
    PF14796. AP3B1_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037096. AP3_complex_beta. 1 hit.
    SUPFAMi SSF48371. SSF48371. 2 hits.
    SSF49348. SSF49348. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Ap3b2, a neuron specific subunit of adaptor protein complex 3 (AP-3)."
      Seong E., Burmeister M.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [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].
    3. "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] OF 1-738.
      Strain: C57BL/6J.
      Tissue: Embryonic head.
    4. "Growth suppression of Escherichia coli by induction of expression of mammalian genes with transmembrane or ATPase domains."
      Inoue S., Sano H., Ohta M.
      Biochem. Biophys. Res. Commun. 268:553-561(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 608-1082.
      Tissue: Brain.
    5. "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations."
      Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M.
      Mol. Cell. Proteomics 6:283-293(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    6. "The schizophrenia susceptibility factor dysbindin and its associated complex sort cargoes from cell bodies to the synapse."
      Larimore J., Tornieri K., Ryder P.V., Gokhale A., Zlatic S.A., Craige B., Lee J.D., Talbot K., Pare J.F., Smith Y., Faundez V.
      Mol. Biol. Cell 22:4854-4867(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ASSOCIATION WITH THE BLOC-1 COMPLEX.

    Entry informationi

    Entry nameiAP3B2_MOUSE
    AccessioniPrimary (citable) accession number: Q9JME5
    Secondary accession number(s): B2RTK2
    , Q3UYP8, Q6QR53, Q8R1E5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 26, 2004
    Last sequence update: October 25, 2004
    Last modified: October 1, 2014
    This is version 98 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