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Q9DBG3

- AP2B1_MOUSE

UniProt

Q9DBG3 - AP2B1_MOUSE

Protein

AP-2 complex subunit beta

Gene

Ap2b1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 110 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly By similarity.By similarity

    GO - Molecular functioni

    1. protein binding Source: IntAct
    2. protein transporter activity Source: InterPro

    GO - Biological processi

    1. clathrin coat assembly Source: Ensembl
    2. endocytosis Source: UniProtKB-KW
    3. intracellular protein transport Source: InterPro

    Keywords - Biological processi

    Endocytosis, Protein transport, Transport

    Enzyme and pathway databases

    ReactomeiREACT_196550. MHC class II antigen presentation.
    REACT_202778. Retrograde neurotrophin signalling.
    REACT_203917. EGFR downregulation.
    REACT_222404. WNT5A-dependent internalization of FZD4.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    AP-2 complex subunit beta
    Alternative name(s):
    AP105B
    Adaptor protein complex AP-2 subunit beta
    Adaptor-related protein complex 2 subunit beta
    Beta-2-adaptin
    Beta-adaptin
    Clathrin assembly protein complex 2 beta large chain
    Plasma membrane adaptor HA2/AP2 adaptin beta subunit
    Gene namesi
    Name:Ap2b1
    Synonyms:Clapb1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 11

    Organism-specific databases

    MGIiMGI:1919020. Ap2b1.

    Subcellular locationi

    Cell membrane By similarity. Membranecoated pit By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
    Note: AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.By similarity

    GO - Cellular componenti

    1. clathrin adaptor complex Source: InterPro
    2. coated pit Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB-SubCell
    4. trans-Golgi network Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Coated pit, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 937936AP-2 complex subunit betaPRO_0000193743Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylthreonineBy similarity
    Modified residuei265 – 2651N6-acetyllysineBy similarity
    Modified residuei737 – 7371PhosphotyrosineBy similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9DBG3.
    PaxDbiQ9DBG3.
    PRIDEiQ9DBG3.

    PTM databases

    PhosphoSiteiQ9DBG3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9DBG3.
    BgeeiQ9DBG3.
    CleanExiMM_AP2B1.
    GenevestigatoriQ9DBG3.

    Interactioni

    Subunit structurei

    Adaptor protein complex 2 (AP-2) is a heterotetramer composed of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small adaptin (sigma-type subunit AP2S1). Interacts with EPN1. Interacts with EPS15; clathrin competes with EPS15. Interacts with SNAP91; clathrin competes with SNAP91. Interacts with CLTC; clathrin competes with EPS15, SNAP91 and PIP5K1C. Interacts with LDLRAP1. Interacts with AMPH and BIN1. Interacts with ARF6 (GDP-bound). Interacts (dephosphorylated at Tyr-737) with ARRB1; phosphorylation of AP2B1 at Tyr-737 disrupts the interaction. Interacts with SLC2A8. Interacts with SCYL1 and SCYL2. Interacts with TGFBR1 and TGFBR2. Interacts with PIP5K1C; clathrin competes with PIP5K1C By similarity. Interacts with DENND1B By similarity. Interacts with FCHO1 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FASLGP480232EBI-775229,EBI-495538From a different organism.
    Pip5k1cO701618EBI-7257021,EBI-773657

    Protein-protein interaction databases

    BioGridi214914. 12 interactions.
    IntActiQ9DBG3. 10 interactions.
    MINTiMINT-1870047.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DBG3.
    SMRiQ9DBG3. Positions 4-582, 705-937.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi576 – 716141Pro-rich (stalk region)Add
    BLAST

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG5096.
    GeneTreeiENSGT00530000063138.
    HOGENOMiHOG000163270.
    HOVERGENiHBG050515.
    KOiK11825.
    OMAiPNQSIDI.
    OrthoDBiEOG7BGHK0.
    TreeFamiTF300318.

    Family and domain databases

    Gene3Di1.25.10.10. 1 hit.
    2.60.40.1150. 1 hit.
    3.30.310.10. 1 hit.
    InterProiIPR026739. AP_beta.
    IPR016342. AP_complex_bsu_1_2_4.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR015151. B-adaptin_app_sub_C.
    IPR012295. Beta2_adaptin/TBP_C_dom.
    IPR002553. Clathrin/coatomer_adapt-like_N.
    IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
    IPR013037. Clathrin_b-adaptin_app_Ig-like.
    IPR009028. Coatomer/calthrin_app_sub_C.
    IPR013041. Coatomer/clathrin_app_Ig-like.
    [Graphical view]
    PANTHERiPTHR11134. PTHR11134. 1 hit.
    PfamiPF01602. Adaptin_N. 1 hit.
    PF02883. Alpha_adaptinC2. 1 hit.
    PF09066. B2-adapt-app_C. 1 hit.
    [Graphical view]
    PIRSFiPIRSF002291. AP_complex_beta. 1 hit.
    SMARTiSM00809. Alpha_adaptinC2. 1 hit.
    SM01020. B2-adapt-app_C. 1 hit.
    [Graphical view]
    SUPFAMiSSF48371. SSF48371. 1 hit.
    SSF49348. SSF49348. 1 hit.
    SSF55711. SSF55711. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9DBG3-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL    50
    FPDVVNCMQT DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP 100
    LIRALAVRTM GCIRVDKITE YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD 150
    INAQMVEDQG FLDSLRDLIA DSNPMVVANA VAALSEISES HPNSNLLDLN 200
    PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI CERVTPRLSH 250
    ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY 300
    VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN 350
    IAQVLAELKE YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ 400
    TKVNYVVQEA IVVIRDIFRK YPNKYESIIA TLCENLDSLD EPDARAAMIW 450
    IVGEYAERID NADELLESFL EGFHDESTQV QLTLLTAIVK LFLKKPSETQ 500
    ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV VLSEKPLISE 550
    ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST 600
    DAGDSPVGTT TTTNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM 650
    GAVDLLGGGL DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI 700
    GMAPGGYVAP KAVWLPAVKA KGLEISGTFT HRQGHIYMEM NFTNKALQHM 750
    TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ SIDVSLPLNT LGPVMKMEPL 800
    NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT WKDIPNENEL 850
    QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL 900
    AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN 937
    Length:937
    Mass (Da):104,583
    Last modified:June 1, 2001 - v1
    Checksum:i452DF0AE91EDB0AE
    GO
    Isoform 2 (identifier: Q9DBG3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         663-663: L → LLGSDLGGGIGGSPA

    Show »
    Length:951
    Mass (Da):105,722
    Checksum:iEBB43F600FC24A3C
    GO

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei663 – 6631L → LLGSDLGGGIGGSPA in isoform 2. 1 PublicationVSP_011491

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004975 mRNA. Translation: BAB23711.1.
    BC046772 mRNA. Translation: AAH46772.1.
    CCDSiCCDS25161.1. [Q9DBG3-2]
    CCDS25162.1. [Q9DBG3-1]
    RefSeqiNP_001030931.1. NM_001035854.2. [Q9DBG3-2]
    NP_082191.1. NM_027915.3. [Q9DBG3-1]
    XP_006534321.1. XM_006534258.1. [Q9DBG3-2]
    UniGeneiMm.39053.

    Genome annotation databases

    EnsembliENSMUST00000018875; ENSMUSP00000018875; ENSMUSG00000035152. [Q9DBG3-2]
    ENSMUST00000065692; ENSMUSP00000070714; ENSMUSG00000035152. [Q9DBG3-1]
    GeneIDi71770.
    KEGGimmu:71770.
    UCSCiuc007kor.1. mouse. [Q9DBG3-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK004975 mRNA. Translation: BAB23711.1 .
    BC046772 mRNA. Translation: AAH46772.1 .
    CCDSi CCDS25161.1. [Q9DBG3-2 ]
    CCDS25162.1. [Q9DBG3-1 ]
    RefSeqi NP_001030931.1. NM_001035854.2. [Q9DBG3-2 ]
    NP_082191.1. NM_027915.3. [Q9DBG3-1 ]
    XP_006534321.1. XM_006534258.1. [Q9DBG3-2 ]
    UniGenei Mm.39053.

    3D structure databases

    ProteinModelPortali Q9DBG3.
    SMRi Q9DBG3. Positions 4-582, 705-937.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 214914. 12 interactions.
    IntActi Q9DBG3. 10 interactions.
    MINTi MINT-1870047.

    PTM databases

    PhosphoSitei Q9DBG3.

    Proteomic databases

    MaxQBi Q9DBG3.
    PaxDbi Q9DBG3.
    PRIDEi Q9DBG3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000018875 ; ENSMUSP00000018875 ; ENSMUSG00000035152 . [Q9DBG3-2 ]
    ENSMUST00000065692 ; ENSMUSP00000070714 ; ENSMUSG00000035152 . [Q9DBG3-1 ]
    GeneIDi 71770.
    KEGGi mmu:71770.
    UCSCi uc007kor.1. mouse. [Q9DBG3-1 ]

    Organism-specific databases

    CTDi 163.
    MGIi MGI:1919020. Ap2b1.

    Phylogenomic databases

    eggNOGi COG5096.
    GeneTreei ENSGT00530000063138.
    HOGENOMi HOG000163270.
    HOVERGENi HBG050515.
    KOi K11825.
    OMAi PNQSIDI.
    OrthoDBi EOG7BGHK0.
    TreeFami TF300318.

    Enzyme and pathway databases

    Reactomei REACT_196550. MHC class II antigen presentation.
    REACT_202778. Retrograde neurotrophin signalling.
    REACT_203917. EGFR downregulation.
    REACT_222404. WNT5A-dependent internalization of FZD4.

    Miscellaneous databases

    ChiTaRSi AP2B1. mouse.
    NextBioi 334467.
    PROi Q9DBG3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9DBG3.
    Bgeei Q9DBG3.
    CleanExi MM_AP2B1.
    Genevestigatori Q9DBG3.

    Family and domain databases

    Gene3Di 1.25.10.10. 1 hit.
    2.60.40.1150. 1 hit.
    3.30.310.10. 1 hit.
    InterProi IPR026739. AP_beta.
    IPR016342. AP_complex_bsu_1_2_4.
    IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR015151. B-adaptin_app_sub_C.
    IPR012295. Beta2_adaptin/TBP_C_dom.
    IPR002553. Clathrin/coatomer_adapt-like_N.
    IPR008152. Clathrin_a/b/g-adaptin_app_Ig.
    IPR013037. Clathrin_b-adaptin_app_Ig-like.
    IPR009028. Coatomer/calthrin_app_sub_C.
    IPR013041. Coatomer/clathrin_app_Ig-like.
    [Graphical view ]
    PANTHERi PTHR11134. PTHR11134. 1 hit.
    Pfami PF01602. Adaptin_N. 1 hit.
    PF02883. Alpha_adaptinC2. 1 hit.
    PF09066. B2-adapt-app_C. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002291. AP_complex_beta. 1 hit.
    SMARTi SM00809. Alpha_adaptinC2. 1 hit.
    SM01020. B2-adapt-app_C. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48371. SSF48371. 1 hit.
    SSF49348. SSF49348. 1 hit.
    SSF55711. SSF55711. 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] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Liver.
    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] (ISOFORM 2).
      Strain: C57BL/6.
      Tissue: Brain.
    3. "Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network."
      Nakatsu F., Ohno H.
      Cell Struct. Funct. 28:419-429(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
    4. "Adaptors for clathrin coats: structure and function."
      Owen D.J., Collins B.M., Evans P.R.
      Annu. Rev. Cell Dev. Biol. 20:153-191(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.

    Entry informationi

    Entry nameiAP2B1_MOUSE
    AccessioniPrimary (citable) accession number: Q9DBG3
    Secondary accession number(s): Q80XJ4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 31, 2004
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 110 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, 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