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P63010 (AP2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
AP-2 complex subunit beta
Alternative name(s):
AP105B
Adapter-related protein complex 2 subunit beta
Adaptor protein complex AP-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 names
Name:AP2B1
Synonyms:ADTB2, CLAPB1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length937 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.8 Ref.10 Ref.11 Ref.16

Subunit structure

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, but not with DENND1A, nor DENND1C. Interacts with FCHO1. Ref.6 Ref.7 Ref.12 Ref.13 Ref.14 Ref.15 Ref.20 Ref.22 Ref.24 Ref.26 Ref.27

Subcellular location

Cell membrane. Membranecoated pit; Peripheral membrane protein; Cytoplasmic side. Note: AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV. Ref.9

Post-translational modification

Phosphorylation at Tyr-737 by SRC occurs at the plasma membrane in clathrin-coated vesicles (CCVs).

Sequence similarities

Belongs to the adaptor complexes large subunit family.

Ontologies

Keywords
   Biological processEndocytosis
Protein transport
Transport
   Cellular componentCell membrane
Coated pit
Membrane
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processantigen processing and presentation of exogenous peptide antigen via MHC class II

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

clathrin coat assembly

Inferred from electronic annotation. Source: Ensembl

endocytosis

Inferred from electronic annotation. Source: UniProtKB-KW

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

intracellular protein transport

Inferred from electronic annotation. Source: InterPro

negative regulation of epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

regulation of defense response to virus by virus

Traceable author statement. Source: Reactome

synaptic transmission

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentclathrin adaptor complex

Inferred from electronic annotation. Source: InterPro

clathrin-coated endocytic vesicle membrane

Traceable author statement. Source: Reactome

coated pit

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

endocytic vesicle membrane

Traceable author statement. Source: Reactome

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

plasma membrane

Traceable author statement. Source: Reactome

trans-Golgi network

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionclathrin binding

Inferred from physical interaction PubMed 19509056. Source: UniProtKB

protein transporter activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ap2m1P840922EBI-432924,EBI-297693From a different organism.
LDLRAP1Q5SW963EBI-432924,EBI-747813
MEA1Q166262EBI-432924,EBI-744921

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P63010-1)

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.
Isoform 2 (identifier: P63010-2)

The sequence of this isoform differs from the canonical sequence as follows:
     663-663: L → LLGSDLGGGIGGSPA
Isoform 3 (identifier: P63010-3)

Also known as: Ap2beta-NY;

The sequence of this isoform differs from the canonical sequence as follows:
     1-57: Missing.
Note: Highly expressed in the testis, spleen, thymus, prostate, ovary, blood leukocyte and brain, but not in the heart, placenta, lung, liver, skeletal muscle, kidney and pancreas. Testis expression is restricted to germ cells and is about 3-fold higher in adults than in embryos.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.23
Chain2 – 937936AP-2 complex subunit beta
PRO_0000193742

Regions

Region841 – 93797Interaction with ARRB1
Compositional bias576 – 716141Pro-rich (stalk region)

Amino acid modifications

Modified residue21N-acetylthreonine Ref.23
Modified residue2651N6-acetyllysine Ref.19
Modified residue7371Phosphotyrosine; by SRC Ref.15 Ref.18

Natural variations

Alternative sequence1 – 5757Missing in isoform 3.
VSP_047805
Alternative sequence6631L → LLGSDLGGGIGGSPA in isoform 2.
VSP_011490

Experimental info

Mutagenesis8151Y → A: Strongly reduces interaction with SNAP91, EPS15, AMPH and BIN1 and clathrin heavy chain. Ref.26 Ref.27
Mutagenesis8411W → A: Abolishes interaction with LDLRAP1 and ARRB1. Greatly reduces DENND1B-binding. Ref.12 Ref.20 Ref.26 Ref.27
Mutagenesis8421K → E: Strongly reduces interaction with ARRB1. Ref.27
Mutagenesis8491E → A: Strongly reduces interaction with LDLRAP1, ARRB1 and EPN1. No effect on DENND1B-binding. Ref.6 Ref.20 Ref.26
Mutagenesis8511Q → A: Strongly reduces interaction with ARRB1. Ref.27
Mutagenesis8791R → A: No effect on interaction with ARRB1. Ref.24 Ref.27
Mutagenesis8791R → E: Strongly reduces interaction with EPN1. Reduces interaction with SNAP91 and clathrin. No effect on EPS15 binding. Ref.24 Ref.27
Mutagenesis8881Y → V: Strongly reduces interaction with SNAP91, EPN1 and clathrin. No effect on EPS15 binding. Abolishes interaction with ARRB1 and with DENND1B. Ref.12 Ref.20 Ref.24 Ref.26 Ref.27
Mutagenesis9021E → A: Strongly reduces interaction with LDLRAP1 and ARRB1. No effect on DENND1B-binding. Ref.6 Ref.20 Ref.26
Mutagenesis9171K → Q: Strongly reduces interaction with LDLRAP1. SNAP91 and clathrin. Reduces interaction with EPN1. No effect on EPS15 binding. Ref.24

Secondary structure

........................................................................................................................................... 937
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 31, 2004. Version 1.
Checksum: B472EE5B2AE176DF

FASTA937104,553
        10         20         30         40         50         60 
MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT 

        70         80         90        100        110        120 
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE 

       130        140        150        160        170        180 
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA 

       190        200        210        220        230        240 
VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI 

       250        260        270        280        290        300 
CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY 

       310        320        330        340        350        360 
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE 

       370        380        390        400        410        420 
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK 

       430        440        450        460        470        480 
YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV 

       490        500        510        520        530        540 
QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV 

       550        560        570        580        590        600 
VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST 

       610        620        630        640        650        660 
DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL 

       670        680        690        700        710        720 
DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI GMAPGGYVAP KAVWLPAVKA 

       730        740        750        760        770        780 
KGLEISGTFT HRQGHIYMEM NFTNKALQHM TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ 

       790        800        810        820        830        840 
SIDVSLPLNT LGPVMKMEPL NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT 

       850        860        870        880        890        900 
WKDIPNENEL QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL 

       910        920        930 
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN 

« Hide

Isoform 2 [UniParc].

Checksum: 3199C9F8C7F027F2
Show »

FASTA951105,692
Isoform 3 (Ap2beta-NY) [UniParc].

Checksum: 468D8B39AD35C7E4
Show »

FASTA88098,118

References

« Hide 'large scale' references
[1]"Conservation and diversity in families of coated vesicle adaptins."
Ponnambalam S., Robinson M.S., Jackson A.P., Peiperl L., Parham P.
J. Biol. Chem. 265:4814-4820(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Brain.
[2]"Expression of a novel beta adaptin subunit mRNA splice variant in human testes."
Zhang X.D., Yin L.L., Zheng Y., Lu L., Zhou Z.M., Sha J.H.
Asian J. Androl. 7:179-188(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING.
Tissue: Testis.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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).
Tissue: Muscle.
[6]"beta-Arrestin/AP-2 interaction in G protein-coupled receptor internalization: identification of a beta-arrestin binding site in beta 2-adaptin."
Laporte S.A., Miller W.E., Kim K.-M., Caron M.G.
J. Biol. Chem. 277:9247-9254(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARRB1, MUTAGENESIS OF GLU-849 AND GLU-902.
[7]"Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit."
Yao D., Ehrlich M., Henis Y.I., Leof E.B.
Mol. Biol. Cell 13:4001-4012(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TGFBR1 AND TGFBR2.
[8]"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.
[9]"The AP-2 complex is excluded from the dynamic population of plasma membrane-associated clathrin."
Rappoport J.Z., Taha B.W., Lemeer S., Benmerah A., Simon S.M.
J. Biol. Chem. 278:47357-47360(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[10]"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.
[11]"Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference."
Huang F., Khvorova A., Marshall W., Sorkin A.
J. Biol. Chem. 279:16657-16661(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[12]"Functional dissection of an AP-2 beta2 appendage-binding sequence within the autosomal recessive hypercholesterolemia protein."
Mishra S.K., Keyel P.A., Edeling M.A., Dupin A.L., Owen D.J., Traub L.M.
J. Biol. Chem. 280:19270-19280(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LDLRAP1, MUTAGENESIS OF TRP-841 AND TYR-888.
[13]"Endocytosis of the glucose transporter GLUT8 is mediated by interaction of a dileucine motif with the beta2-adaptin subunit of the AP-2 adaptor complex."
Schmidt U., Briese S., Leicht K., Schuermann A., Joost H.-G., Al-Hasani H.
J. Cell Sci. 119:2321-2331(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH SLC2A8.
[14]"ARF6 regulates angiotensin II type 1 receptor endocytosis by controlling the recruitment of AP-2 and clathrin."
Poupart M.-E., Fessart D., Cotton M., Laporte S.A., Claing A.
Cell. Signal. 19:2370-2378(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ARF6.
[15]"Src-dependent phosphorylation of beta2-adaptin dissociates the beta-arrestin-AP-2 complex."
Fessart D., Simaan M., Zimmerman B., Comeau J., Hamdan F.F., Wiseman P.W., Bouvier M., Laporte S.A.
J. Cell Sci. 120:1723-1732(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-737, INTERACTION WITH ARRB1.
[16]"The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway."
Lau A.W., Chou M.M.
J. Cell Sci. 121:4008-4017(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
[17]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"c-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway."
Zimmerman B., Simaan M., Lee M.-H., Luttrell L.M., Laporte S.A.
Cell. Signal. 21:103-110(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-737.
[19]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[20]"The connecdenn family, Rab35 guanine nucleotide exchange factors interfacing with the clathrin machinery."
Marat A.L., McPherson P.S.
J. Biol. Chem. 285:10627-10637(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DENND1B, MUTAGENESIS OF TRP-841; GLU-849; TYR-888 AND GLU-902.
[21]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning."
Umasankar P.K., Sanker S., Thieman J.R., Chakraborty S., Wendland B., Tsang M., Traub L.M.
Nat. Cell Biol. 14:488-501(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FCHO1.
[23]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[24]"The structure and function of the beta 2-adaptin appendage domain."
Owen D.J., Vallis Y., Pearse B.M.F., McMahon H.T., Evans P.R.
EMBO J. 19:4216-4227(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 701-937, MUTAGENESIS OF ARG-879; TYR-888 AND LYS-917, INTERACTION WITH EPN1; EPS15; SNAP91 AND CLTC.
[25]"Molecular architecture and functional model of the endocytic AP2 complex."
Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.
Cell 109:523-535(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-591 IN COMPLEX WITH AP2A2; AP2M1; AP2S1 AND AN INOSITOL POLYPHOSPHATE HEADGROUP.
[26]"Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly."
Edeling M.A., Mishra S.K., Keyel P.A., Steinhauser A.L., Collins B.M., Roth R., Heuser J.E., Owen D.J., Traub L.M.
Dev. Cell 10:329-342(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 701-937 IN COMPLEX WITH LDLRAP1, INTERACTION WITH ARRB1; EPN1; SNAP91; AMPH AND BIN1, MUTAGENESIS OF TYR-815; TRP-841; GLU-849; TYR-888 AND GLU-902.
[27]"Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly."
Schmid E.M., Ford M.G.J., Burtey A., Praefcke G.J.K., Peak-Chew S.-Y., Mills I.G., Benmerah A., McMahon H.T.
PLoS Biol. 4:E262-E262(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 700-937 IN COMPLEX WITH EPS15, X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 700-937 IN COMPLEX WITH ARRB1, INTERACTION WITH SCYL1; SCYL2; EPS15; AMPH; SNAP91; ARRB1 AND LDLRAP1, MUTAGENESIS OF TYR-815; TRP-841; LYS-842; GLN-851; ARG-879 AND TYR-888.
[28]"A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex."
Kelly B.T., McCoy A.J., Spaete K., Miller S.E., Evans P.R., Hoening S., Owen D.J.
Nature 456:976-979(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 1-591 IN COMPLEX WITH AP2A2; AP2M1; AP2S1 AND CD4 INTERNALIZATION SIGNAL.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M34175 mRNA. Translation: AAA35583.1.
AY341427 mRNA. Translation: AAQ20044.1.
AC004134 Genomic DNA. No translation available.
AC006237 Genomic DNA. No translation available.
AC015911 Genomic DNA. No translation available.
CH471147 Genomic DNA. Translation: EAW80133.1.
CH471147 Genomic DNA. Translation: EAW80139.1.
BC006201 mRNA. Translation: AAH06201.1.
PIRA35553.
RefSeqNP_001025177.1. NM_001030006.1.
NP_001273.1. NM_001282.2.
XP_005257994.1. XM_005257937.1.
XP_005257995.1. XM_005257938.1.
UniGeneHs.514819.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E42X-ray1.70A/B701-937[»]
2G30X-ray1.60A701-937[»]
2IV8X-ray2.80A700-937[»]
2IV9X-ray1.90A/B700-937[»]
2JKRX-ray2.98B/E1-591[»]
2JKTX-ray3.40B/E1-591[»]
2VGLX-ray2.59B1-591[»]
2XA7X-ray3.10B1-592[»]
ProteinModelPortalP63010.
SMRP63010. Positions 4-582, 705-937.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106672. 55 interactions.
DIPDIP-33098N.
IntActP63010. 38 interactions.
MINTMINT-256705.
STRING9606.ENSP00000314414.

PTM databases

PhosphoSiteP63010.

Polymorphism databases

DMDM51702211.

Proteomic databases

PaxDbP63010.
PRIDEP63010.

Protocols and materials databases

DNASU163.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000262325; ENSP00000262325; ENSG00000006125. [P63010-1]
ENST00000312678; ENSP00000314414; ENSG00000006125. [P63010-2]
ENST00000537622; ENSP00000437413; ENSG00000006125. [P63010-2]
ENST00000538556; ENSP00000440563; ENSG00000006125. [P63010-3]
ENST00000589344; ENSP00000467883; ENSG00000006125. [P63010-2]
ENST00000603960; ENSP00000474789; ENSG00000270478. [P63010-2]
ENST00000604032; ENSP00000474511; ENSG00000270478. [P63010-2]
ENST00000604035; ENSP00000474943; ENSG00000270478. [P63010-3]
ENST00000604623; ENSP00000474435; ENSG00000270478. [P63010-1]
ENST00000605645; ENSP00000474277; ENSG00000270478. [P63010-2]
GeneID163.
KEGGhsa:163.
UCSCuc002hjq.3. human. [P63010-2]
uc002hjr.3. human. [P63010-1]

Organism-specific databases

CTD163.
GeneCardsGC17P033914.
HGNCHGNC:563. AP2B1.
HPACAB017631.
HPA056733.
MIM601025. gene.
neXtProtNX_P63010.
PharmGKBPA24854.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5096.
HOGENOMHOG000163270.
HOVERGENHBG050515.
KOK11825.
OMAYMDMTFT.
OrthoDBEOG7BGHK0.
PhylomeDBP63010.
TreeFamTF300318.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_13685. Neuronal System.
REACT_6900. Immune System.
SignaLinkP63010.

Gene expression databases

ArrayExpressP63010.
BgeeP63010.
CleanExHS_AP2B1.
GenevestigatorP63010.

Family and domain databases

Gene3D1.25.10.10. 1 hit.
2.60.40.1150. 1 hit.
3.30.310.10. 1 hit.
InterProIPR026739. 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]
PANTHERPTHR11134. PTHR11134. 1 hit.
PfamPF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
PF09066. B2-adapt-app_C. 1 hit.
[Graphical view]
PIRSFPIRSF002291. AP_complex_beta. 1 hit.
SMARTSM00809. Alpha_adaptinC2. 1 hit.
SM01020. B2-adapt-app_C. 1 hit.
[Graphical view]
SUPFAMSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAP2B1. human.
EvolutionaryTraceP63010.
GeneWikiAP2B1.
GenomeRNAi163.
NextBio653.
PROP63010.
SOURCESearch...

Entry information

Entry nameAP2B1_HUMAN
AccessionPrimary (citable) accession number: P63010
Secondary accession number(s): A6NJP3 expand/collapse secondary AC list , P21851, Q7Z451, Q96J19
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM