Details for: AP2B1

Gene ID: 163

Symbol: AP2B1

Ensembl ID: ENSG00000006125

Description: adaptor related protein complex 2 subunit beta 1

Associated with

Other Information

Genular Protein ID: 2912025322

Symbol: AP2B1_HUMAN

Name: AP-2 complex subunit beta

UniProtKB Accession Codes:

P63010 A6NJP3 P21851 Q7Z451 Q96J19

Database IDs:

AGR 1 AlphaFoldDB 1 Antibodypedia 1 Bgee 1 BioGRID 1 BioGRID-ORCS 1 BioMuta 1 CCDS 2 CORUM 1 CTD 1 ChiTaRS 1 ComplexPortal 2 DIP 1 DMDM 1 DNASU 1 DisGeNET 1 EMBL 8 EMDB 6 EPD 1 Ensembl 3 EvolutionaryTrace 1 ExpressionAtlas 1 GO 24 Gene3D 3 GeneCards 1 GeneTree 1 GeneWiki 1 Genevisible 1 GenomeRNAi 1 GlyCosmos 1 GlyGen 1 HGNC 1 HPA 1 InParanoid 1 IntAct 1 InterPro 12 KEGG 1 MANE-Select 1 MIM 1 MINT 1 MassIVE 1 MaxQB 1 MetOSite 1 NCBI Taxonomy 1 OMA 1 OpenTargets 1 OrthoDB 1 PANTHER 2 PDB 27 PDBsum 22 PIR 1 PIRSF 1 PRO 1 PathwayCommons 1 PaxDb 1 PeptideAtlas 1 Pfam 3 PharmGKB 1 Pharos 1 PhosphoSitePlus 1 PhylomeDB 1 Proteomes 1 ProteomicsDB 3 Pumba 1 RNAct 1 Reactome 14 RefSeq 7 SIGNOR 1 SMART 3 SMR 1 STRING 1 SUPFAM 3 SignaLink 1 SwissPalm 1 TCDB 1 TreeFam 1 UCSC 1 UniProtKB 1 VEuPathDB 1 eggNOG 1 iPTMnet 1 jPOST 1 neXtProt 1

Citations:

PubMed ID: 1969413

Title: Conservation and diversity in families of coated vesicle adaptins.

PubMed ID: 1969413

DOI: 10.1016/s0021-9258(19)34045-1

PubMed ID: 15897975

Title: Expression of a novel beta adaptin subunit mRNA splice variant in human testes.

PubMed ID: 15897975

DOI: 10.1111/j.1745-7262.2005.00025.x

PubMed ID: 16625196

Title: DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage.

PubMed ID: 16625196

DOI: 10.1038/nature04689

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 11777907

Title: beta-Arrestin/AP-2 interaction in G protein-coupled receptor internalization: identification of a beta-arrestin binding site in beta 2-adaptin.

PubMed ID: 11777907

DOI: 10.1074/jbc.m108490200

PubMed ID: 12429842

Title: Transforming growth factor-beta receptors interact with AP2 by direct binding to beta2 subunit.

PubMed ID: 12429842

DOI: 10.1091/mbc.02-07-0104

PubMed ID: 14745134

Title: Adaptor protein complexes as the key regulators of protein sorting in the post-Golgi network.

PubMed ID: 14745134

DOI: 10.1247/csf.28.419

PubMed ID: 14530274

Title: The AP-2 complex is excluded from the dynamic population of plasma membrane-associated clathrin.

PubMed ID: 14530274

DOI: 10.1074/jbc.c300390200

PubMed ID: 15473838

Title: Adaptors for clathrin coats: structure and function.

PubMed ID: 15473838

DOI: 10.1146/annurev.cellbio.20.010403.104543

PubMed ID: 14985334

Title: Analysis of clathrin-mediated endocytosis of epidermal growth factor receptor by RNA interference.

PubMed ID: 14985334

DOI: 10.1074/jbc.c400046200

PubMed ID: 15728179

Title: Functional dissection of an AP-2 beta2 appendage-binding sequence within the autosomal recessive hypercholesterolemia protein.

PubMed ID: 15728179

DOI: 10.1074/jbc.m501029200

PubMed ID: 16723738

Title: 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.

PubMed ID: 16723738

DOI: 10.1242/jcs.02943

PubMed ID: 17719203

Title: ARF6 regulates angiotensin II type 1 receptor endocytosis by controlling the recruitment of AP-2 and clathrin.

PubMed ID: 17719203

DOI: 10.1016/j.cellsig.2007.07.015

PubMed ID: 17456551

Title: Src-dependent phosphorylation of beta2-adaptin dissociates the beta-arrestin-AP-2 complex.

PubMed ID: 17456551

DOI: 10.1242/jcs.03444

PubMed ID: 19033387

Title: The adaptor complex AP-2 regulates post-endocytic trafficking through the non-clathrin Arf6-dependent endocytic pathway.

PubMed ID: 19033387

DOI: 10.1242/jcs.033522

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18938240

Title: c-Src-mediated phosphorylation of AP-2 reveals a general mechanism for receptors internalizing through the clathrin pathway.

PubMed ID: 18938240

DOI: 10.1016/j.cellsig.2008.09.013

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20154091

Title: The connecdenn family, Rab35 guanine nucleotide exchange factors interfacing with the clathrin machinery.

PubMed ID: 20154091

DOI: 10.1074/jbc.m109.050930

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 22484487

Title: Distinct and separable activities of the endocytic clathrin-coat components Fcho1/2 and AP-2 in developmental patterning.

PubMed ID: 22484487

DOI: 10.1038/ncb2473

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23676497

Title: Endocytosis of synaptic ADAM10 in neuronal plasticity and Alzheimer's disease.

PubMed ID: 23676497

DOI: 10.1172/jci65401

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 25944712

Title: N-terminome analysis of the human mitochondrial proteome.

PubMed ID: 25944712

DOI: 10.1002/pmic.201400617

PubMed ID: 27022195

Title: Raftlin controls lipopolysaccharide-induced TLR4 internalization and TICAM-1 signaling in a cell type-specific manner.

PubMed ID: 27022195

DOI: 10.4049/jimmunol.1501734

PubMed ID: 29262337

Title: APache is an AP2-interacting protein involved in synaptic vesicle trafficking and neuronal development.

PubMed ID: 29262337

DOI: 10.1016/j.celrep.2017.11.073

PubMed ID: 10944104

Title: The structure and function of the beta 2-adaptin appendage domain.

PubMed ID: 10944104

DOI: 10.1093/emboj/19.16.4216

PubMed ID: 12086608

Title: Molecular architecture and functional model of the endocytic AP2 complex.

PubMed ID: 12086608

DOI: 10.1016/s0092-8674(02)00735-3

PubMed ID: 16516836

Title: Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly.

PubMed ID: 16516836

DOI: 10.1016/j.devcel.2006.01.016

PubMed ID: 16903783

Title: Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly.

PubMed ID: 16903783

DOI: 10.1371/journal.pbio.0040262

PubMed ID: 19140243

Title: A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex.

PubMed ID: 19140243

DOI: 10.1038/nature07422

Sequence Information:

  • Length: 937
  • Mass: 104553
  • Checksum: B472EE5B2AE176DF
  • Sequence:
    • MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT 
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE 
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA 
VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI 
CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY 
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE 
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK 
YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV 
QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV 
VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST 
DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL 
DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI GMAPGGYVAP KAVWLPAVKA 
KGLEISGTFT HRQGHIYMEM NFTNKALQHM TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ 
SIDVSLPLNT LGPVMKMEPL NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT 
WKDIPNENEL QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL 
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN

Genular Protein ID: 4071329008

Symbol: Q96EL6_HUMAN

Name: N/A

UniProtKB Accession Codes:

Q96EL6

Database IDs:

ARBA 4 AlphaFoldDB 1 BioGRID-ORCS 1 CTD 1 DNASU 1 EMBL 2 GO 5 Gene3D 3 Genevisible 1 GenomeRNAi 1 Google 1 InterPro 10 NCBI Taxonomy 1 OrthoDB 1 PANTHER 2 PeptideAtlas 1 Pfam 3 PharmGKB 1 RefSeq 1 SMART 4 SUPFAM 3

Sequence Information:

  • Length: 556
  • Mass: 61083
  • Checksum: 9B1818042C855A32
  • Sequence:
    • LDLIQTKVNY VVQEAIVVIR DIFRKYPNKY ESIIATLCEN LDSLDEPDAR AAMIWIVGEY 
AERIDNADEL LESFLEGFHD ESTQVQLTLL TAIVKLFLKK PSETQELVQQ VLSLATQDSD 
NPDLRDRGYI YWRLLSTDPV TAKEVVLSEK PLISEETDLI EPTLLDELIC HIGSLASVYH 
KPPNAFVEGS HGIHRKHLPI HHGSTDAGDS PVGTTTATNL EQPQVIPSQG DLLGDLLNLD 
LGPPVNVPQV SSMQMGAVDL LGGGLDSLLG SDLGGGIGGS PAVGQSFIPS SVPATFAPSP 
TPAVVSSGLN DLFELSTGIG MAPGGYVAPK AVWLPAVKAK GLEISGTFTH RQGHIYMEMN 
FTNKALQHMT DFAIQFNKNS FGVIPSTPLA IHTPLMPNQS IDVSLPLNTL GPVMKMEPLN 
NLQVAVKNNI DVFYFSCLIP LNVLFVEDGK MERQVFLATW KDIPNENELQ FQIKECHLNA 
DTVSSKLQNN NVYTIAKRNV EGQDMLYQSL KLTNGIWILA ELRIQPGNPN YTLSLKCRAP 
EVSQYIYQVY DSILKN

Genular Protein ID: 2391871084

Symbol: A0A140VJE8_HUMAN

Name: N/A

UniProtKB Accession Codes:

A0A140VJE8

Database IDs:

ARBA 5 AlphaFoldDB 1 Antibodypedia 1 BioGRID-ORCS 1 CTD 1 ChiTaRS 1 DNASU 1 EMBL 4 ExpressionAtlas 1 GO 11 Gene3D 3 GenomeRNAi 1 IntAct 1 InterPro 12 NCBI Taxonomy 1 OMA 1 OrthoDB 1 PANTHER 2 PIRNR 1 PIRSF 1 Pfam 3 RefSeq 3 SMART 5 SMR 1 SUPFAM 3 VEuPathDB 1

Citations:

PubMed ID: 11181995

Title: The sequence of the human genome.

PubMed ID: 11181995

DOI: 10.1126/science.1058040

Sequence Information:

  • Length: 951
  • Mass: 105692
  • Checksum: 3199C9F8C7F027F2
  • Sequence:
    • MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL FPDVVNCMQT 
DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP LIRALAVRTM GCIRVDKITE 
YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD INAQMVEDQG FLDSLRDLIA DSNPMVVANA 
VAALSEISES HPNSNLLDLN PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI 
CERVTPRLSH ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY 
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN IAQVLAELKE 
YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ TKVNYVVQEA IVVIRDIFRK 
YPNKYESIIA TLCENLDSLD EPDARAAMIW IVGEYAERID NADELLESFL EGFHDESTQV 
QLTLLTAIVK LFLKKPSETQ ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV 
VLSEKPLISE ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST 
DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM GAVDLLGGGL 
DSLLGSDLGG GIGGSPAVGQ SFIPSSVPAT FAPSPTPAVV SSGLNDLFEL STGIGMAPGG 
YVAPKAVWLP AVKAKGLEIS GTFTHRQGHI YMEMNFTNKA LQHMTDFAIQ FNKNSFGVIP 
STPLAIHTPL MPNQSIDVSL PLNTLGPVMK MEPLNNLQVA VKNNIDVFYF SCLIPLNVLF 
VEDGKMERQV FLATWKDIPN ENELQFQIKE CHLNADTVSS KLQNNNVYTI AKRNVEGQDM 
LYQSLKLTNG IWILAELRIQ PGNPNYTLSL KCRAPEVSQY IYQVYDSILK N

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.