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Protein

AP-2 complex subunit beta

Gene

Ap2b1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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 similarity2 Publications

GO - Molecular functioni

  • clathrin binding Source: BHF-UCL
  • protein complex binding Source: RGD
  • protein transporter activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-RNO-177504. Retrograde neurotrophin signalling.
R-RNO-182971. EGFR downregulation.
R-RNO-2132295. MHC class II antigen presentation.
R-RNO-416993. Trafficking of GluR2-containing AMPA receptors.
R-RNO-437239. Recycling pathway of L1.
R-RNO-5099900. 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
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi71048. Ap2b1.

Subcellular locationi

GO - Cellular componenti

  • AP-type membrane coat adaptor complex Source: ProtInc
  • clathrin adaptor complex Source: InterPro
  • clathrin coat Source: BHF-UCL
  • coated pit Source: UniProtKB-SubCell
  • plasma membrane Source: UniProtKB-SubCell
  • trans-Golgi network Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi756 – 7561Q → A: Abolishes interaction with PIP5K1C. 1 Publication
Mutagenesisi804 – 8041Q → A: Abolishes interaction with PIP5K1C. 1 Publication
Mutagenesisi806 – 8061A → F: Abolishes interaction with PIP5K1C. 1 Publication
Mutagenesisi808 – 8081K → E: Abolishes interaction with PIP5K1C. 1 Publication
Mutagenesisi815 – 8151Y → A: Abolishes interaction with PIP5K1C. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 937936AP-2 complex subunit betaPRO_0000193744Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei265 – 2651N6-acetyllysineBy similarity
Modified residuei737 – 7371PhosphotyrosineBy similarity
Modified residuei928 – 9281PhosphotyrosineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP62944.
PRIDEiP62944.

PTM databases

iPTMnetiP62944.
PhosphoSiteiP62944.

Expressioni

Gene expression databases

GenevisibleiP62944. RN.

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 (By similarity). Interacts with PIP5K1C; clathrin competes with PIP5K1C. Interacts with DENND1B (By similarity). Interacts with FCHO1.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
NumbQ3MUI12EBI-7008032,EBI-7007865

GO - Molecular functioni

  • clathrin binding Source: BHF-UCL
  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi250830. 23 interactions.
DIPiDIP-40944N.
IntActiP62944. 4 interactions.
MINTiMINT-122517.
STRINGi10116.ENSRNOP00000013629.

Structurei

Secondary structure

1
937
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi712 – 7154Combined sources
Helixi717 – 7193Combined sources
Turni720 – 7223Combined sources
Beta strandi723 – 73210Combined sources
Beta strandi735 – 74410Combined sources
Beta strandi746 – 7483Combined sources
Beta strandi754 – 7574Combined sources
Beta strandi765 – 7684Combined sources
Beta strandi781 – 79010Combined sources
Beta strandi802 – 8087Combined sources
Beta strandi813 – 8197Combined sources
Helixi822 – 8254Combined sources
Helixi834 – 84310Combined sources
Helixi846 – 8483Combined sources
Beta strandi850 – 8545Combined sources
Helixi861 – 87010Combined sources
Beta strandi874 – 8818Combined sources
Beta strandi884 – 89310Combined sources
Beta strandi898 – 9058Combined sources
Beta strandi912 – 9176Combined sources
Helixi921 – 9233Combined sources
Helixi924 – 93512Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H1ZX-ray1.83A701-937[»]
3HS9X-ray2.15A701-937[»]
ProteinModelPortaliP62944.
SMRiP62944. Positions 4-582, 705-937.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62944.

Family & Domainsi

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1061. Eukaryota.
COG5096. LUCA.
GeneTreeiENSGT00530000063138.
HOGENOMiHOG000163270.
HOVERGENiHBG050515.
InParanoidiP62944.
KOiK11825.
OMAiCHLNADA.
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.
IPR000225. Armadillo.
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.
SM00185. ARM. 2 hits.
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. AlignAdd to basket

Isoform 1 (identifier: P62944-1) [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

        10         20         30         40         50
MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL
60 70 80 90 100
FPDVVNCMQT DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP
110 120 130 140 150
LIRALAVRTM GCIRVDKITE YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD
160 170 180 190 200
INAQMVEDQG FLDSLRDLIA DSNPMVVANA VAALSEISES HPNSNLLDLN
210 220 230 240 250
PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI CERVTPRLSH
260 270 280 290 300
ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY
310 320 330 340 350
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN
360 370 380 390 400
IAQVLAELKE YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ
410 420 430 440 450
TKVNYVVQEA IVVIRDIFRK YPNKYESIIA TLCENLDSLD EPDARAAMIW
460 470 480 490 500
IVGEYAERID NADELLESFL EGFHDESTQV QLTLLTAIVK LFLKKPSETQ
510 520 530 540 550
ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV VLSEKPLISE
560 570 580 590 600
ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST
610 620 630 640 650
DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM
660 670 680 690 700
GAVDLLGGGL DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI
710 720 730 740 750
GMAPGGYVAP KAVWLPAVKA KGLEISGTFT HRQGHIYMEM NFTNKALQHM
760 770 780 790 800
TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ SIDVSLPLNT LGPVMKMEPL
810 820 830 840 850
NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT WKDIPNENEL
860 870 880 890 900
QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL
910 920 930
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN
Length:937
Mass (Da):104,553
Last modified:August 31, 2004 - v1
Checksum:iB472EE5B2AE176DF
GO
Isoform 2 (identifier: P62944-2) [UniParc]FASTAAdd to basket

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

Note: Brain specific.
Show »
Length:951
Mass (Da):105,692
Checksum:i3199C9F8C7F027F2
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei663 – 6631L → LLGSDLGGGIGGSPA in isoform 2. 1 PublicationVSP_011492

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34176 mRNA. Translation: AAA40797.1.
M77246 mRNA. Translation: AAA40808.1.
PIRiC35553.
RefSeqiNP_542150.1. NM_080583.1. [P62944-2]
XP_008766157.1. XM_008767935.1. [P62944-2]
XP_008766158.1. XM_008767936.1. [P62944-2]
XP_008766159.1. XM_008767937.1. [P62944-2]
XP_008766160.1. XM_008767938.1. [P62944-2]
XP_008766161.1. XM_008767939.1. [P62944-1]
UniGeneiRn.56138.

Genome annotation databases

EnsembliENSRNOT00000085799; ENSRNOP00000072290; ENSRNOG00000061543. [P62944-1]
ENSRNOT00000088198; ENSRNOP00000070905; ENSRNOG00000061543. [P62944-2]
ENSRNOT00000090446; ENSRNOP00000073619; ENSRNOG00000061543. [P62944-2]
GeneIDi140670.
KEGGirno:140670.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M34176 mRNA. Translation: AAA40797.1.
M77246 mRNA. Translation: AAA40808.1.
PIRiC35553.
RefSeqiNP_542150.1. NM_080583.1. [P62944-2]
XP_008766157.1. XM_008767935.1. [P62944-2]
XP_008766158.1. XM_008767936.1. [P62944-2]
XP_008766159.1. XM_008767937.1. [P62944-2]
XP_008766160.1. XM_008767938.1. [P62944-2]
XP_008766161.1. XM_008767939.1. [P62944-1]
UniGeneiRn.56138.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3H1ZX-ray1.83A701-937[»]
3HS9X-ray2.15A701-937[»]
ProteinModelPortaliP62944.
SMRiP62944. Positions 4-582, 705-937.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250830. 23 interactions.
DIPiDIP-40944N.
IntActiP62944. 4 interactions.
MINTiMINT-122517.
STRINGi10116.ENSRNOP00000013629.

PTM databases

iPTMnetiP62944.
PhosphoSiteiP62944.

Proteomic databases

PaxDbiP62944.
PRIDEiP62944.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000085799; ENSRNOP00000072290; ENSRNOG00000061543. [P62944-1]
ENSRNOT00000088198; ENSRNOP00000070905; ENSRNOG00000061543. [P62944-2]
ENSRNOT00000090446; ENSRNOP00000073619; ENSRNOG00000061543. [P62944-2]
GeneIDi140670.
KEGGirno:140670.

Organism-specific databases

CTDi163.
RGDi71048. Ap2b1.

Phylogenomic databases

eggNOGiKOG1061. Eukaryota.
COG5096. LUCA.
GeneTreeiENSGT00530000063138.
HOGENOMiHOG000163270.
HOVERGENiHBG050515.
InParanoidiP62944.
KOiK11825.
OMAiCHLNADA.
OrthoDBiEOG7BGHK0.
TreeFamiTF300318.

Enzyme and pathway databases

ReactomeiR-RNO-177504. Retrograde neurotrophin signalling.
R-RNO-182971. EGFR downregulation.
R-RNO-2132295. MHC class II antigen presentation.
R-RNO-416993. Trafficking of GluR2-containing AMPA receptors.
R-RNO-437239. Recycling pathway of L1.
R-RNO-5099900. WNT5A-dependent internalization of FZD4.

Miscellaneous databases

EvolutionaryTraceiP62944.
PROiP62944.

Gene expression databases

GenevisibleiP62944. RN.

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.
IPR000225. Armadillo.
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.
SM00185. ARM. 2 hits.
SM01020. B2-adapt-app_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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: Lymphocyte.
  2. "Structural and functional division into two domains of the large (100- to 115-kDa) chains of the clathrin-associated protein complex AP-2."
    Kirchhausen T., Nathanson K.L., Matsui W., Vaisberg A., Chow E.P., Burne C., Keen J.H., Davis A.E.
    Proc. Natl. Acad. Sci. U.S.A. 86:2612-2616(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Brain.
  3. "The alpha chain of the AP-2 adaptor is a clathrin binding subunit."
    Goodman O.B. Jr., Keen J.H.
    J. Biol. Chem. 270:23768-23773(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CLATHRIN.
  4. "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.
  5. "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.
  6. "Clathrin regulates the association of PIPKIgamma661 with the AP-2 adaptor beta2 appendage."
    Thieman J.R., Mishra S.K., Ling K., Doray B., Anderson R.A., Traub L.M.
    J. Biol. Chem. 284:13924-13939(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIP5K1C, MUTAGENESIS OF GLN-756; GLN-804; ALA-806; LYS-808 AND TYR-815.
  7. "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.
  8. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-928, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiAP2B1_RAT
AccessioniPrimary (citable) accession number: P62944
Secondary accession number(s): P21851
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: July 6, 2016
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

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.