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InterPro: IPR016342 Adaptor protein complex, beta subunit

Protein matches Help

UniProtKB

Matches:

318 proteins

Overview:	sorted by AC,	sorted by name,	of known structure,	proteins with splice variants
Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
Architectures
Accession List
Matches in BioMart

Accession

IPR016342 AP_complex_bsu

Type

Family

Signatures Help

Database	ID	Name	Proteins
PIRSF	PIRSF002291	AP_complex_beta	318
Signatures in BioMart

InterPro Relationships Help

Contains

IPR002553 Clathrin/coatomer adaptor, adaptin-like, N-terminal
IPR011989 Armadillo-like helical
IPR013037 Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain

GO Term annotation Help

Process

GO:0015031 protein transport

Function

GO:0005515 protein binding
GO:0008565 protein transporter activity

InterPro annotation

Entry Details in BioMart

Abstract

The adaptor protein complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules. Adaptor protein complex 1 (AP-1) is a heterotetramer composed of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Subunits of clathrin-associated adaptor protein complex 1 play a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or in endosomes.

This group represents an adaptor protein complex, beta subunit.

Structural links Help

PDB - click here

SCOP: b.1.10.1 , i.23.1.1

CATH: 1.25.10.10 , 2.60.40.1150

Database links Help

CluSTr: ALLvsALL:46025:80.7

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR016342

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

O35643 AP-1 complex subunit beta-1

O43005 AP-2 complex subunit beta

P27351 AP-2 complex subunit beta

P52303 AP-1 complex subunit beta-1

P63010 AP-2 complex subunit beta

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR008152	Clathrin adaptor, alpha/beta/gamma-adaptin, appendage, Ig-like subdomain
IPR002553	Clathrin/coatomer adaptor, adaptin-like, N-terminal
IPR012295	Beta2-adaptin/TATA-box binding, C-terminal
IPR016024	Armadillo-type fold
IPR016342	Adaptor protein complex, beta subunit
IPR011989	Armadillo-like helical
IPR013041	Clathrin/coatomer adaptor, adaptin-like, appendage, Ig-like subdomain
IPR009028	Clathrin/coatomer adaptor, adaptin-like, appendage, C-terminal subdomain
IPR015151	Clathrin adaptor, beta-adaptin, appendage, C-terminal subdomain
IPR013037	Clathrin adaptor, beta-adaptin, appendage, Ig-like subdomain
	PDB Chain
	ModBase
	CATH Domain
	SWISS-MODEL
	SCOP Domain

Publications Help

Additional Reading Open in usermanual
	Heldwein EE, Macia E, Wang J, Yin HL, Kirchhausen T, Harrison SC. Crystal structure of the clathrin adaptor protein 1 core. Proc. Natl. Acad. Sci. U.S.A. 101 2004 14108-13 [PubMed: 15377783] http://dx.doi.org/10.1073/pnas.0406102101
	Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ. Molecular architecture and functional model of the endocytic AP2 complex. Cell 109 2002 523-35 [PubMed: 12086608] http://dx.doi.org/10.1016/S0092-8674(02)00735-3
	Edeling MA, Mishra SK, Keyel PA, Steinhauser AL, Collins BM, Roth R, Heuser JE, Owen DJ, Traub LM. Molecular switches involving the AP-2 beta2 appendage regulate endocytic cargo selection and clathrin coat assembly. Dev. Cell 10 2006 329-42 [PubMed: 16516836] http://dx.doi.org/10.1016/j.devcel.2006.01.016
	Schmid EM, Ford MG, Burtey A, Praefcke GJ, Peak-Chew SY, Mills IG, Benmerah A, McMahon HT. Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly. PLoS Biol. 4 2006 e262 [PubMed: 16903783] http://dx.doi.org/10.1371/journal.pbio.0040262
	Owen DJ, Vallis Y, Pearse BM, McMahon HT, Evans PR. The structure and function of the beta 2-adaptin appendage domain. EMBO J. 19 2000 4216-27 [PubMed: 10944104] http://dx.doi.org/10.1093/emboj/19.16.4216

InterPro 23.1