P63010 (AP2B1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
AP-2 complex subunit beta

Alternative name(s):
AP105B
Adapter-related protein complex 2 beta subunit
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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	937 AA.
Sequence status	Complete.
Protein existence	Evidence 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 surrrounded 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.7 Ref.9 Ref.10 Ref.17
Subunit structure	Adaptor protein complex 2 (AP-2) is an 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. Ref.5 Ref.6 Ref.11 Ref.13 Ref.15 Ref.16 Ref.22 Ref.24 Ref.26 Ref.27
Subcellular location	Cell membrane. Membrane › coated 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.8
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 process	Protein transport Transport
Cellular component	Cell membrane Coated pit Membrane
Coding sequence diversity	Alternative splicing
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	axon guidance Traceable author statement. Source: Reactome 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 nerve growth factor 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 vesicle-mediated transport Inferred from electronic annotation. Source: InterPro viral reproduction Traceable author statement. Source: Reactome
Cellular component	clathrin adaptor complex Inferred from electronic annotation. Source: InterPro coated pit Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome endocytic vesicle membrane Traceable author statement. Source: Reactome plasma membrane Traceable author statement. Source: Reactome
Molecular function	clathrin binding Inferred from physical interaction. Source: UniProtKB protein transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
Ap2m1	P84092	2	EBI-432924,EBI-297693	From a different organism.
MEA1	Q16626	2	EBI-432924,EBI-744921

Alternative products

This entry describes 2 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 937

937

AP-2 complex subunit beta

PRO_0000193742

Regions

Region

841 – 937

97

Interaction with ARRB1

Compositional bias

576 – 716

141

Pro-rich (stalk region)

Amino acid modifications

Modified residue

2

1

Phosphothreonine Ref.18

Modified residue

4

1

Phosphoserine Ref.18

Modified residue

265

1

N6-acetyllysine Ref.21

Modified residue

276

1

Phosphotyrosine Ref.20

Modified residue

318

1

N6-acetyllysine Ref.21

Modified residue

737

1

Phosphotyrosine; by SRC Ref.12 Ref.14 Ref.16 Ref.19

Modified residue

888

1

Phosphotyrosine Ref.14

Natural variations

Alternative sequence

663

1

L → LLGSDLGGGIGGSPA in isoform 2.

VSP_011490

Experimental info

Mutagenesis

815

1

Y → A: Strongly reduces interaction with SNAP91, EPS15, AMPH and BIN1 and clathrin heavy chain. Ref.26 Ref.27

Mutagenesis

841

1

W → A: Abolishes interaction with LDLRAP1 and ARRB1. Greatly reduces DENND1B-binding. Ref.11 Ref.22 Ref.26 Ref.27

Mutagenesis

842

1

K → E: Strongly reduces interaction with ARRB1. Ref.27

Mutagenesis

849

1

E → A: Strongly reduces interaction with LDLRAP1, ARRB1 and EPN1. No effect on DENND1B-binding. Ref.5 Ref.22 Ref.26

Mutagenesis

851

1

Q → A: Strongly reduces interaction with ARRB1. Ref.27

Mutagenesis

879

1

R → A: No effect on interaction with ARRB1. Ref.24 Ref.27

Mutagenesis

879

1

R → E: Strongly reduces interaction with EPN1. Reduces interaction with SNAP91 and clathrin. No effect on EPS15 binding. Ref.24 Ref.27

Mutagenesis

888

1

Y → V: Strongly reduces interaction with SNAP91, EPN1 and clathrin. No effect on EPS15 binding. Abolishes interaction with ARRB1 and with DENND1B. Ref.11 Ref.22 Ref.24 Ref.26 Ref.27

Mutagenesis

902

1

E → A: Strongly reduces interaction with LDLRAP1 and ARRB1. No effect on DENND1B-binding. Ref.5 Ref.22 Ref.26

Mutagenesis

917

1

K → Q: Strongly reduces interaction with LDLRAP1. SNAP91 and clathrin. Reduces interaction with EPN1. No effect on EPS15 binding. Ref.24

Secondary structure

1

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937

Helix Strand Turn

Details...

Beta strand

11 – 13

3

Helix

14 – 23

10

Helix

27 – 43

17

Helix

48 – 50

3

Helix

51 – 56

6

Beta strand

58 – 61

4

Helix

63 – 78

16

Helix

81 – 85

5

Helix

88 – 91

4

Helix

92 – 94

3

Beta strand

97 – 99

3

Helix

100 – 111

12

Helix

119 – 129

11

Helix

135 – 148

14

Helix

158 – 167

10

Helix

174 – 187

14

Helix

200 – 213

14

Helix

216 – 226

11

Helix

234 – 244

11

Helix

252 – 265

14

Helix

277 – 283

7

Helix

285 – 291

7

Helix

296 – 311

16

Turn

316 – 319

4

Turn

321 – 324

4

Helix

332 – 344

13

Turn

348 – 350

3

Helix

351 – 361

11

Helix

367 – 381

15

Helix

385 – 401

17

Helix

404 – 420

17

Helix

429 – 432

4

Helix

434 – 437

4

Helix

442 – 454

13

Helix

459 – 470

12

Helix

478 – 492

15

Helix

501 – 507

7

Turn

510 – 512

3

Helix

517 – 530

14

Helix

534 – 541

8

Turn

551 – 553

3

Helix

557 – 564

8

Turn

565 – 568

4

Helix

571 – 574

4

Helix

578 – 580

3

Beta strand

712 – 715

4

Helix

717 – 719

3

Turn

720 – 722

3

Beta strand

723 – 732

10

Beta strand

735 – 744

10

Beta strand

746 – 748

3

Beta strand

754 – 757

4

Beta strand

765 – 768

4

Beta strand

781 – 790

10

Beta strand

802 – 808

7

Beta strand

813 – 819

7

Helix

822 – 825

4

Helix

834 – 843

10

Helix

846 – 848

3

Beta strand

850 – 854

5

Helix

861 – 870

10

Beta strand

874 – 881

8

Beta strand

884 – 893

10

Beta strand

898 – 905

8

Beta strand

910 – 920

11

Helix

921 – 923

3

Helix

924 – 936

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified August 31, 2004. Version 1. Checksum: B472EE5B2AE176DF	FASTA	937	104,553
	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
	Isoform 2 [UniParc]. Checksum: 3199C9F8C7F027F2	FASTA	951	105,692
	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 DSLLGSDLGG GIGGSPAVGQ SFIPSSVPAT FAPSPTPAVV SSGLNDLFEL STGIGMAPGG 730 740 750 760 770 780 YVAPKAVWLP AVKAKGLEIS GTFTHRQGHI YMEMNFTNKA LQHMTDFAIQ FNKNSFGVIP 790 800 810 820 830 840 STPLAIHTPL MPNQSIDVSL PLNTLGPVMK MEPLNNLQVA VKNNIDVFYF SCLIPLNVLF 850 860 870 880 890 900 VEDGKMERQV FLATWKDIPN ENELQFQIKE CHLNADTVSS KLQNNNVYTI AKRNVEGQDM 910 920 930 940 950 LYQSLKLTNG IWILAELRIQ PGNPNYTLSL KCRAPEVSQY IYQVYDSILK N

References

	« Hide 'large scale' referencesShow '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: 1969413] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Brain.
[2]	"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. , 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: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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. , 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].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Muscle.
[5]	"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: 11777907] [Abstract] Cited for: INTERACTION WITH ARRB1, MUTAGENESIS OF GLU-849 AND GLU-902.
[6]	"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: 12429842] [Abstract] Cited for: INTERACTION WITH TGFBR1 AND TGFBR2.
[7]	"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: 14745134] [Abstract] Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[8]	"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: 14530274] [Abstract] Cited for: SUBCELLULAR LOCATION.
[9]	"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: 15473838] [Abstract] Cited for: FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[10]	"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: 14985334] [Abstract] Cited for: FUNCTION IN CLATHRIN-MEDIATED ENDOCYTOSIS.
[11]	"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: 15728179] [Abstract] Cited for: INTERACTION WITH LDLRAP1, MUTAGENESIS OF TRP-841 AND TYR-888.
[12]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-737, MASS SPECTROMETRY.
[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: 16723738] [Abstract] Cited for: INTERACTION WITH SLC2A8.
[14]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-737 AND TYR-888, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[15]	"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: 17719203] [Abstract] Cited for: INTERACTION WITH ARF6.
[16]	"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: 17456551] [Abstract] Cited for: PHOSPHORYLATION AT TYR-737, INTERACTION WITH ARRB1.
[17]	"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: 19033387] [Abstract] Cited for: FUNCTION OF THE AP-2 COMPLEX IN NON-CLATHRIN-DEPENDENT ENDOCYTOSIS.
[18]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-2 AND SER-4, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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: 18938240] [Abstract] Cited for: PHOSPHORYLATION AT TYR-737.
[20]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-276, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[21]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-265 AND LYS-318, MASS SPECTROMETRY.
[22]	"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: 20154091] [Abstract] Cited for: INTERACTION WITH DENND1B, MUTAGENESIS OF TRP-841; GLU-849; TYR-888 AND GLU-902.
[23]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [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: 10944104] [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: 12086608] [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: 16516836] [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: 16903783] [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: 18978775] [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.
AC006237 Genomic DNA. No translation available.
CH471147 Genomic DNA. Translation: EAW80133.1.
BC006201 mRNA. Translation: AAH06201.1.

IPI

IPI00784156.
IPI00784366.

PIR

A35553.

RefSeq

NP_001025177.1. NM_001030006.1.
NP_001273.1. NM_001282.2.

UniGene

Hs.514819.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1E42	X-ray	1.70	A/B	701-937	[»]
2G30	X-ray	1.60	A	701-937	[»]
2IV8	X-ray	2.80	A	700-937	[»]
2IV9	X-ray	1.90	A/B	700-937	[»]
2JKR	X-ray	2.98	B/E	1-591	[»]
2JKT	X-ray	3.40	B/E	1-591	[»]
2VGL	X-ray	2.59	B	1-591	[»]
2XA7	X-ray	3.10	B	1-592	[»]

ProteinModelPortal

P63010.

SMR

P63010. Positions 4-582, 705-937.

ModBase

Search...

Protein-protein interaction databases

IntAct

P63010. 32 interactions.

MINT

MINT-256705.

STRING

P63010.

PTM databases

PhosphoSite

P63010.

Polymorphism databases

DMDM

51702211.

Proteomic databases

PRIDE

P63010.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000262325; ENSP00000262325; ENSG00000006125.

GeneID

163.

KEGG

hsa:163.

UCSC

uc002hjq.1. human.
uc002hjr.1. human.

Organism-specific databases

CTD

163.

GeneCards

GC17P033914.

HGNC

HGNC:563. AP2B1.

HPA

CAB017631.

MIM

601025. gene.

neXtProt

NX_P63010.

PharmGKB

PA24854.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG09520.

HOVERGEN

HBG050515.

OMA

DCHLNAD.

OrthoDB

EOG4PG607.

PhylomeDB

P63010.

Enzyme and pathway databases

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_13685. Neuronal System.
REACT_6185. HIV Infection.

Gene expression databases

ArrayExpress

P63010.

Bgee

P63010.

CleanEx

HS_AP2B1.

Genevestigator

P63010.

GermOnline

ENSG00000006125. Homo sapiens.

Family and domain databases

InterPro

IPR016342. AP_complex_bsu.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR015151. B-adaptin_app_sub_C.
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]

Gene3D

G3DSA:1.25.10.10. ARM-like. 1 hit.
G3DSA:2.60.40.1150. Clathrin_b-adaptin_app_Ig-like. 1 hit.

KO

K11825.

Pfam

PF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
PF09066. B2-adapt-app_C. 1 hit.
[Graphical view]

PIRSF

PIRSF002291. AP_complex_beta. 1 hit.

SMART

SM00809. Alpha_adaptinC2. 1 hit.
SM01020. B2-adapt-app_C. 1 hit.
[Graphical view]

SUPFAM

SSF55711. AP2_adap_app. 1 hit.
SSF48371. ARM-type_fold. 1 hit.
SSF49348. Clath_adapt. 1 hit.

ProtoNet

Search...

Other

NextBio

653.

SOURCE

Search...

Entry information

Entry name

AP2B1_HUMAN

Accession

Primary (citable) accession number: P63010
Secondary accession number(s): A6NJP3, P21851, Q96J19

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 31, 2004
Last sequence update:	August 31, 2004
Last modified:	January 25, 2012
This is version 91 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.