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P63010

- AP2B1_HUMAN

UniProt

P63010 - AP2B1_HUMAN

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Protein
AP-2 complex subunit beta
Gene
AP2B1, ADTB2, CLAPB1
Organism
Homo sapiens (Human)
Status
Reviewed - 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.4 Publications

GO - Molecular functioni

  1. clathrin binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. protein transporter activity Source: InterPro

GO - Biological processi

  1. antigen processing and presentation of exogenous peptide antigen via MHC class II Source: Reactome
  2. axon guidance Source: Reactome
  3. clathrin coat assembly Source: Ensembl
  4. endocytosis Source: UniProtKB-KW
  5. epidermal growth factor receptor signaling pathway Source: Reactome
  6. intracellular protein transport Source: InterPro
  7. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
  8. neurotrophin TRK receptor signaling pathway Source: Reactome
  9. regulation of defense response to virus by virus Source: Reactome
  10. synaptic transmission Source: Reactome
  11. viral process Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Enzyme and pathway databases

ReactomeiREACT_11166. Nef Mediated CD4 Down-regulation.
REACT_11200. Nef Mediated CD8 Down-regulation.
REACT_121399. MHC class II antigen presentation.
REACT_12435. Retrograde neurotrophin signalling.
REACT_12484. EGFR downregulation.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_22365. Recycling pathway of L1.
SignaLinkiP63010.

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:ADTB2, CLAPB1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:563. AP2B1.

Subcellular locationi

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.1 Publication

GO - Cellular componenti

  1. clathrin adaptor complex Source: InterPro
  2. clathrin-coated endocytic vesicle membrane Source: Reactome
  3. coated pit Source: UniProtKB-SubCell
  4. cytosol Source: Reactome
  5. endocytic vesicle membrane Source: Reactome
  6. intracellular membrane-bounded organelle Source: HPA
  7. plasma membrane Source: Reactome
  8. trans-Golgi network Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi815 – 8151Y → A: Strongly reduces interaction with SNAP91, EPS15, AMPH and BIN1 and clathrin heavy chain. 2 Publications
Mutagenesisi841 – 8411W → A: Abolishes interaction with LDLRAP1 and ARRB1. Greatly reduces DENND1B-binding. 4 Publications
Mutagenesisi842 – 8421K → E: Strongly reduces interaction with ARRB1. 1 Publication
Mutagenesisi849 – 8491E → A: Strongly reduces interaction with LDLRAP1, ARRB1 and EPN1. No effect on DENND1B-binding. 3 Publications
Mutagenesisi851 – 8511Q → A: Strongly reduces interaction with ARRB1. 1 Publication
Mutagenesisi879 – 8791R → A: No effect on interaction with ARRB1. 2 Publications
Mutagenesisi879 – 8791R → E: Strongly reduces interaction with EPN1. Reduces interaction with SNAP91 and clathrin. No effect on EPS15 binding. 2 Publications
Mutagenesisi888 – 8881Y → V: Strongly reduces interaction with SNAP91, EPN1 and clathrin. No effect on EPS15 binding. Abolishes interaction with ARRB1 and with DENND1B. 5 Publications
Mutagenesisi902 – 9021E → A: Strongly reduces interaction with LDLRAP1 and ARRB1. No effect on DENND1B-binding. 3 Publications
Mutagenesisi917 – 9171K → Q: Strongly reduces interaction with LDLRAP1. SNAP91 and clathrin. Reduces interaction with EPN1. No effect on EPS15 binding. 1 Publication

Organism-specific databases

PharmGKBiPA24854.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 937936AP-2 complex subunit beta
PRO_0000193742Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylthreonine1 Publication
Modified residuei265 – 2651N6-acetyllysine1 Publication
Modified residuei737 – 7371Phosphotyrosine; by SRC2 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP63010.
PaxDbiP63010.
PRIDEiP63010.

PTM databases

PhosphoSiteiP63010.

Expressioni

Gene expression databases

ArrayExpressiP63010.
BgeeiP63010.
CleanExiHS_AP2B1.
GenevestigatoriP63010.

Organism-specific databases

HPAiCAB017631.
HPA056733.

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. Interacts with PIP5K1C; clathrin competes with PIP5K1C By similarity. Interacts with DENND1B, but not with DENND1A, nor DENND1C. Interacts with FCHO1.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
Ap2m1P840922EBI-432924,EBI-297693From a different organism.
LDLRAP1Q5SW963EBI-432924,EBI-747813
MEA1Q166262EBI-432924,EBI-744921

Protein-protein interaction databases

BioGridi106672. 61 interactions.
DIPiDIP-33098N.
IntActiP63010. 38 interactions.
MINTiMINT-256705.
STRINGi9606.ENSP00000314414.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi11 – 133
Helixi14 – 218
Helixi27 – 4216
Helixi48 – 503
Helixi51 – 566
Beta strandi59 – 613
Helixi63 – 7917
Helixi81 – 855
Helixi88 – 914
Helixi92 – 943
Beta strandi95 – 995
Helixi100 – 11112
Helixi116 – 1183
Helixi119 – 12911
Helixi135 – 15016
Helixi156 – 16712
Helixi174 – 1774
Helixi180 – 1878
Turni192 – 1954
Helixi200 – 21314
Helixi216 – 22712
Helixi234 – 24411
Helixi245 – 2473
Helixi254 – 26512
Beta strandi267 – 2704
Turni272 – 2754
Helixi277 – 2837
Helixi285 – 2917
Helixi296 – 31217
Turni316 – 3194
Turni321 – 3244
Helixi332 – 34413
Turni348 – 3503
Helixi351 – 36111
Helixi367 – 38115
Helixi385 – 40016
Helixi404 – 42017
Turni422 – 4243
Helixi425 – 4284
Helixi429 – 4346
Turni435 – 4384
Helixi442 – 45312
Helixi456 – 4583
Helixi462 – 4698
Turni470 – 4723
Beta strandi474 – 4763
Helixi478 – 49215
Beta strandi495 – 4973
Helixi500 – 51112
Helixi517 – 52711
Turni528 – 5325
Helixi536 – 5416
Helixi557 – 5648
Turni565 – 5684
Helixi571 – 5744
Helixi578 – 5803
Beta strandi712 – 7154
Helixi717 – 7193
Turni720 – 7223
Beta strandi723 – 73210
Beta strandi735 – 74410
Beta strandi746 – 7483
Beta strandi754 – 7574
Beta strandi765 – 7684
Beta strandi781 – 79010
Beta strandi802 – 8087
Beta strandi813 – 8197
Helixi822 – 8254
Helixi834 – 84310
Helixi846 – 8483
Beta strandi850 – 8545
Helixi861 – 87010
Beta strandi874 – 8818
Beta strandi884 – 89310
Beta strandi898 – 9058
Beta strandi910 – 92011
Helixi921 – 9233
Helixi924 – 93613

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP63010.
SMRiP63010. Positions 4-582, 705-937.

Miscellaneous databases

EvolutionaryTraceiP63010.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni841 – 93797Interaction with ARRB1
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5096.
HOGENOMiHOG000163270.
HOVERGENiHBG050515.
KOiK11825.
OMAiPNQSIDI.
OrthoDBiEOG7BGHK0.
PhylomeDBiP63010.
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.
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.
SM01020. B2-adapt-app_C. 1 hit.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P63010-1) [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

MTDSKYFTTN KKGEIFELKA ELNNEKKEKR KEAVKKVIAA MTVGKDVSSL    50
FPDVVNCMQT DNLELKKLVY LYLMNYAKSQ PDMAIMAVNS FVKDCEDPNP 100
LIRALAVRTM GCIRVDKITE YLCEPLRKCL KDEDPYVRKT AAVCVAKLHD 150
INAQMVEDQG FLDSLRDLIA DSNPMVVANA VAALSEISES HPNSNLLDLN 200
PQNINKLLTA LNECTEWGQI FILDCLSNYN PKDDREAQSI CERVTPRLSH 250
ANSAVVLSAV KVLMKFLELL PKDSDYYNML LKKLAPPLVT LLSGEPEVQY 300
VALRNINLIV QKRPEILKQE IKVFFVKYND PIYVKLEKLD IMIRLASQAN 350
IAQVLAELKE YATEVDVDFV RKAVRAIGRC AIKVEQSAER CVSTLLDLIQ 400
TKVNYVVQEA IVVIRDIFRK YPNKYESIIA TLCENLDSLD EPDARAAMIW 450
IVGEYAERID NADELLESFL EGFHDESTQV QLTLLTAIVK LFLKKPSETQ 500
ELVQQVLSLA TQDSDNPDLR DRGYIYWRLL STDPVTAKEV VLSEKPLISE 550
ETDLIEPTLL DELICHIGSL ASVYHKPPNA FVEGSHGIHR KHLPIHHGST 600
DAGDSPVGTT TATNLEQPQV IPSQGDLLGD LLNLDLGPPV NVPQVSSMQM 650
GAVDLLGGGL DSLVGQSFIP SSVPATFAPS PTPAVVSSGL NDLFELSTGI 700
GMAPGGYVAP KAVWLPAVKA KGLEISGTFT HRQGHIYMEM NFTNKALQHM 750
TDFAIQFNKN SFGVIPSTPL AIHTPLMPNQ SIDVSLPLNT LGPVMKMEPL 800
NNLQVAVKNN IDVFYFSCLI PLNVLFVEDG KMERQVFLAT WKDIPNENEL 850
QFQIKECHLN ADTVSSKLQN NNVYTIAKRN VEGQDMLYQS LKLTNGIWIL 900
AELRIQPGNP NYTLSLKCRA PEVSQYIYQV YDSILKN 937
Length:937
Mass (Da):104,553
Last modified:August 31, 2004 - v1
Checksum:iB472EE5B2AE176DF
GO
Isoform 2 (identifier: P63010-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:951
Mass (Da):105,692
Checksum:i3199C9F8C7F027F2
GO
Isoform 3 (identifier: P63010-3) [UniParc]FASTAAdd to Basket

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.

Show »
Length:880
Mass (Da):98,118
Checksum:i468D8B39AD35C7E4
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 5757Missing in isoform 3.
VSP_047805Add
BLAST
Alternative sequencei663 – 6631L → LLGSDLGGGIGGSPA in isoform 2.
VSP_011490

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS32621.1. [P63010-2]
CCDS32622.1. [P63010-1]
PIRiA35553.
RefSeqiNP_001025177.1. NM_001030006.1. [P63010-2]
NP_001273.1. NM_001282.2. [P63010-1]
XP_005257994.1. XM_005257937.1. [P63010-2]
XP_005257995.1. XM_005257938.1. [P63010-2]
UniGeneiHs.514819.

Genome annotation databases

EnsembliENST00000262325; 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]
GeneIDi163.
KEGGihsa:163.
UCSCiuc002hjq.3. human. [P63010-2]
uc002hjr.3. human. [P63010-1]

Polymorphism databases

DMDMi51702211.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS32621.1. [P63010-2 ]
CCDS32622.1. [P63010-1 ]
PIRi A35553.
RefSeqi NP_001025177.1. NM_001030006.1. [P63010-2 ]
NP_001273.1. NM_001282.2. [P63010-1 ]
XP_005257994.1. XM_005257937.1. [P63010-2 ]
XP_005257995.1. XM_005257938.1. [P63010-2 ]
UniGenei Hs.514819.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
ProteinModelPortali P63010.
SMRi P63010. Positions 4-582, 705-937.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106672. 61 interactions.
DIPi DIP-33098N.
IntActi P63010. 38 interactions.
MINTi MINT-256705.
STRINGi 9606.ENSP00000314414.

PTM databases

PhosphoSitei P63010.

Polymorphism databases

DMDMi 51702211.

Proteomic databases

MaxQBi P63010.
PaxDbi P63010.
PRIDEi P63010.

Protocols and materials databases

DNASUi 163.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000262325 ; 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 ]
GeneIDi 163.
KEGGi hsa:163.
UCSCi uc002hjq.3. human. [P63010-2 ]
uc002hjr.3. human. [P63010-1 ]

Organism-specific databases

CTDi 163.
GeneCardsi GC17P033914.
HGNCi HGNC:563. AP2B1.
HPAi CAB017631.
HPA056733.
MIMi 601025. gene.
neXtProti NX_P63010.
PharmGKBi PA24854.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5096.
HOGENOMi HOG000163270.
HOVERGENi HBG050515.
KOi K11825.
OMAi PNQSIDI.
OrthoDBi EOG7BGHK0.
PhylomeDBi P63010.
TreeFami TF300318.

Enzyme and pathway databases

Reactomei REACT_11166. Nef Mediated CD4 Down-regulation.
REACT_11200. Nef Mediated CD8 Down-regulation.
REACT_121399. MHC class II antigen presentation.
REACT_12435. Retrograde neurotrophin signalling.
REACT_12484. EGFR downregulation.
REACT_172599. WNT5A-dependent internalization of FZD4.
REACT_18422. Trafficking of GluR2-containing AMPA receptors.
REACT_22365. Recycling pathway of L1.
SignaLinki P63010.

Miscellaneous databases

ChiTaRSi AP2B1. human.
EvolutionaryTracei P63010.
GeneWikii AP2B1.
GenomeRNAii 163.
NextBioi 653.
PROi P63010.
SOURCEi Search...

Gene expression databases

ArrayExpressi P63010.
Bgeei P63010.
CleanExi HS_AP2B1.
Genevestigatori P63010.

Family and domain databases

Gene3Di 1.25.10.10. 1 hit.
2.60.40.1150. 1 hit.
3.30.310.10. 1 hit.
InterProi IPR026739. 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 ]
PANTHERi PTHR11134. PTHR11134. 1 hit.
Pfami PF01602. Adaptin_N. 1 hit.
PF02883. Alpha_adaptinC2. 1 hit.
PF09066. B2-adapt-app_C. 1 hit.
[Graphical view ]
PIRSFi PIRSF002291. AP_complex_beta. 1 hit.
SMARTi SM00809. Alpha_adaptinC2. 1 hit.
SM01020. B2-adapt-app_C. 1 hit.
[Graphical view ]
SUPFAMi SSF48371. SSF48371. 1 hit.
SSF49348. SSF49348. 1 hit.
SSF55711. SSF55711. 1 hit.
ProtoNeti Search...

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: 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiAP2B1_HUMAN
AccessioniPrimary (citable) accession number: P63010
Secondary accession number(s): A6NJP3
, P21851, Q7Z451, Q96J19
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: August 31, 2004
Last modified: September 3, 2014
This is version 119 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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