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Protein

AP-2 complex subunit beta

Gene

AP2B1

Organism
Homo sapiens (Human)
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.4 Publications

GO - Molecular functioni

  • clathrin binding Source: UniProtKB
  • protein transporter activity Source: InterPro
  • signal sequence binding Source: BHF-UCL

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Endocytosis, Protein transport, Transport

Enzyme and pathway databases

BioCyciZFISH:ENSG00000006125-MONOMER.
ReactomeiR-HSA-167590. Nef Mediated CD4 Down-regulation.
R-HSA-171052. LDL-mediated lipid transport.
R-HSA-177504. Retrograde neurotrophin signalling.
R-HSA-182218. Nef Mediated CD8 Down-regulation.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-416993. Trafficking of GluR2-containing AMPA receptors.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5140745. WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-8866427. VLDLR internalisation and degradation.
SignaLinkiP63010.
SIGNORiP63010.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:563. AP2B1.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Coated pit, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi815Y → A: Strongly reduces interaction with SNAP91, EPS15, AMPH and BIN1 and clathrin heavy chain. 2 Publications1
Mutagenesisi841W → A: Abolishes interaction with LDLRAP1 and ARRB1. Greatly reduces DENND1B-binding. 4 Publications1
Mutagenesisi842K → E: Strongly reduces interaction with ARRB1. 1 Publication1
Mutagenesisi849E → A: Strongly reduces interaction with LDLRAP1, ARRB1 and EPN1. No effect on DENND1B-binding. 3 Publications1
Mutagenesisi851Q → A: Strongly reduces interaction with ARRB1. 1 Publication1
Mutagenesisi879R → A: No effect on interaction with ARRB1. 2 Publications1
Mutagenesisi879R → E: Strongly reduces interaction with EPN1. Reduces interaction with SNAP91 and clathrin. No effect on EPS15 binding. 2 Publications1
Mutagenesisi888Y → V: Strongly reduces interaction with SNAP91, EPN1 and clathrin. No effect on EPS15 binding. Abolishes interaction with ARRB1 and with DENND1B. 5 Publications1
Mutagenesisi902E → A: Strongly reduces interaction with LDLRAP1 and ARRB1. No effect on DENND1B-binding. 3 Publications1
Mutagenesisi917K → Q: Strongly reduces interaction with LDLRAP1. SNAP91 and clathrin. Reduces interaction with EPN1. No effect on EPS15 binding. 1 Publication1

Organism-specific databases

DisGeNETi163.
OpenTargetsiENSG00000006125.
PharmGKBiPA24854.

Polymorphism and mutation databases

BioMutaiAP2B1.
DMDMi51702211.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources
ChainiPRO_00001937422 – 937AP-2 complex subunit betaAdd BLAST936

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylthreonineCombined sources1
Modified residuei4PhosphoserineCombined sources1
Modified residuei265N6-acetyllysineCombined sources1
Modified residuei737Phosphotyrosine; by SRC2 Publications1
Modified residuei928PhosphotyrosineBy similarity1

Post-translational modificationi

Phosphorylation at Tyr-737 by SRC occurs at the plasma membrane in clathrin-coated vesicles (CCVs).2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP63010.
MaxQBiP63010.
PaxDbiP63010.
PeptideAtlasiP63010.
PRIDEiP63010.

PTM databases

iPTMnetiP63010.
PhosphoSitePlusiP63010.
SwissPalmiP63010.

Expressioni

Gene expression databases

BgeeiENSG00000006125.
CleanExiHS_AP2B1.
ExpressionAtlasiP63010. baseline and differential.
GenevisibleiP63010. HS.

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.By similarity13 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AFF4Q9UHB73EBI-432924,EBI-395282
AFF4Q9UHB7-23EBI-432924,EBI-10261324
AP1M2Q9Y6Q54EBI-432924,EBI-752250
Ap2m1P840922EBI-432924,EBI-297693From a different organism.
KPNA2Q6NVW73EBI-432924,EBI-9377406
LDLRAP1Q5SW964EBI-432924,EBI-747813
MEA1Q166262EBI-432924,EBI-744921
MLH1P406924EBI-11529439,EBI-744248
NEU4Q8WWR8-23EBI-432924,EBI-10277551
SLC25A6P122363EBI-432924,EBI-356254
THAP1Q9NVV94EBI-432924,EBI-741515
TXN2Q997573EBI-432924,EBI-2932492
U2AF1Q010813EBI-432924,EBI-632461
XRCC6BP1Q8N4L53EBI-432924,EBI-10265517

GO - Molecular functioni

  • clathrin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106672. 110 interactors.
DIPiDIP-33098N.
IntActiP63010. 90 interactors.
MINTiMINT-256705.
STRINGi9606.ENSP00000314414.

Structurei

Secondary structure

1937
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi11 – 13Combined sources3
Helixi14 – 21Combined sources8
Helixi27 – 42Combined sources16
Helixi48 – 50Combined sources3
Helixi51 – 56Combined sources6
Beta strandi59 – 61Combined sources3
Helixi63 – 79Combined sources17
Helixi81 – 85Combined sources5
Helixi88 – 91Combined sources4
Helixi92 – 94Combined sources3
Beta strandi95 – 99Combined sources5
Helixi100 – 111Combined sources12
Helixi116 – 118Combined sources3
Helixi119 – 129Combined sources11
Helixi135 – 150Combined sources16
Helixi156 – 167Combined sources12
Helixi174 – 177Combined sources4
Helixi180 – 187Combined sources8
Turni192 – 195Combined sources4
Helixi200 – 213Combined sources14
Helixi216 – 227Combined sources12
Helixi234 – 244Combined sources11
Helixi245 – 247Combined sources3
Helixi254 – 265Combined sources12
Beta strandi267 – 270Combined sources4
Turni272 – 275Combined sources4
Helixi277 – 283Combined sources7
Helixi285 – 291Combined sources7
Helixi296 – 312Combined sources17
Turni316 – 319Combined sources4
Turni321 – 324Combined sources4
Helixi332 – 344Combined sources13
Turni348 – 350Combined sources3
Helixi351 – 361Combined sources11
Helixi367 – 381Combined sources15
Helixi385 – 400Combined sources16
Helixi404 – 420Combined sources17
Turni422 – 424Combined sources3
Helixi426 – 428Combined sources3
Helixi429 – 434Combined sources6
Turni435 – 438Combined sources4
Helixi442 – 453Combined sources12
Helixi456 – 458Combined sources3
Helixi462 – 469Combined sources8
Turni470 – 472Combined sources3
Beta strandi474 – 476Combined sources3
Helixi478 – 492Combined sources15
Turni496 – 498Combined sources3
Helixi500 – 511Combined sources12
Helixi517 – 527Combined sources11
Turni528 – 532Combined sources5
Helixi536 – 541Combined sources6
Beta strandi552 – 554Combined sources3
Helixi557 – 564Combined sources8
Turni565 – 568Combined sources4
Helixi571 – 574Combined sources4
Helixi578 – 580Combined sources3
Beta strandi619 – 621Combined sources3
Helixi624 – 630Combined sources7
Beta strandi712 – 715Combined sources4
Helixi717 – 719Combined sources3
Turni720 – 722Combined sources3
Beta strandi723 – 732Combined sources10
Beta strandi735 – 744Combined sources10
Beta strandi746 – 748Combined sources3
Beta strandi754 – 757Combined sources4
Beta strandi765 – 768Combined sources4
Beta strandi781 – 790Combined sources10
Beta strandi802 – 808Combined sources7
Beta strandi813 – 819Combined sources7
Helixi822 – 825Combined sources4
Helixi834 – 843Combined sources10
Helixi846 – 848Combined sources3
Beta strandi850 – 854Combined sources5
Helixi861 – 870Combined sources10
Beta strandi874 – 881Combined sources8
Beta strandi884 – 893Combined sources10
Beta strandi898 – 905Combined sources8
Beta strandi910 – 920Combined sources11
Helixi921 – 923Combined sources3
Helixi924 – 936Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4UQIX-ray2.79B1-651[»]
ProteinModelPortaliP63010.
SMRiP63010.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63010.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni841 – 937Interaction with ARRB1Add BLAST97

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi576 – 716Pro-rich (stalk region)Add BLAST141

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1061. Eukaryota.
COG5096. LUCA.
GeneTreeiENSGT00530000063138.
HOGENOMiHOG000163270.
HOVERGENiHBG050515.
InParanoidiP63010.
KOiK11825.
OMAiCHLNADA.
OrthoDBiEOG091G019U.
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.
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 (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. AlignAdd to basket

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

        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: 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)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0478051 – 57Missing in isoform 3. 1 PublicationAdd BLAST57
Alternative sequenceiVSP_011490663L → LLGSDLGGGIGGSPA in isoform 2. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005257937.3. [P63010-2]
XP_005257995.1. XM_005257938.2. [P63010-2]
XP_011522757.1. XM_011524455.2. [P63010-3]
XP_016879773.1. XM_017024284.1. [P63010-1]
XP_016879775.1. XM_017024286.1. [P63010-3]
UniGeneiHs.514819.

Genome annotation databases

EnsembliENST00000610402; ENSP00000483185; ENSG00000006125. [P63010-2]
ENST00000618940; ENSP00000482835; ENSG00000006125. [P63010-2]
ENST00000621914; ENSP00000482315; ENSG00000006125. [P63010-1]
GeneIDi163.
KEGGihsa:163.
UCSCiuc002hjq.4. human. [P63010-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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_005257937.3. [P63010-2]
XP_005257995.1. XM_005257938.2. [P63010-2]
XP_011522757.1. XM_011524455.2. [P63010-3]
XP_016879773.1. XM_017024284.1. [P63010-1]
XP_016879775.1. XM_017024286.1. [P63010-3]
UniGeneiHs.514819.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4UQIX-ray2.79B1-651[»]
ProteinModelPortaliP63010.
SMRiP63010.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106672. 110 interactors.
DIPiDIP-33098N.
IntActiP63010. 90 interactors.
MINTiMINT-256705.
STRINGi9606.ENSP00000314414.

PTM databases

iPTMnetiP63010.
PhosphoSitePlusiP63010.
SwissPalmiP63010.

Polymorphism and mutation databases

BioMutaiAP2B1.
DMDMi51702211.

Proteomic databases

EPDiP63010.
MaxQBiP63010.
PaxDbiP63010.
PeptideAtlasiP63010.
PRIDEiP63010.

Protocols and materials databases

DNASUi163.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000610402; ENSP00000483185; ENSG00000006125. [P63010-2]
ENST00000618940; ENSP00000482835; ENSG00000006125. [P63010-2]
ENST00000621914; ENSP00000482315; ENSG00000006125. [P63010-1]
GeneIDi163.
KEGGihsa:163.
UCSCiuc002hjq.4. human. [P63010-1]

Organism-specific databases

CTDi163.
DisGeNETi163.
GeneCardsiAP2B1.
HGNCiHGNC:563. AP2B1.
HPAiCAB017631.
HPA056733.
MIMi601025. gene.
neXtProtiNX_P63010.
OpenTargetsiENSG00000006125.
PharmGKBiPA24854.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1061. Eukaryota.
COG5096. LUCA.
GeneTreeiENSGT00530000063138.
HOGENOMiHOG000163270.
HOVERGENiHBG050515.
InParanoidiP63010.
KOiK11825.
OMAiCHLNADA.
OrthoDBiEOG091G019U.
PhylomeDBiP63010.
TreeFamiTF300318.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000006125-MONOMER.
ReactomeiR-HSA-167590. Nef Mediated CD4 Down-regulation.
R-HSA-171052. LDL-mediated lipid transport.
R-HSA-177504. Retrograde neurotrophin signalling.
R-HSA-182218. Nef Mediated CD8 Down-regulation.
R-HSA-2132295. MHC class II antigen presentation.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-416993. Trafficking of GluR2-containing AMPA receptors.
R-HSA-437239. Recycling pathway of L1.
R-HSA-5099900. WNT5A-dependent internalization of FZD4.
R-HSA-5140745. WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
R-HSA-8856825. Cargo recognition for clathrin-mediated endocytosis.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-8866427. VLDLR internalisation and degradation.
SignaLinkiP63010.
SIGNORiP63010.

Miscellaneous databases

ChiTaRSiAP2B1. human.
EvolutionaryTraceiP63010.
GeneWikiiAP2B1.
GenomeRNAii163.
PROiP63010.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000006125.
CleanExiHS_AP2B1.
ExpressionAtlasiP63010. baseline and differential.
GenevisibleiP63010. HS.

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...

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: November 30, 2016
This is version 145 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

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.