AP2B1_RAT - dbPTM
AP2B1_RAT - PTM Information in dbPTM
Basic Information of Protein
UniProt ID AP2B1_RAT
UniProt AC P62944
Protein Name AP-2 complex subunit beta
Gene Name Ap2b1
Organism Rattus norvegicus (Rat).
Sequence Length 937
Subcellular Localization Cell membrane. Membrane, coated pit
Peripheral membrane protein
Cytoplasmic side. AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV..
Protein Description 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)..
Protein Sequence MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANAVAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQYVALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRKYPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEVVLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRKHLPIHHGSTDAGDSPVGTTTATNLEQPQVIPSQGDLLGDLLNLDLGPPVNVPQVSSMQMGAVDLLGGGLDSLVGQSFIPSSVPATFAPSPTPAVVSSGLNDLFELSTGIGMAPGGYVAPKAVWLPAVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIHTPLMPNQSIDVSLPLNTLGPVMKMEPLNNLQVAVKNNIDVFYFSCLIPLNVLFVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRIQPGNPNYTLSLKCRAPEVSQYIYQVYDSILKN
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
2Phosphorylation------MTDSKYFTT
------CCCCCCCCC		49.3227097102
2Acetylation------MTDSKYFTT
------CCCCCCCCC		49.32-
4Phosphorylation----MTDSKYFTTNK
----CCCCCCCCCCC		21.7927097102
5Acetylation---MTDSKYFTTNKK
---CCCCCCCCCCCC		47.3922902405
5Ubiquitination---MTDSKYFTTNKK
---CCCCCCCCCCCC		47.39-
6Phosphorylation--MTDSKYFTTNKKG
--CCCCCCCCCCCCC		15.3125575281
8PhosphorylationMTDSKYFTTNKKGEI
CCCCCCCCCCCCCCE		26.7727097102
12UbiquitinationKYFTTNKKGEIFELK
CCCCCCCCCCEEEHH		64.94-
239PhosphorylationKDDREAQSICERVTP
CCHHHHHHHHHHHCC		35.9325403869
265AcetylationSAVKVLMKFLELLPK
HHHHHHHHHHHHCCC		42.5113578139
272AcetylationKFLELLPKDSDYYNM
HHHHHCCCCCHHHHH		70.5922902405
282AcetylationDYYNMLLKKLAPPLV
HHHHHHHHHHCCCCC		41.6022902405
318AcetylationQKRPEILKQEIKVFF
ECCHHHHHHHEEEEE		52.0922902405
327AcetylationEIKVFFVKYNDPIYV
HEEEEEEECCCCEEE		32.9366708747
335AcetylationYNDPIYVKLEKLDIM
CCCCEEEEHHHHHHH		33.68-
347PhosphorylationDIMIRLASQANIAQV
HHHHHHHCCCCHHHH		34.1228689409
393PhosphorylationQSAERCVSTLLDLIQ
HHHHHHHHHHHHHHH		19.5728689409
394PhosphorylationSAERCVSTLLDLIQT
HHHHHHHHHHHHHHH		15.7928689409
605PhosphorylationGSTDAGDSPVGTTTA
CCCCCCCCCCCCCCC		22.1430240740
737PhosphorylationTHRQGHIYMEMNFTN
EECCCEEEEEEECCH		4.9525403869
874PhosphorylationKLQNNNVYTIAKRNV
HHHCCCEEEEEECCC		8.4427097102
875PhosphorylationLQNNNVYTIAKRNVE
HHCCCEEEEEECCCC		15.3527097102
888PhosphorylationVEGQDMLYQSLKLTN
CCCHHHHHHHHHCCC		6.8713578133
926PhosphorylationRAPEVSQYIYQVYDS
CCHHHHHHHHHHHHH		8.2931137095
928PhosphorylationPEVSQYIYQVYDSIL
HHHHHHHHHHHHHHH		6.2319287005
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of AP2B1_RAT !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of AP2B1_RAT !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of AP2B1_RAT !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP180_RATSnap91physical
16903783
ARRB2_RATArrb2physical
16903783
AMPH_RATAmphphysical
16903783
EPN1_RATEpn1physical
16903783
ITSN1_RATItsn1physical
16903783
SYNRG_RATSynrgphysical
16903783
SCYL1_RATScyl1physical
16903783
HSP7C_RATHspa8physical
16903783
K2C1_RATKrt1physical
16903783
EPN2_RATEpn2physical
16903783
TOLIP_RATTollipphysical
16903783
ARFG1_RATArfgap1physical
16903783
CLH1_RATCltcphysical
16903783
DYN1_RATDnm1physical
16903783
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of AP2B1_RAT

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory