| UniProt ID | APBLB_ARATH | |
|---|---|---|
| UniProt AC | Q9SUS3 | |
| Protein Name | Beta-adaptin-like protein B | |
| Gene Name | BETAB-AD | |
| Organism | Arabidopsis thaliana (Mouse-ear cress). | |
| Sequence Length | 894 | |
| Subcellular Localization |
Golgi apparatus. Golgi apparatus, trans-Golgi network. Cytoplasmic vesicle, clathrin-coated vesicle membrane Peripheral membrane protein Cytoplasmic side. Associated with the trans-Golgi network. Component of the coat surrounding the cytoplasmic fa |
|
| Protein Description | Subunit of clathrin-associated adaptor protein complex that plays a role in protein sorting in the late-Golgi/trans-Golgi network (TGN) and/or endosomes. The AP complexes mediate both the recruitment of clathrin to membranes and the recognition of sorting signals within the cytosolic tails of transmembrane cargo molecules (By similarity).. | |
| Protein Sequence | MSGHDSKYFSTTKKGEIPELKEELNSQYKDKRKDAVKKVIAAMTVGKDVSSLFTDVVNCMQTENLELKKLVYLYLINYAKSQPDLAILAVNTFVKDSQDPNPLIRALAVRTMGCIRVDKITEYLCDPLQKCLKDDDPYVRKTAAICVAKLFDINAELVEDRGFLEALKDLISDNNPMVVANAVAALAEIQENSSSPIFEINSTTLTKLLTALNECTEWGQVFILDALSKYKAADPREAENIVERVTPRLQHANCAVVLSAVKMILQQMELITSTDVIRNLCKKMAPPLVTLLSAEPEIQYVALRNINLIVQKRPTILAHEIKVFFCKYNDPIYVKMEKLEIMIKLASDRNIDQVLLEFKEYATEVDVDFVRKAVRAIGRCAIKLERAAERCISVLLELIKIKVNYVVQEAIIVIKDIFRRYPNTYESIIATLCESLDTLDEPEAKASMIWIIGEYAERIDNADELLESFLENFPEEPAQVQLQLLTATVKLFLKKPTEGPQQMIQVVLNNATVETDNPDLRDRAYIYWRLLSTDPEAAKDVVLAEKPVISDDSNQLDPSLLDELLTNISTLSSVYHKPPEAFVTRLKTTVQKTEDEDFAEGSEAGYSSSNPVDSAASPPGNIPQPSGRQPAPAVPAPVPDLLGDLMGLDNAAIVPVDDPITQSGPPLPVVVPASSGQGLQISAQLSRKDGQVFYSMLFENNSQSVLDGFMIQFNKNTFGLAAAGSLQIPPLHPATSARTMLPMVLFQNMSAGPPSSLLQVAVKNNQQPVWYFTDKIILHALFGEDGRMERGTFLETWRSLPDSNEVLKEFPGITITSVESTIELLTAFNMFFIAKRKNGNQDVIYLSAKDPRDVPFLIELTAMVGQPGLKCAVKTPTPEIAPLFFEALELLFKA | |
| Overview of Protein Modification Sites with Functional and Structural Information | ||
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* ASA = Accessible Surface Area
| Locations | Modification | Substrate Peptides & Secondary Structure |
ASA (%) | Reference | Orthologous Protein Cluster |
|---|---|---|---|---|---|
| 6 | Phosphorylation | --MSGHDSKYFSTTK --CCCCCCCCCCCCC | 24.47 | 25561503 | |
| 593 | Phosphorylation | LKTTVQKTEDEDFAE HHHCCEECCCCCCCC | 31.42 | 23776212 | |
| 602 | Phosphorylation | DEDFAEGSEAGYSSS CCCCCCCCCCCCCCC | 18.77 | 23776212 | |
| 606 | Phosphorylation | AEGSEAGYSSSNPVD CCCCCCCCCCCCCCC | 16.66 | 23776212 | |
| 607 | Phosphorylation | EGSEAGYSSSNPVDS CCCCCCCCCCCCCCC | 26.77 | 23776212 | |
| 608 | Phosphorylation | GSEAGYSSSNPVDSA CCCCCCCCCCCCCCC | 26.17 | 23776212 | |
| 609 | Phosphorylation | SEAGYSSSNPVDSAA CCCCCCCCCCCCCCC | 38.93 | 23776212 | |
| 614 | Phosphorylation | SSSNPVDSAASPPGN CCCCCCCCCCCCCCC | 26.43 | 23776212 | |
| 617 | Phosphorylation | NPVDSAASPPGNIPQ CCCCCCCCCCCCCCC | 31.20 | 23776212 | |
| 626 | Phosphorylation | PGNIPQPSGRQPAPA CCCCCCCCCCCCCCC | 41.16 | 23776212 |
| 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 APBLB_ARATH !! | ||||||
| Modified Location | Modified Residue | Modification | Function | Reference | ||
|---|---|---|---|---|---|---|
Oops, there are no descriptions of PTM sites of APBLB_ARATH !! | ||||||
* 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 APBLB_ARATH !! | ||||||
| Interacting Protein | Gene Name | Interaction Type | PPI Reference | Domain-Domain Interactions |
|---|---|---|---|---|
| AP2A1_ARATH | alpha-ADR | physical | 23975899 | |
| AP2S_ARATH | AT1G47830 | physical | 23975899 | |
| AP2M_ARATH | AT5G46630 | physical | 23975899 | |
| CLAH1_ARATH | AT3G11130 | physical | 23975899 | |
| CLC2_ARATH | AT2G40060 | physical | 23975899 |
| Kegg Drug | ||||||
|---|---|---|---|---|---|---|
| DrugBank | ||||||
| There are no disease associations of PTM sites. | ||||||
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