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Details on Person UniProt:Q9UPY8-1 MAPRE3
| Class:Id | ReferenceIsoform:415604 |
|---|---|
| _chainChangeLog | chain:1-281 added on Fri February 6 2015;chain:1-281 removed on Fri May 8 2015;initiator methionine:1 added on Fri May 8 2015;chain:2-281 added on Fri May 8 2015 |
| _displayName | UniProt:Q9UPY8-1 MAPRE3 |
| _timestamp | 2024-11-03 20:01:46 |
| chain | chain:1-281 |
| checksum | 0DA45E89A0B993D3 |
| comment | FUNCTION Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:19255245, PubMed:28814570). Promotes microtubule growth (PubMed:19255245, PubMed:28814570). May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes (PubMed:19255245, PubMed:28814570). Also acts as a regulator of minus-end microtubule organization: interacts with the complex formed by AKAP9 and PDE4DIP, leading to recruit CAMSAP2 to the Golgi apparatus, thereby tethering non-centrosomal minus-end microtubules to the Golgi, an important step for polarized cell movement (PubMed:28814570). Promotes elongation of CAMSAP2-decorated microtubule stretches on the minus-end of microtubules (PubMed:28814570).SUBUNIT Homodimer (PubMed:19255245). Heterodimer with MAPRE1 (PubMed:19255245). Binds monomeric and polymerized GTP-bound tubulin (PubMed:10188731, PubMed:34996871). Interacts with APC2 (PubMed:10644998). Interacts with DCTN1 and SRCIN1 (PubMed:14514668, PubMed:19146815). Binds to the C-terminal domain of APC (PubMed:14514668). Interacts (via C-terminus) with CLIP1 (PubMed:17563362). Interacts with SLAIN2 and SLAIN1 (PubMed:21646404). Interacts with AKAP9 (PubMed:28814570). Interacts with PDE4DIP (PubMed:28814570). Interacts with PDE4DIP isoform 13/MMG8/SMYLE; this interaction is required for its recruitment to the Golgi apparatus (PubMed:25217626).INTERACTION Associated with the microtubule network. Detected at the plus end of microtubules.ALTERNATIVE PRODUCTS Predominantly expressed in brain and muscle.DOMAIN Composed of two functionally independent domains. The N-terminal domain forms a hydrophobic cleft involved in microtubule binding and the C-terminal is involved in the formation of mutually exclusive complexes with APC and DCTN1.SIMILARITY Belongs to the MAPRE family. |
| created | [InstanceEdit:400710] Schmidt, EE, 2009-03-25 05:33:35 |
| description | recommendedName: Microtubule-associated protein RP/EB family member 3 alternativeName: EB1 protein family member 3 shortName: EBF3 alternativeName: End-binding protein 3 shortName: EB3 alternativeName: RP3 |
| geneName | MAPRE3 |
| identifier | Q9UPY8 |
| isoformParent | |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Alternative splicing Cell cycle Cell division Cytoplasm Cytoskeleton Microtubule Mitosis Phosphoprotein Proteomics identification Reference proteome |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 |
| name | MAPRE3 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:9000145] ENSEMBL:ENSG00000084764 MAPRE3 [Homo sapiens] |
| secondaryIdentifier | MARE3_HUMAN B7WPK5 O00265 Q6FHB0 Q6FI15 Q9BZP7 Q9BZP8 |
| sequenceLength | 281 |
| species | [Species:48887] Homo sapiens |
| variantIdentifier | Q9UPY8-1 |
| [Change default viewing format] | |
No pathways have been reviewed or authored by UniProt:Q9UPY8-1 MAPRE3 (415604)
