UniProt functional annotation for Q15691



	UniProt functional annotation for Q15691

UniProt code: Q15691.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes (PubMed:12388762). 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). Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (PubMed:28726242). May play a role in cell migration (By similarity). {ECO:0000250|UniProtKB:Q61166, ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:28726242, ECO:0000269|PubMed:28814570}.

Subunit: Homodimer (PubMed:15616574). Heterodimer with MAPRE3 (PubMed:19255245). Interacts with DCTN1, DCTN2, TERF1 and dynein intermediate chain (PubMed:10226031, PubMed:11943150, PubMed:12388762, PubMed:14514668, PubMed:23874158, PubMed:16109370, PubMed:16949363). Interaction with DIAPH1 and DIAPH2 (By similarity). Interacts with APC (via C-terminal domain), CLASP2, DST, KIF2C and STIM1; probably required for their targeting to the growing microtubule plus ends (PubMed:7606712, PubMed:12388762, PubMed:14514668, PubMed:15631994, PubMed:19543227, PubMed:15616574, PubMed:19632184). Interacts with MTUS2; interaction is direct and probably targets MTUS2 to microtubules (PubMed:19543227). Interacts with APC2 (PubMed:10644998). Interacts with CLASP1 (PubMed:15631994). Interacts with CDK5RAP2 (PubMed:19553473). Interacts with MACF1 (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (By similarity). Interacts with KCNAB2 (By similarity). Interacts (via C-terminus) with CLIP1 (PubMed:17563362, PubMed:21646404). Interacts with SLAIN2 and SLAIN1 (PubMed:21646404). Interacts with KIF18B; this interaction is required for efficient accumulation of KIF18B at microtubule plus ends (PubMed:21820309). Interacts with MISP (PubMed:23509069). Interacts with KNSTRN (PubMed:23035123). Interacts with NCKAP5L (PubMed:26485573). Interacts with CAMSAP2 (PubMed:28726242). Interacts with PDE4DIP isoform 13/MMG8/SMYLE; this interaction is required for its recruitment to the Golgi apparatus (PubMed:25217626, PubMed:28814570). Forms a pericentrosomal complex with AKAP9, CDK5RAP2 and PDE4DIP isoform 13/MMG8/SMYLE; within this complex, MAPRE1 binding to CDK5RAP2 may be mediated by PDE4DIP (PubMed:29162697). Interacts with AKNA (By similarity). Interacts with GAS2L1, GAS2L2, and GAS2L3 (PubMed:24706950). {ECO:0000250|UniProtKB:Q61166, ECO:0000269|PubMed:10226031, ECO:0000269|PubMed:10644998, ECO:0000269|PubMed:11943150, ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:14514668, ECO:0000269|PubMed:15616574, ECO:0000269|PubMed:15631994, ECO:0000269|PubMed:16109370, ECO:0000269|PubMed:16949363, ECO:0000269|PubMed:17563362, ECO:0000269|PubMed:19255245, ECO:0000269|PubMed:19543227, ECO:0000269|PubMed:19553473, ECO:0000269|PubMed:19632184, ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:21820309, ECO:0000269|PubMed:23035123, ECO:0000269|PubMed:23509069, ECO:0000269|PubMed:23874158, ECO:0000269|PubMed:24706950, ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:26485573, ECO:0000269|PubMed:28726242, ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:29162697, ECO:0000269|PubMed:7606712}.

Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10188731, ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:21646404, ECO:0000269|PubMed:28814570, ECO:0000269|PubMed:9724749}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:12388762, ECO:0000269|PubMed:14654843}. Golgi apparatus {ECO:0000269|PubMed:25217626}. Note=Associated with the microtubule growing distal tips (PubMed:28814570). Recruitment to the Golgi apparatus requires the presence of PDE4DIP isoform 13/MMG8/SMYLE (PubMed:25217626). {ECO:0000269|PubMed:25217626, ECO:0000269|PubMed:28814570}.

Tissue specificity: Ubiquitously expressed. {ECO:0000269|PubMed:10644998}.

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. {ECO:0000269|PubMed:12388762}.

Similarity: Belongs to the MAPRE family. {ECO:0000305}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Plus-end tracking protein (+TIP) that binds to the plus-end of microtubules and regulates the dynamics of the microtubule cytoskeleton (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). Promotes cytoplasmic microtubule nucleation and elongation (PubMed:12388762, PubMed:16109370, PubMed:19632184, PubMed:21646404, PubMed:28726242, PubMed:28814570). May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes (PubMed:12388762). 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). Acts as a regulator of autophagosome transport via interaction with CAMSAP2 (PubMed:28726242). May play a role in cell migration (By similarity). {ECO:0000250\|UniProtKB:Q61166, ECO:0000269\|PubMed:12388762, ECO:0000269\|PubMed:16109370, ECO:0000269\|PubMed:19632184, ECO:0000269\|PubMed:21646404, ECO:0000269\|PubMed:28726242, ECO:0000269\|PubMed:28814570}.


Subunit:		Homodimer (PubMed:15616574). Heterodimer with MAPRE3 (PubMed:19255245). Interacts with DCTN1, DCTN2, TERF1 and dynein intermediate chain (PubMed:10226031, PubMed:11943150, PubMed:12388762, PubMed:14514668, PubMed:23874158, PubMed:16109370, PubMed:16949363). Interaction with DIAPH1 and DIAPH2 (By similarity). Interacts with APC (via C-terminal domain), CLASP2, DST, KIF2C and STIM1; probably required for their targeting to the growing microtubule plus ends (PubMed:7606712, PubMed:12388762, PubMed:14514668, PubMed:15631994, PubMed:19543227, PubMed:15616574, PubMed:19632184). Interacts with MTUS2; interaction is direct and probably targets MTUS2 to microtubules (PubMed:19543227). Interacts with APC2 (PubMed:10644998). Interacts with CLASP1 (PubMed:15631994). Interacts with CDK5RAP2 (PubMed:19553473). Interacts with MACF1 (By similarity). Interacts with RABL2/RABL2A; binds preferentially to GTP-bound RABL2 (By similarity). Interacts with KCNAB2 (By similarity). Interacts (via C-terminus) with CLIP1 (PubMed:17563362, PubMed:21646404). Interacts with SLAIN2 and SLAIN1 (PubMed:21646404). Interacts with KIF18B; this interaction is required for efficient accumulation of KIF18B at microtubule plus ends (PubMed:21820309). Interacts with MISP (PubMed:23509069). Interacts with KNSTRN (PubMed:23035123). Interacts with NCKAP5L (PubMed:26485573). Interacts with CAMSAP2 (PubMed:28726242). Interacts with PDE4DIP isoform 13/MMG8/SMYLE; this interaction is required for its recruitment to the Golgi apparatus (PubMed:25217626, PubMed:28814570). Forms a pericentrosomal complex with AKAP9, CDK5RAP2 and PDE4DIP isoform 13/MMG8/SMYLE; within this complex, MAPRE1 binding to CDK5RAP2 may be mediated by PDE4DIP (PubMed:29162697). Interacts with AKNA (By similarity). Interacts with GAS2L1, GAS2L2, and GAS2L3 (PubMed:24706950). {ECO:0000250\|UniProtKB:Q61166, ECO:0000269\|PubMed:10226031, ECO:0000269\|PubMed:10644998, ECO:0000269\|PubMed:11943150, ECO:0000269\|PubMed:12388762, ECO:0000269\|PubMed:14514668, ECO:0000269\|PubMed:15616574, ECO:0000269\|PubMed:15631994, ECO:0000269\|PubMed:16109370, ECO:0000269\|PubMed:16949363, ECO:0000269\|PubMed:17563362, ECO:0000269\|PubMed:19255245, ECO:0000269\|PubMed:19543227, ECO:0000269\|PubMed:19553473, ECO:0000269\|PubMed:19632184, ECO:0000269\|PubMed:21646404, ECO:0000269\|PubMed:21820309, ECO:0000269\|PubMed:23035123, ECO:0000269\|PubMed:23509069, ECO:0000269\|PubMed:23874158, ECO:0000269\|PubMed:24706950, ECO:0000269\|PubMed:25217626, ECO:0000269\|PubMed:26485573, ECO:0000269\|PubMed:28726242, ECO:0000269\|PubMed:28814570, ECO:0000269\|PubMed:29162697, ECO:0000269\|PubMed:7606712}.
Subcellular location:		Cytoplasm, cytoskeleton {ECO:0000269\|PubMed:10188731, ECO:0000269\|PubMed:12388762, ECO:0000269\|PubMed:21646404, ECO:0000269\|PubMed:28814570, ECO:0000269\|PubMed:9724749}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269\|PubMed:12388762, ECO:0000269\|PubMed:14654843}. Golgi apparatus {ECO:0000269\|PubMed:25217626}. Note=Associated with the microtubule growing distal tips (PubMed:28814570). Recruitment to the Golgi apparatus requires the presence of PDE4DIP isoform 13/MMG8/SMYLE (PubMed:25217626). {ECO:0000269\|PubMed:25217626, ECO:0000269\|PubMed:28814570}.
Tissue specificity:		Ubiquitously expressed. {ECO:0000269\|PubMed:10644998}.
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. {ECO:0000269\|PubMed:12388762}.
Similarity:		Belongs to the MAPRE family. {ECO:0000305}.