Reviewed,
UniProtKB/Swiss-Prot P15146 (MAP2_RAT)
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October 13, 2009.
Version 92.
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Microtubule-associated protein 2 Short name=MAP-2 | ||||
| Gene names |
| ||||
| Organism | Rattus norvegicus (Rat) | ||||
| Taxonomic identifier | 10116 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus |
Protein attributes
| Sequence length | 1861 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules. |
| Subcellular location | Cytoplasm › cytoskeleton Probable. |
| Developmental stage | Isoform MAP2C is expressed during embryonic brain development and until postanatal day 10. Isoform MAP2B is expressed throughout brain development. |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. MAP2A/c is phosphorylated. |
| Sequence similarities | Contains 4 Tau/MAP repeats. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton Microtubule |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat |
| Ligand | Calmodulin-binding |
| PTM | Phosphoprotein |
| Gene Ontology (GO) | |
| Biological process | negative regulation of microtubule depolymerization Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW dendriteInferred from direct assay. Source: RGD microtubuleInferred from electronic annotation. Source: UniProtKB-KW rough microsomeInferred from direct assay. Source: RGD smooth microsomeInferred from direct assay. Source: RGD |
| Molecular function | calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 4 isoforms produced by alternative splicing. [Align] [Select] Note: Additional isoforms seem to exist. | ||||||
| Isoform MAP2x (identifier: P15146-1) 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. | ||||||
| Isoform MAP2b (identifier: P15146-2) The sequence of this isoform differs from the canonical sequence as follows: 1695-1725: Missing. | ||||||
| Isoform MAP2c (identifier: P15146-3) The sequence of this isoform differs from the canonical sequence as follows: 152-1514: Missing. 1695-1725: Missing. | ||||||
| Isoform MAP2d (identifier: P15146-4) The sequence of this isoform differs from the canonical sequence as follows: 152-1514: Missing. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1861 | 1861 | Microtubule-associated protein 2 | PRO_0000072749 | |||||
Regions | |||||||||
| Repeat | 1664 – 1694 | 31 | Tau/MAP motif 1 | ||||||
| Repeat | 1695 – 1725 | 31 | Tau/MAP motif 2 | ||||||
| Repeat | 1726 – 1756 | 31 | Tau/MAP motif 3 | ||||||
| Repeat | 1757 – 1788 | 32 | Tau/MAP motif 4 | ||||||
| Region | 1454 – 1474 | 21 | Calmodulin-binding Potential | ||||||
Amino acid modifications | |||||||||
| Modified residue | 63 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 610 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 628 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 657 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 732 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 739 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 748 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 825 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 837 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1162 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1353 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1359 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1427 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1446 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1487 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1541 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1597 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1600 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1601 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1608 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1611 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1614 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1617 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1619 | 1 | Phosphothreonine Ref.7 | ||||||
| Modified residue | 1622 | 1 | Phosphothreonine Ref.7 | ||||||
| Modified residue | 1652 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1659 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1682 | 1 | Phosphoserine; by PKA | ||||||
| Modified residue | 1744 | 1 | Phosphoserine; by PKA | ||||||
| Modified residue | 1776 | 1 | Phosphoserine; by PKA | ||||||
| Modified residue | 1816 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1824 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1832 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1833 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1834 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1836 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 152 – 1514 | 1363 | Missing in isoform MAP2c and isoform MAP2d. | VSP_003198 | |||||
| Alternative sequence | 1695 – 1725 | 31 | Missing in isoform MAP2b and isoform MAP2c. | VSP_003199 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete cDNA sequence encoding rat high and low molecular weight MAP2." Kindler S., Schwanke B., Schulz B., Garner C.C. Nucleic Acids Res. 18:2822-2822(1990) [PubMed: 2339070] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAP2B). Strain: Wistar. Tissue: Brain. |
| [2] | "Molecular structure of microtubule-associated protein 2b and 2c from rat brain." Kindler S., Schulz B., Goedert M., Garner C.C. J. Biol. Chem. 265:19679-19684(1990) [PubMed: 2174050] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAP2B). Strain: Wistar. Tissue: Brain. |
| [3] | "Nucleotide and amino acid sequences of embryonic rat MAP2c." Doll T., Papandrikopoulou A., Matus A. Nucleic Acids Res. 18:361-361(1990) [PubMed: 2326166] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAP2C). |
| [4] | "Embryonic MAP2 lacks the cross-linking sidearm sequences and dendritic targeting signal of adult MAP2." Papandrikopoulou A., Doll T., Tucker R.P., Garner C.C., Matus A. Nature 340:650-652(1989) [PubMed: 2770869] [Abstract] Cited for: DISCUSSION OF SEQUENCE. |
| [5] | "An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif." Doll T., Meichsner M., Riederer B.M., Honegger P., Matus A. J. Cell Sci. 106:633-640(1993) [PubMed: 8282767] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1695-1725 (ISOFORM MAP2X). |
| [6] | "Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton." Ozer R.S., Halpain S. Mol. Biol. Cell 11:3573-3587(2000) [PubMed: 11029056] [Abstract] Cited for: PHOSPHORYLATION. |
| [7] | "Quantitative phosphoproteomics of vasopressin-sensitive renal cells: regulation of aquaporin-2 phosphorylation at two sites." Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A. Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006) [PubMed: 16641100] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1619 AND THR-1622, MASS SPECTROMETRY. Tissue: Kidney. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| X51842 mRNA. Translation: CAA36135.1. X17682 mRNA. Translation: CAA35667.1. X71487 mRNA. Translation: CAA50588.1. | |
| IPI | IPI00206171. IPI00231051. IPI00231052. IPI00231053. |
| PIR | A37981. S33176. I55502. |
| UniGene | Rn.10484 |
3D structure databases | |
| DisProt | DP00122. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | P15146. |
PTM databases | |
| PhosphoSite | P15146. |
Proteomic databases | |
| PRIDE | P15146. |
Genome annotation databases | |
| Ensembl | ENSRNOT00000037974; ENSRNOP00000031915; ENSRNOG00000011841; Rattus norvegicus. [Genome view] ENSRNOT00000045766; ENSRNOP00000050877; ENSRNOG00000011841; Rattus norvegicus. [Genome view] ENSRNOT00000046576; ENSRNOP00000051431; ENSRNOG00000011841; Rattus norvegicus. [Genome view] |
| UCSC | NM_013066. rat. |
Organism-specific databases | |
| RGD | 3044. Mtap2. |
Phylogenomic databases | |
| HOVERGEN | P15146. |
Gene expression databases | |
| ArrayExpress | P15146. |
| Genevestigator | P15146. |
| GermOnline | ENSRNOG00000011841. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR013588. MAP2_projctn. IPR018459. RII_binding_1. IPR001084. Tau_tubulin-bd. [Graphical view] |
| Pfam | PF08377. MAP2_projctn. 1 hit. PF10522. RII_binding_1. 1 hit. PF00418. Tubulin-binding. 4 hits. [Graphical view] |
| PROSITE | PS00229. TAU_MAP. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | MAP2_RAT | ||||||||
| Accession | Primary (citable) accession number: P15146 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
