Q9QYR6 (MAP1A_MOUSE) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 93.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Microtubule-associated protein 1A Short name=MAP-1A Cleaved into the following chain: | ||||
| Gene names |
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| Organism | Mus musculus (Mouse) | ||||
| Taxonomic identifier | 10090 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus |
Protein attributes
| Sequence length | 2776 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Structural protein involved in the filamentous cross-bridging between microtubules and other skeletal elements. |
| Subunit structure | 3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. Interacts with guanylate kinase-like domain of DLG1, DLG2 and DLG4. Binds to CSNK1D By similarity. Interacts with TIAM2. Ref.5 |
| Subcellular location | Cytoplasm › cytoskeleton Probable. |
| Tissue specificity | Both isoforms highly expressed in brain, and to a lesser extent in embryo. Isoform 1 is also expressed at a low level in other tissues including heart and muscle. Ref.3 |
| Domain | The basic region containing the repeats may be responsible for the binding of MAP1A to microtubules. |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylated by MAP1A By similarity. Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 LC2 is generated from MAP1A by proteolytic processing. It is free to associate with both MAP1A and MAP1B By similarity. |
| Sequence similarities | Belongs to the MAP1 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton Microtubule |
| Coding sequence diversity | Alternative splicing |
| Domain | Repeat |
| PTM | Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | sensory perception of sound Inferred from direct assay. Source: MGI |
| Cellular component | cytosol Inferred from direct assay. Source: MGI microtubuleInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | protein binding Inferred from physical interaction. Source: MGI |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q9QYR6-1) 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 2 (identifier: Q9QYR6-2) The sequence of this isoform differs from the canonical sequence as follows: 1-1: M → METTPELGLQ...LNPEPVLPTM |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2776 | 2776 | Microtubule-associated protein 1A | PRO_0000072753 | |||||
| Chain | ?2466 – 2776 | 311 | MAP1 light chain LC2 | PRO_0000269727 | |||||
Regions | |||||||||
| Repeat | 336 – 338 | 3 | 1 | ||||||
| Repeat | 415 – 417 | 3 | 2 | ||||||
| Repeat | 420 – 422 | 3 | 3 | ||||||
| Repeat | 424 – 426 | 3 | 4 | ||||||
| Repeat | 427 – 429 | 3 | 5 | ||||||
| Repeat | 431 – 433 | 3 | 6 | ||||||
| Repeat | 436 – 438 | 3 | 7 | ||||||
| Repeat | 440 – 442 | 3 | 8 | ||||||
| Repeat | 444 – 446 | 3 | 9 | ||||||
| Repeat | 449 – 451 | 3 | 10 | ||||||
| Repeat | 539 – 541 | 3 | 11 | ||||||
| Region | 336 – 541 | 206 | 11 X 3 AA approximate repeats of K-K-[DE] | ||||||
| Compositional bias | 338 – 677 | 340 | Glu-rich | ||||||
| Compositional bias | 1748 – 2303 | 556 | Pro-rich | ||||||
| Compositional bias | 2530 – 2551 | 22 | Pro-rich | ||||||
| Compositional bias | 2747 – 2750 | 4 | Poly-Gln | ||||||
Amino acid modifications | |||||||||
| Modified residue | 114 | 1 | Phosphoserine Ref.8 | ||||||
| Modified residue | 177 | 1 | Phosphotyrosine Ref.7 | ||||||
| Modified residue | 504 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 526 | 1 | Phosphoserine Ref.4 Ref.6 Ref.10 | ||||||
| Modified residue | 527 | 1 | Phosphoserine Ref.4 Ref.6 Ref.8 Ref.9 Ref.10 | ||||||
| Modified residue | 611 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 633 | 1 | Phosphothreonine Ref.4 Ref.8 | ||||||
| Modified residue | 644 | 1 | Phosphoserine Ref.4 | ||||||
| Modified residue | 667 | 1 | Phosphoserine Ref.4 Ref.9 | ||||||
| Modified residue | 772 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 895 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 899 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 991 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 1008 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1062 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1147 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1205 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1310 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1313 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1634 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1648 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1747 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1762 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1768 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1772 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1789 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1990 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1993 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2082 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 2226 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2230 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2234 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2235 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2344 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2425 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 | 1 | M → METTPELGLQSLGAPPAQNP AEPLCEAGAAVAAARWDLRK YSLLIVIGDIGTESQLRAVR AHLEQGILSWNIDLSSFDLN QQLRLFITRHLAHFSSEVKG QRTLCHQSETLETIILVNPT ADSISSEVHHLLSSPSAHKL LILSGQTLEPEGDLILQSGT YSYQNFAQVLHKPEIAQLLS NRDPGIQAFLTVSCLGEGDW SHLGLSSSQETLHLRLNPEP VLPTM in isoform 2. | VSP_003201 | |||||
Experimental info | |||||||||
| Sequence conflict | 349 | 1 | R → C in BAE27940. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The transcriptional landscape of the mammalian genome." Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. Hayashizaki Y.Science 309:1559-1563(2005) [PubMed: 16141072] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Strain: C57BL/6J. Tissue: Corpora quadrigemina. |
| [2] | "Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. Ponting C.P.PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6J. |
| [3] | "Characterization of two promoters that regulate alternative transcripts in the microtubule-associated protein (MAP) 1A gene." Nakayama A., Odajima T., Murakami H., Mori N., Takahashi M. Biochim. Biophys. Acta 1518:260-266(2001) [PubMed: 11311937] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-224 (ISOFORMS 1 AND 2), TISSUE SPECIFICITY. Tissue: Brain. |
| [4] | "Comprehensive identification of phosphorylation sites in postsynaptic density preparations." Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L. Mol. Cell. Proteomics 5:914-922(2006) [PubMed: 16452087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526; SER-527; THR-633; SER-644 AND SER-667, MASS SPECTROMETRY. Tissue: Brain. |
| [5] | "Rho-kinase modulates the function of STEF, a Rac GEF, through its phosphorylation." Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T., Nakayama M., Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K., Amano M. Biochem. Biophys. Res. Commun. 355:788-794(2007) [PubMed: 17320046] [Abstract] Cited for: INTERACTION WITH TIAM2. |
| [6] | "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells." Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D. J. Proteome Res. 6:3174-3186(2007) [PubMed: 17622165] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-527, MASS SPECTROMETRY. Tissue: Teratocarcinoma. |
| [7] | "Large-scale identification and evolution indexing of tyrosine phosphorylation sites from murine brain." Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P. J. Proteome Res. 7:311-318(2008) [PubMed: 18034455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-177, MASS SPECTROMETRY. Tissue: Brain. |
| [8] | "Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations." Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F., Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B., Panse C., Schlapbach R., Mansuy I.M. Mol. Cell. Proteomics 6:283-293(2007) [PubMed: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114; SER-527 AND THR-633, MASS SPECTROMETRY. Tissue: Brain cortex. |
| [9] | "Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-527; SER-667; SER-991 AND SER-2082, MASS SPECTROMETRY. Tissue: Melanoma. |
| [10] | "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry." Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J. Mol. Cell. Proteomics 8:904-912(2009) [PubMed: 19131326] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-526 AND SER-527, MASS SPECTROMETRY. Tissue: Embryonic fibroblast. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK147474 mRNA. Translation: BAE27940.1. AK160546 mRNA. Translation: BAE35863.1. AK163468 mRNA. Translation: BAE37354.1. AL845466 Genomic DNA. Translation: CAM24218.1. AF182211, AF182208, AF182209 Genomic DNA. Translation: AAF06164.1. AF182211 Genomic DNA. Translation: AAF06163.1. AF182213 mRNA. Translation: AAD55790.1. AF182212 mRNA. Translation: AAD55789.1. |
| IPI | IPI00408909. IPI00676243. |
| RefSeq | NP_001166977.1. NM_001173506.1. NP_115769.1. NM_032393.2. |
| UniGene | Mm.36501. |
3D structure databases | |
| ProteinModelPortal | Q9QYR6. |
| SMR | Q9QYR6. Positions 44-105. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q9QYR6. 3 interactions. |
| MINT | MINT-1203191. |
| STRING | Q9QYR6. |
PTM databases | |
| PhosphoSite | Q9QYR6. |
Proteomic databases | |
| PRIDE | Q9QYR6. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENSMUST00000110639; ENSMUSP00000106269; ENSMUSG00000027254. |
| GeneID | 17754. |
| KEGG | mmu:17754. |
| UCSC | uc008lyj.2. mouse. |
Organism-specific databases | |
| CTD | 17754. |
| MGI | MGI:1306776. Mtap1a. |
Phylogenomic databases | |
| eggNOG | roNOG14193. |
| GeneTree | ENSGT00550000074593. |
| HOVERGEN | HBG052408. |
| InParanoid | Q9QYR6. |
| OrthoDB | EOG483D46. |
Gene expression databases | |
| ArrayExpress | Q9QYR6. |
| Bgee | Q9QYR6. |
| CleanEx | MM_MTAP1A. |
| Genevestigator | Q9QYR6. |
| GermOnline | ENSMUSG00000027254. Mus musculus. |
Family and domain databases | |
| KO | K10429. |
| ProtoNet | Search... |
Other | |
| SOURCE | Search... |
Entry information
| Entry name | MAP1A_MOUSE | ||||||||
| Accession | Primary (citable) accession number: Q9QYR6 Secondary accession number(s): A2ARN9 Q9QZI1 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| MGD cross-references Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with