P15205 (MAP1B_RAT) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 109.
History...
Clusters with 
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Microtubule-associated protein 1B Short name=MAP-1B Alternative name(s): Neuraxin Cleaved into the following 2 chains: | ||
| Gene names |
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| Organism | Rattus norvegicus (Rat) [Reference proteome] | ||
| 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 | 2459 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 | Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B Binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing. Facilitates tyrosination of alpha-tubulin in neuronal microtubules. Required for synaptic maturation By similarity. |
| Subunit structure | 3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2. Interacts (via C-terminus) with GAN (via Kelch domains) By similarity. Interacts (via N-terminus) with DAPK1 By similarity. Interacts with the tubulin tyrosine TTL By similarity. |
| Subcellular location | Cytoplasm › cytoskeleton Probable. Cytoplasm By similarity. Cell junction › synapse By similarity. Cell projection › dendritic spine By similarity. Note: Colocalizes with DAPK1 in the microtubules and cortical actin fibers By similarity. |
| Tissue specificity | Nervous system (spinal cord, brain stem, cerebellum and cerebrum). Not expressed in liver, spleen, kidney, heart or muscle. Ref.3 |
| Developmental stage | In cerebral cortex, spinal cord and sciatic nerve levels are high early in development but decrease during postnatal development and are low in adults. In dorsal root ganglia levels remain high throughout development. Ref.4 |
| Induction | By nerve growth factor. Ref.2 |
| Domain | Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules. Ref.2 |
| Post-translational modification | LC1 is coexpressed with MAP1B. It is a polypeptide generated from MAP1B by proteolytic processing. It is free to associate with both MAP1A and MAP1B. It interacts with the N-terminal region of MAP1B By similarity. S-nitrosylation at Cys-2455 enhances interaction with microtubules, and may act as an effector modification for neuronal nitric oxide synthase control of growth-cone size, growth-cone collapse and axon retraction By similarity. |
| Sequence similarities | Belongs to the MAP1 family. |
| Caution | A C-terminal fragment of this protein (residues 1597 to 2459) was originally described as neuraxin in Ref.3. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed By similarity | ||||||
| Chain | 2 – 2459 | 2458 | Microtubule-associated protein 1B | PRO_0000018608 | |||||
| Chain | 2 – 2197 | 2196 | MAP1B heavy chain | PRO_0000418381 | |||||
| Chain | 2198 – 2459 | 262 | MAP1 light chain LC1 | PRO_0000018609 | |||||
Regions | |||||||||
| Repeat | 1869 – 1885 | 17 | MAP1B 1 | ||||||
| Repeat | 1886 – 1902 | 17 | MAP1B 2 | ||||||
| Repeat | 1903 – 1919 | 17 | MAP1B 3 | ||||||
| Repeat | 1920 – 1936 | 17 | MAP1B 4 | ||||||
| Repeat | 1937 – 1953 | 17 | MAP1B 5 | ||||||
| Repeat | 1954 – 1970 | 17 | MAP1B 6 | ||||||
| Repeat | 1988 – 2004 | 17 | MAP1B 7 | ||||||
| Repeat | 2005 – 2021 | 17 | MAP1B 8 | ||||||
| Repeat | 2022 – 2038 | 17 | MAP1B 9 | ||||||
| Repeat | 2039 – 2055 | 17 | MAP1B 10 | ||||||
| Compositional bias | 559 – 1035 | 477 | Glu-rich | ||||||
| Compositional bias | 588 – 786 | 199 | Lys-rich (highly basic, contains many KKEE and KKEI/V repeats) | ||||||
| Compositional bias | 2224 – 2312 | 89 | Lys-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine By similarity | ||||||
| Modified residue | 335 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 526 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 540 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 543 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 560 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 613 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 820 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 823 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 824 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 929 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 984 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 987 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1008 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1147 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1149 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1200 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1243 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1247 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1251 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 1256 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 1267 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1271 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1273 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1304 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1314 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1316 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1328 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 1329 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 1331 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1368 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1370 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1379 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1381 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1388 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1392 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1400 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1419 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1435 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1493 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 1609 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1611 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1616 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1644 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1763 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1770 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1773 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1776 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1779 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1784 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1787 | 1 | Phosphotyrosine By similarity | ||||||
| Modified residue | 1788 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1808 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1810 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1872 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1906 | 1 | Phosphoserine Ref.5 | ||||||
| Modified residue | 1923 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 1940 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 2025 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2063 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2089 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2262 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2280 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 2455 | 1 | S-nitrosocysteine By similarity | ||||||
Experimental info | |||||||||
| Sequence conflict | 127 | 1 | M → V in AAB17068. Ref.1 | ||||||
| Sequence conflict | 140 | 1 | T → S Ref.1 | ||||||
| Sequence conflict | 2112 | 1 | R → K in CAA34620. Ref.3 | ||||||
| Sequence conflict | 2169 | 1 | L → I in CAA34620. Ref.3 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Isolation and sequencing of the 5' end of the rat microtubule-associated protein (MAP1B)-encoding cDNA." Liu D., Fischer I. Gene 171:307-308(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-142. Strain: Sprague-Dawley. Tissue: Testis. |
| [2] | "Identification of two distinct microtubule binding domains on recombinant rat MAP 1B." Zauner W., Kratz J., Staunton J., Feick P., Wiche G. Eur. J. Cell Biol. 57:66-74(1992) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 96-2459, DOMAIN, INDUCTION. Strain: Sprague-Dawley. Tissue: Brain and Glial tumor. |
| [3] | "Neuraxin, a novel putative structural protein of the rat central nervous system that is immunologically related to microtubule-associated protein 5." Rienitz A., Grenningloh G., Hermans-Borgmeyer I., Kirsch J., Littauer U.Z., Prior P., Gundelfinger E.D., Schmitt B., Betz H. EMBO J. 8:2879-2888(1989) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1541-2459, TISSUE SPECIFICITY. Tissue: Spinal cord. |
| [4] | "Differential regulation of microtubule-associated protein 1B (MAP1B) in rat CNS and PNS during development." Ma D., Nothias F., Boyne L.J., Fischer I. J. Neurosci. Res. 49:319-332(1997) [PubMed] [Europe PMC] [Abstract] Cited for: DEVELOPMENTAL STAGE, PHOSPHORYLATION. |
| [5] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1251; SER-1256; SER-1493 AND SER-1906, MASS SPECTROMETRY. Tissue: Renal collecting duct. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U52950 mRNA. Translation: AAB17068.1. X60370 mRNA. Translation: CAC16162.1. X16623 mRNA. Translation: CAA34620.1. Sequence problems. |
| IPI | IPI00372009. |
| PIR | A56577. |
| RefSeq | NP_062090.1. NM_019217.1. |
| UniGene | Rn.220177. Rn.98152. |
3D structure databases | |
| ProteinModelPortal | P15205. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | P15205. 1 interaction. |
PTM databases | |
| PhosphoSite | P15205. |
Proteomic databases | |
| PaxDb | P15205. |
| PRIDE | P15205. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 29456. |
| KEGG | rno:29456. |
| UCSC | RGD:3043. rat. |
Organism-specific databases | |
| CTD | 4131. |
| RGD | 3043. Map1b. |
Phylogenomic databases | |
| eggNOG | NOG12793. |
| HOGENOM | HOG000063256. |
| HOVERGEN | HBG052409. |
| InParanoid | P15205. |
| KO | K10429. |
| OrthoDB | EOG44XJFW. |
Gene expression databases | |
| ArrayExpress | P15205. |
| Genevestigator | P15205. |
| GermOnline | ENSRNOG00000017428. Rattus norvegicus. |
Family and domain databases | |
| InterPro | IPR026074. MAP1. IPR027321. MAP1B. IPR000102. MAP1B_neuraxin. [Graphical view] |
| PANTHER | PTHR13843. PTHR13843. 1 hit. PTHR13843:SF5. PTHR13843:SF5. 1 hit. |
| Pfam | PF00414. MAP1B_neuraxin. 6 hits. [Graphical view] |
| PROSITE | PS00230. MAP1B_NEURAXIN. 8 hits. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 609232. |
Entry information
| Entry name | MAP1B_RAT | ||||||||
| Accession | Primary (citable) accession number: P15205 Secondary accession number(s): Q62958, Q9ER21, Q9QW92 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |