Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 154 (03 Jul 2019)
Sequence version 3 (10 Oct 2018)
Previous versions | rss
Other tutorials and videosHelp videoFeedback
Protein

Microtubule-associated protein 1B

Gene

Map1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

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). Interacts with TMEM185A (By similarity).By similarity

Caution

A C-terminal fragment of this protein (residues 1599 to 2461) was originally described as neuraxin in PubMed:2555150.Curated

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Microtubule-associated protein 1B
Short name:
MAP-1B
Alternative name(s):
Neuraxin
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Map1b
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2

Organism-specific databases

Rat genome database

More...
RGDi
3043 Map1b

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

Cell junction, Cell projection, Cytoplasm, Cytoskeleton, Microtubule, Synapse

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL3217383

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000186082 – 2461Microtubule-associated protein 1BAdd BLAST2460
ChainiPRO_00004183812 – 2199MAP1B heavy chainAdd BLAST2198
ChainiPRO_00000186092200 – 2461MAP1 light chain LC1Add BLAST262

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei336PhosphoserineCombined sources1
Modified residuei339PhosphoserineCombined sources1
Modified residuei341PhosphoserineCombined sources1
Modified residuei343PhosphoserineCombined sources1
Modified residuei527PhosphothreonineCombined sources1
Modified residuei541PhosphoserineCombined sources1
Modified residuei544PhosphoserineBy similarity1
Modified residuei561PhosphoserineBy similarity1
Modified residuei614PhosphoserineBy similarity1
Modified residuei821PhosphoserineCombined sources1
Modified residuei824PhosphoserineCombined sources1
Modified residuei825PhosphoserineCombined sources1
Modified residuei881PhosphoserineBy similarity1
Modified residuei884PhosphoserineBy similarity1
Modified residuei892PhosphothreonineBy similarity1
Modified residuei901PhosphothreonineBy similarity1
Modified residuei929PhosphoserineCombined sources1
Modified residuei930PhosphoserineCombined sources1
Modified residuei941PhosphothreonineCombined sources1
Modified residuei956PhosphoserineCombined sources1
Modified residuei963PhosphoserineCombined sources1
Modified residuei985PhosphoserineCombined sources1
Modified residuei988PhosphoserineCombined sources1
Modified residuei1009PhosphoserineCombined sources1
Modified residuei1148PhosphoserineBy similarity1
Modified residuei1150PhosphoserineBy similarity1
Modified residuei1180PhosphoserineCombined sources1
Modified residuei1183PhosphoserineCombined sources1
Modified residuei1201PhosphoserineCombined sources1
Modified residuei1204PhosphoserineBy similarity1
Modified residuei1205PhosphoserineBy similarity1
Modified residuei1239PhosphoserineCombined sources1
Modified residuei1244PhosphoserineCombined sources1
Modified residuei1248PhosphoserineCombined sources1
Modified residuei1250PhosphoserineCombined sources1
Modified residuei1252PhosphoserineCombined sources1
Modified residuei1254PhosphoserineCombined sources1
Modified residuei1257PhosphoserineCombined sources1
Modified residuei1268PhosphoserineBy similarity1
Modified residuei1272PhosphoserineBy similarity1
Modified residuei1274PhosphothreonineCombined sources1
Modified residuei1291PhosphoserineBy similarity1
Modified residuei1305PhosphoserineBy similarity1
Modified residuei1315PhosphoserineCombined sources1
Modified residuei1317PhosphoserineBy similarity1
Modified residuei1319PhosphoserineBy similarity1
Modified residuei1321PhosphothreonineBy similarity1
Modified residuei1323PhosphoserineCombined sources1
Modified residuei1332PhosphoserineBy similarity1
Modified residuei1369PhosphoserineBy similarity1
Modified residuei1371PhosphoserineCombined sources1
Modified residuei1380PhosphoserineBy similarity1
Modified residuei1382PhosphoserineCombined sources1
Modified residuei1389PhosphoserineBy similarity1
Modified residuei1393PhosphoserineCombined sources1
Modified residuei1401PhosphoserineBy similarity1
Modified residuei1403PhosphotyrosineBy similarity1
Modified residuei1420PhosphoserineCombined sources1
Modified residuei1436PhosphoserineCombined sources1
Modified residuei1494PhosphoserineCombined sources1
Modified residuei1505PhosphoserineCombined sources1
Modified residuei1513PhosphoserineCombined sources1
Modified residuei1515PhosphoserineCombined sources1
Modified residuei1518PhosphothreonineCombined sources1
Modified residuei1520PhosphoserineCombined sources1
Modified residuei1611PhosphoserineBy similarity1
Modified residuei1613PhosphoserineCombined sources1
Modified residuei1618PhosphoserineCombined sources1
Modified residuei1646PhosphoserineCombined sources1
Modified residuei1656PhosphoserineCombined sources1
Modified residuei1659PhosphoserineCombined sources1
Modified residuei1683PhosphoserineBy similarity1
Modified residuei1765PhosphoserineCombined sources1
Modified residuei1772PhosphoserineCombined sources1
Modified residuei1775PhosphoserineBy similarity1
Modified residuei1778PhosphoserineCombined sources1
Modified residuei1781PhosphothreonineCombined sources1
Modified residuei1785PhosphoserineBy similarity1
Modified residuei1786PhosphoserineBy similarity1
Modified residuei1789PhosphotyrosineBy similarity1
Modified residuei1790PhosphoserineBy similarity1
Modified residuei1794PhosphoserineBy similarity1
Modified residuei1812PhosphoserineCombined sources1
Modified residuei1870PhosphoserineCombined sources1
Modified residuei1874PhosphoserineCombined sources1
Modified residuei1908PhosphoserineCombined sources1
Modified residuei1912PhosphoserineBy similarity1
Modified residuei1925PhosphothreonineCombined sources1
Modified residuei1932PhosphoserineBy similarity1
Modified residuei1942PhosphothreonineCombined sources1
Modified residuei2027PhosphoserineCombined sources1
Modified residuei2057Omega-N-methylarginineBy similarity1
Modified residuei2202PhosphoserineBy similarity1
Modified residuei2264PhosphoserineBy similarity1
Modified residuei2282PhosphoserineBy similarity1
Modified residuei2298PhosphothreonineBy similarity1
Modified residuei2407PhosphoserineBy similarity1
Modified residuei2457S-nitrosocysteineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

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).By similarity
S-nitrosylation at Cys-2457 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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, S-nitrosylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P15205

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P15205

PRoteomics IDEntifications database

More...
PRIDEi
P15205

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P15205

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P15205

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Nervous system (spinal cord, brain stem, cerebellum and cerebrum). Not expressed in liver, spleen, kidney, heart or muscle.1 Publication

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

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.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

By nerve growth factor.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000017428 Expressed in 10 organ(s), highest expression level in brain

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

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 with the tubulin tyrosine TTL (By similarity).

Interacts (via C-terminus) with GAN (via Kelch domains).

Interacts (via N-terminus) with DAPK1.

Interacts with TMEM185A.

Interacts with MAP1LC3B.

Interacts with KIRREL3 (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
248099, 9 interactors

Protein interaction database and analysis system

More...
IntActi
P15205, 4 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000023460

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section indicates the positions and types of repeated sequence motifs or repeated domains within the protein.<p><a href='/help/repeat' target='_top'>More...</a></p>Repeati1871 – 1887MAP1B 1CuratedAdd BLAST17
Repeati1888 – 1904MAP1B 2CuratedAdd BLAST17
Repeati1905 – 1921MAP1B 3CuratedAdd BLAST17
Repeati1922 – 1938MAP1B 4CuratedAdd BLAST17
Repeati1939 – 1955MAP1B 5CuratedAdd BLAST17
Repeati1956 – 1972MAP1B 6CuratedAdd BLAST17
Repeati1990 – 2006MAP1B 7CuratedAdd BLAST17
Repeati2007 – 2023MAP1B 8CuratedAdd BLAST17
Repeati2024 – 2040MAP1B 9CuratedAdd BLAST17
Repeati2041 – 2057MAP1B 10CuratedAdd BLAST17

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni2287 – 2459Mediates interaction with TMEM185ABy similarityAdd BLAST173

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi560 – 1036Glu-richPROSITE-ProRule annotationAdd BLAST477
Compositional biasi589 – 787Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)CuratedAdd BLAST199
Compositional biasi2226 – 2314Lys-richPROSITE-ProRule annotationAdd BLAST89

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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.1 Publication

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the MAP1 family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3592 Eukaryota
ENOG410XRYM LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155897

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000063256

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P15205

KEGG Orthology (KO)

More...
KOi
K10429

Identification of Orthologs from Complete Genome Data

More...
OMAi
YETSDQC

Database of Orthologous Groups

More...
OrthoDBi
86642at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P15205

TreeFam database of animal gene trees

More...
TreeFami
TF350229

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR026074 MAP1
IPR027321 MAP1B
IPR000102 MAP1B_neuraxin

The PANTHER Classification System

More...
PANTHERi
PTHR13843 PTHR13843, 1 hit
PTHR13843:SF5 PTHR13843:SF5, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00414 MAP1B_neuraxin, 6 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00230 MAP1B_NEURAXIN, 8 hits

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P15205-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MATVVVEATE PEPSGSIGNP AATTSPSLSH RFLDSKFYLL VVVGETVTEE
60 70 80 90 100
HLRRAIGNIE LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL
110 120 130 140 150
HHRSDVLETV VLINPSDEAV STEVRLMITD AARHKLLVLT GQCFENTGEL
160 170 180 190 200
ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP ANKASLTLFC PEEGDWKNSN
210 220 230 240 250
LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP SPFDILEPPT
260 270 280 290 300
SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH
310 320 330 340 350
LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEERSQGST SNSDWMKNLI
360 370 380 390 400
SPDLGVVFLN VPENLKNPEP NIKMKRSTEE ACFTLQYLNK LSMKPEPLFR
410 420 430 440 450
SVGNAIEPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE
460 470 480 490 500
LILPNGQEVD IPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE
510 520 530 540 550
GLEKLKHLDF LKQPLATQKD LTGQVSTPPV KQVKLKQRAD SRESLKPATK
560 570 580 590 600
PLSSKSVRKE SKEEAPEATK ASQVEKTPKV ESKEKVIVKK DKPGKVESKP
610 620 630 640 650
SVTEKEVPSK EEQSPVKAEV AEKAATESKP KVTKDKVVKK EIKTKPEEKK
660 670 680 690 700
EEKPKKEVAK KEDKTPLKKD EKPKKEEAKK EIKKEIKKEE KKELKKEVKK
710 720 730 740 750
ETPLKDAKKE VKKDEKKEVK KEEKEPKKEI KKISKDIKKS TPLSDTKKPA
760 770 780 790 800
ALKPKVAKKE EPTKKEPIAA GKLKDKGKVK VIKKEGKTTE AAATAVGTAA
810 820 830 840 850
VAAAAGVAAS GPAKELEAER SLMSSPEDLT KDFEELKAEE IDVAKDIKPQ
860 870 880 890 900
LELIEDEEKL KETEPGEAYV IQKETEVSKG SAESPDEGIT TTEGEGECEQ
910 920 930 940 950
TPEELEPVEK QGVDDIEKFE DEGAGFEESS EAGDYEEKAE TEEAEEPEED
960 970 980 990 1000
GEDNVSGSAS KHSPTEDEEI AKAEADVHIK EKRESVASGD DRAEEDMDEA
1010 1020 1030 1040 1050
LEKGEAEQSE EEGEEEEDKA EDAREEDHEP DKTEAEDYVM AVVDKAAEAG
1060 1070 1080 1090 1100
VTEDQYGFLG TPAKQPGVQS PSREPASSIH DETLPGGSES EATASDEENR
1110 1120 1130 1140 1150
EDQPEEFTAT SGYTQSTIEI SSEPTPMDEM STPRDVMSDE TNNEETESPS
1160 1170 1180 1190 1200
QEFVNITKYE SSLYSQEYSK PVVASFNGLS DGSKTDATDG RDYNASASTI
1210 1220 1230 1240 1250
SPPSSMEEDK FSKSALRDAY RPEETDVKTG AELDIKDVSD ERLSPAKSPS
1260 1270 1280 1290 1300
LSPSPPSPIE KTPLGERSVN FSLTPNEIKA SAEGEATAVV SPGVTQAVVE
1310 1320 1330 1340 1350
EHCASPEEKT LEVVSPSQSV TGSAGHTPYY QSPTDEKSSH LPTEVTEKPQ
1360 1370 1380 1390 1400
AVPVSFEFTE AKDENERSSI SPMDEPVPDS ESPIEKVLSP LRSPPLIGSE
1410 1420 1430 1440 1450
SAYEDFLSAD DKALGRRSES PFEGKNGKQG FSDKESPVSD LTSDLYQDKQ
1460 1470 1480 1490 1500
EEKSAGFIPI KEDFSPEKKA SDAEIMSSQS ALALDERKLG GDGSPTQVDV
1510 1520 1530 1540 1550
SQFGSFKEDT KMSISEGTVS DKSATPVDEG VAEDTYSHME GVASVSTASV
1560 1570 1580 1590 1600
ATSSFPEPTT DDVSPSLHAE VGSPHSTEVD DSLSVSVVQT PTTFQETEMS
1610 1620 1630 1640 1650
PSKEECPRPM SISPPDFSPK TAKSRTPVQD HRSEQSSMSI EFGQESPEHS
1660 1670 1680 1690 1700
LAMDFSRQSP DHPTVGAGML HITENGPTEV DYSPSDIQDS SLSHKIPPTE
1710 1720 1730 1740 1750
EPSYTQDNDL SELISVSQVE ASPSTSSAHT PSQIASPLQE DTLSDVVPPR
1760 1770 1780 1790 1800
DMSLYASLAS EKVQSLEGEK LSPKSDISPL TPRESSPTYS PGFSDSTSGA
1810 1820 1830 1840 1850
KESTAAYQTS SSPPIDAAAA EPYGFRSSML FDTMQHHLAL SRDLTTSSVE
1860 1870 1880 1890 1900
KDNGGKTPGD FNYAYQKPES TTESPDEEDY DYESHEKTIQ AHDVGGYYYE
1910 1920 1930 1940 1950
KTERTIKSPC DSGYSYETIE KTTKTPEDGG YSCEITEKTT RTPEEGGYSY
1960 1970 1980 1990 2000
EISEKTTRTP EVSGYTYEKT ERSRRLLDDI SNGYDDTEDG GHTLGDCSYS
2010 2020 2030 2040 2050
YETTEKITSF PESESYSYET TTKTTRSPDT SAYCYETMEK ITKTPQASTY
2060 2070 2080 2090 2100
SYETSDRCYT PERKSPSEAR QDVDLCLVSS CEFKHPKTEL SPSFINPNPL
2110 2120 2130 2140 2150
EWFAGEEPTE ESEKPLTQSG GAPPPSGGKQ QGRQCDETPP TSVSESAPSQ
2160 2170 2180 2190 2200
TDSDVPPETE ECPSITADAN IDSEDESETI PTDKTVTYKH MDPPPAPMQD
2210 2220 2230 2240 2250
RSPSPRHPDV SMVDPEALAI EQNLGKALKK DLKEKAKTKK PGTKTKSSSP
2260 2270 2280 2290 2300
VKKGDGKSKP SAASPKPGAL KESSDKVSRV ASPKKKESVE KAMKTTTTPE
2310 2320 2330 2340 2350
VKATRGEEKD KETKNAANAS ASKSVKTATA GPGTTKTAKS STVPPGLPVY
2360 2370 2380 2390 2400
LDLCYIPNHS NSKNVDVEFF KRVRSSYYVV SGNDPAAEEP SRAVLDALLE
2410 2420 2430 2440 2450
GKAQWGSNMQ VTLIPTHDSE VMREWYQETH EKQQDLNIMV LASSSTVVMQ
2460
DESFPACKIE L
Length:2,461
Mass (Da):269,643
Last modified:October 10, 2018 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB9E2ED2B5F3742A4
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAI58859 differs from that shown. Contaminating sequence. Potential poly-A sequence.Curated
The sequence CAA34620 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti67D → E in AAB17068 (PubMed:8666295).Curated1
Sequence conflicti127M → V in AAB17068 (PubMed:8666295).Curated1
Sequence conflicti140T → S in AAB17068 (PubMed:8666295).Curated1
Sequence conflicti335Missing in CAC16162 (PubMed:1639092).Curated1
Sequence conflicti421E → K in CAC16162 (PubMed:1639092).Curated1
Sequence conflicti467T → A in CAC16162 (PubMed:1639092).Curated1
Sequence conflicti575E → K in AAI58859 (PubMed:15489334).Curated1
Sequence conflicti1057G → D in CAC16162 (PubMed:1639092).Curated1
Sequence conflicti1138S → T in CAC16162 (PubMed:1639092).Curated1
Sequence conflicti1348 – 1349KP → NA in CAC16162 (PubMed:1639092).Curated2
Sequence conflicti1454S → R in CAC16162 (PubMed:1639092).Curated1
Sequence conflicti1531Missing in CAC16162 (PubMed:1639092).Curated1
Sequence conflicti2114K → R in CAC16162 (PubMed:1639092).Curated1
Sequence conflicti2171I → L in CAC16162 (PubMed:1639092).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AABR07007833 Genomic DNA No translation available.
AABR07007832 Genomic DNA No translation available.
BC158858 mRNA Translation: AAI58859.1 Sequence problems.
U52950 mRNA Translation: AAB17068.1
X60370 mRNA Translation: CAC16162.1
X16623 mRNA Translation: CAA34620.1 Different initiation.

Protein sequence database of the Protein Information Resource

More...
PIRi
A56577

NCBI Reference Sequences

More...
RefSeqi
NP_062090.1, NM_019217.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000023460; ENSRNOP00000023460; ENSRNOG00000017428

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29456

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:29456

UCSC genome browser

More...
UCSCi
RGD:3043 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07007833 Genomic DNA No translation available.
AABR07007832 Genomic DNA No translation available.
BC158858 mRNA Translation: AAI58859.1 Sequence problems.
U52950 mRNA Translation: AAB17068.1
X60370 mRNA Translation: CAC16162.1
X16623 mRNA Translation: CAA34620.1 Different initiation.
PIRiA56577
RefSeqiNP_062090.1, NM_019217.1

3D structure databases

Database of comparative protein structure models

More...
ModBasei
Search...

SWISS-MODEL Interactive Workspace

More...
SWISS-MODEL-Workspacei
Submit a new modelling project...

Protein-protein interaction databases

BioGridi248099, 9 interactors
IntActiP15205, 4 interactors
STRINGi10116.ENSRNOP00000023460

Chemistry databases

ChEMBLiCHEMBL3217383

PTM databases

iPTMnetiP15205
PhosphoSitePlusiP15205

Proteomic databases

jPOSTiP15205
PaxDbiP15205
PRIDEiP15205

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000023460; ENSRNOP00000023460; ENSRNOG00000017428
GeneIDi29456
KEGGirno:29456
UCSCiRGD:3043 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
4131
RGDi3043 Map1b

Phylogenomic databases

eggNOGiKOG3592 Eukaryota
ENOG410XRYM LUCA
GeneTreeiENSGT00940000155897
HOGENOMiHOG000063256
InParanoidiP15205
KOiK10429
OMAiYETSDQC
OrthoDBi86642at2759
PhylomeDBiP15205
TreeFamiTF350229

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P15205

Gene expression databases

BgeeiENSRNOG00000017428 Expressed in 10 organ(s), highest expression level in brain

Family and domain databases

InterProiView protein in InterPro
IPR026074 MAP1
IPR027321 MAP1B
IPR000102 MAP1B_neuraxin
PANTHERiPTHR13843 PTHR13843, 1 hit
PTHR13843:SF5 PTHR13843:SF5, 1 hit
PfamiView protein in Pfam
PF00414 MAP1B_neuraxin, 6 hits
PROSITEiView protein in PROSITE
PS00230 MAP1B_NEURAXIN, 8 hits

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiMAP1B_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P15205
Secondary accession number(s): B0BNK3
, F1LRL9, Q62958, Q9ER21, Q9QW92
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: October 10, 2018
Last modified: July 3, 2019
This is version 154 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again