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P14873

- MAP1B_MOUSE

UniProt

P14873 - MAP1B_MOUSE

Protein

Microtubule-associated protein 1B

Gene

Map1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      Previous versions | rss
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    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 By similarity. Facilitates tyrosination of alpha-tubulin in neuronal microtubules. Required for synaptic maturation.By similarity2 Publications

    GO - Molecular functioni

    1. cytoskeletal regulatory protein binding Source: MGI
    2. hydrolase activity Source: InterPro
    3. protein binding Source: IntAct

    GO - Biological processi

    1. axon extension Source: MGI
    2. axonogenesis Source: MGI
    3. dendrite development Source: MGI
    4. establishment of monopolar cell polarity Source: MGI
    5. microtubule-based process Source: MGI
    6. microtubule bundle formation Source: MGI
    7. mitochondrion transport along microtubule Source: MGI
    8. negative regulation of intracellular transport Source: MGI
    9. positive regulation of axon extension Source: MGI

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Microtubule-associated protein 1B
    Short name:
    MAP-1B
    Alternative name(s):
    MAP1(X)
    MAP1.2
    Cleaved into the following 2 chains:
    Gene namesi
    Name:Map1b
    Synonyms:Mtap1b, Mtap5
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:1306778. Map1b.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. Cytoplasm By similarity. Cell junctionsynapse 1 Publication. Cell projectiondendritic spine 1 Publication
    Note: Colocalizes with DAPK1 in the microtubules and cortical actin fibers.By similarity

    GO - Cellular componenti

    1. cell junction Source: UniProtKB-KW
    2. cytosol Source: MGI
    3. dendritic spine Source: UniProtKB-SubCell
    4. microtubule Source: UniProtKB-KW
    5. microtubule associated complex Source: MGI
    6. plasma membrane Source: Ensembl
    7. synapse Source: UniProtKB-SubCell

    Keywords - Cellular componenti

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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 24642463Microtubule-associated protein 1BPRO_0000018606Add
    BLAST
    Chaini2 – 22022201MAP1B heavy chainPRO_0000418380Add
    BLAST
    Chaini2203 – 2464262MAP1 light chain LC1PRO_0000018607Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanineBy similarity
    Modified residuei336 – 3361PhosphoserineBy similarity
    Modified residuei541 – 5411Phosphoserine1 Publication
    Modified residuei544 – 5441Phosphoserine1 Publication
    Modified residuei561 – 5611Phosphoserine1 Publication
    Modified residuei614 – 6141Phosphoserine1 Publication
    Modified residuei825 – 8251PhosphoserineBy similarity
    Modified residuei828 – 8281PhosphoserineBy similarity
    Modified residuei829 – 8291PhosphoserineBy similarity
    Modified residuei934 – 9341PhosphoserineBy similarity
    Modified residuei989 – 9891Phosphoserine1 Publication
    Modified residuei992 – 9921PhosphoserineBy similarity
    Modified residuei1013 – 10131Phosphoserine1 Publication
    Modified residuei1141 – 11411PhosphoserineBy similarity
    Modified residuei1151 – 11511PhosphoserineBy similarity
    Modified residuei1153 – 11531PhosphoserineBy similarity
    Modified residuei1204 – 12041PhosphoserineBy similarity
    Modified residuei1247 – 12471PhosphoserineBy similarity
    Modified residuei1251 – 12511PhosphoserineBy similarity
    Modified residuei1255 – 12551PhosphoserineBy similarity
    Modified residuei1260 – 12601Phosphoserine1 Publication
    Modified residuei1271 – 12711PhosphoserineBy similarity
    Modified residuei1275 – 12751PhosphoserineBy similarity
    Modified residuei1277 – 12771PhosphothreonineBy similarity
    Modified residuei1307 – 13071Phosphoserine1 Publication
    Modified residuei1373 – 13731PhosphoserineBy similarity
    Modified residuei1382 – 13821PhosphoserineBy similarity
    Modified residuei1384 – 13841PhosphoserineBy similarity
    Modified residuei1391 – 13911Phosphoserine1 Publication
    Modified residuei1395 – 13951Phosphoserine1 Publication
    Modified residuei1422 – 14221PhosphoserineBy similarity
    Modified residuei1438 – 14381Phosphoserine2 Publications
    Modified residuei1497 – 14971Phosphoserine1 Publication
    Modified residuei1614 – 16141PhosphoserineBy similarity
    Modified residuei1616 – 16161PhosphoserineBy similarity
    Modified residuei1621 – 16211PhosphoserineBy similarity
    Modified residuei1649 – 16491PhosphoserineBy similarity
    Modified residuei1775 – 17751Phosphoserine2 Publications
    Modified residuei1778 – 17781PhosphoserineBy similarity
    Modified residuei1781 – 17811PhosphoserineBy similarity
    Modified residuei1784 – 17841PhosphothreonineBy similarity
    Modified residuei1793 – 17931PhosphoserineBy similarity
    Modified residuei1911 – 19111Phosphoserine1 Publication
    Modified residuei2267 – 22671PhosphoserineBy similarity
    Modified residuei2285 – 22851PhosphoserineBy similarity
    Modified residuei2460 – 24601S-nitrosocysteine1 Publication

    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.
    S-nitrosylation at Cys-2460 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.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, S-nitrosylation

    Proteomic databases

    MaxQBiP14873.
    PaxDbiP14873.
    PRIDEiP14873.

    PTM databases

    PhosphoSiteiP14873.

    Expressioni

    Gene expression databases

    ArrayExpressiP14873.
    BgeeiP14873.
    CleanExiMM_MTAP1B.
    GenevestigatoriP14873.

    Interactioni

    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 (via C-terminus) with GAN (via Kelch domains). Interacts (via N-terminus) with DAPK1 By similarity. Interacts with the tubulin tyrosine TTL. Interacts with TMEM185A By similarity. Interacts with MAP1LC3B By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Scn8aQ9WTU37EBI-764653,EBI-6396042

    Protein-protein interaction databases

    BioGridi201584. 12 interactions.
    IntActiP14873. 7 interactions.
    MINTiMINT-4101165.

    Structurei

    3D structure databases

    ProteinModelPortaliP14873.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati1874 – 189017MAP1B 1Add
    BLAST
    Repeati1891 – 190717MAP1B 2Add
    BLAST
    Repeati1908 – 192417MAP1B 3Add
    BLAST
    Repeati1925 – 194117MAP1B 4Add
    BLAST
    Repeati1942 – 195817MAP1B 5Add
    BLAST
    Repeati1959 – 197517MAP1B 6Add
    BLAST
    Repeati1993 – 200917MAP1B 7Add
    BLAST
    Repeati2010 – 202617MAP1B 8Add
    BLAST
    Repeati2027 – 204317MAP1B 9Add
    BLAST
    Repeati2044 – 206017MAP1B 10Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2290 – 2464175Mediates interaction with TMEM185ABy similarityAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi589 – 787199Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)Add
    BLAST

    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

    Sequence similaritiesi

    Belongs to the MAP1 family.Curated

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiNOG12793.
    GeneTreeiENSGT00550000074593.
    HOGENOMiHOG000063256.
    HOVERGENiHBG052409.
    InParanoidiP14873.
    KOiK10429.
    OMAiRTPVQDH.
    OrthoDBiEOG773XKP.
    TreeFamiTF350229.

    Family and domain databases

    Gene3Di3.60.15.10. 2 hits.
    InterProiIPR001279. Beta-lactamas-like.
    IPR026074. MAP1.
    IPR027321. MAP1B.
    IPR000102. MAP1B_neuraxin.
    [Graphical view]
    PANTHERiPTHR13843. PTHR13843. 1 hit.
    PTHR13843:SF5. PTHR13843:SF5. 1 hit.
    PfamiPF00414. MAP1B_neuraxin. 6 hits.
    [Graphical view]
    PROSITEiPS00230. MAP1B_NEURAXIN. 8 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P14873-1 [UniParc]FASTAAdd to Basket

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    MATVVVEATE PEPSGSIGNP AASTSPSLSH RFLDSKFYLL VVVGETVTEE     50
    HLRRAIGNIE LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL 100
    HHRSDVLETV VLINPSDEAV STEVRLMITD AARHKLLVLT GQCFENTGEL 150
    ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP ANKASLTLFC PEEGDWKNSN 200
    LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP SPFDILEPPT 250
    SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH 300
    LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEERSQGST SNSDWMKNLI 350
    SPDLGVVFLN VPENLKDPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR 400
    SVGNTIEPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE 450
    LILPNGQEVD IPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE 500
    GLEKLKHLDF LKQPLATQKD LTGQVPTPPV KQVKLKQRAD SRESLKPATK 550
    PVASKSVRKE SKEETPEVTK TSQVEKTPKV ESKEKVLVKK DKPVKTESKP 600
    SVTEKEVSSK EEQSPVKAEV AEKQATESKP KVTKDKVVKK EIKTKLEEKK 650
    EEKPKKEVVK KEDKTPLKKD EKPRKEEVKK EIKKEIKKEE RKELKKEVKK 700
    ETPLKDAKKE VKKEEKKEVK KEEKEPKKEI KKISKDIKKS TPLSDTKKPS 750
    ALKPKVAKKE ESTKKEPLAA GKLKDKGKVK VIKKEGKTTE AAATAVGTAA 800
    TTAAVVAAAG IAASGPVKEL EAERSLMSSP EDLTKDFEEL KAEEIDVAKD 850
    IKPQLELIED EEKLKETQPG EAYVIQKETE VSKGSAESPD EGITTTEGEG 900
    ECEQTPEELE PVEKQGVDDI EKFEDEGAGF EESSETGDYE EKAETEEAEE 950
    PEEDGEDNAS GSASKHSPTE DDESAKAEAD VHLKEKRESV VSGDDRAEED 1000
    MDDVLEKGEA EQSEEEGEEE DKAEDAREEG YEPDKTEAED YVMAVADKAA 1050
    EAGVTEEQYG YLGTSAKQPG IQSPSREPAS SIHDETLPGG SESEATASDE 1100
    ENREDQPEEF TATSGYTQST IEISSEPTPM DEMSTPRDVM SDETNNEETE 1150
    SPSQEFVNIT KYESSLYSQE YSKPAVASFN GLSEGSKTDA TDGKDYNASA 1200
    STISPPSSME EDKFSKSALR DAYCSEEKEL KASAELDIKD VSDERLSPAK 1250
    SPSLSPSPPS PIEKTPLGER SVNFSLTPNE IKVSAEGEAR SVSPGVTQAV 1300
    VEEHCASPEE KTLEVVSPSQ SVTGSAGHTP YYQSPTDEKS SHLPTEVTEK 1350
    PQAVPVSFEF SEAKDENERA SLSPMDEPVP DSESPVEKVL SPLRSPPLLG 1400
    SESPYEDFLS ADSKVLGRRS ESPFEGKNGK QGFPDRESPV SDLTSTGLYQ 1450
    DKQEEKSTGF IPIKEDFGPE KKTSDVETMS SQSALALDER KLGGDVSPTQ 1500
    IDVSQFGSFK EDTKMSISEG TVSDKSATPV DEGVAEDTYS HMEGVASVST 1550
    ASVATSSFPE PTTDDVSPSL HAEVGSPHST EVDDSLSVSV VQTPTTFQET 1600
    EMSPSKEECP RPMSISPPDF SPKTAKSRTP VQDHRSEQSS MSIEFGQESP 1650
    EHSLAMDFSR QSPDHPTLGA SVLHITENGP TEVDYSPSDI QDSSLSHKIP 1700
    PTEEPSYTQD NDLSELISVS QVEASPSTSS AHTPSQIASP LQEDTLSDVV 1750
    PPREMSLYAS LASEKVQSLE GEKLSPKSDI SPLTPRESSP LYSPGFSDST 1800
    SAAKETAAAH QASSSPPIDA ATAEPYGFRS SMLFDTMQHH LALNRDLTTS 1850
    SVEKDSGGKT PGDFNYAYQK PENAAGSPDE EDYDYESQEK TIRTHDVGGY 1900
    YYEKTERTIK SPCDSGYSYE TIEKTIKTPE DGGYTCEITE KTTRTPEEGG 1950
    YSYEISEKTT RTPEVSGYTY EKTERSRRLL DDISNGYDDT EDGGHTLGDC 2000
    SYSYETTEKI TSFPESESYS YETSTKTTRS PDTSAYCYET MEKITKTPQA 2050
    STYSYETSDR CYTTEKKSPS EARQDVDLCL VSSCEFKHPK TELSPSFINP 2100
    NPLEWFAGEE PTEESEKPLT QSGGAPPPSG GKQQGRQCDE TPPTSVSESA 2150
    PSQTDSDVPP ETEECPSITA DANIDSEDES ETIPTDKTVT YKHMDPPPAP 2200
    MQDRSPSPRH PDVSMVDPDA LAVDQNLGKA LKKDLKEKTK TKKPGTKTKS 2250
    SSPVKKGDGK SKPLAASPKP GALKESSDKV SRVASPKKKE SVEKATKTTT 2300
    TPEVKATRGE EKDKETKNAA NASASKSAKT ATAGPGTTKT AKSSTVPPGL 2350
    PVYLDLCYIP NHSNSKNVDV EFFKRVRSSY YVVSGNDPAA EEPSRAVLDA 2400
    LLEGKAQWGS NMQVTLIPTH DSEVMREWYQ ETHEKQQDLN IMVLASSSTV 2450
    VMQDESFPAC KIEL 2464
    Length:2,464
    Mass (Da):270,255
    Last modified:July 27, 2011 - v2
    Checksum:i2835101531B0694A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti743 – 7431L → Q in CAA35761. (PubMed:2480963)Curated
    Sequence conflicti1348 – 13514TEKP → SENA in CAA35761. (PubMed:2480963)Curated
    Sequence conflicti1654 – 16541L → F in CAA35761. (PubMed:2480963)Curated
    Sequence conflicti1688 – 16881S → C in CAA35761. (PubMed:2480963)Curated
    Sequence conflicti1898 – 18992GG → VR in CAA35761. (PubMed:2480963)Curated
    Sequence conflicti1926 – 19261I → T in CAA35761. (PubMed:2480963)Curated
    Sequence conflicti2231 – 22311L → V in CAA35761. (PubMed:2480963)Curated
    Sequence conflicti2333 – 23331A → T in CAA35761. (PubMed:2480963)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51396 mRNA. Translation: CAA35761.1.
    AC170188 Genomic DNA. No translation available.
    CCDSiCCDS26723.1.
    PIRiS07549. QRMSP1.
    RefSeqiNP_032660.2. NM_008634.2.
    UniGeneiMm.4173.
    Mm.474609.
    Mm.474896.

    Genome annotation databases

    EnsembliENSMUST00000064762; ENSMUSP00000068374; ENSMUSG00000052727.
    GeneIDi17755.
    KEGGimmu:17755.
    UCSCiuc007rpr.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X51396 mRNA. Translation: CAA35761.1 .
    AC170188 Genomic DNA. No translation available.
    CCDSi CCDS26723.1.
    PIRi S07549. QRMSP1.
    RefSeqi NP_032660.2. NM_008634.2.
    UniGenei Mm.4173.
    Mm.474609.
    Mm.474896.

    3D structure databases

    ProteinModelPortali P14873.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201584. 12 interactions.
    IntActi P14873. 7 interactions.
    MINTi MINT-4101165.

    PTM databases

    PhosphoSitei P14873.

    Proteomic databases

    MaxQBi P14873.
    PaxDbi P14873.
    PRIDEi P14873.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000064762 ; ENSMUSP00000068374 ; ENSMUSG00000052727 .
    GeneIDi 17755.
    KEGGi mmu:17755.
    UCSCi uc007rpr.2. mouse.

    Organism-specific databases

    CTDi 4131.
    MGIi MGI:1306778. Map1b.

    Phylogenomic databases

    eggNOGi NOG12793.
    GeneTreei ENSGT00550000074593.
    HOGENOMi HOG000063256.
    HOVERGENi HBG052409.
    InParanoidi P14873.
    KOi K10429.
    OMAi RTPVQDH.
    OrthoDBi EOG773XKP.
    TreeFami TF350229.

    Miscellaneous databases

    NextBioi 292427.
    PROi P14873.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P14873.
    Bgeei P14873.
    CleanExi MM_MTAP1B.
    Genevestigatori P14873.

    Family and domain databases

    Gene3Di 3.60.15.10. 2 hits.
    InterProi IPR001279. Beta-lactamas-like.
    IPR026074. MAP1.
    IPR027321. MAP1B.
    IPR000102. MAP1B_neuraxin.
    [Graphical view ]
    PANTHERi PTHR13843. PTHR13843. 1 hit.
    PTHR13843:SF5. PTHR13843:SF5. 1 hit.
    Pfami PF00414. MAP1B_neuraxin. 6 hits.
    [Graphical view ]
    PROSITEi PS00230. MAP1B_NEURAXIN. 8 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The microtubule binding domain of microtubule-associated protein MAP1B contains a repeated sequence motif unrelated to that of MAP2 and tau."
      Noble M., Lewis S.A., Cowan N.J.
      J. Cell Biol. 109:3367-3376(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], DOMAIN.
      Strain: Swiss Webster.
      Tissue: Brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: C57BL/6J.
    3. "Microtubule-associated protein 1B: a neuronal binding partner for gigaxonin."
      Ding J., Liu J.-J., Kowal A.S., Nardine T., Bhattacharya P., Lee A., Yang Y.
      J. Cell Biol. 158:427-433(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAN.
    4. "Mapmodulin/leucine-rich acidic nuclear protein binds the light chain of microtubule-associated protein 1B and modulates neuritogenesis."
      Opal P., Garcia J.J., Propst F., Matilla A., Orr H.T., Zoghbi H.Y.
      J. Biol. Chem. 278:34691-34699(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ANP32A.
    5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1260; SER-1391 AND SER-1395, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    6. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-541; SER-544; SER-561; SER-989; SER-1013; SER-1307; SER-1438; SER-1775 AND SER-1911, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain.
    7. Cited for: INTERACTION WITH TIAM2.
    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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Brain cortex.
    9. "S-nitrosylation of microtubule-associated protein 1B mediates nitric-oxide-induced axon retraction."
      Stroissnigg H., Trancikova A., Descovich L., Fuhrmann J., Kutschera W., Kostan J., Meixner A., Nothias F., Propst F.
      Nat. Cell Biol. 9:1035-1045(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: S-NITROSYLATION AT CYS-2460.
    10. "Microtubule-associated protein 1B interaction with tubulin tyrosine ligase contributes to the control of microtubule tyrosination."
      Utreras E., Jimenez-Mateos E.M., Contreras-Vallejos E., Tortosa E., Perez M., Rojas S., Saragoni L., Maccioni R.B., Avila J., Gonzalez-Billault C.
      Dev. Neurosci. 30:200-210(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN REGULATION OF ALPHA-TUBULIN TYROSINATION, INTERACTION WITH TTL.
    11. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-614; SER-1438; SER-1497 AND SER-1775, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.
    12. "Microtubule-associated protein 1B (MAP1B) is required for dendritic spine development and synaptic maturation."
      Tortosa E., Montenegro-Venegas C., Benoist M., Hartel S., Gonzalez-Billault C., Esteban J.A., Avila J.
      J. Biol. Chem. 286:40638-40648(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiMAP1B_MOUSE
    AccessioniPrimary (citable) accession number: P14873
    Secondary accession number(s): E9QM11
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 135 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3