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P14873

- MAP1B_MOUSE

UniProt

P14873 - MAP1B_MOUSE

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Protein

Microtubule-associated protein 1B

Gene

Map1b

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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

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
Complete GO annotation...

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. cell projection Source: UniProtKB-KW
  3. cytosol Source: MGI
  4. microtubule Source: UniProtKB-KW
  5. microtubule associated complex Source: MGI
  6. plasma membrane Source: Ensembl
  7. postsynaptic density Source: MGI
Complete GO annotation...

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

BgeeiP14873.
CleanExiMM_MTAP1B.
ExpressionAtlasiP14873. baseline and differential.
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

« Hide

        10         20         30         40         50
MATVVVEATE PEPSGSIGNP AASTSPSLSH 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 VPENLKDPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR
410 420 430 440 450
SVGNTIEPVI LFQKMGVGKL EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE
460 470 480 490 500
LILPNGQEVD IPISYLTSVS SLIVWHPANP AEKIIRVLFP GNSTQYNILE
510 520 530 540 550
GLEKLKHLDF LKQPLATQKD LTGQVPTPPV KQVKLKQRAD SRESLKPATK
560 570 580 590 600
PVASKSVRKE SKEETPEVTK TSQVEKTPKV ESKEKVLVKK DKPVKTESKP
610 620 630 640 650
SVTEKEVSSK EEQSPVKAEV AEKQATESKP KVTKDKVVKK EIKTKLEEKK
660 670 680 690 700
EEKPKKEVVK KEDKTPLKKD EKPRKEEVKK EIKKEIKKEE RKELKKEVKK
710 720 730 740 750
ETPLKDAKKE VKKEEKKEVK KEEKEPKKEI KKISKDIKKS TPLSDTKKPS
760 770 780 790 800
ALKPKVAKKE ESTKKEPLAA GKLKDKGKVK VIKKEGKTTE AAATAVGTAA
810 820 830 840 850
TTAAVVAAAG IAASGPVKEL EAERSLMSSP EDLTKDFEEL KAEEIDVAKD
860 870 880 890 900
IKPQLELIED EEKLKETQPG EAYVIQKETE VSKGSAESPD EGITTTEGEG
910 920 930 940 950
ECEQTPEELE PVEKQGVDDI EKFEDEGAGF EESSETGDYE EKAETEEAEE
960 970 980 990 1000
PEEDGEDNAS GSASKHSPTE DDESAKAEAD VHLKEKRESV VSGDDRAEED
1010 1020 1030 1040 1050
MDDVLEKGEA EQSEEEGEEE DKAEDAREEG YEPDKTEAED YVMAVADKAA
1060 1070 1080 1090 1100
EAGVTEEQYG YLGTSAKQPG IQSPSREPAS SIHDETLPGG SESEATASDE
1110 1120 1130 1140 1150
ENREDQPEEF TATSGYTQST IEISSEPTPM DEMSTPRDVM SDETNNEETE
1160 1170 1180 1190 1200
SPSQEFVNIT KYESSLYSQE YSKPAVASFN GLSEGSKTDA TDGKDYNASA
1210 1220 1230 1240 1250
STISPPSSME EDKFSKSALR DAYCSEEKEL KASAELDIKD VSDERLSPAK
1260 1270 1280 1290 1300
SPSLSPSPPS PIEKTPLGER SVNFSLTPNE IKVSAEGEAR SVSPGVTQAV
1310 1320 1330 1340 1350
VEEHCASPEE KTLEVVSPSQ SVTGSAGHTP YYQSPTDEKS SHLPTEVTEK
1360 1370 1380 1390 1400
PQAVPVSFEF SEAKDENERA SLSPMDEPVP DSESPVEKVL SPLRSPPLLG
1410 1420 1430 1440 1450
SESPYEDFLS ADSKVLGRRS ESPFEGKNGK QGFPDRESPV SDLTSTGLYQ
1460 1470 1480 1490 1500
DKQEEKSTGF IPIKEDFGPE KKTSDVETMS SQSALALDER KLGGDVSPTQ
1510 1520 1530 1540 1550
IDVSQFGSFK EDTKMSISEG TVSDKSATPV DEGVAEDTYS HMEGVASVST
1560 1570 1580 1590 1600
ASVATSSFPE PTTDDVSPSL HAEVGSPHST EVDDSLSVSV VQTPTTFQET
1610 1620 1630 1640 1650
EMSPSKEECP RPMSISPPDF SPKTAKSRTP VQDHRSEQSS MSIEFGQESP
1660 1670 1680 1690 1700
EHSLAMDFSR QSPDHPTLGA SVLHITENGP TEVDYSPSDI QDSSLSHKIP
1710 1720 1730 1740 1750
PTEEPSYTQD NDLSELISVS QVEASPSTSS AHTPSQIASP LQEDTLSDVV
1760 1770 1780 1790 1800
PPREMSLYAS LASEKVQSLE GEKLSPKSDI SPLTPRESSP LYSPGFSDST
1810 1820 1830 1840 1850
SAAKETAAAH QASSSPPIDA ATAEPYGFRS SMLFDTMQHH LALNRDLTTS
1860 1870 1880 1890 1900
SVEKDSGGKT PGDFNYAYQK PENAAGSPDE EDYDYESQEK TIRTHDVGGY
1910 1920 1930 1940 1950
YYEKTERTIK SPCDSGYSYE TIEKTIKTPE DGGYTCEITE KTTRTPEEGG
1960 1970 1980 1990 2000
YSYEISEKTT RTPEVSGYTY EKTERSRRLL DDISNGYDDT EDGGHTLGDC
2010 2020 2030 2040 2050
SYSYETTEKI TSFPESESYS YETSTKTTRS PDTSAYCYET MEKITKTPQA
2060 2070 2080 2090 2100
STYSYETSDR CYTTEKKSPS EARQDVDLCL VSSCEFKHPK TELSPSFINP
2110 2120 2130 2140 2150
NPLEWFAGEE PTEESEKPLT QSGGAPPPSG GKQQGRQCDE TPPTSVSESA
2160 2170 2180 2190 2200
PSQTDSDVPP ETEECPSITA DANIDSEDES ETIPTDKTVT YKHMDPPPAP
2210 2220 2230 2240 2250
MQDRSPSPRH PDVSMVDPDA LAVDQNLGKA LKKDLKEKTK TKKPGTKTKS
2260 2270 2280 2290 2300
SSPVKKGDGK SKPLAASPKP GALKESSDKV SRVASPKKKE SVEKATKTTT
2310 2320 2330 2340 2350
TPEVKATRGE EKDKETKNAA NASASKSAKT ATAGPGTTKT AKSSTVPPGL
2360 2370 2380 2390 2400
PVYLDLCYIP NHSNSKNVDV EFFKRVRSSY YVVSGNDPAA EEPSRAVLDA
2410 2420 2430 2440 2450
LLEGKAQWGS NMQVTLIPTH DSEVMREWYQ ETHEKQQDLN IMVLASSSTV
2460
VMQDESFPAC KIEL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

Bgeei P14873.
CleanExi MM_MTAP1B.
ExpressionAtlasi P14873. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 136 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