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Protein

Microtubule-associated protein 1B

Gene

Map1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: 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. Facilitates tyrosination of alpha-tubulin in neuronal microtubules. Required for synaptic maturation (By similarity). Interacts with TMEM185A (By similarity).By similarity

GO - Molecular functioni

  • actin binding Source: RGD
  • microtubule binding Source: RGD
  • phospholipid binding Source: RGD
  • protein complex binding Source: RGD

GO - Biological processi

  • cellular response to growth factor stimulus Source: RGD
  • cellular response to peptide hormone stimulus Source: RGD
  • developmental maturation Source: RGD
  • induction of synaptic plasticity by chemical substance Source: RGD
  • microtubule bundle formation Source: RGD
  • negative regulation of microtubule depolymerization Source: RGD
  • nervous system development Source: RGD
  • neuron development Source: RGD
  • peripheral nervous system axon regeneration Source: RGD
  • positive regulation of axon extension Source: RGD
  • positive regulation of microtubule polymerization Source: RGD
  • positive regulation of neuron differentiation Source: RGD
  • response to axon injury Source: RGD
  • response to carbohydrate Source: RGD
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to inorganic substance Source: RGD
  • response to insecticide Source: RGD
  • response to mechanical stimulus Source: RGD
  • response to nutrient levels Source: RGD
  • response to vitamin A Source: RGD
  • response to wounding Source: RGD
  • synapse assembly Source: RGD
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 1B
Short name:
MAP-1B
Alternative name(s):
Neuraxin
Cleaved into the following 2 chains:
Gene namesi
Name:Map1b
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3043. Map1b.

Subcellular locationi

GO - Cellular componenti

  • axon Source: RGD
  • cell junction Source: UniProtKB-KW
  • cytoskeleton Source: RGD
  • dendrite Source: RGD
  • dendritic spine Source: UniProtKB-SubCell
  • growth cone Source: RGD
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: RGD
  • neuronal cell body Source: RGD
  • perikaryon Source: RGD
  • perinuclear region of cytoplasm Source: RGD
  • plasma membrane Source: RGD
  • postsynaptic density Source: RGD
  • varicosity Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Chemistry

ChEMBLiCHEMBL3217383.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 24592458Microtubule-associated protein 1BPRO_0000018608Add
BLAST
Chaini2 – 21972196MAP1B heavy chainPRO_0000418381Add
BLAST
Chaini2198 – 2459262MAP1 light chain LC1PRO_0000018609Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei335 – 3351PhosphoserineCombined sources
Modified residuei338 – 3381PhosphoserineCombined sources
Modified residuei340 – 3401PhosphoserineCombined sources
Modified residuei342 – 3421PhosphoserineCombined sources
Modified residuei526 – 5261PhosphothreonineCombined sources
Modified residuei540 – 5401PhosphoserineCombined sources
Modified residuei543 – 5431PhosphoserineBy similarity
Modified residuei560 – 5601PhosphoserineBy similarity
Modified residuei613 – 6131PhosphoserineBy similarity
Modified residuei820 – 8201PhosphoserineCombined sources
Modified residuei823 – 8231PhosphoserineCombined sources
Modified residuei824 – 8241PhosphoserineCombined sources
Modified residuei880 – 8801PhosphoserineBy similarity
Modified residuei883 – 8831PhosphoserineBy similarity
Modified residuei891 – 8911PhosphothreonineBy similarity
Modified residuei900 – 9001PhosphothreonineBy similarity
Modified residuei928 – 9281PhosphoserineCombined sources
Modified residuei929 – 9291PhosphoserineCombined sources
Modified residuei940 – 9401PhosphothreonineCombined sources
Modified residuei955 – 9551PhosphoserineCombined sources
Modified residuei962 – 9621PhosphoserineCombined sources
Modified residuei984 – 9841PhosphoserineCombined sources
Modified residuei987 – 9871PhosphoserineCombined sources
Modified residuei1008 – 10081PhosphoserineCombined sources
Modified residuei1147 – 11471PhosphoserineBy similarity
Modified residuei1149 – 11491PhosphoserineBy similarity
Modified residuei1179 – 11791PhosphoserineCombined sources
Modified residuei1182 – 11821PhosphoserineCombined sources
Modified residuei1200 – 12001PhosphoserineCombined sources
Modified residuei1203 – 12031PhosphoserineBy similarity
Modified residuei1204 – 12041PhosphoserineBy similarity
Modified residuei1238 – 12381PhosphoserineCombined sources
Modified residuei1243 – 12431PhosphoserineCombined sources
Modified residuei1247 – 12471PhosphoserineCombined sources
Modified residuei1249 – 12491PhosphoserineCombined sources
Modified residuei1251 – 12511PhosphoserineCombined sources
Modified residuei1253 – 12531PhosphoserineCombined sources
Modified residuei1256 – 12561PhosphoserineCombined sources
Modified residuei1267 – 12671PhosphoserineBy similarity
Modified residuei1271 – 12711PhosphoserineBy similarity
Modified residuei1273 – 12731PhosphothreonineCombined sources
Modified residuei1304 – 13041PhosphoserineBy similarity
Modified residuei1314 – 13141PhosphoserineCombined sources
Modified residuei1316 – 13161PhosphoserineBy similarity
Modified residuei1318 – 13181PhosphoserineBy similarity
Modified residuei1320 – 13201PhosphothreonineBy similarity
Modified residuei1322 – 13221PhosphoserineCombined sources
Modified residuei1331 – 13311PhosphoserineBy similarity
Modified residuei1368 – 13681PhosphoserineBy similarity
Modified residuei1370 – 13701PhosphoserineCombined sources
Modified residuei1379 – 13791PhosphoserineBy similarity
Modified residuei1381 – 13811PhosphoserineCombined sources
Modified residuei1388 – 13881PhosphoserineBy similarity
Modified residuei1392 – 13921PhosphoserineCombined sources
Modified residuei1400 – 14001PhosphoserineBy similarity
Modified residuei1402 – 14021PhosphotyrosineBy similarity
Modified residuei1419 – 14191PhosphoserineCombined sources
Modified residuei1435 – 14351PhosphoserineBy similarity
Modified residuei1493 – 14931PhosphoserineCombined sources
Modified residuei1504 – 15041PhosphoserineCombined sources
Modified residuei1512 – 15121PhosphoserineCombined sources
Modified residuei1514 – 15141PhosphoserineCombined sources
Modified residuei1517 – 15171PhosphothreonineCombined sources
Modified residuei1519 – 15191PhosphoserineCombined sources
Modified residuei1609 – 16091PhosphoserineBy similarity
Modified residuei1611 – 16111PhosphoserineCombined sources
Modified residuei1616 – 16161PhosphoserineCombined sources
Modified residuei1644 – 16441PhosphoserineCombined sources
Modified residuei1654 – 16541PhosphoserineCombined sources
Modified residuei1657 – 16571PhosphoserineBy similarity
Modified residuei1681 – 16811PhosphoserineBy similarity
Modified residuei1763 – 17631PhosphoserineCombined sources
Modified residuei1770 – 17701PhosphoserineCombined sources
Modified residuei1773 – 17731PhosphoserineBy similarity
Modified residuei1776 – 17761PhosphoserineCombined sources
Modified residuei1779 – 17791PhosphothreonineCombined sources
Modified residuei1783 – 17831PhosphoserineBy similarity
Modified residuei1784 – 17841PhosphoserineBy similarity
Modified residuei1787 – 17871PhosphotyrosineBy similarity
Modified residuei1788 – 17881PhosphoserineBy similarity
Modified residuei1792 – 17921PhosphoserineBy similarity
Modified residuei1810 – 18101PhosphoserineCombined sources
Modified residuei1868 – 18681PhosphoserineCombined sources
Modified residuei1872 – 18721PhosphoserineCombined sources
Modified residuei1906 – 19061PhosphoserineCombined sources
Modified residuei1923 – 19231PhosphothreonineCombined sources
Modified residuei1940 – 19401PhosphothreonineCombined sources
Modified residuei2025 – 20251PhosphoserineCombined sources
Modified residuei2262 – 22621PhosphoserineBy similarity
Modified residuei2280 – 22801PhosphoserineBy similarity
Modified residuei2405 – 24051PhosphoserineBy similarity
Modified residuei2455 – 24551S-nitrosocysteineBy similarity

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-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

Keywords - PTMi

Acetylation, Phosphoprotein, S-nitrosylation

Proteomic databases

PaxDbiP15205.
PRIDEiP15205.

PTM databases

iPTMnetiP15205.
PhosphoSiteiP15205.

Expressioni

Tissue specificityi

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

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

Inductioni

By nerve growth factor.1 Publication

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 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

  • actin binding Source: RGD
  • microtubule binding Source: RGD
  • protein complex binding Source: RGD

Protein-protein interaction databases

BioGridi248099. 5 interactions.
IntActiP15205. 2 interactions.
STRINGi10116.ENSRNOP00000023460.

Structurei

3D structure databases

ProteinModelPortaliP15205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1869 – 188517MAP1B 1Add
BLAST
Repeati1886 – 190217MAP1B 2Add
BLAST
Repeati1903 – 191917MAP1B 3Add
BLAST
Repeati1920 – 193617MAP1B 4Add
BLAST
Repeati1937 – 195317MAP1B 5Add
BLAST
Repeati1954 – 197017MAP1B 6Add
BLAST
Repeati1988 – 200417MAP1B 7Add
BLAST
Repeati2005 – 202117MAP1B 8Add
BLAST
Repeati2022 – 203817MAP1B 9Add
BLAST
Repeati2039 – 205517MAP1B 10Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2285 – 2459175Mediates interaction with TMEM185ABy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi559 – 1035477Glu-richAdd
BLAST
Compositional biasi588 – 786199Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)Add
BLAST
Compositional biasi2224 – 231289Lys-richAdd
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

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP15205.
KOiK10429.
PhylomeDBiP15205.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
IPR001279. Metallo-B-lactamas.
[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.

P15205-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATVVVEATE PEPSGSIGNP AATTSPSLSH RFLDSKFYLL VVVGETVTEE
60 70 80 90 100
HLRRAIGNIE LGIRSWETNL 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 LEEESQGSTS NSDWMKNLIS
360 370 380 390 400
PDLGVVFLNV PENLKNPEPN IKMKRSTEEA CFTLQYLNKL SMKPEPLFRS
410 420 430 440 450
VGNAIEPVIL FQKMGVGKLK MYVLNPVKSS KEMQYFMQQW TGTNKDKAEL
460 470 480 490 500
ILPNGQEVDI PISYLASVSS LIVWHPANPA EKIIRVLFPG NSTQYNILEG
510 520 530 540 550
LEKLKHLDFL KQPLATQKDL TGQVSTPPVK QVKLKQRADS RESLKPATKP
560 570 580 590 600
LSSKSVRKES KEEAPEATKA SQVEKTPKVE SKEKVIVKKD KPGKVESKPS
610 620 630 640 650
VTEKEVPSKE EQSPVKAEVA EKAATESKPK VTKDKVVKKE IKTKPEEKKE
660 670 680 690 700
EKPKKEVAKK EDKTPLKKDE KPKKEEAKKE IKKEIKKEEK KELKKEVKKE
710 720 730 740 750
TPLKDAKKEV KKDEKKEVKK EEKEPKKEIK KISKDIKKST PLSDTKKPAA
760 770 780 790 800
LKPKVAKKEE PTKKEPIAAG KLKDKGKVKV IKKEGKTTEA AATAVGTAAV
810 820 830 840 850
AAAAGVAASG PAKELEAERS LMSSPEDLTK DFEELKAEEI DVAKDIKPQL
860 870 880 890 900
ELIEDEEKLK ETEPGEAYVI QKETEVSKGS AESPDEGITT TEGEGECEQT
910 920 930 940 950
PEELEPVEKQ GVDDIEKFED EGAGFEESSE AGDYEEKAET EEAEEPEEDG
960 970 980 990 1000
EDNVSGSASK HSPTEDEEIA KAEADVHIKE KRESVASGDD RAEEDMDEAL
1010 1020 1030 1040 1050
EKGEAEQSEE EGEEEEDKAE DAREEDHEPD KTEAEDYVMA VVDKAAEAGV
1060 1070 1080 1090 1100
TEDQYDFLGT PAKQPGVQSP SREPASSIHD ETLPGGSESE ATASDEENRE
1110 1120 1130 1140 1150
DQPEEFTATS GYTQSTIEIS SEPTPMDEMS TPRDVMTDET NNEETESPSQ
1160 1170 1180 1190 1200
EFVNITKYES SLYSQEYSKP VVASFNGLSD GSKTDATDGR DYNASASTIS
1210 1220 1230 1240 1250
PPSSMEEDKF SKSALRDAYR PEETDVKTGA ELDIKDVSDE RLSPAKSPSL
1260 1270 1280 1290 1300
SPSPPSPIEK TPLGERSVNF SLTPNEIKAS AEGEATAVVS PGVTQAVVEE
1310 1320 1330 1340 1350
HCASPEEKTL EVVSPSQSVT GSAGHTPYYQ SPTDEKSSHL PTEVTENAQA
1360 1370 1380 1390 1400
VPVSFEFTEA KDENERSSIS PMDEPVPDSE SPIEKVLSPL RSPPLIGSES
1410 1420 1430 1440 1450
AYEDFLSADD KALGRRSESP FEGKNGKQGF SDKESPVSDL TSDLYQDKQE
1460 1470 1480 1490 1500
EKRAGFIPIK EDFSPEKKAS DAEIMSSQSA LALDERKLGG DGSPTQVDVS
1510 1520 1530 1540 1550
QFGSFKEDTK MSISEGTVSD KSATPVDEGA EDTYSHMEGV ASVSTASVAT
1560 1570 1580 1590 1600
SSFPEPTTDD VSPSLHAEVG SPHSTEVDDS LSVSVVQTPT TFQETEMSPS
1610 1620 1630 1640 1650
KEECPRPMSI SPPDFSPKTA KSRTPVQDHR SEQSSMSIEF GQESPEHSLA
1660 1670 1680 1690 1700
MDFSRQSPDH PTVGAGMLHI TENGPTEVDY SPSDIQDSSL SHKIPPTEEP
1710 1720 1730 1740 1750
SYTQDNDLSE LISVSQVEAS PSTSSAHTPS QIASPLQEDT LSDVVPPRDM
1760 1770 1780 1790 1800
SLYASLASEK VQSLEGEKLS PKSDISPLTP RESSPTYSPG FSDSTSGAKE
1810 1820 1830 1840 1850
STAAYQTSSS PPIDAAAAEP YGFRSSMLFD TMQHHLALSR DLTTSSVEKD
1860 1870 1880 1890 1900
NGGKTPGDFN YAYQKPESTT ESPDEEDYDY ESHEKTIQAH DVGGYYYEKT
1910 1920 1930 1940 1950
ERTIKSPCDS GYSYETIEKT TKTPEDGGYS CEITEKTTRT PEEGGYSYEI
1960 1970 1980 1990 2000
SEKTTRTPEV SGYTYEKTER SRRLLDDISN GYDDTEDGGH TLGDCSYSYE
2010 2020 2030 2040 2050
TTEKITSFPE SESYSYETTT KTTRSPDTSA YCYETMEKIT KTPQASTYSY
2060 2070 2080 2090 2100
ETSDRCYTPE RKSPSEARQD VDLCLVSSCE FKHPKTELSP SFINPNPLEW
2110 2120 2130 2140 2150
FAGEEPTEES ERPLTQSGGA PPPSGGKQQG RQCDETPPTS VSESAPSQTD
2160 2170 2180 2190 2200
SDVPPETEEC PSITADANLD SEDESETIPT DKTVTYKHMD PPPAPMQDRS
2210 2220 2230 2240 2250
PSPRHPDVSM VDPEALAIEQ NLGKALKKDL KEKAKTKKPG TKTKSSSPVK
2260 2270 2280 2290 2300
KGDGKSKPSA ASPKPGALKE SSDKVSRVAS PKKKESVEKA MKTTTTPEVK
2310 2320 2330 2340 2350
ATRGEEKDKE TKNAANASAS KSVKTATAGP GTTKTAKSST VPPGLPVYLD
2360 2370 2380 2390 2400
LCYIPNHSNS KNVDVEFFKR VRSSYYVVSG NDPAAEEPSR AVLDALLEGK
2410 2420 2430 2440 2450
AQWGSNMQVT LIPTHDSEVM REWYQETHEK QQDLNIMVLA SSSTVVMQDE

SFPACKIEL
Length:2,459
Mass (Da):269,500
Last modified:September 26, 2001 - v2
Checksum:i2E3F6872DEDB8BA2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti127 – 1271M → V in AAB17068 (PubMed:8666295).Curated
Sequence conflicti140 – 1401T → S (PubMed:8666295).Curated
Sequence conflicti2112 – 21121R → K in CAA34620 (PubMed:2555150).Curated
Sequence conflicti2169 – 21691L → I in CAA34620 (PubMed:2555150).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52950 mRNA. Translation: AAB17068.1.
X60370 mRNA. Translation: CAC16162.1.
X16623 mRNA. Translation: CAA34620.1. Sequence problems.
PIRiA56577.
RefSeqiNP_062090.1. NM_019217.1.
UniGeneiRn.220177.
Rn.98152.

Genome annotation databases

GeneIDi29456.
KEGGirno:29456.
UCSCiRGD:3043. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U52950 mRNA. Translation: AAB17068.1.
X60370 mRNA. Translation: CAC16162.1.
X16623 mRNA. Translation: CAA34620.1. Sequence problems.
PIRiA56577.
RefSeqiNP_062090.1. NM_019217.1.
UniGeneiRn.220177.
Rn.98152.

3D structure databases

ProteinModelPortaliP15205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248099. 5 interactions.
IntActiP15205. 2 interactions.
STRINGi10116.ENSRNOP00000023460.

Chemistry

ChEMBLiCHEMBL3217383.

PTM databases

iPTMnetiP15205.
PhosphoSiteiP15205.

Proteomic databases

PaxDbiP15205.
PRIDEiP15205.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi29456.
KEGGirno:29456.
UCSCiRGD:3043. rat.

Organism-specific databases

CTDi4131.
RGDi3043. Map1b.

Phylogenomic databases

eggNOGiKOG3592. Eukaryota.
ENOG410XRYM. LUCA.
HOGENOMiHOG000063256.
HOVERGENiHBG052409.
InParanoidiP15205.
KOiK10429.
PhylomeDBiP15205.

Miscellaneous databases

NextBioi609232.
PROiP15205.

Family and domain databases

Gene3Di3.60.15.10. 2 hits.
InterProiIPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
IPR001279. Metallo-B-lactamas.
[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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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-1906, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  6. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-335; SER-338; SER-340; SER-342; THR-526; SER-540; SER-820; SER-823; SER-824; SER-928; SER-929; THR-940; SER-955; SER-962; SER-984; SER-987; SER-1008; SER-1179; SER-1182; SER-1200; SER-1238; SER-1243; SER-1247; SER-1249; SER-1251; SER-1253; SER-1256; THR-1273; SER-1314; SER-1322; SER-1370; SER-1381; SER-1392; SER-1419; SER-1493; SER-1504; SER-1512; SER-1514; THR-1517; SER-1519; SER-1611; SER-1616; SER-1644; SER-1654; SER-1763; SER-1770; SER-1776; THR-1779; SER-1810; SER-1868; SER-1872; SER-1906; THR-1923; THR-1940 AND SER-2025, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMAP1B_RAT
AccessioniPrimary (citable) accession number: P15205
Secondary accession number(s): Q62958, Q9ER21, Q9QW92
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: September 26, 2001
Last modified: May 11, 2016
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

Caution

A C-terminal fragment of this protein (residues 1597 to 2459) was originally described as neuraxin in PubMed:2555150.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.