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P14873 (MAP1B_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 134. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein 1B

Short name=MAP-1B
Alternative name(s):
MAP1(X)
MAP1.2

Cleaved into the following 2 chains:

  1. MAP1B heavy chain
  2. MAP1 light chain LC1
Gene names
Name:Map1b
Synonyms:Mtap1b, Mtap5
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length2464 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Phosphorylated MAP1B may play a role in the cytoskeletal changes that accompany neurite extension. Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule polymerization and in stabilizing microtubules. Acts as a positive cofactor in DAPK1-mediated autophagic vesicle formation and membrane blebbing By similarity. Facilitates tyrosination of alpha-tubulin in neuronal microtubules. Required for synaptic maturation. Ref.10 Ref.12

Subunit structure

3 different light chains, LC1, LC2 and LC3, can associate with MAP1A and MAP1B proteins. LC1 interacts with the amino-terminal region of MAP1B. Interacts with ANP32A and TIAM2. Interacts (via C-terminus) with GAN (via Kelch domains). Interacts (via N-terminus) with DAPK1 By similarity. Interacts with the tubulin tyrosine TTL. Interacts with TMEM185A By similarity. Interacts with MAP1LC3B By similarity. Ref.3 Ref.4 Ref.7 Ref.10

Subcellular location

Cytoplasmcytoskeleton Probable. Cytoplasm By similarity. Cell junctionsynapse. Cell projectiondendritic spine. Note: Colocalizes with DAPK1 in the microtubules and cortical actin fibers By similarity. Ref.12

Domain

Has a highly basic region with many copies of the sequence KKEE and KKEI/V, repeated but not at fixed intervals, which is responsible for the binding of MAP1B to microtubules. Ref.1

Post-translational modification

LC1 is coexpressed with MAP1B. It is a polypeptide generated from MAP1B by proteolytic processing. It is free to associate with both MAP1A and MAP1B. It interacts with the N-terminal region of MAP1B.

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.

Sequence similarities

Belongs to the MAP1 family.

Ontologies

Keywords
   Cellular componentCell junction
Cell projection
Cytoplasm
Cytoskeleton
Microtubule
Synapse
   DomainRepeat
   PTMAcetylation
Phosphoprotein
S-nitrosylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxon extension

Inferred from mutant phenotype PubMed 16536727. Source: MGI

axonogenesis

Inferred from genetic interaction PubMed 11891784. Source: MGI

dendrite development

Inferred from mutant phenotype PubMed 11581286. Source: MGI

establishment of monopolar cell polarity

Inferred from mutant phenotype PubMed 11029282. Source: MGI

microtubule bundle formation

Inferred from mutant phenotype PubMed 11581286. Source: MGI

microtubule-based process

Traceable author statement PubMed 11581286. Source: MGI

mitochondrion transport along microtubule

Inferred from mutant phenotype PubMed 16536727. Source: MGI

negative regulation of intracellular transport

Inferred from mutant phenotype PubMed 16536727. Source: MGI

positive regulation of axon extension

Inferred from mutant phenotype PubMed 16536727. Source: MGI

   Cellular_componentcell junction

Inferred from electronic annotation. Source: UniProtKB-KW

cytosol

Inferred from direct assay PubMed 16885219. Source: MGI

dendritic spine

Inferred from electronic annotation. Source: UniProtKB-SubCell

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Traceable author statement PubMed 11581286. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

synapse

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncytoskeletal regulatory protein binding

Traceable author statement PubMed 11581286. Source: MGI

hydrolase activity

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 22474336. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Scn8aQ9WTU37EBI-764653,EBI-6396042

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 24642463Microtubule-associated protein 1B
PRO_0000018606
Chain2 – 22022201MAP1B heavy chain
PRO_0000418380
Chain2203 – 2464262MAP1 light chain LC1
PRO_0000018607

Regions

Repeat1874 – 189017MAP1B 1
Repeat1891 – 190717MAP1B 2
Repeat1908 – 192417MAP1B 3
Repeat1925 – 194117MAP1B 4
Repeat1942 – 195817MAP1B 5
Repeat1959 – 197517MAP1B 6
Repeat1993 – 200917MAP1B 7
Repeat2010 – 202617MAP1B 8
Repeat2027 – 204317MAP1B 9
Repeat2044 – 206017MAP1B 10
Region2290 – 2464175Mediates interaction with TMEM185A By similarity
Compositional bias589 – 787199Lys-rich (highly basic, contains many KKEE and KKEI/V repeats)

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue3361Phosphoserine By similarity
Modified residue5411Phosphoserine Ref.6
Modified residue5441Phosphoserine Ref.6
Modified residue5611Phosphoserine Ref.6
Modified residue6141Phosphoserine Ref.11
Modified residue8251Phosphoserine By similarity
Modified residue8281Phosphoserine By similarity
Modified residue8291Phosphoserine By similarity
Modified residue9341Phosphoserine By similarity
Modified residue9891Phosphoserine Ref.6
Modified residue9921Phosphoserine By similarity
Modified residue10131Phosphoserine Ref.6
Modified residue11411Phosphoserine By similarity
Modified residue11511Phosphoserine By similarity
Modified residue11531Phosphoserine By similarity
Modified residue12041Phosphoserine By similarity
Modified residue12471Phosphoserine By similarity
Modified residue12511Phosphoserine By similarity
Modified residue12551Phosphoserine By similarity
Modified residue12601Phosphoserine Ref.5
Modified residue12711Phosphoserine By similarity
Modified residue12751Phosphoserine By similarity
Modified residue12771Phosphothreonine By similarity
Modified residue13071Phosphoserine Ref.6
Modified residue13731Phosphoserine By similarity
Modified residue13821Phosphoserine By similarity
Modified residue13841Phosphoserine By similarity
Modified residue13911Phosphoserine Ref.5
Modified residue13951Phosphoserine Ref.5
Modified residue14221Phosphoserine By similarity
Modified residue14381Phosphoserine Ref.6 Ref.11
Modified residue14971Phosphoserine Ref.11
Modified residue16141Phosphoserine By similarity
Modified residue16161Phosphoserine By similarity
Modified residue16211Phosphoserine By similarity
Modified residue16491Phosphoserine By similarity
Modified residue17751Phosphoserine Ref.6 Ref.11
Modified residue17781Phosphoserine By similarity
Modified residue17811Phosphoserine By similarity
Modified residue17841Phosphothreonine By similarity
Modified residue17931Phosphoserine By similarity
Modified residue19111Phosphoserine Ref.6
Modified residue22671Phosphoserine By similarity
Modified residue22851Phosphoserine By similarity
Modified residue24601S-nitrosocysteine Ref.9

Experimental info

Sequence conflict7431L → Q in CAA35761. Ref.1
Sequence conflict1348 – 13514TEKP → SENA in CAA35761. Ref.1
Sequence conflict16541L → F in CAA35761. Ref.1
Sequence conflict16881S → C in CAA35761. Ref.1
Sequence conflict1898 – 18992GG → VR in CAA35761. Ref.1
Sequence conflict19261I → T in CAA35761. Ref.1
Sequence conflict22311L → V in CAA35761. Ref.1
Sequence conflict23331A → T in CAA35761. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P14873 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 2835101531B0694A

FASTA2,464270,255
        10         20         30         40         50         60 
MATVVVEATE PEPSGSIGNP AASTSPSLSH RFLDSKFYLL VVVGETVTEE HLRRAIGNIE 

        70         80         90        100        110        120 
LGIRSWDTNL IECNLDQELK LFVSRHSARF SPEVPGQKIL HHRSDVLETV VLINPSDEAV 

       130        140        150        160        170        180 
STEVRLMITD AARHKLLVLT GQCFENTGEL ILQSGSFSFQ NFIEIFTDQE IGELLSTTHP 

       190        200        210        220        230        240 
ANKASLTLFC PEEGDWKNSN LDRHNLQDFI NIKLNSASIL PEMEGLSEFT EYLSESVEVP 

       250        260        270        280        290        300 
SPFDILEPPT SGGFLKLSKP CCYIFPGGRG DSALFAVNGF NMLINGGSER KSCFWKLIRH 

       310        320        330        340        350        360 
LDRVDSILLT HIGDDNLPGI NSMLQRKIAE LEEERSQGST SNSDWMKNLI SPDLGVVFLN 

       370        380        390        400        410        420 
VPENLKDPEP NIKMKRSIEE ACFTLQYLNK LSMKPEPLFR SVGNTIEPVI LFQKMGVGKL 

       430        440        450        460        470        480 
EMYVLNPVKS SKEMQYFMQQ WTGTNKDKAE LILPNGQEVD IPISYLTSVS SLIVWHPANP 

       490        500        510        520        530        540 
AEKIIRVLFP GNSTQYNILE GLEKLKHLDF LKQPLATQKD LTGQVPTPPV KQVKLKQRAD 

       550        560        570        580        590        600 
SRESLKPATK PVASKSVRKE SKEETPEVTK TSQVEKTPKV ESKEKVLVKK DKPVKTESKP 

       610        620        630        640        650        660 
SVTEKEVSSK EEQSPVKAEV AEKQATESKP KVTKDKVVKK EIKTKLEEKK EEKPKKEVVK 

       670        680        690        700        710        720 
KEDKTPLKKD EKPRKEEVKK EIKKEIKKEE RKELKKEVKK ETPLKDAKKE VKKEEKKEVK 

       730        740        750        760        770        780 
KEEKEPKKEI KKISKDIKKS TPLSDTKKPS ALKPKVAKKE ESTKKEPLAA GKLKDKGKVK 

       790        800        810        820        830        840 
VIKKEGKTTE AAATAVGTAA TTAAVVAAAG IAASGPVKEL EAERSLMSSP EDLTKDFEEL 

       850        860        870        880        890        900 
KAEEIDVAKD IKPQLELIED EEKLKETQPG EAYVIQKETE VSKGSAESPD EGITTTEGEG 

       910        920        930        940        950        960 
ECEQTPEELE PVEKQGVDDI EKFEDEGAGF EESSETGDYE EKAETEEAEE PEEDGEDNAS 

       970        980        990       1000       1010       1020 
GSASKHSPTE DDESAKAEAD VHLKEKRESV VSGDDRAEED MDDVLEKGEA EQSEEEGEEE 

      1030       1040       1050       1060       1070       1080 
DKAEDAREEG YEPDKTEAED YVMAVADKAA EAGVTEEQYG YLGTSAKQPG IQSPSREPAS 

      1090       1100       1110       1120       1130       1140 
SIHDETLPGG SESEATASDE ENREDQPEEF TATSGYTQST IEISSEPTPM DEMSTPRDVM 

      1150       1160       1170       1180       1190       1200 
SDETNNEETE SPSQEFVNIT KYESSLYSQE YSKPAVASFN GLSEGSKTDA TDGKDYNASA 

      1210       1220       1230       1240       1250       1260 
STISPPSSME EDKFSKSALR DAYCSEEKEL KASAELDIKD VSDERLSPAK SPSLSPSPPS 

      1270       1280       1290       1300       1310       1320 
PIEKTPLGER SVNFSLTPNE IKVSAEGEAR SVSPGVTQAV VEEHCASPEE KTLEVVSPSQ 

      1330       1340       1350       1360       1370       1380 
SVTGSAGHTP YYQSPTDEKS SHLPTEVTEK PQAVPVSFEF SEAKDENERA SLSPMDEPVP 

      1390       1400       1410       1420       1430       1440 
DSESPVEKVL SPLRSPPLLG SESPYEDFLS ADSKVLGRRS ESPFEGKNGK QGFPDRESPV 

      1450       1460       1470       1480       1490       1500 
SDLTSTGLYQ DKQEEKSTGF IPIKEDFGPE KKTSDVETMS SQSALALDER KLGGDVSPTQ 

      1510       1520       1530       1540       1550       1560 
IDVSQFGSFK EDTKMSISEG TVSDKSATPV DEGVAEDTYS HMEGVASVST ASVATSSFPE 

      1570       1580       1590       1600       1610       1620 
PTTDDVSPSL HAEVGSPHST EVDDSLSVSV VQTPTTFQET EMSPSKEECP RPMSISPPDF 

      1630       1640       1650       1660       1670       1680 
SPKTAKSRTP VQDHRSEQSS MSIEFGQESP EHSLAMDFSR QSPDHPTLGA SVLHITENGP 

      1690       1700       1710       1720       1730       1740 
TEVDYSPSDI QDSSLSHKIP PTEEPSYTQD NDLSELISVS QVEASPSTSS AHTPSQIASP 

      1750       1760       1770       1780       1790       1800 
LQEDTLSDVV PPREMSLYAS LASEKVQSLE GEKLSPKSDI SPLTPRESSP LYSPGFSDST 

      1810       1820       1830       1840       1850       1860 
SAAKETAAAH QASSSPPIDA ATAEPYGFRS SMLFDTMQHH LALNRDLTTS SVEKDSGGKT 

      1870       1880       1890       1900       1910       1920 
PGDFNYAYQK PENAAGSPDE EDYDYESQEK TIRTHDVGGY YYEKTERTIK SPCDSGYSYE 

      1930       1940       1950       1960       1970       1980 
TIEKTIKTPE DGGYTCEITE KTTRTPEEGG YSYEISEKTT RTPEVSGYTY EKTERSRRLL 

      1990       2000       2010       2020       2030       2040 
DDISNGYDDT EDGGHTLGDC SYSYETTEKI TSFPESESYS YETSTKTTRS PDTSAYCYET 

      2050       2060       2070       2080       2090       2100 
MEKITKTPQA STYSYETSDR CYTTEKKSPS EARQDVDLCL VSSCEFKHPK TELSPSFINP 

      2110       2120       2130       2140       2150       2160 
NPLEWFAGEE PTEESEKPLT QSGGAPPPSG GKQQGRQCDE TPPTSVSESA PSQTDSDVPP 

      2170       2180       2190       2200       2210       2220 
ETEECPSITA DANIDSEDES ETIPTDKTVT YKHMDPPPAP MQDRSPSPRH PDVSMVDPDA 

      2230       2240       2250       2260       2270       2280 
LAVDQNLGKA LKKDLKEKTK TKKPGTKTKS SSPVKKGDGK SKPLAASPKP GALKESSDKV 

      2290       2300       2310       2320       2330       2340 
SRVASPKKKE SVEKATKTTT TPEVKATRGE EKDKETKNAA NASASKSAKT ATAGPGTTKT 

      2350       2360       2370       2380       2390       2400 
AKSSTVPPGL PVYLDLCYIP NHSNSKNVDV EFFKRVRSSY YVVSGNDPAA EEPSRAVLDA 

      2410       2420       2430       2440       2450       2460 
LLEGKAQWGS NMQVTLIPTH DSEVMREWYQ ETHEKQQDLN IMVLASSSTV VMQDESFPAC 


KIEL 

« Hide

References

« Hide 'large scale' references
[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]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
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]"Phosphoproteomic analysis of the developing mouse brain."
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.
Mol. Cell. Proteomics 3:1093-1101(2004) [PubMed] [Europe PMC] [Abstract]
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]"Rho-kinase modulates the function of STEF, a Rac GEF, through its phosphorylation."
Takefuji M., Mori K., Morita Y., Arimura N., Nishimura T., Nakayama M., Hoshino M., Iwamatsu A., Murohara T., Kaibuchi K., Amano M.
Biochem. Biophys. Res. Commun. 355:788-794(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X51396 mRNA. Translation: CAA35761.1.
AC170188 Genomic DNA. No translation available.
CCDSCCDS26723.1.
PIRQRMSP1. S07549.
RefSeqNP_032660.2. NM_008634.2.
UniGeneMm.4173.
Mm.474609.
Mm.474896.

3D structure databases

ProteinModelPortalP14873.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201584. 12 interactions.
IntActP14873. 7 interactions.
MINTMINT-4101165.

PTM databases

PhosphoSiteP14873.

Proteomic databases

MaxQBP14873.
PaxDbP14873.
PRIDEP14873.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000064762; ENSMUSP00000068374; ENSMUSG00000052727.
GeneID17755.
KEGGmmu:17755.
UCSCuc007rpr.2. mouse.

Organism-specific databases

CTD4131.
MGIMGI:1306778. Map1b.

Phylogenomic databases

eggNOGNOG12793.
GeneTreeENSGT00550000074593.
HOGENOMHOG000063256.
HOVERGENHBG052409.
InParanoidP14873.
KOK10429.
OMARTPVQDH.
OrthoDBEOG773XKP.
TreeFamTF350229.

Gene expression databases

ArrayExpressP14873.
BgeeP14873.
CleanExMM_MTAP1B.
GenevestigatorP14873.

Family and domain databases

Gene3D3.60.15.10. 2 hits.
InterProIPR001279. Beta-lactamas-like.
IPR026074. MAP1.
IPR027321. MAP1B.
IPR000102. MAP1B_neuraxin.
[Graphical view]
PANTHERPTHR13843. PTHR13843. 1 hit.
PTHR13843:SF5. PTHR13843:SF5. 1 hit.
PfamPF00414. MAP1B_neuraxin. 6 hits.
[Graphical view]
PROSITEPS00230. MAP1B_NEURAXIN. 8 hits.
[Graphical view]
ProtoNetSearch...

Other

NextBio292427.
PROP14873.
SOURCESearch...

Entry information

Entry nameMAP1B_MOUSE
AccessionPrimary (citable) accession number: P14873
Secondary accession number(s): E9QM11
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: July 27, 2011
Last modified: July 9, 2014
This is version 134 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot