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UniProtKB/Swiss-Prot entry P20357


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name MAP2_MOUSE
Primary accession number P20357
Secondary accession numbers None
Integrated into Swiss-Prot on February 1, 1991
Sequence was last modified on February 1, 1991 (Sequence version 1)
Annotations were last modified on    May 5, 2009 (Entry version 84)
Name and origin of the protein
Protein name Microtubule-associated protein 2
Synonym MAP-2
Gene name
Name: Map2
Synonyms: Mtap2
From
Mus musculus (Mouse) [TaxID: 10090] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; Muroidea; Muridae; Murinae; Mus.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/16.23.11369; PubMed=3205744 [NCBI, ExPASy, EBI, Israel, Japan]
Wang D., Lewis S.A., Cowan N.J.;
"Complete sequence of a cDNA encoding mouse MAP2.";
Nucleic Acids Res. 16:11369-11370(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1126/science.3142041; PubMed=3142041 [NCBI, ExPASy, EBI, Israel, Japan]
Lewis S.A., Wang D., Cowan N.J.;
"Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein.";
Science 242:936-939(1988).
[3]
PROTEIN SEQUENCE OF 94-107; 583-597; 909-920; 989-1004; 1159-1174; 1403-1414 AND 1511-1538, AND MASS SPECTROMETRY.
STRAIN=OF1;
TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-626; SER-655; SER-730; SER-737; SER-823; SER-1352; THR-1358; SER-1595; THR-1598; THR-1606; THR-1609 AND SER-1615, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/mcp.M400085-MCP200; PubMed=15345747 [NCBI, ExPASy, EBI, Israel, Japan]
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-746; SER-1161; SER-1352; THR-1358; SER-1539 AND SER-1783, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/jbc.M411220200; PubMed=15572359 [NCBI, ExPASy, EBI, Israel, Japan]
Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G.;
"Proteomic analysis of in vivo phosphorylated synaptic proteins.";
J. Biol. Chem. 280:5972-5982(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1352; THR-1358; SER-1426; THR-1445; SER-1485; SER-1539; THR-1609 AND THR-1650, AND MASS SPECTROMETRY.
TISSUE=Brain;
DOI=10.1074/mcp.T500041-MCP200; PubMed=16452087 [NCBI, ExPASy, EBI, Israel, Japan]
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
"Comprehensive identification of phosphorylation sites in postsynaptic density preparations.";
Mol. Cell. Proteomics 5:914-922(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-823; SER-1352; THR-1358; THR-1599; THR-1609; SER-1612; THR-1620 AND SER-1783, AND MASS SPECTROMETRY.
TISSUE=Brain cortex;
DOI=10.1074/mcp.M600046-MCP200; PubMed=17114649 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Qualitative and quantitative analyses of protein phosphorylation in naive and stimulated mouse synaptosomal preparations.";
Mol. Cell. Proteomics 6:283-293(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1791, AND MASS SPECTROMETRY.
TISSUE=Liver;
DOI=10.1073/pnas.0609836104; PubMed=17242355 [NCBI, ExPASy, EBI, Israel, Japan]
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
Comments
  • FUNCTION: The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules.
  • PTM: Phosphorylated upon DNA damage, probably by ATM or ATR (By similarity).
  • SIMILARITY: Contains 3 Tau/MAP repeats.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M21041; AAA39490.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00118075; -.
PIR A40115; A40115.
UniGene Mm.256966
3D structure databases
ModBase P20357.
PTM databases
PhosphoSite P20357; -.
Organism-specific databases
MGI MGI:97175; Mtap2.
Gene expression databases
ArrayExpress P20357; -.
Bgee P20357; -.
CleanEx MM_MTAP2; -.
GermOnline ENSMUSG00000015222; Mus musculus.
Ontologies
GO
GO:0043025; Cellular component: cell soma (inferred from direct assay from MGI).
GO:0005737; Cellular component: cytoplasm (inferred from direct assay from MGI).
GO:0043198; Cellular component: dendritic shaft (inferred from direct assay from MGI).
GO:0005874; Cellular component: microtubule (inferred from electronic annotation from UniProtKB-KW).
GO:0005875; Cellular component: microtubule associated complex (traceable author statement from MGI).
GO:0005516; Molecular function: calmodulin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005519; Molecular function: cytoskeletal regulatory protein binding (traceable author statement from MGI).
GO:0016358; Biological process: dendrite development (inferred from mutant phenotype from MGI).
GO:0001578; Biological process: microtubule bundle formation (inferred from mutant phenotype from MGI).
GO:0007026; Biological process: negative regulation of microtubule depolymerization (inferred from electronic annotation from InterPro).
GO:0018107; Biological process: peptidyl-threonine phosphorylation (inferred from direct assay from MGI).
QuickGo view.
Family and domain databases
InterPro IPR013588; MAP2_projctn.
IPR018459; RII_binding_1.
IPR001084; Tau_tubulin-bd.
Graphical view of domain structure.
Pfam PF08377; MAP2_projctn; 1.
PF10522; RII_binding_1; 1.
PF00418; Tubulin-binding; 3.
Pfam graphical view of domain structure.
PROSITE PS00229; TAU_MAP; 2.
Proteomic databases
PRIDE P20357; -.
Genome annotation databases
Ensembl ENSMUSG00000015222; Mus musculus. [Contig view]
Phylogenomic databases
HOGENOM P20357; -.
HOVERGEN P20357; -.
Other
SOURCE Map2; Mus musculus.
ProtoNet P20357.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Calmodulin-binding; Direct protein sequencing; Microtubule; Phosphoprotein; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   1828  1828     Microtubule-associated protein 2. PRO_0000072748
REPEAT   1662   1692  31     Tau/MAP motif 1. 
REPEAT   1693   1723  31     Tau/MAP motif 2. 
REPEAT   1724   1755  32     Tau/MAP motif 3. 
REGION   1452   1472  21     Calmodulin-binding (Potential). 
MOD_RES   63     63        Phosphoserine (By similarity). 
MOD_RES   608    608        Phosphoserine. 
MOD_RES   626    626        Phosphoserine. 
MOD_RES   655    655        Phosphoserine. 
MOD_RES   730    730        Phosphoserine. 
MOD_RES   737    737        Phosphoserine. 
MOD_RES   746    746        Phosphotyrosine. 
MOD_RES   823    823        Phosphoserine. 
MOD_RES   835    835        Phosphoserine (By similarity). 
MOD_RES   1161   1161        Phosphoserine. 
MOD_RES   1352   1352        Phosphoserine. 
MOD_RES   1358   1358        Phosphothreonine. 
MOD_RES   1426   1426        Phosphoserine. 
MOD_RES   1445   1445        Phosphothreonine. 
MOD_RES   1485   1485        Phosphoserine. 
MOD_RES   1539   1539        Phosphoserine. 
MOD_RES   1595   1595        Phosphoserine. 
MOD_RES   1598   1598        Phosphothreonine. 
MOD_RES   1599   1599        Phosphothreonine. 
MOD_RES   1606   1606        Phosphothreonine. 
MOD_RES   1609   1609        Phosphothreonine. 
MOD_RES   1612   1612        Phosphoserine. 
MOD_RES   1615   1615        Phosphoserine. 
MOD_RES   1617   1617        Phosphothreonine (By similarity). 
MOD_RES   1620   1620        Phosphothreonine. 
MOD_RES   1650   1650        Phosphothreonine. 
MOD_RES   1783   1783        Phosphoserine. 
MOD_RES   1791   1791        Phosphoserine. 
MOD_RES   1799   1799        Phosphoserine (By similarity). 
MOD_RES   1800   1800        Phosphoserine (By similarity). 
MOD_RES   1801   1801        Phosphoserine (By similarity). 
MOD_RES   1803   1803        Phosphoserine (By similarity). 
Sequence information
Length: 1828 AA [This is the length of the unprocessed precursor] Molecular weight: 198982 Da [This is the MW of the unprocessed precursor] CRC64: 200BC59E360538CA [This is a checksum on the sequence]
        10         20         30         40         50         60 
MADERKDEGK APHWTSASLT EAAAHPHSPE MKDQGGAGEG LSRNANGFPY REEEEGAFGE 

        70         80         90        100        110        120 
HRSQGTYSDT KENGINGELT SADRETAEEV SARIVQVVTA EAVAVLKGEQ EKEAQYKDQP 

       130        140        150        160        170        180 
AALPLAAEET ANLPPSPPPS PASEQTATVE EDLLTASKME FPEQEKFPSS FAEPLDKGEM 

       190        200        210        220        230        240 
EFKMPSKPGE DFEHAALVPD TSKTPQDKKD LQGMEGEKLP PVPFAQTFGT NLEDRKQSTE 

       250        260        270        280        290        300 
PSIVMPSIGL SAEPPAPKEP KDWFIEMPTE SKKDEWGLAA PISPGPLTPM REKDVLEDIP 

       310        320        330        340        350        360 
RWEGKQFDSP MPSPFHGGSF TLPLDTMKNE RVSEGPRPFA PVFFQSDDKV SLQDPSALAT 

       370        380        390        400        410        420 
SKESSKDEEP LKDKADKVAD VSISEVTTLL GNVHSPVVEG YVGENISGEV KVTTDQEKKE 

       430        440        450        460        470        480 
TSAPSVQEPT LTETEPQTKL DEKSTVSIEE AVAKEEESLK LRDDKTGVIQ TSTEQSFSKE 

       490        500        510        520        530        540 
DQKGQEHTID ELKQDSFPIS LEQAVTDAAM TSKTLGKVTS EPEAVSERRE IQGLFEEKTA 

       550        560        570        580        590        600 
DKNKLEGAGS ATIAEVEMPF YEDKSGMSKY FETSALKEDM TRSTELGSDY YELSDSRGSA 

       610        620        630        640        650        660 
QESLDTISPK NQHDEKELQA KASQPSPPAQ EAGYSTLAQS YTPGHPSELP EEPSSPQERM 

       670        680        690        700        710        720 
FTIDPKVYGE KRDLHSKNKD DLTLSRSLGL GGRSAIEQRS MSINLPMSCL DSIALGFNFG 

       730        740        750        760        770        780 
RGHDLSPLAS DILTNTSGSM DEGDDYLPPT TPAVEKMPCF PIESKEEEDK AEQAKVTGGQ 

       790        800        810        820        830        840 
TIQVETSSES PFPAKEYYKN GTVMAPDLPE MLDLAGTRSR LASVSADAEV ARRKSVPSEA 

       850        860        870        880        890        900 
MLAESSTSLP PVADESPVTV KPDSQLEDMG YCVFNKYTVP LPSPVQDSEN LSGESGSFYE 

       910        920        930        940        950        960 
GTDDKVRRDL ATDLSLIEVK LAAAGRVKDE FTAEKEATPP TSADKSGLSR EFDHDRKAND 

       970        980        990       1000       1010       1020 
KLDTVLEKSE EHIDSKEHAK ESEEMGGKVE LFGLGITYDQ ASTKELITTK DTSPEKTEKG 

      1030       1040       1050       1060       1070       1080 
LSSVPEVAEV EPTTKADQGL DFAATKAEPS QLDIKVSDFG QMASGMNVDA GKAIELKFEV 

      1090       1100       1110       1120       1130       1140 
AQELTLSSEA PQEADSFMGV ESGHIKEGGK VNETEVKEKV TKPDLVHQEA VDKEESYESS 

      1150       1160       1170       1180       1190       1200 
GEHESLTMES LKPDEGKKET SPETSLIQDE VALKLSVEIP CPPPVSEADL STDEKGEVQM 

      1210       1220       1230       1240       1250       1260 
EFIQLPKEES TETPDIPAIP SDVTQPQPEA IVSEPAEVPS EEEEIEAGGE YDKLLFRSDT 

      1270       1280       1290       1300       1310       1320 
LQISDLLVSE SREEFVETCP GELKGVVESV VTIEDDFITV VQTTTDEGES GSHSVRFAAP 

      1330       1340       1350       1360       1370       1380 
AQPEEERRPR PHDEELEIEM AAEAQAEPKD GSPDAPATPE KEEVAFSEYK TETYDDYKDE 

      1390       1400       1410       1420       1430       1440 
TTIDDSIMDA DSLWVDTQDD DRSILTEQLE TIPKEERAEK DARRPSLEKH RKEKPFKTGR 

      1450       1460       1470       1480       1490       1500 
GRISTPERKV AKKEPSTVSR DEVRRKKAVY KKAELAKKSE VQAHSPSRKL ILKPAIKYTR 

      1510       1520       1530       1540       1550       1560 
PTHLSCVKRK TTAASGDLAQ APGAFKQAKD KVTDGISKSP EKRSSLPRPS SILPPRRGVS 

      1570       1580       1590       1600       1610       1620 
GDREENSFSL NSSISSARRT TRSEPIRRAG KSGTSTPTTP GSTAITPGTP PSYSSRTPGT 

      1630       1640       1650       1660       1670       1680 
PGTPSYPRTP GTPKSGILVP SEKKVAIIRT PPKSPATPKQ LRLINQPLPD LKNVKSKIGS 

      1690       1700       1710       1720       1730       1740 
TDNIKYQPKG GQVQIVTKKI DLSHVTSKCG SLKNIRHRPG GGRVKIESVK LDFKEKAQAK 

      1750       1760       1770       1780       1790       1800 
VGSLDNAHHV PGGGNVKIDS QKLNFREHAK ARVDHGAEII TQSPSRSSVA SPRRLSNVSS 

      1810       1820 
SGSINLLESP QLATLAEDVT AALAKQGL 

P20357 in FASTA format

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