Microtubule-associated protein 2 - Mus musculus (Mouse)

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P20357 (MAP2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 105. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Microtubule-associated protein 2
Short name=MAP-2

Gene names

Name:	Map2
Synonyms:	Mtap2

Organism

Mus musculus (Mouse)

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	1828 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (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.
Subcellular location	Cytoplasm › cytoskeleton Probable.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylated at serine residues in K-X-G-S motifs by causing MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), detachment from microtubules, and their disassembly By similarity. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10
Sequence similarities	Contains 3 Tau/MAP repeats.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton Microtubule
Domain	Repeat
Ligand	Calmodulin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	axonogenesis Inferred from mutant phenotype. Source: MGI microtubule bundle formation Inferred from mutant phenotype. Source: MGI negative regulation of microtubule depolymerization Inferred from electronic annotation. Source: InterPro peptidyl-threonine phosphorylation Inferred from direct assay. Source: MGI
Cellular component	cytoplasm Inferred from direct assay. Source: MGI dendritic shaft Inferred from direct assay. Source: MGI microtubule Inferred from electronic annotation. Source: UniProtKB-KW microtubule associated complex Traceable author statement. Source: MGI neuronal cell body Inferred from direct assay. Source: MGI nuclear periphery Inferred from direct assay. Source: MGI
Molecular function	calmodulin binding Inferred from electronic annotation. Source: UniProtKB-KW cytoskeletal regulatory protein binding Traceable author statement. Source: MGI
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 1828

1828

Microtubule-associated protein 2

PRO_0000072748

Regions

Repeat

1662 – 1692

Tau/MAP 1

Repeat

1693 – 1723

Tau/MAP 2

Repeat

1724 – 1755

Tau/MAP 3

Region

1452 – 1472

Calmodulin-binding Potential

Amino acid modifications

Modified residue

Phosphoserine By similarity

Modified residue

608

Phosphoserine Ref.5 Ref.8

Modified residue

626

Phosphoserine Ref.5

Modified residue

655

Phosphoserine Ref.5

Modified residue

730

Phosphoserine Ref.5

Modified residue

737

Phosphoserine Ref.5

Modified residue

746

Phosphotyrosine Ref.6

Modified residue

823

Phosphoserine Ref.5 Ref.8

Modified residue

835

Phosphoserine By similarity

Modified residue

1161

Phosphoserine Ref.6

Modified residue

1352

Phosphoserine Ref.5 Ref.6 Ref.7 Ref.8

Modified residue

1358

Phosphothreonine Ref.5 Ref.6 Ref.7 Ref.8

Modified residue

1426

Phosphoserine Ref.7

Modified residue

1445

Phosphothreonine Ref.7

Modified residue

1485

Phosphoserine Ref.7

Modified residue

1539

Phosphoserine Ref.6 Ref.7

Modified residue

1595

Phosphoserine Ref.5

Modified residue

1598

Phosphothreonine Ref.5

Modified residue

1599

Phosphothreonine Ref.8

Modified residue

1606

Phosphothreonine Ref.5

Modified residue

1609

Phosphothreonine Ref.5 Ref.7 Ref.8

Modified residue

1612

Phosphoserine Ref.8

Modified residue

1615

Phosphoserine Ref.5

Modified residue

1617

Phosphothreonine By similarity

Modified residue

1620

Phosphothreonine Ref.8

Modified residue

1650

Phosphothreonine Ref.7 Ref.10

Modified residue

1657

Phosphothreonine Ref.10

Modified residue

1680

Phosphoserine; by MARK1 By similarity

Modified residue

1783

Phosphoserine Ref.6 Ref.8 Ref.10

Modified residue

1791

Phosphoserine Ref.9

Modified residue

1799

Phosphoserine By similarity

Modified residue

1800

Phosphoserine By similarity

Modified residue

1801

Phosphoserine By similarity

Modified residue

1803

Phosphoserine By similarity

Experimental info

Sequence conflict

116

H → Y no nucleotide entry Ref.1

Sequence conflict

116

H → Y in AAA39490. Ref.2

Sequence conflict

455

K → E no nucleotide entry Ref.1

Sequence conflict

455

K → E in AAA39490. Ref.2

Sequence conflict

459

F → L no nucleotide entry Ref.1

Sequence conflict

459

F → L in AAA39490. Ref.2

Sequence conflict

644

D → G no nucleotide entry Ref.1

Sequence conflict

644

D → G in AAA39490. Ref.2

Sequence conflict

938

S → T no nucleotide entry Ref.1

Sequence conflict

938

S → T in AAA39490. Ref.2

Sequence conflict

947

R → G no nucleotide entry Ref.1

Sequence conflict

947

R → G in AAA39490. Ref.2

Sequences

Sequence

Length

Mass (Da)

Tools

P20357 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: E8FA7621C45D5A0D
Show »

FASTA

1,828

199,132

        10         20         30         40         50         60 
MADERKDEGK APHWTSASLT EAAAHPHSPE MKDQGGAGEG LSRNANGFPY REEEEGAFGE 

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

       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 AVAKKEESFK 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 YTPDHPSELP 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 FTAEKEASPP TSADKSRLSR 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

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Complete sequence of a cDNA encoding mouse MAP2." Wang D., Lewis S.A., Cowan N.J. Nucleic Acids Res. 16:11369-11370(1988) [PubMed: 3205744] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Microtubule-associated protein MAP2 shares a microtubule binding motif with tau protein." Lewis S.A., Wang D., Cowan N.J. Science 242:936-939(1988) [PubMed: 3142041] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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. Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed: 19468303] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: C57BL/6.
[4]	Lubec G., Sunyer B., Chen W.-Q. Submitted (JAN-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 94-107; 583-597; 909-920; 989-1004; 1159-1174; 1403-1414 AND 1511-1538, MASS SPECTROMETRY. Strain: OF1. Tissue: Hippocampus.
[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: 15345747] [Abstract] Cited for: 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, MASS SPECTROMETRY. Tissue: Embryonic brain.
[6]	"Proteomic analysis of in vivo phosphorylated synaptic proteins." Collins M.O., Yu L., Coba M.P., Husi H., Campuzano I., Blackstock W.P., Choudhary J.S., Grant S.G. J. Biol. Chem. 280:5972-5982(2005) [PubMed: 15572359] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-746; SER-1161; SER-1352; THR-1358; SER-1539 AND SER-1783, MASS SPECTROMETRY. Tissue: Forebrain.
[7]	"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: 16452087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1352; THR-1358; SER-1426; THR-1445; SER-1485; SER-1539; THR-1609 AND THR-1650, MASS SPECTROMETRY. Tissue: Brain.
[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: 17114649] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-608; SER-823; SER-1352; THR-1358; THR-1599; THR-1609; SER-1612; THR-1620 AND SER-1783, MASS SPECTROMETRY. Tissue: Brain cortex.
[9]	"Large-scale phosphorylation analysis of mouse liver." Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed: 17242355] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1791, MASS SPECTROMETRY. Tissue: Liver.
[10]	"Solid tumor proteome and phosphoproteome analysis by high resolution mass spectrometry." Zanivan S., Gnad F., Wickstroem S.A., Geiger T., Macek B., Cox J., Faessler R., Mann M. J. Proteome Res. 7:5314-5326(2008) [PubMed: 19367708] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1650; THR-1657 AND SER-1783, MASS SPECTROMETRY. Tissue: Melanoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M21041 mRNA. Translation: AAA39490.1. AC091465 Genomic DNA. No translation available.
IPI	IPI00118075.
PIR	A40115.
UniGene	Mm.256966.
3D structure databases
ProteinModelPortal	P20357.
ModBase	Search...
Protein-protein interaction databases
IntAct	P20357. 8 interactions.
MINT	MINT-4101182.
STRING	P20357.
PTM databases
PhosphoSite	P20357.
Proteomic databases
PRIDE	P20357.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000114013; ENSMUSP00000109646; ENSMUSG00000015222.
Organism-specific databases
MGI	MGI:97175. Mtap2.
Phylogenomic databases
eggNOG	roNOG04591.
HOGENOM	HBG281882.
HOVERGEN	HBG006322.
InParanoid	P20357.
OrthoDB	EOG4QVCB3.
Gene expression databases
ArrayExpress	P20357.
Bgee	P20357.
CleanEx	MM_MTAP2.
Genevestigator	P20357.
GermOnline	ENSMUSG00000015222. Mus musculus.
Family and domain databases
InterPro	IPR013588. MAP2_projctn. IPR001084. Tau_tubulin-bd. [Graphical view]
Pfam	PF08377. MAP2_projctn. 1 hit. PF00418. Tubulin-binding. 3 hits. [Graphical view]
PROSITE	PS00229. TAU_MAP_1. 2 hits. PS51491. TAU_MAP_2. 3 hits. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

MAP2_MOUSE

Accession

Primary (citable) accession number: P20357
Secondary accession number(s): E9QLE1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1991
Last sequence update:	July 27, 2011
Last modified:	November 16, 2011
This is version 105 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

MGD cross-references

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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents