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P15146 (MAP2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein 2
Short name=MAP-2
Gene names
Name:Map2
Synonyms:Mtap2
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length1861 AA.
Sequence statusComplete.
Protein existenceEvidence 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.

Developmental stage

Isoform MAP2C is expressed during embryonic brain development and until postanatal day 10. Isoform MAP2B is expressed throughout brain development.

Post-translational modification

MAP2A/c is phosphorylated. Phosphorylated at serine residues in K-X-G-S motifs by MAP/microtubule affinity-regulating kinase (MARK1 or MARK2), causing detachment from microtubules, and their disassembly. Isoform MAP2c is phosphorylated by FYN at Tyr-67 By similarity. Ref.6 Ref.7

Sequence similarities

Contains 4 Tau/MAP repeats.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Note: Additional isoforms seem to exist.
Isoform MAP2x (identifier: P15146-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform MAP2b (identifier: P15146-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1695-1725: Missing.
Isoform MAP2c (identifier: P15146-3)

The sequence of this isoform differs from the canonical sequence as follows:
     152-1514: Missing.
     1695-1725: Missing.
Note: Phosphorylated on Tyr-67 by FYN (By similarity).
Isoform MAP2d (identifier: P15146-4)

The sequence of this isoform differs from the canonical sequence as follows:
     152-1514: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18611861Microtubule-associated protein 2
PRO_0000072749

Regions

Repeat1664 – 169431Tau/MAP 1
Repeat1695 – 172531Tau/MAP 2
Repeat1726 – 175631Tau/MAP 3
Repeat1757 – 178832Tau/MAP 4
Region1454 – 147421Calmodulin-binding Potential

Amino acid modifications

Modified residue6101Phosphoserine By similarity
Modified residue6281Phosphoserine By similarity
Modified residue6571Phosphoserine By similarity
Modified residue7321Phosphoserine By similarity
Modified residue7391Phosphoserine By similarity
Modified residue7481Phosphotyrosine By similarity
Modified residue8251Phosphoserine By similarity
Modified residue11621Phosphoserine By similarity
Modified residue13531Phosphoserine By similarity
Modified residue13591Phosphothreonine By similarity
Modified residue14271Phosphoserine By similarity
Modified residue14461Phosphothreonine By similarity
Modified residue14871Phosphoserine By similarity
Modified residue15411Phosphoserine By similarity
Modified residue15971Phosphoserine By similarity
Modified residue16001Phosphothreonine By similarity
Modified residue16011Phosphothreonine By similarity
Modified residue16081Phosphothreonine By similarity
Modified residue16111Phosphothreonine By similarity
Modified residue16141Phosphoserine By similarity
Modified residue16171Phosphoserine By similarity
Modified residue16191Phosphothreonine Ref.8
Modified residue16221Phosphothreonine Ref.8
Modified residue16521Phosphothreonine By similarity
Modified residue16591Phosphothreonine By similarity
Modified residue16821Phosphoserine; by PKA and MARK1 Ref.6
Modified residue17441Phosphoserine; by PKA
Modified residue17761Phosphoserine; by PKA
Modified residue18161Phosphoserine By similarity
Modified residue18241Phosphoserine By similarity

Natural variations

Alternative sequence152 – 15141363Missing in isoform MAP2c and isoform MAP2d.
VSP_003198
Alternative sequence1695 – 172531Missing in isoform MAP2b and isoform MAP2c.
VSP_003199

Sequences

Sequence LengthMass (Da)Tools
Isoform MAP2x [UniParc].

Last modified June 1, 1994. Version 3.
Checksum: 42DCF116D21EF54E

FASTA1,861202,411
        10         20         30         40         50         60 
MADERKDEGK APHWTSASLT EAAAHPHSPE MKDQGGSGEG LSRSANGFPY REEEEGAFGE 

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

       130        140        150        160        170        180 
AALPLAAEET VNLPPSPPPS PASEQTAALE EDLLTASKME FPEQQKLPSS FAEPLDKEET 

       190        200        210        220        230        240 
EFKMQSKPGE DFEHAALVPQ PDTSKTPQDK KDPQDMEGEK SPASPFAQTF GTNLEDIKQI 

       250        260        270        280        290        300 
TEPSITVPSI GLSAEPLAPK DQKDWFIEMP VESKKDEWGL AAPISPGPLT PMREKDVLED 

       310        320        330        340        350        360 
IPRWEGKQFD SPMPSPFHGG SFTLPLDTVK DERVTEGSQP FAPVFFQSDD KMSLQDTSGS 

       370        380        390        400        410        420 
ATSKESSKDE EPQKDKADKV ADVPVSEATT VLGDVHSPAV EGFVGENISG EEKGTTDQEK 

       430        440        450        460        470        480 
KETSTPSVQE PTLTETEPQT KLEETSKVSI EETVAKEEES LKLKDDKAGV IQTSTEQSFS 

       490        500        510        520        530        540 
KEDQKGQEQT IEALKQDSFP ISLEQAVTDA AMATKTLEKV TSEPEAVSEK REIQGLFEED 

       550        560        570        580        590        600 
IADKSKLEGA GSATVAEVEM PFYEDKSGMS KYFETSALKE DVTRSTGLGS DYYELSDSRG 

       610        620        630        640        650        660 
NAQESLDTVS PKNQQDEKEL LAKASQPSPP AHEAGYSTLA QSYTSDHPSE LPEEPSSPQE 

       670        680        690        700        710        720 
RMFTIDPKVY GEKRDLHSKN KDDLTLSRSL GLGGRSAIEQ RSMSINLPMS CLDSIALGFN 

       730        740        750        760        770        780 
FGRGHDLSPL ASDILTNTSG SMDEGDDYLP PTTPAVEKIP CFPIESKEEE DKTEQAKVTG 

       790        800        810        820        830        840 
GQTTQVETSS ESPFPAKEYY KNGTVMAPDL PEMLDLAGTR SRLASVSADA EVARRKSVPS 

       850        860        870        880        890        900 
EAVVAESSTG LPPVADDSQP VKPDSQLEDM GYCVFNKYTV PLPSPVQDSE NLSGESGSFY 

       910        920        930        940        950        960 
EGTDDKVRRD LATDLSLIEV KLAAAGRVKD EFTAEKEASP PSSADKSGLS REFDQDRKAN 

       970        980        990       1000       1010       1020 
DKLDTVLEKS EEHVDSKEHA KESEEVGDKV ELFGLGVTYE QTSAKELITT KETAPERAEK 

      1030       1040       1050       1060       1070       1080 
GLSSVPEVAE VETTTKADQG LDVAAKKDDQ SPLDIKVSDF GQMASGMSVD AGKTIELKFE 

      1090       1100       1110       1120       1130       1140 
VDQQLTLSSE APQETDSFMG IESSHVKDGA KVSETEVKEK VAKPDLVHQE AVDKEESYES 

      1150       1160       1170       1180       1190       1200 
SGEHESLTME SLKPDEGKKE TSPETSLIQD EVALKLSVEI PCPPPVSEAD SSIDEKAEVQ 

      1210       1220       1230       1240       1250       1260 
MEFIQLPKEE STETPDIPAI PSDVTQPQPE AVVSEPAEVR GEEEEIEAEG EYDKLLFRSD 

      1270       1280       1290       1300       1310       1320 
TLQITDLLVP GSREEFVETC PGEHKGVVES VVTIEDDFIT VVQTTTDEGE LGSHSVRFAA 

      1330       1340       1350       1360       1370       1380 
PVQPEEERRP YPHDEELEVL MAAEAQAEPK DGSPDAPATP EKEEVPFSEY KTETYDDYKD 

      1390       1400       1410       1420       1430       1440 
ETTIDDSIMD ADSLWVDTQD DDRSILTEQL ETIPKEERAE KEARRPSLEK HRKEKPFKTG 

      1450       1460       1470       1480       1490       1500 
RGRISTPERR EVAKKEPSTV SRDEVRRKKA VYKKAELAKE SEVQAHSPSR KLILKPAIKY 

      1510       1520       1530       1540       1550       1560 
TRPTHLSCVK RKTTATSGES AQAPSAFKQA KDKVTDGITK SPEKRSSLPR PSSILPPRRG 

      1570       1580       1590       1600       1610       1620 
VSGDREENSF SLNSSISSAR RTTRSEPIRR AGKSGTSTPT TPGSTAITPG TPPSYSSRTP 

      1630       1640       1650       1660       1670       1680 
GTPGTPSYPR TPGTPKSGIL VPSEKKVAII RTPPKSPATP KQLRLINQPL PDLKNVKSKI 

      1690       1700       1710       1720       1730       1740 
GSTDNIKYQP KGGQVRILNK KMDFSKVQSR CGSKDNIKHS AGGGNVQIVT KKIDLSHVTS 

      1750       1760       1770       1780       1790       1800 
KCGSLKNIRH RPGGGRVKIE SVKLDFKEKA QAKVGSLDNA HHVPGGGNVK IDSQKLNFRE 

      1810       1820       1830       1840       1850       1860 
HAKARVDHGA EIITQSPSRS SVASPRRLSN VSSSGSINLL ESPQLATLAE DVTAALAKQG 


L

« Hide

Isoform MAP2b [UniParc].

Checksum: 2A52B720268B0551
Show »

FASTA1,830199,053
Isoform MAP2c [UniParc].

Checksum: 35ACB5CA6E542606
Show »

FASTA46749,300
Isoform MAP2d [UniParc].

Checksum: D0CE2BD6CE0ABA3E
Show »

FASTA49852,658

References

« Hide 'large scale' references
[1]"Complete cDNA sequence encoding rat high and low molecular weight MAP2."
Kindler S., Schwanke B., Schulz B., Garner C.C.
Nucleic Acids Res. 18:2822-2822(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAP2B).
Strain: Wistar.
Tissue: Brain.
[2]"Molecular structure of microtubule-associated protein 2b and 2c from rat brain."
Kindler S., Schulz B., Goedert M., Garner C.C.
J. Biol. Chem. 265:19679-19684(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAP2B).
Strain: Wistar.
Tissue: Brain.
[3]"Nucleotide and amino acid sequences of embryonic rat MAP2c."
Doll T., Papandrikopoulou A., Matus A.
Nucleic Acids Res. 18:361-361(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM MAP2C).
[4]"Embryonic MAP2 lacks the cross-linking sidearm sequences and dendritic targeting signal of adult MAP2."
Papandrikopoulou A., Doll T., Tucker R.P., Garner C.C., Matus A.
Nature 340:650-652(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: DISCUSSION OF SEQUENCE.
[5]"An isoform of microtubule-associated protein 2 (MAP2) containing four repeats of the tubulin-binding motif."
Doll T., Meichsner M., Riederer B.M., Honegger P., Matus A.
J. Cell Sci. 106:633-640(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1695-1725 (ISOFORM MAP2X).
[6]"MARK - a novel family of protein kinases that phosphorylate microtubule-associated proteins and trigger microtubule disruption."
Drewes G., Ebneth A., Preuss U., Mandelkow E.-M., Mandelkow E.
Cell 89:297-308(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1682.
Strain: Sprague-Dawley.
Tissue: Brain.
[7]"Phosphorylation-dependent localization of microtubule-associated protein MAP2c to the actin cytoskeleton."
Ozer R.S., Halpain S.
Mol. Biol. Cell 11:3573-3587(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION.
[8]"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 THR-1619 AND THR-1622, MASS SPECTROMETRY.
Tissue: Renal collecting duct.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X51842 mRNA. Translation: CAA36135.1.
X17682 mRNA. Translation: CAA35667.1.
X71487 mRNA. Translation: CAA50588.1.
IPIIPI00206171.
IPI00231051.
IPI00231052.
IPI00231053.
PIRA37981.
S33176. I55502.
UniGeneRn.10484.

3D structure databases

DisProtDP00122.
ModBaseSearch...

Protein-protein interaction databases

MINTMINT-261227.

PTM databases

PhosphoSiteP15146.

Proteomic databases

PaxDbP15146.
PRIDEP15146.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:3044. rat.

Organism-specific databases

RGD3044. Map2.

Phylogenomic databases

eggNOGNOG148882.
HOGENOMHOG000113477.
HOVERGENHBG006322.
InParanoidP15146.

Gene expression databases

ArrayExpressP15146.
GenevestigatorP15146.
GermOnlineENSRNOG00000011841. Rattus norvegicus.

Family and domain databases

InterProIPR027324. MAP2/MAP4/Tau.
IPR013588. MAP2_projctn.
IPR001084. Tau/MAP_tubulin-bd_rpt.
[Graphical view]
PANTHERPTHR11501. PTHR11501. 1 hit.
PfamPF08377. MAP2_projctn. 1 hit.
PF00418. Tubulin-binding. 4 hits.
[Graphical view]
PROSITEPS00229. TAU_MAP_1. 3 hits.
PS51491. TAU_MAP_2. 4 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMAP2_RAT
AccessionPrimary (citable) accession number: P15146
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: June 1, 1994
Last modified: May 1, 2013
This is version 117 of the entry and version 3 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

to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents