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Protein

Microtubule-associated protein 2

Gene

Map2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

GO - Molecular functioni

  • cytoskeletal regulatory protein binding Source: MGI
  • dystroglycan binding Source: MGI
  • microtubule binding Source: MGI

GO - Biological processi

  • axonogenesis Source: MGI
  • cellular response to organic substance Source: MGI
  • central nervous system neuron development Source: InterPro
  • dendrite development Source: MGI
  • establishment of cell polarity Source: MGI
  • microtubule bundle formation Source: MGI
  • regulation of axonogenesis Source: MGI
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 2
Short name:
MAP-2
Gene namesi
Name:Map2
Synonyms:Mtap2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:97175. Map2.

Subcellular locationi

GO - Cellular componenti

  • CA3 pyramidal cell dendrite Source: MGI
  • cell body Source: MGI
  • cytoplasm Source: MGI
  • dendrite Source: MGI
  • dendritic shaft Source: MGI
  • intracellular Source: MGI
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: MGI
  • neuronal cell body Source: MGI
  • neuronal postsynaptic density Source: MGI
  • neuron projection Source: MGI
  • nuclear periphery Source: MGI
  • nucleolus Source: MGI
  • postsynaptic density Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18281828Microtubule-associated protein 2PRO_0000072748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei28 – 281PhosphoserineCombined sources
Modified residuei136 – 1361PhosphoserineCombined sources
Modified residuei140 – 1401PhosphoserineCombined sources
Modified residuei143 – 1431PhosphoserineCombined sources
Modified residuei283 – 2831PhosphoserineCombined sources
Modified residuei333 – 3331PhosphoserineCombined sources
Modified residuei346 – 3461PhosphoserineBy similarity
Modified residuei476 – 4761PhosphoserineCombined sources
Modified residuei496 – 4961PhosphoserineCombined sources
Modified residuei520 – 5201PhosphoserineBy similarity
Modified residuei550 – 5501PhosphoserineCombined sources
Modified residuei596 – 5961PhosphoserineCombined sources
Modified residuei599 – 5991PhosphoserineCombined sources
Modified residuei603 – 6031PhosphoserineCombined sources
Modified residuei608 – 6081PhosphoserineCombined sources
Modified residuei626 – 6261PhosphoserineBy similarity
Modified residuei726 – 7261PhosphoserineCombined sources
Modified residuei730 – 7301PhosphoserineCombined sources
Modified residuei734 – 7341PhosphothreonineCombined sources
Modified residuei737 – 7371PhosphoserineCombined sources
Modified residuei739 – 7391PhosphoserineCombined sources
Modified residuei746 – 7461PhosphotyrosineCombined sources
Modified residuei823 – 8231PhosphoserineCombined sources
Modified residuei883 – 8831PhosphoserineBy similarity
Modified residuei892 – 8921PhosphoserineBy similarity
Modified residuei938 – 9381PhosphoserineBy similarity
Modified residuei1050 – 10501PhosphoserineBy similarity
Modified residuei1139 – 11391PhosphoserineCombined sources
Modified residuei1140 – 11401PhosphoserineCombined sources
Modified residuei1145 – 11451PhosphoserineCombined sources
Modified residuei1160 – 11601PhosphothreonineBy similarity
Modified residuei1161 – 11611PhosphoserineCombined sources
Modified residuei1165 – 11651PhosphoserineCombined sources
Modified residuei1352 – 13521PhosphoserineCombined sources
Modified residuei1358 – 13581PhosphothreonineCombined sources
Modified residuei1539 – 15391PhosphoserineCombined sources
Modified residuei1560 – 15601PhosphoserineCombined sources
Modified residuei1592 – 15921PhosphoserineCombined sources
Modified residuei1606 – 16061PhosphothreonineCombined sources
Modified residuei1609 – 16091PhosphothreonineCombined sources
Modified residuei1620 – 16201PhosphothreonineCombined sources
Modified residuei1623 – 16231PhosphothreonineCombined sources
Modified residuei1650 – 16501PhosphothreonineCombined sources
Modified residuei1654 – 16541PhosphoserineBy similarity
Modified residuei1680 – 16801Phosphoserine; by MARK1By similarity
Modified residuei1783 – 17831PhosphoserineCombined sources
Modified residuei1788 – 17881PhosphoserineCombined sources
Modified residuei1791 – 17911PhosphoserineCombined sources
Modified residuei1796 – 17961PhosphoserineBy similarity
Modified residuei1809 – 18091PhosphoserineBy similarity

Post-translational modificationi

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

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP20357.
PaxDbiP20357.
PeptideAtlasiP20357.
PRIDEiP20357.

PTM databases

iPTMnetiP20357.
PhosphoSiteiP20357.

Expressioni

Gene expression databases

BgeeiP20357.
CleanExiMM_MTAP2.
ExpressionAtlasiP20357. baseline and differential.
GenevisibleiP20357. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Kndc1Q0KK559EBI-397863,EBI-8605532

GO - Molecular functioni

  • cytoskeletal regulatory protein binding Source: MGI
  • dystroglycan binding Source: MGI
  • microtubule binding Source: MGI

Protein-protein interaction databases

BioGridi201585. 8 interactions.
IntActiP20357. 19 interactions.
MINTiMINT-4101182.
STRINGi10090.ENSMUSP00000109650.

Structurei

3D structure databases

ProteinModelPortaliP20357.
SMRiP20357. Positions 1685-1726.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati1662 – 169231Tau/MAP 1Add
BLAST
Repeati1693 – 172331Tau/MAP 2Add
BLAST
Repeati1724 – 175532Tau/MAP 3Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1452 – 147221Calmodulin-bindingSequence analysisAdd
BLAST

Sequence similaritiesi

Contains 3 Tau/MAP repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2418. Eukaryota.
ENOG4111J07. LUCA.
GeneTreeiENSGT00530000063491.
HOGENOMiHOG000113477.
HOVERGENiHBG006322.
InParanoidiP20357.
KOiK10430.
OMAiEHKGVIE.
OrthoDBiEOG75XGKK.

Family and domain databases

InterProiIPR030797. MAP2.
IPR027324. MAP2/MAP4/Tau.
IPR013588. MAP2_projctn.
IPR001084. MAP_tubulin-bd_rpt.
[Graphical view]
PANTHERiPTHR11501. PTHR11501. 1 hit.
PTHR11501:SF15. PTHR11501:SF15. 1 hit.
PfamiPF08377. MAP2_projctn. 1 hit.
PF00418. Tubulin-binding. 3 hits.
[Graphical view]
PROSITEiPS00229. TAU_MAP_1. 2 hits.
PS51491. TAU_MAP_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P20357-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MADERKDEGK APHWTSASLT EAAAHPHSPE MKDQGGAGEG LSRNANGFPY
60 70 80 90 100
REEEEGAFGE HRSQGTYSDT KENGINGELT SADRETAEEV SARIVQVVTA
110 120 130 140 150
EAVAVLKGEQ EKEAQHKDQP AALPLAAEET ANLPPSPPPS PASEQTATVE
160 170 180 190 200
EDLLTASKME FPEQEKFPSS FAEPLDKGEM EFKMPSKPGE DFEHAALVPD
210 220 230 240 250
TSKTPQDKKD LQGMEGEKLP PVPFAQTFGT NLEDRKQSTE PSIVMPSIGL
260 270 280 290 300
SAEPPAPKEP KDWFIEMPTE SKKDEWGLAA PISPGPLTPM REKDVLEDIP
310 320 330 340 350
RWEGKQFDSP MPSPFHGGSF TLPLDTMKNE RVSEGPRPFA PVFFQSDDKV
360 370 380 390 400
SLQDPSALAT SKESSKDEEP LKDKADKVAD VSISEVTTLL GNVHSPVVEG
410 420 430 440 450
YVGENISGEV KVTTDQEKKE TSAPSVQEPT LTETEPQTKL DEKSTVSIEE
460 470 480 490 500
AVAKKEESFK LRDDKTGVIQ TSTEQSFSKE DQKGQEHTID ELKQDSFPIS
510 520 530 540 550
LEQAVTDAAM TSKTLGKVTS EPEAVSERRE IQGLFEEKTA DKNKLEGAGS
560 570 580 590 600
ATIAEVEMPF YEDKSGMSKY FETSALKEDM TRSTELGSDY YELSDSRGSA
610 620 630 640 650
QESLDTISPK NQHDEKELQA KASQPSPPAQ EAGYSTLAQS YTPDHPSELP
660 670 680 690 700
EEPSSPQERM FTIDPKVYGE KRDLHSKNKD DLTLSRSLGL GGRSAIEQRS
710 720 730 740 750
MSINLPMSCL DSIALGFNFG RGHDLSPLAS DILTNTSGSM DEGDDYLPPT
760 770 780 790 800
TPAVEKMPCF PIESKEEEDK AEQAKVTGGQ TIQVETSSES PFPAKEYYKN
810 820 830 840 850
GTVMAPDLPE MLDLAGTRSR LASVSADAEV ARRKSVPSEA MLAESSTSLP
860 870 880 890 900
PVADESPVTV KPDSQLEDMG YCVFNKYTVP LPSPVQDSEN LSGESGSFYE
910 920 930 940 950
GTDDKVRRDL ATDLSLIEVK LAAAGRVKDE FTAEKEASPP TSADKSRLSR
960 970 980 990 1000
EFDHDRKAND KLDTVLEKSE EHIDSKEHAK ESEEMGGKVE LFGLGITYDQ
1010 1020 1030 1040 1050
ASTKELITTK DTSPEKTEKG LSSVPEVAEV EPTTKADQGL DFAATKAEPS
1060 1070 1080 1090 1100
QLDIKVSDFG QMASGMNVDA GKAIELKFEV AQELTLSSEA PQEADSFMGV
1110 1120 1130 1140 1150
ESGHIKEGGK VNETEVKEKV TKPDLVHQEA VDKEESYESS GEHESLTMES
1160 1170 1180 1190 1200
LKPDEGKKET SPETSLIQDE VALKLSVEIP CPPPVSEADL STDEKGEVQM
1210 1220 1230 1240 1250
EFIQLPKEES TETPDIPAIP SDVTQPQPEA IVSEPAEVPS EEEEIEAGGE
1260 1270 1280 1290 1300
YDKLLFRSDT LQISDLLVSE SREEFVETCP GELKGVVESV VTIEDDFITV
1310 1320 1330 1340 1350
VQTTTDEGES GSHSVRFAAP AQPEEERRPR PHDEELEIEM AAEAQAEPKD
1360 1370 1380 1390 1400
GSPDAPATPE KEEVAFSEYK TETYDDYKDE TTIDDSIMDA DSLWVDTQDD
1410 1420 1430 1440 1450
DRSILTEQLE TIPKEERAEK DARRPSLEKH RKEKPFKTGR GRISTPERKV
1460 1470 1480 1490 1500
AKKEPSTVSR DEVRRKKAVY KKAELAKKSE VQAHSPSRKL ILKPAIKYTR
1510 1520 1530 1540 1550
PTHLSCVKRK TTAASGDLAQ APGAFKQAKD KVTDGISKSP EKRSSLPRPS
1560 1570 1580 1590 1600
SILPPRRGVS GDREENSFSL NSSISSARRT TRSEPIRRAG KSGTSTPTTP
1610 1620 1630 1640 1650
GSTAITPGTP PSYSSRTPGT PGTPSYPRTP GTPKSGILVP SEKKVAIIRT
1660 1670 1680 1690 1700
PPKSPATPKQ LRLINQPLPD LKNVKSKIGS TDNIKYQPKG GQVQIVTKKI
1710 1720 1730 1740 1750
DLSHVTSKCG SLKNIRHRPG GGRVKIESVK LDFKEKAQAK VGSLDNAHHV
1760 1770 1780 1790 1800
PGGGNVKIDS QKLNFREHAK ARVDHGAEII TQSPSRSSVA SPRRLSNVSS
1810 1820
SGSINLLESP QLATLAEDVT AALAKQGL
Length:1,828
Mass (Da):199,132
Last modified:July 27, 2011 - v2
Checksum:iE8FA7621C45D5A0D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti116 – 1161H → Y no nucleotide entry (PubMed:3205744).Curated
Sequence conflicti116 – 1161H → Y in AAA39490 (PubMed:3142041).Curated
Sequence conflicti455 – 4551K → E no nucleotide entry (PubMed:3205744).Curated
Sequence conflicti455 – 4551K → E in AAA39490 (PubMed:3142041).Curated
Sequence conflicti459 – 4591F → L no nucleotide entry (PubMed:3205744).Curated
Sequence conflicti459 – 4591F → L in AAA39490 (PubMed:3142041).Curated
Sequence conflicti644 – 6441D → G no nucleotide entry (PubMed:3205744).Curated
Sequence conflicti644 – 6441D → G in AAA39490 (PubMed:3142041).Curated
Sequence conflicti938 – 9381S → T no nucleotide entry (PubMed:3205744).Curated
Sequence conflicti938 – 9381S → T in AAA39490 (PubMed:3142041).Curated
Sequence conflicti947 – 9471R → G no nucleotide entry (PubMed:3205744).Curated
Sequence conflicti947 – 9471R → G in AAA39490 (PubMed:3142041).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21041 mRNA. Translation: AAA39490.1.
AC091465 Genomic DNA. No translation available.
PIRiA40115.
RefSeqiNP_001297563.1. NM_001310634.1.
XP_006495817.1. XM_006495754.2.
UniGeneiMm.256966.
Mm.436793.

Genome annotation databases

EnsembliENSMUST00000114013; ENSMUSP00000109646; ENSMUSG00000015222.
GeneIDi17756.
KEGGimmu:17756.
UCSCiuc007bhz.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M21041 mRNA. Translation: AAA39490.1.
AC091465 Genomic DNA. No translation available.
PIRiA40115.
RefSeqiNP_001297563.1. NM_001310634.1.
XP_006495817.1. XM_006495754.2.
UniGeneiMm.256966.
Mm.436793.

3D structure databases

ProteinModelPortaliP20357.
SMRiP20357. Positions 1685-1726.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201585. 8 interactions.
IntActiP20357. 19 interactions.
MINTiMINT-4101182.
STRINGi10090.ENSMUSP00000109650.

PTM databases

iPTMnetiP20357.
PhosphoSiteiP20357.

Proteomic databases

MaxQBiP20357.
PaxDbiP20357.
PeptideAtlasiP20357.
PRIDEiP20357.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114013; ENSMUSP00000109646; ENSMUSG00000015222.
GeneIDi17756.
KEGGimmu:17756.
UCSCiuc007bhz.1. mouse.

Organism-specific databases

CTDi4133.
MGIiMGI:97175. Map2.

Phylogenomic databases

eggNOGiKOG2418. Eukaryota.
ENOG4111J07. LUCA.
GeneTreeiENSGT00530000063491.
HOGENOMiHOG000113477.
HOVERGENiHBG006322.
InParanoidiP20357.
KOiK10430.
OMAiEHKGVIE.
OrthoDBiEOG75XGKK.

Miscellaneous databases

PROiP20357.
SOURCEiSearch...

Gene expression databases

BgeeiP20357.
CleanExiMM_MTAP2.
ExpressionAtlasiP20357. baseline and differential.
GenevisibleiP20357. MM.

Family and domain databases

InterProiIPR030797. MAP2.
IPR027324. MAP2/MAP4/Tau.
IPR013588. MAP2_projctn.
IPR001084. MAP_tubulin-bd_rpt.
[Graphical view]
PANTHERiPTHR11501. PTHR11501. 1 hit.
PTHR11501:SF15. PTHR11501:SF15. 1 hit.
PfamiPF08377. MAP2_projctn. 1 hit.
PF00418. Tubulin-binding. 3 hits.
[Graphical view]
PROSITEiPS00229. TAU_MAP_1. 2 hits.
PS51491. TAU_MAP_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: OF1.
    Tissue: Hippocampus.
  5. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-726; SER-1352; THR-1358; THR-1606 AND THR-1609, 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-1352; THR-1358 AND THR-1609, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.
  7. "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.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-28; SER-136; SER-140; SER-143; SER-283; SER-333; SER-476; SER-496; SER-550; SER-596; SER-599; SER-603; SER-608; SER-726; SER-730; THR-734; SER-737; SER-739; TYR-746; SER-823; SER-1139; SER-1140; SER-1145; SER-1161; SER-1165; SER-1352; THR-1358; SER-1539; SER-1560; SER-1592; THR-1606; THR-1609; THR-1620; THR-1623; THR-1650; SER-1783; SER-1788 AND SER-1791, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas and Testis.

Entry informationi

Entry nameiMTAP2_MOUSE
AccessioniPrimary (citable) accession number: P20357
Secondary accession number(s): E9QLE1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 142 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. 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.