UniProtKB - P20357 (MTAP2_MOUSE)
Protein
Microtubule-associated protein 2
Gene
Map2
Organism
Mus musculus (Mouse)
Status
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
- actin binding Source: MGI
- calmodulin binding Source: UniProtKB-KW
- cytoskeletal regulatory protein binding Source: MGI
- dystroglycan binding Source: MGI
- microtubule binding Source: MGI
- protein kinase 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
- microtubule cytoskeleton organization Source: ARUK-UCL
- negative regulation of axon extension Source: ARUK-UCL
- negative regulation of microtubule binding Source: MGI
- negative regulation of microtubule depolymerization Source: MGI
- negative regulation of microtubule motor activity Source: MGI
- negative regulation of microtubule polymerization Source: MGI
- neuron projection development Source: GO_Central
- positive regulation of anterograde dense core granule transport Source: MGI
- positive regulation of anterograde synaptic vesicle transport Source: MGI
- regulation of cellular protein localization Source: ARUK-UCL
- regulation of organelle transport along microtubule Source: MGI
Keywordsi
Molecular function | Calmodulin-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Microtubule-associated protein 2Short name: MAP-2 |
Gene namesi | Name:Map2 Synonyms:Mtap2 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:97175, Map2 |
Subcellular locationi
Cytoskeleton
- cytoskeleton Curated
Other locations
- dendrite 1 Publication
Cytoskeleton
- actin cytoskeleton Source: MGI
- microtubule Source: UniProtKB-KW
- microtubule associated complex Source: MGI
- microtubule cytoskeleton Source: MGI
Endoplasmic reticulum
- rough endoplasmic reticulum Source: MGI
- smooth endoplasmic reticulum Source: MGI
Nucleus
- nuclear periphery Source: MGI
Plasma Membrane
- ruffle membrane Source: MGI
Other locations
- apical dendrite Source: MGI
- apical distal dendrite Source: MGI
- axon Source: MGI
- axon hillock Source: ARUK-UCL
- axon initial segment Source: ARUK-UCL
- basal dendrite Source: MGI
- CA3 pyramidal cell dendrite Source: MGI
- cell body Source: MGI
- cytoplasm Source: MGI
- dendrite Source: UniProtKB
- dendrite cytoplasm Source: MGI
- dendritic branch Source: MGI
- dendritic filopodium Source: MGI
- dendritic growth cone Source: MGI
- dendritic shaft Source: MGI
- distal dendrite Source: MGI
- neuron projection Source: MGI
- neuronal cell body Source: ARUK-UCL
- postsynaptic density Source: MGI
- primary dendrite Source: MGI
- protein-containing complex Source: MGI
- proximal dendrite Source: MGI
- proximal neuron projection Source: ARUK-UCL
Keywords - Cellular componenti
Cell projection, Cytoplasm, Cytoskeleton, MicrotubulePTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000072748 | 1 – 1828 | Microtubule-associated protein 2Add BLAST | 1828 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 28 | PhosphoserineCombined sources | 1 | |
Modified residuei | 136 | PhosphoserineCombined sources | 1 | |
Modified residuei | 140 | PhosphoserineCombined sources | 1 | |
Modified residuei | 143 | PhosphoserineCombined sources | 1 | |
Modified residuei | 283 | PhosphoserineCombined sources | 1 | |
Modified residuei | 333 | PhosphoserineCombined sources | 1 | |
Modified residuei | 346 | PhosphoserineBy similarity | 1 | |
Modified residuei | 476 | PhosphoserineCombined sources | 1 | |
Modified residuei | 496 | PhosphoserineCombined sources | 1 | |
Modified residuei | 520 | PhosphoserineBy similarity | 1 | |
Modified residuei | 550 | PhosphoserineCombined sources | 1 | |
Modified residuei | 596 | PhosphoserineCombined sources | 1 | |
Modified residuei | 599 | PhosphoserineCombined sources | 1 | |
Modified residuei | 603 | PhosphoserineCombined sources | 1 | |
Modified residuei | 608 | PhosphoserineCombined sources | 1 | |
Modified residuei | 626 | PhosphoserineBy similarity | 1 | |
Modified residuei | 726 | PhosphoserineCombined sources | 1 | |
Modified residuei | 730 | PhosphoserineCombined sources | 1 | |
Modified residuei | 734 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 737 | PhosphoserineCombined sources | 1 | |
Modified residuei | 739 | PhosphoserineCombined sources | 1 | |
Modified residuei | 746 | PhosphotyrosineCombined sources | 1 | |
Modified residuei | 823 | PhosphoserineCombined sources | 1 | |
Modified residuei | 883 | PhosphoserineBy similarity | 1 | |
Modified residuei | 892 | PhosphoserineBy similarity | 1 | |
Modified residuei | 938 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1050 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1139 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1140 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1145 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1160 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 1161 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1165 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1352 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1358 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1539 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1560 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1592 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1606 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1609 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1620 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1623 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1650 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 1654 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1680 | Phosphoserine; by MARK1By similarity | 1 | |
Modified residuei | 1783 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1788 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1791 | PhosphoserineCombined sources | 1 | |
Modified residuei | 1796 | PhosphoserineBy similarity | 1 | |
Modified residuei | 1809 | PhosphoserineBy similarity | 1 |
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). The interaction with KNDC1 enhances MAP2 threonine phosphorylation (PubMed:17984326).By similarity1 Publication
Keywords - PTMi
PhosphoproteinProteomic databases
jPOSTi | P20357 |
MaxQBi | P20357 |
PaxDbi | P20357 |
PeptideAtlasi | P20357 |
PRIDEi | P20357 |
ProteomicsDBi | 291359 |
PTM databases
iPTMneti | P20357 |
PhosphoSitePlusi | P20357 |
SwissPalmi | P20357 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000015222, Expressed in olfactory bulb and 253 other tissues |
Genevisiblei | P20357, MM |
Interactioni
Subunit structurei
Interacts with KNDC1 (via KIND2); the interaction enhances MAP2 phosphorylation and localizes KNDC1 to dendrites.
1 PublicationBinary interactionsi
P20357
With | #Exp. | IntAct |
---|---|---|
Kndc1 [Q0KK55] | 9 | EBI-397863,EBI-8605532 |
GO - Molecular functioni
- actin binding Source: MGI
- calmodulin binding Source: UniProtKB-KW
- cytoskeletal regulatory protein binding Source: MGI
- dystroglycan binding Source: MGI
- microtubule binding Source: MGI
- protein kinase binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 201585, 27 interactors |
IntActi | P20357, 20 interactors |
MINTi | P20357 |
STRINGi | 10090.ENSMUSP00000076577 |
Miscellaneous databases
RNActi | P20357, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 1662 – 1692 | Tau/MAP 1Add BLAST | 31 | |
Repeati | 1693 – 1723 | Tau/MAP 2Add BLAST | 31 | |
Repeati | 1724 – 1755 | Tau/MAP 3Add BLAST | 32 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 702 – 745 | Interaction with KNDC11 PublicationAdd BLAST | 44 | |
Regioni | 1452 – 1472 | Calmodulin-bindingSequence analysisAdd BLAST | 21 |
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG2418, Eukaryota |
GeneTreei | ENSGT00940000156597 |
HOGENOMi | CLU_002538_0_0_1 |
InParanoidi | P20357 |
OMAi | FIEMPME |
OrthoDBi | 716848at2759 |
Family and domain databases
InterProi | View protein in InterPro IPR030797, MAP2 IPR013588, MAP2_projctn IPR001084, MAP_tubulin-bd_rpt |
PANTHERi | PTHR11501:SF15, PTHR11501:SF15, 1 hit |
Pfami | View protein in Pfam PF08377, MAP2_projctn, 1 hit PF00418, Tubulin-binding, 3 hits |
PROSITEi | View protein in PROSITE PS00229, TAU_MAP_1, 2 hits PS51491, TAU_MAP_2, 3 hits |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 13 potential isoforms that are computationally mapped.Show allAlign All
P20357-1 [UniParc]FASTAAdd to basket
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
Computationally mapped potential isoform sequencesi
There are 13 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketQ80ZL4 | Q80ZL4_MOUSE | Microtubule-associated protein | Map2 Mtap2 | 467 | Annotation score: | ||
Q3TLQ0 | Q3TLQ0_MOUSE | Microtubule-associated protein | Map2 Mtap2 | 498 | Annotation score: | ||
G3UWW1 | G3UWW1_MOUSE | Microtubule-associated protein | Map2 Mtap2 | 336 | Annotation score: | ||
G3UZJ2 | G3UZJ2_MOUSE | Microtubule-associated protein | Map2 Mtap2 | 240 | Annotation score: | ||
G3UZV6 | G3UZV6_MOUSE | Microtubule-associated protein | Map2 Mtap2 | 381 | Annotation score: | ||
Q80X35 | Q80X35_MOUSE | Microtubule-associated protein | Map2 Mtap2 | 466 | Annotation score: | ||
A0A668KLC6 | A0A668KLC6_MOUSE | Microtubule-associated protein | Map2 | 1,989 | Annotation score: | ||
G3UZE9 | G3UZE9_MOUSE | Microtubule-associated protein 2 | Map2 Mtap2 | 565 | Annotation score: | ||
G3UZK9 | G3UZK9_MOUSE | Microtubule-associated protein 2 | Map2 Mtap2 | 608 | Annotation score: | ||
F7ALC8 | F7ALC8_MOUSE | Microtubule-associated protein 2 | Map2 Mtap2 | 262 | Annotation score: | ||
There are more potential isoformsShow all |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 116 | H → Y no nucleotide entry (PubMed:3205744).Curated | 1 | |
Sequence conflicti | 116 | H → Y in AAA39490 (PubMed:3142041).Curated | 1 | |
Sequence conflicti | 455 | K → E no nucleotide entry (PubMed:3205744).Curated | 1 | |
Sequence conflicti | 455 | K → E in AAA39490 (PubMed:3142041).Curated | 1 | |
Sequence conflicti | 459 | F → L no nucleotide entry (PubMed:3205744).Curated | 1 | |
Sequence conflicti | 459 | F → L in AAA39490 (PubMed:3142041).Curated | 1 | |
Sequence conflicti | 644 | D → G no nucleotide entry (PubMed:3205744).Curated | 1 | |
Sequence conflicti | 644 | D → G in AAA39490 (PubMed:3142041).Curated | 1 | |
Sequence conflicti | 938 | S → T no nucleotide entry (PubMed:3205744).Curated | 1 | |
Sequence conflicti | 938 | S → T in AAA39490 (PubMed:3142041).Curated | 1 | |
Sequence conflicti | 947 | R → G no nucleotide entry (PubMed:3205744).Curated | 1 | |
Sequence conflicti | 947 | R → G in AAA39490 (PubMed:3142041).Curated | 1 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M21041 mRNA Translation: AAA39490.1 AC091465 Genomic DNA No translation available. |
CCDSi | CCDS83550.1 |
PIRi | A40115 |
RefSeqi | NP_001297563.1, NM_001310634.1 XP_006495817.1, XM_006495754.2 |
Genome annotation databases
Ensembli | ENSMUST00000114013; ENSMUSP00000109646; ENSMUSG00000015222 |
GeneIDi | 17756 |
KEGGi | mmu:17756 |
UCSCi | uc007bhz.1, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M21041 mRNA Translation: AAA39490.1 AC091465 Genomic DNA No translation available. |
CCDSi | CCDS83550.1 |
PIRi | A40115 |
RefSeqi | NP_001297563.1, NM_001310634.1 XP_006495817.1, XM_006495754.2 |
3D structure databases
SMRi | P20357 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 201585, 27 interactors |
IntActi | P20357, 20 interactors |
MINTi | P20357 |
STRINGi | 10090.ENSMUSP00000076577 |
PTM databases
iPTMneti | P20357 |
PhosphoSitePlusi | P20357 |
SwissPalmi | P20357 |
Proteomic databases
jPOSTi | P20357 |
MaxQBi | P20357 |
PaxDbi | P20357 |
PeptideAtlasi | P20357 |
PRIDEi | P20357 |
ProteomicsDBi | 291359 |
Protocols and materials databases
ABCDi | P20357, 2 sequenced antibodies |
Antibodypediai | 2169, 1322 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000114013; ENSMUSP00000109646; ENSMUSG00000015222 |
GeneIDi | 17756 |
KEGGi | mmu:17756 |
UCSCi | uc007bhz.1, mouse |
Organism-specific databases
CTDi | 4133 |
MGIi | MGI:97175, Map2 |
Phylogenomic databases
eggNOGi | KOG2418, Eukaryota |
GeneTreei | ENSGT00940000156597 |
HOGENOMi | CLU_002538_0_0_1 |
InParanoidi | P20357 |
OMAi | FIEMPME |
OrthoDBi | 716848at2759 |
Miscellaneous databases
BioGRID-ORCSi | 17756, 0 hits in 53 CRISPR screens |
ChiTaRSi | Map2, mouse |
PROi | PR:P20357 |
RNActi | P20357, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000015222, Expressed in olfactory bulb and 253 other tissues |
Genevisiblei | P20357, MM |
Family and domain databases
InterProi | View protein in InterPro IPR030797, MAP2 IPR013588, MAP2_projctn IPR001084, MAP_tubulin-bd_rpt |
PANTHERi | PTHR11501:SF15, PTHR11501:SF15, 1 hit |
Pfami | View protein in Pfam PF08377, MAP2_projctn, 1 hit PF00418, Tubulin-binding, 3 hits |
PROSITEi | View protein in PROSITE PS00229, TAU_MAP_1, 2 hits PS51491, TAU_MAP_2, 3 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MTAP2_MOUSE | |
Accessioni | P20357Primary (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: | April 7, 2021 | |
This is version 177 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot