UniProtKB - P15146 (MTAP2_RAT)
Protein
Microtubule-associated protein 2
Gene
Map2
Organism
Rattus norvegicus (Rat)
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: CAFA
- calmodulin binding Source: UniProtKB-KW
- dystroglycan binding Source: RGD
- microtubule binding Source: CAFA
- protein kinase binding Source: ARUK-UCL
GO - Biological processi
- axonogenesis Source: RGD
- cellular response to organic substance Source: RGD
- central nervous system neuron development Source: RGD
- dendrite development Source: RGD
- dendrite morphogenesis Source: RGD
- establishment of cell polarity Source: RGD
- microtubule bundle formation Source: RGD
- microtubule cytoskeleton organization Source: RGD
- negative regulation of axon extension Source: ARUK-UCL
- negative regulation of microtubule binding Source: ARUK-UCL
- negative regulation of microtubule depolymerization Source: CAFA
- negative regulation of microtubule motor activity Source: ARUK-UCL
- negative regulation of microtubule polymerization Source: ARUK-UCL
- neuron projection development Source: RGD
- positive regulation of anterograde dense core granule transport Source: ARUK-UCL
- positive regulation of anterograde synaptic vesicle transport Source: ARUK-UCL
- regulation of cellular protein localization Source: ARUK-UCL
- regulation of organelle transport along microtubule Source: ARUK-UCL
- response to estradiol Source: RGD
- response to progesterone Source: RGD
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 | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 3044, Map2 |
Subcellular locationi
Cytoskeleton
- cytoskeleton Curated
Other locations
- dendrite By similarity
Cytoskeleton
- actin cytoskeleton Source: CAFA
- microtubule Source: UniProtKB-KW
- microtubule cytoskeleton Source: CAFA
Endoplasmic reticulum
- rough endoplasmic reticulum Source: RGD
- smooth endoplasmic reticulum Source: RGD
Nucleus
- nuclear periphery Source: RGD
Plasma Membrane
- ruffle membrane Source: CAFA
Other locations
- apical distal dendrite Source: ARUK-UCL
- axon Source: RGD
- axon hillock Source: ARUK-UCL
- axon initial segment Source: ARUK-UCL
- basal dendrite Source: ARUK-UCL
- CA3 pyramidal cell dendrite Source: RGD
- cell body Source: RGD
- cytoplasm Source: ARUK-UCL
- dendrite Source: UniProtKB
- dendrite cytoplasm Source: ARUK-UCL
- dendritic branch Source: ARUK-UCL
- dendritic filopodium Source: ARUK-UCL
- dendritic growth cone Source: ARUK-UCL
- dendritic shaft Source: ARUK-UCL
- distal dendrite Source: ARUK-UCL
- neuron projection Source: RGD
- neuronal cell body Source: ARUK-UCL
- postsynaptic density Source: RGD
- primary dendrite Source: ARUK-UCL
- protein-containing complex Source: RGD
- proximal dendrite Source: ARUK-UCL
- 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_0000072749 | 1 – 1861 | Microtubule-associated protein 2Add BLAST | 1861 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length | |
---|---|---|---|---|---|
Modified residuei | 28 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 37 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 136 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 140 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 143 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 221 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 224 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 285 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 348 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 478 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 498 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 522 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 552 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 598 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 605 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 610 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 628 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 728 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 732 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 736 | PhosphothreonineBy similarity | 1 | ||
Modified residuei | 739 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 741 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 748 | PhosphotyrosineBy similarity | 1 | ||
Modified residuei | 825 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 884 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 893 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 939 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1051 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1140 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1141 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1146 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 1161 | PhosphothreonineCombined sources | 1 | ||
Modified residuei | 1162 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1166 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 1353 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1359 | PhosphothreonineCombined sources | 1 | ||
Modified residuei | 1541 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1562 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 1594 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 1608 | PhosphothreonineBy similarity | 1 | ||
Modified residuei | 1611 | PhosphothreonineCombined sources | 1 | ||
Modified residuei | 1622 | PhosphothreonineCombined sources | 1 | ||
Modified residuei | 1625 | PhosphothreonineCombined sources | 1 | ||
Modified residuei | 1652 | PhosphothreonineCombined sources | 1 | ||
Modified residuei | 1656 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1682 | Phosphoserine; by MARK11 Publication | 1 | ||
Modified residuei | 1816 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1821 | PhosphoserineBy similarity | 1 | ||
Modified residuei | 1824 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1829 | PhosphoserineCombined sources | 1 | ||
Modified residuei | 1842 | PhosphoserineCombined sources | 1 | ||
Isoform 3 (identifier: P15146-3) | |||||
Modified residuei | 319 | Phosphoserine1 Publication | 1 | ||
Modified residuei | 350 | Phosphoserine1 Publication | 1 | ||
Modified residuei | 382 | Phosphoserine1 Publication | 1 |
Post-translational modificationi
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 3/MAP2c is probably phosphorylated by PKA at Ser-319, Ser-350 and Ser-382 and by FYN at Tyr-67. The interaction with KNDC1 enhances MAP2 threonine phosphorylation (By similarity).By similarity2 Publications
Keywords - PTMi
PhosphoproteinProteomic databases
PaxDbi | P15146 |
PRIDEi | P15146 |
PTM databases
iPTMneti | P15146 |
PhosphoSitePlusi | P15146 |
SwissPalmi | P15146 |
Expressioni
Developmental stagei
Isoform 3/MAP2c is expressed during embryonic brain development and until postanatal day 10. Isoform 2 is expressed throughout brain development.
Interactioni
Subunit structurei
Interacts with KNDC1 (via KIND2); the interaction enhances MAP2 phosphorylation and localizes KNDC1 to dendrites.
By similarityGO - Molecular functioni
- actin binding Source: CAFA
- calmodulin binding Source: UniProtKB-KW
- dystroglycan binding Source: RGD
- microtubule binding Source: CAFA
- protein kinase binding Source: ARUK-UCL
Protein-protein interaction databases
BioGRIDi | 247625, 7 interactors |
IntActi | P15146, 4 interactors |
MINTi | P15146 |
STRINGi | 10116.ENSRNOP00000050877 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Repeati | 1664 – 1694 | Tau/MAP 1Add BLAST | 31 | |
Repeati | 1695 – 1725 | Tau/MAP 2Add BLAST | 31 | |
Repeati | 1726 – 1756 | Tau/MAP 3Add BLAST | 31 | |
Repeati | 1757 – 1788 | Tau/MAP 4Add BLAST | 32 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 704 – 747 | Interaction with KNDC1By similarityAdd BLAST | 44 | |
Regioni | 1454 – 1474 | Calmodulin-bindingSequence analysisAdd BLAST | 21 |
Keywords - Domaini
RepeatPhylogenomic databases
eggNOGi | KOG2418, Eukaryota |
InParanoidi | P15146 |
PhylomeDBi | P15146 |
Family and domain databases
DisProti | DP00122 |
InterProi | View protein in InterPro IPR030797, MAP2 IPR027324, MAP2/MAP4/Tau IPR013588, MAP2_projctn IPR001084, MAP_tubulin-bd_rpt |
PANTHERi | PTHR11501, PTHR11501, 2 hits PTHR11501:SF15, PTHR11501:SF15, 2 hits |
Pfami | View protein in Pfam PF08377, MAP2_projctn, 1 hit PF00418, Tubulin-binding, 4 hits |
PROSITEi | View protein in PROSITE PS00229, TAU_MAP_1, 3 hits PS51491, TAU_MAP_2, 4 hits |
s (4+)i Sequence
Sequence statusi: Complete.
This entry describes 4 produced by isoformsialternative splicing. AlignAdd to basketNote: Additional isoforms seem to exist.
This entry has 4 described isoforms and 7 potential isoforms that are computationally mapped.Show allAlign All
Isoform 1 (identifier: P15146-1) [UniParc]FASTAAdd to basket
Also known as: MAP2x
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MADERKDEGK APHWTSASLT EAAAHPHSPE MKDQGGSGEG LSRSANGFPY
60 70 80 90 100
REEEEGAFGE HGSQGTYSDT KENGINGELT SADRETAEEV SARIVQVVTA
110 120 130 140 150
EAVAVLKGEQ EKEAQHKDQP AALPLAAEET VNLPPSPPPS PASEQTAALE
160 170 180 190 200
EDLLTASKME FPEQQKLPSS FAEPLDKEET EFKMQSKPGE DFEHAALVPQ
210 220 230 240 250
PDTSKTPQDK KDPQDMEGEK SPASPFAQTF GTNLEDIKQI TEPSITVPSI
260 270 280 290 300
GLSAEPLAPK DQKDWFIEMP VESKKDEWGL AAPISPGPLT PMREKDVLED
310 320 330 340 350
IPRWEGKQFD SPMPSPFHGG SFTLPLDTVK DERVTEGSQP FAPVFFQSDD
360 370 380 390 400
KMSLQDTSGS ATSKESSKDE EPQKDKADKV ADVPVSEATT VLGDVHSPAV
410 420 430 440 450
EGFVGENISG EEKGTTDQEK KETSTPSVQE PTLTETEPQT KLEETSKVSI
460 470 480 490 500
EETVAKEEES LKLKDDKAGV IQTSTEQSFS KEDQKGQEQT IEALKQDSFP
510 520 530 540 550
ISLEQAVTDA AMATKTLEKV TSEPEAVSEK REIQGLFEED IADKSKLEGA
560 570 580 590 600
GSATVAEVEM PFYEDKSGMS KYFETSALKE DVTRSTGLGS DYYELSDSRG
610 620 630 640 650
NAQESLDTVS PKNQQDEKEL LAKASQPSPP AHEAGYSTLA QSYTSDHPSE
660 670 680 690 700
LPEEPSSPQE RMFTIDPKVY GEKRDLHSKN KDDLTLSRSL GLGGRSAIEQ
710 720 730 740 750
RSMSINLPMS CLDSIALGFN FGRGHDLSPL ASDILTNTSG SMDEGDDYLP
760 770 780 790 800
PTTPAVEKIP CFPIESKEEE DKTEQAKVTG GQTTQVETSS ESPFPAKEYY
810 820 830 840 850
KNGTVMAPDL PEMLDLAGTR SRLASVSADA EVARRKSVPS EAVVAESSTG
860 870 880 890 900
LPPVADDSQP VKPDSQLEDM GYCVFNKYTV PLPSPVQDSE NLSGESGSFY
910 920 930 940 950
EGTDDKVRRD LATDLSLIEV KLAAAGRVKD EFTAEKEASP PSSADKSGLS
960 970 980 990 1000
REFDQDRKAN DKLDTVLEKS EEHVDSKEHA KESEEVGDKV ELFGLGVTYE
1010 1020 1030 1040 1050
QTSAKELITT KETAPERAEK GLSSVPEVAE VETTTKADQG LDVAAKKDDQ
1060 1070 1080 1090 1100
SPLDIKVSDF GQMASGMSVD AGKTIELKFE VDQQLTLSSE APQETDSFMG
1110 1120 1130 1140 1150
IESSHVKDGA KVSETEVKEK VAKPDLVHQE AVDKEESYES SGEHESLTME
1160 1170 1180 1190 1200
SLKPDEGKKE TSPETSLIQD EVALKLSVEI PCPPPVSEAD SSIDEKAEVQ
1210 1220 1230 1240 1250
MEFIQLPKEE STETPDIPAI PSDVTQPQPE AVVSEPAEVR GEEEEIEAEG
1260 1270 1280 1290 1300
EYDKLLFRSD TLQITDLLVP GSREEFVETC PGEHKGVVES VVTIEDDFIT
1310 1320 1330 1340 1350
VVQTTTDEGE LGSHSVRFAA PVQPEEERRP YPHDEELEVL MAAEAQAEPK
1360 1370 1380 1390 1400
DGSPDAPATP EKEEVPFSEY KTETYDDYKD ETTIDDSIMD ADSLWVDTQD
1410 1420 1430 1440 1450
DDRSILTEQL ETIPKEERAE KEARRPSLEK HRKEKPFKTG RGRISTPERR
1460 1470 1480 1490 1500
EVAKKEPSTV SRDEVRRKKA VYKKAELAKE SEVQAHSPSR KLILKPAIKY
1510 1520 1530 1540 1550
TRPTHLSCVK RKTTATSGES AQAPSAFKQA KDKVTDGITK SPEKRSSLPR
1560 1570 1580 1590 1600
PSSILPPRRG VSGDREENSF SLNSSISSAR RTTRSEPIRR AGKSGTSTPT
1610 1620 1630 1640 1650
TPGSTAITPG TPPSYSSRTP GTPGTPSYPR TPGTPKSGIL VPSEKKVAII
1660 1670 1680 1690 1700
RTPPKSPATP KQLRLINQPL PDLKNVKSKI GSTDNIKYQP KGGQVRILNK
1710 1720 1730 1740 1750
KMDFSKVQSR CGSKDNIKHS AGGGNVQIVT KKIDLSHVTS KCGSLKNIRH
1760 1770 1780 1790 1800
RPGGGRVKIE SVKLDFKEKA QAKVGSLDNA HHVPGGGNVK IDSQKLNFRE
1810 1820 1830 1840 1850
HAKARVDHGA EIITQSPSRS SVASPRRLSN VSSSGSINLL ESPQLATLAE
1860
DVTAALAKQG L
Computationally mapped potential isoform sequencesi
There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF1MAQ5 | F1MAQ5_RAT | Microtubule-associated protein | Map2 Mtap2, rCG_24983 | 1,825 | Annotation score: | ||
Q78DZ1 | Q78DZ1_RAT | Microtubule-associated protein | Map2 MAP2, Mtap2, rCG_24983 | 498 | Annotation score: | ||
F1LNK0 | F1LNK0_RAT | Microtubule-associated protein | Map2 | 1,942 | Annotation score: | ||
A0A0U1RRX4 | A0A0U1RRX4_RAT | Microtubule-associated protein | Map2 | 1,829 | Annotation score: | ||
A0A0U1RRQ0 | A0A0U1RRQ0_RAT | Microtubule-associated protein | Map2 | 336 | Annotation score: | ||
A0A0U1RS27 | A0A0U1RS27_RAT | Microtubule-associated protein 2 | Map2 | 143 | Annotation score: | ||
A0A0U1RS09 | A0A0U1RS09_RAT | Microtubule-associated protein 2 | Map2 | 89 | Annotation score: |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_003198 | 152 – 1514 | Missing in isoform 3 and isoform 4. 1 PublicationAdd BLAST | 1363 | |
Alternative sequenceiVSP_003199 | 1695 – 1725 | Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST | 31 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X51842 mRNA Translation: CAA36135.1 X17682 mRNA Translation: CAA35667.1 X71487 mRNA Translation: CAA50588.1 |
PIRi | A37981 I55502, S33176 |
RefSeqi | XP_008765430.1, XM_008767208.2 [P15146-3] |
Genome annotation databases
GeneIDi | 25595 |
UCSCi | RGD:3044, rat [P15146-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X51842 mRNA Translation: CAA36135.1 X17682 mRNA Translation: CAA35667.1 X71487 mRNA Translation: CAA50588.1 |
PIRi | A37981 I55502, S33176 |
RefSeqi | XP_008765430.1, XM_008767208.2 [P15146-3] |
3D structure databases
SASBDBi | P15146 |
SMRi | P15146 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 247625, 7 interactors |
IntActi | P15146, 4 interactors |
MINTi | P15146 |
STRINGi | 10116.ENSRNOP00000050877 |
PTM databases
iPTMneti | P15146 |
PhosphoSitePlusi | P15146 |
SwissPalmi | P15146 |
Proteomic databases
PaxDbi | P15146 |
PRIDEi | P15146 |
Genome annotation databases
GeneIDi | 25595 |
UCSCi | RGD:3044, rat [P15146-1] |
Organism-specific databases
CTDi | 4133 |
RGDi | 3044, Map2 |
Phylogenomic databases
eggNOGi | KOG2418, Eukaryota |
InParanoidi | P15146 |
PhylomeDBi | P15146 |
Miscellaneous databases
PROi | PR:P15146 |
Family and domain databases
DisProti | DP00122 |
InterProi | View protein in InterPro IPR030797, MAP2 IPR027324, MAP2/MAP4/Tau IPR013588, MAP2_projctn IPR001084, MAP_tubulin-bd_rpt |
PANTHERi | PTHR11501, PTHR11501, 2 hits PTHR11501:SF15, PTHR11501:SF15, 2 hits |
Pfami | View protein in Pfam PF08377, MAP2_projctn, 1 hit PF00418, Tubulin-binding, 4 hits |
PROSITEi | View protein in PROSITE PS00229, TAU_MAP_1, 3 hits PS51491, TAU_MAP_2, 4 hits |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | MTAP2_RAT | |
Accessioni | P15146Primary (citable) accession number: P15146 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 1, 1990 |
Last sequence update: | June 1, 1994 | |
Last modified: | December 2, 2020 | |
This is version 174 of the entry and version 3 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |