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Protein

Microtubule-associated protein 2

Gene

MAP2

Organism
Homo sapiens (Human)
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

  • dystroglycan binding Source: UniProtKB
  • microtubule binding Source: GO_Central
  • structural molecule activity Source: ProtInc

GO - Biological processi

  • central nervous system neuron development Source: DFLAT
  • dendrite morphogenesis Source: DFLAT
  • microtubule bundle formation Source: InterPro
  • microtubule cytoskeleton organization Source: GO_Central
  • neuron projection development Source: DFLAT
Complete GO annotation...

Keywords - Ligandi

Calmodulin-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000078018-MONOMER.
SIGNORiP11137.

Names & Taxonomyi

Protein namesi
Recommended name:
Microtubule-associated protein 2
Short name:
MAP-2
Gene namesi
Name:MAP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:6839. MAP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • microtubule Source: UniProtKB-KW
  • microtubule associated complex Source: ProtInc
  • neuron projection Source: GO_Central
  • nucleolus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Microtubule

Pathology & Biotechi

Organism-specific databases

DisGeNETi4133.
OpenTargetsiENSG00000078018.
PharmGKBiPA30583.

Chemistry databases

ChEMBLiCHEMBL2390810.
DrugBankiDB01248. Docetaxel.
DB01196. Estramustine.
DB01229. Paclitaxel.

Polymorphism and mutation databases

BioMutaiMAP2.
DMDMi215274255.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000727471 – 1827Microtubule-associated protein 2Add BLAST1827

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei136PhosphoserineBy similarity1
Modified residuei140PhosphoserineBy similarity1
Modified residuei143PhosphoserineBy similarity1
Modified residuei285PhosphoserineBy similarity1
Modified residuei498PhosphoserineBy similarity1
Modified residuei601PhosphoserineBy similarity1
Modified residuei605PhosphoserineBy similarity1
Modified residuei610PhosphoserineBy similarity1
Modified residuei629PhosphoserineBy similarity1
Modified residuei725PhosphoserineBy similarity1
Modified residuei729PhosphoserineBy similarity1
Modified residuei733PhosphothreonineBy similarity1
Modified residuei736PhosphoserineBy similarity1
Modified residuei738PhosphoserineBy similarity1
Modified residuei745PhosphotyrosineBy similarity1
Modified residuei821PhosphoserineBy similarity1
Modified residuei881PhosphoserineBy similarity1
Modified residuei890PhosphoserineBy similarity1
Modified residuei936PhosphoserineBy similarity1
Modified residuei1133PhosphoserineBy similarity1
Modified residuei1134PhosphoserineBy similarity1
Modified residuei1139PhosphoserineBy similarity1
Modified residuei1154PhosphothreonineBy similarity1
Modified residuei1155PhosphoserineBy similarity1
Modified residuei1159PhosphoserineBy similarity1
Modified residuei1347PhosphoserineCombined sources1
Modified residuei1353PhosphoserineCombined sources1
Modified residuei1534PhosphoserineBy similarity1
Modified residuei1555PhosphoserineBy similarity1
Modified residuei1588PhosphoserineBy similarity1
Modified residuei1602PhosphothreonineBy similarity1
Modified residuei1605PhosphothreonineBy similarity1
Modified residuei1616PhosphothreonineBy similarity1
Modified residuei1619PhosphothreonineBy similarity1
Modified residuei1649PhosphothreonineBy similarity1
Modified residuei1653PhosphoserineBy similarity1
Modified residuei1679Phosphoserine; by MARK1By similarity1
Modified residuei1782PhosphoserineCombined sources1
Modified residuei1787PhosphoserineBy similarity1
Modified residuei1790PhosphoserineBy similarity1
Modified residuei1795PhosphoserineBy similarity1
Modified residuei1808PhosphoserineBy similarity1
Isoform 2 (identifier: P11137-2)
Modified residuei67PhosphotyrosineBy similarity1
Modified residuei323PhosphoserineBy similarity1
Modified residuei354PhosphoserineBy similarity1
Modified residuei386PhosphoserineBy similarity1

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 (By similarity). Isoform 2 is probably phosphorylated by PKA at Ser-323, Ser-354 and Ser-386 and by FYN at Tyr-67.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiP11137.
MaxQBiP11137.
PaxDbiP11137.
PeptideAtlasiP11137.
PRIDEiP11137.

PTM databases

iPTMnetiP11137.
PhosphoSitePlusiP11137.

Expressioni

Gene expression databases

BgeeiENSG00000078018.
CleanExiHS_MAP2.
ExpressionAtlasiP11137. baseline and differential.
GenevisibleiP11137. HS.

Organism-specific databases

HPAiCAB001984.
HPA008273.
HPA012828.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CBFBQ139512EBI-2682460,EBI-718750

GO - Molecular functioni

  • dystroglycan binding Source: UniProtKB
  • microtubule binding Source: GO_Central

Protein-protein interaction databases

BioGridi110305. 42 interactors.
DIPiDIP-577N.
IntActiP11137. 9 interactors.
MINTiMINT-1210186.
STRINGi9606.ENSP00000353508.

Chemistry databases

BindingDBiP11137.

Structurei

3D structure databases

ProteinModelPortaliP11137.
SMRiP11137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1661 – 1691Tau/MAP 1Add BLAST31
Repeati1692 – 1722Tau/MAP 2Add BLAST31
Repeati1723 – 1754Tau/MAP 3Add BLAST32

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1447 – 1467Calmodulin-bindingSequence analysisAdd BLAST21

Sequence similaritiesi

Contains 3 Tau/MAP repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG2418. Eukaryota.
ENOG4111J07. LUCA.
GeneTreeiENSGT00530000063491.
HOGENOMiHOG000113477.
HOVERGENiHBG000991.
InParanoidiP11137.
KOiK10430.
OMAiPFKTGRG.
OrthoDBiEOG091G00IT.
PhylomeDBiP11137.
TreeFamiTF316358.

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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P11137-1) [UniParc]FASTAAdd to basket
Also known as: MAP2b

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.

« Hide

        10         20         30         40         50
MADERKDEAK APHWTSAPLT EASAHSHPPE IKDQGGAGEG LVRSANGFPY
60 70 80 90 100
REDEEGAFGE HGSQGTYSNT KENGINGELT SADRETAEEV SARIVQVVTA
110 120 130 140 150
EAVAVLKGEQ EKEAQHKDQT AALPLAAEET ANLPPSPPPS PASEQTVTVE
160 170 180 190 200
EDLLTASKME FHDQQELTPS TAEPSDQKEK ESEKQSKPGE DLKHAALVSQ
210 220 230 240 250
PETTKTYPDK KDMQGTEEEK APLALFGHTL VASLEDMKQK TEPSLVVPGI
260 270 280 290 300
DLPKEPPTPK EQKDWFIEMP TEAKKDEWGL VAPISPGPLT PMREKDVFDD
310 320 330 340 350
IPKWEGKQFD SPMPSPFQGG SFTLPLDVMK NEIVTETSPF APAFLQPDDK
360 370 380 390 400
KSLQQTSGPA TAKDSFKIEE PHEAKPDKMA EAPPSEAMTL PKDAHIPVVE
410 420 430 440 450
EHVMGKVLEE EKEAINQETV QQRDTFTPSG QEPILTEKET ELKLEEKTTI
460 470 480 490 500
SDKEAVPKES KPPKPADEEI GIIQTSTEHT FSEQKDQEPT TDMLKQDSFP
510 520 530 540 550
VSLEQAVTDS AMTSKTLEKA MTEPSALIEK SSIQELFEMR VDDKDKIEGV
560 570 580 590 600
GAATSAELDM PFYEDKSGMS KYFETSALKE EATKSIEPGS DYYELSDTRE
610 620 630 640 650
SVHESIDTMS PMHKNGDKEF QTGKESQPSP PAQEAGYSTL AQSYPSDLPE
660 670 680 690 700
EPSSPQERMF TIDPKVYGEK RDLHSKNKDD LTLSRSLGLG GRSAIEQRSM
710 720 730 740 750
SINLPMSCLD SIALGFNFGR GHDLSPLASD ILTNTSGSMD EGDDYLPATT
760 770 780 790 800
PALEKAPCFP VESKEEEQIE KVKATGEEST QAEISCESPF LAKDFYKNGT
810 820 830 840 850
VMAPDLPEML DLAGTRSRLA SVSADAEVAR RKSVPSETVV EDSRTGLPPV
860 870 880 890 900
TDENHVIVKT DSQLEDLGYC VFNKYTVPLP SPVQDSENLS GESGTFYEGT
910 920 930 940 950
DDKVRRDLAT DLSLIEVKLA AAGRVKDEFS VDKEASAHIS GDKSGLSKEF
960 970 980 990 1000
DQEKKANDRL DTVLEKSEEH ADSKEHAKKT EEAGDEIETF GLGVTYEQAL
1010 1020 1030 1040 1050
AKDLSIPTDA SSEKAEKGLS SVPEIAEVEP SKKVEQGLDF AVQGQLDVKI
1060 1070 1080 1090 1100
SDFGQMASGL NIDDRRATEL KLEATQDMTP SSKAPQEADA FMGVESGHMK
1110 1120 1130 1140 1150
EGTKVSETEV KEKVAKPDLV HQEAVDKEES YESSGEHESL TMESLKADEG
1160 1170 1180 1190 1200
KKETSPESSL IQDEIAVKLS VEIPCPPAVS EADLATDERA DVQMEFIQGP
1210 1220 1230 1240 1250
KEESKETPDI SITPSDVAEP LHETIVSEPA EIQSEEEEIE AQGEYDKLLF
1260 1270 1280 1290 1300
RSDTLQITDL GVSGAREEFV ETCPSEHKGV IESVVTIEDD FITVVQTTTD
1310 1320 1330 1340 1350
EGESGSHSVR FAALEQPEVE RRPSPHDEEE FEVEEAAEAQ AEPKDGSPEA
1360 1370 1380 1390 1400
PASPEREEVA LSEYKTETYD DYKDETTIDD SIMDADSLWV DTQDDDRSIM
1410 1420 1430 1440 1450
TEQLETIPKE EKAEKEARRS SLEKHRKEKP FKTGRGRIST PERKVAKKEP
1460 1470 1480 1490 1500
STVSRDEVRR KKAVYKKAEL AKKTEVQAHS PSRKFILKPA IKYTRPTHLS
1510 1520 1530 1540 1550
CVKRKTTAAG GESALAPSVF KQAKDKVSDG VTKSPEKRSS LPRPSSILPP
1560 1570 1580 1590 1600
RRGVSGDRDE NSFSLNSSIS SSARRTTRSE PIRRAGKSGT STPTTPGSTA
1610 1620 1630 1640 1650
ITPGTPPSYS SRTPGTPGTP SYPRTPHTPG TPKSAILVPS EKKVAIIRTP
1660 1670 1680 1690 1700
PKSPATPKQL RLINQPLPDL KNVKSKIGST DNIKYQPKGG QVQIVTKKID
1710 1720 1730 1740 1750
LSHVTSKCGS LKNIRHRPGG GRVKIESVKL DFKEKAQAKV GSLDNAHHVP
1760 1770 1780 1790 1800
GGGNVKIDSQ KLNFREHAKA RVDHGAEIIT QSPGRSSVAS PRRLSNVSSS
1810 1820
GSINLLESPQ LATLAEDVTA ALAKQGL
Length:1,827
Mass (Da):199,526
Last modified:November 25, 2008 - v4
Checksum:i2C4801C589086603
GO
Isoform 2 (identifier: P11137-2) [UniParc]FASTAAdd to basket
Also known as: MAP2c

The sequence of this isoform differs from the canonical sequence as follows:
     152-1507: Missing.

Show »
Length:471
Mass (Da):49,640
Checksum:iCE8BB23BCD16A159
GO
Isoform 3 (identifier: P11137-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-155: Missing.

Show »
Length:1,823
Mass (Da):199,084
Checksum:i7E474A0F3B691188
GO
Isoform 4 (identifier: P11137-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-229: DLLTASKMEF...KAPLALFGHT → AAGGESALAP...RLPYSKSGNK
     230-1528: Missing.
     1691-1691: Q → QVRILNKKIDFSKVQSRCGSKDNIKHSAGGGN

Note: No experimental confirmation available.
Show »
Length:559
Mass (Da):58,954
Checksum:i2A4E43681AE8C196
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti9A → G in AAB48098 (PubMed:8294038).Curated1
Sequence conflicti9A → G in AAB48097 (PubMed:8294038).Curated1
Sequence conflicti37A → R in AAA03354 (Ref. 1) Curated1
Sequence conflicti108G → A in AAA03354 (Ref. 1) Curated1
Sequence conflicti187K → S in AAA03354 (Ref. 1) Curated1
Sequence conflicti1112E → Q in AAA03354 (Ref. 1) Curated1
Sequence conflicti1112E → Q in AAB48098 (PubMed:8294038).Curated1
Sequence conflicti1112E → Q in AAA59552 (PubMed:15489334).Curated1
Sequence conflicti1655A → GL in AAB48098 (PubMed:8294038).Curated1
Sequence conflicti1655A → GL in AAB48097 (PubMed:8294038).Curated1
Sequence conflicti1715 – 1716RH → D in AAA03354 (Ref. 1) Curated2
Sequence conflicti1736A → V in AAA03354 (Ref. 1) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01961282A → G.Corresponds to variant rs2271251dbSNPEnsembl.1
Natural variantiVAR_050019179E → G.Corresponds to variant rs6749066dbSNPEnsembl.1
Natural variantiVAR_036014277E → D in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_019613423R → K.Corresponds to variant rs741006dbSNPEnsembl.1
Natural variantiVAR_036015705P → L in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs146432517dbSNPEnsembl.1
Natural variantiVAR_050020976H → L.Corresponds to variant rs13425372dbSNPEnsembl.1
Natural variantiVAR_050021991G → R.Corresponds to variant rs35927101dbSNPEnsembl.1
Natural variantiVAR_0500221099M → V.Corresponds to variant rs17745550dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003197152 – 1507Missing in isoform 2. 2 PublicationsAdd BLAST1356
Alternative sequenceiVSP_043596152 – 229DLLTA…LFGHT → AAGGESALAPSVFKQAKDKV SNSTLSKIPALQGSTKSPRY SSACPSTTKRATFSDSLLIQ PTSAGSTDRLPYSKSGNK in isoform 4. 1 PublicationAdd BLAST78
Alternative sequenceiVSP_011302152 – 155Missing in isoform 3. 1 Publication4
Alternative sequenceiVSP_043597230 – 1528Missing in isoform 4. 1 PublicationAdd BLAST1299
Alternative sequenceiVSP_0435981691Q → QVRILNKKIDFSKVQSRCGS KDNIKHSAGGGN in isoform 4. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01828 mRNA. Translation: AAA03354.1.
U89330 mRNA. Translation: AAB48098.1.
U89329 mRNA. Translation: AAB48097.1.
AC006385 Genomic DNA. No translation available.
AC019106 Genomic DNA. No translation available.
AC079833 Genomic DNA. No translation available.
AC108072 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70459.1.
BC038857 mRNA. Translation: AAH38857.1.
BC110423 mRNA. Translation: AAI10424.1.
BC117123 mRNA. Translation: AAI17124.1.
BC143245 mRNA. Translation: AAI43246.1.
M25668 mRNA. Translation: AAA59552.1.
CCDSiCCDS2384.1. [P11137-1]
CCDS2385.1. [P11137-2]
CCDS33369.1. [P11137-4]
PIRiI53693. QRHUMT.
I67793.
RefSeqiNP_001034627.1. NM_001039538.1. [P11137-4]
NP_002365.3. NM_002374.3. [P11137-1]
NP_114033.2. NM_031845.2. [P11137-2]
NP_114035.2. NM_031847.2.
XP_016859607.1. XM_017004118.1. [P11137-1]
XP_016859612.1. XM_017004123.1. [P11137-3]
XP_016859613.1. XM_017004124.1. [P11137-3]
XP_016859627.1. XM_017004138.1. [P11137-4]
XP_016859628.1. XM_017004139.1. [P11137-4]
XP_016859629.1. XM_017004140.1. [P11137-2]
UniGeneiHs.368281.

Genome annotation databases

EnsembliENST00000199940; ENSP00000199940; ENSG00000078018. [P11137-4]
ENST00000360351; ENSP00000353508; ENSG00000078018. [P11137-1]
ENST00000361559; ENSP00000355290; ENSG00000078018. [P11137-2]
ENST00000392194; ENSP00000376032; ENSG00000078018. [P11137-2]
ENST00000447185; ENSP00000392164; ENSG00000078018. [P11137-3]
GeneIDi4133.
KEGGihsa:4133.
UCSCiuc002vdd.2. human. [P11137-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U01828 mRNA. Translation: AAA03354.1.
U89330 mRNA. Translation: AAB48098.1.
U89329 mRNA. Translation: AAB48097.1.
AC006385 Genomic DNA. No translation available.
AC019106 Genomic DNA. No translation available.
AC079833 Genomic DNA. No translation available.
AC108072 Genomic DNA. No translation available.
CH471063 Genomic DNA. Translation: EAW70459.1.
BC038857 mRNA. Translation: AAH38857.1.
BC110423 mRNA. Translation: AAI10424.1.
BC117123 mRNA. Translation: AAI17124.1.
BC143245 mRNA. Translation: AAI43246.1.
M25668 mRNA. Translation: AAA59552.1.
CCDSiCCDS2384.1. [P11137-1]
CCDS2385.1. [P11137-2]
CCDS33369.1. [P11137-4]
PIRiI53693. QRHUMT.
I67793.
RefSeqiNP_001034627.1. NM_001039538.1. [P11137-4]
NP_002365.3. NM_002374.3. [P11137-1]
NP_114033.2. NM_031845.2. [P11137-2]
NP_114035.2. NM_031847.2.
XP_016859607.1. XM_017004118.1. [P11137-1]
XP_016859612.1. XM_017004123.1. [P11137-3]
XP_016859613.1. XM_017004124.1. [P11137-3]
XP_016859627.1. XM_017004138.1. [P11137-4]
XP_016859628.1. XM_017004139.1. [P11137-4]
XP_016859629.1. XM_017004140.1. [P11137-2]
UniGeneiHs.368281.

3D structure databases

ProteinModelPortaliP11137.
SMRiP11137.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110305. 42 interactors.
DIPiDIP-577N.
IntActiP11137. 9 interactors.
MINTiMINT-1210186.
STRINGi9606.ENSP00000353508.

Chemistry databases

BindingDBiP11137.
ChEMBLiCHEMBL2390810.
DrugBankiDB01248. Docetaxel.
DB01196. Estramustine.
DB01229. Paclitaxel.

PTM databases

iPTMnetiP11137.
PhosphoSitePlusiP11137.

Polymorphism and mutation databases

BioMutaiMAP2.
DMDMi215274255.

Proteomic databases

EPDiP11137.
MaxQBiP11137.
PaxDbiP11137.
PeptideAtlasiP11137.
PRIDEiP11137.

Protocols and materials databases

DNASUi4133.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000199940; ENSP00000199940; ENSG00000078018. [P11137-4]
ENST00000360351; ENSP00000353508; ENSG00000078018. [P11137-1]
ENST00000361559; ENSP00000355290; ENSG00000078018. [P11137-2]
ENST00000392194; ENSP00000376032; ENSG00000078018. [P11137-2]
ENST00000447185; ENSP00000392164; ENSG00000078018. [P11137-3]
GeneIDi4133.
KEGGihsa:4133.
UCSCiuc002vdd.2. human. [P11137-1]

Organism-specific databases

CTDi4133.
DisGeNETi4133.
GeneCardsiMAP2.
HGNCiHGNC:6839. MAP2.
HPAiCAB001984.
HPA008273.
HPA012828.
MIMi157130. gene.
neXtProtiNX_P11137.
OpenTargetsiENSG00000078018.
PharmGKBiPA30583.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2418. Eukaryota.
ENOG4111J07. LUCA.
GeneTreeiENSGT00530000063491.
HOGENOMiHOG000113477.
HOVERGENiHBG000991.
InParanoidiP11137.
KOiK10430.
OMAiPFKTGRG.
OrthoDBiEOG091G00IT.
PhylomeDBiP11137.
TreeFamiTF316358.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000078018-MONOMER.
SIGNORiP11137.

Miscellaneous databases

ChiTaRSiMAP2. human.
GeneWikiiMAP2.
GenomeRNAii4133.
PROiP11137.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000078018.
CleanExiHS_MAP2.
ExpressionAtlasiP11137. baseline and differential.
GenevisibleiP11137. HS.

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...

Entry informationi

Entry nameiMTAP2_HUMAN
AccessioniPrimary (citable) accession number: P11137
Secondary accession number(s): Q17S04
, Q8IUX2, Q99975, Q99976
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 25, 2008
Last modified: November 2, 2016
This is version 168 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.