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P11137 (MTAP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Microtubule-associated protein 2

Short name=MAP-2
Gene names
Name:MAP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1827 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

Cytoplasmcytoskeleton Probable.

Post-translational modification

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/MAP2cis probably phosphorylated by PKA at Ser-323, Ser-354 and Ser-386 and by FYN at Tyr-67. Ref.8

Sequence similarities

Contains 3 Tau/MAP repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
Microtubule
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
   LigandCalmodulin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processaxonogenesis

Inferred from electronic annotation. Source: Ensembl

cellular response to organic substance

Inferred from electronic annotation. Source: Ensembl

central nervous system neuron development

Inferred from expression pattern PubMed 20846339. Source: DFLAT

dendrite morphogenesis

Inferred from expression pattern PubMed 20846339. Source: DFLAT

microtubule bundle formation

Inferred from electronic annotation. Source: Ensembl

neuron projection development

Inferred from expression pattern PubMed 20846339. Source: DFLAT

peptidyl-threonine phosphorylation

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-KW

dendritic shaft

Inferred from electronic annotation. Source: Ensembl

microtubule

Inferred from electronic annotation. Source: UniProtKB-KW

microtubule associated complex

Traceable author statement PubMed 9588626. Source: ProtInc

neuronal cell body

Inferred from electronic annotation. Source: Ensembl

nuclear periphery

Inferred from electronic annotation. Source: Ensembl

   Molecular_functiondystroglycan binding

Inferred from physical interaction PubMed 18341635. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 20195357. Source: IntAct

structural molecule activity

Non-traceable author statement PubMed 9588626. Source: ProtInc

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

CBFBQ139512EBI-2682460,EBI-718750

Alternative products

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

Note: Additional isoforms seem to exist.
Isoform 1 (identifier: P11137-1)

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.
Isoform 2 (identifier: P11137-2)

Also known as: MAP2c;

The sequence of this isoform differs from the canonical sequence as follows:
     152-1507: Missing.
Note: Contains a phosphoserine at position 323 (By similarity). Contains a phosphoserine at position 354 (By similarity). Contains a phosphoserine at position 386 (By similarity). Contains a phosphotyrosine at position 67.
Isoform 3 (identifier: P11137-3)

The sequence of this isoform differs from the canonical sequence as follows:
     152-155: Missing.
Isoform 4 (identifier: P11137-4)

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18271827Microtubule-associated protein 2
PRO_0000072747

Regions

Repeat1661 – 169131Tau/MAP 1
Repeat1692 – 172231Tau/MAP 2
Repeat1723 – 175432Tau/MAP 3
Region1447 – 146721Calmodulin-binding Potential

Amino acid modifications

Modified residue7251Phosphoserine By similarity
Modified residue13471Phosphoserine Ref.11
Modified residue13531Phosphoserine Ref.11
Modified residue16021Phosphothreonine By similarity
Modified residue16051Phosphothreonine By similarity
Modified residue16791Phosphoserine; by MARK1 By similarity

Natural variations

Alternative sequence152 – 15071356Missing in isoform 2.
VSP_003197
Alternative sequence152 – 22978DLLTA…LFGHT → AAGGESALAPSVFKQAKDKV SNSTLSKIPALQGSTKSPRY SSACPSTTKRATFSDSLLIQ PTSAGSTDRLPYSKSGNK in isoform 4.
VSP_043596
Alternative sequence152 – 1554Missing in isoform 3.
VSP_011302
Alternative sequence230 – 15281299Missing in isoform 4.
VSP_043597
Alternative sequence16911Q → QVRILNKKIDFSKVQSRCGS KDNIKHSAGGGN in isoform 4.
VSP_043598
Natural variant821A → G.
Corresponds to variant rs2271251 [ dbSNP | Ensembl ].
VAR_019612
Natural variant1791E → G.
Corresponds to variant rs6749066 [ dbSNP | Ensembl ].
VAR_050019
Natural variant2771E → D in a colorectal cancer sample; somatic mutation. Ref.12
VAR_036014
Natural variant4231R → K.
Corresponds to variant rs741006 [ dbSNP | Ensembl ].
VAR_019613
Natural variant7051P → L in a colorectal cancer sample; somatic mutation. Ref.12
VAR_036015
Natural variant9761H → L.
Corresponds to variant rs13425372 [ dbSNP | Ensembl ].
VAR_050020
Natural variant9911G → R.
Corresponds to variant rs35927101 [ dbSNP | Ensembl ].
VAR_050021
Natural variant10991M → V.
Corresponds to variant rs17745550 [ dbSNP | Ensembl ].
VAR_050022

Experimental info

Sequence conflict91A → G in AAB48098. Ref.2
Sequence conflict91A → G in AAB48097. Ref.2
Sequence conflict371A → R in AAA03354. Ref.1
Sequence conflict1081G → A in AAA03354. Ref.1
Sequence conflict1871K → S in AAA03354. Ref.1
Sequence conflict11121E → Q in AAA03354. Ref.1
Sequence conflict11121E → Q in AAB48098. Ref.2
Sequence conflict11121E → Q in AAA59552. Ref.5
Sequence conflict16551A → GL in AAB48098. Ref.2
Sequence conflict16551A → GL in AAB48097. Ref.2
Sequence conflict1715 – 17162RH → D in AAA03354. Ref.1
Sequence conflict17361A → V in AAA03354. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (MAP2b) [UniParc].

Last modified November 25, 2008. Version 4.
Checksum: 2C4801C589086603

FASTA1,827199,526
        10         20         30         40         50         60 
MADERKDEAK APHWTSAPLT EASAHSHPPE IKDQGGAGEG LVRSANGFPY REDEEGAFGE 

        70         80         90        100        110        120 
HGSQGTYSNT KENGINGELT SADRETAEEV SARIVQVVTA EAVAVLKGEQ EKEAQHKDQT 

       130        140        150        160        170        180 
AALPLAAEET ANLPPSPPPS PASEQTVTVE EDLLTASKME FHDQQELTPS TAEPSDQKEK 

       190        200        210        220        230        240 
ESEKQSKPGE DLKHAALVSQ PETTKTYPDK KDMQGTEEEK APLALFGHTL VASLEDMKQK 

       250        260        270        280        290        300 
TEPSLVVPGI DLPKEPPTPK EQKDWFIEMP TEAKKDEWGL VAPISPGPLT PMREKDVFDD 

       310        320        330        340        350        360 
IPKWEGKQFD SPMPSPFQGG SFTLPLDVMK NEIVTETSPF APAFLQPDDK KSLQQTSGPA 

       370        380        390        400        410        420 
TAKDSFKIEE PHEAKPDKMA EAPPSEAMTL PKDAHIPVVE EHVMGKVLEE EKEAINQETV 

       430        440        450        460        470        480 
QQRDTFTPSG QEPILTEKET ELKLEEKTTI SDKEAVPKES KPPKPADEEI GIIQTSTEHT 

       490        500        510        520        530        540 
FSEQKDQEPT TDMLKQDSFP VSLEQAVTDS AMTSKTLEKA MTEPSALIEK SSIQELFEMR 

       550        560        570        580        590        600 
VDDKDKIEGV GAATSAELDM PFYEDKSGMS KYFETSALKE EATKSIEPGS DYYELSDTRE 

       610        620        630        640        650        660 
SVHESIDTMS PMHKNGDKEF QTGKESQPSP PAQEAGYSTL AQSYPSDLPE EPSSPQERMF 

       670        680        690        700        710        720 
TIDPKVYGEK RDLHSKNKDD LTLSRSLGLG GRSAIEQRSM SINLPMSCLD SIALGFNFGR 

       730        740        750        760        770        780 
GHDLSPLASD ILTNTSGSMD EGDDYLPATT PALEKAPCFP VESKEEEQIE KVKATGEEST 

       790        800        810        820        830        840 
QAEISCESPF LAKDFYKNGT VMAPDLPEML DLAGTRSRLA SVSADAEVAR RKSVPSETVV 

       850        860        870        880        890        900 
EDSRTGLPPV TDENHVIVKT DSQLEDLGYC VFNKYTVPLP SPVQDSENLS GESGTFYEGT 

       910        920        930        940        950        960 
DDKVRRDLAT DLSLIEVKLA AAGRVKDEFS VDKEASAHIS GDKSGLSKEF DQEKKANDRL 

       970        980        990       1000       1010       1020 
DTVLEKSEEH ADSKEHAKKT EEAGDEIETF GLGVTYEQAL AKDLSIPTDA SSEKAEKGLS 

      1030       1040       1050       1060       1070       1080 
SVPEIAEVEP SKKVEQGLDF AVQGQLDVKI SDFGQMASGL NIDDRRATEL KLEATQDMTP 

      1090       1100       1110       1120       1130       1140 
SSKAPQEADA FMGVESGHMK EGTKVSETEV KEKVAKPDLV HQEAVDKEES YESSGEHESL 

      1150       1160       1170       1180       1190       1200 
TMESLKADEG KKETSPESSL IQDEIAVKLS VEIPCPPAVS EADLATDERA DVQMEFIQGP 

      1210       1220       1230       1240       1250       1260 
KEESKETPDI SITPSDVAEP LHETIVSEPA EIQSEEEEIE AQGEYDKLLF RSDTLQITDL 

      1270       1280       1290       1300       1310       1320 
GVSGAREEFV ETCPSEHKGV IESVVTIEDD FITVVQTTTD EGESGSHSVR FAALEQPEVE 

      1330       1340       1350       1360       1370       1380 
RRPSPHDEEE FEVEEAAEAQ AEPKDGSPEA PASPEREEVA LSEYKTETYD DYKDETTIDD 

      1390       1400       1410       1420       1430       1440 
SIMDADSLWV DTQDDDRSIM TEQLETIPKE EKAEKEARRS SLEKHRKEKP FKTGRGRIST 

      1450       1460       1470       1480       1490       1500 
PERKVAKKEP STVSRDEVRR KKAVYKKAEL AKKTEVQAHS PSRKFILKPA IKYTRPTHLS 

      1510       1520       1530       1540       1550       1560 
CVKRKTTAAG GESALAPSVF KQAKDKVSDG VTKSPEKRSS LPRPSSILPP RRGVSGDRDE 

      1570       1580       1590       1600       1610       1620 
NSFSLNSSIS SSARRTTRSE PIRRAGKSGT STPTTPGSTA ITPGTPPSYS SRTPGTPGTP 

      1630       1640       1650       1660       1670       1680 
SYPRTPHTPG TPKSAILVPS EKKVAIIRTP PKSPATPKQL RLINQPLPDL KNVKSKIGST 

      1690       1700       1710       1720       1730       1740 
DNIKYQPKGG QVQIVTKKID LSHVTSKCGS LKNIRHRPGG GRVKIESVKL DFKEKAQAKV 

      1750       1760       1770       1780       1790       1800 
GSLDNAHHVP GGGNVKIDSQ KLNFREHAKA RVDHGAEIIT QSPGRSSVAS PRRLSNVSSS 

      1810       1820 
GSINLLESPQ LATLAEDVTA ALAKQGL 

« Hide

Isoform 2 (MAP2c) [UniParc].

Checksum: CE8BB23BCD16A159
Show »

FASTA47149,640
Isoform 3 [UniParc].

Checksum: 7E474A0F3B691188
Show »

FASTA1,823199,084
Isoform 4 [UniParc].

Checksum: 2A4E43681AE8C196
Show »

FASTA55958,954

References

« Hide 'large scale' references
[1]"Complete cDNA of human MAP2 gene and a profile of two RFLPs for BglII/BclI."
Price R.
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Characterization of the transcripts encoding two isoforms of human microtubule-associated protein-2 (MAP-2)."
Albala J.S., Kalcheva N., Shafit-Zagardo B.
Gene 136:377-378(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
Tissue: Brain.
[3]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
Tissue: Brain and Pancreas.
[6]"Sequence of a human MAP-2 region sharing epitopes with Alzheimer neurofibrillary tangles."
Dammerman M., Yen S.H., Shafit-Zagardo B.
J. Neurosci. Res. 24:487-495(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 77-649 (ISOFORM 1).
[7]"Partial sequence of MAP2 in the region of a shared epitope with Alzheimer neurofibrillary tangles."
Kosik K.S., Orecchio L.D., Bakalis S., Duffy L., Neve R.L.
J. Neurochem. 51:587-598(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 494-1562 (ISOFORM 1).
[8]"Fyn phosphorylates human MAP-2c on tyrosine 67."
Zamora-Leon S.P., Bresnick A., Backer J.M., Shafit-Zagardo B.
J. Biol. Chem. 280:1962-1970(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-67 (ISOFORM 2) BY FYN.
[9]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1347 AND SER-1353, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] ASP-277 AND LEU-705.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2384.1. [P11137-1]
CCDS2385.1. [P11137-2]
CCDS33369.1. [P11137-4]
PIRQRHUMT. I53693.
I67793.
RefSeqNP_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_005246620.1. XM_005246563.1. [P11137-1]
XP_005246621.1. XM_005246564.1. [P11137-3]
UniGeneHs.368281.

3D structure databases

ProteinModelPortalP11137.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110305. 37 interactions.
DIPDIP-577N.
IntActP11137. 7 interactions.
MINTMINT-1210186.
STRING9606.ENSP00000353508.

Chemistry

ChEMBLCHEMBL2390810.
DrugBankDB01196. Estramustine.

PTM databases

PhosphoSiteP11137.

Polymorphism databases

DMDM215274255.

Proteomic databases

MaxQBP11137.
PaxDbP11137.
PRIDEP11137.

Protocols and materials databases

DNASU4133.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000199940; ENSP00000199940; ENSG00000078018. [P11137-4]
ENST00000360351; ENSP00000353508; ENSG00000078018. [P11137-1]
ENST00000361559; ENSP00000355290; ENSG00000078018. [P11137-2]
ENST00000392194; ENSP00000376032; ENSG00000078018. [P11137-2]
ENST00000447185; ENSP00000392164; ENSG00000078018. [P11137-3]
GeneID4133.
KEGGhsa:4133.
UCSCuc002vdc.1. human. [P11137-1]
uc002vdd.1. human. [P11137-4]
uc002vdg.1. human. [P11137-2]
uc002vdi.1. human. [P11137-3]

Organism-specific databases

CTD4133.
GeneCardsGC02P210252.
HGNCHGNC:6839. MAP2.
HPACAB001984.
HPA008273.
HPA012828.
MIM157130. gene.
neXtProtNX_P11137.
PharmGKBPA30583.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG148882.
HOGENOMHOG000113477.
HOVERGENHBG000991.
InParanoidP11137.
KOK10430.
OMATEFREQP.
OrthoDBEOG75XGKK.
PhylomeDBP11137.
TreeFamTF316358.

Gene expression databases

ArrayExpressP11137.
BgeeP11137.
CleanExHS_MAP2.
GenevestigatorP11137.

Family and domain databases

InterProIPR027324. MAP2/MAP4/Tau.
IPR013588. MAP2_projctn.
IPR001084. MAP_tubulin-bd_rpt.
[Graphical view]
PANTHERPTHR11501. PTHR11501. 1 hit.
PfamPF08377. MAP2_projctn. 1 hit.
PF00418. Tubulin-binding. 3 hits.
[Graphical view]
PROSITEPS00229. TAU_MAP_1. 2 hits.
PS51491. TAU_MAP_2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMAP2. human.
GeneWikiMAP2.
GenomeRNAi4133.
NextBio16222.
PROP11137.
SOURCESearch...

Entry information

Entry nameMTAP2_HUMAN
AccessionPrimary (citable) accession number: P11137
Secondary accession number(s): Q17S04 expand/collapse secondary AC list , Q8IUX2, Q99975, Q99976
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: November 25, 2008
Last modified: July 9, 2014
This is version 145 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM