Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Microtubule-associated protein 2 (MAP-2)

 MTAP2_HUMAN             Reviewed;        1827 AA.
P11137; Q17S04; Q8IUX2; Q99975; Q99976;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 4.
12-SEP-2018, entry version 183.
RecName: Full=Microtubule-associated protein 2;
Short=MAP-2;
Name=MAP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Price R.;
"Complete cDNA of human MAP2 gene and a profile of two RFLPs for
BglII/BclI.";
Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
TISSUE=Brain;
PubMed=8294038; DOI=10.1016/0378-1119(93)90502-T;
Albala J.S., Kalcheva N., Shafit-Zagardo B.;
"Characterization of the transcripts encoding two isoforms of human
microtubule-associated protein-2 (MAP-2).";
Gene 136:377-378(1993).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
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., 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.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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., 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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
TISSUE=Brain, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 77-649 (ISOFORM 1).
PubMed=2481044; DOI=10.1002/jnr.490240405;
Dammerman M., Yen S.H., Shafit-Zagardo B.;
"Sequence of a human MAP-2 region sharing epitopes with Alzheimer
neurofibrillary tangles.";
J. Neurosci. Res. 24:487-495(1989).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 494-1562 (ISOFORM 1).
PubMed=2455776; DOI=10.1111/j.1471-4159.1988.tb01079.x;
Kosik K.S., Orecchio L.D., Bakalis S., Duffy L., Neve R.L.;
"Partial sequence of MAP2 in the region of a shared epitope with
Alzheimer neurofibrillary tangles.";
J. Neurochem. 51:587-598(1988).
[8]
PHOSPHORYLATION AT TYR-67 (ISOFORM 2) BY FYN.
PubMed=15536091; DOI=10.1074/jbc.M411380200;
Zamora-Leon S.P., Bresnick A., Backer J.M., Shafit-Zagardo B.;
"Fyn phosphorylates human MAP-2c on tyrosine 67.";
J. Biol. Chem. 280:1962-1970(2005).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1347 AND SER-1353, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1782, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
VARIANTS [LARGE SCALE ANALYSIS] ASP-277 AND LEU-705.
PubMed=16959974; DOI=10.1126/science.1133427;
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., 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.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- 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.
-!- SUBUNIT: Interacts with KNDC1 (via KIND2); the interaction
enhances MAP2 phosphorylation and localizes KNDC1 to dendrites.
{ECO:0000250|UniProtKB:P20357}.
-!- INTERACTION:
Q13951:CBFB; NbExp=2; IntAct=EBI-2682460, EBI-718750;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cell
projection, dendrite {ECO:0000250|UniProtKB:P20357}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=1; Synonyms=MAP2b;
IsoId=P11137-1; Sequence=Displayed;
Name=2; Synonyms=MAP2c;
IsoId=P11137-2; Sequence=VSP_003197;
Note=Contains a phosphoserine at position 323. Contains a
phosphoserine at position 354. Contains a phosphoserine at
position 386. Contains a phosphotyrosine at position 67.
{ECO:0000250|UniProtKB:P15146, ECO:0000269|PubMed:15536091};
Name=3;
IsoId=P11137-3; Sequence=VSP_011302;
Name=4;
IsoId=P11137-4; Sequence=VSP_043596, VSP_043597, VSP_043598;
Note=No experimental confirmation available.;
-!- PTM: 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. The interaction
with KNDC1 enhances MAP2 threonine phosphorylation (By
similarity). {ECO:0000250|UniProtKB:P15146,
ECO:0000250|UniProtKB:P20357}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/MAP2ID44216ch2q34.html";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; U01828; AAA03354.1; -; mRNA.
EMBL; U89330; AAB48098.1; -; mRNA.
EMBL; U89329; AAB48097.1; -; mRNA.
EMBL; AC006385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC019106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC079833; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC108072; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471063; EAW70459.1; -; Genomic_DNA.
EMBL; BC038857; AAH38857.1; -; mRNA.
EMBL; BC110423; AAI10424.1; -; mRNA.
EMBL; BC117123; AAI17124.1; -; mRNA.
EMBL; BC143245; AAI43246.1; -; mRNA.
EMBL; M25668; AAA59552.1; -; mRNA.
CCDS; CCDS2384.1; -. [P11137-1]
CCDS; CCDS2385.1; -. [P11137-2]
CCDS; CCDS33369.1; -. [P11137-4]
CCDS; CCDS86916.1; -. [P11137-3]
PIR; I53693; QRHUMT.
PIR; I67793; I67793.
RefSeq; NP_001034627.1; NM_001039538.1. [P11137-4]
RefSeq; NP_002365.3; NM_002374.3. [P11137-1]
RefSeq; NP_114033.2; NM_031845.2. [P11137-2]
RefSeq; NP_114035.2; NM_031847.2.
RefSeq; XP_016859607.1; XM_017004118.1. [P11137-1]
RefSeq; XP_016859612.1; XM_017004123.1. [P11137-3]
RefSeq; XP_016859613.1; XM_017004124.1. [P11137-3]
RefSeq; XP_016859627.1; XM_017004138.1. [P11137-4]
RefSeq; XP_016859628.1; XM_017004139.1. [P11137-4]
RefSeq; XP_016859629.1; XM_017004140.1. [P11137-2]
UniGene; Hs.368281; -.
ProteinModelPortal; P11137; -.
SMR; P11137; -.
BioGrid; 110305; 48.
DIP; DIP-577N; -.
IntAct; P11137; 9.
MINT; P11137; -.
STRING; 9606.ENSP00000353508; -.
BindingDB; P11137; -.
ChEMBL; CHEMBL2390810; -.
DrugBank; DB01248; Docetaxel.
DrugBank; DB01196; Estramustine.
DrugBank; DB01229; Paclitaxel.
iPTMnet; P11137; -.
PhosphoSitePlus; P11137; -.
BioMuta; MAP2; -.
DMDM; 215274255; -.
EPD; P11137; -.
MaxQB; P11137; -.
PaxDb; P11137; -.
PeptideAtlas; P11137; -.
PRIDE; P11137; -.
ProteomicsDB; 52694; -.
ProteomicsDB; 52695; -. [P11137-2]
ProteomicsDB; 52696; -. [P11137-3]
ProteomicsDB; 52697; -. [P11137-4]
DNASU; 4133; -.
Ensembl; ENST00000199940; ENSP00000199940; ENSG00000078018. [P11137-4]
Ensembl; ENST00000360351; ENSP00000353508; ENSG00000078018. [P11137-1]
Ensembl; ENST00000361559; ENSP00000355290; ENSG00000078018. [P11137-2]
Ensembl; ENST00000392194; ENSP00000376032; ENSG00000078018. [P11137-2]
Ensembl; ENST00000447185; ENSP00000392164; ENSG00000078018. [P11137-3]
GeneID; 4133; -.
KEGG; hsa:4133; -.
UCSC; uc002vdd.2; human. [P11137-1]
CTD; 4133; -.
DisGeNET; 4133; -.
EuPathDB; HostDB:ENSG00000078018.19; -.
GeneCards; MAP2; -.
HGNC; HGNC:6839; MAP2.
HPA; CAB001984; -.
HPA; HPA008273; -.
HPA; HPA012828; -.
MIM; 157130; gene.
neXtProt; NX_P11137; -.
OpenTargets; ENSG00000078018; -.
PharmGKB; PA30583; -.
eggNOG; KOG2418; Eukaryota.
eggNOG; ENOG4111J07; LUCA.
GeneTree; ENSGT00530000063491; -.
HOGENOM; HOG000113477; -.
HOVERGEN; HBG000991; -.
InParanoid; P11137; -.
KO; K10430; -.
OMA; PFKTGRG; -.
OrthoDB; EOG091G00IT; -.
PhylomeDB; P11137; -.
TreeFam; TF316358; -.
SIGNOR; P11137; -.
ChiTaRS; MAP2; human.
GeneWiki; MAP2; -.
GenomeRNAi; 4133; -.
PRO; PR:P11137; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000078018; Expressed in 213 organ(s), highest expression level in dorsolateral prefrontal cortex.
CleanEx; HS_MAP2; -.
ExpressionAtlas; P11137; baseline and differential.
Genevisible; P11137; HS.
GO; GO:0150014; C:apical distal dendrite; ISS:ARUK-UCL.
GO; GO:0043203; C:axon hillock; ISS:ARUK-UCL.
GO; GO:0043194; C:axon initial segment; ISS:ARUK-UCL.
GO; GO:0097441; C:basal dendrite; ISS:ARUK-UCL.
GO; GO:0097442; C:CA3 pyramidal cell dendrite; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; ISS:ARUK-UCL.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0032839; C:dendrite cytoplasm; ISS:ARUK-UCL.
GO; GO:0044307; C:dendritic branch; ISS:ARUK-UCL.
GO; GO:1902737; C:dendritic filopodium; ISS:ARUK-UCL.
GO; GO:0044294; C:dendritic growth cone; ISS:ARUK-UCL.
GO; GO:0043198; C:dendritic shaft; ISS:ARUK-UCL.
GO; GO:0150002; C:distal dendrite; ISS:ARUK-UCL.
GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
GO; GO:0043005; C:neuron projection; IBA:GO_Central.
GO; GO:0043025; C:neuronal cell body; ISS:ARUK-UCL.
GO; GO:0034399; C:nuclear periphery; IEA:Ensembl.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0014069; C:postsynaptic density; IEA:Ensembl.
GO; GO:0150001; C:primary dendrite; ISS:ARUK-UCL.
GO; GO:1990635; C:proximal dendrite; ISS:ARUK-UCL.
GO; GO:1990769; C:proximal neuron projection; ISS:ARUK-UCL.
GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
GO; GO:0002162; F:dystroglycan binding; IPI:UniProtKB.
GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
GO; GO:0005198; F:structural molecule activity; NAS:ProtInc.
GO; GO:0007409; P:axonogenesis; IEA:Ensembl.
GO; GO:0071310; P:cellular response to organic substance; IEA:Ensembl.
GO; GO:0021954; P:central nervous system neuron development; IEP:DFLAT.
GO; GO:0016358; P:dendrite development; TAS:ARUK-UCL.
GO; GO:0048813; P:dendrite morphogenesis; IEP:DFLAT.
GO; GO:0030010; P:establishment of cell polarity; IEA:Ensembl.
GO; GO:0001578; P:microtubule bundle formation; IEA:Ensembl.
GO; GO:0000226; P:microtubule cytoskeleton organization; ISS:ARUK-UCL.
GO; GO:0030517; P:negative regulation of axon extension; ISS:ARUK-UCL.
GO; GO:1904527; P:negative regulation of microtubule binding; ISS:ARUK-UCL.
GO; GO:2000575; P:negative regulation of microtubule motor activity; ISS:ARUK-UCL.
GO; GO:0031115; P:negative regulation of microtubule polymerization; ISS:ARUK-UCL.
GO; GO:0031175; P:neuron projection development; IEP:DFLAT.
GO; GO:1901953; P:positive regulation of anterograde dense core granule transport; ISS:ARUK-UCL.
GO; GO:1903744; P:positive regulation of anterograde synaptic vesicle transport; ISS:ARUK-UCL.
GO; GO:1903827; P:regulation of cellular protein localization; ISS:ARUK-UCL.
GO; GO:0031113; P:regulation of microtubule polymerization; TAS:ARUK-UCL.
GO; GO:1902513; P:regulation of organelle transport along microtubule; ISS:ARUK-UCL.
InterPro; IPR030797; MAP2.
InterPro; IPR013588; MAP2_projctn.
InterPro; IPR001084; MAP_tubulin-bd_rpt.
PANTHER; PTHR11501:SF15; PTHR11501:SF15; 1.
Pfam; PF08377; MAP2_projctn; 1.
Pfam; PF00418; Tubulin-binding; 3.
PROSITE; PS00229; TAU_MAP_1; 2.
PROSITE; PS51491; TAU_MAP_2; 3.
1: Evidence at protein level;
Alternative splicing; Calmodulin-binding; Cell projection;
Complete proteome; Cytoplasm; Cytoskeleton; Microtubule;
Phosphoprotein; Polymorphism; Reference proteome; Repeat.
CHAIN 1 1827 Microtubule-associated protein 2.
/FTId=PRO_0000072747.
REPEAT 1661 1691 Tau/MAP 1.
REPEAT 1692 1722 Tau/MAP 2.
REPEAT 1723 1754 Tau/MAP 3.
REGION 701 744 Interaction with KNDC1.
{ECO:0000250|UniProtKB:P20357}.
REGION 1447 1467 Calmodulin-binding. {ECO:0000255}.
MOD_RES 136 136 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 140 140 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 285 285 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 498 498 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 601 601 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 605 605 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 629 629 Phosphoserine.
{ECO:0000250|UniProtKB:P15146}.
MOD_RES 725 725 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 729 729 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 733 733 Phosphothreonine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 736 736 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 738 738 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 745 745 Phosphotyrosine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 881 881 Phosphoserine.
{ECO:0000250|UniProtKB:P15146}.
MOD_RES 890 890 Phosphoserine.
{ECO:0000250|UniProtKB:P15146}.
MOD_RES 936 936 Phosphoserine.
{ECO:0000250|UniProtKB:P15146}.
MOD_RES 1133 1133 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1134 1134 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1139 1139 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1154 1154 Phosphothreonine.
{ECO:0000250|UniProtKB:P15146}.
MOD_RES 1155 1155 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1159 1159 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1347 1347 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1353 1353 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 1534 1534 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1555 1555 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1588 1588 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1602 1602 Phosphothreonine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1605 1605 Phosphothreonine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1616 1616 Phosphothreonine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1619 1619 Phosphothreonine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1649 1649 Phosphothreonine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1653 1653 Phosphoserine.
{ECO:0000250|UniProtKB:P15146}.
MOD_RES 1679 1679 Phosphoserine; by MARK1.
{ECO:0000250|UniProtKB:P15146}.
MOD_RES 1782 1782 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1787 1787 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1790 1790 Phosphoserine.
{ECO:0000250|UniProtKB:P20357}.
MOD_RES 1795 1795 Phosphoserine.
{ECO:0000250|UniProtKB:P15146}.
MOD_RES 1808 1808 Phosphoserine.
{ECO:0000250|UniProtKB:P15146}.
VAR_SEQ 152 1507 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:8294038}.
/FTId=VSP_003197.
VAR_SEQ 152 229 DLLTASKMEFHDQQELTPSTAEPSDQKEKESEKQSKPGEDL
KHAALVSQPETTKTYPDKKDMQGTEEEKAPLALFGHT ->
AAGGESALAPSVFKQAKDKVSNSTLSKIPALQGSTKSPRYS
SACPSTTKRATFSDSLLIQPTSAGSTDRLPYSKSGNK (in
isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043596.
VAR_SEQ 152 155 Missing (in isoform 3).
{ECO:0000303|PubMed:8294038}.
/FTId=VSP_011302.
VAR_SEQ 230 1528 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043597.
VAR_SEQ 1691 1691 Q -> QVRILNKKIDFSKVQSRCGSKDNIKHSAGGGN (in
isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043598.
VARIANT 82 82 A -> G (in dbSNP:rs2271251).
/FTId=VAR_019612.
VARIANT 179 179 E -> G (in dbSNP:rs6749066).
/FTId=VAR_050019.
VARIANT 277 277 E -> D (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036014.
VARIANT 423 423 R -> K (in dbSNP:rs741006).
/FTId=VAR_019613.
VARIANT 705 705 P -> L (in a colorectal cancer sample;
somatic mutation; dbSNP:rs146432517).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036015.
VARIANT 976 976 H -> L (in dbSNP:rs13425372).
/FTId=VAR_050020.
VARIANT 991 991 G -> R (in dbSNP:rs35927101).
/FTId=VAR_050021.
VARIANT 1099 1099 M -> V (in dbSNP:rs17745550).
/FTId=VAR_050022.
CONFLICT 9 9 A -> G (in Ref. 2; AAB48098/AAB48097).
{ECO:0000305}.
CONFLICT 37 37 A -> R (in Ref. 1; AAA03354).
{ECO:0000305}.
CONFLICT 108 108 G -> A (in Ref. 1; AAA03354).
{ECO:0000305}.
CONFLICT 187 187 K -> S (in Ref. 1; AAA03354).
{ECO:0000305}.
CONFLICT 1112 1112 E -> Q (in Ref. 1; AAA03354, 2; AAB48098
and 5; AAA59552). {ECO:0000305}.
CONFLICT 1655 1655 A -> GL (in Ref. 2; AAB48098/AAB48097).
{ECO:0000305}.
CONFLICT 1715 1716 RH -> D (in Ref. 1; AAA03354).
{ECO:0000305}.
CONFLICT 1736 1736 A -> V (in Ref. 1; AAA03354).
{ECO:0000305}.
SEQUENCE 1827 AA; 199526 MW; 2C4801C589086603 CRC64;
MADERKDEAK APHWTSAPLT EASAHSHPPE IKDQGGAGEG LVRSANGFPY REDEEGAFGE
HGSQGTYSNT KENGINGELT SADRETAEEV SARIVQVVTA EAVAVLKGEQ EKEAQHKDQT
AALPLAAEET ANLPPSPPPS PASEQTVTVE EDLLTASKME FHDQQELTPS TAEPSDQKEK
ESEKQSKPGE DLKHAALVSQ PETTKTYPDK KDMQGTEEEK APLALFGHTL VASLEDMKQK
TEPSLVVPGI DLPKEPPTPK EQKDWFIEMP TEAKKDEWGL VAPISPGPLT PMREKDVFDD
IPKWEGKQFD SPMPSPFQGG SFTLPLDVMK NEIVTETSPF APAFLQPDDK KSLQQTSGPA
TAKDSFKIEE PHEAKPDKMA EAPPSEAMTL PKDAHIPVVE EHVMGKVLEE EKEAINQETV
QQRDTFTPSG QEPILTEKET ELKLEEKTTI SDKEAVPKES KPPKPADEEI GIIQTSTEHT
FSEQKDQEPT TDMLKQDSFP VSLEQAVTDS AMTSKTLEKA MTEPSALIEK SSIQELFEMR
VDDKDKIEGV GAATSAELDM PFYEDKSGMS KYFETSALKE EATKSIEPGS DYYELSDTRE
SVHESIDTMS PMHKNGDKEF QTGKESQPSP PAQEAGYSTL AQSYPSDLPE EPSSPQERMF
TIDPKVYGEK RDLHSKNKDD LTLSRSLGLG GRSAIEQRSM SINLPMSCLD SIALGFNFGR
GHDLSPLASD ILTNTSGSMD EGDDYLPATT PALEKAPCFP VESKEEEQIE KVKATGEEST
QAEISCESPF LAKDFYKNGT VMAPDLPEML DLAGTRSRLA SVSADAEVAR RKSVPSETVV
EDSRTGLPPV TDENHVIVKT DSQLEDLGYC VFNKYTVPLP SPVQDSENLS GESGTFYEGT
DDKVRRDLAT DLSLIEVKLA AAGRVKDEFS VDKEASAHIS GDKSGLSKEF DQEKKANDRL
DTVLEKSEEH ADSKEHAKKT EEAGDEIETF GLGVTYEQAL AKDLSIPTDA SSEKAEKGLS
SVPEIAEVEP SKKVEQGLDF AVQGQLDVKI SDFGQMASGL NIDDRRATEL KLEATQDMTP
SSKAPQEADA FMGVESGHMK EGTKVSETEV KEKVAKPDLV HQEAVDKEES YESSGEHESL
TMESLKADEG KKETSPESSL IQDEIAVKLS VEIPCPPAVS EADLATDERA DVQMEFIQGP
KEESKETPDI SITPSDVAEP LHETIVSEPA EIQSEEEEIE AQGEYDKLLF RSDTLQITDL
GVSGAREEFV ETCPSEHKGV IESVVTIEDD FITVVQTTTD EGESGSHSVR FAALEQPEVE
RRPSPHDEEE FEVEEAAEAQ AEPKDGSPEA PASPEREEVA LSEYKTETYD DYKDETTIDD
SIMDADSLWV DTQDDDRSIM TEQLETIPKE EKAEKEARRS SLEKHRKEKP FKTGRGRIST
PERKVAKKEP STVSRDEVRR KKAVYKKAEL AKKTEVQAHS PSRKFILKPA IKYTRPTHLS
CVKRKTTAAG GESALAPSVF KQAKDKVSDG VTKSPEKRSS LPRPSSILPP RRGVSGDRDE
NSFSLNSSIS SSARRTTRSE PIRRAGKSGT STPTTPGSTA ITPGTPPSYS SRTPGTPGTP
SYPRTPHTPG TPKSAILVPS EKKVAIIRTP PKSPATPKQL RLINQPLPDL KNVKSKIGST
DNIKYQPKGG QVQIVTKKID LSHVTSKCGS LKNIRHRPGG GRVKIESVKL DFKEKAQAKV
GSLDNAHHVP GGGNVKIDSQ KLNFREHAKA RVDHGAEIIT QSPGRSSVAS PRRLSNVSSS
GSINLLESPQ LATLAEDVTA ALAKQGL


Related products :

Catalog number Product name Quantity
EIAAB35342 Fam82b,Microtubule-associated protein,Mouse,mRMD-1,Mus musculus,Protein FAM82B,Regulator of microtubule dynamics protein 1,RMD-1
EIAAB25789 Cardiac zipper protein,CAZIP,Homo sapiens,Human,KIAA0774,Microtubule plus-end tracking protein TIP150,Microtubule-associated tumor suppressor candidate 2,MTUS2,TIP150,Tracking protein of 150 kDa
EIAAB25788 Cardiac zipper protein,Cazip,Kiaa0774,Microtubule plus-end tracking protein TIP150,Microtubule-associated tumor suppressor candidate 2 homolog,Mouse,Mtus2,Mus musculus,Tip150,Tracking protein of 150 k
EIAAB12889 Echinoderm microtubule-associated protein-like 5-like,Echinoderm microtubule-associated protein-like 6,EMAP-6,EML5L,EML6,Homo sapiens,Human
EIAAB12890 Echinoderm microtubule-associated protein-like 5-like,Echinoderm microtubule-associated protein-like 6,EMAP-6,Eml5l,Eml6,Mouse,Mus musculus
6242-0039 RABBIT ANTI BOVINE MICROTUBULE ASSOCIATED PROTEIN 2 (+ TAU), Product Type Polyclonal Antibody, Specificity MICROTUBULE ASSOCIATED PROTEIN 2 , Target Species Bovine, Host Rabbit, Format Purified, 0.2 ml
SCH-6242-0039 RABBIT ANTI BOVINE MICROTUBULE ASSOCIATED PROTEIN 2 (+ TAU), Product Type Polyclonal Antibody, Specificity MICROTUBULE ASSOCIATED PROTEIN 2 , Target Species Bovine, Host Rabbit, Format Purified, 0.2 ml
6242-0206 MOUSE ANTI BOVINE MICROTUBULE ASSOCIATED PROTEIN TAU, Product Type Monoclonal Antibody, Specificity MICROTUBULE ASSOCIATED PROTEIN TAU, Target Species Bovine, Host Mouse, Format Ascites, Isotypes 0.1 ml
SCH-6242-0206 MOUSE ANTI BOVINE MICROTUBULE ASSOCIATED PROTEIN TAU, Product Type Monoclonal Antibody, Specificity MICROTUBULE ASSOCIATED PROTEIN TAU, Target Species Bovine, Host Mouse, Format Ascites, Isotypes 0.1 ml
EIAAB44014 CEV14,Clonal evolution-related gene on chromosome 14 protein,GMAP-210,Golgi-associated microtubule-binding protein 210,Homo sapiens,Human,Thyroid receptor-interacting protein 11,TR-interacting protein
SEQ641Ra ELISA Kit for Echinoderm Microtubule Associated Protein Like Protein 2 (EML2) Rattus norvegicus (Rat) 96T
orb81209 Human Microtubule-Associated Protein Light Chain Alpha protein Proteins 5
bs-1847P Peptides: MAP1A_Mtap1a(microtubule associated protein 1A) Protein Length:12-25 amino acids. 200ug lyophilized
bs-1369P Peptides: MAP-2(microtubule associated protein 2) Protein Length:12-25 amino acids. 200ug lyophilized
E-EL-M1121 Mouse MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
E-EL-Ch2091 Chicken MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
E-EL-P1842 Porcine MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
E-EL-MK1019 Monkey MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
E-EL-H0948 Human MAPτ (Microtubule Associated Protein Tau_Tau Protein) ELISA Kit 96T
SEQ641Hu ELISA Kit for Echinoderm Microtubule Associated Protein Like Protein 2 (EML2) Homo sapiens (Human) 96T
E84641Ra ELISA Kit for Echinoderm Microtubule Associated Protein Like Protein 2 (EML2) Organism: Rattus norvegicus (Rat) 96T
EIAAB35353 Cerebral protein 10,FAM82A2,FAM82C,Homo sapiens,hRMD-3,hucep-10,Human,Protein FAM82A2,Protein FAM82C,Protein tyrosine phosphatase-interacting protein 51,PTPIP51,Regulator of microtubule dynamics prote
MC-734 MAP 2a,b,c (Microtubule Associated Protein) 100 ug
MC-734 MAP 2a,b,c (Microtubule Associated Protein) 100 ug
bs-1534P Peptides: MAP1LC3A(microtubule-associated protein 1 light chain 3) Protein Length:12-25 amino acids. 200ug lyophilized


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur