ID MAP7_HUMAN Reviewed; 749 AA.
AC Q14244; B7Z290; B7Z400; B7Z5S7; B7Z9U7; C9JPS0; E9PCP3; F5H1E2; Q7Z6S0;
AC Q8TAU5; Q9NY82; Q9NY83;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 182.
DE RecName: Full=Ensconsin;
DE AltName: Full=Epithelial microtubule-associated protein of 115 kDa;
DE Short=E-MAP-115;
DE AltName: Full=Microtubule-associated protein 7;
DE Short=MAP-7;
GN Name=MAP7;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8408219; DOI=10.1083/jcb.123.2.357;
RA Masson D., Kreis T.E.;
RT "Identification and molecular characterization of E-MAP-115, a novel
RT microtubule-associated protein predominantly expressed in epithelial
RT cells.";
RL J. Cell Biol. 123:357-371(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
RA Fabre-Jonca N., Masson D.;
RT "Novel features of E-MAP-115 revealed by the characterization of its
RT variants E-MAP-115/105 and E-MAP-115/95.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5; 6 AND 7), AND
RP VARIANT TRP-558.
RC TISSUE=Amygdala, Hippocampus, and Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT TRP-558.
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION.
RX PubMed=7490279; DOI=10.1083/jcb.131.4.1015;
RA Masson D., Kreis T.E.;
RT "Binding of E-MAP-115 to microtubules is regulated by cell cycle-dependent
RT phosphorylation.";
RL J. Cell Biol. 131:1015-1024(1995).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=9989799; DOI=10.1046/j.1523-1747.1999.00500.x;
RA Fabre-Jonca N., Viard I., French L.E., Masson D.;
RT "Upregulation and redistribution of E-MAP-115 (epithelial microtubule-
RT associated protein of 115 kDa) in terminally differentiating keratinocytes
RT is coincident with the formation of intercellular contacts.";
RL J. Invest. Dermatol. 112:216-225(1999).
RN [8]
RP FUNCTION.
RX PubMed=11719555; DOI=10.1242/jcs.114.21.3885;
RA Bulinski J.C., Odde D.J., Howell B.J., Salmon T.D., Waterman-Storer C.M.;
RT "Rapid dynamics of the microtubule binding of ensconsin in vivo.";
RL J. Cell Sci. 114:3885-3897(2001).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-219; SER-254 AND
RP THR-277, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-219, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209 AND SER-219, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-219; THR-231;
RP SER-254 AND THR-277, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-209; SER-219; THR-277 AND
RP THR-673, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-183, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-165; SER-183;
RP SER-200; SER-202; SER-209; SER-219; THR-231; THR-277; SER-282; SER-335 AND
RP SER-365, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-365, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-406, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-406, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-406, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-273; LYS-295; LYS-373; LYS-377
RP AND LYS-406, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Microtubule-stabilizing protein that may play an important
CC role during reorganization of microtubules during polarization and
CC differentiation of epithelial cells. Associates with microtubules in a
CC dynamic manner. May play a role in the formation of intercellular
CC contacts. Colocalization with TRPV4 results in the redistribution of
CC TRPV4 toward the membrane and may link cytoskeletal microfilaments.
CC {ECO:0000269|PubMed:11719555, ECO:0000269|PubMed:8408219,
CC ECO:0000269|PubMed:9989799}.
CC -!- SUBUNIT: Interacts with TRPV4. {ECO:0000250}.
CC -!- INTERACTION:
CC Q14244; Q6NSX1: CCDC70; NbExp=3; IntAct=EBI-2211064, EBI-6873045;
CC Q14244; Q8N3C7: CLIP4; NbExp=3; IntAct=EBI-2211064, EBI-5655540;
CC Q14244; Q8NC26: ZNF114; NbExp=3; IntAct=EBI-2211064, EBI-10265237;
CC Q14244; A0A0H3JP21: espL2; Xeno; NbExp=4; IntAct=EBI-2211064, EBI-13951059;
CC Q14244; Q8XBX8: nleB1; Xeno; NbExp=4; IntAct=EBI-2211064, EBI-10039153;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Basolateral cell
CC membrane. Cytoplasm, cytoskeleton. Note=Colocalized on microtubules. An
CC intracellular redistribution is triggered during induction of
CC keratinocyte terminal differentiation from microtubules with a
CC perinuclear localization to cortical microtubules organized in spike-
CC like bundles facing intercellular contacts.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1;
CC IsoId=Q14244-1; Sequence=Displayed;
CC Name=2; Synonyms=E-MAP-115-105;
CC IsoId=Q14244-2; Sequence=VSP_021317;
CC Name=3; Synonyms=E-MAP-115-95;
CC IsoId=Q14244-3; Sequence=VSP_021316;
CC Name=4;
CC IsoId=Q14244-4; Sequence=VSP_043336, VSP_021317;
CC Name=5;
CC IsoId=Q14244-5; Sequence=VSP_043335;
CC Name=6;
CC IsoId=Q14244-6; Sequence=VSP_046758;
CC Name=7;
CC IsoId=Q14244-7; Sequence=VSP_043336;
CC -!- TISSUE SPECIFICITY: Expressed in the skin and cells of epithelial
CC origin. Predominantly expressed in the suprabasal layers of the normal
CC epidermis and relatively abundant in squamous cell carcinomas but
CC barely detectable in basal cell carcinomas.
CC {ECO:0000269|PubMed:8408219, ECO:0000269|PubMed:9989799}.
CC -!- INDUCTION: Up-regulated upon terminal differentiation of primary
CC keratinocytes.
CC -!- PTM: The association with microtubules is regulated by phosphorylation
CC during the cell cycle. During interphase only phosphorylated on serine.
CC Phosphorylated on threonine in mitosis. {ECO:0000269|PubMed:7490279}.
CC -!- SIMILARITY: Belongs to the MAP7 family. {ECO:0000305}.
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DR EMBL; X73882; CAA52086.1; -; mRNA.
DR EMBL; AJ242501; CAB88030.1; -; mRNA.
DR EMBL; AJ242502; CAB88031.1; -; mRNA.
DR EMBL; AK294461; BAH11776.1; -; mRNA.
DR EMBL; AK296556; BAH12386.1; -; mRNA.
DR EMBL; AK299355; BAH13013.1; -; mRNA.
DR EMBL; AK316062; BAH14433.1; -; mRNA.
DR EMBL; AL024508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL023284; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133511; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025777; AAH25777.1; -; mRNA.
DR CCDS; CCDS5178.1; -. [Q14244-1]
DR CCDS; CCDS56452.1; -. [Q14244-5]
DR CCDS; CCDS56453.1; -. [Q14244-6]
DR CCDS; CCDS56454.1; -. [Q14244-4]
DR CCDS; CCDS56455.1; -. [Q14244-7]
DR CCDS; CCDS75528.1; -. [Q14244-3]
DR CCDS; CCDS75529.1; -. [Q14244-2]
DR PIR; I37356; I37356.
DR RefSeq; NP_001185537.1; NM_001198608.1. [Q14244-7]
DR RefSeq; NP_001185538.1; NM_001198609.1.
DR RefSeq; NP_001185540.1; NM_001198611.1. [Q14244-4]
DR RefSeq; NP_001185543.1; NM_001198614.1. [Q14244-7]
DR RefSeq; NP_001185544.1; NM_001198615.1. [Q14244-6]
DR RefSeq; NP_001185545.1; NM_001198616.1. [Q14244-2]
DR RefSeq; NP_001185546.1; NM_001198617.1. [Q14244-3]
DR RefSeq; NP_001185547.1; NM_001198618.1. [Q14244-5]
DR RefSeq; NP_001185548.1; NM_001198619.1. [Q14244-5]
DR RefSeq; NP_003971.1; NM_003980.4. [Q14244-1]
DR RefSeq; XP_006715663.1; XM_006715600.2.
DR RefSeq; XP_016866960.1; XM_017011471.1.
DR PDB; 7SGS; EM; 3.30 A; A=1-749.
DR PDBsum; 7SGS; -.
DR AlphaFoldDB; Q14244; -.
DR EMDB; EMD-25120; -.
DR SMR; Q14244; -.
DR BioGRID; 114515; 270.
DR IntAct; Q14244; 60.
DR MINT; Q14244; -.
DR STRING; 9606.ENSP00000482335; -.
DR GlyGen; Q14244; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q14244; -.
DR PhosphoSitePlus; Q14244; -.
DR BioMuta; MAP7; -.
DR DMDM; 74739817; -.
DR EPD; Q14244; -.
DR jPOST; Q14244; -.
DR MassIVE; Q14244; -.
DR MaxQB; Q14244; -.
DR PaxDb; 9606-ENSP00000482335; -.
DR PeptideAtlas; Q14244; -.
DR ProteomicsDB; 19484; -.
DR ProteomicsDB; 25627; -.
DR ProteomicsDB; 59940; -. [Q14244-1]
DR ProteomicsDB; 59941; -. [Q14244-2]
DR ProteomicsDB; 59942; -. [Q14244-3]
DR ProteomicsDB; 59943; -. [Q14244-4]
DR ProteomicsDB; 59944; -. [Q14244-5]
DR Pumba; Q14244; -.
DR Antibodypedia; 33011; 187 antibodies from 24 providers.
DR DNASU; 9053; -.
DR Ensembl; ENST00000354570.8; ENSP00000346581.2; ENSG00000135525.19. [Q14244-1]
DR Ensembl; ENST00000432797.6; ENSP00000414879.2; ENSG00000135525.19. [Q14244-5]
DR Ensembl; ENST00000438100.6; ENSP00000400790.2; ENSG00000135525.19. [Q14244-4]
DR Ensembl; ENST00000454590.5; ENSP00000414712.1; ENSG00000135525.19. [Q14244-7]
DR Ensembl; ENST00000544465.5; ENSP00000445737.1; ENSG00000135525.19. [Q14244-6]
DR Ensembl; ENST00000611373.1; ENSP00000482998.1; ENSG00000135525.19. [Q14244-5]
DR Ensembl; ENST00000616617.4; ENSP00000483511.1; ENSG00000135525.19. [Q14244-3]
DR Ensembl; ENST00000618822.4; ENSP00000482356.1; ENSG00000135525.19. [Q14244-2]
DR GeneID; 9053; -.
DR KEGG; hsa:9053; -.
DR MANE-Select; ENST00000354570.8; ENSP00000346581.2; NM_003980.6; NP_003971.1.
DR UCSC; uc003qgz.4; human. [Q14244-1]
DR AGR; HGNC:6869; -.
DR CTD; 9053; -.
DR DisGeNET; 9053; -.
DR GeneCards; MAP7; -.
DR HGNC; HGNC:6869; MAP7.
DR HPA; ENSG00000135525; Tissue enhanced (brain).
DR MIM; 604108; gene.
DR neXtProt; NX_Q14244; -.
DR OpenTargets; ENSG00000135525; -.
DR PharmGKB; PA30615; -.
DR VEuPathDB; HostDB:ENSG00000135525; -.
DR eggNOG; ENOG502QTDQ; Eukaryota.
DR GeneTree; ENSGT00950000182941; -.
DR HOGENOM; CLU_017315_2_1_1; -.
DR InParanoid; Q14244; -.
DR OrthoDB; 4337790at2759; -.
DR PhylomeDB; Q14244; -.
DR TreeFam; TF332273; -.
DR PathwayCommons; Q14244; -.
DR SignaLink; Q14244; -.
DR BioGRID-ORCS; 9053; 14 hits in 1155 CRISPR screens.
DR ChiTaRS; MAP7; human.
DR GeneWiki; MAP7; -.
DR GenomeRNAi; 9053; -.
DR Pharos; Q14244; Tbio.
DR PRO; PR:Q14244; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q14244; Protein.
DR Bgee; ENSG00000135525; Expressed in endothelial cell and 188 other cell types or tissues.
DR ExpressionAtlas; Q14244; baseline and differential.
DR Genevisible; Q14244; HS.
DR GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; TAS:ProtInc.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005102; F:signaling receptor binding; ISS:BHF-UCL.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0007163; P:establishment or maintenance of cell polarity; TAS:ProtInc.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0072659; P:protein localization to plasma membrane; ISS:BHF-UCL.
DR GO; GO:0006970; P:response to osmotic stress; ISS:BHF-UCL.
DR InterPro; IPR008604; MAP7_fam.
DR PANTHER; PTHR15073:SF4; ENSCONSIN; 1.
DR PANTHER; PTHR15073; MICROTUBULE-ASSOCIATED PROTEIN; 1.
DR Pfam; PF05672; MAP7; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Membrane;
KW Microtubule; Phosphoprotein; Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330"
FT CHAIN 2..749
FT /note="Ensconsin"
FT /id="PRO_0000255949"
FT REGION 1..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 104..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 307..688
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 702..723
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 89..152
FT /evidence="ECO:0000255"
FT COILED 477..612
FT /evidence="ECO:0000255"
FT COMPBIAS 33..54
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 59..91
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..322
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 372..394
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 424..452
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 479..625
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 639..688
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 165
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 183
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 200
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 202
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 209
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18220336, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:17924679, ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 231
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 235
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 254
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648"
FT MOD_RES 277
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 282
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 335
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 673
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT CROSSLNK 273
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 373
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 377
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 406
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..146
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043335"
FT VAR_SEQ 1..23
FT /note="MAELGAGGDGHRGGDGAVRSETA -> MEDTKLYS (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046758"
FT VAR_SEQ 1..22
FT /note="MAELGAGGDGHRGGDGAVRSET -> MPGSATALRHERLKKTNARPIPLGLF
FT TINEEDEQQKNGNSRRPK (in isoform 4 and isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_043336"
FT VAR_SEQ 82..175
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_021316"
FT VAR_SEQ 176..212
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_021317"
FT VARIANT 361
FT /note="V -> I (in dbSNP:rs35350783)"
FT /id="VAR_034091"
FT VARIANT 526
FT /note="R -> P (in dbSNP:rs35107962)"
FT /id="VAR_034092"
FT VARIANT 558
FT /note="R -> W (in dbSNP:rs2076190)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_028880"
FT CONFLICT 318
FT /note="N -> D (in Ref. 3; BAH13013)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="Q -> R (in Ref. 3; BAH12386)"
FT /evidence="ECO:0000305"
FT CONFLICT 725
FT /note="F -> S (in Ref. 3; BAH13013)"
FT /evidence="ECO:0000305"
FT HELIX 88..138
FT /evidence="ECO:0007829|PDB:7SGS"
SQ SEQUENCE 749 AA; 84052 MW; CB69BDE25C9540E3 CRC64;
MAELGAGGDG HRGGDGAVRS ETAPDSYKVQ DKKNASSRPA SAISGQNNNH SGNKPDPPPV
LRVDDRQRLA RERREEREKQ LAAREIVWLE REERARQHYE KHLEERKKRL EEQRQKEERR
RAAVEEKRRQ RLEEDKERHE AVVRRTMERS QKPKQKHNRW SWGGSLHGSP SIHSADPDRR
SVSTMNLSKY VDPVISKRLS SSSATLLNSP DRARRLQLSP WESSVVNRLL TPTHSFLARS
KSTAALSGEA ASCSPIIMPY KAAHSRNSMD RPKLFVTPPE GSSRRRIIHG TASYKKERER
ENVLFLTSGT RRAVSPSNPK ARQPARSRLW LPSKSLPHLP GTPRPTSSLP PGSVKAAPAQ
VRPPSPGNIR PVKREVKVEP EKKDPEKEPQ KVANEPSLKG RAPLVKVEEA TVEERTPAEP
EVGPAAPAMA PAPASAPAPA SAPAPAPVPT PAMVSAPSST VNASASVKTS AGTTDPEEAT
RLLAEKRRLA REQREKEERE RREQEELERQ KREELAQRVA EERTTRREEE SRRLEAEQAR
EKEEQLQRQA EERALREREE AERAQRQKEE EARVREEAER VRQEREKHFQ REEQERLERK
KRLEEIMKRT RRTEATDKKT SDQRNGDIAK GALTGGTEVS ALPCTTNAPG NGKPVGSPHV
VTSHQSKVTV ESTPDLEKQP NENGVSVQNE NFEEIINLPI GSKPSRLDVT NSESPEIPLN
PILAFDDEGT LGPLPQVDGV QTQQTAEVI
//
