MAP1S_HUMAN
ID MAP1S_HUMAN Reviewed; 1059 AA.
AC Q66K74; B4DH53; Q27QB1; Q6NXF1; Q8N3L8; Q8N3W5; Q8NI88; Q96H94; Q96IT4;
AC Q96SP8; Q9BRC6; Q9H928; Q9NVK7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Microtubule-associated protein 1S;
DE Short=MAP-1S;
DE AltName: Full=BPY2-interacting protein 1;
DE AltName: Full=Microtubule-associated protein 8;
DE AltName: Full=Variable charge Y chromosome 2-interacting protein 1;
DE Short=VCY2-interacting protein 1;
DE Short=VCY2IP-1;
DE Contains:
DE RecName: Full=MAP1S heavy chain;
DE Contains:
DE RecName: Full=MAP1S light chain;
GN Name=MAP1S; Synonyms=BPY2IP1, C19orf5, MAP8, VCY2IP1;
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), INTERACTION WITH VCY2, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=14627543; DOI=10.1095/biolreprod.103.018531;
RA Wong E.Y., Tse J.Y., Yao K.-M., Lui V.C., Tam P.-C., Yeung W.S.;
RT "Identification and characterization of a VCY2 interacting protein-1;
RT VCY2IP-1, a MAP-like protein.";
RL Biol. Reprod. 70:775-784(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=16297881; DOI=10.1016/j.bbrc.2005.10.199;
RA Ding J., Valle A., Allen E., Wang W., Nardine T., Zhang Y., Peng L.,
RA Yang Y.;
RT "Microtubule-associated protein 8 contains two microtubule binding sites.";
RL Biochem. Biophys. Res. Commun. 339:172-179(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain;
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 MRNA] (ISOFORM 1).
RC TISSUE=Amygdala;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT CYS-411.
RC TISSUE=Brain, Lung, Lymph, and Muscle;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 314-1059 (ISOFORM 1/2).
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that recognized by tumor-reactive CTL
RT generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH LRPPRC, AND TISSUE SPECIFICITY.
RX PubMed=11827465; DOI=10.1006/geno.2001.6679;
RA Liu L., McKeehan W.L.;
RT "Sequence analysis of LRPPRC and its SEC1 domain interaction partners
RT suggests roles in cytoskeletal organization, vesicular trafficking,
RT nucleocytosolic shuttling, and chromosome activity.";
RL Genomics 79:124-136(2002).
RN [9]
RP INTERACTION WITH LRPPRC, AND SUBCELLULAR LOCATION.
RX PubMed=12762840; DOI=10.1290/1543-706x(2002)38<582:ncimat>2.0.co;2;
RA Liu L., Amy V., Liu G., McKeehan W.L.;
RT "Novel complex integrating mitochondria and the microtubular cytoskeleton
RT with chromosome remodeling and tumor suppressor RASSF1 deduced by in silico
RT homology analysis, interaction cloning in yeast, and colocalization in
RT cultured cells.";
RL In Vitro Cell. Dev. Biol. Anim. 38:582-594(2002).
RN [10]
RP INTERACTION WITH RASSF1.
RX PubMed=15205320; DOI=10.1158/0008-5472.can-04-0267;
RA Dallol A., Agathanggelou A., Fenton S.L., Ahmed-Choudhury J., Hesson L.,
RA Vos M.D., Clark G.J., Downward J., Maher E.R., Latif F.;
RT "RASSF1A interacts with microtubule-associated proteins and modulates
RT microtubule dynamics.";
RL Cancer Res. 64:4112-4116(2004).
RN [11]
RP INTERACTION WITH LRPPRC, AND DNA-BINDING.
RX PubMed=15907802; DOI=10.1016/j.bbrc.2005.05.006;
RA Liu L., Vo A., Liu G., McKeehan W.L.;
RT "Putative tumor suppressor RASSF1 interactive protein and cell death
RT inducer C19ORF5 is a DNA binding protein.";
RL Biochem. Biophys. Res. Commun. 332:670-676(2005).
RN [12]
RP INTERACTION WITH RASSF1, AND SUBCELLULAR LOCATION.
RX PubMed=15753381; DOI=10.1158/0008-5472.can-04-3896;
RA Liu L., Vo A., McKeehan W.L.;
RT "Specificity of the methylation-suppressed A isoform of candidate tumor
RT suppressor RASSF1 for microtubule hyperstabilization is determined by cell
RT death inducer C19ORF5.";
RL Cancer Res. 65:1830-1838(2005).
RN [13]
RP FUNCTION, INTERACTION WITH MICROTUBULES, AND SUBCELLULAR LOCATION.
RX PubMed=15899810; DOI=10.1158/0008-5472.can-04-3865;
RA Liu L., Vo A., Liu G., McKeehan W.L.;
RT "Distinct structural domains within C19ORF5 support association with
RT stabilized microtubules and mitochondrial aggregation and genome
RT destruction.";
RL Cancer Res. 65:4191-4201(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP INTERACTION WITH ESR1, AND TISSUE SPECIFICITY.
RX PubMed=17658481; DOI=10.1016/j.bbrc.2007.06.179;
RA Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L.,
RA Benedikz E., Sundstroem E.;
RT "The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in
RT the brain.";
RL Biochem. Biophys. Res. Commun. 361:127-132(2007).
RN [16]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17234756; DOI=10.1158/0008-5472.can-06-3604;
RA Dallol A., Cooper W.N., Al-Mulla F., Agathanggelou A., Maher E.R.,
RA Latif F.;
RT "Depletion of the Ras association domain family 1, isoform A-associated
RT novel microtubule-associated protein, C19ORF5/MAP1S, causes mitotic
RT abnormalities.";
RL Cancer Res. 67:492-500(2007).
RN [17]
RP CLEAVAGE SITE.
RX PubMed=18419581; DOI=10.1042/bj20071449;
RA Zou B., Yan H., Kawasaki F., Ordway R.W.;
RT "MAP1 structural organization in Drosophila: in vivo analysis of FUTSCH
RT reveals heavy- and light-chain subunits generated by proteolytic processing
RT at a conserved cleavage site.";
RL Biochem. J. 414:63-71(2008).
RN [18]
RP SUBCELLULAR LOCATION.
RX PubMed=18445686; DOI=10.1242/jcs.019174;
RA Tegha-Dunghu J., Neumann B., Reber S., Krause R., Erfle H., Walter T.,
RA Held M., Rogers P., Hupfeld K., Ruppert T., Ellenberg J., Gruss O.J.;
RT "EML3 is a nuclear microtubule-binding protein required for the correct
RT alignment of chromosomes in metaphase.";
RL J. Cell Sci. 121:1718-1726(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND IDENTIFICATION BY
RP 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 [20]
RP IDENTIFICATION BY 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 [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-640; SER-657 AND
RP SER-759, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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 [22]
RP IDENTIFICATION BY MASS SPECTROMETRY [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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.m800588-mcp200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [24]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759 AND SER-809, AND
RP 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 [26]
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 [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-657; SER-759 AND
RP SER-809, AND IDENTIFICATION BY 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 [28]
RP INTERACTION WITH WDR47.
RX PubMed=22523538; DOI=10.1371/journal.pone.0033094;
RA Wang W., Lundin V.F., Millan I., Zeng A., Chen X., Yang J., Allen E.,
RA Chen N., Bach G., Hsu A., Maloney M.T., Kapur M., Yang Y.;
RT "Nemitin, a novel Map8/Map1s interacting protein with Wd40 repeats.";
RL PLoS ONE 7:E33094-E33094(2012).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-472; SER-582;
RP THR-638; SER-640; SER-655; SER-657 AND SER-759, AND IDENTIFICATION BY MASS
RP 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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-321; SER-657; SER-759 AND
RP SER-809, AND 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).
CC -!- FUNCTION: Microtubule-associated protein that mediates aggregation of
CC mitochondria resulting in cell death and genomic destruction (MAGD).
CC Plays a role in anchoring the microtubule organizing center to the
CC centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the
CC formation of microtubule bundles (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:15899810, ECO:0000269|PubMed:17234756}.
CC -!- SUBUNIT: Heterodimer of a heavy and a light chain. Interacts with
CC microtubules and actin. Both MAP1S heavy and light chains interact with
CC microtubules. MAP1S light chain interacts with actin. Interacts (via C-
CC terminus) with GAN (via Kelch domains) (By similarity). Interacts with
CC ESR1, LRPPRC, RASSF1 isoform A and isoform C, microtubules and VCY2.
CC Interacts with WDR47 (via N-terminus of light chain). {ECO:0000250,
CC ECO:0000269|PubMed:11827465, ECO:0000269|PubMed:12762840,
CC ECO:0000269|PubMed:14627543, ECO:0000269|PubMed:15205320,
CC ECO:0000269|PubMed:15753381, ECO:0000269|PubMed:15899810,
CC ECO:0000269|PubMed:15907802, ECO:0000269|PubMed:17658481,
CC ECO:0000269|PubMed:22523538}.
CC -!- INTERACTION:
CC Q66K74; O14599: BPY2B; NbExp=3; IntAct=EBI-2133734, EBI-2133713;
CC Q66K74; Q9H492: MAP1LC3A; NbExp=3; IntAct=EBI-2133734, EBI-720768;
CC Q66K74; O14543: SOCS3; NbExp=6; IntAct=EBI-2133734, EBI-714146;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Cytoplasm,
CC cytoskeleton {ECO:0000269|PubMed:18445686}. Cytoplasm, cytoskeleton,
CC spindle {ECO:0000269|PubMed:18445686}. Note=Detected in filopodia-like
CC protrusions and synapses (By similarity). Detected in perinuclear
CC punctate network corresponding to mitochondrial aggregates and in the
CC nucleus in cells exhibiting apoptosis. Associated specifically with
CC microtubules stabilized by paclitaxel and colocalizes with RASSF1
CC isoform A. In interphase cells, shows a diffuse cytoplasmic staining
CC with partial localization to the microtubules. During the different
CC stages of mitosis detected at the spindle microtubules. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66K74-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66K74-2; Sequence=VSP_056043;
CC -!- TISSUE SPECIFICITY: Expressed in neurons (at protein level). Expressed
CC in spermatocytes, spermatids and spermatozoa. Expressed in the cerebral
CC cortex. Highly expressed in testis. Moderately expressed in the brain,
CC colon, heart, kidney, liver, lung, placenta, small intestine, spleen
CC and stomach. Weakly expressed in muscle. {ECO:0000269|PubMed:11827465,
CC ECO:0000269|PubMed:14627543, ECO:0000269|PubMed:17658481}.
CC -!- DOMAIN: The N-terminus of the heavy chain associates with the C-
CC terminus of the light chain to form the heterodimer complex (By
CC similarity). Its C-terminal part of the heavy chain interacts with
CC ESR1. {ECO:0000250}.
CC -!- MISCELLANEOUS: Depletion of MAP1S by RNAi causes mitotic abnormalities
CC that consist of failure to form a stable metaphase plate, premature
CC sister chromatid separation, lagging chromosomes, and multipolar
CC spindles.
CC -!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07253.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH07253.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. At the N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH67115.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA91743.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14415.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB55242.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAB93493.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAD38911.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AJ440784; CAD29574.1; -; mRNA.
DR EMBL; DQ387861; ABD47682.1; -; mRNA.
DR EMBL; AK027623; BAB55242.1; ALT_FRAME; mRNA.
DR EMBL; AK001531; BAA91743.1; ALT_INIT; mRNA.
DR EMBL; AK023118; BAB14415.1; ALT_INIT; mRNA.
DR EMBL; AK294936; BAG58014.1; -; mRNA.
DR EMBL; AL834233; CAD38911.1; ALT_INIT; mRNA.
DR EMBL; AC008761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC006358; AAH06358.2; -; mRNA.
DR EMBL; BC007253; AAH07253.1; ALT_INIT; mRNA.
DR EMBL; BC008806; AAH08806.2; -; mRNA.
DR EMBL; BC067115; AAH67115.1; ALT_INIT; mRNA.
DR EMBL; BC080547; AAH80547.1; -; mRNA.
DR EMBL; BC113952; AAI13953.1; -; mRNA.
DR EMBL; AB062430; BAB93493.1; ALT_INIT; mRNA.
DR CCDS; CCDS32954.1; -. [Q66K74-1]
DR CCDS; CCDS77262.1; -. [Q66K74-2]
DR RefSeq; NP_001295292.1; NM_001308363.1. [Q66K74-2]
DR RefSeq; NP_060644.4; NM_018174.5. [Q66K74-1]
DR AlphaFoldDB; Q66K74; -.
DR BioGRID; 120498; 108.
DR IntAct; Q66K74; 49.
DR MINT; Q66K74; -.
DR STRING; 9606.ENSP00000325313; -.
DR GlyGen; Q66K74; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q66K74; -.
DR MetOSite; Q66K74; -.
DR PhosphoSitePlus; Q66K74; -.
DR BioMuta; MAP1S; -.
DR DMDM; 160410004; -.
DR EPD; Q66K74; -.
DR jPOST; Q66K74; -.
DR MassIVE; Q66K74; -.
DR MaxQB; Q66K74; -.
DR PaxDb; Q66K74; -.
DR PeptideAtlas; Q66K74; -.
DR PRIDE; Q66K74; -.
DR ProteomicsDB; 4197; -.
DR ProteomicsDB; 65957; -. [Q66K74-1]
DR Antibodypedia; 27783; 201 antibodies from 24 providers.
DR DNASU; 55201; -.
DR Ensembl; ENST00000324096.9; ENSP00000325313.3; ENSG00000130479.11. [Q66K74-1]
DR Ensembl; ENST00000544059.2; ENSP00000439243.1; ENSG00000130479.11. [Q66K74-2]
DR GeneID; 55201; -.
DR KEGG; hsa:55201; -.
DR MANE-Select; ENST00000324096.9; ENSP00000325313.3; NM_018174.6; NP_060644.4.
DR UCSC; uc002nhe.2; human. [Q66K74-1]
DR CTD; 55201; -.
DR DisGeNET; 55201; -.
DR GeneCards; MAP1S; -.
DR HGNC; HGNC:15715; MAP1S.
DR HPA; ENSG00000130479; Tissue enhanced (brain).
DR MIM; 607573; gene.
DR neXtProt; NX_Q66K74; -.
DR OpenTargets; ENSG00000130479; -.
DR PharmGKB; PA38031; -.
DR VEuPathDB; HostDB:ENSG00000130479; -.
DR eggNOG; KOG3592; Eukaryota.
DR GeneTree; ENSGT00940000160221; -.
DR HOGENOM; CLU_000285_2_0_1; -.
DR InParanoid; Q66K74; -.
DR OMA; ECGCSGL; -.
DR OrthoDB; 86642at2759; -.
DR PhylomeDB; Q66K74; -.
DR TreeFam; TF350229; -.
DR PathwayCommons; Q66K74; -.
DR SignaLink; Q66K74; -.
DR SIGNOR; Q66K74; -.
DR BioGRID-ORCS; 55201; 16 hits in 1085 CRISPR screens.
DR ChiTaRS; MAP1S; human.
DR GeneWiki; MAP1S; -.
DR GenomeRNAi; 55201; -.
DR Pharos; Q66K74; Tbio.
DR PRO; PR:Q66K74; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q66K74; protein.
DR Bgee; ENSG00000130479; Expressed in right testis and 184 other tissues.
DR ExpressionAtlas; Q66K74; baseline and differential.
DR Genevisible; Q66K74; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0042995; C:cell projection; IDA:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:ARUK-UCL.
DR GO; GO:0005829; C:cytosol; IDA:HGNC-UCL.
DR GO; GO:0030425; C:dendrite; ISS:HGNC-UCL.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0005815; C:microtubule organizing center; IDA:ARUK-UCL.
DR GO; GO:1990498; C:mitotic spindle microtubule; IDA:ARUK-UCL.
DR GO; GO:0043025; C:neuronal cell body; ISS:HGNC-UCL.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:HGNC-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC-UCL.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; IDA:HGNC-UCL.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:HGNC-UCL.
DR GO; GO:0003677; F:DNA binding; IDA:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0008017; F:microtubule binding; IDA:HGNC-UCL.
DR GO; GO:0015631; F:tubulin binding; IDA:HGNC-UCL.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006914; P:autophagy; TAS:BHF-UCL.
DR GO; GO:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; ISS:HGNC-UCL.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0051310; P:metaphase plate congression; IMP:ARUK-UCL.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; IMP:ARUK-UCL.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:HGNC-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; TAS:HGNC-UCL.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:ARUK-UCL.
DR GO; GO:0007399; P:nervous system development; ISS:HGNC-UCL.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEP:HGNC-UCL.
DR GO; GO:0031114; P:regulation of microtubule depolymerization; IBA:GO_Central.
DR InterPro; IPR026074; MAP1.
DR InterPro; IPR027322; MAP1S.
DR PANTHER; PTHR13843; PTHR13843; 2.
DR PANTHER; PTHR13843:SF11; PTHR13843:SF11; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Apoptosis; Cytoplasm; Cytoskeleton; DNA-binding;
KW Microtubule; Nucleus; Phosphoprotein; Reference proteome.
FT CHAIN 1..1059
FT /note="Microtubule-associated protein 1S"
FT /id="PRO_0000311379"
FT CHAIN 1..829
FT /note="MAP1S heavy chain"
FT /id="PRO_0000311380"
FT CHAIN 830..1059
FT /note="MAP1S light chain"
FT /id="PRO_0000311381"
FT REGION 1..797
FT /note="Necessary for the microtubule-organizing center
FT localization"
FT REGION 461..733
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 666..1059
FT /note="Necessary for interaction with RASSF1 isoform A and
FT isoform C"
FT REGION 714..966
FT /note="Necessary for association with microtubules"
FT REGION 751..942
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 960..1059
FT /note="Necessary for association with actin"
FT /evidence="ECO:0000250"
FT REGION 967..991
FT /note="Necessary for the mitochondrial aggregation and
FT genome destruction"
FT COMPBIAS 467..537
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 539..554
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 669..708
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 824..839
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..940
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 321
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 582
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 638
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 640
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 655
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 731
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C052"
FT MOD_RES 759
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18220336,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19369195,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 809
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..39
FT /note="MAAVAGSGAAAAPSSLLLVVGSEFGSPGLLTYVLEELER -> MAGMIDRFS
FT PANT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056043"
FT VARIANT 372
FT /note="L -> V (in dbSNP:rs17710707)"
FT /id="VAR_050023"
FT VARIANT 411
FT /note="S -> C (in dbSNP:rs17710707)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_037236"
FT VARIANT 538
FT /note="P -> Q (in dbSNP:rs7252905)"
FT /id="VAR_037237"
FT CONFLICT 120
FT /note="P -> L (in Ref. 1; CAD29574 and 3; BAB55242)"
FT /evidence="ECO:0000305"
FT CONFLICT 178
FT /note="L -> P (in Ref. 1; CAD29574 and 3; BAB55242)"
FT /evidence="ECO:0000305"
FT CONFLICT 440
FT /note="C -> Y (in Ref. 4; CAD38911)"
FT /evidence="ECO:0000305"
FT CONFLICT 521
FT /note="T -> A (in Ref. 7; BAB93493)"
FT /evidence="ECO:0000305"
FT CONFLICT 526
FT /note="K -> R (in Ref. 1; CAD29574 and 3; BAB55242)"
FT /evidence="ECO:0000305"
FT CONFLICT 967
FT /note="F -> L (in Ref. 3; BAB14415)"
FT /evidence="ECO:0000305"
FT CONFLICT 1043
FT /note="S -> G (in Ref. 3; BAA91743)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1059 AA; 112211 MW; 30AB33FFE26DDF91 CRC64;
MAAVAGSGAA AAPSSLLLVV GSEFGSPGLL TYVLEELERG IRSWDVDPGV CNLDEQLKVF
VSRHSATFSS IVKGQRSLHH RGDNLETLVL LNPSDKSLYD ELRNLLLDPA SHKLLVLAGP
CLEETGELLL QTGGFSPHHF LQVLKDREIR DILATTPPPV QPPILTITCP TFGDWAQLAP
AVPGLQGALR LQLRLNPPAQ LPNSEGLCEF LEYVAESLEP PSPFELLEPP TSGGFLRLGR
PCCYIFPGGL GDAAFFAVNG FTVLVNGGSN PKSSFWKLVR HLDRVDAVLV THPGADSLPG
LNSLLRRKLA ERSEVAAGGG SWDDRLRRLI SPNLGVVFFN ACEAASRLAR GEDEAELALS
LLAQLGITPL PLSRGPVPAK PTVLFEKMGV GRLDMYVLHP PSAGAERTLA SVCALLVWHP
AGPGEKVVRV LFPGCTPPAC LLDGLVRLQH LRFLREPVVT PQDLEGPGRA ESKESVGSRD
SSKREGLLAT HPRPGQERPG VARKEPARAE APRKTEKEAK TPRELKKDPK PSVSRTQPRE
VRRAASSVPN LKKTNAQAAP KPRKAPSTSH SGFPPVANGP RSPPSLRCGE ASPPSAACGS
PASQLVATPS LELGPIPAGE EKALELPLAA SSIPRPRTPS PESHRSPAEG SERLSLSPLR
GGEAGPDASP TVTTPTVTTP SLPAEVGSPH STEVDESLSV SFEQVLPPSA PTSEAGLSLP
LRGPRARRSA SPHDVDLCLV SPCEFEHRKA VPMAPAPASP GSSNDSSARS QERAGGLGAE
ETPPTSVSES LPTLSDSDPV PLAPGAADSD EDTEGFGVPR HDPLPDPLKV PPPLPDPSSI
CMVDPEMLPP KTARQTENVS RTRKPLARPN SRAAAPKATP VAAAKTKGLA GGDRASRPLS
ARSEPSEKGG RAPLSRKSST PKTATRGPSG SASSRPGVSA TPPKSPVYLD LAYLPSGSSA
HLVDEEFFQR VRALCYVISG QDQRKEEGMR AVLDALLASK QHWDRDLQVT LIPTFDSVAM
HTWYAETHAR HQALGITVLG SNSMVSMQDD AFPACKVEF
