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 27-MAR-2024, entry version 158. 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; 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 119. DR IntAct; Q66K74; 50. 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; 9606-ENSP00000325313; -. DR PeptideAtlas; Q66K74; -. DR ProteomicsDB; 4197; -. DR ProteomicsDB; 65957; -. [Q66K74-1] DR Pumba; Q66K74; -. DR Antibodypedia; 27783; 225 antibodies from 25 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 AGR; HGNC:15715; -. DR CTD; 55201; -. DR DisGeNET; 55201; -. DR GeneCards; MAP1S; -. DR HGNC; HGNC:15715; MAP1S. DR HPA; ENSG00000130479; Tissue enhanced (testis). 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; GSEEHIH; -. DR OrthoDB; 5305272at2759; -. DR PhylomeDB; Q66K74; -. DR TreeFam; TF350229; -. DR PathwayCommons; Q66K74; -. DR SignaLink; Q66K74; -. DR SIGNOR; Q66K74; -. DR BioGRID-ORCS; 55201; 18 hits in 1170 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 186 other cell types or tissues. DR ExpressionAtlas; Q66K74; baseline and differential. 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 chromosome alignment; 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 PANTHER; PTHR13843; MICROTUBULE-ASSOCIATED PROTEIN; 1. DR PANTHER; PTHR13843:SF11; MICROTUBULE-ASSOCIATED PROTEIN 1S; 1. DR Genevisible; Q66K74; HS. 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 //