MTUS1_HUMAN
ID MTUS1_HUMAN Reviewed; 1270 AA.
AC Q9ULD2; A8K135; B2RBJ6; B3KWJ9; B4DH03; B9EGA1; D3DSP8; Q63HJ6; Q659F4;
AC Q6PK49; Q6URW7; Q8N4M6; Q8WTT9; Q9H7T2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Microtubule-associated tumor suppressor 1;
DE AltName: Full=AT2 receptor-binding protein;
DE AltName: Full=Angiotensin-II type 2 receptor-interacting protein;
DE AltName: Full=Mitochondrial tumor suppressor 1;
GN Name=MTUS1; Synonyms=ATBP, ATIP, GK1, KIAA1288, MTSG1;
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), TISSUE SPECIFICITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=10697957; DOI=10.1007/s100380050003;
RA Kinjo T., Isomura M., Iwamasa T., Nakamura Y.;
RT "Molecular cloning and characterization of two novel genes on chromosome
RT 8p21.3.";
RL J. Hum. Genet. 45:12-17(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, TISSUE SPECIFICITY, AND
RP SUBCELLULAR LOCATION.
RX PubMed=12692079; DOI=10.1096/fj.02-0934fje;
RA Seibold S., Rudroff C., Weber M., Galle J., Wanner C., Marx M.;
RT "Identification of a new tumor suppressor gene located at chromosome
RT 8p21.3-22.";
RL FASEB J. 17:1180-1182(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), ALTERNATIVE SPLICING (ISOFORMS 1; 5
RP AND 6), SUBUNIT, AND TISSUE SPECIFICITY.
RC TISSUE=Lung;
RX PubMed=15123706; DOI=10.1074/jbc.m403880200;
RA Nouet S., Amzallag N., Li J.-M., Louis S., Seitz I., Cui T.-X.,
RA Alleaume A.-M., Di Benedetto M., Boden C., Masson M., Strosberg A.D.,
RA Horiuchi M., Couraud P.-O., Nahmias C.;
RT "Trans-inactivation of receptor tyrosine kinases by novel angiotensin II
RT AT2 receptor-interacting protein, ATIP.";
RL J. Biol. Chem. 279:28989-28997(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 6 AND 7), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 875-1270 (ISOFORM 1).
RC TISSUE=Brain, Fetal brain, and Placenta;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 266-1270 (ISOFORM 5).
RC TISSUE=Salivary gland, and Uterus;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-148.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANTS
RP ARG-148 AND THR-1063.
RC TISSUE=Ovary, Skin, and Testis;
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 [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-891 (ISOFORM 2), AND VARIANTS ARG-148 AND
RP ARG-575.
RA Abadie P.A., Genti-Raimondi S.;
RT "Differential expression in normal trophoblast and gestational tumors.";
RL Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 26-1270 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=16270321; DOI=10.1002/cncr.21538;
RA Pils D., Horak P., Gleiss A., Sax C., Fabjani G., Moebus V.J.,
RA Zielinski C., Reinthaller A., Zeillinger R., Krainer M.;
RT "Five genes from chromosomal band 8p22 are significantly down-regulated in
RT ovarian carcinoma: N33 and EFA6R have a potential impact on overall
RT survival.";
RL Cancer 104:2417-2429(2005).
RN [12]
RP ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX PubMed=16887298; DOI=10.1016/j.gene.2006.05.021;
RA Di Benedetto M., Bieche I., Deshayes F., Vacher S., Nouet S., Collura V.,
RA Seitz I., Louis S., Pineau P., Amsellem-Ouazana D., Couraud P.-O.,
RA Strosberg A.D., Stoppa-Lyonnet D., Lidereau R., Nahmias C.;
RT "Structural organization and expression of human MTUS1, a candidate 8p22
RT tumor suppressor gene encoding a family of angiotensin II AT2 receptor-
RT interacting proteins, ATIP.";
RL Gene 380:127-136(2006).
RN [13]
RP TISSUE SPECIFICITY.
RX PubMed=16969489;
RA Lee S., Bang S., Song K., Lee I.;
RT "Differential expression in normal-adenoma-carcinoma sequence suggests
RT complex molecular carcinogenesis in colon.";
RL Oncol. Rep. 16:747-754(2006).
RN [14]
RP 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 [15]
RP IDENTIFICATION BY 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 [16]
RP FUNCTION, ASSOCIATION WITH MICROTUBULES, SUBCELLULAR LOCATION, AND
RP INDUCTION.
RX PubMed=19794912; DOI=10.1371/journal.pone.0007239;
RA Rodrigues-Ferreira S., Di Tommaso A., Dimitrov A., Cazaubon S., Gruel N.,
RA Colasson H., Nicolas A., Chaverot N., Molinie V., Reyal F.,
RA Sigal-Zafrani B., Terris B., Delattre O., Radvanyi F., Perez F.,
RA Vincent-Salomon A., Nahmias C.;
RT "8p22 MTUS1 gene product ATIP3 is a novel anti-mitotic protein
RT underexpressed in invasive breast carcinoma of poor prognosis.";
RL PLoS ONE 4:E7239-E7239(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1264 AND SER-1268, AND
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1224 AND SER-1268, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-399; SER-443 AND SER-1268,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-186; SER-629 AND SER-1245,
RP 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).
RN [21]
RP VARIANTS HCC LYS-75; SER-563; HIS-873 AND ARG-1201, AND VARIANTS ARG-148;
RP MET-425; THR-453; ARG-575; THR-911 AND GLN-1105.
RX PubMed=16650523; DOI=10.1016/j.mce.2006.03.014;
RA Di Benedetto M., Pineau P., Nouet S., Berhouet S., Seitz I., Louis S.,
RA Dejean A., Couraud P.-O., Strosberg A.D., Stoppa-Lyonnet D., Nahmias C.;
RT "Mutation analysis of the 8p22 candidate tumor suppressor gene ATIP/MTUS1
RT in hepatocellular carcinoma.";
RL Mol. Cell. Endocrinol. 252:207-215(2006).
RN [22]
RP VARIANTS ARG-148 AND THR-453, VARIANT HNSCC SER-186, AND TISSUE
RP SPECIFICITY.
RX PubMed=17656251; DOI=10.1016/j.cancergencyto.2007.04.003;
RA Ye H., Pungpravat N., Huang B.-L., Muzio L.L., Mariggio M.A., Chen Z.,
RA Wong D.T., Zhou X.;
RT "Genomic assessments of the frequent loss of heterozygosity region on
RT 8p21.3 approximately p22 in head and neck squamous cell carcinoma.";
RL Cancer Genet. Cytogenet. 176:100-106(2007).
CC -!- FUNCTION: Cooperates with AGTR2 to inhibit ERK2 activation and cell
CC proliferation. May be required for AGTR2 cell surface expression.
CC Together with PTPN6, induces UBE2V2 expression upon angiotensin-II
CC stimulation. Isoform 1 inhibits breast cancer cell proliferation,
CC delays the progression of mitosis by prolonging metaphase and reduces
CC tumor growth. {ECO:0000269|PubMed:12692079,
CC ECO:0000269|PubMed:19794912}.
CC -!- SUBUNIT: Homodimer. Interacts with AGTR2. Interacts with PTPN6 (By
CC similarity). Isoform 1 associates with microtubules. {ECO:0000250,
CC ECO:0000269|PubMed:15123706}.
CC -!- INTERACTION:
CC Q9ULD2-3; P42858: HTT; NbExp=3; IntAct=EBI-18051665, EBI-466029;
CC Q9ULD2-3; P63208: SKP1; NbExp=3; IntAct=EBI-18051665, EBI-307486;
CC Q9ULD2-3; Q13190: STX5; NbExp=3; IntAct=EBI-18051665, EBI-714206;
CC Q9ULD2-3; O15400: STX7; NbExp=3; IntAct=EBI-18051665, EBI-3221827;
CC Q9ULD2-4; P42858: HTT; NbExp=9; IntAct=EBI-25866497, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10697957,
CC ECO:0000269|PubMed:12692079, ECO:0000269|PubMed:19794912}. Golgi
CC apparatus {ECO:0000250}. Cell membrane {ECO:0000250}. Nucleus
CC {ECO:0000250}. Note=In neurons, translocates into the nucleus after
CC treatment with angiotensin-II. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Cytoplasm, cytoskeleton, spindle.
CC Note=Localizes with the mitotic spindle during mitosis and with the
CC intercellular bridge during cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=7;
CC Name=1; Synonyms=ATIP3a;
CC IsoId=Q9ULD2-1; Sequence=Displayed;
CC Name=2; Synonyms=ATIP3b;
CC IsoId=Q9ULD2-2; Sequence=VSP_028274;
CC Name=3; Synonyms=ATIP1;
CC IsoId=Q9ULD2-3; Sequence=VSP_028271, VSP_028277;
CC Name=4;
CC IsoId=Q9ULD2-4; Sequence=VSP_028270, VSP_028278;
CC Name=5; Synonyms=ATIP2;
CC IsoId=Q9ULD2-5; Sequence=VSP_028275, VSP_028276;
CC Name=6; Synonyms=ATIP4;
CC IsoId=Q9ULD2-6; Sequence=VSP_028272, VSP_028273;
CC Name=7;
CC IsoId=Q9ULD2-7; Sequence=VSP_044849;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed (at protein level). Highly
CC expressed in brain. Down-regulated in ovarian carcinoma, pancreas
CC carcinoma, colon carcinoma and head and neck squamous cell carcinoma
CC (HNSCC). Isoform 1 is the major isoform in most peripheral tissues.
CC Isoform 2 is abundant in most peripheral tissues. Isoform 3 is the
CC major isoform in brain, female reproductive tissues, thyroid and heart.
CC Within brain it is highly expressed in corpus callosum and pons.
CC Isoform 6 is brain-specific, it is the major isoform in cerebellum and
CC fetal brain. {ECO:0000269|PubMed:10697957, ECO:0000269|PubMed:12692079,
CC ECO:0000269|PubMed:15123706, ECO:0000269|PubMed:16270321,
CC ECO:0000269|PubMed:16887298, ECO:0000269|PubMed:16969489,
CC ECO:0000269|PubMed:17656251}.
CC -!- INDUCTION: [Isoform 1]: Down-regulated in invasive breast carcinomas
CC (at protein level). {ECO:0000269|PubMed:19794912}.
CC -!- DISEASE: Hepatocellular carcinoma (HCC) [MIM:114550]: A primary
CC malignant neoplasm of epithelial liver cells. The major risk factors
CC for HCC are chronic hepatitis B virus (HBV) infection, chronic
CC hepatitis C virus (HCV) infection, prolonged dietary aflatoxin
CC exposure, alcoholic cirrhosis, and cirrhosis due to other causes.
CC {ECO:0000269|PubMed:16650523}. Note=The gene represented in this entry
CC may be involved in disease pathogenesis.
CC -!- MISCELLANEOUS: [Isoform 5]: Expressed at very low levels in most
CC tissues. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the MTUS1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07328.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH33842.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14894.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/MTUS1ID41451ch8p22.html";
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DR EMBL; AF121259; AAG33674.1; -; mRNA.
DR EMBL; AF293357; AAL37035.1; -; mRNA.
DR EMBL; AK024357; BAB14894.1; ALT_INIT; mRNA.
DR EMBL; AK125188; BAG54161.1; -; mRNA.
DR EMBL; AK289750; BAF82439.1; -; mRNA.
DR EMBL; AK294860; BAG57964.1; -; mRNA.
DR EMBL; AK314692; BAG37243.1; -; mRNA.
DR EMBL; AL096842; CAB50791.1; -; mRNA.
DR EMBL; BX648879; CAH56128.1; -; mRNA.
DR EMBL; AC027117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124069; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471080; EAW63804.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63805.1; -; Genomic_DNA.
DR EMBL; CH471080; EAW63810.1; -; Genomic_DNA.
DR EMBL; BC007328; AAH07328.1; ALT_SEQ; mRNA.
DR EMBL; BC033842; AAH33842.1; ALT_INIT; mRNA.
DR EMBL; BC136320; AAI36321.1; -; mRNA.
DR EMBL; BC142971; AAI42972.1; -; mRNA.
DR EMBL; AY363099; AAQ24172.1; -; mRNA.
DR EMBL; AB033114; BAA86602.1; -; mRNA.
DR CCDS; CCDS43716.1; -. [Q9ULD2-2]
DR CCDS; CCDS43717.1; -. [Q9ULD2-1]
DR CCDS; CCDS43718.1; -. [Q9ULD2-6]
DR CCDS; CCDS43719.1; -. [Q9ULD2-3]
DR CCDS; CCDS55204.1; -. [Q9ULD2-7]
DR CCDS; CCDS83254.1; -. [Q9ULD2-4]
DR RefSeq; NP_001001924.1; NM_001001924.2. [Q9ULD2-1]
DR RefSeq; NP_001001925.1; NM_001001925.2. [Q9ULD2-2]
DR RefSeq; NP_001001931.1; NM_001001931.2. [Q9ULD2-6]
DR RefSeq; NP_001159865.1; NM_001166393.1. [Q9ULD2-7]
DR RefSeq; NP_001317399.1; NM_001330470.1. [Q9ULD2-4]
DR RefSeq; NP_065800.1; NM_020749.4. [Q9ULD2-3]
DR RefSeq; XP_005273636.1; XM_005273579.3.
DR RefSeq; XP_005273639.1; XM_005273582.3.
DR RefSeq; XP_016869189.1; XM_017013700.1.
DR RefSeq; XP_016869190.1; XM_017013701.1.
DR RefSeq; XP_016869191.1; XM_017013702.1.
DR AlphaFoldDB; Q9ULD2; -.
DR SMR; Q9ULD2; -.
DR BioGRID; 121573; 109.
DR IntAct; Q9ULD2; 33.
DR MINT; Q9ULD2; -.
DR STRING; 9606.ENSP00000262102; -.
DR iPTMnet; Q9ULD2; -.
DR MetOSite; Q9ULD2; -.
DR PhosphoSitePlus; Q9ULD2; -.
DR BioMuta; MTUS1; -.
DR DMDM; 158706128; -.
DR EPD; Q9ULD2; -.
DR jPOST; Q9ULD2; -.
DR MassIVE; Q9ULD2; -.
DR MaxQB; Q9ULD2; -.
DR PaxDb; Q9ULD2; -.
DR PeptideAtlas; Q9ULD2; -.
DR PRIDE; Q9ULD2; -.
DR ProteomicsDB; 4177; -.
DR ProteomicsDB; 84989; -. [Q9ULD2-1]
DR ProteomicsDB; 84990; -. [Q9ULD2-2]
DR ProteomicsDB; 84991; -. [Q9ULD2-3]
DR ProteomicsDB; 84992; -. [Q9ULD2-4]
DR ProteomicsDB; 84993; -. [Q9ULD2-5]
DR ProteomicsDB; 84994; -. [Q9ULD2-6]
DR Antibodypedia; 5109; 233 antibodies from 29 providers.
DR DNASU; 57509; -.
DR Ensembl; ENST00000262102.10; ENSP00000262102.6; ENSG00000129422.15. [Q9ULD2-1]
DR Ensembl; ENST00000297488.10; ENSP00000297488.6; ENSG00000129422.15. [Q9ULD2-3]
DR Ensembl; ENST00000381861.7; ENSP00000371285.3; ENSG00000129422.15. [Q9ULD2-6]
DR Ensembl; ENST00000381869.5; ENSP00000371293.3; ENSG00000129422.15. [Q9ULD2-2]
DR Ensembl; ENST00000519263.5; ENSP00000430167.1; ENSG00000129422.15. [Q9ULD2-2]
DR Ensembl; ENST00000544260.3; ENSP00000445738.1; ENSG00000129422.15. [Q9ULD2-7]
DR Ensembl; ENST00000634613.1; ENSP00000489288.1; ENSG00000129422.15. [Q9ULD2-4]
DR Ensembl; ENST00000693296.1; ENSP00000509719.1; ENSG00000129422.15. [Q9ULD2-1]
DR GeneID; 57509; -.
DR KEGG; hsa:57509; -.
DR MANE-Select; ENST00000693296.1; ENSP00000509719.1; NM_001363059.2; NP_001349988.1.
DR UCSC; uc003wxs.4; human. [Q9ULD2-1]
DR CTD; 57509; -.
DR DisGeNET; 57509; -.
DR GeneCards; MTUS1; -.
DR HGNC; HGNC:29789; MTUS1.
DR HPA; ENSG00000129422; Low tissue specificity.
DR MalaCards; MTUS1; -.
DR MIM; 114550; phenotype.
DR MIM; 609589; gene.
DR neXtProt; NX_Q9ULD2; -.
DR OpenTargets; ENSG00000129422; -.
DR PharmGKB; PA134968054; -.
DR VEuPathDB; HostDB:ENSG00000129422; -.
DR eggNOG; ENOG502QPVG; Eukaryota.
DR GeneTree; ENSGT00950000183026; -.
DR HOGENOM; CLU_029786_1_0_1; -.
DR InParanoid; Q9ULD2; -.
DR OMA; HQSYQEE; -.
DR OrthoDB; 91479at2759; -.
DR PhylomeDB; Q9ULD2; -.
DR TreeFam; TF333416; -.
DR PathwayCommons; Q9ULD2; -.
DR SignaLink; Q9ULD2; -.
DR BioGRID-ORCS; 57509; 13 hits in 1074 CRISPR screens.
DR ChiTaRS; MTUS1; human.
DR GeneWiki; MTUS1; -.
DR GenomeRNAi; 57509; -.
DR Pharos; Q9ULD2; Tbio.
DR PRO; PR:Q9ULD2; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9ULD2; protein.
DR Bgee; ENSG00000129422; Expressed in corpus callosum and 209 other tissues.
DR ExpressionAtlas; Q9ULD2; baseline and differential.
DR Genevisible; Q9ULD2; HS.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR GO; GO:0010758; P:regulation of macrophage chemotaxis; IBA:GO_Central.
DR InterPro; IPR029786; MTUS1.
DR PANTHER; PTHR24200:SF7; PTHR24200:SF7; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Coiled coil; Cytoplasm; Cytoskeleton;
KW Disease variant; Golgi apparatus; Membrane; Microtubule; Mitochondrion;
KW Nucleus; Phosphoprotein; Reference proteome; Tumor suppressor.
FT CHAIN 1..1270
FT /note="Microtubule-associated tumor suppressor 1"
FT /id="PRO_0000305197"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 524..560
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 592..622
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..815
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1237..1270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 940..1231
FT /evidence="ECO:0000255"
FT COMPBIAS 19..50
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 530..558
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..779
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 792..815
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1241..1270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 186
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5HZI1"
FT MOD_RES 399
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 443
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 629
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1203
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IMY1"
FT MOD_RES 1224
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1245
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 1255
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5HZI1"
FT MOD_RES 1259
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IMY1"
FT MOD_RES 1261
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5HZI1"
FT MOD_RES 1264
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 1268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..928
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028270"
FT VAR_SEQ 1..855
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044849"
FT VAR_SEQ 1..834
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12692079,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15123706,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028271"
FT VAR_SEQ 1..753
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028272"
FT VAR_SEQ 754..817
FT /note="QRIRRVSSSGKPTSLKTAQSSWVNLPRPLPKSKASLKSPALRRTGSTPSIAS
FT THSELSTYSNNS -> MTVPGGFRSCTETDISSKIFINSTLTPPAGSERHYDATLLTLL
FT VVGSYSLCIIPLLATFTGKKT (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028273"
FT VAR_SEQ 763..817
FT /note="GKPTSLKTAQSSWVNLPRPLPKSKASLKSPALRRTGSTPSIASTHSELSTYS
FT NNS -> A (in isoform 2)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_028274"
FT VAR_SEQ 763..770
FT /note="GKPTSLKT -> VLPKAAFS (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028275"
FT VAR_SEQ 771..1270
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028276"
FT VAR_SEQ 835..874
FT /note="QNGSSGSFYLKPLVSRAHVHLMKTPPKGPSRKNLFTALNA -> MLLSPKFS
FT LSTIHIRLTAKGLLRNLRLPSGFRRSTVVFHT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:12692079,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15123706,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028277"
FT VAR_SEQ 929..946
FT /note="GNTKFEALTVVIQHLLSE -> MGCPSSKLCLYSPCAATR (in isoform
FT 4)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_028278"
FT VARIANT 75
FT /note="Q -> K (in HCC; dbSNP:rs61733703)"
FT /evidence="ECO:0000269|PubMed:16650523"
FT /id="VAR_035173"
FT VARIANT 148
FT /note="C -> R (in dbSNP:rs3739407)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:16650523, ECO:0000269|PubMed:17656251,
FT ECO:0000269|Ref.7, ECO:0000269|Ref.9"
FT /id="VAR_035174"
FT VARIANT 186
FT /note="T -> S (in HNSCC cell lines; dbSNP:rs141609607)"
FT /evidence="ECO:0000269|PubMed:17656251"
FT /id="VAR_035175"
FT VARIANT 425
FT /note="T -> M (in dbSNP:rs61733694)"
FT /evidence="ECO:0000269|PubMed:16650523"
FT /id="VAR_035176"
FT VARIANT 453
FT /note="K -> T (in dbSNP:rs17690844)"
FT /evidence="ECO:0000269|PubMed:16650523,
FT ECO:0000269|PubMed:17656251"
FT /id="VAR_035177"
FT VARIANT 563
FT /note="A -> S (in HCC)"
FT /evidence="ECO:0000269|PubMed:16650523"
FT /id="VAR_035178"
FT VARIANT 575
FT /note="H -> R (in dbSNP:rs209569)"
FT /evidence="ECO:0000269|PubMed:16650523, ECO:0000269|Ref.9"
FT /id="VAR_035179"
FT VARIANT 873
FT /note="N -> H (in HCC; dbSNP:rs187103704)"
FT /evidence="ECO:0000269|PubMed:16650523"
FT /id="VAR_035180"
FT VARIANT 911
FT /note="K -> T (in dbSNP:rs61748836)"
FT /evidence="ECO:0000269|PubMed:16650523"
FT /id="VAR_035181"
FT VARIANT 1063
FT /note="K -> T (in dbSNP:rs17853231)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_035182"
FT VARIANT 1105
FT /note="E -> Q (in dbSNP:rs61733705)"
FT /evidence="ECO:0000269|PubMed:16650523"
FT /id="VAR_035183"
FT VARIANT 1201
FT /note="Q -> R (in HCC; dbSNP:rs567116808)"
FT /evidence="ECO:0000269|PubMed:16650523"
FT /id="VAR_035184"
FT CONFLICT 266
FT /note="C -> G (in Ref. 5; CAB50791)"
FT /evidence="ECO:0000305"
FT CONFLICT 918
FT /note="F -> L (in Ref. 4; BAG37243)"
FT /evidence="ECO:0000305"
FT CONFLICT 999
FT /note="E -> G (in Ref. 5; CAH56128)"
FT /evidence="ECO:0000305"
FT CONFLICT 1149
FT /note="I -> T (in Ref. 4; BAB14894)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1270 AA; 141397 MW; 2EAE962F627BFFE3 CRC64;
MTDDNSDDKI EDELQTFFTS DKDGNTHAYN PKSPPTQNSS ASSVNWNSAN PDDMVVDYET
DPAVVTGENI SLSLQGVEVF GHEKSSSDFI SKQVLDMHKD SICQCPALVG TEKPKYLQHS
CHSLEAVEGQ SVEPSLPFVW KPNDNLNCAG YCDALELNQT FDMTVDKVNC TFISHHAIGK
SQSFHTAGSL PPTGRRSGST SSLSYSTWTS SHSDKTHARE TTYDRESFEN PQVTPSEAQD
MTYTAFSDVV MQSEVFVSDI GNQCACSSGK VTSEYTDGSQ QRLVGEKETQ ALTPVSDGME
VPNDSALQEF FCLSHDESNS EPHSQSSYRH KEMGQNLRET VSYCLIDDEC PLMVPAFDKS
EAQVLNPEHK VTETEDTQMV SKGKDLGTQN HTSELILSSP PGQKVGSSFG LTWDANDMVI
STDKTMCMST PVLEPTKVTF SVSPIEATEK CKKVEKGNRG LKNIPDSKEA PVNLCKPSLG
KSTIKTNTPI GCKVRKTEII SYPRPNFKNV KAKVMSRAVL QPKDAALSKV TPRPQQTSAS
SPSSVNSRQQ TVLSRTPRSD LNADKKAEIL INKTHKQQFN KLITSQAVHV TTHSKNASHR
VPRTTSAVKS NQEDVDKASS SNSACETGSV SALFQKIKGI LPVKMESAEC LEMTYVPNID
RISPEKKGEK ENGTSMEKQE LKQEIMNETF EYGSLFLGSA SKTTTTSGRN ISKPDSCGLR
QIAAPKAKVG PPVSCLRRNS DNRNPSADRA VSPQRIRRVS SSGKPTSLKT AQSSWVNLPR
PLPKSKASLK SPALRRTGST PSIASTHSEL STYSNNSGNA AVIKYEEKPP KPAFQNGSSG
SFYLKPLVSR AHVHLMKTPP KGPSRKNLFT ALNAVEKSRQ KNPRSLCIQP QTAPDALPPE
KTLELTQYKT KCENQSGFIL QLKQLLACGN TKFEALTVVI QHLLSEREEA LKQHKTLSQE
LVNLRGELVT ASTTCEKLEK ARNELQTVYE AFVQQHQAEK TERENRLKEF YTREYEKLRD
TYIEEAEKYK MQLQEQFDNL NAAHETSKLE IEASHSEKLE LLKKAYEASL SEIKKGHEIE
KKSLEDLLSE KQESLEKQIN DLKSENDALN EKLKSEEQKR RAREKANLKN PQIMYLEQEL
ESLKAVLEIK NEKLHQQDIK LMKMEKLVDN NTALVDKLKR FQQENEELKA RMDKHMAISR
QLSTEQAVLQ ESLEKESKVN KRLSMENEEL LWKLHNGDLC SPKRSPTSSA IPLQSPRNSG
SFPSPSISPR
