Full text data of MAP1S
MAP1S
(BPY2IP1, C19orf5, MAP8, VCY2IP1)
[Confidence: low (only semi-automatic identification from reviews)]
Microtubule-associated protein 1S; MAP-1S (BPY2-interacting protein 1; Microtubule-associated protein 8; Variable charge Y chromosome 2-interacting protein 1; VCY2-interacting protein 1; VCY2IP-1; MAP1S heavy chain; MAP1S light chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Microtubule-associated protein 1S; MAP-1S (BPY2-interacting protein 1; Microtubule-associated protein 8; Variable charge Y chromosome 2-interacting protein 1; VCY2-interacting protein 1; VCY2IP-1; MAP1S heavy chain; MAP1S light chain)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q66K74
ID MAP1S_HUMAN Reviewed; 1059 AA.
AC Q66K74; Q27QB1; Q6NXF1; Q8N3L8; Q8N3W5; Q8NI88; Q96H94; Q96IT4;
read moreAC Q96SP8; Q9BRC6; Q9H928; Q9NVK7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 22-JAN-2014, entry version 87.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 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].
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
RT sites.";
RL Biochem. Biophys. Res. Commun. 339:172-179(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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 MRNA], 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 314-1059.
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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
RT cytoskeleton with chromosome remodeling and tumor suppressor RASSF1
RT deduced by in silico homology analysis, interaction cloning in yeast,
RT and colocalization in cultured cells.";
RL In Vitro Cell. Dev. Biol. Anim. 38:582-594(2002).
RN [9]
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.,
RA Hesson L., 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 [10]
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 [11]
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
RT tumor suppressor RASSF1 for microtubule hyperstabilization is
RT determined by cell death inducer C19ORF5.";
RL Cancer Res. 65:1830-1838(2005).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [14]
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
RT 1S in the brain.";
RL Biochem. Biophys. Res. Commun. 361:127-132(2007).
RN [15]
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-
RT associated novel microtubule-associated protein, C19ORF5/MAP1S, causes
RT mitotic abnormalities.";
RL Cancer Res. 67:492-500(2007).
RN [16]
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
RT FUTSCH reveals heavy- and light-chain subunits generated by
RT proteolytic processing at a conserved cleavage site.";
RL Biochem. J. 414:63-71(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [18]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-640; SER-657
RP AND SER-759, AND MASS SPECTROMETRY.
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 [20]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND MASS
RP SPECTROMETRY.
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 [22]
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759 AND SER-809, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
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.,
RA Buerckstuemmer T., 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-657; SER-759
RP AND SER-809, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
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 [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Microtubule-associated protein that mediates aggregation
CC of mitochondria resulting in cell death and genomic destruction
CC (MAGD). Plays a role in anchoring the microtubule organizing
CC center to the centrosomes. Binds to DNA. Plays a role in
CC apoptosis. Involved in the formation of microtubule bundles (By
CC similarity).
CC -!- SUBUNIT: Heterodimer of a heavy and a light chain. Interacts with
CC microtubules and actin. Both MAP1S heavy and light chains interact
CC with microtubules. MAP1S light chain interacts with actin.
CC Interacts (via C-terminus) with GAN (via Kelch domains) (By
CC similarity). Interacts with ESR1, LRPPRC, RASSF1 isoform A and
CC isoform C, microtubules and VCY2. Interacts with WDR47 (via N-
CC terminus of light chain).
CC -!- INTERACTION:
CC O14599:BPY2B; NbExp=3; IntAct=EBI-2133734, EBI-2133713;
CC O14543:SOCS3; NbExp=6; IntAct=EBI-2133734, EBI-714146;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Cytoplasm,
CC cytoskeleton. Cytoplasm, cytoskeleton, spindle. Note=Detected in
CC filopodia-like protrusions and synapses (By similarity). Detected
CC in perinuclear punctate network corresponding to mitochondrial
CC aggregates and in the nucleus in cells exhibiting apoptosis.
CC Associated specifically with microtubules stabilized by paclitaxel
CC and colocalizes with RASSF1 isoform A. In interphase cells, shows
CC a diffuse cytoplasmic staining with partial localization to the
CC microtubules. During the different stages of mitosis detected at
CC the spindle microtubules.
CC -!- TISSUE SPECIFICITY: Expressed in neurons (at protein level).
CC Expressed in spermatocytes, spermatids and spermatozoa. Expressed
CC in the cerebral cortex. Highly expressed in testis. Moderately
CC expressed in the brain, colon, heart, kidney, liver, lung,
CC placenta, small intestine, spleen and stomach. Weakly expressed in
CC muscle.
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.
CC -!- MISCELLANEOUS: Depletion of MAP1S by RNAi causes mitotic
CC abnormalities that consist of failure to form a stable metaphase
CC plate, premature sister chromatid separation, lagging chromosomes,
CC and multipolar spindles.
CC -!- SIMILARITY: Belongs to the MAP1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07253.1; Type=Erroneous initiation;
CC Sequence=AAH07253.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. At the N-terminus;
CC Sequence=AAH67115.1; Type=Erroneous initiation;
CC Sequence=BAA91743.1; Type=Erroneous initiation;
CC Sequence=BAB14415.1; Type=Erroneous initiation;
CC Sequence=BAB55242.1; Type=Frameshift; Positions=851;
CC Sequence=BAB93493.1; Type=Erroneous initiation;
CC Sequence=CAD38911.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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; AL834233; CAD38911.1; ALT_INIT; mRNA.
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 RefSeq; NP_060644.4; NM_018174.4.
DR UniGene; Hs.66048; -.
DR ProteinModelPortal; Q66K74; -.
DR SMR; Q66K74; 247-307.
DR IntAct; Q66K74; 9.
DR PhosphoSite; Q66K74; -.
DR DMDM; 160410004; -.
DR PaxDb; Q66K74; -.
DR PRIDE; Q66K74; -.
DR Ensembl; ENST00000324096; ENSP00000325313; ENSG00000130479.
DR GeneID; 55201; -.
DR KEGG; hsa:55201; -.
DR UCSC; uc002nhe.1; human.
DR CTD; 55201; -.
DR GeneCards; GC19P017832; -.
DR H-InvDB; HIX0014899; -.
DR HGNC; HGNC:15715; MAP1S.
DR HPA; HPA050934; -.
DR HPA; HPA054637; -.
DR MIM; 607573; gene.
DR neXtProt; NX_Q66K74; -.
DR PharmGKB; PA38031; -.
DR eggNOG; NOG12793; -.
DR HOVERGEN; HBG108117; -.
DR InParanoid; Q66K74; -.
DR KO; K10429; -.
DR OMA; PCEFEHR; -.
DR OrthoDB; EOG773XKP; -.
DR ChiTaRS; MAP1S; human.
DR GeneWiki; MAP1S; -.
DR GenomeRNAi; 55201; -.
DR NextBio; 59090; -.
DR PRO; PR:Q66K74; -.
DR ArrayExpress; Q66K74; -.
DR Bgee; Q66K74; -.
DR Genevestigator; Q66K74; -.
DR GO; GO:0005829; C:cytosol; IDA:HGNC.
DR GO; GO:0030425; C:dendrite; ISS:HGNC.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:HGNC.
DR GO; GO:0005634; C:nucleus; IDA:HGNC.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:HGNC.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:HGNC.
DR GO; GO:0003677; F:DNA binding; IDA:HGNC.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IDA:HGNC.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:BHF-UCL.
DR GO; GO:0007420; P:brain development; ISS:HGNC.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:HGNC.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; TAS:HGNC.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEP:HGNC.
DR Gene3D; 3.60.15.10; -; 2.
DR InterPro; IPR001279; Beta-lactamas-like.
DR InterPro; IPR026074; MAP1.
DR InterPro; IPR027322; MAP1S.
DR PANTHER; PTHR13843; PTHR13843; 1.
DR PANTHER; PTHR13843:SF1; PTHR13843:SF1; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Complete proteome; Cytoplasm; Cytoskeleton; DNA-binding;
KW Microtubule; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 1059 Microtubule-associated protein 1S.
FT /FTId=PRO_0000311379.
FT CHAIN 1 829 MAP1S heavy chain.
FT /FTId=PRO_0000311380.
FT CHAIN 830 1059 MAP1S light chain.
FT /FTId=PRO_0000311381.
FT REGION 1 797 Necessary for the microtubule-organizing
FT center localization.
FT REGION 666 1059 Necessary for interaction with RASSF1
FT isoform A and isoform C.
FT REGION 714 966 Necessary for association with
FT microtubules.
FT REGION 960 1059 Necessary for association with actin (By
FT similarity).
FT REGION 967 991 Necessary for the mitochondrial
FT aggregation and genome destruction.
FT COMPBIAS 560 850 Pro-rich.
FT MOD_RES 472 472 Phosphoserine.
FT MOD_RES 640 640 Phosphoserine.
FT MOD_RES 657 657 Phosphoserine.
FT MOD_RES 759 759 Phosphoserine.
FT MOD_RES 809 809 Phosphoserine.
FT VARIANT 372 372 L -> V (in dbSNP:rs17710707).
FT /FTId=VAR_050023.
FT VARIANT 411 411 S -> C (in dbSNP:rs17710707).
FT /FTId=VAR_037236.
FT VARIANT 538 538 P -> Q (in dbSNP:rs7252905).
FT /FTId=VAR_037237.
FT CONFLICT 120 120 P -> L (in Ref. 1; CAD29574 and 3;
FT BAB55242).
FT CONFLICT 178 178 L -> P (in Ref. 1; CAD29574 and 3;
FT BAB55242).
FT CONFLICT 440 440 C -> Y (in Ref. 4; CAD38911).
FT CONFLICT 521 521 T -> A (in Ref. 6; BAB93493).
FT CONFLICT 526 526 K -> R (in Ref. 1; CAD29574 and 3;
FT BAB55242).
FT CONFLICT 967 967 F -> L (in Ref. 3; BAB14415).
FT CONFLICT 1043 1043 S -> G (in Ref. 3; BAA91743).
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
//
ID MAP1S_HUMAN Reviewed; 1059 AA.
AC Q66K74; Q27QB1; Q6NXF1; Q8N3L8; Q8N3W5; Q8NI88; Q96H94; Q96IT4;
read moreAC Q96SP8; Q9BRC6; Q9H928; Q9NVK7;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 22-JAN-2014, entry version 87.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], 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].
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
RT sites.";
RL Biochem. Biophys. Res. Commun. 339:172-179(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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].
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.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., 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 MRNA], 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 314-1059.
RA Shichijo S., Itoh K.;
RT "Identification of immuno-peptidmics that recognized by tumor-reactive
RT CTL generated from TIL of colon cancer patients.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
RN [7]
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 [8]
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
RT cytoskeleton with chromosome remodeling and tumor suppressor RASSF1
RT deduced by in silico homology analysis, interaction cloning in yeast,
RT and colocalization in cultured cells.";
RL In Vitro Cell. Dev. Biol. Anim. 38:582-594(2002).
RN [9]
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.,
RA Hesson L., 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 [10]
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 [11]
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
RT tumor suppressor RASSF1 for microtubule hyperstabilization is
RT determined by cell death inducer C19ORF5.";
RL Cancer Res. 65:1830-1838(2005).
RN [12]
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472, AND MASS
RP SPECTROMETRY.
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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [14]
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
RT 1S in the brain.";
RL Biochem. Biophys. Res. Commun. 361:127-132(2007).
RN [15]
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-
RT associated novel microtubule-associated protein, C19ORF5/MAP1S, causes
RT mitotic abnormalities.";
RL Cancer Res. 67:492-500(2007).
RN [16]
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
RT FUTSCH reveals heavy- and light-chain subunits generated by
RT proteolytic processing at a conserved cleavage site.";
RL Biochem. J. 414:63-71(2008).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND MASS
RP SPECTROMETRY.
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.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [18]
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
RT the kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-640; SER-657
RP AND SER-759, AND MASS SPECTROMETRY.
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 [20]
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.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759, AND MASS
RP SPECTROMETRY.
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 [22]
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 [23]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-759 AND SER-809, AND
RP MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [24]
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.,
RA Buerckstuemmer T., 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 [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-472; SER-657; SER-759
RP AND SER-809, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [26]
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 [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Microtubule-associated protein that mediates aggregation
CC of mitochondria resulting in cell death and genomic destruction
CC (MAGD). Plays a role in anchoring the microtubule organizing
CC center to the centrosomes. Binds to DNA. Plays a role in
CC apoptosis. Involved in the formation of microtubule bundles (By
CC similarity).
CC -!- SUBUNIT: Heterodimer of a heavy and a light chain. Interacts with
CC microtubules and actin. Both MAP1S heavy and light chains interact
CC with microtubules. MAP1S light chain interacts with actin.
CC Interacts (via C-terminus) with GAN (via Kelch domains) (By
CC similarity). Interacts with ESR1, LRPPRC, RASSF1 isoform A and
CC isoform C, microtubules and VCY2. Interacts with WDR47 (via N-
CC terminus of light chain).
CC -!- INTERACTION:
CC O14599:BPY2B; NbExp=3; IntAct=EBI-2133734, EBI-2133713;
CC O14543:SOCS3; NbExp=6; IntAct=EBI-2133734, EBI-714146;
CC -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm, cytosol. Cytoplasm,
CC cytoskeleton. Cytoplasm, cytoskeleton, spindle. Note=Detected in
CC filopodia-like protrusions and synapses (By similarity). Detected
CC in perinuclear punctate network corresponding to mitochondrial
CC aggregates and in the nucleus in cells exhibiting apoptosis.
CC Associated specifically with microtubules stabilized by paclitaxel
CC and colocalizes with RASSF1 isoform A. In interphase cells, shows
CC a diffuse cytoplasmic staining with partial localization to the
CC microtubules. During the different stages of mitosis detected at
CC the spindle microtubules.
CC -!- TISSUE SPECIFICITY: Expressed in neurons (at protein level).
CC Expressed in spermatocytes, spermatids and spermatozoa. Expressed
CC in the cerebral cortex. Highly expressed in testis. Moderately
CC expressed in the brain, colon, heart, kidney, liver, lung,
CC placenta, small intestine, spleen and stomach. Weakly expressed in
CC muscle.
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.
CC -!- MISCELLANEOUS: Depletion of MAP1S by RNAi causes mitotic
CC abnormalities that consist of failure to form a stable metaphase
CC plate, premature sister chromatid separation, lagging chromosomes,
CC and multipolar spindles.
CC -!- SIMILARITY: Belongs to the MAP1 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH07253.1; Type=Erroneous initiation;
CC Sequence=AAH07253.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. At the N-terminus;
CC Sequence=AAH67115.1; Type=Erroneous initiation;
CC Sequence=BAA91743.1; Type=Erroneous initiation;
CC Sequence=BAB14415.1; Type=Erroneous initiation;
CC Sequence=BAB55242.1; Type=Frameshift; Positions=851;
CC Sequence=BAB93493.1; Type=Erroneous initiation;
CC Sequence=CAD38911.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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; AL834233; CAD38911.1; ALT_INIT; mRNA.
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 RefSeq; NP_060644.4; NM_018174.4.
DR UniGene; Hs.66048; -.
DR ProteinModelPortal; Q66K74; -.
DR SMR; Q66K74; 247-307.
DR IntAct; Q66K74; 9.
DR PhosphoSite; Q66K74; -.
DR DMDM; 160410004; -.
DR PaxDb; Q66K74; -.
DR PRIDE; Q66K74; -.
DR Ensembl; ENST00000324096; ENSP00000325313; ENSG00000130479.
DR GeneID; 55201; -.
DR KEGG; hsa:55201; -.
DR UCSC; uc002nhe.1; human.
DR CTD; 55201; -.
DR GeneCards; GC19P017832; -.
DR H-InvDB; HIX0014899; -.
DR HGNC; HGNC:15715; MAP1S.
DR HPA; HPA050934; -.
DR HPA; HPA054637; -.
DR MIM; 607573; gene.
DR neXtProt; NX_Q66K74; -.
DR PharmGKB; PA38031; -.
DR eggNOG; NOG12793; -.
DR HOVERGEN; HBG108117; -.
DR InParanoid; Q66K74; -.
DR KO; K10429; -.
DR OMA; PCEFEHR; -.
DR OrthoDB; EOG773XKP; -.
DR ChiTaRS; MAP1S; human.
DR GeneWiki; MAP1S; -.
DR GenomeRNAi; 55201; -.
DR NextBio; 59090; -.
DR PRO; PR:Q66K74; -.
DR ArrayExpress; Q66K74; -.
DR Bgee; Q66K74; -.
DR Genevestigator; Q66K74; -.
DR GO; GO:0005829; C:cytosol; IDA:HGNC.
DR GO; GO:0030425; C:dendrite; ISS:HGNC.
DR GO; GO:0005874; C:microtubule; IDA:UniProtKB.
DR GO; GO:0043025; C:neuronal cell body; ISS:HGNC.
DR GO; GO:0005634; C:nucleus; IDA:HGNC.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:HGNC.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0045202; C:synapse; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:HGNC.
DR GO; GO:0048487; F:beta-tubulin binding; IDA:HGNC.
DR GO; GO:0003677; F:DNA binding; IDA:HGNC.
DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; IDA:HGNC.
DR GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:BHF-UCL.
DR GO; GO:0007420; P:brain development; ISS:HGNC.
DR GO; GO:0001578; P:microtubule bundle formation; IMP:HGNC.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; TAS:HGNC.
DR GO; GO:0048812; P:neuron projection morphogenesis; IEP:HGNC.
DR Gene3D; 3.60.15.10; -; 2.
DR InterPro; IPR001279; Beta-lactamas-like.
DR InterPro; IPR026074; MAP1.
DR InterPro; IPR027322; MAP1S.
DR PANTHER; PTHR13843; PTHR13843; 1.
DR PANTHER; PTHR13843:SF1; PTHR13843:SF1; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Complete proteome; Cytoplasm; Cytoskeleton; DNA-binding;
KW Microtubule; Nucleus; Phosphoprotein; Polymorphism;
KW Reference proteome.
FT CHAIN 1 1059 Microtubule-associated protein 1S.
FT /FTId=PRO_0000311379.
FT CHAIN 1 829 MAP1S heavy chain.
FT /FTId=PRO_0000311380.
FT CHAIN 830 1059 MAP1S light chain.
FT /FTId=PRO_0000311381.
FT REGION 1 797 Necessary for the microtubule-organizing
FT center localization.
FT REGION 666 1059 Necessary for interaction with RASSF1
FT isoform A and isoform C.
FT REGION 714 966 Necessary for association with
FT microtubules.
FT REGION 960 1059 Necessary for association with actin (By
FT similarity).
FT REGION 967 991 Necessary for the mitochondrial
FT aggregation and genome destruction.
FT COMPBIAS 560 850 Pro-rich.
FT MOD_RES 472 472 Phosphoserine.
FT MOD_RES 640 640 Phosphoserine.
FT MOD_RES 657 657 Phosphoserine.
FT MOD_RES 759 759 Phosphoserine.
FT MOD_RES 809 809 Phosphoserine.
FT VARIANT 372 372 L -> V (in dbSNP:rs17710707).
FT /FTId=VAR_050023.
FT VARIANT 411 411 S -> C (in dbSNP:rs17710707).
FT /FTId=VAR_037236.
FT VARIANT 538 538 P -> Q (in dbSNP:rs7252905).
FT /FTId=VAR_037237.
FT CONFLICT 120 120 P -> L (in Ref. 1; CAD29574 and 3;
FT BAB55242).
FT CONFLICT 178 178 L -> P (in Ref. 1; CAD29574 and 3;
FT BAB55242).
FT CONFLICT 440 440 C -> Y (in Ref. 4; CAD38911).
FT CONFLICT 521 521 T -> A (in Ref. 6; BAB93493).
FT CONFLICT 526 526 K -> R (in Ref. 1; CAD29574 and 3;
FT BAB55242).
FT CONFLICT 967 967 F -> L (in Ref. 3; BAB14415).
FT CONFLICT 1043 1043 S -> G (in Ref. 3; BAA91743).
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
//
MIM
607573
*RECORD*
*FIELD* NO
607573
*FIELD* TI
*607573 BPY2-INTERACTING PROTEIN 1; BPY2IP1
;;VCY2-INTERACTING PROTEIN 1; VCY2IP1;;
read moreCHROMOSOME 19 OPEN READING FRAME 5; C19ORF5
*FIELD* TX
CLONING
Using the SEC1 homology domain of LRPPRC (607544) as probe in a yeast
2-hybrid screen, Liu and McKeehan (2002) cloned VCY2IP1 (BPY2IP1), which
they called C19ORF5, from a liver cDNA library. The deduced 672-amino
acid protein is proline-rich (12.8%) and contains an arginine-rich
potential RNA-binding motif. VCY2IP1 shares significant homology with
several microtubule-associated proteins. Northern blot analysis revealed
a major transcript of about 3 kb in all 12 tissues tested. Additional
less-abundant transcripts were detected in some tissues.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VCY2IP1
gene to chromosome 19 (TMAP D19S1132).
*FIELD* RF
1. Liu, L.; McKeehan, W. L.: Sequence analysis of LRPPRC and its
SEC1 domain interaction partners suggest roles in cytoskeletal organization,
vesicular trafficking, nucleocytosolic shuttling, and chromosome activity. Genomics 79:
124-136, 2002.
*FIELD* CD
Patricia A. Hartz: 2/24/2003
*FIELD* ED
carol: 08/23/2005
mgross: 2/25/2003
mgross: 2/24/2003
*RECORD*
*FIELD* NO
607573
*FIELD* TI
*607573 BPY2-INTERACTING PROTEIN 1; BPY2IP1
;;VCY2-INTERACTING PROTEIN 1; VCY2IP1;;
read moreCHROMOSOME 19 OPEN READING FRAME 5; C19ORF5
*FIELD* TX
CLONING
Using the SEC1 homology domain of LRPPRC (607544) as probe in a yeast
2-hybrid screen, Liu and McKeehan (2002) cloned VCY2IP1 (BPY2IP1), which
they called C19ORF5, from a liver cDNA library. The deduced 672-amino
acid protein is proline-rich (12.8%) and contains an arginine-rich
potential RNA-binding motif. VCY2IP1 shares significant homology with
several microtubule-associated proteins. Northern blot analysis revealed
a major transcript of about 3 kb in all 12 tissues tested. Additional
less-abundant transcripts were detected in some tissues.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the VCY2IP1
gene to chromosome 19 (TMAP D19S1132).
*FIELD* RF
1. Liu, L.; McKeehan, W. L.: Sequence analysis of LRPPRC and its
SEC1 domain interaction partners suggest roles in cytoskeletal organization,
vesicular trafficking, nucleocytosolic shuttling, and chromosome activity. Genomics 79:
124-136, 2002.
*FIELD* CD
Patricia A. Hartz: 2/24/2003
*FIELD* ED
carol: 08/23/2005
mgross: 2/25/2003
mgross: 2/24/2003