MAP1S_MOUSE
ID MAP1S_MOUSE Reviewed; 973 AA.
AC Q8C052; E9QKR8; Q3TSD6; Q7TMW8;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 129.
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 Contains:
DE RecName: Full=MAP1S heavy chain;
DE Contains:
DE RecName: Full=MAP1S light chain;
GN Name=Map1s; Synonyms=Bpy2ip1, Map8, Mtap1s;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH MICROTUBULES AND
RP ACTIN, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Egg, and Olfactory bulb;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 380-973.
RC STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
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 [5]
RP FUNCTION, SUBUNIT, INTERACTION WITH MICROTUBULES AND ACTIN, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15528209; DOI=10.1074/jbc.m408984200;
RA Orban-Nemeth Z., Simader H., Badurek S., Trancikova A., Propst F.;
RT "Microtubule-associated protein 1S, a short and ubiquitously expressed
RT member of the microtubule-associated protein 1 family.";
RL J. Biol. Chem. 280:2257-2265(2005).
RN [6]
RP INTERACTION WITH GAN.
RX PubMed=16565160; DOI=10.1093/hmg/ddl069;
RA Ding J., Allen E., Wang W., Valle A., Wu C., Nardine T., Cui B., Yi J.,
RA Taylor A., Jeon N.L., Chu S., So Y., Vogel H., Tolwani R., Mobley W.,
RA Yang Y.;
RT "Gene targeting of GAN in mouse causes a toxic accumulation of microtubule-
RT associated protein 8 and impaired retrograde axonal transport.";
RL Hum. Mol. Genet. 15:1451-1463(2006).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462; SER-660 AND SER-724, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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 (By similarity).
CC Involved in the formation of microtubule bundles. {ECO:0000250,
CC ECO:0000269|PubMed:15528209}.
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 with
CC ESR1, LRPPRC, RASSF1, microtubules and VCY2. Interacts with WDR47 (via
CC N-terminus of light chain) (By similarity). Interacts (via C-terminus)
CC with GAN (via Kelch domains). {ECO:0000250,
CC ECO:0000269|PubMed:15528209, ECO:0000269|PubMed:16297881,
CC ECO:0000269|PubMed:16565160}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15528209}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:15528209}.
CC Note=Detected in perinuclear punctate network corresponding to
CC mitochondrial aggregates and in the nucleus in cells exhibiting
CC apoptosis. Associated specifically with microtubules stabilized by
CC paclitaxel and colocalizes with RASSF1. In interphase cells, shows a
CC diffuse cytoplasmic staining with partial localization to the
CC microtubules. During the different stages of mitosis detected at the
CC spindle microtubules. Detected in filopodia-like protrusions and
CC synapses (By similarity). {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in ventral and dorsal horns of the spinal
CC cord, hippocampus, cerebral cortex, molecular, Purkinje and granular
CC cell layers of the cerebellum and in dorsal root ganglia of the PNS (at
CC protein level). Expressed in brain, testis, heart, lung, kidney and
CC liver. {ECO:0000269|PubMed:15528209, ECO:0000269|PubMed:16297881}.
CC -!- DEVELOPMENTAL STAGE: Expressed in embryo at 10 dpc onwards (at protein
CC level). {ECO:0000269|PubMed:16297881}.
CC -!- DOMAIN: Its C-terminal part of the heavy chain interacts with ESR1 (By
CC similarity). The N-terminus of the heavy chain associates with the C-
CC terminus of the light chain to form the heterodimer complex.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH52828.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH52828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. At the N-terminus.; Evidence={ECO:0000305};
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DR EMBL; DQ387862; ABD47683.1; -; mRNA.
DR EMBL; AK032300; BAC27800.1; -; mRNA.
DR EMBL; AK162124; BAE36739.1; -; mRNA.
DR EMBL; AC019302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052828; AAH52828.1; ALT_INIT; mRNA.
DR CCDS; CCDS22387.1; -.
DR RefSeq; NP_766601.2; NM_173013.3.
DR AlphaFoldDB; Q8C052; -.
DR SMR; Q8C052; -.
DR BioGRID; 234753; 17.
DR IntAct; Q8C052; 4.
DR MINT; Q8C052; -.
DR STRING; 10090.ENSMUSP00000019405; -.
DR iPTMnet; Q8C052; -.
DR PhosphoSitePlus; Q8C052; -.
DR EPD; Q8C052; -.
DR jPOST; Q8C052; -.
DR MaxQB; Q8C052; -.
DR PaxDb; Q8C052; -.
DR PeptideAtlas; Q8C052; -.
DR PRIDE; Q8C052; -.
DR ProteomicsDB; 252730; -.
DR Antibodypedia; 27783; 201 antibodies from 24 providers.
DR DNASU; 270058; -.
DR Ensembl; ENSMUST00000019405; ENSMUSP00000019405; ENSMUSG00000019261.
DR GeneID; 270058; -.
DR KEGG; mmu:270058; -.
DR UCSC; uc009mcd.2; mouse.
DR CTD; 55201; -.
DR MGI; MGI:2443304; Map1s.
DR VEuPathDB; HostDB:ENSMUSG00000019261; -.
DR eggNOG; KOG3592; Eukaryota.
DR GeneTree; ENSGT00940000160221; -.
DR HOGENOM; CLU_000285_2_0_1; -.
DR InParanoid; Q8C052; -.
DR OMA; ECGCSGL; -.
DR OrthoDB; 86642at2759; -.
DR PhylomeDB; Q8C052; -.
DR TreeFam; TF350229; -.
DR BioGRID-ORCS; 270058; 6 hits in 72 CRISPR screens.
DR ChiTaRS; Map1s; mouse.
DR PRO; PR:Q8C052; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; Q8C052; protein.
DR Bgee; ENSMUSG00000019261; Expressed in embryonic brain and 229 other tissues.
DR ExpressionAtlas; Q8C052; baseline and differential.
DR Genevisible; Q8C052; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0042995; C:cell projection; ISO:MGI.
DR GO; GO:0005813; C:centrosome; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISS:HGNC-UCL.
DR GO; GO:0030425; C:dendrite; IDA:HGNC-UCL.
DR GO; GO:0005874; C:microtubule; ISO:MGI.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0005815; C:microtubule organizing center; ISO:MGI.
DR GO; GO:1990498; C:mitotic spindle microtubule; ISO:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:HGNC-UCL.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC-UCL.
DR GO; GO:0005819; C:spindle; ISO:MGI.
DR GO; GO:0045202; C:synapse; ISO:MGI.
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; ISS:HGNC-UCL.
DR GO; GO:0003677; F:DNA binding; ISS:HGNC-UCL.
DR GO; GO:0042802; F:identical protein binding; IDA:MGI.
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:0007409; P:axonogenesis; IBA:GO_Central.
DR GO; GO:0007420; P:brain development; IEP:HGNC-UCL.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0051310; P:metaphase plate congression; ISO:MGI.
DR GO; GO:0034454; P:microtubule anchoring at centrosome; ISO:MGI.
DR GO; GO:0001578; P:microtubule bundle formation; ISS:HGNC-UCL.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI.
DR GO; GO:0007052; P:mitotic spindle organization; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IEP:HGNC-UCL.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISS:HGNC-UCL.
DR GO; GO:0031114; P:regulation of microtubule depolymerization; IBA:GO_Central.
DR InterPro; IPR026074; MAP1.
DR InterPro; IPR027322; MAP1S.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR PANTHER; PTHR13843; PTHR13843; 2.
DR PANTHER; PTHR13843:SF11; PTHR13843:SF11; 2.
DR SUPFAM; SSF56281; SSF56281; 1.
PE 1: Evidence at protein level;
KW Apoptosis; Cytoplasm; Cytoskeleton; DNA-binding; Microtubule; Nucleus;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..973
FT /note="Microtubule-associated protein 1S"
FT /id="PRO_0000311382"
FT CHAIN 1..742
FT /note="MAP1S heavy chain"
FT /id="PRO_0000311383"
FT CHAIN 743..973
FT /note="MAP1S light chain"
FT /id="PRO_0000311384"
FT REGION 1..716
FT /note="Necessary for the microtubule-organizing center
FT localization"
FT /evidence="ECO:0000250"
FT REGION 452..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..973
FT /note="Necessary for interaction with RASSF1"
FT /evidence="ECO:0000250"
FT REGION 645..880
FT /note="Necessary for association with microtubules"
FT REGION 875..973
FT /note="Necessary for association with actin"
FT REGION 881..905
FT /note="Necessary for the mitochondrial aggregation and
FT genome destruction"
FT /evidence="ECO:0000250"
FT COMPBIAS 567..585
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 605..634
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..714
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..752
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..793
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 586
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P0C5W1"
FT MOD_RES 591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 660
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 724
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 475
FT /note="E -> G (in Ref. 4; AAH52828)"
FT /evidence="ECO:0000305"
FT CONFLICT 680
FT /note="P -> T (in Ref. 1; ABD47683 and 2; BAC27800)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 973 AA; 102939 MW; 3DD3E1A43F70E8DD CRC64;
MAAVMAAPEA VEAPSSLLLL VVGGECGCPG LLAYVMEELE RGVRSWEDVD PAVCSLDEQL
KAFVSRHSAT FSSIVKGQRS LHHRGETLET LVLLNPSDKS LCDELRNLLM DPAPHKLLVL
AGPCLEETGE LLLQTGGFSA HHFLQVLGDK EVQDALASAP AAPALTVSCP TFGDWALLGP
VPGLQLRLNP PAQLPASEGL RAFLEYVAES LEPPSPFELL EPPAAGGFLR LARPCCYVFP
GGLGDAAFFA VNGFTVLVNG GSNPKSSFWK LVRHLDRVDA VLVTHAGADS LPGLNSLLRR
KLAEREAAAG PQGQHEERLR RLLSPALGVV FLNAREAASR LRGGEDEAVC ARSLLRSLGI
APLPLQRGPQ PSCPTVLFEK LGVGRLELFV LHPPPGDPAA PACALLVWQP AAPGDKVVRV
LFPGRTPPAR LLDGLQRLQH LPCLRRPVVT THDLEAPSRA NSQDSLASRD SARKEPVRGT
VGSIANRSTV RREPALATRD QKKDTRSGPT QPTARDTRRS GPGVVNTKPR VSQNGPRAPV
LAAPLTAPVA ECPGEAENIL ESERPPAPSP TLSPAQSPPP TAPGNSPERL SLSPLRPEPA
PDASPSATTP TLTTPSLPAE LGSPHSTEVD ESLSVSFEQV LPAGDPGLSL PLRLARRSTS
PHDVDLCLVS PCEFSHRKPP PPASPGSSDS SARSQERPPE TPPTSVSESL PTLSDSDPVP
VADSDDDAGS ESAARDPPPT PRVPPPLPDV PGICMVDPEA LPPRARQPLN TTNPSRSRKA
PARPSSASAT PRAATVAAKT KGPAGDRNRP LSARSEPADR PGRVPLTRKP SVPKTVPKMA
SATRLSSGPS GRPAPLAAGS PVYLDLAYLP GGGAGHLDQN FFLRVRALCY VISGQGQRQE
EGLRAVLDAL LAGKRQWDLD LQVTLIPTFD SAVMHRWYEE THAQHQALGI RVLGSGSLVS
MQDEAFPACK VEF
