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Microtubule-associated protein 1S (MAP-1S) (BPY2-interacting protein 1) (Microtubule-associated protein 8) [Cleaved into: MAP1S heavy chain; MAP1S light chain]

 MAP1S_MOUSE             Reviewed;         973 AA.
Q8C052; E9QKR8; Q3TSD6; Q7TMW8;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 109.
RecName: Full=Microtubule-associated protein 1S;
Short=MAP-1S;
AltName: Full=BPY2-interacting protein 1;
AltName: Full=Microtubule-associated protein 8;
Contains:
RecName: Full=MAP1S heavy chain;
Contains:
RecName: Full=MAP1S light chain;
Name=Map1s; Synonyms=Bpy2ip1, Map8, Mtap1s;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, INTERACTION WITH MICROTUBULES AND
ACTIN, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=16297881; DOI=10.1016/j.bbrc.2005.10.199;
Ding J., Valle A., Allen E., Wang W., Nardine T., Zhang Y., Peng L.,
Yang Y.;
"Microtubule-associated protein 8 contains two microtubule binding
sites.";
Biochem. Biophys. Res. Commun. 339:172-179(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Egg, and Olfactory bulb;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 380-973.
STRAIN=C57BL/6NCr; TISSUE=Hematopoietic stem cell;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION, SUBUNIT, INTERACTION WITH MICROTUBULES AND ACTIN,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15528209; DOI=10.1074/jbc.M408984200;
Orban-Nemeth Z., Simader H., Badurek S., Trancikova A., Propst F.;
"Microtubule-associated protein 1S, a short and ubiquitously expressed
member of the microtubule-associated protein 1 family.";
J. Biol. Chem. 280:2257-2265(2005).
[6]
INTERACTION WITH GAN.
PubMed=16565160; DOI=10.1093/hmg/ddl069;
Ding J., Allen E., Wang W., Valle A., Wu C., Nardine T., Cui B.,
Yi J., Taylor A., Jeon N.L., Chu S., So Y., Vogel H., Tolwani R.,
Mobley W., Yang Y.;
"Gene targeting of GAN in mouse causes a toxic accumulation of
microtubule-associated protein 8 and impaired retrograde axonal
transport.";
Hum. Mol. Genet. 15:1451-1463(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462; SER-660 AND
SER-724, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: Microtubule-associated protein that mediates aggregation
of mitochondria resulting in cell death and genomic destruction
(MAGD). Plays a role in anchoring the microtubule organizing
center to the centrosomes. Binds to DNA. Plays a role in apoptosis
(By similarity). Involved in the formation of microtubule bundles.
{ECO:0000250, ECO:0000269|PubMed:15528209}.
-!- SUBUNIT: Heterodimer of a heavy and a light chain. Interacts with
microtubules and actin. Both MAP1S heavy and light chains interact
with microtubules. MAP1S light chain interacts with actin.
Interacts with ESR1, LRPPRC, RASSF1, microtubules and VCY2.
Interacts with WDR47 (via N-terminus of light chain) (By
similarity). Interacts (via C-terminus) with GAN (via Kelch
domains). {ECO:0000250, ECO:0000269|PubMed:15528209,
ECO:0000269|PubMed:16297881, ECO:0000269|PubMed:16565160}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
{ECO:0000250}. Cytoplasm, cytoskeleton
{ECO:0000269|PubMed:15528209}. Cytoplasm, cytoskeleton, spindle
{ECO:0000269|PubMed:15528209}. Note=Detected in perinuclear
punctate network corresponding to mitochondrial aggregates and in
the nucleus in cells exhibiting apoptosis. Associated specifically
with microtubules stabilized by paclitaxel and colocalizes with
RASSF1. In interphase cells, shows a diffuse cytoplasmic staining
with partial localization to the microtubules. During the
different stages of mitosis detected at the spindle microtubules.
Detected in filopodia-like protrusions and synapses (By
similarity). {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in ventral and dorsal horns of the
spinal cord, hippocampus, cerebral cortex, molecular, Purkinje and
granular cell layers of the cerebellum and in dorsal root ganglia
of the PNS (at protein level). Expressed in brain, testis, heart,
lung, kidney and liver. {ECO:0000269|PubMed:15528209,
ECO:0000269|PubMed:16297881}.
-!- DEVELOPMENTAL STAGE: Expressed in embryo at 10 dpc onwards (at
protein level). {ECO:0000269|PubMed:16297881}.
-!- DOMAIN: Its C-terminal part of the heavy chain interacts with ESR1
(By similarity). The N-terminus of the heavy chain associates with
the C-terminus of the light chain to form the heterodimer complex.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the MAP1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH52828.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH52828.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. At the N-terminus.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; DQ387862; ABD47683.1; -; mRNA.
EMBL; AK032300; BAC27800.1; -; mRNA.
EMBL; AK162124; BAE36739.1; -; mRNA.
EMBL; AC019302; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC052828; AAH52828.1; ALT_INIT; mRNA.
CCDS; CCDS22387.1; -.
RefSeq; NP_766601.2; NM_173013.3.
UniGene; Mm.248559; -.
ProteinModelPortal; Q8C052; -.
IntAct; Q8C052; 3.
MINT; Q8C052; -.
STRING; 10090.ENSMUSP00000019405; -.
iPTMnet; Q8C052; -.
PhosphoSitePlus; Q8C052; -.
EPD; Q8C052; -.
MaxQB; Q8C052; -.
PaxDb; Q8C052; -.
PeptideAtlas; Q8C052; -.
PRIDE; Q8C052; -.
Ensembl; ENSMUST00000019405; ENSMUSP00000019405; ENSMUSG00000019261.
GeneID; 270058; -.
KEGG; mmu:270058; -.
UCSC; uc009mcd.2; mouse.
CTD; 55201; -.
MGI; MGI:2443304; Map1s.
eggNOG; KOG3592; Eukaryota.
eggNOG; ENOG410XRYM; LUCA.
GeneTree; ENSGT00550000074593; -.
HOGENOM; HOG000072716; -.
HOVERGEN; HBG108117; -.
InParanoid; Q8C052; -.
KO; K10429; -.
OMA; PCEFEHR; -.
OrthoDB; EOG091G12OH; -.
TreeFam; TF350229; -.
ChiTaRS; Map1s; mouse.
PRO; PR:Q8C052; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000019261; Expressed in 244 organ(s), highest expression level in CA1 field of hippocampus.
CleanEx; MM_MTAP1S; -.
ExpressionAtlas; Q8C052; baseline and differential.
Genevisible; Q8C052; MM.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0042995; C:cell projection; ISO:MGI.
GO; GO:0005829; C:cytosol; ISS:HGNC.
GO; GO:0030425; C:dendrite; IDA:HGNC.
GO; GO:0005874; C:microtubule; ISO:MGI.
GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
GO; GO:0043025; C:neuronal cell body; IDA:HGNC.
GO; GO:0005730; C:nucleolus; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:HGNC.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISS:HGNC.
GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
GO; GO:0045202; C:synapse; ISO:MGI.
GO; GO:0051015; F:actin filament binding; IDA:HGNC.
GO; GO:0048487; F:beta-tubulin binding; ISS:HGNC.
GO; GO:0003677; F:DNA binding; ISS:HGNC.
GO; GO:0042802; F:identical protein binding; IDA:MGI.
GO; GO:0008017; F:microtubule binding; IDA:HGNC.
GO; GO:0015631; F:tubulin binding; IDA:HGNC.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0007420; P:brain development; IEP:HGNC.
GO; GO:0001578; P:microtubule bundle formation; ISS:HGNC.
GO; GO:0000226; P:microtubule cytoskeleton organization; IDA:MGI.
GO; GO:0007399; P:nervous system development; IEP:HGNC.
GO; GO:0048812; P:neuron projection morphogenesis; ISS:HGNC.
GO; GO:0010848; P:regulation of chromatin disassembly; ISS:BHF-UCL.
InterPro; IPR026074; MAP1.
InterPro; IPR027322; MAP1S.
InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
PANTHER; PTHR13843; PTHR13843; 2.
PANTHER; PTHR13843:SF11; PTHR13843:SF11; 2.
SUPFAM; SSF56281; SSF56281; 2.
1: Evidence at protein level;
Apoptosis; Complete proteome; Cytoplasm; Cytoskeleton; DNA-binding;
Microtubule; Nucleus; Phosphoprotein; Reference proteome.
CHAIN 1 973 Microtubule-associated protein 1S.
/FTId=PRO_0000311382.
CHAIN 1 742 MAP1S heavy chain.
/FTId=PRO_0000311383.
CHAIN 743 973 MAP1S light chain.
/FTId=PRO_0000311384.
REGION 1 716 Necessary for the microtubule-organizing
center localization. {ECO:0000250}.
REGION 601 973 Necessary for interaction with RASSF1.
{ECO:0000250}.
REGION 645 880 Necessary for association with
microtubules.
REGION 875 973 Necessary for association with actin.
REGION 881 905 Necessary for the mitochondrial
aggregation and genome destruction.
{ECO:0000250}.
COMPBIAS 560 850 Pro-rich.
MOD_RES 462 462 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 586 586 Phosphoserine.
{ECO:0000250|UniProtKB:P0C5W1}.
MOD_RES 591 591 Phosphoserine.
{ECO:0000250|UniProtKB:Q66K74}.
MOD_RES 593 593 Phosphoserine.
{ECO:0000250|UniProtKB:Q66K74}.
MOD_RES 660 660 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 684 684 Phosphoserine.
{ECO:0000250|UniProtKB:Q66K74}.
MOD_RES 724 724 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CONFLICT 475 475 E -> G (in Ref. 4; AAH52828).
{ECO:0000305}.
CONFLICT 680 680 P -> T (in Ref. 1; ABD47683 and 2;
BAC27800). {ECO:0000305}.
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


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