MAP1S_RAT
ID MAP1S_RAT Reviewed; 972 AA.
AC P0C5W1;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Microtubule-associated protein 1S;
DE Short=MAP-1S;
DE Contains:
DE RecName: Full=MAP1S heavy chain;
DE Contains:
DE RecName: Full=MAP1S light chain;
GN Name=Map1s;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP INTERACTION WITH ESR1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=17658481; DOI=10.1016/j.bbrc.2007.06.179;
RA Eriksson M., Samuelsson H., Samuelsson E.-B., Liu L., McKeehan W.L.,
RA Benedikz E., Sundstroem E.;
RT "The NMDAR subunit NR3A interacts with microtubule-associated protein 1S in
RT the brain.";
RL Biochem. Biophys. Res. Commun. 361:127-132(2007).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-462; SER-585 AND SER-723, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Microtubule-associated protein that mediates aggregation of
CC mitochondria resulting in cell death and genomic destruction (MAGD).
CC Plays a role in anchoring the microtubule organizing center to the
CC centrosomes. Binds to DNA. Plays a role in apoptosis. Involved in the
CC formation of microtubule bundles (By similarity). {ECO:0000250}.
CC -!- 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 LRPPRC, RASSF1, microtubules and VCY2. Interacts (via C-terminus) with
CC GAN (via Kelch domains). Interacts with WDR47 (via N-terminus of light
CC chain) (By similarity). Interacts with ESR1. {ECO:0000250,
CC ECO:0000269|PubMed:17658481}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm, cytosol
CC {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17658481}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:17658481}.
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 (By similarity). Detected in filopodia-like
CC protrusions and synapses. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in cortex cerebellum, dorsal root
CC ganglia, frontal cortex, hippocampus, hypothalamus, mesencephalon,
CC medulla oblongata, occipital cortex, pons, spinal cord, striatum of the
CC brain, neurons, heart, testis and skeletal muscle (at protein level).
CC {ECO:0000269|PubMed:17658481}.
CC -!- DOMAIN: The N-terminus of the heavy chain associates with the C-
CC terminus of the light chain to form the heterodimer complex. Its C-
CC terminal part of the heavy chain interacts with ESR1 (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the MAP1A/MAP1B/MAP1S family. {ECO:0000305}.
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DR EMBL; AABR03102209; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03103182; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001099540.1; NM_001106070.1.
DR AlphaFoldDB; P0C5W1; -.
DR BioGRID; 253262; 2.
DR IntAct; P0C5W1; 1.
DR STRING; 10116.ENSRNOP00000025385; -.
DR iPTMnet; P0C5W1; -.
DR PhosphoSitePlus; P0C5W1; -.
DR SwissPalm; P0C5W1; -.
DR jPOST; P0C5W1; -.
DR PaxDb; P0C5W1; -.
DR PRIDE; P0C5W1; -.
DR GeneID; 290640; -.
DR KEGG; rno:290640; -.
DR UCSC; RGD:1308266; rat.
DR CTD; 55201; -.
DR RGD; 1308266; Map1s.
DR eggNOG; KOG3592; Eukaryota.
DR HOGENOM; CLU_000285_2_0_1; -.
DR InParanoid; P0C5W1; -.
DR OrthoDB; 86642at2759; -.
DR PhylomeDB; P0C5W1; -.
DR TreeFam; TF350229; -.
DR PRO; PR:P0C5W1; -.
DR Proteomes; UP000002494; Unplaced.
DR Genevisible; P0C5W1; RN.
DR GO; GO:0042995; C:cell projection; ISO:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0030425; C:dendrite; ISO:RGD.
DR GO; GO:0005874; C:microtubule; ISO:RGD.
DR GO; GO:0005875; C:microtubule associated complex; IBA:GO_Central.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISO:RGD.
DR GO; GO:0043025; C:neuronal cell body; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005819; C:spindle; ISO:RGD.
DR GO; GO:0045202; C:synapse; ISO:RGD.
DR GO; GO:0003779; F:actin binding; IBA:GO_Central.
DR GO; GO:0051015; F:actin filament binding; ISO:RGD.
DR GO; GO:0048487; F:beta-tubulin binding; ISO:RGD.
DR GO; GO:0003677; F:DNA binding; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; ISO:RGD.
DR GO; GO:0008017; F:microtubule binding; ISO:RGD.
DR GO; GO:0015631; F:tubulin binding; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0016358; P:dendrite development; IBA:GO_Central.
DR GO; GO:0001578; P:microtubule bundle formation; ISO:RGD.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; ISO:RGD.
DR GO; GO:0007399; P:nervous system development; ISO:RGD.
DR GO; GO:0048812; P:neuron projection morphogenesis; ISO:RGD.
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..972
FT /note="Microtubule-associated protein 1S"
FT /id="PRO_0000311385"
FT CHAIN 1..741
FT /note="MAP1S heavy chain"
FT /id="PRO_0000311386"
FT CHAIN 742..972
FT /note="MAP1S light chain"
FT /id="PRO_0000311387"
FT REGION 1..715
FT /note="Necessary for the microtubule-organizing center
FT localization"
FT /evidence="ECO:0000250"
FT REGION 454..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 600..972
FT /note="Necessary for interaction with RASSF1"
FT /evidence="ECO:0000250"
FT REGION 644..879
FT /note="Necessary for association with microtubules"
FT /evidence="ECO:0000250"
FT REGION 671..854
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 874..972
FT /note="Necessary for association with actin"
FT /evidence="ECO:0000250"
FT REGION 880..904
FT /note="Necessary for the mitochondrial aggregation and
FT genome destruction"
FT /evidence="ECO:0000250"
FT COMPBIAS 492..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 566..584
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..632
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 766..780
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 837..852
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 462
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 585
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 592
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 659
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8C052"
FT MOD_RES 683
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q66K74"
FT MOD_RES 723
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 972 AA; 102806 MW; 7C666A9BA457E678 CRC64;
MAAVMAAPEP AEAPSSLLLL VVGGECGCPG LLAYVLEELE RGVRSWEDVD PDVCSLDEQL
KAFVSRHSAT FSSIVKGQRS LHHRGETLET LVLLNPSDKS LCDELRNLLM DPAPHKLLVL
AGPCLEETGE LLLQTGGFSA HHFLQVLGDK EVQDALASAP AAPALTVSCP TFGDWALLGP
APGLRLRLNP PARLPSSEGL RAFLEYVAES LEPPSPFELL EPPATGGFLR LARPCCYVFP
GGLGDAAFFA VNGFTVLVNG GSNPKSSFWK LVRHLDRVDA VLVTHAGADS LPGLNSLLRR
KLAEREAAAG PQGQHEERLR RLLSPALGVV FLNAREAGSR LRGGEDEAVC ARSLLRSLGI
VPLPLQRGPQ PSCPTVLFEK LGVGRLELFV LHPPPGDPAA PACALLVWQP AAPGDKVVRV
LFPGRTPPAR LLDGLQRLQH LPCLRRPVVT TQDLEVPSRA NSQDSLASRD STRKEPVRGT
VGATSRSAVR REPALATRDQ KKDTKPGPTR STVRDVRRSG PGVVTTKPRV SQNGPRAPVP
AAPPAAPAPE FPGEAENIVE SERPPAPSPT LSPAQSPPPT APGNSPERLS LSPLRPEPAP
DASPSATTPT LTTPSLPAEL GSPHSTEVDE SLSVSFEQVL PAGDAGLSLP LRLARRSTSP
HDVDLCLVSP CEFSHRKPPP PASPGSSDSS ARSQERPPET PPTSVSESLP TLSDSDPVPV
ADSDDDAGSE SAARDPLPTP RVPPPLPDAP GICMVDPEAL PPRARQPLST ANSSRGRKAP
ARPSSASAAP RAATVAAKTK GPVGDRSRPL SARSEPADKP GRVPLTRKPS VPKTVPKMAS
ATRNSSGPSS RPAPLAAGSP VYLDLAYLPG GGAGHLDQNF FLRVRALCYV ISGQGQRQEE
GLRGVLDALL AGKRQWDLDL QVTLIPTFDS AVMHRWYEET HEQHQALGIR VLGSGSLVSM
QDEAFPACKV EF
