MAP9_MOUSE
ID MAP9_MOUSE Reviewed; 646 AA.
AC Q3TRR0; Q3UUD1; Q3UX85; Q3UXE7; Q5M8N8; Q6P8K1; Q8BMM4; Q8BYP7;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-JUL-2006, sequence version 2.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Microtubule-associated protein 9;
DE AltName: Full=Aster-associated protein;
GN Name=Map9; Synonyms=Asap, Mtap9;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-493 (ISOFORM 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Cerebellum, Egg, Hypothalamus, Pituitary, and Spinal cord;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-495.
RC TISSUE=Pituitary;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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: Involved in organization of the bipolar mitotic spindle.
CC Required for bipolar spindle assembly, mitosis progression and
CC cytokinesis. May act by stabilizing interphase microtubules (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Binds to purified microtubules via its C-terminus.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton {ECO:0000250}.
CC Cytoplasm, cytoskeleton, spindle {ECO:0000250}. Note=Localizes to
CC microtubules in interphase, associates with the mitotic spindle during
CC mitosis, localizes to the central body during cytokinesis.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q3TRR0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q3TRR0-2; Sequence=VSP_020039;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH61216.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AAH87935.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
CC Sequence=AK147287; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK030527; BAC27004.2; -; mRNA.
DR EMBL; AK038737; BAC30117.1; -; mRNA.
DR EMBL; AK135702; BAE22616.1; -; mRNA.
DR EMBL; AK135823; BAE22678.1; -; mRNA.
DR EMBL; AK138540; BAE23696.1; -; mRNA.
DR EMBL; AK147287; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK162555; BAE36967.1; -; mRNA.
DR EMBL; BC061216; AAH61216.1; ALT_SEQ; mRNA.
DR EMBL; BC087935; AAH87935.1; ALT_SEQ; mRNA.
DR CCDS; CCDS38461.1; -. [Q3TRR0-1]
DR RefSeq; NP_001074699.1; NM_001081230.1. [Q3TRR0-1]
DR RefSeq; XP_006501341.1; XM_006501278.3.
DR AlphaFoldDB; Q3TRR0; -.
DR SMR; Q3TRR0; -.
DR BioGRID; 229458; 6.
DR IntAct; Q3TRR0; 3.
DR STRING; 10090.ENSMUSP00000088535; -.
DR iPTMnet; Q3TRR0; -.
DR PhosphoSitePlus; Q3TRR0; -.
DR MaxQB; Q3TRR0; -.
DR PaxDb; Q3TRR0; -.
DR PeptideAtlas; Q3TRR0; -.
DR PRIDE; Q3TRR0; -.
DR ProteomicsDB; 295822; -. [Q3TRR0-1]
DR ProteomicsDB; 295823; -. [Q3TRR0-2]
DR Antibodypedia; 48220; 93 antibodies from 21 providers.
DR DNASU; 213582; -.
DR Ensembl; ENSMUST00000091014; ENSMUSP00000088535; ENSMUSG00000033900. [Q3TRR0-1]
DR Ensembl; ENSMUST00000195640; ENSMUSP00000142206; ENSMUSG00000033900. [Q3TRR0-1]
DR GeneID; 213582; -.
DR KEGG; mmu:213582; -.
DR UCSC; uc008pow.1; mouse. [Q3TRR0-1]
DR UCSC; uc012cqt.1; mouse. [Q3TRR0-2]
DR CTD; 79884; -.
DR MGI; MGI:2442208; Map9.
DR VEuPathDB; HostDB:ENSMUSG00000033900; -.
DR eggNOG; ENOG502R2PC; Eukaryota.
DR GeneTree; ENSGT00730000111184; -.
DR HOGENOM; CLU_030160_0_0_1; -.
DR InParanoid; Q3TRR0; -.
DR OMA; YMKEERD; -.
DR OrthoDB; 1024159at2759; -.
DR PhylomeDB; Q3TRR0; -.
DR TreeFam; TF328794; -.
DR BioGRID-ORCS; 213582; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Map9; mouse.
DR PRO; PR:Q3TRR0; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; Q3TRR0; protein.
DR Bgee; ENSMUSG00000033900; Expressed in otolith organ and 208 other tissues.
DR ExpressionAtlas; Q3TRR0; baseline and differential.
DR Genevisible; Q3TRR0; MM.
DR GO; GO:0005818; C:aster; IDA:MGI.
DR GO; GO:0000235; C:astral microtubule; IDA:MGI.
DR GO; GO:0030424; C:axon; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:1990023; C:mitotic spindle midzone; IDA:MGI.
DR GO; GO:0051233; C:spindle midzone; ISO:MGI.
DR GO; GO:0008017; F:microtubule binding; ISO:MGI.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR GO; GO:0090307; P:mitotic spindle assembly; IDA:MGI.
DR GO; GO:0046602; P:regulation of mitotic centrosome separation; ISO:MGI.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; ISO:MGI.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; ISO:MGI.
DR InterPro; IPR026106; MAP9.
DR PANTHER; PTHR14739; PTHR14739; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Coiled coil;
KW Cytoplasm; Cytoskeleton; Microtubule; Mitosis; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q49MG5"
FT CHAIN 2..646
FT /note="Microtubule-associated protein 9"
FT /id="PRO_0000247754"
FT REGION 75..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 242..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 531..554
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 570..597
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..646
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 442..596
FT /evidence="ECO:0000255"
FT COMPBIAS 75..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..128
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 129..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..226
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..295
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..324
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..341
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..361
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..402
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 609..628
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q49MG5"
FT MOD_RES 12
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q49MG5"
FT VAR_SEQ 429..458
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_020039"
FT CONFLICT 185
FT /note="K -> P (in Ref. 1; BAE36967)"
FT /evidence="ECO:0000305"
FT CONFLICT 205
FT /note="S -> H (in Ref. 1; BAE36967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 646 AA; 73511 MW; F5309EDE68557839 CRC64;
MSDEIFSTTL AYTKSPKATK RTSFQDELIR AITARSARQR SSEYSDDFDS DEIVSLGEFS
DTSTDESLVR KKMNDFHISD DEEKNSPRLS FLKTKKVNRA ISNDALDSST PGSEGSSPDA
QEDVTGDSLP KSQNDDREVG REIITVKPTP RMHPVKRSTS SGETSSGLDA DGHFKPSPQP
RSMLKKSSHT EEGVRPGVDK EHSISEASAP TPSLPRQNGT ELQTEEKIYS ENLDLEDSLL
QSLTSSSFKE SPGGCTSPGS QEKVPIKDHD GEPTEIWDSL LSNENEGSSV LVNCVTPELE
QPKDGQVAAD DLEEEREKGG FTEDDLTTDP LLSTSPSVIT PTEPAEPAKK ANEDRNTKNK
KTTNNRVSSA SGRLMTSEFL KRSGPTKRSP SAATSSHYLG SLKVLDQKQP RKQSLEPDKA
DHIRAAVYQE WLEKKNVYLH EMHRIKRIES ENLRIQNEQK KAAKREEALA SFEAWKAMKE
KEAKRIAAKK RLEEKNKKKT EEENAMRKGE ALQAFEKWKE KKLEYLKEKT RREKEYERAK
KQKEEEAVAE KKKDSLTAFE KWSERKEALL KQKEKEKINE RRKEELKRAE KKDKDKQAIS
EYEKWLEKKE RQERIERKQK KRHSFLESET HPPWSPPSRT APSKVF
