MAP9_HUMAN
ID MAP9_HUMAN Reviewed; 647 AA.
AC Q49MG5; Q4W5I7; Q68DU1; Q9H781; Q9H7B6;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Microtubule-associated protein 9;
DE AltName: Full=Aster-associated protein;
GN Name=MAP9; Synonyms=ASAP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND VARIANT TRP-177.
RX PubMed=16049101; DOI=10.1073/pnas.0500964102;
RA Saffin J.-M., Venoux M., Prigent C., Espeut J., Poulat F., Giorgi D.,
RA Abrieu A., Rouquier S.;
RT "ASAP, a human microtubule-associated protein required for bipolar spindle
RT assembly and cytokinesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11302-11307(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 114-574 (ISOFORM 1), AND VARIANT TRP-177.
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 456-647, AND VARIANT ASP-601.
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA 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 ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-12, AND IDENTIFICATION BY
RP 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).
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.
CC {ECO:0000269|PubMed:16049101}.
CC -!- SUBUNIT: Binds to purified microtubules via its C-terminus.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16049101}.
CC Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16049101}. Cytoplasm,
CC cytoskeleton, spindle {ECO:0000269|PubMed:16049101}. Note=Localizes to
CC microtubules in interphase, associates with the mitotic spindle during
CC mitosis, localizes to the central body during cytokinesis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q49MG5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q49MG5-2; Sequence=VSP_020037, VSP_020038;
CC -!- DEVELOPMENTAL STAGE: Constitutively expressed during the cell cycle.
CC {ECO:0000269|PubMed:16049101}.
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DR EMBL; AY690636; AAW02921.1; -; mRNA.
DR EMBL; AK024730; BAB14978.1; ALT_SEQ; mRNA.
DR EMBL; AK024812; BAB15017.1; -; mRNA.
DR EMBL; AC097467; AAY40981.1; -; Genomic_DNA.
DR EMBL; CR749274; CAH18129.1; -; mRNA.
DR CCDS; CCDS35493.1; -. [Q49MG5-1]
DR RefSeq; NP_001034669.1; NM_001039580.1. [Q49MG5-1]
DR RefSeq; XP_011530555.1; XM_011532253.1. [Q49MG5-1]
DR RefSeq; XP_011530556.1; XM_011532254.2. [Q49MG5-1]
DR AlphaFoldDB; Q49MG5; -.
DR SMR; Q49MG5; -.
DR BioGRID; 122969; 44.
DR IntAct; Q49MG5; 8.
DR STRING; 9606.ENSP00000310593; -.
DR iPTMnet; Q49MG5; -.
DR PhosphoSitePlus; Q49MG5; -.
DR BioMuta; MAP9; -.
DR DMDM; 116242626; -.
DR EPD; Q49MG5; -.
DR jPOST; Q49MG5; -.
DR MassIVE; Q49MG5; -.
DR MaxQB; Q49MG5; -.
DR PaxDb; Q49MG5; -.
DR PeptideAtlas; Q49MG5; -.
DR PRIDE; Q49MG5; -.
DR ProteomicsDB; 62073; -. [Q49MG5-1]
DR ProteomicsDB; 62074; -. [Q49MG5-2]
DR Antibodypedia; 48220; 93 antibodies from 21 providers.
DR DNASU; 79884; -.
DR Ensembl; ENST00000311277.9; ENSP00000310593.4; ENSG00000164114.19. [Q49MG5-1]
DR Ensembl; ENST00000650955.1; ENSP00000498412.1; ENSG00000164114.19. [Q49MG5-1]
DR GeneID; 79884; -.
DR KEGG; hsa:79884; -.
DR MANE-Select; ENST00000311277.9; ENSP00000310593.4; NM_001039580.2; NP_001034669.1.
DR UCSC; uc003ios.4; human. [Q49MG5-1]
DR CTD; 79884; -.
DR DisGeNET; 79884; -.
DR GeneCards; MAP9; -.
DR HGNC; HGNC:26118; MAP9.
DR HPA; ENSG00000164114; Tissue enhanced (brain, parathyroid gland).
DR MIM; 610070; gene.
DR neXtProt; NX_Q49MG5; -.
DR OpenTargets; ENSG00000164114; -.
DR PharmGKB; PA145148442; -.
DR VEuPathDB; HostDB:ENSG00000164114; -.
DR eggNOG; ENOG502R2PC; Eukaryota.
DR GeneTree; ENSGT00730000111184; -.
DR InParanoid; Q49MG5; -.
DR OMA; YMKEERD; -.
DR OrthoDB; 1024159at2759; -.
DR PhylomeDB; Q49MG5; -.
DR TreeFam; TF328794; -.
DR PathwayCommons; Q49MG5; -.
DR SignaLink; Q49MG5; -.
DR SIGNOR; Q49MG5; -.
DR BioGRID-ORCS; 79884; 5 hits in 1072 CRISPR screens.
DR ChiTaRS; MAP9; human.
DR GenomeRNAi; 79884; -.
DR Pharos; Q49MG5; Tbio.
DR PRO; PR:Q49MG5; -.
DR Proteomes; UP000005640; Chromosome 4.
DR RNAct; Q49MG5; protein.
DR Bgee; ENSG00000164114; Expressed in lateral nuclear group of thalamus and 190 other tissues.
DR ExpressionAtlas; Q49MG5; baseline and differential.
DR Genevisible; Q49MG5; HS.
DR GO; GO:0000235; C:astral microtubule; IDA:UniProtKB.
DR GO; GO:0030424; C:axon; ISS:ARUK-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0072686; C:mitotic spindle; IDA:UniProtKB.
DR GO; GO:1990023; C:mitotic spindle midzone; IEA:Ensembl.
DR GO; GO:0051233; C:spindle midzone; IDA:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; IMP:UniProtKB.
DR GO; GO:0000281; P:mitotic cytokinesis; IEA:InterPro.
DR GO; GO:0090307; P:mitotic spindle assembly; IDA:UniProtKB.
DR GO; GO:0046602; P:regulation of mitotic centrosome separation; IMP:UniProtKB.
DR GO; GO:1902412; P:regulation of mitotic cytokinesis; IMP:UniProtKB.
DR GO; GO:0060236; P:regulation of mitotic spindle organization; IMP:UniProtKB.
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:0007744|PubMed:19413330"
FT CHAIN 2..647
FT /note="Microtubule-associated protein 9"
FT /id="PRO_0000247753"
FT REGION 127..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 344..421
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 491..514
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 530..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..600
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 613..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 184..210
FT /evidence="ECO:0000255"
FT COILED 298..328
FT /evidence="ECO:0000255"
FT COILED 443..628
FT /evidence="ECO:0000255"
FT COMPBIAS 129..149
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..267
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 363..380
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..412
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 613..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:0007744|PubMed:19413330"
FT MOD_RES 12
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT VAR_SEQ 374..377
FT /note="RLMT -> ARSG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020037"
FT VAR_SEQ 378..647
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_020038"
FT VARIANT 146
FT /note="M -> V (in dbSNP:rs34082815)"
FT /id="VAR_051152"
FT VARIANT 177
FT /note="R -> W (in dbSNP:rs3733391)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:16049101"
FT /id="VAR_027151"
FT VARIANT 499
FT /note="K -> R (in dbSNP:rs1058992)"
FT /id="VAR_051153"
FT VARIANT 601
FT /note="N -> D (in dbSNP:rs2305050)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_051154"
FT CONFLICT 116
FT /note="M -> L (in Ref. 2; BAB14978)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="E -> G (in Ref. 2; BAB14978)"
FT /evidence="ECO:0000305"
FT CONFLICT 575
FT /note="E -> K (in Ref. 1; AAW02921)"
FT /evidence="ECO:0000305"
FT CONFLICT 631
FT /note="A -> T (in Ref. 4; CAH18129)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 647 AA; 74234 MW; 1F0BDE2986845B39 CRC64;
MSDEVFSTTL AYTKSPKVTK RTTFQDELIR AITARSARQR SSEYSDDFDS DEIVSLGDFS
DTSADENSVN KKMNDFHISD DEEKNPSKLL FLKTNKSNGN ITKDEPVCAI KNEEEMAPDG
CEDIVVKSFS ESQNKDEEFE KDKIKMKPKP RILSIKSTSS AENNSLDTDD HFKPSPRPRS
MLKKKSHMEE KDGLEDKETA LSEELELHSA PSSLPTPNGI QLEAEKKAFS ENLDPEDSCL
TSLASSSLKQ ILGDSFSPGS EGNASGKDPN EEITENHNSL KSDENKENSF SADHVTTAVE
KSKESQVTAD DLEEEKAKAE LIMDDDRTVD PLLSKSQSIL ISTSATASSK KTIEDRNIKN
KKSTNNRASS ASARLMTSEF LKKSSSKRRT PSTTTSSHYL GTLKVLDQKP SQKQSIEPDR
ADNIRAAVYQ EWLEKKNVYL HEMHRIKRIE SENLRIQNEQ KKAAKREEAL ASFEAWKAMK
EKEAKKIAAK KRLEEKNKKK TEEENAARKG EALQAFEKWK EKKMEYLKEK NRKEREYERA
KKQKEEETVA EKKKDNLTAV EKWNEKKEAF FKQKEKEKIN EKRKEELKRA EKKDKDKQAI
NEYEKWLENK EKQERIERKQ KKRHSFLESE ALPPWSPPSR TVFAKVF
