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MTUS2_MOUSE
ID   MTUS2_MOUSE             Reviewed;        1353 AA.
AC   Q3UHD3; B9EKJ2; Q7TPP7; Q8CHD2; Q9CY74;
DT   06-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
DE   RecName: Full=Microtubule-associated tumor suppressor candidate 2 homolog;
DE   AltName: Full=Cardiac zipper protein;
DE   AltName: Full=Microtubule plus-end tracking protein TIP150;
DE            Short=Tracking protein of 150 kDa;
GN   Name=Mtus2; Synonyms=Cazip, Kiaa0774, Tip150;
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] (ISOFORMS 1 AND 4).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, and Placenta;
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] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, and Eye;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 201-1117 AND 1155-1353 (ISOFORM
RP   1).
RX   PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT   The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 9:179-188(2002).
RN   [4]
RP   ALTERNATIVE SPLICING, AND TISSUE SPECIFICITY.
RX   PubMed=19806667; DOI=10.1002/dvdy.22107;
RA   Du Puy L., Beqqali A., Monshouwer-Kloots J., Haagsman H.P., Roelen B.A.,
RA   Passier R.;
RT   "CAZIP, a novel protein expressed in the developing heart and nervous
RT   system.";
RL   Dev. Dyn. 238:2903-2911(2009).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364 AND SER-365, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, and Heart;
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: Binds microtubules. Together with MAPRE1 may target the
CC       microtubule depolymerase KIF2C to the plus-end of microtubules. May
CC       regulate the dynamics of microtubules at their growing distal tip (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer. Interacts with KIF2C and MAPRE1; the interaction is
CC       direct and probably targets MTUS2 and KIF2C to microtubules (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Note=Associated with the
CC       microtubule network at the growing distal tip (the plus-end) of
CC       microtubules. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3UHD3-1; Sequence=Displayed;
CC       Name=3;
CC         IsoId=Q3UHD3-3; Sequence=VSP_023545, VSP_023546;
CC       Name=4;
CC         IsoId=Q3UHD3-4; Sequence=VSP_023544, VSP_023548;
CC   -!- TISSUE SPECIFICITY: Expressed in heart from early embryonic development
CC       onwards. Later during embryonic development, expressed in brain and
CC       nervous system, in limb buds and in the epithelium lining the bronchia
CC       of the lung. Detected in adult brain, heart and eye, but not detected
CC       in other adult tissues examined. {ECO:0000269|PubMed:19806667}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the MTUS1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC41447.2; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; AK019985; BAB31952.1; -; mRNA.
DR   EMBL; AK147457; BAE27924.1; -; mRNA.
DR   EMBL; BC055016; AAH55016.1; -; mRNA.
DR   EMBL; BC150942; AAI50943.1; -; mRNA.
DR   EMBL; AB093263; BAC41447.2; ALT_SEQ; Unassigned_RNA.
DR   CCDS; CCDS19881.1; -. [Q3UHD3-1]
DR   RefSeq; NP_084196.4; NM_029920.7. [Q3UHD3-1]
DR   RefSeq; XP_006504953.1; XM_006504890.3.
DR   AlphaFoldDB; Q3UHD3; -.
DR   SMR; Q3UHD3; -.
DR   BioGRID; 218742; 1.
DR   IntAct; Q3UHD3; 1.
DR   MINT; Q3UHD3; -.
DR   STRING; 10090.ENSMUSP00000082694; -.
DR   iPTMnet; Q3UHD3; -.
DR   PhosphoSitePlus; Q3UHD3; -.
DR   EPD; Q3UHD3; -.
DR   MaxQB; Q3UHD3; -.
DR   PaxDb; Q3UHD3; -.
DR   PeptideAtlas; Q3UHD3; -.
DR   PRIDE; Q3UHD3; -.
DR   ProteomicsDB; 290120; -. [Q3UHD3-1]
DR   ProteomicsDB; 290121; -. [Q3UHD3-3]
DR   ProteomicsDB; 290122; -. [Q3UHD3-4]
DR   Antibodypedia; 22727; 93 antibodies from 24 providers.
DR   Ensembl; ENSMUST00000085554; ENSMUSP00000082690; ENSMUSG00000029651. [Q3UHD3-4]
DR   Ensembl; ENSMUST00000085558; ENSMUSP00000082694; ENSMUSG00000029651. [Q3UHD3-1]
DR   Ensembl; ENSMUST00000110515; ENSMUSP00000106144; ENSMUSG00000029651. [Q3UHD3-3]
DR   GeneID; 77521; -.
DR   KEGG; mmu:77521; -.
DR   UCSC; uc009aon.2; mouse. [Q3UHD3-1]
DR   UCSC; uc009aop.2; mouse. [Q3UHD3-3]
DR   UCSC; uc009aoq.2; mouse. [Q3UHD3-4]
DR   CTD; 23281; -.
DR   MGI; MGI:1915388; Mtus2.
DR   VEuPathDB; HostDB:ENSMUSG00000029651; -.
DR   eggNOG; ENOG502QQFP; Eukaryota.
DR   GeneTree; ENSGT00950000183026; -.
DR   HOGENOM; CLU_005465_0_0_1; -.
DR   InParanoid; Q3UHD3; -.
DR   OMA; NTCQQKI; -.
DR   OrthoDB; 250283at2759; -.
DR   PhylomeDB; Q3UHD3; -.
DR   TreeFam; TF333416; -.
DR   BioGRID-ORCS; 77521; 1 hit in 58 CRISPR screens.
DR   ChiTaRS; Mtus2; mouse.
DR   PRO; PR:Q3UHD3; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q3UHD3; protein.
DR   Bgee; ENSMUSG00000029651; Expressed in interventricular septum and 175 other tissues.
DR   ExpressionAtlas; Q3UHD3; baseline and differential.
DR   Genevisible; Q3UHD3; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005881; C:cytoplasmic microtubule; ISO:MGI.
DR   GO; GO:0045171; C:intercellular bridge; ISO:MGI.
DR   GO; GO:0015630; C:microtubule cytoskeleton; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; ISO:MGI.
DR   GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR   GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB.
DR   InterPro; IPR033339; MTUS2.
DR   PANTHER; PTHR24200:SF14; PTHR24200:SF14; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Microtubule;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..1353
FT                   /note="Microtubule-associated tumor suppressor candidate 2
FT                   homolog"
FT                   /id="PRO_0000280112"
FT   REGION          1..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          81..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          125..259
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          274..615
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          626..964
FT                   /note="Mediates interaction with MAPRE1"
FT                   /evidence="ECO:0000250"
FT   REGION          786..1134
FT                   /note="Localization to the growing distal tip of
FT                   microtubules"
FT                   /evidence="ECO:0000250"
FT   REGION          786..874
FT                   /note="Sufficient for interaction with KIF2C"
FT                   /evidence="ECO:0000250"
FT   REGION          799..823
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          847..972
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1315..1353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          976..1319
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        86..101
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        125..139
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..170
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        226..249
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        329..343
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        346..360
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        445..478
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..513
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        520..584
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        594..615
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..814
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        847..874
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..914
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         364
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         365
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..1201
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_023544"
FT   VAR_SEQ         1..1005
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023545"
FT   VAR_SEQ         1006..1023
FT                   /note="AIQGFDALAVSTKHFFGK -> MGHHCCKPYICLQCLDKT (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_023546"
FT   VAR_SEQ         1202..1210
FT                   /note="RKTTEEQLE -> MSLRTWARH (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_023548"
SQ   SEQUENCE   1353 AA;  147356 MW;  BFBFF33BA1A91B43 CRC64;
     MSVPLAPKKS CFGQLRDHRE GAKNNNESIL RTGDTNANQI MLEVSSSCDE AKSRDLDDEL
     GNSNLSRPQY HSHFQKEPLH LQGFGKGSQA GSTSQRESQA SLTVHRQLSE EHAVKRGALQ
     APQCVQGPSL SSWRNAVGQA SPEASAKKDA EIPRHIPKDK LAKTLDNEEL KRASSCSAAA
     GSVPPTDLQP VQLDTLGPQD HVPARGEGPQ RTPASHSPGK GFSPGEGTSE GNSVYLPKPS
     TSEAKGSSPS DTKMEGPHGL DVYNERITHA ELTPSSASAS KENPGLRHPE VCLGQGTGKS
     KVELKSVQPR NEEGLTSAQA QGPGCHEERS MSPVERQELL EKAYREATSQ GNSSHRQLGV
     RRGSSLEEMT GVSAGVEGSQ QATPTLSAAP AGEAGTRLTG KMSAGVGRMA RETASGQTAP
     DVGQAAPVRR DPTESVPSEV SGEERRLGSG NSGSTKLLAS GPSAGGSRTD TSGLLSPRGS
     NLEARKGKEM VAENRNLLEN AAQTDNTPAG VDSAFSTPAP LLHPETTVNS SHHPTPPGSS
     SQELGVFSGD TGSPSVASPP TDGGQVLNTS PKVPDRTTCS SGIPKPPTHP KDTPSSQEAR
     EKLETEKMEE RAEAKPILMP KPKHVRPKII TYIRRNPQAL SQGDASLVPV GLPYAPPTCG
     MPLPQEEKAA SRDLQPSANM YEKLKPDLQK PRVFPSGLMV SGIKPPAHHF SQMSEKFLQE
     VADHPGKEEF CSPPYTHYEV PPTFYRSAML LKPQLGLGAM SRLPSTKSRI LIASQRSSAS
     AIHPPGSLTT AASFYGSDPS DLKKASNSNA AKASLPKSGL RPPGYSRLPA AKLAAFGFVR
     SSSISAVPSS QSLDSVQPEQ SRPVTRSTFG NEEQAPLKQA LPSKDTPKGA GRAAPASSSN
     ATTPRRSLLP APKSTSTPAG AKKELQKDPE AKKPAVSSPK RTASAATKPH SPGYPKQRTS
     APRNEFPPKP DLQAREAERQ LAQRLRDRCE WQARQLGLAR RELKKAIQGF DALAVSTKHF
     FGKSERALAK EKELSIELAN IRDEVAFNTA KCEKLQKEKE TLERRFEEEL RRLGWQQQAE
     VQELQERLQQ QFQAESARLQ AEHQDQLLRM RCQHQEQVED ITASHEAALL EMENNHTVAI
     TILQDDHDHK VQELMSTHEF EKKELEENFE KLRLTLQDQV DTLTFQSQSL RDRARRFEEA
     LRKTTEEQLE IALAPYQHLE EDMQSLKQVL EMKNQQIHLQ EKKIIELEKL VEKNIILEER
     IQVLQQQNED LKARIDQNTV VTRQLSEENA NLQEYVEKET QEKKRLSRTN EELLWKLQTG
     DPTSPIKLSP TSPVYRGSSS GPSSPARVST TPR
 
 
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