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MTUS1_XENLA
ID   MTUS1_XENLA             Reviewed;        1338 AA.
AC   Q7SZL5; Q9PTL6;
DT   02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 54.
DE   RecName: Full=Microtubule-associated tumor suppressor 1 homolog;
DE   AltName: Full=F-box protein 27;
DE   AltName: Full=Inner centromere KinI stimulator;
DE   AltName: Full=Mitochondrial tumor suppressor 1 homolog;
GN   Name=mtus1; Synonyms=fbx27, icis;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), IDENTIFICATION BY MASS
RP   SPECTROMETRY, SUBUNIT, INTERACTION WITH KIF2C; AURKB; INCENP AND SKP1,
RP   TISSUE SPECIFICITY, FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=12919681; DOI=10.1016/s1534-5807(03)00229-6;
RA   Ohi R., Coughlin M.L., Lane W.S., Mitchison T.J.;
RT   "An inner centromere protein that stimulates the microtubule depolymerizing
RT   activity of a KinI kinesin.";
RL   Dev. Cell 5:309-321(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 672-1140 (ISOFORM 2), AND POSSIBLE
RP   INTERACTION WITH SKP1.
RC   TISSUE=Oocyte;
RX   PubMed=10531041; DOI=10.1016/s0960-9822(00)80006-8;
RA   Regan-Reimann J.D., Duong Q.V., Jackson P.K.;
RT   "Identification of novel F-box proteins in Xenopus laevis.";
RL   Curr. Biol. 9:R762-R763(1999).
CC   -!- FUNCTION: Regulates microtubule dynamics during mitosis by stimulating
CC       kif2c. Probably recognizes and binds to some phosphorylated proteins
CC       and promotes their ubiquitination and degradation.
CC       {ECO:0000269|PubMed:12919681}.
CC   -!- SUBUNIT: Homodimer (Probable). Binds microtubules. Interacts with
CC       kif2c, aurkb, incenp and SKP1. Probably part of a SCF (SKP1-CUL1-F-box)
CC       protein ligase complex. {ECO:0000269|PubMed:12919681, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12919681}. Cytoplasm,
CC       cytoskeleton {ECO:0000269|PubMed:12919681}. Chromosome
CC       {ECO:0000269|PubMed:12919681}. Midbody {ECO:0000269|PubMed:12919681}.
CC       Note=Chromosomal until metaphase. Located at the midbody during
CC       telophase.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q7SZL5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q7SZL5-2; Sequence=VSP_028286;
CC   -!- TISSUE SPECIFICITY: Present in egg (at protein level).
CC       {ECO:0000269|PubMed:12919681}.
CC   -!- SIMILARITY: Belongs to the MTUS1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF14556.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR   EMBL; AY352638; AAQ22723.1; -; mRNA.
DR   EMBL; AF176665; AAF14556.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001082742.1; NM_001089273.1. [Q7SZL5-1]
DR   AlphaFoldDB; Q7SZL5; -.
DR   SMR; Q7SZL5; -.
DR   IntAct; Q7SZL5; 1.
DR   MaxQB; Q7SZL5; -.
DR   PRIDE; Q7SZL5; -.
DR   GeneID; 398697; -.
DR   KEGG; xla:398697; -.
DR   CTD; 398697; -.
DR   Xenbase; XB-GENE-979441; mtus1.L.
DR   OrthoDB; 91479at2759; -.
DR   Proteomes; UP000186698; Chromosome 1L.
DR   Bgee; 398697; Expressed in heart and 19 other tissues.
DR   GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR029786; MTUS1.
DR   PANTHER; PTHR24200:SF7; PTHR24200:SF7; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell cycle; Chromosome; Coiled coil; Cytoplasm;
KW   Cytoskeleton; Microtubule; Nucleus; Reference proteome;
KW   Ubl conjugation pathway.
FT   CHAIN           1..1338
FT                   /note="Microtubule-associated tumor suppressor 1 homolog"
FT                   /id="PRO_0000305202"
FT   DOMAIN          731..774
FT                   /note="F-box"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          536..585
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          636..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          788..808
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          883..925
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          938..962
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1309..1338
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          469..494
FT                   /evidence="ECO:0000255"
FT   COILED          966..1298
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        542..585
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..671
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        883..923
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        940..961
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1319..1338
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         798..938
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:10531041"
FT                   /id="VSP_028286"
SQ   SEQUENCE   1338 AA;  147067 MW;  628843528301A2EF CRC64;
     MSVQTATTEN RFQSTLDDNN GNNSESKNIA RCPKYEWNAN VNDQGPGVID HSILDQQSDN
     EINKHYLLQS PNALELDSTL DYIGNAAGHC DTFNLKADKG CKTVNSSLLH ENPGEEDETV
     DYINNELCNK MQDTLCPPSI PIQTSASDEI HKGLGAITDR GSAYNKIAEQ SLCVQESTDY
     LCKMEPKWTV QAFFGDADKL CRNEANNLVD ISTTDHKYDH NSSFGIFTLS LDFSDEKCMR
     EDSLVLSGSE KPLSASILEG SALPNSSIDV FTGSVKKTDN IDGFCQGAEL SLRDLDYLEV
     PHQKDSTETP QSKLSLTSEH SVFTSETSEV MLEVDARRVM DKTVESHLPN LRLSSNVGKE
     DSAPGASLEE FVSGSVPAVA PEELASNLIK DKNTIKNKES HGEAHSLESP ARPDSSSSEL
     KDLLSNLSGQ NCEDTFIISS PNSGIGSKAF TSTPLPESKN MTFSVPVLES ITENNELQQN
     LDAIKYDLEG LRHSSDSNIV TKPTNKKPAV GSVVGKAKKN EVISFPKPSF KNVKAKVLTR
     PSLQAKDSNP YASKTSPRSP PSLSNASSPA QSPRPLSSAV KTVQKRSVIN QDMKTEAAIA
     KSQKQPITKQ LFPTHSAHVP THSKHALGKV PRAAALKHTQ NETERASSSN STRSSGSAAA
     ALTCTAGSRV TENKSEKAKT SAKPSAPNVR LMGPNKIEQK GIIQPHFDKA QSLKEAKEGT
     VSADMDILAN IVPLPTKLAI PSSRNLHKEL ILGIKNVASQ PAKGRVQTTV QRRGSLGKNI
     LTIRVSSPPR EKPQVTVEGG LNSPKGRPIS VKASAANGTG SLPRTRLPCR GTTLQRTASV
     SSVCSTQSEL SNLSTRSTTT TSSIKTEDIP TAKCIRPNSA SGALTAKSSI PRGRSQSLKV
     TQTVTGTKKS PSIIPTLPRS SGPALSLTKK LEARSLQNVE KNKQKTSPRG PVTQAQTPPV
     DPKSIELTKC KAACEQQRGV IENLKNLLSS SNQRFEALTV VVQQLINQRE ETLKKRKALS
     QELLNLRGDL VCASSTCERL EKEKNELLKA YEGILQKVKE EHHAELSDLE EKLKQFYTGE
     CEKLQSIFIE EAEKYKNELQ EKVDDLNTTH EAYRLQAETS QIETIHTLKE DYEKSLTELK
     DAKDKENKIL EDSFKEKQAE VEKKILELKD VNESLKEKLK YEEEQRKLTK EKSVQKNPQV
     MYLEQELESL KAVLEIKNEK LHQQDKKLMQ VEKLVETNTT LVERLNKCQQ ENEDLKARMV
     NHVALSRQLS TEQEVLQRSL EKESKANKRL SMENEELLWK LHNGDLCSPK KLSPSSPGIP
     FHPSRNSGSF SSPTVSPR
 
 
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