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STU1_KLULA
ID   STU1_KLULA              Reviewed;        1358 AA.
AC   Q6CVG0;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Protein STU1;
GN   Name=STU1; OrderedLocusNames=KLLA0B12331g;
OS   Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 /
OS   NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kluyveromyces.
OX   NCBI_TaxID=284590;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37;
RX   PubMed=15229592; DOI=10.1038/nature02579;
RA   Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I.,
RA   de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L.,
RA   Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S.,
RA   Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J.,
RA   Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E.,
RA   Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C.,
RA   Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M.,
RA   Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S.,
RA   Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F.,
RA   Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M.,
RA   Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M.,
RA   Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C.,
RA   Weissenbach J., Wincker P., Souciet J.-L.;
RT   "Genome evolution in yeasts.";
RL   Nature 430:35-44(2004).
CC   -!- FUNCTION: Microtubule binding protein that promotes the stabilization
CC       of dynamic microtubules. Required for mitotic spindle formation (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with microtubules. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Cytoplasm, cytoskeleton, spindle {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR   EMBL; CR382122; CAH02472.1; -; Genomic_DNA.
DR   RefSeq; XP_452079.1; XM_452079.1.
DR   AlphaFoldDB; Q6CVG0; -.
DR   SMR; Q6CVG0; -.
DR   STRING; 28985.XP_452079.1; -.
DR   EnsemblFungi; CAH02472; CAH02472; KLLA0_B12331g.
DR   GeneID; 2897534; -.
DR   KEGG; kla:KLLA0_B12331g; -.
DR   eggNOG; ENOG502QT5T; Eukaryota.
DR   HOGENOM; CLU_256206_0_0_1; -.
DR   InParanoid; Q6CVG0; -.
DR   OMA; TFWYYYK; -.
DR   Proteomes; UP000000598; Chromosome B.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   Gene3D; 1.25.10.10; -; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024395; CLASP_N_dom.
DR   Pfam; PF12348; CLASP_N; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Cytoplasm; Cytoskeleton; Microtubule; Mitosis;
KW   Nucleus; Reference proteome.
FT   CHAIN           1..1358
FT                   /note="Protein STU1"
FT                   /id="PRO_0000272291"
FT   REGION          915..950
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          970..990
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        922..950
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1358 AA;  154330 MW;  26D9B713C6001B24 CRC64;
     MSDEFNGLDG LSDELLSAER KLDILTQFKA HVKKTLVNEQ VCVKYFENLS RLLVERGSNR
     RRGNDGDDVV FALAHSALCY LIKRVAMQAQ HKFQHDLIEL IVSTLFSIPF ADKKVWQSSV
     KALEAIYLAK PNEFCQVLNE SIAYNGSIRT NVLLLIDELA RMESSNGRNG SMFLQKFIPF
     WVQEMNTNDS ISNTDIELIY DIVANRCPEP MVRSMVDSVI RESAAKVFKS RLVGKLNNHG
     SESDMKDDFD RSITHTNSIN SQVFNLQNEL QSIMHQAPQF PTVPAPEPIS YSNLSYLIKD
     LESMLPAFEG SRETEQNWKI RQTNVTKLRS IVLGNVSIEF PDKFLELWKD LNLQYCVTKS
     ALSLRTSLCT HGCSLVKDLC CVFNSMLDIS IIENLWSCLA KLMSNTKKIA NQNAFICLIT
     LLSTVPFHSR LFNHCFALIR DKNNVSRLYS STFLRILIVR FHKRLISQHH VYVEEWLQKG
     LTDAQTTIRE SMRITFWYWF KVSPMSGKKM LNLFQPQIKR ALENSIPTHL DINYEAAIPP
     QSKESSRRSS LLPKRFPSYA APTQSSHLPR SSIKRSLTDL AQGTQSFSKR SLRTPPDHDM
     NIDLTSELTN SQTNPLLNRY MKREEVEPEP LHVILSKDPK LGLDLLQKYL LSDTKIGDEE
     KVQSAIVSLI RTNPKAFKPL LHLPKFYQLI PLNFSMVLLP LNDLDISMIE TQFKTYDIIN
     NVISILQSLE DKNSEWSIFY VRFKYQIYNF CFNTIAKMLN TVTLSDQLIN ELINACGKDM
     DAEKYYKLIL NIYLADKTKF VRLLKSTSTA STKLKIANVI QKKDSEFKIK SILNYPSVPE
     PIVSPEEHHL LEMTMVNPLG KRTVSSNTVI HNSLEGLDES ESNPNIIADE DNHSEKEDLV
     TVPPVAKNSV NTVSFVADSP SDSDNDDTKK NGSDVVDHEE IRDHEESHGF TKFGGFSKLT
     EMTKVHSVFQ PETVDENVDP MEVDSPDESN LDQKSLLTDI FLKNQHQEGS VSPIFKPQEL
     NNDPRHDYDS DMLSDAINGI EIKTNDGSVA NRSEDDIKTL GTNMGSVSDP KTFKPINLAH
     FANDSLFSFE LKFIDASIGI VNLTQLKLIV QSIINNGTFK MNELQYILKC FLCYDQEVLE
     WIHDQHELKD VWAITELLLS SSSSESQIPT NIAYKSIILT ACLLTIDDEL EHTVLKDSSI
     SQLFEHIISL VAKLDTFENE IYFACTELRT LLLSQDNNKH LPSFLEKCLK ALCDTKEQYI
     VKISFLLETI NGIISSMGNL LSVDVLRDLA KTISRYTPSD VAEWRFASCT ALATIYSQLI
     SRSTPVGYIR SLMPLLDPSD FEVVRSLSTT KDATRRLG
 
 
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