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STU1_YARLI
ID   STU1_YARLI              Reviewed;        1597 AA.
AC   Q6C882;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 84.
DE   RecName: Full=Protein STU1;
GN   Name=STU1; OrderedLocusNames=YALI0D21912g;
OS   Yarrowia lipolytica (strain CLIB 122 / E 150) (Yeast) (Candida lipolytica).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Dipodascaceae; Yarrowia.
OX   NCBI_TaxID=284591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CLIB 122 / E 150;
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAG81328.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CR382130; CAG81328.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; XP_503130.1; XM_503130.1.
DR   AlphaFoldDB; Q6C882; -.
DR   STRING; 4952.CAG81328; -.
DR   PRIDE; Q6C882; -.
DR   GeneID; 2910152; -.
DR   KEGG; yli:YALI0D21912g; -.
DR   InParanoid; Q6C882; -.
DR   Proteomes; UP000001300; Chromosome D.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0072686; C:mitotic spindle; IBA:GO_Central.
DR   GO; GO:1990023; C:mitotic spindle midzone; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR   GO; GO:0008017; F:microtubule binding; IBA:GO_Central.
DR   GO; GO:0060172; P:astral microtubule depolymerization; IBA:GO_Central.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR   Gene3D; 1.25.10.10; -; 2.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR024395; CLASP_N_dom.
DR   InterPro; IPR034085; TOG.
DR   Pfam; PF12348; CLASP_N; 1.
DR   SMART; SM01349; TOG; 1.
DR   SUPFAM; SSF48371; SSF48371; 2.
PE   3: Inferred from homology;
KW   Cell cycle; Cell division; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Microtubule; Mitosis; Nucleus; Reference proteome.
FT   CHAIN           1..1597
FT                   /note="Protein STU1"
FT                   /id="PRO_0000272296"
FT   REPEAT          1537..1573
FT                   /note="HEAT"
FT   REGION          220..265
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          519..958
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1005..1154
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1307..1332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        534..552
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        571..641
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        655..670
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        705..726
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        750..784
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        798..823
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        833..866
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        893..907
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        923..950
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1079..1093
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1118..1143
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1597 AA;  174259 MW;  29B9D0CC88900D35 CRC64;
     MKSDQLGRVL SDDDLPTKLS IANEFKAFVK KNSVPRDLIH PYFLTLSRAI KSREDPQLTS
     VCFSCFCHLF KRVSIQDKQL LDDSATVAVV TDLLIDRLSD RSTGVRATAN KVLLDYWVLV
     PQAVAVAMRQ SAVVSSSHVT LGESLKWLQS VFDLSSAFNF SAFVQPVVDM LRYPQLQSSV
     CELLKKVYSV SDRRELEECL AATGVNEMLK KSILNGLPGG NSSSAVSDPK TTAPRSLSSQ
     KSVASKPAQQ PNSQEPGNEN APSSSLAFLN SLPNFRVDSL APENVYSASD LESKINNMHV
     AFADKESEKN WSLREKHVTQ IRKLLRGNAL QDYPSQFAAA YKSVIDGVLK SATSLRTTLS
     NQGLLLVKES GQLGGNAFVD PVMDIVFPQI IRLTGQMKKI TSNNAHITVC GLLTSATFST
     KLINHVTSAT VEKNAQPRTF AAVWLRILIL SHSQTHKSAM QNHGGLDQIE KAIAKGLQDP
     TPSVKENMRV TYWSFAEYWP SEADKIYRKL DTKAKAMLDK VNPSGAKNAP IKKPAPRESL
     KEVMRRSRES SVNRDANAPS ATAPPQRAKM GAPQRTSSGL VGRSLSGSNL TDRSNRLSST
     STSSRDQQRA VSDSTRPTQM TRPVSGRLSR EPSLTRSSRD QSLTRSSRET VSREPSLTRG
     SRELPKQRVD QNRQRVPSIS RDSRYGQRPV GSRESSRQSR ESSLDPSRES SLAPSVHSST
     AISRESSLPR DDLPSYDVEM DEDDPFVTQQ LKLSLKQEDA MSQPEETMNE VTTAEATATT
     APMKIPKSTP PRESTPPNSS PFVLAKSPAT QGVSTSPATG KSASPPATAE DELSRDLNGE
     SKHLKEVDDD NGSMDADERI ESDVVMGDAE ESAANFEPSE VEPAGVQLGL KSPKRETPTS
     ALQGNEQAEP ESHDAVADSQ SHGADSADLQ SEPRNVPVSP PTTSDASNVP ILSPRPIHPA
     KFELDSDAMI VDEVAPEVNT VIDAQTQAEE TPTEEIPAVV KVGFDAEAKS EPTEQTEAVK
     TSDTATEPGE PVDIPNSEQG PSTEPTELAK SAGSVEHVTE AIQEDPFGDA LPAKQENGAK
     ASDEIETDHT KSNNTESDGP VSAHDESEPM EICDSDNDAV DNGTNPDTKC QDQQDSTTPP
     MDFSSHDLKD ELNTSSPESL TALLSNPDQY KEILDHVPAE LFLLCVILFS ESHVMDAQSV
     ISRDTNLALS TASSMVMVCA RDVYPSDSRW SQATVEELKH VTVTCLEWLT KLVNESSEAS
     TLLATNKRYR TSLVHLLSTS VELHKQKFGD VTHNSLIHVI ESMDKLSQRP PDKRTSRAFL
     EAPSPSPDSS LVEDVTDKLS HVTVKENFKT IRILPPQLAS GQLIFPGSEV TWSKLELERL
     ARSPSCSDSN EAILDAVSRD KVSVTQLSTL ASRIPELEDV DLVTATILAY LHISHPPALT
     TAALVAIKQV LIKPELKLSM GHVTEIFSTL NHVNSHIDSR SPLAAAIEEL VADLLTHTDS
     SEMLEFLLLS RSRDSKTQNK LLLLNTVYHV ITPDLLPSYE TQLLALITEL ISDPDPLVRR
     VTVGLVVRVL RVSPEMEGTI SLAIKSKMDL VRYYMGA
 
 
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