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CLAS2_CAEEL
ID   CLAS2_CAEEL             Reviewed;        1020 AA.
AC   P32744;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 3.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Protein CLASP-2;
GN   Name=cls-2; ORFNames=R107.6;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=7906398; DOI=10.1038/368032a0;
RA   Wilson R., Ainscough R., Anderson K., Baynes C., Berks M., Bonfield J.,
RA   Burton J., Connell M., Copsey T., Cooper J., Coulson A., Craxton M.,
RA   Dear S., Du Z., Durbin R., Favello A., Fraser A., Fulton L., Gardner A.,
RA   Green P., Hawkins T., Hillier L., Jier M., Johnston L., Jones M.,
RA   Kershaw J., Kirsten J., Laisster N., Latreille P., Lightning J., Lloyd C.,
RA   Mortimore B., O'Callaghan M., Parsons J., Percy C., Rifken L., Roopra A.,
RA   Saunders D., Shownkeen R., Sims M., Smaldon N., Smith A., Smith M.,
RA   Sonnhammer E., Staden R., Sulston J., Thierry-Mieg J., Thomas K.,
RA   Vaudin M., Vaughan K., Waterston R., Watson A., Weinstock L.,
RA   Wilkinson-Sproat J., Wohldman P.;
RT   "2.2 Mb of contiguous nucleotide sequence from chromosome III of C.
RT   elegans.";
RL   Nature 368:32-38(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [3]
RP   FUNCTION.
RX   PubMed=12885567; DOI=10.1016/s0012-1606(03)00216-1;
RA   Yang H.-Y., McNally K., McNally F.J.;
RT   "MEI-1/katanin is required for translocation of the meiosis I spindle to
RT   the oocyte cortex in C elegans.";
RL   Dev. Biol. 260:245-259(2003).
RN   [4]
RP   SUBCELLULAR LOCATION.
RX   PubMed=14522947; DOI=10.1101/gad.1126303;
RA   Desai A., Rybina S., Mueller-Reichert T., Shevchenko A., Shevchenko A.,
RA   Hyman A., Oegema K.;
RT   "KNL-1 directs assembly of the microtubule-binding interface of the
RT   kinetochore in C. elegans.";
RL   Genes Dev. 17:2421-2435(2003).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH HCP-1 AND
RP   HCP-2, AND SUBCELLULAR LOCATION.
RX   PubMed=15854912; DOI=10.1016/j.cub.2005.03.018;
RA   Cheeseman I.M., MacLeod I., Yates J.R. III, Oegema K., Desai A.;
RT   "The CENP-F-like proteins HCP-1 and HCP-2 target CLASP to kinetochores to
RT   mediate chromosome segregation.";
RL   Curr. Biol. 15:771-777(2005).
CC   -!- FUNCTION: Probable microtubule plus-end tracking protein that promotes
CC       the stabilization of dynamic microtubules. Required for the formation
CC       of mitotic and meiotic spindles. Specifically promotes the
CC       polymerization of kinetochore-bound microtubules. Also required for
CC       cytoplasmic streaming. Essential for embryonic development.
CC       {ECO:0000269|PubMed:12885567, ECO:0000269|PubMed:15854912}.
CC   -!- SUBUNIT: Interacts with hcp-1 and hcp-2. {ECO:0000269|PubMed:15854912}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome. Chromosome, centromere,
CC       kinetochore. Cytoplasm, cytoskeleton, spindle. Note=Localized to
CC       kinetochores during metaphase, and to the spindle region. Kinetochore
CC       localization requires hcp-1 and hcp-2.
CC   -!- SIMILARITY: Belongs to the CLASP family. {ECO:0000305}.
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DR   EMBL; Z14092; CAA78472.2; -; Genomic_DNA.
DR   PIR; E88546; E88546.
DR   PIR; S30876; S30876.
DR   RefSeq; NP_499005.2; NM_066604.3.
DR   AlphaFoldDB; P32744; -.
DR   SMR; P32744; -.
DR   BioGRID; 41479; 6.
DR   IntAct; P32744; 3.
DR   STRING; 6239.R107.6b; -.
DR   iPTMnet; P32744; -.
DR   EPD; P32744; -.
DR   PaxDb; P32744; -.
DR   PeptideAtlas; P32744; -.
DR   EnsemblMetazoa; R107.6a.1; R107.6a.1; WBGene00000549.
DR   GeneID; 176280; -.
DR   UCSC; R107.6.2; c. elegans.
DR   CTD; 176280; -.
DR   WormBase; R107.6a; CE37546; WBGene00000549; cls-2.
DR   eggNOG; KOG2956; Eukaryota.
DR   GeneTree; ENSGT00940000168069; -.
DR   InParanoid; P32744; -.
DR   PhylomeDB; P32744; -.
DR   PRO; PR:P32744; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00000549; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   ExpressionAtlas; P32744; baseline and differential.
DR   GO; GO:0045180; C:basal cortex; IBA:GO_Central.
DR   GO; GO:0005813; C:centrosome; IDA:WormBase.
DR   GO; GO:0005737; C:cytoplasm; IDA:WormBase.
DR   GO; GO:0005881; C:cytoplasmic microtubule; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; IEA:GOC.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR   GO; GO:0005815; C:microtubule organizing center; IBA:GO_Central.
DR   GO; GO:0072686; C:mitotic spindle; IDA:WormBase.
DR   GO; GO:0005634; C:nucleus; IDA:WormBase.
DR   GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR   GO; GO:0051233; C:spindle midzone; IDA:WormBase.
DR   GO; GO:0008017; F:microtubule binding; ISS:WormBase.
DR   GO; GO:0030953; P:astral microtubule organization; IMP:WormBase.
DR   GO; GO:0051316; P:attachment of spindle microtubules to kinetochore involved in meiotic chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0099636; P:cytoplasmic streaming; IMP:WormBase.
DR   GO; GO:0040001; P:establishment of mitotic spindle localization; IMP:WormBase.
DR   GO; GO:0051307; P:meiotic chromosome separation; IMP:UniProtKB.
DR   GO; GO:0051257; P:meiotic spindle midzone assembly; IMP:UniProtKB.
DR   GO; GO:0000212; P:meiotic spindle organization; IMP:UniProtKB.
DR   GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR   GO; GO:0046785; P:microtubule polymerization; IDA:WormBase.
DR   GO; GO:0000281; P:mitotic cytokinesis; IMP:WormBase.
DR   GO; GO:0051306; P:mitotic sister chromatid separation; IMP:WormBase.
DR   GO; GO:0090307; P:mitotic spindle assembly; IBA:GO_Central.
DR   GO; GO:0051256; P:mitotic spindle midzone assembly; IMP:WormBase.
DR   GO; GO:0031134; P:sister chromatid biorientation; IMP:WormBase.
DR   Gene3D; 1.25.10.10; -; 3.
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; 2.
DR   SUPFAM; SSF48371; SSF48371; 2.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Cytoplasm; Cytoskeleton;
KW   Kinetochore; Meiosis; Microtubule; Mitosis; Reference proteome.
FT   CHAIN           1..1020
FT                   /note="Protein CLASP-2"
FT                   /id="PRO_0000089874"
FT   REPEAT          954..992
FT                   /note="HEAT"
FT   REGION          259..280
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          329..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          419..461
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        259..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        431..445
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1020 AA;  112285 MW;  0E909E7AFA73A05C CRC64;
     MSRVISRSTP GGTCIVSKDD FLKSFEEVPK MEISSPSDFK EKLDQTIETL SKGQEDWNKR
     MNKLKQIRSM VVHGEDVIGR EQLLSQLVRL TDCLDLSVKD LRSQILREAA ITCGFLFKRF
     GTDVRQIAER CLPSAFAQVA VSTKVMATCG AVLTLFIVEF IQTKQIFTCI ASYSTSKDKN
     QRRQLCALLE IVLEHWNEKI KRTVLPQIGE LIKAAICDAD PETRVAGRKA FSKLDALHST
     EADKLFASVD SSKQKMLRAS DAASSSTSIN SERGTAPFRS KLSAGSIGGI RNAPNISSKF
     LAQRSASAID TKQVTRMATS VSRTPNIRPM TTRTLSKIDT SPGGSKFARP TVGALGSRTS
     SNLRARGSVP TSQPGSRNGS PPRRPSATEA FPAEMQRVKS NLGSNSFVSS LSAEEATKLQ
     KAMNTAKESL RQPSRNDDDE FLLPKRPTPQ KATPQKSALD TSRVEEVIRA CSSTSANEKR
     EGIKMLAGIV SEPNLSNAEI KSLGAVLNRL LGESTNQIVL ESISSFVKTH HPRLSDWLKL
     GLGKLFAKKG AEMTLNSKKQ ISTTISCILS SFDPTLQLKS TCELVCDPIH LMSPKSRVVL
     LEYLNELLGK YMERGSSFNT KEMKATILKM FSWMADQRNE QLITPHGEKV LCSLFALNNA
     DFSALFNDFN PDYRDWAYKV LQSHGHDQHV PQQDAVSEEA CVRATISTTA AQIEDFVVSR
     NLDMTPVKSP STRAISSGFK RVDAEPLRPL SSEMNSQHRD EELSFNESFD RLKLNSTTHL
     IDDTSEQSKY VASKLAQISG DMGAQQYEGL LSIQTMLCEG SFTLWEQNFA KLLIAVFDVL
     SKSESDANKK VALRVLTKMC TSQASRLFDS TEMAICKVLD AAVNSQDGTM NVTADDCLKT
     LATHLPLAKV VNISQLILNE EKAQEPKASL VLKMMTRLFE GLQADELSPV VDDLAPCVIK
     SYDSPSSAVR KTAVYCLVAM VNKLGMKTME PHLQNLSSGK LNLVQVYVNR AMSSSSHSHV
 
 
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