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KNL1_CAEEL
ID   KNL1_CAEEL              Reviewed;        1010 AA.
AC   P34278;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1996, sequence version 3.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Kinetochore null protein 1;
GN   Name=knl-1; ORFNames=C02F5.1;
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, COMPLEX WITH HCP-3 AND HCP-4, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP   STAGE, AND DISRUPTION PHENOTYPE.
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   [4]
RP   FUNCTION, INTERACTION WITH HCP-4; HIM-10; KBP-1; KBP-2; KBP-3; KBP-4;
RP   KBP-5; KNL-3; MIS-12 AND NDC-80, AND SUBCELLULAR LOCATION.
RX   PubMed=15371340; DOI=10.1101/gad.1234104;
RA   Cheeseman I.M., Niessen S., Anderson S., Hyndman F., Yates J.R. III,
RA   Oegema K., Desai A.;
RT   "A conserved protein network controls assembly of the outer kinetochore and
RT   its ability to sustain tension.";
RL   Genes Dev. 18:2255-2268(2004).
RN   [5]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=15767665; DOI=10.1128/mcb.25.7.2583-2592.2005;
RA   Moore L.L., Stanvitch G., Roth M.B., Rosen D.;
RT   "HCP-4/CENP-C promotes the prophase timing of centromere resolution by
RT   enabling the centromere association of HCP-6 in Caenorhabditis elegans.";
RL   Mol. Cell. Biol. 25:2583-2592(2005).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=16273096; DOI=10.1038/ncb1331;
RA   Monen J., Maddox P.S., Hyndman F., Oegema K., Desai A.;
RT   "Differential role of CENP-A in the segregation of holocentric C. elegans
RT   chromosomes during meiosis and mitosis.";
RL   Nat. Cell Biol. 7:1248-1255(2005).
RN   [7]
RP   FUNCTION, AND INTERACTION WITH MIS12 COMPLEX.
RX   PubMed=17129783; DOI=10.1016/j.cell.2006.09.039;
RA   Cheeseman I.M., Chappie J.S., Wilson-Kubalek E.M., Desai A.;
RT   "The conserved KMN network constitutes the core microtubule-binding site of
RT   the kinetochore.";
RL   Cell 127:983-997(2006).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=17339379; DOI=10.1083/jcb.200701065;
RA   Maddox P.S., Hyndman F., Monen J., Oegema K., Desai A.;
RT   "Functional genomics identifies a Myb domain-containing protein family
RT   required for assembly of CENP-A chromatin.";
RL   J. Cell Biol. 176:757-763(2007).
RN   [9]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18070910; DOI=10.1083/jcb.200705108;
RA   Oishi K., Okano H., Sawa H.;
RT   "RMD-1, a novel microtubule-associated protein, functions in chromosome
RT   segregation in Caenorhabditis elegans.";
RL   J. Cell Biol. 179:1149-1162(2007).
RN   [10]
RP   FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18765790; DOI=10.1101/gad.1687508;
RA   Gassmann R., Essex A., Hu J.-S., Maddox P.S., Motegi F., Sugimoto A.,
RA   O'Rourke S.M., Bowerman B., McLeod I., Yates J.R. III, Oegema K.,
RA   Cheeseman I.M., Desai A.;
RT   "A new mechanism controlling kinetochore-microtubule interactions revealed
RT   by comparison of two dynein-targeting components: SPDL-1 and the
RT   Rod/Zwilch/Zw10 complex.";
RL   Genes Dev. 22:2385-2399(2008).
RN   [11]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=18936247; DOI=10.1083/jcb.200805185;
RA   Yamamoto T.G., Watanabe S., Essex A., Kitagawa R.;
RT   "SPDL-1 functions as a kinetochore receptor for MDF-1 in Caenorhabditis
RT   elegans.";
RL   J. Cell Biol. 183:187-194(2008).
RN   [12]
RP   FUNCTION.
RX   PubMed=19109417; DOI=10.1091/mbc.e08-10-1047;
RA   Essex A., Dammermann A., Lewellyn L., Oegema K., Desai A.;
RT   "Systematic analysis in Caenorhabditis elegans reveals that the spindle
RT   checkpoint is composed of two largely independent branches.";
RL   Mol. Biol. Cell 20:1252-1267(2009).
RN   [13]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=20729837; DOI=10.1038/ncb2093;
RA   Dumont J., Oegema K., Desai A.;
RT   "A kinetochore-independent mechanism drives anaphase chromosome separation
RT   during acentrosomal meiosis.";
RL   Nat. Cell Biol. 12:894-901(2010).
RN   [14]
RP   FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND REPEATS.
RX   PubMed=24567362; DOI=10.1083/jcb.201311015;
RA   Moyle M.W., Kim T., Hattersley N., Espeut J., Cheerambathur D.K.,
RA   Oegema K., Desai A.;
RT   "A Bub1-Mad1 interaction targets the Mad1-Mad2 complex to unattached
RT   kinetochores to initiate the spindle checkpoint.";
RL   J. Cell Biol. 204:647-657(2014).
CC   -!- FUNCTION: Proposed to be part of the KMN network incorporating the
CC       MIS12 complex and NDC80 complex that is required for establishing the
CC       kinetochore-microtubule interface that aids in chromosome segregation
CC       during meiotic and mitotic cell division (PubMed:14522947,
CC       PubMed:15371340, PubMed:17129783, PubMed:18070910). Appears to function
CC       downstream of hcp-3 (CENP-A) and hcp-4 (CENP-C) in the kinetochore
CC       assembly hierarchy (PubMed:15767665, PubMed:16273096). Has a role in
CC       the correct localization of the spindly-like protein spdl-1 and the RZZ
CC       complex that is composed of rod-1, czw-1 and zwl-1 to kinetochores
CC       (PubMed:18765790, PubMed:18936247). Required for the recruitment of
CC       spindle-assembly checkpoint components bub-1 and mdf-1/2 to unattached
CC       kinetochores (PubMed:19109417, PubMed:20729837, PubMed:24567362).
CC       {ECO:0000269|PubMed:14522947, ECO:0000269|PubMed:15371340,
CC       ECO:0000269|PubMed:15767665, ECO:0000269|PubMed:16273096,
CC       ECO:0000269|PubMed:17129783, ECO:0000269|PubMed:18070910,
CC       ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:18936247,
CC       ECO:0000269|PubMed:19109417, ECO:0000269|PubMed:20729837,
CC       ECO:0000269|PubMed:24567362}.
CC   -!- SUBUNIT: Interacts with hcp-3 and hcp-4 to form a complex
CC       (PubMed:14522947). Interacts with hcp-4, him-10, kbp-3, kbp-4, kbp-5,
CC       knl-3, and ndc-80 (PubMed:15371340). Interacts with kbp-1, kbp-2 and
CC       mis-12; which make up the MIS12 complex (PubMed:17129783).
CC       {ECO:0000269|PubMed:14522947, ECO:0000269|PubMed:15371340,
CC       ECO:0000269|PubMed:17129783}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cell cortex
CC       {ECO:0000269|PubMed:20729837}. Chromosome, centromere, kinetochore
CC       {ECO:0000269|PubMed:14522947, ECO:0000269|PubMed:15371340,
CC       ECO:0000269|PubMed:16273096, ECO:0000269|PubMed:17339379,
CC       ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:24567362}. Note=Also
CC       found on the surface of chromosomes (PubMed:14522947). Subcellular
CC       localization dependent on expression of hcp-3, hcp-4, knl-3 and knl-2
CC       (PubMed:14522947, PubMed:15371340, PubMed:16273096, PubMed:17339379).
CC       During anaphase of meiosis I, localized also to spindle-associated rod-
CC       shaped structures which depends on zwl-1 (PubMed:20729837).
CC       {ECO:0000269|PubMed:14522947, ECO:0000269|PubMed:15371340,
CC       ECO:0000269|PubMed:16273096, ECO:0000269|PubMed:17339379,
CC       ECO:0000269|PubMed:20729837}.
CC   -!- DEVELOPMENTAL STAGE: Expressed on chromosomes from early prophase until
CC       late anaphase. {ECO:0000269|PubMed:14522947}.
CC   -!- DOMAIN: The N-terminus contains a number of repeats which contribute
CC       additively to bub-1 recruitment to unattached kinetochores. The repeats
CC       are not required for localization to kinetochores.
CC       {ECO:0000269|PubMed:24567362}.
CC   -!- DISRUPTION PHENOTYPE: Perturbed spindle-kinetochore interactions,
CC       segregation defects and premature spindle elongation (PubMed:14522947,
CC       PubMed:15767665, PubMed:18070910). RNAi-mediated knockdown results in
CC       reduced localization of the spindly-like protein spdl-1 and the RZZ
CC       complex component zwl-1 to kinetochores (PubMed:18765790,
CC       PubMed:18936247). Does not affect spdl-1 localization to microtubules
CC       (PubMed:18936247). {ECO:0000269|PubMed:14522947,
CC       ECO:0000269|PubMed:15767665, ECO:0000269|PubMed:18070910,
CC       ECO:0000269|PubMed:18765790, ECO:0000269|PubMed:18936247}.
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DR   EMBL; FO080288; CCD62626.1; -; Genomic_DNA.
DR   RefSeq; NP_498811.1; NM_066410.3.
DR   AlphaFoldDB; P34278; -.
DR   SMR; P34278; -.
DR   BioGRID; 41368; 27.
DR   ComplexPortal; CPX-808; Knl-1/Mis12/MIND complex.
DR   ComplexPortal; CPX-812; Knl1-Zwint1 complex.
DR   DIP; DIP-25115N; -.
DR   IntAct; P34278; 18.
DR   STRING; 6239.C02F5.1; -.
DR   EPD; P34278; -.
DR   PaxDb; P34278; -.
DR   PeptideAtlas; P34278; -.
DR   PRIDE; P34278; -.
DR   EnsemblMetazoa; C02F5.1.1; C02F5.1.1; WBGene00002231.
DR   GeneID; 176164; -.
DR   KEGG; cel:CELE_C02F5.1; -.
DR   CTD; 176164; -.
DR   WormBase; C02F5.1; CE02450; WBGene00002231; knl-1.
DR   eggNOG; ENOG502TGNI; Eukaryota.
DR   HOGENOM; CLU_296876_0_0_1; -.
DR   InParanoid; P34278; -.
DR   OMA; NDTMAVF; -.
DR   OrthoDB; 1487822at2759; -.
DR   PhylomeDB; P34278; -.
DR   PRO; PR:P34278; -.
DR   Proteomes; UP000001940; Chromosome III.
DR   Bgee; WBGene00002231; Expressed in germ line (C elegans) and 4 other tissues.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR   GO; GO:0005694; C:chromosome; IDA:UniProtKB.
DR   GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR   GO; GO:0000940; C:outer kinetochore; IDA:UniProtKB.
DR   GO; GO:0008017; F:microtubule binding; IDA:WormBase.
DR   GO; GO:0044877; F:protein-containing complex binding; IPI:UniProtKB.
DR   GO; GO:0030953; P:astral microtubule organization; IMP:UniProtKB.
DR   GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:ComplexPortal.
DR   GO; GO:0051301; P:cell division; IMP:UniProtKB.
DR   GO; GO:0007059; P:chromosome segregation; IMP:UniProtKB.
DR   GO; GO:0045184; P:establishment of protein localization; IDA:UniProtKB.
DR   GO; GO:0051382; P:kinetochore assembly; IDA:UniProtKB.
DR   GO; GO:0051307; P:meiotic chromosome separation; IMP:UniProtKB.
DR   GO; GO:0043060; P:meiotic metaphase I plate congression; IMP:UniProtKB.
DR   GO; GO:0000212; P:meiotic spindle organization; IMP:UniProtKB.
DR   GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IMP:WormBase.
DR   GO; GO:1905342; P:positive regulation of protein localization to kinetochore; IMP:UniProtKB.
DR   GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
DR   GO; GO:1903394; P:protein localization to kinetochore involved in kinetochore assembly; IMP:UniProtKB.
DR   GO; GO:0051988; P:regulation of attachment of spindle microtubules to kinetochore; IDA:ComplexPortal.
PE   1: Evidence at protein level;
KW   Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW   Coiled coil; Cytoplasm; Kinetochore; Meiosis; Mitosis; Reference proteome;
KW   Repeat.
FT   CHAIN           1..1010
FT                   /note="Kinetochore null protein 1"
FT                   /id="PRO_0000065107"
FT   REPEAT          85..88
FT                   /note="1"
FT                   /evidence="ECO:0000305"
FT   REPEAT          109..112
FT                   /note="2"
FT                   /evidence="ECO:0000305"
FT   REPEAT          228..231
FT                   /note="3"
FT                   /evidence="ECO:0000305"
FT   REPEAT          255..258
FT                   /note="4"
FT                   /evidence="ECO:0000305"
FT   REPEAT          278..281
FT                   /note="5"
FT                   /evidence="ECO:0000305"
FT   REPEAT          323..326
FT                   /note="6"
FT                   /evidence="ECO:0000305"
FT   REPEAT          346..349
FT                   /note="7"
FT                   /evidence="ECO:0000305"
FT   REPEAT          402..405
FT                   /note="8"
FT                   /evidence="ECO:0000305"
FT   REPEAT          428..431
FT                   /note="9"
FT                   /evidence="ECO:0000305"
FT   REGION          85..431
FT                   /note="9 X 4 AA repeats of M-[D/E]-[I/L/M]-[S/T]"
FT                   /evidence="ECO:0000305"
FT   COILED          820..915
FT                   /evidence="ECO:0000255"
FT   COILED          956..988
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   1010 AA;  113231 MW;  15E19DD975824D94 CRC64;
     MSMEPRKKRN SILKVRQAVE TIEETVMNSG PSSTTTNRRV SFHNVKHVKQ YDRDHGKILD
     ATPVKEKITD TIGSDGILTP RGGNMDISES PACTSSFQVF GGGNLDKTMD MSLETTINEN
     NETARLFETT RDPTLLYEKI VETTTKVTER IVSMPLDDTL AMFNTTNQED KDMSVDRSVL
     FTIPKVPKHN ATMNRTIPMD LDESKAAGGQ CDETMNVFNF TNLEAAEMDT SKLDENNTMN
     AIRIPINSNV MPVDMDITEH HTLIEEKKND TFGPSQLMDI SAPQVQVNDT LAIFNSPRDI
     CNKGLGVPQN LINIASNVVP VDMDITDQAV LNAEKKNDQF ETSQLMDISI PKVLVNDTMA
     MFNSPKHVSK SSMDLEKTIE AADKSTKYPS IADEVEDLDM DMDITEQQPC EAGNQQNDGL
     QLQKEDLMDI SVIRDSPAVN DTMAVFQSPA RVKIGANNSI IDSQKSIVFG DEMSIDETQN
     DGTLTLPKSN VEVTTTNDVY TSLERQEENA SENVSMINES SVHSEIDKKS FMLIEEERAF
     MHSSMIDVAQ KLEDDGSSKT PVILASQSAS LATKEPSALH NSSATLNNSM ELDNNTLLKT
     MQITTCEDIS MVHESIAVEL NSNKEQEQFG DETLQKNDTS NTGANFTFQG HNETSQIMNN
     VDSEAVNTSK ISTYSAFNLS INQSISKRRR SLLNSARESP RRVALENSIM SMNGQTMEAL
     TEYRQNKTMQ TSQDSMPSMS LNDSGRDILA MNTSVRSPHL NSSKTAAPGT PSLMSQNVQL
     PPPSPQFEMP DFDPAVVNVV YLTSEDPSTE QHPEALKFQR IVENEKMKVQ HEIDSLNSTN
     QLSAEKIDML KTKELLKFSH DEREAIMIAR KDAEIKFLEL RLKFALEKKI ESDQEIAELE
     QGNSKMAEQL RGLDKMAVVQ KELEKLRSLP PSREESGKIR KEWMEMKQWE FDQKMKALRN
     VRSNMIALRS EKNALEMKVA EEHEKFAQRN DLKKSRMLVF SKAVKKIVNF
 
 
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