KNL1_MOUSE
ID KNL1_MOUSE Reviewed; 1612 AA.
AC Q66JQ7; A3KGI4; Q8CCH6; Q9CV38;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Kinetochore scaffold 1;
DE AltName: Full=Cancer susceptibility candidate gene 5 protein homolog;
DE AltName: Full=Kinetochore-null protein 1;
DE AltName: Full=Protein CASC5;
GN Name=Knl1 {ECO:0000312|MGI:MGI:1923714}; Synonyms=Casc5;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryonic germ cell;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-507.
RC STRAIN=C57BL/6J; TISSUE=Testis, and Tongue;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-794, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Performs two crucial functions during mitosis: it is
CC essential for spindle-assembly checkpoint signaling and for correct
CC chromosome alignment. Directly links spindle checkpoint proteins BUB1
CC and BUB1B to kinetochores. Part of the MIS12 complex, which may be
CC fundamental for kinetochore formation and proper chromosome segregation
CC during mitosis. Acts in coordination with CENPK to recruit the NDC80
CC complex to the outer kinetochore (By similarity).
CC {ECO:0000250|UniProtKB:Q8NG31}.
CC -!- SUBUNIT: Interacts with DSN1, MIS12, BUB1, BUB1B, NSL1 and ZWINT.
CC {ECO:0000250|UniProtKB:Q8NG31}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q8NG31}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8NG31}.
CC Note=Weakly expressed in interphase nuclei. Expression increases from
CC prophase to late anaphase, but greatly diminishes from the telophase
CC and cytokinesis to early G1 phase of cell cycle (By similarity).
CC {ECO:0000250|UniProtKB:Q8NG31}.
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DR EMBL; AL772264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC080815; AAH80815.1; -; mRNA.
DR EMBL; AK009772; BAB26494.1; -; mRNA.
DR EMBL; AK033132; BAC28167.2; -; mRNA.
DR CCDS; CCDS89540.1; -.
DR AlphaFoldDB; Q66JQ7; -.
DR SMR; Q66JQ7; -.
DR ComplexPortal; CPX-5702; Kinetochore KNL1 complex.
DR IntAct; Q66JQ7; 15.
DR MINT; Q66JQ7; -.
DR STRING; 10090.ENSMUSP00000028802; -.
DR iPTMnet; Q66JQ7; -.
DR PhosphoSitePlus; Q66JQ7; -.
DR EPD; Q66JQ7; -.
DR jPOST; Q66JQ7; -.
DR MaxQB; Q66JQ7; -.
DR PaxDb; Q66JQ7; -.
DR PRIDE; Q66JQ7; -.
DR ProteomicsDB; 264789; -.
DR Antibodypedia; 23122; 121 antibodies from 20 providers.
DR Ensembl; ENSMUST00000028799; ENSMUSP00000028799; ENSMUSG00000027326.
DR UCSC; uc008ltb.1; mouse.
DR MGI; MGI:1923714; Knl1.
DR VEuPathDB; HostDB:ENSMUSG00000027326; -.
DR eggNOG; ENOG502QW5H; Eukaryota.
DR GeneTree; ENSGT00410000025918; -.
DR InParanoid; Q66JQ7; -.
DR Reactome; R-MMU-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-MMU-2467813; Separation of Sister Chromatids.
DR Reactome; R-MMU-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-MMU-5663220; RHO GTPases Activate Formins.
DR Reactome; R-MMU-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR ChiTaRS; Knl1; mouse.
DR PRO; PR:Q66JQ7; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q66JQ7; protein.
DR Bgee; ENSMUSG00000027326; Expressed in humerus cartilage element and 125 other tissues.
DR ExpressionAtlas; Q66JQ7; baseline and differential.
DR Genevisible; Q66JQ7; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0034501; P:protein localization to kinetochore; ISO:MGI.
DR InterPro; IPR037388; Blinkin.
DR InterPro; IPR043651; KNL1_MELT_rep.
DR PANTHER; PTHR16520; PTHR16520; 1.
DR Pfam; PF19221; MELT; 9.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Kinetochore; Mitosis; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1612
FT /note="Kinetochore scaffold 1"
FT /id="PRO_0000235983"
FT REPEAT 723..827
FT /note="1"
FT REPEAT 923..1027
FT /note="2"
FT REGION 1..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 723..1027
FT /note="2 X 104 AA approximate repeats"
FT REGION 1557..1602
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 1577..1590
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 1565..1600
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NG31"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NG31"
FT MOD_RES 538
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NG31"
FT MOD_RES 540
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NG31"
FT MOD_RES 794
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 878
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NG31"
FT MOD_RES 1243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NG31"
FT MOD_RES 1464
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NG31"
FT CONFLICT 128
FT /note="D -> G (in Ref. 2; AAH80815)"
FT /evidence="ECO:0000305"
FT CONFLICT 375
FT /note="H -> R (in Ref. 2; AAH80815)"
FT /evidence="ECO:0000305"
FT CONFLICT 1151
FT /note="P -> L (in Ref. 2; AAH80815)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1612 AA; 179337 MW; A9BE2BB20E008621 CRC64;
MDGVYSEANE ENDNTQRPVR RQHSSILKPP RSPLQDLKCG NQTNQEPNPP RKRKSSRRVS
FADTIKVFQT ESHMKTERNS EISGMNTLLC APIQTQMQQK EFSITDCNHE RKHANDQTVI
FSDENQMDLT ASHTVMITKG LSDCTKNENS TKIDTTSFLE NLKHHAANSR IKKDLACSTV
SLSQNIFSEK INSDNFIKRL KTGKHISSST ELDKENAEIP VYSKDSNSAS STYQMHASLG
VDENSSNRTR IFREQDDGMN LTQCHTACIK TWIPPSTEAK IGEFKGDKTI YGNECMELTT
NYTIQVLSSE NNLSERETQT QNGMNVTTVD GATAPAPEKK TALKDKLNAA FQGSFPNPEN
KIHIIKCHPI ESETHTVTQI SSQSASTLAV TSKSICSSPA IEGYKTIFHS SSNDAMELTK
CLSAMEEEKK LLKADDKYSK ICTNPDAGPL REKTIYLEED SMDITKSHTV AIDNKIFKHD
QENIKKEIIA IPIFEKEMVL RNLMPMSKDE KRDVNYISVP QVSKESLQRS QTNTLSVSLT
DKKMEFLADE DMDLTKSHTT KLSQVIPTTF DLASKNVTKS YSHSKSPLNE WESLDKQVVL
GQHSKLPLPQ RKDRDDPDCS HHKIMYSEEL QTMDLTKSHT IVIGFGPSEV QEHSKINLEH
KNSQLTAESI QTAVNVPAAN SRVVTTNDMD MLKDRSTHKP ELLKEKQNIK IYGRKSIGRL
KIDKTILFSE GNEGDMDITK SCTVKINHRS LLDKHDSHLV SLAGTSKTIL HARGQVEMEI
NRSHTTPLEC KIISPSDITP GDLDKTMMSI DDHEELDMTK SHTVFIDYQA EAKGVLPDRL
DFQLSKKESL QKPKVTSLAE EIYISKNSES NHLPAKGSQL TILEEGSNSG LGEETNDAQK
PGFLNELLSG KTQRRKSLSL KNKSITFPEN DKSYREIPQS SAVEINNETR LEDRKGFSFV
PLAGTSKPVL SAYGPEDMEI SIGQTTASEY KTVPPEEITT IPMDKTVMFV DNFGDLDVTR
SHTVFIDCQA KEKVLDEYTN LGIQKTKTLS GSEGDTHIQE ITKNPAAQHK HHMTTVIPSS
TVVSDQSSMK IKFHKADRDE EVKGKEVEAN MLKQTKPESC LLNITDGKNV DFTSSYTADV
CRSSDKYSSL PNISSSDNSG GNTMSLCDKN KEKAYNCQVP NEFTYAAILP STYHMDSKKL
SVFPPCPSKE VTQTESAIAL LKDEDPVEEP LGEMATFNSK HVSLNLAKDQ TEAFVDVSVA
SQPHLSAQQS PSTQKGQDVA RRDEGILAKA GKKALPFLLE NVAASTWENE SKIPTNVEHF
AVTYEKELSI SIQTDKCNTN VQSPSNSALT TQVIQTHANA EGALDFLVPS TVSCFSSTKP
SLSNLNRKTE EVLDFQTVNL LPPAEQLLEE GSQAHSMSIV QATEIYRLGS RNDRDEESKT
FCNEAETTSV PLKTAVKDKT RRCSLGIFLP KLPSKRSCSI TGVDDLEQIL ADAADLTQLE
TQPVCSKDPG IGSVAAKLNL SPSQFINEEN LPVYPGEILS SDSVSLDIEE SVLIDTSQRE
SLPSENKTEN CRAQKRTRVE ENDVTNEKKI RTHDSAQDQE VSCLEPKNVL EF
