DSN1_MOUSE
ID DSN1_MOUSE Reviewed; 348 AA.
AC Q9CYC5; Q9CYF2; Q9DA26;
DT 01-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Kinetochore-associated protein DSN1 homolog;
GN Name=Dsn1;
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 MRNA].
RC STRAIN=C57BL/6J; TISSUE=Embryo, and Testis;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-331, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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: Part of the MIS12 complex which is required for normal
CC chromosome alignment and segregation and kinetochore formation during
CC mitosis. {ECO:0000250|UniProtKB:Q9H410}.
CC -!- SUBUNIT: Component of the MIS12 complex composed of MIS12, DSN1, NSL1
CC and PMF1. Also interacts with KNL1, CBX3 and CBX5. Interacts with
CC KNSTRN. {ECO:0000250|UniProtKB:Q9H410}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H410}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q9H410}.
CC Note=Associated with the kinetochore. {ECO:0000250|UniProtKB:Q9H410}.
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DR EMBL; AK017813; BAB30950.1; -; mRNA.
DR EMBL; AK006246; BAB24479.1; -; mRNA.
DR EMBL; AK017740; BAB30906.1; -; mRNA.
DR EMBL; BC025079; AAH25079.1; -; mRNA.
DR EMBL; BC046807; AAH46807.1; -; mRNA.
DR CCDS; CCDS16972.1; -.
DR RefSeq; NP_080129.2; NM_025853.3.
DR AlphaFoldDB; Q9CYC5; -.
DR SMR; Q9CYC5; -.
DR BioGRID; 211821; 1.
DR ComplexPortal; CPX-5701; Kinetochore MIS12 complex.
DR IntAct; Q9CYC5; 2.
DR MINT; Q9CYC5; -.
DR STRING; 10090.ENSMUSP00000099418; -.
DR iPTMnet; Q9CYC5; -.
DR PhosphoSitePlus; Q9CYC5; -.
DR EPD; Q9CYC5; -.
DR jPOST; Q9CYC5; -.
DR MaxQB; Q9CYC5; -.
DR PaxDb; Q9CYC5; -.
DR PeptideAtlas; Q9CYC5; -.
DR PRIDE; Q9CYC5; -.
DR ProteomicsDB; 275407; -.
DR Antibodypedia; 1232; 186 antibodies from 26 providers.
DR DNASU; 66934; -.
DR Ensembl; ENSMUST00000103129; ENSMUSP00000099418; ENSMUSG00000027635.
DR Ensembl; ENSMUST00000103130; ENSMUSP00000099419; ENSMUSG00000027635.
DR GeneID; 66934; -.
DR KEGG; mmu:66934; -.
DR UCSC; uc008noj.2; mouse.
DR CTD; 79980; -.
DR MGI; MGI:1914184; Dsn1.
DR VEuPathDB; HostDB:ENSMUSG00000027635; -.
DR eggNOG; ENOG502S0JV; Eukaryota.
DR GeneTree; ENSGT00390000011347; -.
DR HOGENOM; CLU_042801_0_0_1; -.
DR InParanoid; Q9CYC5; -.
DR OMA; KSQSWRR; -.
DR OrthoDB; 922920at2759; -.
DR PhylomeDB; Q9CYC5; -.
DR TreeFam; TF335504; -.
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-6798695; Neutrophil degranulation.
DR Reactome; R-MMU-68877; Mitotic Prometaphase.
DR Reactome; R-MMU-9648025; EML4 and NUDC in mitotic spindle formation.
DR BioGRID-ORCS; 66934; 14 hits in 75 CRISPR screens.
DR PRO; PR:Q9CYC5; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q9CYC5; protein.
DR Bgee; ENSMUSG00000027635; Expressed in animal zygote and 195 other tissues.
DR ExpressionAtlas; Q9CYC5; baseline and differential.
DR Genevisible; Q9CYC5; MM.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0001650; C:fibrillar center; ISO:MGI.
DR GO; GO:0000776; C:kinetochore; ISO:MGI.
DR GO; GO:0000444; C:MIS12/MIND type complex; ISS:UniProtKB.
DR GO; GO:0031617; C:NMS complex; IC:ComplexPortal.
DR GO; GO:0016604; C:nuclear body; ISO:MGI.
DR GO; GO:0000818; C:nuclear MIS12/MIND complex; IBA:GO_Central.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IBA:GO_Central.
DR InterPro; IPR013218; Dsn1/Mis13.
DR PANTHER; PTHR14778; PTHR14778; 1.
DR Pfam; PF08202; MIS13; 1.
PE 1: Evidence at protein level;
KW Cell cycle; Cell division; Centromere; Chromosome; Chromosome partition;
KW Isopeptide bond; Kinetochore; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..348
FT /note="Kinetochore-associated protein DSN1 homolog"
FT /id="PRO_0000079482"
FT REGION 1..105
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 325..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..87
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H410"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H410"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H410"
FT MOD_RES 107
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H410"
FT MOD_RES 123
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H410"
FT MOD_RES 331
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CROSSLNK 253
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H410"
FT CONFLICT 6
FT /note="R -> G (in Ref. 1; BAB30906)"
FT /evidence="ECO:0000305"
FT CONFLICT 330
FT /note="S -> T (in Ref. 1; BAB24479)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 348 AA; 39553 MW; 951795E67E65062E CRC64;
MTSVTRSEDQ EPTMSETQDR PLQPSLKPLE ALPQSSAYQE MMTQGVSEEK NHLGSNPGEG
ESCGADHQEG SQLRSFHLSP QEQSIRPQDR RQSWRRASMK EVNRRKSLAP FHPGITELCR
SISVKLAQSQ RLGALLLSSF QFSVEKLEPF LKNTKDFSLE CFRAKASSLS EELKHFTDRL
GNDGTLQKCF VEDSKEKAAD FSLEASVAEV KEYITKFSLE RQAWDRLLLQ YQNEVPPEEM
PRGSTETRIT EVKVDPAAYL RSSQKEVLST KPDYQRIVQD QNQVFAYVEL VMDELQGSVK
QLQALMDEST QYLQKVSVQL KKRSMDQLDS SPARKLLKLP LQSSPSTQ
