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DCTN6_MOUSE
ID   DCTN6_MOUSE             Reviewed;         190 AA.
AC   Q9WUB4; Q8C2M9; Q9QZB8;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Dynactin subunit 6;
DE   AltName: Full=Dynactin subunit p27;
DE   AltName: Full=Protein WS-3;
GN   Name=Dctn6; Synonyms=Ws3;
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 [MRNA], INDUCTION, AND POSSIBLE FUNCTION.
RC   STRAIN=BALB/cJ; TISSUE=Skeletal muscle;
RX   PubMed=10318868; DOI=10.1074/jbc.274.20.14429;
RA   Murdock D.G., Boone B.E., Esposito L.A., Wallace D.C.;
RT   "Up-regulation of nuclear and mitochondrial genes in the skeletal muscle of
RT   mice lacking the heart/muscle isoform of the adenine nucleotide
RT   translocator.";
RL   J. Biol. Chem. 274:14429-14433(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND SUBUNIT.
RX   PubMed=10525537; DOI=10.1083/jcb.147.2.307;
RA   Eckley D.M., Gill S.R., Melkonian K.A., Bingham J.B., Goodson H.V.,
RA   Heuser J.E., Schroer T.A.;
RT   "Analysis of dynactin subcomplexes reveals a novel actin-related protein
RT   associated with the Arp1 minifilament pointed end.";
RL   J. Cell Biol. 147:307-320(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Embryo, and Thymus;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
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   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Heart, Kidney, Lung, Spleen, and 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   -!- SUBUNIT: Member of the pointed-end complex of the dynactin shoulder
CC       complex which contains DCTN4, DCTN5 and DCTN6 subunits and ACTR10.
CC       Within the complex DCTN6 forms a heterodimer with DCTN5. Interacts with
CC       PLK1 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}.
CC       Chromosome, centromere, kinetochore {ECO:0000250}.
CC   -!- INDUCTION: Up-regulated in Ant1-deficient mice.
CC       {ECO:0000269|PubMed:10318868}.
CC   -!- PTM: Phosphorylation at Thr-186 by CDK1 during mitotic prometaphase
CC       creates a binding site for PLK1 that facilitates its recruitment to
CC       kinetochores. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the dynactin subunits 5/6 family. Dynactin
CC       subunit 6 subfamily. {ECO:0000305}.
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DR   EMBL; AF124788; AAD30477.1; -; mRNA.
DR   EMBL; AF190796; AAF05616.1; -; mRNA.
DR   EMBL; AK003618; BAB22892.1; -; mRNA.
DR   EMBL; AK088312; BAC40276.1; -; mRNA.
DR   EMBL; BC029249; AAH29249.1; -; mRNA.
DR   CCDS; CCDS22238.1; -.
DR   RefSeq; NP_001280686.1; NM_001293757.1.
DR   RefSeq; NP_001280687.1; NM_001293758.1.
DR   RefSeq; NP_001280688.1; NM_001293759.1.
DR   RefSeq; NP_035852.1; NM_011722.4.
DR   AlphaFoldDB; Q9WUB4; -.
DR   SMR; Q9WUB4; -.
DR   BioGRID; 204585; 6.
DR   IntAct; Q9WUB4; 2.
DR   MINT; Q9WUB4; -.
DR   STRING; 10090.ENSMUSP00000033913; -.
DR   iPTMnet; Q9WUB4; -.
DR   PhosphoSitePlus; Q9WUB4; -.
DR   EPD; Q9WUB4; -.
DR   MaxQB; Q9WUB4; -.
DR   PaxDb; Q9WUB4; -.
DR   PRIDE; Q9WUB4; -.
DR   ProteomicsDB; 279605; -.
DR   Antibodypedia; 10535; 174 antibodies from 25 providers.
DR   DNASU; 22428; -.
DR   Ensembl; ENSMUST00000033913; ENSMUSP00000033913; ENSMUSG00000031516.
DR   GeneID; 22428; -.
DR   KEGG; mmu:22428; -.
DR   UCSC; uc009lko.3; mouse.
DR   CTD; 10671; -.
DR   MGI; MGI:1343154; Dctn6.
DR   VEuPathDB; HostDB:ENSMUSG00000031516; -.
DR   eggNOG; KOG4042; Eukaryota.
DR   GeneTree; ENSGT00390000017890; -.
DR   InParanoid; Q9WUB4; -.
DR   OMA; PDYTVVY; -.
DR   OrthoDB; 1278795at2759; -.
DR   PhylomeDB; Q9WUB4; -.
DR   TreeFam; TF352888; -.
DR   Reactome; R-MMU-2132295; MHC class II antigen presentation.
DR   Reactome; R-MMU-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR   Reactome; R-MMU-6807878; COPI-mediated anterograde transport.
DR   Reactome; R-MMU-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR   BioGRID-ORCS; 22428; 29 hits in 74 CRISPR screens.
DR   ChiTaRS; Dctn6; mouse.
DR   PRO; PR:Q9WUB4; -.
DR   Proteomes; UP000000589; Chromosome 8.
DR   RNAct; Q9WUB4; protein.
DR   Bgee; ENSMUSG00000031516; Expressed in rostral migratory stream and 261 other tissues.
DR   ExpressionAtlas; Q9WUB4; baseline and differential.
DR   Genevisible; Q9WUB4; MM.
DR   GO; GO:0005813; C:centrosome; ISO:MGI.
DR   GO; GO:0005869; C:dynactin complex; IDA:UniProtKB.
DR   GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; NAS:UniProtKB.
DR   GO; GO:0003824; F:catalytic activity; NAS:UniProtKB.
DR   GO; GO:0070840; F:dynein complex binding; IDA:UniProtKB.
DR   GO; GO:0008610; P:lipid biosynthetic process; NAS:UniProtKB.
DR   GO; GO:0007005; P:mitochondrion organization; NAS:UniProtKB.
DR   GO; GO:0007052; P:mitotic spindle organization; IDA:MGI.
DR   InterPro; IPR027777; DCTN6.
DR   InterPro; IPR001451; Hexapep.
DR   InterPro; IPR011004; Trimer_LpxA-like_sf.
DR   PANTHER; PTHR13072; PTHR13072; 1.
DR   Pfam; PF00132; Hexapep; 1.
DR   SUPFAM; SSF51161; SSF51161; 1.
PE   1: Evidence at protein level;
KW   Centromere; Chromosome; Cytoplasm; Cytoskeleton; Kinetochore;
KW   Phosphoprotein; Reference proteome.
FT   CHAIN           1..190
FT                   /note="Dynactin subunit 6"
FT                   /id="PRO_0000079831"
FT   MOD_RES         186
FT                   /note="Phosphothreonine; by CDK1"
FT                   /evidence="ECO:0000250|UniProtKB:O00399"
FT   CONFLICT        100
FT                   /note="K -> T (in Ref. 2; AAF05616)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        168
FT                   /note="M -> I (in Ref. 3; BAC40276)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   190 AA;  20670 MW;  F18919A1089EB69A CRC64;
     MAEKTQKSVK IAPGAVVCVE SEIRGDVTIG PRTVIHPKAR IIAEAGPIII GEGNLIEEQA
     LIINAHPDNI IPDTEDTEPK PMIIGTNNVF EVGCHSQAMK MGDNNVIESK AYVGRNVILT
     SGCIIGACCS LNTFEAIPEN TVIYGADCLR RVQTERPQPQ TLQLDFLMKI LPNYHHLKKT
     MKGSSTPVKN
 
 
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