Full text data of DCTN3
DCTN3
(DCTN22)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Dynactin subunit 3 (Dynactin complex subunit 22 kDa subunit; p22)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Dynactin subunit 3 (Dynactin complex subunit 22 kDa subunit; p22)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O75935
ID DCTN3_HUMAN Reviewed; 186 AA.
AC O75935; A6NII7; B2RBM5; Q5T1I5; Q5T1I7; Q5T8G3; Q9BPU8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Dynactin subunit 3;
DE AltName: Full=Dynactin complex subunit 22 kDa subunit;
DE Short=p22;
GN Name=DCTN3; Synonyms=DCTN22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 20-28 AND
RP 67-75, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Neuron;
RX PubMed=9722614; DOI=10.1083/jcb.142.4.1023;
RA Karki S., LaMonte B., Holzbaur E.L.F.;
RT "Characterization of the p22 subunit of dynactin reveals the
RT localization of cytoplasmic dynein and dynactin to the midbody of
RT dividing cells.";
RL J. Cell Biol. 142:1023-1034(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Together with dynein may be involved in spindle assembly
CC and cytokinesis.
CC -!- SUBUNIT: Subunit of dynactin, a multiprotein complex associated
CC with dynein.
CC -!- INTERACTION:
CC P40425:PBX2; NbExp=1; IntAct=EBI-347442, EBI-348489;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Chromosome, centromere,
CC kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow.
CC Midbody. Note=Localizes to punctate cytoplasmic structures and to
CC the centrosome during interphase, and to kinetochores and to
CC spindle poles throughout mitosis. Colocalizes with dynein to the
CC cleavage furrow and to midbody of dividing cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75935-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75935-2; Sequence=VSP_051964;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O75935-3; Sequence=VSP_051961;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC muscle and pancreas and detected at lower levels in brain.
CC -!- SIMILARITY: Belongs to the dynactin subunit 3 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI13144.1; Type=Erroneous initiation;
CC Sequence=CAI14178.1; Type=Erroneous gene model prediction;
CC Sequence=CAI14180.1; Type=Erroneous initiation;
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DR EMBL; AF082513; AAC61280.1; -; mRNA.
DR EMBL; CR541889; CAG46687.1; -; mRNA.
DR EMBL; AK314730; BAG37272.1; -; mRNA.
DR EMBL; AL160270; CAI13143.1; -; Genomic_DNA.
DR EMBL; AL450283; CAI13143.1; JOINED; Genomic_DNA.
DR EMBL; AL160270; CAI13144.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL450283; CAI13144.1; JOINED; Genomic_DNA.
DR EMBL; AL160270; CAI13145.1; -; Genomic_DNA.
DR EMBL; AL450283; CAI13145.1; JOINED; Genomic_DNA.
DR EMBL; AL450283; CAI14178.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL450283; CAI14180.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL160270; CAI14180.1; JOINED; Genomic_DNA.
DR EMBL; AL450283; CAI14181.1; -; Genomic_DNA.
DR EMBL; AL160270; CAI14181.1; JOINED; Genomic_DNA.
DR EMBL; AL450283; CAI14182.1; -; Genomic_DNA.
DR EMBL; AL160270; CAI14182.1; JOINED; Genomic_DNA.
DR EMBL; CH471071; EAW58440.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58441.1; -; Genomic_DNA.
DR EMBL; BC000319; AAH00319.1; -; mRNA.
DR EMBL; BC003004; AAH03004.1; -; mRNA.
DR EMBL; BC107697; AAI07698.1; -; mRNA.
DR RefSeq; NP_001268354.1; NM_001281425.1.
DR RefSeq; NP_001268355.1; NM_001281426.1.
DR RefSeq; NP_009165.1; NM_007234.4.
DR RefSeq; NP_077324.1; NM_024348.3.
DR UniGene; Hs.511768; -.
DR ProteinModelPortal; O75935; -.
DR IntAct; O75935; 9.
DR MINT; MINT-1033946; -.
DR STRING; 9606.ENSP00000259632; -.
DR PhosphoSite; O75935; -.
DR PaxDb; O75935; -.
DR PRIDE; O75935; -.
DR DNASU; 11258; -.
DR Ensembl; ENST00000259632; ENSP00000259632; ENSG00000137100.
DR Ensembl; ENST00000341694; ENSP00000343986; ENSG00000137100.
DR Ensembl; ENST00000378916; ENSP00000368196; ENSG00000137100.
DR GeneID; 11258; -.
DR KEGG; hsa:11258; -.
DR UCSC; uc003zux.1; human.
DR CTD; 11258; -.
DR GeneCards; GC09M034614; -.
DR HGNC; HGNC:2713; DCTN3.
DR HPA; HPA044905; -.
DR MIM; 607387; gene.
DR neXtProt; NX_O75935; -.
DR PharmGKB; PA27182; -.
DR eggNOG; NOG83082; -.
DR HOGENOM; HOG000231666; -.
DR HOVERGEN; HBG053181; -.
DR InParanoid; O75935; -.
DR KO; K10425; -.
DR OMA; NTANKRE; -.
DR OrthoDB; EOG7JDQZV; -.
DR PhylomeDB; O75935; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; DCTN3; human.
DR GeneWiki; DCTN3; -.
DR GenomeRNAi; 11258; -.
DR NextBio; 42838; -.
DR PRO; PR:O75935; -.
DR ArrayExpress; O75935; -.
DR Bgee; O75935; -.
DR CleanEx; HS_DCTN3; -.
DR Genevestigator; O75935; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; IPI:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0000910; P:cytokinesis; IDA:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007017; P:microtubule-based process; IEA:Ensembl.
DR GO; GO:0007067; P:mitosis; TAS:ProtInc.
DR InterPro; IPR009991; Dynactin_p22.
DR Pfam; PF07426; Dynactin_p22; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Centromere; Chromosome; Coiled coil; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Kinetochore; Mitosis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 186 Dynactin subunit 3.
FT /FTId=PRO_0000225603.
FT COILED 135 157 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 90 117 Missing (in isoform 3).
FT /FTId=VSP_051961.
FT VAR_SEQ 138 186 DQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAA
FT TQVKPAEE -> APWGVGVRDEAGSLVEDVGFAQFLSVLHF
FT GPTGPVCGNH (in isoform 2).
FT /FTId=VSP_051964.
SQ SEQUENCE 186 AA; 21119 MW; 70A0B26E24603A77 CRC64;
MAGLTDLQRL QARVEELERW VYGPGGARGS RKVADGLVKV QVALGNISSK RERVKILYKK
IEDLIKYLDP EYIDRIAIPD ASKLQFILAE EQFILSQVAL LEQVNALVPM LDSAHIKAVP
EHAARLQRLA QIHIQQQDQC VEITEESKAL LEEYNKTTML LSKQFVQWDE LLCQLEAATQ
VKPAEE
//
ID DCTN3_HUMAN Reviewed; 186 AA.
AC O75935; A6NII7; B2RBM5; Q5T1I5; Q5T1I7; Q5T8G3; Q9BPU8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1998, sequence version 1.
DT 22-JAN-2014, entry version 110.
DE RecName: Full=Dynactin subunit 3;
DE AltName: Full=Dynactin complex subunit 22 kDa subunit;
DE Short=p22;
GN Name=DCTN3; Synonyms=DCTN22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 20-28 AND
RP 67-75, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Neuron;
RX PubMed=9722614; DOI=10.1083/jcb.142.4.1023;
RA Karki S., LaMonte B., Holzbaur E.L.F.;
RT "Characterization of the p22 subunit of dynactin reveals the
RT localization of cytoplasmic dynein and dynactin to the midbody of
RT dividing cells.";
RL J. Cell Biol. 142:1023-1034(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Together with dynein may be involved in spindle assembly
CC and cytokinesis.
CC -!- SUBUNIT: Subunit of dynactin, a multiprotein complex associated
CC with dynein.
CC -!- INTERACTION:
CC P40425:PBX2; NbExp=1; IntAct=EBI-347442, EBI-348489;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome. Chromosome, centromere,
CC kinetochore. Cytoplasm, cytoskeleton, spindle. Cleavage furrow.
CC Midbody. Note=Localizes to punctate cytoplasmic structures and to
CC the centrosome during interphase, and to kinetochores and to
CC spindle poles throughout mitosis. Colocalizes with dynein to the
CC cleavage furrow and to midbody of dividing cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O75935-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O75935-2; Sequence=VSP_051964;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O75935-3; Sequence=VSP_051961;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in
CC muscle and pancreas and detected at lower levels in brain.
CC -!- SIMILARITY: Belongs to the dynactin subunit 3 family.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI13144.1; Type=Erroneous initiation;
CC Sequence=CAI14178.1; Type=Erroneous gene model prediction;
CC Sequence=CAI14180.1; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; AF082513; AAC61280.1; -; mRNA.
DR EMBL; CR541889; CAG46687.1; -; mRNA.
DR EMBL; AK314730; BAG37272.1; -; mRNA.
DR EMBL; AL160270; CAI13143.1; -; Genomic_DNA.
DR EMBL; AL450283; CAI13143.1; JOINED; Genomic_DNA.
DR EMBL; AL160270; CAI13144.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL450283; CAI13144.1; JOINED; Genomic_DNA.
DR EMBL; AL160270; CAI13145.1; -; Genomic_DNA.
DR EMBL; AL450283; CAI13145.1; JOINED; Genomic_DNA.
DR EMBL; AL450283; CAI14178.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL450283; CAI14180.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL160270; CAI14180.1; JOINED; Genomic_DNA.
DR EMBL; AL450283; CAI14181.1; -; Genomic_DNA.
DR EMBL; AL160270; CAI14181.1; JOINED; Genomic_DNA.
DR EMBL; AL450283; CAI14182.1; -; Genomic_DNA.
DR EMBL; AL160270; CAI14182.1; JOINED; Genomic_DNA.
DR EMBL; CH471071; EAW58440.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58441.1; -; Genomic_DNA.
DR EMBL; BC000319; AAH00319.1; -; mRNA.
DR EMBL; BC003004; AAH03004.1; -; mRNA.
DR EMBL; BC107697; AAI07698.1; -; mRNA.
DR RefSeq; NP_001268354.1; NM_001281425.1.
DR RefSeq; NP_001268355.1; NM_001281426.1.
DR RefSeq; NP_009165.1; NM_007234.4.
DR RefSeq; NP_077324.1; NM_024348.3.
DR UniGene; Hs.511768; -.
DR ProteinModelPortal; O75935; -.
DR IntAct; O75935; 9.
DR MINT; MINT-1033946; -.
DR STRING; 9606.ENSP00000259632; -.
DR PhosphoSite; O75935; -.
DR PaxDb; O75935; -.
DR PRIDE; O75935; -.
DR DNASU; 11258; -.
DR Ensembl; ENST00000259632; ENSP00000259632; ENSG00000137100.
DR Ensembl; ENST00000341694; ENSP00000343986; ENSG00000137100.
DR Ensembl; ENST00000378916; ENSP00000368196; ENSG00000137100.
DR GeneID; 11258; -.
DR KEGG; hsa:11258; -.
DR UCSC; uc003zux.1; human.
DR CTD; 11258; -.
DR GeneCards; GC09M034614; -.
DR HGNC; HGNC:2713; DCTN3.
DR HPA; HPA044905; -.
DR MIM; 607387; gene.
DR neXtProt; NX_O75935; -.
DR PharmGKB; PA27182; -.
DR eggNOG; NOG83082; -.
DR HOGENOM; HOG000231666; -.
DR HOVERGEN; HBG053181; -.
DR InParanoid; O75935; -.
DR KO; K10425; -.
DR OMA; NTANKRE; -.
DR OrthoDB; EOG7JDQZV; -.
DR PhylomeDB; O75935; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; DCTN3; human.
DR GeneWiki; DCTN3; -.
DR GenomeRNAi; 11258; -.
DR NextBio; 42838; -.
DR PRO; PR:O75935; -.
DR ArrayExpress; O75935; -.
DR Bgee; O75935; -.
DR CleanEx; HS_DCTN3; -.
DR Genevestigator; O75935; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; IPI:UniProtKB.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IEA:UniProtKB-SubCell.
DR GO; GO:0005198; F:structural molecule activity; TAS:ProtInc.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0000910; P:cytokinesis; IDA:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007017; P:microtubule-based process; IEA:Ensembl.
DR GO; GO:0007067; P:mitosis; TAS:ProtInc.
DR InterPro; IPR009991; Dynactin_p22.
DR Pfam; PF07426; Dynactin_p22; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division;
KW Centromere; Chromosome; Coiled coil; Complete proteome; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Kinetochore; Mitosis;
KW Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 186 Dynactin subunit 3.
FT /FTId=PRO_0000225603.
FT COILED 135 157 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT VAR_SEQ 90 117 Missing (in isoform 3).
FT /FTId=VSP_051961.
FT VAR_SEQ 138 186 DQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAA
FT TQVKPAEE -> APWGVGVRDEAGSLVEDVGFAQFLSVLHF
FT GPTGPVCGNH (in isoform 2).
FT /FTId=VSP_051964.
SQ SEQUENCE 186 AA; 21119 MW; 70A0B26E24603A77 CRC64;
MAGLTDLQRL QARVEELERW VYGPGGARGS RKVADGLVKV QVALGNISSK RERVKILYKK
IEDLIKYLDP EYIDRIAIPD ASKLQFILAE EQFILSQVAL LEQVNALVPM LDSAHIKAVP
EHAARLQRLA QIHIQQQDQC VEITEESKAL LEEYNKTTML LSKQFVQWDE LLCQLEAATQ
VKPAEE
//
MIM
607387
*RECORD*
*FIELD* NO
607387
*FIELD* TI
*607387 DYNACTIN 3; DCTN3
;;DYNACTIN COMPLEX, 22-KD SUBUNIT; DCTN22
*FIELD* TX
DESCRIPTION
read more
DCTN3 is a component of the dynactin macromolecular complex. Dynactin,
along with dynein (see 600112), is required for diverse cellular
functions, including intracellular vesicular transport, spindle
formation, chromosome movement, nuclear positioning, and axonogenesis.
CLONING
Karki et al. (1998) affinity purified DCTN3, which they called p22, from
brain using recombinant dynein intermediate chain (see 603331) as
ligand. They used the amino acid sequences of peptide fragments to clone
full-length DCTN3 from a neuron cDNA library. The deduced 185-amino acid
protein has a calculated molecular mass of about 21 kD and is primarily
an alpha-helical protein with no significant coiled-coil regions.
Northern blot analysis revealed expression of a 1-kb transcript in all
tissues examined, with highest expression in muscle and pancreas and
lower levels in brain. Western blot analysis of rat brain cytosol
revealed an apparent molecular mass of about 22 kD.
GENE FUNCTION
By affinity chromatography of rat brain cytosol, Karki et al. (1998)
found that Dctn3 binds directly to the p150 subunit of dynactin (DCTN1;
601143). Immunolocalization of Dctn3 in rat cell lines revealed that it
associates with punctate cytoplasmic structures. Dctn3 localized to the
centrosome during interphase and to kinetochores and to spindle poles
throughout mitosis. Cytoplasmic dynein and dynactin subunits, including
DCTN3, localized to the cleavage furrow and to the midbodies of dividing
cells.
MAPPING
By radiation hybrid analysis, Mills and Jackson (2001) mapped the DCTN3
gene to chromosome 9p13.
*FIELD* RF
1. Karki, S.; LaMonte, B.; Holzbaur, E. L. F.: Characterization of
the p22 subunit of dynactin reveals the localization of cytoplasmic
dynein and dynactin to the midbody of dividing cells. J. Cell Biol. 142:
1023-1034, 1998. Note: Erratum: J. Cell Biol. 143: page following
560 only, 1998.
2. Mills, D. R.; Jackson, C. L.: Assignment of p22 dynactin light
chain (DCTN3) to human chromosome region 9p13 by radiation hybrid
mapping. Cytogenet. Cell Genet. 92: 166 only, 2001.
*FIELD* CD
Patricia A. Hartz: 11/26/2002
*FIELD* ED
terry: 07/05/2012
mgross: 11/26/2002
*RECORD*
*FIELD* NO
607387
*FIELD* TI
*607387 DYNACTIN 3; DCTN3
;;DYNACTIN COMPLEX, 22-KD SUBUNIT; DCTN22
*FIELD* TX
DESCRIPTION
read more
DCTN3 is a component of the dynactin macromolecular complex. Dynactin,
along with dynein (see 600112), is required for diverse cellular
functions, including intracellular vesicular transport, spindle
formation, chromosome movement, nuclear positioning, and axonogenesis.
CLONING
Karki et al. (1998) affinity purified DCTN3, which they called p22, from
brain using recombinant dynein intermediate chain (see 603331) as
ligand. They used the amino acid sequences of peptide fragments to clone
full-length DCTN3 from a neuron cDNA library. The deduced 185-amino acid
protein has a calculated molecular mass of about 21 kD and is primarily
an alpha-helical protein with no significant coiled-coil regions.
Northern blot analysis revealed expression of a 1-kb transcript in all
tissues examined, with highest expression in muscle and pancreas and
lower levels in brain. Western blot analysis of rat brain cytosol
revealed an apparent molecular mass of about 22 kD.
GENE FUNCTION
By affinity chromatography of rat brain cytosol, Karki et al. (1998)
found that Dctn3 binds directly to the p150 subunit of dynactin (DCTN1;
601143). Immunolocalization of Dctn3 in rat cell lines revealed that it
associates with punctate cytoplasmic structures. Dctn3 localized to the
centrosome during interphase and to kinetochores and to spindle poles
throughout mitosis. Cytoplasmic dynein and dynactin subunits, including
DCTN3, localized to the cleavage furrow and to the midbodies of dividing
cells.
MAPPING
By radiation hybrid analysis, Mills and Jackson (2001) mapped the DCTN3
gene to chromosome 9p13.
*FIELD* RF
1. Karki, S.; LaMonte, B.; Holzbaur, E. L. F.: Characterization of
the p22 subunit of dynactin reveals the localization of cytoplasmic
dynein and dynactin to the midbody of dividing cells. J. Cell Biol. 142:
1023-1034, 1998. Note: Erratum: J. Cell Biol. 143: page following
560 only, 1998.
2. Mills, D. R.; Jackson, C. L.: Assignment of p22 dynactin light
chain (DCTN3) to human chromosome region 9p13 by radiation hybrid
mapping. Cytogenet. Cell Genet. 92: 166 only, 2001.
*FIELD* CD
Patricia A. Hartz: 11/26/2002
*FIELD* ED
terry: 07/05/2012
mgross: 11/26/2002