DCTN3_HUMAN
ID DCTN3_HUMAN Reviewed; 186 AA.
AC O75935; A6NII7; B2RBM5; Q5T1I5; Q5T1I7; Q5T8G3; Q9BPU8;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Dynactin subunit 3;
DE AltName: Full=Dynactin complex subunit 22 kDa subunit;
DE Short=p22;
GN Name=DCTN3 {ECO:0000312|EMBL:CAG46687.1}; Synonyms=DCTN22;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAC61280.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 20-28 AND
RP 67-75, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Neuron {ECO:0000269|PubMed:9722614};
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 localization
RT of cytoplasmic dynein and dynactin to the midbody of dividing cells.";
RL J. Cell Biol. 142:1023-1034(1998).
RN [2] {ECO:0000305, ECO:0000312|EMBL:CAG46687.1}
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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] {ECO:0000305, ECO:0000312|EMBL:CAI13143.1}
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., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., 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., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., 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., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:CAG46687.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000305, ECO:0000312|EMBL:AAI07698.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lung {ECO:0000312|EMBL:AAH03004.1};
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 [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., Buerckstuemmer T.,
RA 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, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
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., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT 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 and
CC cytokinesis. {ECO:0000269|PubMed:9722614}.
CC -!- SUBUNIT: Subunit of dynactin, a multiprotein complex associated with
CC dynein.
CC -!- INTERACTION:
CC O75935-2; P54253: ATXN1; NbExp=6; IntAct=EBI-12091947, EBI-930964;
CC O75935-2; Q14203-5: DCTN1; NbExp=3; IntAct=EBI-12091947, EBI-25840379;
CC O75935-2; O14901: KLF11; NbExp=3; IntAct=EBI-12091947, EBI-948266;
CC O75935-2; O76011: KRT34; NbExp=3; IntAct=EBI-12091947, EBI-1047093;
CC O75935-2; Q7Z3B4: NUP54; NbExp=3; IntAct=EBI-12091947, EBI-741048;
CC O75935-2; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-12091947, EBI-2811583;
CC O75935-2; P78337: PITX1; NbExp=3; IntAct=EBI-12091947, EBI-748265;
CC O75935-2; Q15645: TRIP13; NbExp=3; IntAct=EBI-12091947, EBI-358993;
CC O75935-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-12091947, EBI-739895;
CC O75935-2; A5D8V6: VPS37C; NbExp=3; IntAct=EBI-12091947, EBI-2559305;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9722614}.
CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
CC {ECO:0000269|PubMed:9722614}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:9722614}. Cytoplasm, cytoskeleton, spindle
CC {ECO:0000269|PubMed:9722614}. Cleavage furrow
CC {ECO:0000269|PubMed:9722614}. Midbody {ECO:0000269|PubMed:9722614}.
CC Note=Localizes to punctate cytoplasmic structures and to the centrosome
CC during interphase, and to kinetochores and to spindle poles throughout
CC mitosis. Colocalizes with dynein to the cleavage furrow and to midbody
CC of dividing cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1 {ECO:0000269|PubMed:9722614};
CC IsoId=O75935-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15164053};
CC IsoId=O75935-2; Sequence=VSP_051964;
CC Name=3 {ECO:0000305};
CC IsoId=O75935-3; Sequence=VSP_051961;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed. Highly expressed in muscle
CC and pancreas and detected at lower levels in brain.
CC {ECO:0000269|PubMed:9722614}.
CC -!- SIMILARITY: Belongs to the dynactin subunit 3 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI13144.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAI14178.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAI14180.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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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 CCDS; CCDS65028.1; -. [O75935-3]
DR CCDS; CCDS6560.1; -. [O75935-1]
DR CCDS; CCDS6561.1; -. [O75935-2]
DR RefSeq; NP_001268354.1; NM_001281425.1. [O75935-3]
DR RefSeq; NP_001268355.1; NM_001281426.1.
DR RefSeq; NP_009165.1; NM_007234.4. [O75935-1]
DR RefSeq; NP_077324.1; NM_024348.3. [O75935-2]
DR AlphaFoldDB; O75935; -.
DR SMR; O75935; -.
DR BioGRID; 116418; 139.
DR IntAct; O75935; 50.
DR MINT; O75935; -.
DR STRING; 9606.ENSP00000259632; -.
DR iPTMnet; O75935; -.
DR PhosphoSitePlus; O75935; -.
DR BioMuta; DCTN3; -.
DR EPD; O75935; -.
DR jPOST; O75935; -.
DR MassIVE; O75935; -.
DR MaxQB; O75935; -.
DR PaxDb; O75935; -.
DR PeptideAtlas; O75935; -.
DR PRIDE; O75935; -.
DR ProteomicsDB; 50298; -. [O75935-1]
DR ProteomicsDB; 50299; -. [O75935-2]
DR ProteomicsDB; 50300; -. [O75935-3]
DR TopDownProteomics; O75935-1; -. [O75935-1]
DR TopDownProteomics; O75935-3; -. [O75935-3]
DR Antibodypedia; 25511; 208 antibodies from 29 providers.
DR DNASU; 11258; -.
DR Ensembl; ENST00000259632.12; ENSP00000259632.7; ENSG00000137100.16. [O75935-1]
DR Ensembl; ENST00000341694.6; ENSP00000343986.2; ENSG00000137100.16. [O75935-2]
DR Ensembl; ENST00000378916.8; ENSP00000368196.4; ENSG00000137100.16. [O75935-3]
DR GeneID; 11258; -.
DR KEGG; hsa:11258; -.
DR MANE-Select; ENST00000259632.12; ENSP00000259632.7; NM_007234.5; NP_009165.1.
DR UCSC; uc003zuw.3; human. [O75935-1]
DR CTD; 11258; -.
DR DisGeNET; 11258; -.
DR GeneCards; DCTN3; -.
DR HGNC; HGNC:2713; DCTN3.
DR HPA; ENSG00000137100; Low tissue specificity.
DR MIM; 607387; gene.
DR neXtProt; NX_O75935; -.
DR OpenTargets; ENSG00000137100; -.
DR PharmGKB; PA27182; -.
DR VEuPathDB; HostDB:ENSG00000137100; -.
DR eggNOG; ENOG502RYZ0; Eukaryota.
DR GeneTree; ENSGT00390000016210; -.
DR InParanoid; O75935; -.
DR OMA; EYNKMTI; -.
DR OrthoDB; 1444664at2759; -.
DR PhylomeDB; O75935; -.
DR TreeFam; TF105248; -.
DR PathwayCommons; O75935; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-3371497; HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand.
DR Reactome; R-HSA-380259; Loss of Nlp from mitotic centrosomes.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380284; Loss of proteins required for interphase microtubule organization from the centrosome.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR Reactome; R-HSA-5620912; Anchoring of the basal body to the plasma membrane.
DR Reactome; R-HSA-6807878; COPI-mediated anterograde transport.
DR Reactome; R-HSA-6811436; COPI-independent Golgi-to-ER retrograde traffic.
DR Reactome; R-HSA-8854518; AURKA Activation by TPX2.
DR SignaLink; O75935; -.
DR BioGRID-ORCS; 11258; 662 hits in 1089 CRISPR screens.
DR ChiTaRS; DCTN3; human.
DR GeneWiki; DCTN3; -.
DR GenomeRNAi; 11258; -.
DR Pharos; O75935; Tbio.
DR PRO; PR:O75935; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O75935; protein.
DR Bgee; ENSG00000137100; Expressed in cortical plate and 208 other tissues.
DR ExpressionAtlas; O75935; baseline and differential.
DR Genevisible; O75935; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0032154; C:cleavage furrow; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005869; C:dynactin complex; IPI:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0030496; C:midbody; IEA:UniProtKB-SubCell.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
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:0061640; P:cytoskeleton-dependent cytokinesis; IDA:UniProtKB.
DR GO; GO:0007017; P:microtubule-based process; IEA:Ensembl.
DR GO; GO:0000278; P:mitotic cell cycle; TAS:ProtInc.
DR InterPro; IPR009991; DCTN3.
DR PANTHER; PTHR28360; PTHR28360; 1.
DR Pfam; PF07426; Dynactin_p22; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cell cycle; Cell division; Centromere;
KW Chromosome; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Kinetochore; Mitosis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22814378"
FT CHAIN 2..186
FT /note="Dynactin subunit 3"
FT /id="PRO_0000225603"
FT COILED 135..157
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT VAR_SEQ 90..117
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_051961"
FT VAR_SEQ 138..186
FT /note="DQCVEITEESKALLEEYNKTTMLLSKQFVQWDELLCQLEAATQVKPAEE ->
FT APWGVGVRDEAGSLVEDVGFAQFLSVLHFGPTGPVCGNH (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15164053,
FT ECO:0000303|PubMed:15489334"
FT /id="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
