ID F8VW18_HUMAN Unreviewed; 278 AA. AC F8VW18; DT 21-SEP-2011, integrated into UniProtKB/TrEMBL. DT 21-SEP-2011, sequence version 1. DT 27-NOV-2024, entry version 91. DE RecName: Full=Dynactin subunit 2 {ECO:0000256|ARBA:ARBA00034866}; DE Flags: Fragment; GN Name=DCTN2 {ECO:0000313|Ensembl:ENSP00000449855.1}; 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 {ECO:0000313|Ensembl:ENSP00000449855.1, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000449855.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=11237011; DOI=10.1038/35057062; RG International Human Genome Sequencing Consortium; RA Lander E.S., Linton L.M., Birren B., Nusbaum C., Zody M.C., Baldwin J., RA Devon K., Dewar K., Doyle M., FitzHugh W., Funke R., Gage D., Harris K., RA Heaford A., Howland J., Kann L., Lehoczky J., LeVine R., McEwan P., RA McKernan K., Meldrim J., Mesirov J.P., Miranda C., Morris W., Naylor J., RA Raymond C., Rosetti M., Santos R., Sheridan A., Sougnez C., RA Stange-Thomann N., Stojanovic N., Subramanian A., Wyman D., Rogers J., RA Sulston J., Ainscough R., Beck S., Bentley D., Burton J., Clee C., RA Carter N., Coulson A., Deadman R., Deloukas P., Dunham A., Dunham I., RA Durbin R., French L., Grafham D., Gregory S., Hubbard T., Humphray S., RA Hunt A., Jones M., Lloyd C., McMurray A., Matthews L., Mercer S., Milne S., RA Mullikin J.C., Mungall A., Plumb R., Ross M., Shownkeen R., Sims S., RA Waterston R.H., Wilson R.K., Hillier L.W., McPherson J.D., Marra M.A., RA Mardis E.R., Fulton L.A., Chinwalla A.T., Pepin K.H., Gish W.R., RA Chissoe S.L., Wendl M.C., Delehaunty K.D., Miner T.L., Delehaunty A., RA Kramer J.B., Cook L.L., Fulton R.S., Johnson D.L., Minx P.J., Clifton S.W., RA Hawkins T., Branscomb E., Predki P., Richardson P., Wenning S., Slezak T., RA Doggett N., Cheng J.F., Olsen A., Lucas S., Elkin C., Uberbacher E., RA Frazier M., Gibbs R.A., Muzny D.M., Scherer S.E., Bouck J.B., RA Sodergren E.J., Worley K.C., Rives C.M., Gorrell J.H., Metzker M.L., RA Naylor S.L., Kucherlapati R.S., Nelson D.L., Weinstock G.M., Sakaki Y., RA Fujiyama A., Hattori M., Yada T., Toyoda A., Itoh T., Kawagoe C., RA Watanabe H., Totoki Y., Taylor T., Weissenbach J., Heilig R., Saurin W., RA Artiguenave F., Brottier P., Bruls T., Pelletier E., Robert C., Wincker P., RA Smith D.R., Doucette-Stamm L., Rubenfield M., Weinstock K., Lee H.M., RA Dubois J., Rosenthal A., Platzer M., Nyakatura G., Taudien S., Rump A., RA Yang H., Yu J., Wang J., Huang G., Gu J., Hood L., Rowen L., Madan A., RA Qin S., Davis R.W., Federspiel N.A., Abola A.P., Proctor M.J., Myers R.M., RA Schmutz J., Dickson M., Grimwood J., Cox D.R., Olson M.V., Kaul R., RA Raymond C., Shimizu N., Kawasaki K., Minoshima S., Evans G.A., RA Athanasiou M., Schultz R., Roe B.A., Chen F., Pan H., Ramser J., RA Lehrach H., Reinhardt R., McCombie W.R., de la Bastide M., Dedhia N., RA Blocker H., Hornischer K., Nordsiek G., Agarwala R., Aravind L., RA Bailey J.A., Bateman A., Batzoglou S., Birney E., Bork P., Brown D.G., RA Burge C.B., Cerutti L., Chen H.C., Church D., Clamp M., Copley R.R., RA Doerks T., Eddy S.R., Eichler E.E., Furey T.S., Galagan J., Gilbert J.G., RA Harmon C., Hayashizaki Y., Haussler D., Hermjakob H., Hokamp K., Jang W., RA Johnson L.S., Jones T.A., Kasif S., Kaspryzk A., Kennedy S., Kent W.J., RA Kitts P., Koonin E.V., Korf I., Kulp D., Lancet D., Lowe T.M., RA McLysaght A., Mikkelsen T., Moran J.V., Mulder N., Pollara V.J., RA Ponting C.P., Schuler G., Schultz J., Slater G., Smit A.F., Stupka E., RA Szustakowski J., Thierry-Mieg D., Thierry-Mieg J., Wagner L., Wallis J., RA Wheeler R., Williams A., Wolf Y.I., Wolfe K.H., Yang S.P., Yeh R.F., RA Collins F., Guyer M.S., Peterson J., Felsenfeld A., Wetterstrand K.A., RA Patrinos A., Morgan M.J., de Jong P., Catanese J.J., Osoegawa K., RA Shizuya H., Choi S., Chen Y.J.; RT "Initial sequencing and analysis of the human genome."; RL Nature 409:860-921(2001). RN [2] {ECO:0007829|PubMed:15144186} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=15144186; DOI=10.1021/ac035352d; RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., RA Peters E.C.; RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from RT human T cells using immobilized metal affinity chromatography and tandem RT mass spectrometry."; RL Anal. Chem. 76:2763-2772(2004). RN [3] {ECO:0000313|Ensembl:ENSP00000449855.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15496913; DOI=10.1038/nature03001; RG International Human Genome Sequencing Consortium; RT "Finishing the euchromatic sequence of the human genome."; RL Nature 431:931-945(2004). RN [4] {ECO:0000313|Ensembl:ENSP00000449855.1, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16541075; DOI=10.1038/nature04569; RG Baylor College of Medicine Human Genome Sequencing Center Sequence Production Team; RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., RA Song X.Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., RA Nguyen B.V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J., RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., RA Perrin W., Pickens A., Primus E.L., Pu L.L., Puazo M., Quiles M.M., RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., RA Gibbs R.A., null.; RT "The finished DNA sequence of human chromosome 12."; RL Nature 440:346-351(2006). RN [5] {ECO:0007829|PubMed:18669648} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [6] {ECO:0007829|PubMed:19690332} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [7] {ECO:0007829|PubMed:20068231} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [8] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [9] {ECO:0007829|PubMed:22905912} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=22905912; DOI=10.1021/pr300539b; RA Rosenow A., Noben J.P., Jocken J., Kallendrusch S., Fischer-Posovszky P., RA Mariman E.C., Renes J.; RT "Resveratrol-induced changes of the human adipocyte secretion profile."; RL J. Proteome Res. 11:4733-4743(2012). RN [10] {ECO:0007829|PubMed:22814378} RP IDENTIFICATION BY MASS SPECTROMETRY [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). RN [11] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [12] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [13] {ECO:0000313|Ensembl:ENSP00000449855.1} RP IDENTIFICATION. RG Ensembl; RL Submitted (AUG-2024) to UniProtKB. CC -!- FUNCTION: Part of the dynactin complex that activates the molecular CC motor dynein for ultra-processive transport along microtubules. In the CC dynactin soulder domain, binds the ACTR1A filament and acts as a CC molecular ruler to determine the length. Modulates cytoplasmic dynein CC binding to an organelle, and plays a role in prometaphase chromosome CC alignment and spindle organization during mitosis. Involved in CC anchoring microtubules to centrosomes. May play a role in synapse CC formation during brain development. {ECO:0000256|ARBA:ARBA00046220}. CC -!- SUBUNIT: Subunit of dynactin, a multiprotein complex part of a CC tripartite complex with dynein and a adapter, such as BICDL1, BICD2 or CC HOOK3. The dynactin complex is built around ACTR1A/ACTB filament and CC consists of an actin-related filament composed of a shoulder domain, a CC pointed end and a barbed end. Its length is defined by its flexible CC shoulder domain. The soulder is composed of 2 DCTN1 subunits, 4 DCTN2 CC and 2 DCTN3. The 4 DCNT2 (via N-terminus) bind the ACTR1A filament and CC act as molecular rulers to determine the length. The pointed end is CC important for binding dynein-dynactin cargo adapters and consists of 4 CC subunits: ACTR10, DCNT4, DCTN5 and DCTN6. The barbed end is composed of CC a CAPZA1:CAPZB heterodimers, which binds ACTR1A/ACTB filament and CC dynactin and stabilizes dynactin. Interacts with BICD2 and CEP135. CC Interacts with DYNAP. Interacts with ECPAS. Interacts with MAPRE1. CC {ECO:0000256|ARBA:ARBA00047142}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. CC -!- SIMILARITY: Belongs to the dynactin subunit 2 family. CC {ECO:0000256|ARBA:ARBA00006176}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AC022506; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; F8VW18; -. DR SMR; F8VW18; -. DR MassIVE; F8VW18; -. DR Antibodypedia; 28711; 370 antibodies from 34 providers. DR Ensembl; ENST00000550954.5; ENSP00000449855.1; ENSG00000175203.17. DR UCSC; uc058pys.1; human. DR HGNC; HGNC:2712; DCTN2. DR VEuPathDB; HostDB:ENSG00000175203; -. DR GeneTree; ENSGT00390000003427; -. DR HOGENOM; CLU_049964_1_0_1; -. DR ChiTaRS; DCTN2; human. DR Proteomes; UP000005640; Chromosome 12. DR Bgee; ENSG00000175203; Expressed in cortical plate and 213 other cell types or tissues. DR ExpressionAtlas; F8VW18; baseline and differential. DR GO; GO:0005813; C:centrosome; IDA:HPA. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005869; C:dynactin complex; IEA:InterPro. DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW. DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro. DR InterPro; IPR028133; Dynamitin. DR PANTHER; PTHR15346; DYNACTIN SUBUNIT; 1. DR PANTHER; PTHR15346:SF0; DYNACTIN SUBUNIT 2; 1. DR Pfam; PF04912; Dynamitin; 1. PE 1: Evidence at protein level; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490}; KW Dynein {ECO:0000256|ARBA:ARBA00023017}; KW Proteomics identification {ECO:0007829|PeptideAtlas:F8VW18, KW ECO:0007829|ProteomicsDB:F8VW18}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}. FT REGION 1..25 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 198..217 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COILED 117..144 FT /evidence="ECO:0000256|SAM:Coils" FT NON_TER 278 FT /evidence="ECO:0000313|Ensembl:ENSP00000449855.1" SQ SEQUENCE 278 AA; 30526 MW; 586DCA5CBB29E924 CRC64; MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAELVRS LTFHLLFNGE ELTSTSVEHI IVNPNAAYDK FKDKRVGTKG LDFSDRIGKT KRTGYESGEY EMLGEGLGVK ETPQQKYQRL LHEVQELTTE VEKIKTTVKE SATEEKLTPV LLAKQLAALK QQLVASHLEK LLGPDAAINL TDPDGALAKR LLLQLEATKN SKGGSGGKTT GTPPDSSLVT YELHSRPEQD KFSQAAKVAE LEKRLTELET AVRCDQDAQN PLSAGLQGAC LMETVELL //