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}.
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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
//