DCTN2_HUMAN
ID DCTN2_HUMAN Reviewed; 401 AA.
AC Q13561; B2RBK5; Q86YN2; Q9BW17;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Dynactin subunit 2;
DE AltName: Full=50 kDa dynein-associated polypeptide;
DE AltName: Full=Dynactin complex 50 kDa subunit;
DE Short=DCTN-50;
DE AltName: Full=p50 dynamitin;
GN Name=DCTN2; Synonyms=DCTN50;
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]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PARTIAL PROTEIN SEQUENCE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=8647893; DOI=10.1083/jcb.132.4.617;
RA Echeverri C.J., Paschal B.M., Vaughan K.T., Vallee R.B.;
RT "Molecular characterization of the 50-kD subunit of dynactin reveals
RT function for the complex in chromosome alignment and spindle organization
RT during mitosis.";
RL J. Cell Biol. 132:617-633(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
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.H.,
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.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, Skin, and Uterus;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-385 (ISOFORM 3).
RA Aumais J.P., Yu-Lee L.-Y.;
RT "Human 50 kD dynactin subunit, p50 dynamitin, isolated from HeLa cells.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 2-14.
RC TISSUE=Platelet;
RX PubMed=12665801; DOI=10.1038/nbt810;
RA Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R.,
RA Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass spectrometric
RT identification of sorted N-terminal peptides.";
RL Nat. Biotechnol. 21:566-569(2003).
RN [7]
RP PROTEIN SEQUENCE OF 2-14, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT
RP ALA-2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Ramsay A., Leung H.Y.;
RL Submitted (FEB-2009) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 6-14; 79-96; 106-119; 157-185; 231-282 AND 366-395, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP INTERACTION WITH MAPRE1.
RX PubMed=10226031; DOI=10.1016/s0960-9822(99)80190-0;
RA Berrueta L., Tirnauer J.S., Schuyler S.C., Pellman D., Bierer B.E.;
RT "The APC-associated protein EB1 associates with components of the dynactin
RT complex and cytoplasmic dynein intermediate chain.";
RL Curr. Biol. 9:425-428(1999).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
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 [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
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 [14]
RP INTERACTION WITH ECPAS.
RX PubMed=20682791; DOI=10.1074/jbc.m110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S., Hughes R.E.,
RA Rechsteiner M.;
RT "A protein interaction network for Ecm29 links the 26 S proteasome to
RT molecular motors and endosomal components.";
RL J. Biol. Chem. 285:31616-31633(2010).
RN [15]
RP INTERACTION WITH DYNAP.
RX PubMed=20978158; DOI=10.1158/1535-7163.mct-10-0730;
RA Kunoh T., Noda T., Koseki K., Sekigawa M., Takagi M., Shin-ya K.,
RA Goshima N., Iemura S., Natsume T., Wada S., Mukai Y., Ohta S., Sasaki R.,
RA Mizukami T.;
RT "A novel human dynactin-associated protein, dynAP, promotes activation of
RT Akt, and ergosterol-related compounds induce dynAP-dependent apoptosis of
RT human cancer cells.";
RL Mol. Cancer Ther. 9:2934-2942(2010).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [17]
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 [18]
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 [19]
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).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83; THR-134 AND THR-198, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
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).
CC -!- FUNCTION: Modulates cytoplasmic dynein binding to an organelle, and
CC plays a role in prometaphase chromosome alignment and spindle
CC organization during mitosis. Involved in anchoring microtubules to
CC centrosomes. May play a role in synapse formation during brain
CC development.
CC -!- SUBUNIT: Subunit of dynactin, a multiprotein complex associated with
CC dynein. Interacts with BICD2 and CEP135 (By similarity). Interacts with
CC DYNAP (PubMed:20978158). Interacts with ECPAS (PubMed:20682791).
CC Interacts with MAPRE1 (PubMed:10226031). {ECO:0000250|UniProtKB:Q99KJ8,
CC ECO:0000269|PubMed:10226031, ECO:0000269|PubMed:20682791,
CC ECO:0000269|PubMed:20978158}.
CC -!- INTERACTION:
CC Q13561; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-715074, EBI-11096309;
CC Q13561; P05067: APP; NbExp=3; IntAct=EBI-715074, EBI-77613;
CC Q13561; P78537: BLOC1S1; NbExp=3; IntAct=EBI-715074, EBI-348630;
CC Q13561; Q6QNY1: BLOC1S2; NbExp=3; IntAct=EBI-715074, EBI-465872;
CC Q13561; Q9UL45: BLOC1S6; NbExp=3; IntAct=EBI-715074, EBI-465781;
CC Q13561; Q96GS4: BORCS6; NbExp=3; IntAct=EBI-715074, EBI-10193358;
CC Q13561; P0C7W6: CCDC172; NbExp=4; IntAct=EBI-715074, EBI-2548868;
CC Q13561; Q9H3R5: CENPH; NbExp=5; IntAct=EBI-715074, EBI-1003700;
CC Q13561; Q9C0F1: CEP44; NbExp=4; IntAct=EBI-715074, EBI-744115;
CC Q13561; Q96JB2-2: COG3; NbExp=3; IntAct=EBI-715074, EBI-9091495;
CC Q13561; Q13561: DCTN2; NbExp=4; IntAct=EBI-715074, EBI-715074;
CC Q13561; P24522: GADD45A; NbExp=7; IntAct=EBI-715074, EBI-448167;
CC Q13561; O95257: GADD45G; NbExp=5; IntAct=EBI-715074, EBI-448202;
CC Q13561; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-715074, EBI-2514791;
CC Q13561; P42858: HTT; NbExp=12; IntAct=EBI-715074, EBI-466029;
CC Q13561; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-715074, EBI-2125614;
CC Q13561; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-715074, EBI-14069005;
CC Q13561; Q9UPY8: MAPRE3; NbExp=3; IntAct=EBI-715074, EBI-726739;
CC Q13561; O75340: PDCD6; NbExp=4; IntAct=EBI-715074, EBI-352915;
CC Q13561; Q9UJ41-4: RABGEF1; NbExp=3; IntAct=EBI-715074, EBI-14093916;
CC Q13561; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-715074, EBI-726876;
CC Q13561; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-715074, EBI-358489;
CC Q13561; Q8N3L3: TXLNB; NbExp=3; IntAct=EBI-715074, EBI-6116822;
CC Q13561; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-715074, EBI-739895;
CC Q13561; Q96AX1: VPS33A; NbExp=3; IntAct=EBI-715074, EBI-2527283;
CC Q13561; P59634: 6; Xeno; NbExp=2; IntAct=EBI-715074, EBI-25489038;
CC Q13561; Q7TLC7: ORF14; Xeno; NbExp=2; IntAct=EBI-715074, EBI-25488942;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, centrosome {ECO:0000269|PubMed:14654843,
CC ECO:0000269|PubMed:8647893}. Membrane {ECO:0000269|PubMed:8647893};
CC Peripheral membrane protein {ECO:0000269|PubMed:8647893}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q13561-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q13561-2; Sequence=VSP_040485;
CC Name=3;
CC IsoId=Q13561-3; Sequence=VSP_040486;
CC -!- SIMILARITY: Belongs to the dynactin subunit 2 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO34395.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U50733; AAC50423.1; -; mRNA.
DR EMBL; AK314705; BAG37252.1; -; mRNA.
DR EMBL; AC022366; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022506; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000718; AAH00718.1; -; mRNA.
DR EMBL; BC009468; AAH09468.1; -; mRNA.
DR EMBL; BC014083; AAH14083.1; -; mRNA.
DR EMBL; AY189155; AAO34395.1; ALT_FRAME; mRNA.
DR CCDS; CCDS44930.1; -. [Q13561-2]
DR CCDS; CCDS58245.1; -. [Q13561-1]
DR CCDS; CCDS73489.1; -. [Q13561-3]
DR RefSeq; NP_001248341.1; NM_001261412.1. [Q13561-3]
DR RefSeq; NP_001248342.1; NM_001261413.1. [Q13561-1]
DR RefSeq; NP_006391.1; NM_006400.4. [Q13561-2]
DR AlphaFoldDB; Q13561; -.
DR SMR; Q13561; -.
DR BioGRID; 115794; 283.
DR DIP; DIP-37545N; -.
DR IntAct; Q13561; 127.
DR MINT; Q13561; -.
DR STRING; 9606.ENSP00000408910; -.
DR GlyGen; Q13561; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q13561; -.
DR MetOSite; Q13561; -.
DR PhosphoSitePlus; Q13561; -.
DR BioMuta; DCTN2; -.
DR DMDM; 22096346; -.
DR REPRODUCTION-2DPAGE; IPI00220503; -.
DR EPD; Q13561; -.
DR jPOST; Q13561; -.
DR MassIVE; Q13561; -.
DR MaxQB; Q13561; -.
DR PaxDb; Q13561; -.
DR PeptideAtlas; Q13561; -.
DR PRIDE; Q13561; -.
DR ProteomicsDB; 59558; -. [Q13561-1]
DR ProteomicsDB; 59559; -. [Q13561-2]
DR ProteomicsDB; 59560; -. [Q13561-3]
DR Antibodypedia; 28711; 385 antibodies from 35 providers.
DR DNASU; 10540; -.
DR Ensembl; ENST00000434715.7; ENSP00000408910.3; ENSG00000175203.17. [Q13561-2]
DR Ensembl; ENST00000543672.6; ENSP00000439376.2; ENSG00000175203.17. [Q13561-3]
DR Ensembl; ENST00000548249.6; ENSP00000447824.1; ENSG00000175203.17. [Q13561-1]
DR GeneID; 10540; -.
DR KEGG; hsa:10540; -.
DR MANE-Select; ENST00000548249.6; ENSP00000447824.1; NM_001261413.2; NP_001248342.1.
DR UCSC; uc001som.3; human. [Q13561-1]
DR CTD; 10540; -.
DR DisGeNET; 10540; -.
DR GeneCards; DCTN2; -.
DR GeneReviews; DCTN2; -.
DR HGNC; HGNC:2712; DCTN2.
DR HPA; ENSG00000175203; Low tissue specificity.
DR MalaCards; DCTN2; -.
DR MIM; 607376; gene.
DR neXtProt; NX_Q13561; -.
DR OpenTargets; ENSG00000175203; -.
DR PharmGKB; PA27181; -.
DR VEuPathDB; HostDB:ENSG00000175203; -.
DR eggNOG; KOG3958; Eukaryota.
DR GeneTree; ENSGT00390000003427; -.
DR InParanoid; Q13561; -.
DR OMA; RGYDMRG; -.
DR OrthoDB; 951183at2759; -.
DR PhylomeDB; Q13561; -.
DR TreeFam; TF105247; -.
DR PathwayCommons; Q13561; -.
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; Q13561; -.
DR SIGNOR; Q13561; -.
DR BioGRID-ORCS; 10540; 661 hits in 1088 CRISPR screens.
DR ChiTaRS; DCTN2; human.
DR GeneWiki; DCTN2; -.
DR GenomeRNAi; 10540; -.
DR Pharos; Q13561; Tbio.
DR PRO; PR:Q13561; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q13561; protein.
DR Bgee; ENSG00000175203; Expressed in cortical plate and 211 other tissues.
DR ExpressionAtlas; Q13561; baseline and differential.
DR Genevisible; Q13561; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005869; C:dynactin complex; IDA:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0031982; C:vesicle; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0019901; F:protein kinase binding; IPI:ARUK-UCL.
DR GO; GO:0030507; F:spectrin binding; IDA:MGI.
DR GO; GO:0032402; P:melanosome transport; IEA:Ensembl.
DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro.
DR GO; GO:0007080; P:mitotic metaphase plate congression; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:UniProtKB.
DR GO; GO:0071539; P:protein localization to centrosome; IMP:SYSCILIA_CCNET.
DR InterPro; IPR028133; Dynamitin.
DR PANTHER; PTHR15346; PTHR15346; 1.
DR Pfam; PF04912; Dynamitin; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Dynein; Membrane; Microtubule; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:12665801, ECO:0000269|Ref.7,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..401
FT /note="Dynactin subunit 2"
FT /id="PRO_0000079821"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 99..132
FT /evidence="ECO:0000255"
FT COILED 214..244
FT /evidence="ECO:0000255"
FT COILED 379..399
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.7, ECO:0007744|PubMed:22814378"
FT MOD_RES 6
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:15144186"
FT MOD_RES 83
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 86
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q99KJ8"
FT MOD_RES 134
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 198
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99KJ8"
FT VAR_SEQ 35
FT /note="A -> AFAQEL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:8647893"
FT /id="VSP_040485"
FT VAR_SEQ 35
FT /note="A -> AEL (in isoform 3)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_040486"
SQ SEQUENCE 401 AA; 44231 MW; C2FF01A9739337B2 CRC64;
MADPKYADLP GIARNEPDVY ETSDLPEDDQ AEFDAEELTS TSVEHIIVNP NAAYDKFKDK
RVGTKGLDFS DRIGKTKRTG YESGEYEMLG EGLGVKETPQ QKYQRLLHEV QELTTEVEKI
KTTVKESATE EKLTPVLLAK QLAALKQQLV ASHLEKLLGP DAAINLTDPD GALAKRLLLQ
LEATKNSKGG SGGKTTGTPP DSSLVTYELH SRPEQDKFSQ AAKVAELEKR LTELETAVRC
DQDAQNPLSA GLQGACLMET VELLQAKVSA LDLAVLDQVE ARLQSVLGKV NEIAKHKASV
EDADTQSKVH QLYETIQRWS PIASTLPELV QRLVTIKQLH EQAMQFGQLL THLDTTQQMI
ANSLKDNTTL LTQVQTTMRE NLATVEGNFA SIDERMKKLG K
