Full text data of DCTN2
DCTN2
(DCTN50)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Dynactin subunit 2 (50 kDa dynein-associated polypeptide; Dynactin complex 50 kDa subunit; DCTN-50; p50 dynamitin)
Dynactin subunit 2 (50 kDa dynein-associated polypeptide; Dynactin complex 50 kDa subunit; DCTN-50; p50 dynamitin)
UniProt
Q13561
ID DCTN2_HUMAN Reviewed; 401 AA.
AC Q13561; B2RBK5; Q86YN2; Q9BW17;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 135.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT organization 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.,
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 [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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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
RT project: 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
RT 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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,
RP ACETYLATION AT ALA-2, AND 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
RP 366-395, AND 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
RT dynactin complex and cytoplasmic dynein intermediate chain.";
RL Curr. Biol. 9:425-428(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6, AND MASS
RP SPECTROMETRY.
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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP SPECTROMETRY.
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 [13]
RP INTERACTION WITH ECM29.
RX PubMed=20682791; DOI=10.1074/jbc.M110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
RA Hughes R.E., 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 [14]
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.,
RA Sasaki R., Mizukami T.;
RT "A novel human dynactin-associated protein, dynAP, promotes activation
RT of Akt, and ergosterol-related compounds induce dynAP-dependent
RT apoptosis of human cancer cells.";
RL Mol. Cancer Ther. 9:2934-2942(2010).
RN [15]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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: Modulates cytoplasmic dynein binding to an organelle,
CC and 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
CC with dynein. Interacts with BICD2 and CEP135 (By similarity).
CC Interacts with DYNAP, ECM29 and MAPRE1.
CC -!- INTERACTION:
CC Q9NRI5:DISC1; NbExp=3; IntAct=EBI-715074, EBI-529989;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Membrane; Peripheral membrane
CC protein.
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO34395.1; Type=Frameshift; Positions=381;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001248341.1; NM_001261412.1.
DR RefSeq; NP_001248342.1; NM_001261413.1.
DR RefSeq; NP_006391.1; NM_006400.4.
DR UniGene; Hs.289123; -.
DR ProteinModelPortal; Q13561; -.
DR IntAct; Q13561; 23.
DR MINT; MINT-206219; -.
DR STRING; 9606.ENSP00000408910; -.
DR PhosphoSite; Q13561; -.
DR DMDM; 22096346; -.
DR REPRODUCTION-2DPAGE; IPI00220503; -.
DR PaxDb; Q13561; -.
DR PRIDE; Q13561; -.
DR DNASU; 10540; -.
DR Ensembl; ENST00000434715; ENSP00000408910; ENSG00000175203.
DR Ensembl; ENST00000548249; ENSP00000447824; ENSG00000175203.
DR GeneID; 10540; -.
DR KEGG; hsa:10540; -.
DR UCSC; uc009zpv.2; human.
DR CTD; 10540; -.
DR GeneCards; GC12M057924; -.
DR H-InvDB; HIX0010763; -.
DR HGNC; HGNC:2712; DCTN2.
DR HPA; HPA039715; -.
DR HPA; HPA040040; -.
DR MIM; 607376; gene.
DR neXtProt; NX_Q13561; -.
DR PharmGKB; PA27181; -.
DR eggNOG; NOG39555; -.
DR HOVERGEN; HBG051323; -.
DR InParanoid; Q13561; -.
DR KO; K10424; -.
DR OMA; TQQMIAN; -.
DR OrthoDB; EOG7JT6WG; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q13561; -.
DR ChiTaRS; DCTN2; human.
DR GeneWiki; DCTN2; -.
DR GenomeRNAi; 10540; -.
DR NextBio; 39989; -.
DR PMAP-CutDB; Q13561; -.
DR PRO; PR:Q13561; -.
DR ArrayExpress; Q13561; -.
DR Bgee; Q13561; -.
DR CleanEx; HS_DCTN2; -.
DR Genevestigator; Q13561; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; IDA:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
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:0003774; F:motor activity; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007067; P:mitosis; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:Ensembl.
DR InterPro; IPR028133; Dynamitin.
DR PANTHER; PTHR15346:SF0; PTHR15346:SF0; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Dynein; Membrane;
KW Microtubule; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 401 Dynactin subunit 2.
FT /FTId=PRO_0000079821.
FT COILED 99 132 Potential.
FT COILED 214 244 Potential.
FT COILED 379 399 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 6 6 Phosphotyrosine.
FT MOD_RES 83 83 Phosphoserine.
FT MOD_RES 86 86 Phosphotyrosine (By similarity).
FT VAR_SEQ 35 35 A -> AFAQEL (in isoform 2).
FT /FTId=VSP_040485.
FT VAR_SEQ 35 35 A -> AEL (in isoform 3).
FT /FTId=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
//
ID DCTN2_HUMAN Reviewed; 401 AA.
AC Q13561; B2RBK5; Q86YN2; Q9BW17;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 4.
DT 22-JAN-2014, entry version 135.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT organization 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.,
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 [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.,
RA Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
RA Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
RA Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
RA Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
RA Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
RA Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
RA Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
RA Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
RA Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
RA Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
RA Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
RA 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.,
RA Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
RA Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
RA Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
RA Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
RA Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
RA Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
RA Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
RA Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
RA Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
RA Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
RA Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
RA Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
RA 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.,
RA Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
RA Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
RA Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
RA Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
RA Kucherlapati R., Weinstock G., 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
RT project: 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
RT 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.,
RA Thomas G.R., Vandekerckhove J.;
RT "Exploring proteomes and analyzing protein processing by mass
RT spectrometric 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,
RP ACETYLATION AT ALA-2, AND 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
RP 366-395, AND 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
RT dynactin complex and cytoplasmic dynein intermediate chain.";
RL Curr. Biol. 9:425-428(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-6, AND MASS
RP SPECTROMETRY.
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
RT from human T cells using immobilized metal affinity chromatography and
RT tandem mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [11]
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 [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-83, AND MASS
RP SPECTROMETRY.
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 [13]
RP INTERACTION WITH ECM29.
RX PubMed=20682791; DOI=10.1074/jbc.M110.154120;
RA Gorbea C., Pratt G., Ustrell V., Bell R., Sahasrabudhe S.,
RA Hughes R.E., 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 [14]
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.,
RA Sasaki R., Mizukami T.;
RT "A novel human dynactin-associated protein, dynAP, promotes activation
RT of Akt, and ergosterol-related compounds induce dynAP-dependent
RT apoptosis of human cancer cells.";
RL Mol. Cancer Ther. 9:2934-2942(2010).
RN [15]
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [16]
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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
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: Modulates cytoplasmic dynein binding to an organelle,
CC and 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
CC with dynein. Interacts with BICD2 and CEP135 (By similarity).
CC Interacts with DYNAP, ECM29 and MAPRE1.
CC -!- INTERACTION:
CC Q9NRI5:DISC1; NbExp=3; IntAct=EBI-715074, EBI-529989;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Membrane; Peripheral membrane
CC protein.
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.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO34395.1; Type=Frameshift; Positions=381;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_001248341.1; NM_001261412.1.
DR RefSeq; NP_001248342.1; NM_001261413.1.
DR RefSeq; NP_006391.1; NM_006400.4.
DR UniGene; Hs.289123; -.
DR ProteinModelPortal; Q13561; -.
DR IntAct; Q13561; 23.
DR MINT; MINT-206219; -.
DR STRING; 9606.ENSP00000408910; -.
DR PhosphoSite; Q13561; -.
DR DMDM; 22096346; -.
DR REPRODUCTION-2DPAGE; IPI00220503; -.
DR PaxDb; Q13561; -.
DR PRIDE; Q13561; -.
DR DNASU; 10540; -.
DR Ensembl; ENST00000434715; ENSP00000408910; ENSG00000175203.
DR Ensembl; ENST00000548249; ENSP00000447824; ENSG00000175203.
DR GeneID; 10540; -.
DR KEGG; hsa:10540; -.
DR UCSC; uc009zpv.2; human.
DR CTD; 10540; -.
DR GeneCards; GC12M057924; -.
DR H-InvDB; HIX0010763; -.
DR HGNC; HGNC:2712; DCTN2.
DR HPA; HPA039715; -.
DR HPA; HPA040040; -.
DR MIM; 607376; gene.
DR neXtProt; NX_Q13561; -.
DR PharmGKB; PA27181; -.
DR eggNOG; NOG39555; -.
DR HOVERGEN; HBG051323; -.
DR InParanoid; Q13561; -.
DR KO; K10424; -.
DR OMA; TQQMIAN; -.
DR OrthoDB; EOG7JT6WG; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; Q13561; -.
DR ChiTaRS; DCTN2; human.
DR GeneWiki; DCTN2; -.
DR GenomeRNAi; 10540; -.
DR NextBio; 39989; -.
DR PMAP-CutDB; Q13561; -.
DR PRO; PR:Q13561; -.
DR ArrayExpress; Q13561; -.
DR Bgee; Q13561; -.
DR CleanEx; HS_DCTN2; -.
DR Genevestigator; Q13561; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; IDA:UniProtKB.
DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW.
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:0003774; F:motor activity; IEA:UniProtKB-KW.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR GO; GO:0008283; P:cell proliferation; IMP:UniProtKB.
DR GO; GO:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0007067; P:mitosis; IMP:UniProtKB.
DR GO; GO:0007052; P:mitotic spindle organization; IEA:Ensembl.
DR InterPro; IPR028133; Dynamitin.
DR PANTHER; PTHR15346:SF0; PTHR15346:SF0; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Coiled coil; Complete proteome;
KW Cytoplasm; Cytoskeleton; Direct protein sequencing; Dynein; Membrane;
KW Microtubule; Phosphoprotein; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 401 Dynactin subunit 2.
FT /FTId=PRO_0000079821.
FT COILED 99 132 Potential.
FT COILED 214 244 Potential.
FT COILED 379 399 Potential.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 6 6 Phosphotyrosine.
FT MOD_RES 83 83 Phosphoserine.
FT MOD_RES 86 86 Phosphotyrosine (By similarity).
FT VAR_SEQ 35 35 A -> AFAQEL (in isoform 2).
FT /FTId=VSP_040485.
FT VAR_SEQ 35 35 A -> AEL (in isoform 3).
FT /FTId=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
//
MIM
607376
*RECORD*
*FIELD* NO
607376
*FIELD* TI
*607376 DYNACTIN 2; DCTN2
;;DYNAMITIN;;
DYNACTIN COMPLEX, 50-KD SUBUNIT; DCTN50
*FIELD* TX
read more
DESCRIPTION
DCTN2 is a 50-kD subunit of dynactin, a multiprotein complex associated
with dynein. Cytoplasmic dynein is a molecular motor responsible for
minus-end-directed movement along microtubules. See DCTN1 (601143) and
DNCH1 (600112) for additional information about the dynactin complex and
dynein.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DCTN2
gene to chromosome 12 (TMAP RH70660).
ANIMAL MODEL
LaMonte et al. (2002) generated a mouse model of amyotrophic lateral
sclerosis (ALS; 105400) by overexpressing dynamitin in postnatal motor
neurons of transgenic mice. They found that dynamitin overexpression
disrupted the dynein-dynactin complex, resulting in an inhibition of
retrograde axonal transport. The authors observed a late-onset, slowly
progressive motor neuron degenerative disease in the transgenic mice and
concluded that their mouse model confirms the critical role of disrupted
axonal transport in the pathogenesis of motor neuron degenerative
disease.
*FIELD* RF
1. LaMonte, B. H.; Wallace, K. E.; Holloway, B. A.; Shelly, S. S.;
Ascano, J.; Tokito, M.; Van Winkle, T.; Howland, D. S.; Holzbaur,
E. L. F.: Disruption of dynein/dynactin inhibits axonal transport
in motor neurons causing late-onset progressive degeneration. Neuron 34:
715-727, 2002.
*FIELD* CD
Dawn Watkins-Chow: 11/22/2002
*FIELD* ED
mgross: 11/22/2002
*RECORD*
*FIELD* NO
607376
*FIELD* TI
*607376 DYNACTIN 2; DCTN2
;;DYNAMITIN;;
DYNACTIN COMPLEX, 50-KD SUBUNIT; DCTN50
*FIELD* TX
read more
DESCRIPTION
DCTN2 is a 50-kD subunit of dynactin, a multiprotein complex associated
with dynein. Cytoplasmic dynein is a molecular motor responsible for
minus-end-directed movement along microtubules. See DCTN1 (601143) and
DNCH1 (600112) for additional information about the dynactin complex and
dynein.
MAPPING
The International Radiation Hybrid Mapping Consortium mapped the DCTN2
gene to chromosome 12 (TMAP RH70660).
ANIMAL MODEL
LaMonte et al. (2002) generated a mouse model of amyotrophic lateral
sclerosis (ALS; 105400) by overexpressing dynamitin in postnatal motor
neurons of transgenic mice. They found that dynamitin overexpression
disrupted the dynein-dynactin complex, resulting in an inhibition of
retrograde axonal transport. The authors observed a late-onset, slowly
progressive motor neuron degenerative disease in the transgenic mice and
concluded that their mouse model confirms the critical role of disrupted
axonal transport in the pathogenesis of motor neuron degenerative
disease.
*FIELD* RF
1. LaMonte, B. H.; Wallace, K. E.; Holloway, B. A.; Shelly, S. S.;
Ascano, J.; Tokito, M.; Van Winkle, T.; Howland, D. S.; Holzbaur,
E. L. F.: Disruption of dynein/dynactin inhibits axonal transport
in motor neurons causing late-onset progressive degeneration. Neuron 34:
715-727, 2002.
*FIELD* CD
Dawn Watkins-Chow: 11/22/2002
*FIELD* ED
mgross: 11/22/2002