ID DCTN2_HUMAN Reviewed; 401 AA. AC Q13561; Q86YN2; Q9BW17; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 07-JUL-2009, entry version 86. DE RecName: Full=Dynactin subunit 2; DE AltName: Full=Dynactin complex 50 kDa subunit; DE Short=DCTN-50; DE AltName: Full=50 kDa dynein-associated polypeptide; 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], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=96178072; 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]. 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 [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-385. 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 [4] RP PROTEIN SEQUENCE OF 2-14. RC TISSUE=Platelet; RX MEDLINE=22608298; 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 [5] 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 [6] 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 [7] 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 [8] RP IDENTIFICATION [LARGE SCALE ANALYSIS], AND MASS SPECTROMETRY. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. CC -!- FUNCTION: Modulates cytoplasmic dynein binding to an organelle, CC and plays a role in prometaphase chromosome alignment and spindle CC organization during mitosis. May play a role in synapse formation CC during brain development. CC -!- SUBUNIT: Subunit of dynactin, a multiprotein complex associated CC with dynein. Interacts with BICD2 (By similarity). Interacts with CC MAPRE1. CC -!- INTERACTION: CC Q9NRI5:DISC1; NbExp=2; IntAct=EBI-715074, EBI-529989; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Membrane; CC Peripheral membrane protein. CC -!- SIMILARITY: Belongs to the dynactin subunit 2 family. 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; BC000718; AAH00718.1; -; mRNA. DR EMBL; BC009468; AAH09468.1; -; mRNA. DR EMBL; BC014083; AAH14083.1; -; mRNA. DR EMBL; AY189155; AAO34395.1; -; mRNA. DR IPI; IPI00220503; -. DR RefSeq; NP_006391.1; -. DR UniGene; Hs.151219; -. DR UniGene; Hs.289123; -. DR IntAct; Q13561; 5. DR PhosphoSite; Q13561; -. DR REPRODUCTION-2DPAGE; IPI00220503; -. DR PRIDE; Q13561; -. DR Ensembl; ENSG00000175203; Homo sapiens. DR GeneID; 10540; -. DR KEGG; hsa:10540; -. DR UCSC; uc001som.1; human. DR GeneCards; GC12M056210; -. DR HGNC; HGNC:2712; DCTN2. DR MIM; 607376; gene. DR PharmGKB; PA27181; -. DR HOVERGEN; Q13561; -. DR Reactome; REACT_152; Cell Cycle, Mitotic. DR NextBio; 39989; -. DR PMAP-CutDB; Q13561; -. DR Bgee; Q13561; -. DR CleanEx; HS_DCTN2; -. DR GermOnline; ENSG00000175203; Homo sapiens. DR GO; GO:0005813; C:centrosome; IDA:UniProtKB. DR GO; GO:0005869; C:dynactin complex; IDA:UniProtKB. DR GO; GO:0030286; C:dynein complex; IEA:UniProtKB-KW. 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:0003774; F:motor activity; IEA:UniProtKB-KW. DR GO; GO:0005515; F:protein binding; IPI:UniProtKB. DR GO; GO:0008283; P:cell proliferation; IMP:UniProtKB. DR GO; GO:0007017; P:microtubule-based process; IEA:InterPro. DR GO; GO:0007067; P:mitosis; IMP:UniProtKB. DR InterPro; IPR006996; Dynamitin. DR Pfam; PF04912; Dynamitin; 1. PE 1: Evidence at protein level; KW Acetylation; Coiled coil; Complete proteome; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Dynein; Membrane; Microtubule; KW Phosphoprotein. 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 83 83 Phosphoserine (By similarity). FT MOD_RES 86 86 Phosphotyrosine (By similarity). FT CONFLICT 35 35 A -> AFAQEL (in Ref. 1; AAC50423). FT CONFLICT 36 36 E -> ELE (in Ref. 3). FT CONFLICT 382 385 LATV -> PGHS (in Ref. 3). 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 //