Full text data of DCTN5
DCTN5
[Confidence: low (only semi-automatic identification from reviews)]
Dynactin subunit 5 (Dynactin subunit p25)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Dynactin subunit 5 (Dynactin subunit p25)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9BTE1
ID DCTN5_HUMAN Reviewed; 182 AA.
AC Q9BTE1; A8K9X8; H3BN51; H3BQA4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Dynactin subunit 5;
DE AltName: Full=Dynactin subunit p25;
GN Name=DCTN5;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland, and Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Trophoblast;
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 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
RN [7]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23455152; DOI=10.1038/emboj.2013.30;
RA Yeh T.Y., Kowalska A.K., Scipioni B.R., Cheong F.K., Zheng M.,
RA Derewenda U., Derewenda Z.S., Schroer T.A.;
RT "Dynactin helps target Polo-like kinase 1 to kinetochores via its
RT left-handed beta-helical p27 subunit.";
RL EMBO J. 32:1023-1035(2013).
CC -!- SUBUNIT: Member of the pointed-end complex of the dynactin
CC shoulder complex which contains DCTN4, DCTN5 and DCTN6 subunits
CC and ACTR10. Within the complex DCTN6 forms a heterodimer with
CC DCTN5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Chromosome, centromere, kinetochore.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BTE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTE1-2; Sequence=VSP_046023;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9BTE1-3; Sequence=VSP_046697;
CC -!- SIMILARITY: Belongs to the dynactin subunits 5/6 family. Dynactin
CC subunit 5 subfamily.
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; AK027387; BAB55077.1; -; mRNA.
DR EMBL; AK292843; BAF85532.1; -; mRNA.
DR EMBL; AC008870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471145; EAW55809.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55810.1; -; Genomic_DNA.
DR EMBL; BC004191; AAH04191.1; -; mRNA.
DR EMBL; CD388246; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001185940.1; NM_001199011.1.
DR RefSeq; NP_001186672.1; NM_001199743.1.
DR RefSeq; NP_115875.1; NM_032486.3.
DR UniGene; Hs.435941; -.
DR ProteinModelPortal; Q9BTE1; -.
DR SMR; Q9BTE1; 22-159.
DR IntAct; Q9BTE1; 6.
DR MINT; MINT-1474973; -.
DR STRING; 9606.ENSP00000300087; -.
DR PhosphoSite; Q9BTE1; -.
DR DMDM; 62900103; -.
DR PaxDb; Q9BTE1; -.
DR PRIDE; Q9BTE1; -.
DR Ensembl; ENST00000300087; ENSP00000300087; ENSG00000166847.
DR Ensembl; ENST00000563998; ENSP00000454691; ENSG00000166847.
DR Ensembl; ENST00000568272; ENSP00000455685; ENSG00000166847.
DR GeneID; 84516; -.
DR KEGG; hsa:84516; -.
DR UCSC; uc021tfj.1; human.
DR CTD; 84516; -.
DR GeneCards; GC16P023652; -.
DR H-InvDB; HIX0134374; -.
DR HGNC; HGNC:24594; DCTN5.
DR HPA; HPA042003; -.
DR MIM; 612962; gene.
DR neXtProt; NX_Q9BTE1; -.
DR PharmGKB; PA142672007; -.
DR eggNOG; NOG282896; -.
DR HOGENOM; HOG000198229; -.
DR HOVERGEN; HBG051325; -.
DR InParanoid; Q9BTE1; -.
DR KO; K10427; -.
DR OMA; PPYKTYR; -.
DR OrthoDB; EOG751NGQ; -.
DR PhylomeDB; Q9BTE1; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; DCTN5; human.
DR GeneWiki; DCTN5; -.
DR GenomeRNAi; 84516; -.
DR NextBio; 74322; -.
DR PRO; PR:Q9BTE1; -.
DR ArrayExpress; Q9BTE1; -.
DR Bgee; Q9BTE1; -.
DR CleanEx; HS_DCTN5; -.
DR Genevestigator; Q9BTE1; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR InterPro; IPR001451; Hexapep_transf.
DR InterPro; IPR011004; Trimer_LpxA-like.
DR Pfam; PF00132; Hexapep; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Centromere; Chromosome;
KW Complete proteome; Cytoplasm; Cytoskeleton; Kinetochore;
KW Reference proteome.
FT CHAIN 1 182 Dynactin subunit 5.
FT /FTId=PRO_0000079827.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 40 182 TIVMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGV
FT AFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCV
FT LKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQ
FT ELMIDVTKSYYQKFLPLTQV -> NFVISVFLSPYIRCHSA
FT CRDRKRSDESVRLSVNNREWWGLVNWRM (in isoform
FT 3).
FT /FTId=VSP_046697.
FT VAR_SEQ 151 182 GLFSGELPECTQELMIDVTKSYYQKFLPLTQV -> AP
FT (in isoform 2).
FT /FTId=VSP_046023.
SQ SEQUENCE 182 AA; 20127 MW; 476DBD27A6CA1C35 CRC64;
MELGELLYNK SEYIETASGN KVSRQSVLCG SQNIVLNGKT IVMNDCIIRG DLANVRVGRH
CVVKSRSVIR PPFKKFSKGV AFFPLHIGDH VFIEEDCVVN AAQIGSYVHV GKNCVIGRRC
VLKDCCKILD NTVLPPETVV PPFTVFSGCP GLFSGELPEC TQELMIDVTK SYYQKFLPLT
QV
//
ID DCTN5_HUMAN Reviewed; 182 AA.
AC Q9BTE1; A8K9X8; H3BN51; H3BQA4;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 95.
DE RecName: Full=Dynactin subunit 5;
DE AltName: Full=Dynactin subunit p25;
GN Name=DCTN5;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland, and Trachea;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X.,
RA Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A.,
RA Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.,
RA Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L.,
RA Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A.,
RA Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D.,
RA Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J.,
RA Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I.,
RA Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W.,
RA Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A.,
RA Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S.,
RA Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L.,
RA Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A.,
RA Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L.,
RA Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N.,
RA Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M.,
RA Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L.,
RA Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D.,
RA Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P.,
RA Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M.,
RA Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Kidney, and Trophoblast;
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 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 [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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).
RN [7]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=23455152; DOI=10.1038/emboj.2013.30;
RA Yeh T.Y., Kowalska A.K., Scipioni B.R., Cheong F.K., Zheng M.,
RA Derewenda U., Derewenda Z.S., Schroer T.A.;
RT "Dynactin helps target Polo-like kinase 1 to kinetochores via its
RT left-handed beta-helical p27 subunit.";
RL EMBO J. 32:1023-1035(2013).
CC -!- SUBUNIT: Member of the pointed-end complex of the dynactin
CC shoulder complex which contains DCTN4, DCTN5 and DCTN6 subunits
CC and ACTR10. Within the complex DCTN6 forms a heterodimer with
CC DCTN5.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity).
CC Chromosome, centromere, kinetochore.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9BTE1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BTE1-2; Sequence=VSP_046023;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q9BTE1-3; Sequence=VSP_046697;
CC -!- SIMILARITY: Belongs to the dynactin subunits 5/6 family. Dynactin
CC subunit 5 subfamily.
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; AK027387; BAB55077.1; -; mRNA.
DR EMBL; AK292843; BAF85532.1; -; mRNA.
DR EMBL; AC008870; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471145; EAW55809.1; -; Genomic_DNA.
DR EMBL; CH471145; EAW55810.1; -; Genomic_DNA.
DR EMBL; BC004191; AAH04191.1; -; mRNA.
DR EMBL; CD388246; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_001185940.1; NM_001199011.1.
DR RefSeq; NP_001186672.1; NM_001199743.1.
DR RefSeq; NP_115875.1; NM_032486.3.
DR UniGene; Hs.435941; -.
DR ProteinModelPortal; Q9BTE1; -.
DR SMR; Q9BTE1; 22-159.
DR IntAct; Q9BTE1; 6.
DR MINT; MINT-1474973; -.
DR STRING; 9606.ENSP00000300087; -.
DR PhosphoSite; Q9BTE1; -.
DR DMDM; 62900103; -.
DR PaxDb; Q9BTE1; -.
DR PRIDE; Q9BTE1; -.
DR Ensembl; ENST00000300087; ENSP00000300087; ENSG00000166847.
DR Ensembl; ENST00000563998; ENSP00000454691; ENSG00000166847.
DR Ensembl; ENST00000568272; ENSP00000455685; ENSG00000166847.
DR GeneID; 84516; -.
DR KEGG; hsa:84516; -.
DR UCSC; uc021tfj.1; human.
DR CTD; 84516; -.
DR GeneCards; GC16P023652; -.
DR H-InvDB; HIX0134374; -.
DR HGNC; HGNC:24594; DCTN5.
DR HPA; HPA042003; -.
DR MIM; 612962; gene.
DR neXtProt; NX_Q9BTE1; -.
DR PharmGKB; PA142672007; -.
DR eggNOG; NOG282896; -.
DR HOGENOM; HOG000198229; -.
DR HOVERGEN; HBG051325; -.
DR InParanoid; Q9BTE1; -.
DR KO; K10427; -.
DR OMA; PPYKTYR; -.
DR OrthoDB; EOG751NGQ; -.
DR PhylomeDB; Q9BTE1; -.
DR Reactome; REACT_6900; Immune System.
DR ChiTaRS; DCTN5; human.
DR GeneWiki; DCTN5; -.
DR GenomeRNAi; 84516; -.
DR NextBio; 74322; -.
DR PRO; PR:Q9BTE1; -.
DR ArrayExpress; Q9BTE1; -.
DR Bgee; Q9BTE1; -.
DR CleanEx; HS_DCTN5; -.
DR Genevestigator; Q9BTE1; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0000777; C:condensed chromosome kinetochore; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; TAS:Reactome.
DR InterPro; IPR001451; Hexapep_transf.
DR InterPro; IPR011004; Trimer_LpxA-like.
DR Pfam; PF00132; Hexapep; 1.
DR SUPFAM; SSF51161; SSF51161; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Centromere; Chromosome;
KW Complete proteome; Cytoplasm; Cytoskeleton; Kinetochore;
KW Reference proteome.
FT CHAIN 1 182 Dynactin subunit 5.
FT /FTId=PRO_0000079827.
FT MOD_RES 1 1 N-acetylmethionine.
FT VAR_SEQ 40 182 TIVMNDCIIRGDLANVRVGRHCVVKSRSVIRPPFKKFSKGV
FT AFFPLHIGDHVFIEEDCVVNAAQIGSYVHVGKNCVIGRRCV
FT LKDCCKILDNTVLPPETVVPPFTVFSGCPGLFSGELPECTQ
FT ELMIDVTKSYYQKFLPLTQV -> NFVISVFLSPYIRCHSA
FT CRDRKRSDESVRLSVNNREWWGLVNWRM (in isoform
FT 3).
FT /FTId=VSP_046697.
FT VAR_SEQ 151 182 GLFSGELPECTQELMIDVTKSYYQKFLPLTQV -> AP
FT (in isoform 2).
FT /FTId=VSP_046023.
SQ SEQUENCE 182 AA; 20127 MW; 476DBD27A6CA1C35 CRC64;
MELGELLYNK SEYIETASGN KVSRQSVLCG SQNIVLNGKT IVMNDCIIRG DLANVRVGRH
CVVKSRSVIR PPFKKFSKGV AFFPLHIGDH VFIEEDCVVN AAQIGSYVHV GKNCVIGRRC
VLKDCCKILD NTVLPPETVV PPFTVFSGCP GLFSGELPEC TQELMIDVTK SYYQKFLPLT
QV
//
MIM
612962
*RECORD*
*FIELD* NO
612962
*FIELD* TI
*612962 DYNACTIN 5; DCTN5
;;p25
*FIELD* TX
DESCRIPTION
Dynactin (see 601143) is a multimeric protein essential for
read moreminus-end-directed transport driven by the microtubule-based motor
dynein (see DYNC1H1; 600112). DCTN5 is a subunit of the pointed-end
subcomplex of dynactin that is thought to interact with membranous cargo
(Parisi et al., 2004).
CLONING
Eckley et al. (1999) identified Dctn5, which they called p25, as a
component of the pointed-end dynactin subcomplex in bovine brain. By
database analysis, they identified mouse p25, which encodes a 182-amino
acid protein with a calculated molecular mass of 20.1 kD. Eckley et al.
(1999) also identified p25 orthologs in fly and worm.
By searching databases for proteins containing an isoleucine-patch motif
predicted to adopt a left-handed parallel beta-helix fold, Parisi et al.
(2004) identified mouse p25.
MAPPING
Hartz (2009) mapped the DCTN5 gene to chromosome 16p12.2 based on an
alignment of the DCTN5 sequence (GenBank GENBANK AK027387) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Eckley, D. M.; Gill, S. R.; Melkonian, K. A.; Bingham, J. B.; Goodson,
H. V.; Heuser, J. E.; Schroer, T. A.: Analysis of dynactin subcomplexes
reveals a novel actin-related protein associated with the Arp1 minifilament
pointed end. J. Cell Biol. 147: 307-319, 1999.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/13/2009.
3. Parisi, G.; Fornasari, M. S.; Echave, J.: Dynactins p25 and p27
are predicted to adopt the L-beta-H fold. FEBS Lett. 562: 1-4, 2004.
*FIELD* CD
Patricia A. Hartz: 8/13/2009
*FIELD* ED
mgross: 08/13/2009
*RECORD*
*FIELD* NO
612962
*FIELD* TI
*612962 DYNACTIN 5; DCTN5
;;p25
*FIELD* TX
DESCRIPTION
Dynactin (see 601143) is a multimeric protein essential for
read moreminus-end-directed transport driven by the microtubule-based motor
dynein (see DYNC1H1; 600112). DCTN5 is a subunit of the pointed-end
subcomplex of dynactin that is thought to interact with membranous cargo
(Parisi et al., 2004).
CLONING
Eckley et al. (1999) identified Dctn5, which they called p25, as a
component of the pointed-end dynactin subcomplex in bovine brain. By
database analysis, they identified mouse p25, which encodes a 182-amino
acid protein with a calculated molecular mass of 20.1 kD. Eckley et al.
(1999) also identified p25 orthologs in fly and worm.
By searching databases for proteins containing an isoleucine-patch motif
predicted to adopt a left-handed parallel beta-helix fold, Parisi et al.
(2004) identified mouse p25.
MAPPING
Hartz (2009) mapped the DCTN5 gene to chromosome 16p12.2 based on an
alignment of the DCTN5 sequence (GenBank GENBANK AK027387) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Eckley, D. M.; Gill, S. R.; Melkonian, K. A.; Bingham, J. B.; Goodson,
H. V.; Heuser, J. E.; Schroer, T. A.: Analysis of dynactin subcomplexes
reveals a novel actin-related protein associated with the Arp1 minifilament
pointed end. J. Cell Biol. 147: 307-319, 1999.
2. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/13/2009.
3. Parisi, G.; Fornasari, M. S.; Echave, J.: Dynactins p25 and p27
are predicted to adopt the L-beta-H fold. FEBS Lett. 562: 1-4, 2004.
*FIELD* CD
Patricia A. Hartz: 8/13/2009
*FIELD* ED
mgross: 08/13/2009