Full text data of ACTR1A
ACTR1A
(CTRN1)
[Confidence: low (only semi-automatic identification from reviews)]
Alpha-centractin; Centractin (ARP1; Actin-RPV; Centrosome-associated actin homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Alpha-centractin; Centractin (ARP1; Actin-RPV; Centrosome-associated actin homolog)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P61163
ID ACTZ_HUMAN Reviewed; 376 AA.
AC P61163; B2R6B0; P42024;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Alpha-centractin;
DE Short=Centractin;
DE AltName: Full=ARP1;
DE AltName: Full=Actin-RPV;
DE AltName: Full=Centrosome-associated actin homolog;
GN Name=ACTR1A; Synonyms=CTRN1;
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].
RX PubMed=7696711; DOI=10.1091/mbc.5.12.1301;
RA Clark S.W., Staub O., Holzbaur E.L.F., Paschal B.M., Vallee R.B.,
RA Meyer D.I., Clark I.B.;
RT "Beta-centractin: characterization and distribution of a new member of
RT the centractin family of actin-related proteins.";
RL Mol. Biol. Cell 5:1301-1310(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=1528266; DOI=10.1038/359244a0;
RA Lees-Miller J.P., Helfman D.M., Schroer T.A.;
RT "A vertebrate actin-related protein is a component of a multisubunit
RT complex involved in microtubule-based vesicle motility.";
RL Nature 359:244-246(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Muscle;
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 [7]
RP PROTEIN SEQUENCE OF 1-22; 239-255 AND 330-336, AND MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Glen H., Frame M.C.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 97-118; 201-215 AND 239-255, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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).
CC -!- FUNCTION: Component of a multi-subunit complex involved in
CC microtubule based vesicle motility. It is associated with the
CC centrosome.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome.
CC -!- SIMILARITY: Belongs to the actin family. ARP1 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; X82206; CAA57690.1; -; mRNA.
DR EMBL; Z14978; CAA78701.1; -; mRNA.
DR EMBL; AK312506; BAG35407.1; -; mRNA.
DR EMBL; AL121928; CAC08404.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49685.1; -; Genomic_DNA.
DR EMBL; BC000693; AAH00693.1; -; mRNA.
DR EMBL; BC026016; AAH26016.1; -; mRNA.
DR PIR; S29089; S29089.
DR RefSeq; NP_005727.1; NM_005736.3.
DR UniGene; Hs.153961; -.
DR ProteinModelPortal; P61163; -.
DR SMR; P61163; 10-374.
DR IntAct; P61163; 9.
DR MINT; MINT-5001146; -.
DR STRING; 9606.ENSP00000358921; -.
DR PhosphoSite; P61163; -.
DR DMDM; 47117651; -.
DR OGP; P42024; -.
DR REPRODUCTION-2DPAGE; IPI00029468; -.
DR UCD-2DPAGE; P61163; -.
DR PaxDb; P61163; -.
DR PeptideAtlas; P61163; -.
DR PRIDE; P61163; -.
DR DNASU; 10121; -.
DR Ensembl; ENST00000369905; ENSP00000358921; ENSG00000138107.
DR GeneID; 10121; -.
DR KEGG; hsa:10121; -.
DR UCSC; uc001kvv.3; human.
DR CTD; 10121; -.
DR GeneCards; GC10M104228; -.
DR HGNC; HGNC:167; ACTR1A.
DR HPA; CAB037193; -.
DR MIM; 605143; gene.
DR neXtProt; NX_P61163; -.
DR PharmGKB; PA24486; -.
DR eggNOG; COG5277; -.
DR HOGENOM; HOG000233340; -.
DR HOVERGEN; HBG003771; -.
DR InParanoid; P61163; -.
DR KO; K16575; -.
DR OMA; DMERIWS; -.
DR OrthoDB; EOG72G17C; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P61163; -.
DR ChiTaRS; ACTR1A; human.
DR GeneWiki; ACTR1A; -.
DR GenomeRNAi; 10121; -.
DR NextBio; 38283; -.
DR PRO; PR:P61163; -.
DR ArrayExpress; P61163; -.
DR Bgee; P61163; -.
DR CleanEx; HS_ACTR1A; -.
DR Genevestigator; P61163; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; 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:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR InterPro; IPR004000; Actin-related.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nucleotide-binding; Reference proteome.
FT CHAIN 1 376 Alpha-centractin.
FT /FTId=PRO_0000089058.
FT MOD_RES 1 1 N-acetylmethionine.
SQ SEQUENCE 376 AA; 42614 MW; 4A978E7AB3739436 CRC64;
MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP
KAEEHRGLLS IRYPMEHGIV KDWNDMERIW QYVYSKDQLQ TFSEEHPVLL TEAPLNPRKN
RERAAEVFFE TFNVPALFIS MQAVLSLYAT GRTTGVVLDS GDGVTHAVPI YEGFAMPHSI
MRIDIAGRDV SRFLRLYLRK EGYDFHSSSE FEIVKAIKER ACYLSINPQK DETLETEKAQ
YYLPDGSTIE IGPSRFRAPE LLFRPDLIGE ESEGIHEVLV FAIQKSDMDL RRTLFSNIVL
SGGSTLFKGF GDRLLSEVKK LAPKDVKIRI SAPQERLYST WIGGSILASL DTFKKMWVSK
KEYEEDGARS IHRKTF
//
ID ACTZ_HUMAN Reviewed; 376 AA.
AC P61163; B2R6B0; P42024;
DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
read moreDT 10-MAY-2004, sequence version 1.
DT 22-JAN-2014, entry version 104.
DE RecName: Full=Alpha-centractin;
DE Short=Centractin;
DE AltName: Full=ARP1;
DE AltName: Full=Actin-RPV;
DE AltName: Full=Centrosome-associated actin homolog;
GN Name=ACTR1A; Synonyms=CTRN1;
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].
RX PubMed=7696711; DOI=10.1091/mbc.5.12.1301;
RA Clark S.W., Staub O., Holzbaur E.L.F., Paschal B.M., Vallee R.B.,
RA Meyer D.I., Clark I.B.;
RT "Beta-centractin: characterization and distribution of a new member of
RT the centractin family of actin-related proteins.";
RL Mol. Biol. Cell 5:1301-1310(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
RX PubMed=1528266; DOI=10.1038/359244a0;
RA Lees-Miller J.P., Helfman D.M., Schroer T.A.;
RT "A vertebrate actin-related protein is a component of a multisubunit
RT complex involved in microtubule-based vesicle motility.";
RL Nature 359:244-246(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thalamus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney, and Muscle;
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 [7]
RP PROTEIN SEQUENCE OF 1-22; 239-255 AND 330-336, AND MASS SPECTROMETRY.
RC TISSUE=Osteosarcoma;
RA Bienvenut W.V., Glen H., Frame M.C.;
RL Submitted (MAR-2008) to UniProtKB.
RN [8]
RP PROTEIN SEQUENCE OF 97-118; 201-215 AND 239-255, AND MASS
RP SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Vishwanath V.;
RL Submitted (MAR-2007) to UniProtKB.
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
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).
CC -!- FUNCTION: Component of a multi-subunit complex involved in
CC microtubule based vesicle motility. It is associated with the
CC centrosome.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm,
CC cytoskeleton, microtubule organizing center, centrosome.
CC -!- SIMILARITY: Belongs to the actin family. ARP1 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; X82206; CAA57690.1; -; mRNA.
DR EMBL; Z14978; CAA78701.1; -; mRNA.
DR EMBL; AK312506; BAG35407.1; -; mRNA.
DR EMBL; AL121928; CAC08404.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49685.1; -; Genomic_DNA.
DR EMBL; BC000693; AAH00693.1; -; mRNA.
DR EMBL; BC026016; AAH26016.1; -; mRNA.
DR PIR; S29089; S29089.
DR RefSeq; NP_005727.1; NM_005736.3.
DR UniGene; Hs.153961; -.
DR ProteinModelPortal; P61163; -.
DR SMR; P61163; 10-374.
DR IntAct; P61163; 9.
DR MINT; MINT-5001146; -.
DR STRING; 9606.ENSP00000358921; -.
DR PhosphoSite; P61163; -.
DR DMDM; 47117651; -.
DR OGP; P42024; -.
DR REPRODUCTION-2DPAGE; IPI00029468; -.
DR UCD-2DPAGE; P61163; -.
DR PaxDb; P61163; -.
DR PeptideAtlas; P61163; -.
DR PRIDE; P61163; -.
DR DNASU; 10121; -.
DR Ensembl; ENST00000369905; ENSP00000358921; ENSG00000138107.
DR GeneID; 10121; -.
DR KEGG; hsa:10121; -.
DR UCSC; uc001kvv.3; human.
DR CTD; 10121; -.
DR GeneCards; GC10M104228; -.
DR HGNC; HGNC:167; ACTR1A.
DR HPA; CAB037193; -.
DR MIM; 605143; gene.
DR neXtProt; NX_P61163; -.
DR PharmGKB; PA24486; -.
DR eggNOG; COG5277; -.
DR HOGENOM; HOG000233340; -.
DR HOVERGEN; HBG003771; -.
DR InParanoid; P61163; -.
DR KO; K16575; -.
DR OMA; DMERIWS; -.
DR OrthoDB; EOG72G17C; -.
DR Reactome; REACT_115566; Cell Cycle.
DR Reactome; REACT_6900; Immune System.
DR SignaLink; P61163; -.
DR ChiTaRS; ACTR1A; human.
DR GeneWiki; ACTR1A; -.
DR GenomeRNAi; 10121; -.
DR NextBio; 38283; -.
DR PRO; PR:P61163; -.
DR ArrayExpress; P61163; -.
DR Bgee; P61163; -.
DR CleanEx; HS_ACTR1A; -.
DR Genevestigator; P61163; -.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; TAS:ProtInc.
DR GO; GO:0005524; F:ATP binding; 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:0000086; P:G2/M transition of mitotic cell cycle; TAS:Reactome.
DR GO; GO:0016192; P:vesicle-mediated transport; TAS:ProtInc.
DR InterPro; IPR004000; Actin-related.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Complete proteome; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nucleotide-binding; Reference proteome.
FT CHAIN 1 376 Alpha-centractin.
FT /FTId=PRO_0000089058.
FT MOD_RES 1 1 N-acetylmethionine.
SQ SEQUENCE 376 AA; 42614 MW; 4A978E7AB3739436 CRC64;
MESYDVIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHVRVMAG ALEGDIFIGP
KAEEHRGLLS IRYPMEHGIV KDWNDMERIW QYVYSKDQLQ TFSEEHPVLL TEAPLNPRKN
RERAAEVFFE TFNVPALFIS MQAVLSLYAT GRTTGVVLDS GDGVTHAVPI YEGFAMPHSI
MRIDIAGRDV SRFLRLYLRK EGYDFHSSSE FEIVKAIKER ACYLSINPQK DETLETEKAQ
YYLPDGSTIE IGPSRFRAPE LLFRPDLIGE ESEGIHEVLV FAIQKSDMDL RRTLFSNIVL
SGGSTLFKGF GDRLLSEVKK LAPKDVKIRI SAPQERLYST WIGGSILASL DTFKKMWVSK
KEYEEDGARS IHRKTF
//
MIM
605143
*RECORD*
*FIELD* NO
605143
*FIELD* TI
*605143 ACTIN-RELATED PROTEIN 1A; ACTR1A
;;ARP1;;
CENTRACTIN, ALPHA
*FIELD* TX
DESCRIPTION
read more
ACTR1A is an essential subunit of the 20S dynactin complex, which is
involved in microtubule-dependent vesicular transport, spindle assembly,
and cell division. Polymers of 8 to 13 ACTR1 molecules make up the
central 37-nm filament that forms the base of the dynactin complex
(summary by Karki et al., 2000).
CLONING
By randomly sequencing a brain cDNA library, Adams et al. (1991)
identified a cDNA (EST00370) encoding a 37-amino acid peptide with 76%
similarity to actin.
Using oligonucleotide probes derived from clone EST00370 to screen a
teratocarcinoma library, Lees-Miller et al. (1992) obtained a cDNA
encoding ACTR1A, which they called actin-RPV (vertebrate actin-related
protein). Sequence analysis predicted that the 376-amino acid ACTR1A
protein shares only 69% amino acid similarity with vertebrate actins;
most of the nonconservative substitutions occur in the surface loops of
ACTR1A rather than the core structure. Two-dimensional immunoblot
analysis of the dynactin complex, an activator of dynein-driven vesicle
movement (see 601143), determined that ACTR1A is the most abundant
molecule in the complex and is expressed as a 45-kD protein with a pI of
6.8.
By screening a testis cDNA library with a canine alpha-centractin probe,
Clark et al. (1994) isolated cDNAs encoding ACTR1A, which they called
alpha-centractin. Northern blot analysis detected variable levels of a
3.0-kb ACTR1A transcript in all tissues tested. The same probe also
detected a 1.3-kb transcript representing a putative truncated isoform,
which the authors called centractin-gamma. Two-dimensional immunoblot
analysis determined that ACTR1A is expressed in the cytosol as part of
the dynactin complex as a 43-kD protein with a pI of 6.6; levels of
ACTR1A were at least 15-fold greater than those of ACTR1B (605144).
GENE FUNCTION
Eaton et al. (2002) disrupted the dynactin complex in Drosophila, using
3 separate perturbations: dsRNA interference with arp1, mutation in
p150/Glued (homolog of DCTN1; 601143), and a dominant-negative Glued
transgene. In all 3 cases, the disruption resulted in an increase in the
frequency and extent of synaptic retraction events at the neuromuscular
junction. Eaton et al. (2002) concluded that dynactin functions locally
within the presynaptic arbor to promote synapse stability at the
neuromuscular junction.
Karki et al. (2000) noted that one end of the ARP1 filament is likely
capped by the alpha (see 601580) and beta (CAPZB; 601572) subunits of
capping protein. They found that the other end of ARP1 was bound by p62
dynactin (DCTN4; 614758).
MAPPING
Gross (2012) mapped the ACTR1A gene to chromosome 10q24.32 based on an
alignment of the ACTR1A sequence (GenBank GENBANK AK302072) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Adams, M. D.; Kelley, J. M.; Gocayne, J. D.; Dubnick, M.; Polymeropoulos,
M. H.; Xiao, H.; Merril, C. R.; Wu, A.; Olde, B.; Moreno, R. F.; Kerlavage,
A. R.; McCombie, W. R.; Venter, J. C.: Complementary DNA sequencing:
expressed sequence tags and human genome project. Science 252: 1651-1656,
1991.
2. Clark, S. W.; Staub, O.; Clark, I. B.; Holzbaur, E. L. F.; Paschal,
B. M.; Vallee, R. B.; Meyer, D. I.: Beta-centractin: characterization
and distribution of a new member of the centractin family of actin-related
proteins. Molec. Biol. Cell 5: 1301-1310, 1994.
3. Eaton, B. A.; Fetter, R. D.; Davis, G. W.: Dynactin is necessary
for synapse stabilization. Neuron 34: 729-741, 2002.
4. Gross, M. B.: Personal Communication. Baltimore, Md. 8/10/2012.
5. Karki, S.; Tokito, M. K.; Holzbaur, E. L. F.: A dynactin subunit
with a highly conserved cysteine-rich motif interacts directly with
Arp1. J. Biol. Chem. 275: 4834-4839, 2000.
6. Lees-Miller, J. P.; Helfman, D. M.; Schroer, T. A.: A vertebrate
actin-related protein is a component of a multisubunit complex involved
in microtubule-based vesicle motility. Nature 359: 244-246, 1992.
*FIELD* CN
Matthew B. Gross - updated: 08/10/2012
Patricia A. Hartz - updated: 8/9/2012
Dawn Watkins-Chow - updated: 11/27/2002
*FIELD* CD
Paul J. Converse: 7/13/2000
*FIELD* ED
mgross: 08/10/2012
terry: 8/9/2012
carol: 12/6/2002
tkritzer: 11/27/2002
mgross: 7/13/2000
*RECORD*
*FIELD* NO
605143
*FIELD* TI
*605143 ACTIN-RELATED PROTEIN 1A; ACTR1A
;;ARP1;;
CENTRACTIN, ALPHA
*FIELD* TX
DESCRIPTION
read more
ACTR1A is an essential subunit of the 20S dynactin complex, which is
involved in microtubule-dependent vesicular transport, spindle assembly,
and cell division. Polymers of 8 to 13 ACTR1 molecules make up the
central 37-nm filament that forms the base of the dynactin complex
(summary by Karki et al., 2000).
CLONING
By randomly sequencing a brain cDNA library, Adams et al. (1991)
identified a cDNA (EST00370) encoding a 37-amino acid peptide with 76%
similarity to actin.
Using oligonucleotide probes derived from clone EST00370 to screen a
teratocarcinoma library, Lees-Miller et al. (1992) obtained a cDNA
encoding ACTR1A, which they called actin-RPV (vertebrate actin-related
protein). Sequence analysis predicted that the 376-amino acid ACTR1A
protein shares only 69% amino acid similarity with vertebrate actins;
most of the nonconservative substitutions occur in the surface loops of
ACTR1A rather than the core structure. Two-dimensional immunoblot
analysis of the dynactin complex, an activator of dynein-driven vesicle
movement (see 601143), determined that ACTR1A is the most abundant
molecule in the complex and is expressed as a 45-kD protein with a pI of
6.8.
By screening a testis cDNA library with a canine alpha-centractin probe,
Clark et al. (1994) isolated cDNAs encoding ACTR1A, which they called
alpha-centractin. Northern blot analysis detected variable levels of a
3.0-kb ACTR1A transcript in all tissues tested. The same probe also
detected a 1.3-kb transcript representing a putative truncated isoform,
which the authors called centractin-gamma. Two-dimensional immunoblot
analysis determined that ACTR1A is expressed in the cytosol as part of
the dynactin complex as a 43-kD protein with a pI of 6.6; levels of
ACTR1A were at least 15-fold greater than those of ACTR1B (605144).
GENE FUNCTION
Eaton et al. (2002) disrupted the dynactin complex in Drosophila, using
3 separate perturbations: dsRNA interference with arp1, mutation in
p150/Glued (homolog of DCTN1; 601143), and a dominant-negative Glued
transgene. In all 3 cases, the disruption resulted in an increase in the
frequency and extent of synaptic retraction events at the neuromuscular
junction. Eaton et al. (2002) concluded that dynactin functions locally
within the presynaptic arbor to promote synapse stability at the
neuromuscular junction.
Karki et al. (2000) noted that one end of the ARP1 filament is likely
capped by the alpha (see 601580) and beta (CAPZB; 601572) subunits of
capping protein. They found that the other end of ARP1 was bound by p62
dynactin (DCTN4; 614758).
MAPPING
Gross (2012) mapped the ACTR1A gene to chromosome 10q24.32 based on an
alignment of the ACTR1A sequence (GenBank GENBANK AK302072) with the
genomic sequence (GRCh37).
*FIELD* RF
1. Adams, M. D.; Kelley, J. M.; Gocayne, J. D.; Dubnick, M.; Polymeropoulos,
M. H.; Xiao, H.; Merril, C. R.; Wu, A.; Olde, B.; Moreno, R. F.; Kerlavage,
A. R.; McCombie, W. R.; Venter, J. C.: Complementary DNA sequencing:
expressed sequence tags and human genome project. Science 252: 1651-1656,
1991.
2. Clark, S. W.; Staub, O.; Clark, I. B.; Holzbaur, E. L. F.; Paschal,
B. M.; Vallee, R. B.; Meyer, D. I.: Beta-centractin: characterization
and distribution of a new member of the centractin family of actin-related
proteins. Molec. Biol. Cell 5: 1301-1310, 1994.
3. Eaton, B. A.; Fetter, R. D.; Davis, G. W.: Dynactin is necessary
for synapse stabilization. Neuron 34: 729-741, 2002.
4. Gross, M. B.: Personal Communication. Baltimore, Md. 8/10/2012.
5. Karki, S.; Tokito, M. K.; Holzbaur, E. L. F.: A dynactin subunit
with a highly conserved cysteine-rich motif interacts directly with
Arp1. J. Biol. Chem. 275: 4834-4839, 2000.
6. Lees-Miller, J. P.; Helfman, D. M.; Schroer, T. A.: A vertebrate
actin-related protein is a component of a multisubunit complex involved
in microtubule-based vesicle motility. Nature 359: 244-246, 1992.
*FIELD* CN
Matthew B. Gross - updated: 08/10/2012
Patricia A. Hartz - updated: 8/9/2012
Dawn Watkins-Chow - updated: 11/27/2002
*FIELD* CD
Paul J. Converse: 7/13/2000
*FIELD* ED
mgross: 08/10/2012
terry: 8/9/2012
carol: 12/6/2002
tkritzer: 11/27/2002
mgross: 7/13/2000