ACTY_HUMAN
ID ACTY_HUMAN Reviewed; 376 AA.
AC P42025; D3DVH2; Q53SK5; Q9BRB7;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Beta-centractin;
DE AltName: Full=Actin-related protein 1B;
DE Short=ARP1B;
GN Name=ACTR1B; Synonyms=CTRN2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Testis;
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 the
RT centractin family of actin-related proteins.";
RL Mol. Biol. Cell 5:1301-1310(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-93.
RC TISSUE=Lymph, and Placenta;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 239-255, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, and Cajal-Retzius cell;
RA Lubec G., Afjehi-Sadat L.;
RL Submitted (MAR-2007) to UniProtKB.
RN [6]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Component of a multi-subunit complex involved in microtubule
CC based vesicle motility. It is associated with the centrosome.
CC -!- INTERACTION:
CC P42025; Q14203: DCTN1; NbExp=3; IntAct=EBI-367493, EBI-724352;
CC P42025; P42858: HTT; NbExp=3; IntAct=EBI-367493, EBI-466029;
CC P42025; Q9QZB7: Actr10; Xeno; NbExp=2; IntAct=EBI-367493, EBI-367600;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome.
CC -!- SIMILARITY: Belongs to the actin family. ARP1 subfamily. {ECO:0000305}.
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DR EMBL; X82207; CAA57691.1; -; mRNA.
DR EMBL; AC017099; AAY24280.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01924.1; -; Genomic_DNA.
DR EMBL; CH471127; EAX01927.1; -; Genomic_DNA.
DR EMBL; BC004374; AAH04374.1; -; mRNA.
DR EMBL; BC006372; AAH06372.1; -; mRNA.
DR EMBL; BC010090; AAH10090.1; -; mRNA.
DR CCDS; CCDS2033.1; -.
DR RefSeq; NP_005726.1; NM_005735.3.
DR AlphaFoldDB; P42025; -.
DR SMR; P42025; -.
DR BioGRID; 115424; 98.
DR IntAct; P42025; 53.
DR MINT; P42025; -.
DR STRING; 9606.ENSP00000289228; -.
DR iPTMnet; P42025; -.
DR MetOSite; P42025; -.
DR PhosphoSitePlus; P42025; -.
DR BioMuta; ACTR1B; -.
DR DMDM; 1168333; -.
DR OGP; P42025; -.
DR REPRODUCTION-2DPAGE; IPI00029469; -.
DR EPD; P42025; -.
DR jPOST; P42025; -.
DR MassIVE; P42025; -.
DR MaxQB; P42025; -.
DR PaxDb; P42025; -.
DR PeptideAtlas; P42025; -.
DR PRIDE; P42025; -.
DR ProteomicsDB; 55480; -.
DR Antibodypedia; 32643; 159 antibodies from 29 providers.
DR DNASU; 10120; -.
DR Ensembl; ENST00000289228.7; ENSP00000289228.5; ENSG00000115073.8.
DR GeneID; 10120; -.
DR KEGG; hsa:10120; -.
DR MANE-Select; ENST00000289228.7; ENSP00000289228.5; NM_005735.4; NP_005726.1.
DR UCSC; uc002syb.3; human.
DR CTD; 10120; -.
DR DisGeNET; 10120; -.
DR GeneCards; ACTR1B; -.
DR HGNC; HGNC:168; ACTR1B.
DR HPA; ENSG00000115073; Low tissue specificity.
DR MIM; 605144; gene.
DR neXtProt; NX_P42025; -.
DR OpenTargets; ENSG00000115073; -.
DR PharmGKB; PA24487; -.
DR VEuPathDB; HostDB:ENSG00000115073; -.
DR eggNOG; KOG0676; Eukaryota.
DR GeneTree; ENSGT00940000161587; -.
DR HOGENOM; CLU_027965_0_1_1; -.
DR InParanoid; P42025; -.
DR OMA; YTTWTGG; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; P42025; -.
DR TreeFam; TF300420; -.
DR PathwayCommons; P42025; -.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; P42025; -.
DR BioGRID-ORCS; 10120; 195 hits in 1077 CRISPR screens.
DR ChiTaRS; ACTR1B; human.
DR GeneWiki; ACTR1B; -.
DR GenomeRNAi; 10120; -.
DR Pharos; P42025; Tbio.
DR PRO; PR:P42025; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P42025; protein.
DR Bgee; ENSG00000115073; Expressed in right frontal lobe and 208 other tissues.
DR Genevisible; P42025; HS.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:LIFEdb.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005869; C:dynactin complex; TAS:ProtInc.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0015630; C:microtubule cytoskeleton; IDA:HPA.
DR GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR020902; Actin/actin-like_CS.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00432; ACTINS_2; 1.
DR PROSITE; PS01132; ACTINS_ACT_LIKE; 1.
PE 1: Evidence at protein level;
KW Acetylation; ATP-binding; Cytoplasm; Cytoskeleton;
KW Direct protein sequencing; Nitration; Nucleotide-binding;
KW Reference proteome.
FT CHAIN 1..376
FT /note="Beta-centractin"
FT /id="PRO_0000089060"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895"
FT MOD_RES 4
FT /note="3'-nitrotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q8R5C5"
FT VARIANT 93
FT /note="V -> A (in dbSNP:rs11547231)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_025315"
FT VARIANT 143
FT /note="A -> V (in dbSNP:rs11692435)"
FT /id="VAR_048187"
SQ SEQUENCE 376 AA; 42293 MW; 24C24ECEE18B83BD CRC64;
MESYDIIANQ PVVIDNGSGV IKAGFAGDQI PKYCFPNYVG RPKHMRVMAG ALEGDLFIGP
KAEEHRGLLT IRYPMEHGVV RDWNDMERIW QYVYSKDQLQ TFSEEHPVLL TEAPLNPSKN
REKAAEVFFE TFNVPALFIS MQAVLSLYAT GRTTGVVLDS GDGVTHAVPI YEGFAMPHSI
MRVDIAGRDV SRYLRLLLRK EGVDFHTSAE FEVVRTIKER ACYLSINPQK DEALETEKVQ
YTLPDGSTLD VGPARFRAPE LLFQPDLVGD ESEGLHEVVA FAIHKSDMDL RRTLFANIVL
SGGSTLFKGF GDRLLSEVKK LAPKDIKIKI SAPQERLYST WIGGSILASL DTFKKMWVSK
KEYEEDGSRA IHRKTF