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UniProtKB/Swiss-Prot entry P63261


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ACTG_HUMAN
Primary accession number P63261
Secondary accession numbers A8K7C2 P02571 P14104 P99022 Q5U032 Q96E67
Integrated into Swiss-Prot on July 21, 1986
Sequence was last modified on July 21, 1986 (Sequence version 1)
Annotations were last modified on    June 16, 2009 (Entry version 66)
Name and origin of the protein
Protein name Actin, cytoplasmic 2
Synonym Gamma-actin
Contains Actin, cytoplasmic 2, N-terminally processed
Gene name
Name: ACTG1
Synonyms: ACTB, ACTG
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1093/nar/14.13.5275; PubMed=3737401 [NCBI, ExPASy, EBI, Israel, Japan]
Erba H.P., Gunning P., Kedes L.;
"Nucleotide sequence of the human gamma cytoskeletal actin mRNA: anomalous evolution of vertebrate non-muscle actin genes.";
Nucleic Acids Res. 14:5275-5294(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2837653 [NCBI, ExPASy, EBI, Israel, Japan]
Erba H.P., Eddy R., Shows T., Kedes L., Gunning P.;
"Structure, chromosome location, and expression of the human gamma-actin gene: differential evolution, location, and expression of the cytoskeletal beta- and gamma-actin genes.";
Mol. Cell. Biol. 8:1775-1789(1988).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=B-cell, Eye, Lung, Ovary, Placenta, Skin, and Uterus;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
PROTEIN SEQUENCE OF 2-28.
TISSUE=Platelet;
DOI=10.1038/nbt810; PubMed=12665801 [NCBI, ExPASy, EBI, Israel, Japan]
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[7]
PROTEIN SEQUENCE OF 2-18; 29-37; 40-50; 85-113; 148-177; 184-191; 197-206; 239-254; 292-312 AND 316-326, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLU-2, AND MASS SPECTROMETRY.
TISSUE=B-cell lymphoma;
Bienvenut W.V.;
Submitted (JUN-2005) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 2-113; 119-177; 184-191; 197-206; 239-254; 291-312; 316-326 AND 329-372, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLU-2, METHYLATION AT HIS-73, AND MASS SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[9]
PROTEIN SEQUENCE OF 29-39; 85-113; 239-254 AND 292-312, AND MASS SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Afjehi-Sadat L.;
Submitted (MAR-2007) to UniProtKB.
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 144-375.
DOI=10.1073/pnas.84.9.2575; PubMed=3472224 [NCBI, ExPASy, EBI, Israel, Japan]
Chou C.C., Davis R.C., Fuller M.L., Slovin J.P., Wong A., Wright J., Kania S., Shaked R., Gatti R.A., Salser W.A.;
"Gamma-actin: unusual mRNA 3'-untranslated sequence conservation and amino acid substitutions that may be cancer related.";
Proc. Natl. Acad. Sci. U.S.A. 84:2575-2579(1987).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198 AND TYR-294, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, AND MASS SPECTROMETRY.
TISSUE=Platelet;
DOI=10.1021/pr0704130; PubMed=18088087 [NCBI, ExPASy, EBI, Israel, Japan]
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A.;
"Phosphoproteome of resting human platelets.";
J. Proteome Res. 7:526-534(2008).
[13]
VARIANTS DFNA20 ILE-89; MET-118; LEU-264 AND ALA-332.
DOI=10.1086/379286; PubMed=13680526 [NCBI, ExPASy, EBI, Israel, Japan]
Zhu M., Yang T., Wei S., DeWan A.T., Morell R.J., Elfenbein J.L., Fisher R.A., Leal S.M., Smith R.J.H., Friderici K.H.;
"Mutations in the gamma-actin gene (ACTG1) are associated with dominant progressive deafness (DFNA20/26).";
Am. J. Hum. Genet. 73:1082-1091(2003).
[14]
VARIANT DFNA20 ILE-278.
DOI=10.1136/jmg.40.12.879; PubMed=14684684 [NCBI, ExPASy, EBI, Israel, Japan]
van Wijk E., Krieger E., Kemperman M.H., De Leenheer E.M.R., Huygen P.L.M., Cremers C.W.R.J., Cremers F.P.M., Kremer H.;
"A mutation in the gamma actin 1 (ACTG1) gene causes autosomal dominant hearing loss (DFNA20/26).";
J. Med. Genet. 40:879-884(2003).
[15]
VARIANT DFNA20 ALA-370, AND CHARACTERIZATION OF VARIANT DFNA20 ALA-370.
DOI=10.1038/sj.ejhg.5201670; PubMed=16773128 [NCBI, ExPASy, EBI, Israel, Japan]
Rendtorff N.D., Zhu M., Fagerheim T., Antal T.L., Jones M., Teslovich T.M., Gillanders E.M., Barmada M., Teig E., Trent J.M., Friderici K.H., Stephan D.A., Tranebjaerg L.;
"A novel missense mutation in ACTG1 causes dominant deafness in a Norwegian DFNA20/26 family, but ACTG1 mutations are not frequent among families with hereditary hearing impairment.";
Eur. J. Hum. Genet. 14:1097-1105(2006).
Comments
  • FUNCTION: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
  • SUBUNIT: Polymerization of globular actin (G-actin) leads to a structural filament (F-actin) in the form of a two-stranded helix. Each actin can bind to 4 others.
  • INTERACTION:
    Self; NbExp=1; IntAct=EBI-351292, EBI-351292;
    Q9Y281:CFL2; NbExp=1; IntAct=EBI-351292, EBI-351218;
    Q92597:NDRG1; NbExp=1; IntAct=EBI-351292, EBI-716486;
  • SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton.
  • DISEASE: Defects in ACTG1 are the cause of non-syndromic sensorineural deafness autosomal dominant type 20 (DFNA20) [MIM:604717]; also called autosomal dominant deafness type 26 (DFNA26). DFNA20 is a form of sensorineural hearing loss. Sensorineural deafness results from damage to the neural receptors of the inner ear, the nerve pathways to the brain, or the area of the brain that receives sound information.
  • MISCELLANEOUS: In vertebrates 3 main groups of actin isoforms, alpha, beta and gamma have been identified. The alpha actins are found in muscle tissues and are a major constituent of the contractile apparatus. The beta and gamma actins coexist in most cell types as components of the cytoskeleton and as mediators of internal cell motility.
  • SIMILARITY: Belongs to the actin family.
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X04098; CAA27723.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M19283; AAA51579.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291937; BAF84626.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BT019856; AAV38659.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC000292; AAH00292.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC001920; AAH01920.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007442; AAH07442.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC009848; AAH09848.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC010999; AAH10999.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012050; AAH12050.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015005; AAH15005.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015695; AAH15695.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015779; AAH15779.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018774; AAH18774.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC053572; AAH53572.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M16247; AAA51580.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00021440; -.
PIR A28098; ATHUG.
JC5818; JC5818.
RefSeq NP_001605.1; -.
UniGene Hs.514581
3D structure databases
HSSP P02570; 2BTF. [HSSP ENTRY / PDB]
SMR P63261; 4-371.
ModBase P63261.
Protein-protein interaction databases
IntAct P63261; 40.
PTM databases
PhosphoSite P63261; -.
2D gel databases
SWISS-2DPAGE P63261; -.
DOSAC-COBS-2DPAGE P63261; -.
OGP P63261; -.
PMMA-2DPAGE P63261; -.
REPRODUCTION-2DPAGE P63261; -.
Organism-specific databases
GeneCards GC17M077091; -.
H-InvDB HIX0020804; -.
HIX0080324; -.
HGNC HGNC:144; ACTG1.
GenAtlas ACTG1.
HPA CAB013531; -.
MIM 102560; gene. [NCBI / EBI]
604717; phenotype. [NCBI / EBI]
Orphanet 90635; Deafness, autosomal dominant, nonsyndromic, sensorineural, type DFNA.
87884; Nonsyndromic genetic deafness.
PharmGKB PA24468; -.
Gene expression databases
ArrayExpress P63261; -.
Bgee P63261; -.
CleanEx HS_ACTB; -.
HS_ACTG1; -.
GermOnline ENSG00000184009; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (inferred from electronic annotation from UniProtKB-SubCell).
GO:0005856; Cellular component: cytoskeleton (traceable author statement from UniProtKB).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0042802; Molecular function: identical protein binding (inferred from physical interaction from IntAct).
GO:0005200; Molecular function: structural constituent of cytoskeleton (inferred by curator from UniProtKB).
GO:0006928; Biological process: cell motion (traceable author statement from UniProtKB).
GO:0007605; Biological process: sensory perception of sound (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR004000; Actin-like.
IPR004001; Actin_CS.
Graphical view of domain structure.
PANTHER PTHR11937; Actin_like; 1.
Pfam PF00022; Actin; 1.
Pfam graphical view of domain structure.
PRINTS PR00190; ACTIN.
SMART SM00268; ACTIN; 1.
SMART graphical view of domain structure.
PROSITE PS00406; ACTINS_1; 1.
PS00432; ACTINS_2; 1.
PS01132; ACTINS_ACT_LIKE; 1.
Proteomic databases
PRIDE P63261; -.
Genome annotation databases
Ensembl ENSG00000184009; Homo sapiens. [Contig view]
GeneID 71; -.
KEGG hsa:71; -.
Phylogenomic databases
HOGENOM P63261; -.
HOVERGEN P63261; -.
OMA P63261; MAESEDI.
Other
NextBio 279; -.
PMAP-CutDB P63261; -.
SOURCE ACTG1; Homo sapiens.
ProtoNet P63261.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; ATP-binding; Cytoplasm; Cytoskeleton; Deafness; Direct protein sequencing; Disease mutation; Methylation; Non-syndromic deafness; Nucleotide-binding; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   375  375     Actin, cytoplasmic 2. PRO_0000367100
INIT_MET   1     1        Removed; alternate. 
CHAIN   2   375  374     Actin, cytoplasmic 2, N-terminally processed. PRO_0000000831
MOD_RES   1     1        N-acetylmethionine; in Actin, cytoplasmic 2; alternate (By similarity). 
MOD_RES   2     2        N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed. 
MOD_RES   73    73        Methylhistidine. 
MOD_RES   169   169        Phosphotyrosine (By similarity). 
MOD_RES   198   198        Phosphotyrosine. 
MOD_RES   294   294        Phosphotyrosine. 
MOD_RES   318   318        Phosphothreonine. 
VARIANT   89    89  1     T -> I (in DFNA20; dbSNP:rs28999111 [NCBI]). VAR_032434 [3D]
VARIANT   118   118  1     K -> M (in DFNA20). VAR_032435 [3D]
VARIANT   160   160  1     T -> I (in dbSNP:rs11549206 [NCBI]). VAR_048186 [3D]
VARIANT   243   243  1     P -> L (in dbSNP:rs11546899 [NCBI]). VAR_055482 [3D]
VARIANT   264   264  1     P -> L (in DFNA20). VAR_032436 [3D]
VARIANT   278   278  1     T -> I (in DFNA20; dbSNP:rs28999112 [NCBI]). VAR_032437 [3D]
VARIANT   332   332  1     P -> A (in DFNA20). VAR_032438 [3D]
VARIANT   370   370  1     V -> A (in DFNA20; restricts cell growth at elevated temperature or under hyperosmolar stress as measured in growth assays with yeast expressing the mutation). VAR_032439 
CONFLICT   316   316        E -> K (in Ref. 10; AAA51580). 
CONFLICT   344   344        S -> F (in Ref. 10; AAA51580). 
Sequence information
Length: 375 AA [This is the length of the unprocessed precursor] Molecular weight: 41793 Da [This is the MW of the unprocessed precursor] CRC64: 54D08F986964EFD5 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS 

        70         80         90        100        110        120 
KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE HPVLLTEAPL NPKANREKMT 

       130        140        150        160        170        180 
QIMFETFNTP AMYVAIQAVL SLYASGRTTG IVMDSGDGVT HTVPIYEGYA LPHAILRLDL 

       190        200        210        220        230        240 
AGRDLTDYLM KILTERGYSF TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY 

       250        260        270        280        290        300 
ELPDGQVITI GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 

       310        320        330        340        350        360 
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS TFQQMWISKQ 

       370 
EYDESGPSIV HRKCF 

P63261 in FASTA format

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