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P63261 (ACTG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Actin, cytoplasmic 2
Alternative name(s):
Gamma-actin

Cleaved into the following chain:

  1. Actin, cytoplasmic 2, N-terminally processed
Gene names
Name:ACTG1
Synonyms:ACTB, ACTG
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length375 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (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 structure

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.

Subcellular location

Cytoplasmcytoskeleton.

Post-translational modification

The methylhistidine determined by Bienvenut et al is assumed to be the tele-methylhistidine isomer by similarity to the mouse ortholog.

Oxidation of Met-44 and Met-47 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. MICAL1 and MICAL2 produce the (R)-S-oxide form. The (R)-S-oxide form is reverted by MSRB1 and MSRB2, which promote actin repolymerization By similarity.

Monomethylation at Lys-84 (K84me1) regulates actin-myosin interaction and actomyosin-dependent processes. Demethylation by ALKBH4 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration.

Involvement in disease

Deafness, autosomal dominant, 20 (DFNA20) [MIM:604717]: A form of non-syndromic 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.15 Ref.16 Ref.17 Ref.18

Baraitser-Winter syndrome 2 (BRWS2) [MIM:614583]: A rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior-predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.19

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.

Sequence similarities

Belongs to the actin family.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityPolymorphism
   DiseaseDeafness
Disease mutation
Mental retardation
Non-syndromic deafness
   LigandATP-binding
Nucleotide-binding
   PTMAcetylation
Methylation
Oxidation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-gamma receptor signaling pathway involved in phagocytosis

Traceable author statement. Source: Reactome

adherens junction organization

Traceable author statement. Source: Reactome

axon guidance

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

cell-cell junction organization

Traceable author statement. Source: Reactome

cellular component movement

Traceable author statement PubMed 16130169. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

membrane organization

Traceable author statement. Source: Reactome

retina homeostasis

Inferred from expression pattern PubMed 23580065. Source: UniProt

sarcomere organization

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentblood microparticle

Inferred from direct assay PubMed 22516433. Source: UniProt

cytoskeleton

Traceable author statement PubMed 16130169. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

extracellular space

Inferred from direct assay PubMed 16502470PubMed 23580065. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 21557262. Source: UniProtKB

filamentous actin

Inferred from electronic annotation. Source: Ensembl

myofibril

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

identical protein binding

Inferred from physical interaction PubMed 16189514PubMed 21516116. Source: IntAct

protein binding

Inferred from physical interaction PubMed 16189514PubMed 20706999PubMed 21516116. Source: IntAct

structural constituent of cytoskeleton

Inferred by curator PubMed 16130169. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 375375Actin, cytoplasmic 2
PRO_0000367100
Initiator methionine11Removed; alternate Ref.6 Ref.7 Ref.8
Chain2 – 375374Actin, cytoplasmic 2, N-terminally processed
PRO_0000000831

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12
Modified residue21N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed; partial Ref.7 Ref.8 Ref.11 Ref.12
Modified residue441Methionine (R)-sulfoxide By similarity
Modified residue471Methionine (R)-sulfoxide By similarity
Modified residue731Tele-methylhistidine Ref.8
Modified residue841N6-methyllysine Ref.13

Natural variations

Natural variant891T → I in DFNA20. Ref.14
Corresponds to variant rs28999111 [ dbSNP | Ensembl ].
VAR_032434
Natural variant1181K → M in DFNA20. Ref.14
VAR_032435
Natural variant1181K → N in DFNA20. Ref.18
Corresponds to variant rs267606630 [ dbSNP | Ensembl ].
VAR_067824
Natural variant1201T → I in BRWS2. Ref.19
Corresponds to variant rs281875325 [ dbSNP | Ensembl ].
VAR_067814
Natural variant1221I → V in DFNA20. Ref.17
Corresponds to variant rs281875330 [ dbSNP | Ensembl ].
VAR_067825
Natural variant1351A → V in BRWS2. Ref.19
Corresponds to variant rs11549190 [ dbSNP | Ensembl ].
VAR_067815
Natural variant1551S → F in BRWS2. Ref.19
Corresponds to variant rs281875326 [ dbSNP | Ensembl ].
VAR_067816
Natural variant1601T → I.
Corresponds to variant rs11549206 [ dbSNP | Ensembl ].
VAR_048186
Natural variant2031T → K in BRWS2. Ref.19
Corresponds to variant rs281875327 [ dbSNP | Ensembl ].
VAR_067817
Natural variant2411E → K in DFNA20. Ref.18
Corresponds to variant rs267606631 [ dbSNP | Ensembl ].
VAR_067826
Natural variant2431P → L.
Corresponds to variant rs11546899 [ dbSNP | Ensembl ].
VAR_055482
Natural variant2541R → W in BRWS2. Ref.19
Corresponds to variant rs281875328 [ dbSNP | Ensembl ].
VAR_067818
Natural variant2561R → W in BRWS2. Ref.19
Corresponds to variant rs281875329 [ dbSNP | Ensembl ].
VAR_067819
Natural variant2641P → L in DFNA20. Ref.14
VAR_032436
Natural variant2781T → I in DFNA20. Ref.15
Corresponds to variant rs28999112 [ dbSNP | Ensembl ].
VAR_032437
Natural variant3321P → A in DFNA20. Ref.14
VAR_032438
Natural variant3701V → A in DFNA20; restricts cell growth at elevated temperature or under hyperosmolar stress as measured in growth assays with yeast expressing the mutation. Ref.16
VAR_032439

Experimental info

Sequence conflict3161E → K in AAA51580. Ref.10
Sequence conflict3441S → F in AAA51580. Ref.10

Sequences

Sequence LengthMass (Da)Tools
P63261 [UniParc].

Last modified July 21, 1986. Version 1.
Checksum: 54D08F986964EFD5

FASTA37541,793
        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 

« Hide

References

« Hide 'large scale' references
[1]"Nucleotide sequence of the human gamma cytoskeletal actin mRNA: anomalous evolution of vertebrate non-muscle actin genes."
Erba H.P., Gunning P., Kedes L.
Nucleic Acids Res. 14:5275-5294(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Structure, chromosome location, and expression of the human gamma-actin gene: differential evolution, location, and expression of the cytoskeletal beta- and gamma-actin genes."
Erba H.P., Eddy R., Shows T., Kedes L., Gunning P.
Mol. Cell. Biol. 8:1775-1789(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
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. expand/collapse author list , 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.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
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.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: B-cell, Eye, Lung, Ovary, Placenta, Skin and Uterus.
[6]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-28.
Tissue: Platelet.
[7]Bienvenut W.V.
Submitted (JUN-2005) to UniProtKB
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[8]Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W., Dozynkiewicz M., Norman J.C.
Submitted (JUN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-116; 119-210; 216-254 AND 291-372, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLU-2, METHYLATION AT HIS-73, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[9]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 29-39; 85-113; 239-254 AND 292-312, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[10]"Gamma-actin: unusual mRNA 3'-untranslated sequence conservation and amino acid substitutions that may be cancer related."
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.
Proc. Natl. Acad. Sci. U.S.A. 84:2575-2579(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-375.
[11]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT GLU-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND GLU-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"ALKBH4-dependent demethylation of actin regulates actomyosin dynamics."
Li M.M., Nilsen A., Shi Y., Fusser M., Ding Y.H., Fu Y., Liu B., Niu Y., Wu Y.S., Huang C.M., Olofsson M., Jin K.X., Lv Y., Xu X.Z., He C., Dong M.Q., Rendtlew Danielsen J.M., Klungland A., Yang Y.G.
Nat. Commun. 4:1832-1832(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: METHYLATION AT LYS-84, DEMETHYLATION BY ALKBH4.
[14]"Mutations in the gamma-actin gene (ACTG1) are associated with dominant progressive deafness (DFNA20/26)."
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.
Am. J. Hum. Genet. 73:1082-1091(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DFNA20 ILE-89; MET-118; LEU-264 AND ALA-332.
[15]"A mutation in the gamma actin 1 (ACTG1) gene causes autosomal dominant hearing loss (DFNA20/26)."
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.
J. Med. Genet. 40:879-884(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNA20 ILE-278.
[16]"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."
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.
Eur. J. Hum. Genet. 14:1097-1105(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNA20 ALA-370, CHARACTERIZATION OF VARIANT DFNA20 ALA-370.
[17]"Novel ACTG1 mutation causing autosomal dominant non-syndromic hearing impairment in a Chinese family."
Liu P., Li H., Ren X., Mao H., Zhu Q., Zhu Z., Yang R., Yuan W., Liu J., Wang Q., Liu M.
J. Genet. Genomics 35:553-558(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT DFNA20 VAL-122.
[18]"In vivo and in vitro effects of two novel gamma-actin (ACTG1) mutations that cause DFNA20/26 hearing impairment."
Morin M., Bryan K.E., Mayo-Merino F., Goodyear R., Mencia A., Modamio-Hoybjor S., del Castillo I., Cabalka J.M., Richardson G., Moreno F., Rubenstein P.A., Moreno-Pelayo M.A.
Hum. Mol. Genet. 18:3075-3089(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS DFNA20 ASN-118 AND LYS-241.
[19]"De novo mutations in the actin genes ACTB and ACTG1 cause Baraitser-Winter syndrome."
Riviere J.B., van Bon B.W., Hoischen A., Kholmanskikh S.S., O'Roak B.J., Gilissen C., Gijsen S., Sullivan C.T., Christian S.L., Abdul-Rahman O.A., Atkin J.F., Chassaing N., Drouin-Garraud V., Fry A.E., Fryns J.P., Gripp K.W., Kempers M., Kleefstra T. expand/collapse author list , Mancini G.M., Nowaczyk M.J., van Ravenswaaij-Arts C.M., Roscioli T., Marble M., Rosenfeld J.A., Siu V.M., de Vries B.B., Shendure J., Verloes A., Veltman J.A., Brunner H.G., Ross M.E., Pilz D.T., Dobyns W.B.
Nat. Genet. 44:440-444(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BRWS2 ILE-120; VAL-135; PHE-155; LYS-203; TRP-254 AND TRP-256.
+Additional computationally mapped references.

Web resources

Mendelian genes actin, gamma 1 (ACTG1)

Leiden Open Variation Database (LOVD)

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X04098 mRNA. Translation: CAA27723.1.
M19283 Genomic DNA. Translation: AAA51579.1.
AK291937 mRNA. Translation: BAF84626.1.
BT019856 mRNA. Translation: AAV38659.1.
BC000292 mRNA. Translation: AAH00292.1.
BC001920 mRNA. Translation: AAH01920.1.
BC007442 mRNA. Translation: AAH07442.1.
BC009848 mRNA. Translation: AAH09848.1.
BC010999 mRNA. Translation: AAH10999.1.
BC012050 mRNA. Translation: AAH12050.1.
BC015005 mRNA. Translation: AAH15005.1.
BC015695 mRNA. Translation: AAH15695.1.
BC015779 mRNA. Translation: AAH15779.1.
BC018774 mRNA. Translation: AAH18774.1.
BC053572 mRNA. Translation: AAH53572.1.
M16247 mRNA. Translation: AAA51580.1.
CCDSCCDS11782.1.
PIRATHUG. A28098.
JC5818.
RefSeqNP_001186883.1. NM_001199954.1.
NP_001605.1. NM_001614.3.
UniGeneHs.514581.
Hs.713764.

3D structure databases

ProteinModelPortalP63261.
SMRP63261. Positions 6-375.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106586. 89 interactions.
IntActP63261. 37 interactions.
MINTMINT-4998686.
STRING9606.ENSP00000331514.

PTM databases

PhosphoSiteP63261.

Polymorphism databases

DMDM54036678.

2D gel databases

DOSAC-COBS-2DPAGEP60709_OR_P63261.
P63261.
OGPP63261.
REPRODUCTION-2DPAGEP63261.
SWISS-2DPAGEP63261.

Proteomic databases

MaxQBP63261.
PRIDEP63261.

Protocols and materials databases

DNASU71.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000331925; ENSP00000331514; ENSG00000184009.
ENST00000573283; ENSP00000458435; ENSG00000184009.
ENST00000575087; ENSP00000459124; ENSG00000184009.
ENST00000575842; ENSP00000458162; ENSG00000184009.
ENST00000576544; ENSP00000461672; ENSG00000184009.
ENST00000593601; ENSP00000470102; ENSG00000267807.
ENST00000597869; ENSP00000471522; ENSG00000267807.
ENST00000598366; ENSP00000470446; ENSG00000267807.
ENST00000601143; ENSP00000472125; ENSG00000267807.
ENST00000601845; ENSP00000469093; ENSG00000267807.
GeneID71.
KEGGhsa:71.
UCSCuc002kak.2. human.

Organism-specific databases

CTD71.
GeneCardsGC17M079476.
GeneReviewsACTG1.
H-InvDBHIX0001479.
HIX0199868.
HGNCHGNC:144. ACTG1.
HPACAB013531.
HPA041264.
HPA041271.
MIM102560. gene.
604717. phenotype.
614583. phenotype.
neXtProtNX_P63261.
Orphanet90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
2995. Baraitser-Winter syndrome.
PharmGKBPA24468.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG003771.
InParanoidP63261.
KOK05692.
OMADARAPIM.
PhylomeDBP63261.
TreeFamTF354237.

Enzyme and pathway databases

ReactomeREACT_111045. Developmental Biology.
REACT_111155. Cell-Cell communication.
REACT_11123. Membrane Trafficking.
REACT_6900. Immune System.
SignaLinkP63261.

Gene expression databases

BgeeP63261.
CleanExHS_ACTB.
HS_ACTG1.
GenevestigatorP63261.

Family and domain databases

InterProIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACTG1. human.
GeneWikiACTG1.
GenomeRNAi71.
NextBio279.
PMAP-CutDBP63261.
PROP63261.
SOURCESearch...

Entry information

Entry nameACTG_HUMAN
AccessionPrimary (citable) accession number: P63261
Secondary accession number(s): A8K7C2 expand/collapse secondary AC list , P02571, P14104, P99022, Q5U032, Q96E67
Entry history
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: July 9, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM