P63261 (ACTG_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	375 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton.
Post-translational modification	The methylhistidine determined by Bienvenut et al is assumed to be the tele-methylhistidine isomer by similarity to the mouse ortholog.
Involvement in disease	Defects in ACTG1 are the cause of 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. Ref.13 Ref.14 Ref.15
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 component	Cytoplasm Cytoskeleton
Coding sequence diversity	Polymorphism
Disease	Deafness Disease mutation Non-syndromic deafness
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Methylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	adherens junction organization Traceable author statement. Source: Reactome axon guidance Traceable author statement. Source: Reactome blood coagulation Traceable author statement. Source: Reactome cell junction assembly Traceable author statement. Source: Reactome cellular component movement Traceable author statement. Source: UniProtKB
Cellular component	cytosol Traceable author statement. Source: Reactome
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW identical protein binding Inferred from physical interaction. Source: IntAct structural constituent of cytoskeleton Inferred by curator. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-351292,EBI-351292
CFL2	Q9Y281	2	EBI-351292,EBI-351218
MLH1	P40692	7	EBI-351292,EBI-744248

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 375	375	Actin, cytoplasmic 2		PRO_0000367100
	Initiator methionine	1	1	Removed; alternate Ref.6 Ref.7 Ref.8
	Chain	2 – 375	374	Actin, cytoplasmic 2, N-terminally processed		PRO_0000000831
Amino acid modifications
	Modified residue	1	1	N-acetylmethionine; in Actin, cytoplasmic 2; alternate By similarity
	Modified residue	2	1	N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed; partial Ref.7 Ref.8
	Modified residue	73	1	Tele-methylhistidine Ref.8
	Modified residue	169	1	Phosphotyrosine By similarity
	Modified residue	198	1	Phosphotyrosine Ref.11
	Modified residue	294	1	Phosphotyrosine Ref.11
	Modified residue	318	1	Phosphothreonine Ref.12
Natural variations
	Natural variant	89	1	T → I in DFNA20. Ref.13 Corresponds to variant rs28999111 [ dbSNP | Ensembl ].		VAR_032434
	Natural variant	118	1	K → M in DFNA20. Ref.13		VAR_032435
	Natural variant	160	1	T → I. Corresponds to variant rs11549206 [ dbSNP | Ensembl ].		VAR_048186
	Natural variant	243	1	P → L. Corresponds to variant rs11546899 [ dbSNP | Ensembl ].		VAR_055482
	Natural variant	264	1	P → L in DFNA20. Ref.13		VAR_032436
	Natural variant	278	1	T → I in DFNA20. Ref.14 Corresponds to variant rs28999112 [ dbSNP | Ensembl ].		VAR_032437
	Natural variant	332	1	P → A in DFNA20. Ref.13		VAR_032438
	Natural variant	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. Ref.15		VAR_032439
Experimental info
	Sequence conflict	316	1	E → K in AAA51580. Ref.10
	Sequence conflict	344	1	S → F in AAA51580. Ref.10

Sequences

	Sequence		Length	Mass (Da)
	P63261 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 54D08F986964EFD5	FASTA	375	41,793
	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

References

	« Hide 'large scale' referencesShow '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: 3737401] [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: 2837653] [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. , 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: 14702039] [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: 15489334] [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: 12665801] [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, 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, 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, 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: 3472224] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-375.
[11]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." 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. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-198 AND TYR-294, MASS SPECTROMETRY. Tissue: Lung carcinoma.
[12]	"Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-318, MASS SPECTROMETRY. Tissue: Platelet.
[13]	"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: 13680526] [Abstract] Cited for: VARIANTS DFNA20 ILE-89; MET-118; LEU-264 AND ALA-332.
[14]	"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: 14684684] [Abstract] Cited for: VARIANT DFNA20 ILE-278.
[15]	"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: 16773128] [Abstract] Cited for: VARIANT DFNA20 ALA-370, CHARACTERIZATION OF VARIANT DFNA20 ALA-370.
+	Additional computationally mapped references.

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.
IPI	IPI00021440.
PIR	ATHUG. A28098. JC5818.
RefSeq	NP_001186883.1. NM_001199954.1. NP_001605.1. NM_001614.3.
UniGene	Hs.514581.
3D structure databases
ProteinModelPortal	P63261.
SMR	P63261. Positions 2-375.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63261. 34 interactions.
MINT	MINT-4998686.
STRING	P63261.
PTM databases
PhosphoSite	P63261.
Polymorphism databases
DMDM	54036678.
2D gel databases
SWISS-2DPAGE	P63261.
DOSAC-COBS-2DPAGE	P60709_OR_P63261. P63261.
OGP	P63261.
PMMA-2DPAGE	P63261.
REPRODUCTION-2DPAGE	P63261.
Proteomic databases
PRIDE	P63261.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000331925; ENSP00000331514; ENSG00000184009.
GeneID	71.
KEGG	hsa:71.
UCSC	uc002kaj.1. human.
Organism-specific databases
CTD	71.
GeneCards	GC17M079476.
H-InvDB	HIX0020804.
HGNC	HGNC:144. ACTG1.
HPA	CAB013531.
MIM	102560. gene. 604717. phenotype.
neXtProt	NX_P63261.
Orphanet	90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
PharmGKB	PA24468.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG003771.
InParanoid	P63261.
OMA	IAMEEEI.
OrthoDB	EOG41JZC9.
PhylomeDB	P63261.
Enzyme and pathway databases
Reactome	REACT_111045. Developmental Biology. REACT_111155. Cell-Cell communication. REACT_11123. Membrane Trafficking. REACT_604. Hemostasis.
Gene expression databases
ArrayExpress	P63261.
Bgee	P63261.
CleanEx	HS_ACTB. HS_ACTG1.
Genevestigator	P63261.
GermOnline	ENSG00000184009. Homo sapiens.
Family and domain databases
InterPro	IPR004000. Actin-like. IPR020902. Actin/actin-like_CS. IPR004001. Actin_CS. [Graphical view]
KO	K05692.
PANTHER	PTHR11937. Actin_like. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
PRINTS	PR00190. ACTIN.
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS00406. ACTINS_1. 1 hit. PS00432. ACTINS_2. 1 hit. PS01132. ACTINS_ACT_LIKE. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	279.
PMAP-CutDB	P63261.
SOURCE	Search...

Entry information

Entry name

ACTG_HUMAN

Accession

Primary (citable) accession number: P63261
Secondary accession number(s): A8K7C2 , P02571, P14104, P99022, Q5U032, Q96E67

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	January 25, 2012
This is version 97 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.