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) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › 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. Oxidation of Met-44 by MICALs (MICAL1, MICAL2 or MICAL3) to form methionine sulfoxide promotes actin filament depolymerization. Methionine sulfoxide is produced stereospecifically, but it is not known whether the (S)-S-oxide or the (R)-S-oxide is produced By similarity.
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.11 Ref.12 Ref.13 Ref.14 Ref.15 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.16
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 Mental retardation Non-syndromic deafness
Ligand	ATP-binding Nucleotide-binding
PTM	Acetylation Methylation Oxidation 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 PubMed 16130169. Source: UniProtKB sarcomere organization Inferred from electronic annotation. Source: Compara
Cellular_component	cytoskeleton Traceable author statement PubMed 16130169. Source: UniProtKB cytosol Traceable author statement. Source: Reactome extracellular vesicular exosome Inferred from direct assay PubMed 21557262. Source: UniProtKB filamentous actin Inferred from electronic annotation. Source: Compara myofibril Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW structural constituent of cytoskeleton Inferred by curator PubMed 16130169. 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 By similarity
	Modified residue	2	1	N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed; partial Ref.7 Ref.8
	Modified residue	44	1	Methionine sulfoxide By similarity
	Modified residue	73	1	Tele-methylhistidine Ref.8
	Modified residue	169	1	Phosphotyrosine By similarity
Natural variations
	Natural variant	89	1	T → I in DFNA20. Ref.11 Corresponds to variant rs28999111 [ dbSNP | Ensembl ].		VAR_032434
	Natural variant	118	1	K → M in DFNA20. Ref.11		VAR_032435
	Natural variant	118	1	K → N in DFNA20. Ref.15		VAR_067824
	Natural variant	120	1	T → I in BRWS2. Ref.16		VAR_067814
	Natural variant	122	1	I → V in DFNA20. Ref.14		VAR_067825
	Natural variant	135	1	A → V in BRWS2. Ref.16		VAR_067815
	Natural variant	155	1	S → F in BRWS2. Ref.16		VAR_067816
	Natural variant	160	1	T → I. Corresponds to variant rs11549206 [ dbSNP | Ensembl ].		VAR_048186
	Natural variant	203	1	T → K in BRWS2. Ref.16		VAR_067817
	Natural variant	241	1	E → K in DFNA20. Ref.15		VAR_067826
	Natural variant	243	1	P → L. Corresponds to variant rs11546899 [ dbSNP | Ensembl ].		VAR_055482
	Natural variant	254	1	R → W in BRWS2. Ref.16		VAR_067818
	Natural variant	256	1	R → W in BRWS2. Ref.16		VAR_067819
	Natural variant	264	1	P → L in DFNA20. Ref.11		VAR_032436
	Natural variant	278	1	T → I in DFNA20. Ref.12 Corresponds to variant rs28999112 [ dbSNP | Ensembl ].		VAR_032437
	Natural variant	332	1	P → A in DFNA20. Ref.11		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.13		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] [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. , 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, 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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 144-375.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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. , 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.
IPI	IPI00021440.
PIR	ATHUG. A28098. JC5818.
RefSeq	NP_001186883.1. NM_001199954.1. NP_001605.1. NM_001614.3.
UniGene	Hs.514581. Hs.731391.
3D structure databases
ProteinModelPortal	P63261.
ModBase	Search...
Protein-protein interaction databases
IntAct	P63261. 33 interactions.
MINT	MINT-4998686.
STRING	9606.ENSP00000331514.
PTM databases
PhosphoSite	P63261.
Polymorphism databases
DMDM	54036678.
2D gel databases
DOSAC-COBS-2DPAGE	P60709_OR_P63261. P63261.
OGP	P63261.
REPRODUCTION-2DPAGE	P63261.
SWISS-2DPAGE	P63261.
Proteomic databases
PRIDE	P63261.
Protocols and materials databases
DNASU	71.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000331925; 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.
GeneID	71.
KEGG	hsa:71.
UCSC	uc002kak.2. human.
Organism-specific databases
CTD	71.
GeneCards	GC17M079476.
H-InvDB	HIX0001479. HIX0199868.
HGNC	HGNC:144. ACTG1.
HPA	CAB013531. HPA041264. HPA041271.
MIM	102560. gene. 604717. phenotype. 614583. phenotype.
neXtProt	NX_P63261.
Orphanet	90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA. 2995. Iris coloboma with ptosis - intellectual deficit.
PharmGKB	PA24468.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG003771.
InParanoid	P63261.
KO	K05692.
OMA	ADTEDIQ.
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-related. IPR020902. Actin/actin-like_CS. IPR004001. Actin_CS. [Graphical view]
PANTHER	PTHR11937. PTHR11937. 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
ChiTaRS	ACTG1. human.
GenomeRNAi	71.
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:	May 1, 2013
This is version 112 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.