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P63261

- ACTG_HUMAN

UniProt

P63261 - ACTG_HUMAN

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Protein
Actin, cytoplasmic 2
Gene
ACTG1, ACTB, ACTG
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. identical protein binding Source: IntAct
  3. protein binding Source: IntAct
  4. structural constituent of cytoskeleton Source: UniProtKB

GO - Biological processi

  1. Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  2. adherens junction organization Source: Reactome
  3. axon guidance Source: Reactome
  4. cell junction assembly Source: Reactome
  5. cell-cell junction organization Source: Reactome
  6. cellular component movement Source: UniProtKB
  7. innate immune response Source: Reactome
  8. membrane organization Source: Reactome
  9. retina homeostasis Source: UniProt
  10. sarcomere organization Source: Ensembl
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_11035. Gap junction degradation.
REACT_11049. Formation of annular gap junctions.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19195. Adherens junctions interactions.
REACT_20649. Cell-extracellular matrix interactions.
REACT_22266. Interaction between L1 and Ankyrins.
REACT_22365. Recycling pathway of L1.
SignaLinkiP63261.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 2
Alternative name(s):
Gamma-actin
Cleaved into the following chain:
Gene namesi
Name:ACTG1
Synonyms:ACTB, ACTG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 17

Organism-specific databases

HGNCiHGNC:144. ACTG1.

Subcellular locationi

GO - Cellular componenti

  1. blood microparticle Source: UniProt
  2. cytoskeleton Source: UniProtKB
  3. cytosol Source: Reactome
  4. extracellular space Source: UniProt
  5. extracellular vesicular exosome Source: UniProtKB
  6. filamentous actin Source: Ensembl
  7. myofibril Source: Ensembl
  8. nucleus Source: UniProt
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

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.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891T → I in DFNA20. 1 Publication
Corresponds to variant rs28999111 [ dbSNP | Ensembl ].
VAR_032434
Natural varianti118 – 1181K → M in DFNA20. 1 Publication
VAR_032435
Natural varianti118 – 1181K → N in DFNA20. 1 Publication
Corresponds to variant rs267606630 [ dbSNP | Ensembl ].
VAR_067824
Natural varianti122 – 1221I → V in DFNA20. 1 Publication
Corresponds to variant rs281875330 [ dbSNP | Ensembl ].
VAR_067825
Natural varianti241 – 2411E → K in DFNA20. 1 Publication
Corresponds to variant rs267606631 [ dbSNP | Ensembl ].
VAR_067826
Natural varianti264 – 2641P → L in DFNA20. 1 Publication
VAR_032436
Natural varianti278 – 2781T → I in DFNA20. 1 Publication
Corresponds to variant rs28999112 [ dbSNP | Ensembl ].
VAR_032437
Natural varianti332 – 3321P → A in DFNA20. 1 Publication
VAR_032438
Natural varianti370 – 3701V → A in DFNA20; restricts cell growth at elevated temperature or under hyperosmolar stress as measured in growth assays with yeast expressing the mutation. 1 Publication
VAR_032439
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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti120 – 1201T → I in BRWS2. 1 Publication
Corresponds to variant rs281875325 [ dbSNP | Ensembl ].
VAR_067814
Natural varianti135 – 1351A → V in BRWS2. 1 Publication
Corresponds to variant rs11549190 [ dbSNP | Ensembl ].
VAR_067815
Natural varianti155 – 1551S → F in BRWS2. 1 Publication
Corresponds to variant rs281875326 [ dbSNP | Ensembl ].
VAR_067816
Natural varianti203 – 2031T → K in BRWS2. 1 Publication
Corresponds to variant rs281875327 [ dbSNP | Ensembl ].
VAR_067817
Natural varianti254 – 2541R → W in BRWS2. 1 Publication
Corresponds to variant rs281875328 [ dbSNP | Ensembl ].
VAR_067818
Natural varianti256 – 2561R → W in BRWS2. 1 Publication
Corresponds to variant rs281875329 [ dbSNP | Ensembl ].
VAR_067819

Keywords - Diseasei

Deafness, Disease mutation, Mental retardation, Non-syndromic deafness

Organism-specific databases

MIMi604717. phenotype.
614583. phenotype.
Orphaneti90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
2995. Baraitser-Winter syndrome.
PharmGKBiPA24468.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 2
PRO_0000367100Add
BLAST
Initiator methioninei1 – 11Removed; alternate3 Publications
Chaini2 – 375374Actin, cytoplasmic 2, N-terminally processed
PRO_0000000831Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei2 – 21N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed; partial4 Publications
Modified residuei44 – 441Methionine (R)-sulfoxide By similarity
Modified residuei47 – 471Methionine (R)-sulfoxide By similarity
Modified residuei73 – 731Tele-methylhistidine1 Publication
Modified residuei84 – 841N6-methyllysine1 Publication

Post-translational modificationi

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.

Keywords - PTMi

Acetylation, Methylation, Oxidation

Proteomic databases

MaxQBiP63261.
PRIDEiP63261.

2D gel databases

DOSAC-COBS-2DPAGEP60709_OR_P63261.
P63261.
OGPiP63261.
REPRODUCTION-2DPAGEP63261.
SWISS-2DPAGEP63261.

PTM databases

PhosphoSiteiP63261.

Miscellaneous databases

PMAP-CutDBP63261.

Expressioni

Gene expression databases

BgeeiP63261.
CleanExiHS_ACTB.
HS_ACTG1.
GenevestigatoriP63261.

Organism-specific databases

HPAiCAB013531.
HPA041264.
HPA041271.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-351292,EBI-351292
ACTBP607093EBI-351292,EBI-353944
CFL2Q9Y2812EBI-351292,EBI-351218
MLH1P406927EBI-351292,EBI-744248

Protein-protein interaction databases

BioGridi106586. 91 interactions.
IntActiP63261. 38 interactions.
MINTiMINT-4998686.
STRINGi9606.ENSP00000331514.

Structurei

3D structure databases

ProteinModelPortaliP63261.
SMRiP63261. Positions 6-375.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.

Phylogenomic databases

HOVERGENiHBG003771.
InParanoidiP63261.
KOiK05692.
OMAiDARAPIM.
PhylomeDBiP63261.
TreeFamiTF354237.

Family and domain databases

InterProiIPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P63261-1 [UniParc]FASTAAdd to Basket

« Hide

MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK    50
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE 100
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG 150
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF 200
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI 250
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS 300
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS 350
TFQQMWISKQ EYDESGPSIV HRKCF 375
Length:375
Mass (Da):41,793
Last modified:July 21, 1986 - v1
Checksum:i54D08F986964EFD5
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti89 – 891T → I in DFNA20. 1 Publication
Corresponds to variant rs28999111 [ dbSNP | Ensembl ].
VAR_032434
Natural varianti118 – 1181K → M in DFNA20. 1 Publication
VAR_032435
Natural varianti118 – 1181K → N in DFNA20. 1 Publication
Corresponds to variant rs267606630 [ dbSNP | Ensembl ].
VAR_067824
Natural varianti120 – 1201T → I in BRWS2. 1 Publication
Corresponds to variant rs281875325 [ dbSNP | Ensembl ].
VAR_067814
Natural varianti122 – 1221I → V in DFNA20. 1 Publication
Corresponds to variant rs281875330 [ dbSNP | Ensembl ].
VAR_067825
Natural varianti135 – 1351A → V in BRWS2. 1 Publication
Corresponds to variant rs11549190 [ dbSNP | Ensembl ].
VAR_067815
Natural varianti155 – 1551S → F in BRWS2. 1 Publication
Corresponds to variant rs281875326 [ dbSNP | Ensembl ].
VAR_067816
Natural varianti160 – 1601T → I.
Corresponds to variant rs11549206 [ dbSNP | Ensembl ].
VAR_048186
Natural varianti203 – 2031T → K in BRWS2. 1 Publication
Corresponds to variant rs281875327 [ dbSNP | Ensembl ].
VAR_067817
Natural varianti241 – 2411E → K in DFNA20. 1 Publication
Corresponds to variant rs267606631 [ dbSNP | Ensembl ].
VAR_067826
Natural varianti243 – 2431P → L.
Corresponds to variant rs11546899 [ dbSNP | Ensembl ].
VAR_055482
Natural varianti254 – 2541R → W in BRWS2. 1 Publication
Corresponds to variant rs281875328 [ dbSNP | Ensembl ].
VAR_067818
Natural varianti256 – 2561R → W in BRWS2. 1 Publication
Corresponds to variant rs281875329 [ dbSNP | Ensembl ].
VAR_067819
Natural varianti264 – 2641P → L in DFNA20. 1 Publication
VAR_032436
Natural varianti278 – 2781T → I in DFNA20. 1 Publication
Corresponds to variant rs28999112 [ dbSNP | Ensembl ].
VAR_032437
Natural varianti332 – 3321P → A in DFNA20. 1 Publication
VAR_032438
Natural varianti370 – 3701V → A in DFNA20; restricts cell growth at elevated temperature or under hyperosmolar stress as measured in growth assays with yeast expressing the mutation. 1 Publication
VAR_032439

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti316 – 3161E → K in AAA51580. 1 Publication
Sequence conflicti344 – 3441S → F in AAA51580. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS11782.1.
PIRiA28098. ATHUG.
JC5818.
RefSeqiNP_001186883.1. NM_001199954.1.
NP_001605.1. NM_001614.3.
UniGeneiHs.514581.
Hs.713764.

Genome annotation databases

EnsembliENST00000331925; 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.
GeneIDi71.
KEGGihsa:71.
UCSCiuc002kak.2. human.

Polymorphism databases

DMDMi54036678.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Mendelian genes actin, gamma 1 (ACTG1)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS11782.1.
PIRi A28098. ATHUG.
JC5818.
RefSeqi NP_001186883.1. NM_001199954.1.
NP_001605.1. NM_001614.3.
UniGenei Hs.514581.
Hs.713764.

3D structure databases

ProteinModelPortali P63261.
SMRi P63261. Positions 6-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106586. 91 interactions.
IntActi P63261. 38 interactions.
MINTi MINT-4998686.
STRINGi 9606.ENSP00000331514.

PTM databases

PhosphoSitei P63261.

Polymorphism databases

DMDMi 54036678.

2D gel databases

DOSAC-COBS-2DPAGE P60709_OR_P63261.
P63261.
OGPi P63261.
REPRODUCTION-2DPAGE P63261.
SWISS-2DPAGE P63261.

Proteomic databases

MaxQBi P63261.
PRIDEi P63261.

Protocols and materials databases

DNASUi 71.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli 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 .
GeneIDi 71.
KEGGi hsa:71.
UCSCi uc002kak.2. human.

Organism-specific databases

CTDi 71.
GeneCardsi GC17M079476.
GeneReviewsi ACTG1.
H-InvDB HIX0001479.
HIX0199868.
HGNCi HGNC:144. ACTG1.
HPAi CAB013531.
HPA041264.
HPA041271.
MIMi 102560. gene.
604717. phenotype.
614583. phenotype.
neXtProti NX_P63261.
Orphaneti 90635. Autosomal dominant nonsyndromic sensorineural deafness type DFNA.
2995. Baraitser-Winter syndrome.
PharmGKBi PA24468.
GenAtlasi Search...

Phylogenomic databases

HOVERGENi HBG003771.
InParanoidi P63261.
KOi K05692.
OMAi DARAPIM.
PhylomeDBi P63261.
TreeFami TF354237.

Enzyme and pathway databases

Reactomei REACT_11035. Gap junction degradation.
REACT_11049. Formation of annular gap junctions.
REACT_147867. Translocation of GLUT4 to the plasma membrane.
REACT_160086. Regulation of actin dynamics for phagocytic cup formation.
REACT_19195. Adherens junctions interactions.
REACT_20649. Cell-extracellular matrix interactions.
REACT_22266. Interaction between L1 and Ankyrins.
REACT_22365. Recycling pathway of L1.
SignaLinki P63261.

Miscellaneous databases

ChiTaRSi ACTG1. human.
GeneWikii ACTG1.
GenomeRNAii 71.
NextBioi 279.
PMAP-CutDB P63261.
PROi P63261.
SOURCEi Search...

Gene expression databases

Bgeei P63261.
CleanExi HS_ACTB.
HS_ACTG1.
Genevestigatori P63261.

Family and domain databases

InterProi IPR004000. Actin-related.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
[Graphical view ]
PANTHERi PTHR11937. PTHR11937. 1 hit.
Pfami PF00022. Actin. 1 hit.
[Graphical view ]
PRINTSi PR00190. ACTIN.
SMARTi SM00268. ACTIN. 1 hit.
[Graphical view ]
PROSITEi PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma.
  8. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND GLU-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. 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. Cited for: VARIANTS BRWS2 ILE-120; VAL-135; PHE-155; LYS-203; TRP-254 AND TRP-256.

Entry informationi

Entry nameiACTG_HUMAN
AccessioniPrimary (citable) accession number: P63261
Secondary accession number(s): A8K7C2
, P02571, P14104, P99022, Q5U032, Q96E67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: September 3, 2014
This is version 126 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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