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P63260

- ACTG_MOUSE

UniProt

P63260 - ACTG_MOUSE

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Protein

Actin, cytoplasmic 2

Gene

Actg1

Organism
Mus musculus (Mouse)
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. structural constituent of cytoskeleton Source: MGI

GO - Biological processi

  1. retina homeostasis Source: Ensembl
  2. sarcomere organization Source: MGI
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_209040. Gap junction degradation.
REACT_220352. Formation of annular gap junctions.
REACT_230395. Adherens junctions interactions.
REACT_243772. Cell-extracellular matrix interactions.
REACT_244931. Interaction between L1 and Ankyrins.
REACT_257088. VEGFA-VEGFR2 Pathway.
REACT_257656. EPHB-mediated forward signaling.
REACT_257923. Recycling pathway of L1.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 2
Alternative name(s):
Gamma-actin
Cleaved into the following chain:
Gene namesi
Name:Actg1
Synonyms:Actg
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:87906. Actg1.

Subcellular locationi

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 2PRO_0000367101Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 375374Actin, cytoplasmic 2, N-terminally processedPRO_0000000833Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylglutamate; in Actin, cytoplasmic 2, N-terminally processed1 Publication
Modified residuei44 – 441Methionine (R)-sulfoxide1 Publication
Modified residuei47 – 471Methionine (R)-sulfoxide1 Publication
Modified residuei73 – 731Tele-methylhistidine1 Publication
Modified residuei84 – 841N6-methyllysineBy similarity

Post-translational modificationi

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.1 Publication
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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Oxidation

Proteomic databases

MaxQBiP63260.
PRIDEiP63260.

2D gel databases

COMPLUYEAST-2DPAGEP63260.
REPRODUCTION-2DPAGEP63260.
UCD-2DPAGEP63260.

PTM databases

PhosphoSiteiP63260.

Miscellaneous databases

PMAP-CutDBP63260.

Expressioni

Gene expression databases

BgeeiP63260.
CleanExiMM_ACTG1.
ExpressionAtlasiP63260. baseline and differential.
GenevestigatoriP63260.

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
Kcnma1Q084604EBI-351301,EBI-1633915

Protein-protein interaction databases

BioGridi197946. 19 interactions.
IntActiP63260. 25 interactions.

Structurei

3D structure databases

ProteinModelPortaliP63260.
SMRiP63260. Positions 6-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP63260.
KOiK05692.
OMAiDARAPIM.
OrthoDBiEOG72RMZ1.
PhylomeDBiP63260.
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.

P63260-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEEEIAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
HPVLLTEAPL NPKANREKMT QIMFETFNTP AMYVAIQAVL SLYASGRTTG
160 170 180 190 200
IVMDSGDGVT HTVPIYEGYA LPHAILRLDL AGRDLTDYLM KILTERGYSF
210 220 230 240 250
TTTAEREIVR DIKEKLCYVA LDFEQEMATA ASSSSLEKSY ELPDGQVITI
260 270 280 290 300
GNERFRCPEA LFQPSFLGME SCGIHETTFN SIMKCDVDIR KDLYANTVLS
310 320 330 340 350
GGTTMYPGIA DRMQKEITAL APSTMKIKII APPERKYSVW IGGSILASLS
360 370
TFQQMWISKQ EYDESGPSIV HRKCF
Length:375
Mass (Da):41,793
Last modified:July 21, 1986 - v1
Checksum:i54D08F986964EFD5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13055 mRNA. Translation: CAA31455.1.
AK076081 mRNA. Translation: BAC36167.1.
AK087983 mRNA. Translation: BAC40075.1.
BC003337 mRNA. Translation: AAH03337.1.
BC021796 mRNA. Translation: AAH21796.1.
BC023248 mRNA. Translation: AAH23248.1.
M21495 mRNA. Translation: AAA37168.1.
CCDSiCCDS25730.1.
PIRiA30243. ATMSG.
RefSeqiNP_033739.1. NM_009609.2.
UniGeneiMm.196173.
Mm.426706.
Mm.470166.

Genome annotation databases

EnsembliENSMUST00000071555; ENSMUSP00000071486; ENSMUSG00000062825.
ENSMUST00000106215; ENSMUSP00000101822; ENSMUSG00000062825.
GeneIDi11465.
KEGGimmu:11465.
UCSCiuc007msi.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13055 mRNA. Translation: CAA31455.1 .
AK076081 mRNA. Translation: BAC36167.1 .
AK087983 mRNA. Translation: BAC40075.1 .
BC003337 mRNA. Translation: AAH03337.1 .
BC021796 mRNA. Translation: AAH21796.1 .
BC023248 mRNA. Translation: AAH23248.1 .
M21495 mRNA. Translation: AAA37168.1 .
CCDSi CCDS25730.1.
PIRi A30243. ATMSG.
RefSeqi NP_033739.1. NM_009609.2.
UniGenei Mm.196173.
Mm.426706.
Mm.470166.

3D structure databases

ProteinModelPortali P63260.
SMRi P63260. Positions 6-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 197946. 19 interactions.
IntActi P63260. 25 interactions.

PTM databases

PhosphoSitei P63260.

2D gel databases

COMPLUYEAST-2DPAGE P63260.
REPRODUCTION-2DPAGE P63260.
UCD-2DPAGE P63260.

Proteomic databases

MaxQBi P63260.
PRIDEi P63260.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000071555 ; ENSMUSP00000071486 ; ENSMUSG00000062825 .
ENSMUST00000106215 ; ENSMUSP00000101822 ; ENSMUSG00000062825 .
GeneIDi 11465.
KEGGi mmu:11465.
UCSCi uc007msi.1. mouse.

Organism-specific databases

CTDi 71.
MGIi MGI:87906. Actg1.

Phylogenomic databases

HOGENOMi HOG000233340.
HOVERGENi HBG003771.
InParanoidi P63260.
KOi K05692.
OMAi DARAPIM.
OrthoDBi EOG72RMZ1.
PhylomeDBi P63260.
TreeFami TF354237.

Enzyme and pathway databases

Reactomei REACT_198374. Regulation of actin dynamics for phagocytic cup formation.
REACT_199054. Translocation of GLUT4 to the plasma membrane.
REACT_209040. Gap junction degradation.
REACT_220352. Formation of annular gap junctions.
REACT_230395. Adherens junctions interactions.
REACT_243772. Cell-extracellular matrix interactions.
REACT_244931. Interaction between L1 and Ankyrins.
REACT_257088. VEGFA-VEGFR2 Pathway.
REACT_257656. EPHB-mediated forward signaling.
REACT_257923. Recycling pathway of L1.

Miscellaneous databases

ChiTaRSi Actg1. mouse.
NextBioi 278792.
PMAP-CutDB P63260.
PROi P63260.
SOURCEi Search...

Gene expression databases

Bgeei P63260.
CleanExi MM_ACTG1.
ExpressionAtlasi P63260. baseline and differential.
Genevestigatori P63260.

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. "Actin amino-acid sequences. Comparison of actins from calf thymus, bovine brain, and SV40-transformed mouse 3T3 cells with rabbit skeletal muscle actin."
    Vandekerckhove J., Weber K.
    Eur. J. Biochem. 90:451-462(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-375, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT GLU-2, METHYLATION AT HIS-73.
  2. "Isolation of cDNA clones for mouse cytoskeletal gamma-actin and differential expression of cytoskeletal actin mRNAs in mouse cells."
    Tokunaga K., Takeda K., Kamiyama K., Kageyama H., Takenaga K., Sakiyama S.
    Mol. Cell. Biol. 8:3929-3933(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Thymus.
  4. "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].
    Strain: FVB/N and NMRI.
    Tissue: Colon and Mammary tumor.
  5. "Mouse cytoskeletal gamma-actin: analysis and implications of the structure of cloned cDNA and processed pseudogenes."
    Peter B., Man Y.M., Begg C.E., Gall I., Leader D.P.
    J. Mol. Biol. 203:665-675(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 8-375.
  6. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 29-39.
    Tissue: Brain.
  7. "MsrB1 and MICALs regulate actin assembly and macrophage function via reversible stereoselective methionine oxidation."
    Lee B.C., Peterfi Z., Hoffmann F.W., Moore R.E., Kaya A., Avanesov A., Tarrago L., Zhou Y., Weerapana E., Fomenko D.E., Hoffmann P.R., Gladyshev V.N.
    Mol. Cell 51:397-404(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: OXIDATION AT MET-44 AND MET-47, DEOXIDATION AT MET-44 AND MET-47.

Entry informationi

Entry nameiACTG_MOUSE
AccessioniPrimary (citable) accession number: P63260
Secondary accession number(s): P02571, P14104, P99022
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: November 26, 2014
This is version 105 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3