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Protein

Actin, alpha skeletal muscle

Gene

ACTA1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed-Annotation score: 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

  • ATP binding Source: UniProtKB-KW
  • calcium-dependent protein binding Source: AgBase
  • identical protein binding Source: IntAct

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Muscle protein

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, alpha skeletal muscle
Alternative name(s):
Alpha-actin-1
Gene namesi
Name:ACTA1
Synonyms:ACTA
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature form2 PublicationsPRO_0000000850
Chaini3 – 377375Actin, alpha skeletal musclePRO_0000000851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylaspartate
Modified residuei63 – 631N6-malonyllysineBy similarity
Modified residuei75 – 751Tele-methylhistidineBy similarity
Modified residuei86 – 861N6-methyllysineBy similarity
Modified residuei179 – 1791ADP-ribosylarginine; by SpvB1 Publication

Post-translational modificationi

Can be mono-ADP-ribosylated on Arg-179 by SpvB of Salmonella spp. This modification blocks subsequent polymerization and leads to cell death.
Monomethylation at Lys-86 (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, ADP-ribosylation, Methylation

Proteomic databases

PRIDEiP68135.

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. Interacts with TTID. Interacts (via its C-terminus) with USP25 (By similarity). Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself5EBI-367540,EBI-367540
Q05193-55EBI-367540,EBI-8446026From a different organism.
ARP8Q123862EBI-367540,EBI-2967From a different organism.
CNN1P269325EBI-367540,EBI-8602797From a different organism.
Mkl1Q8K4J615EBI-367540,EBI-8291665From a different organism.

Protein-protein interaction databases

DIPiDIP-29021N.
IntActiP68135. 29 interactions.
MINTiMINT-1489367.
STRINGi9986.ENSOCUP00000006542.

Structurei

Secondary structure

1
377
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 85Combined sources
Beta strandi10 – 145Combined sources
Beta strandi16 – 238Combined sources
Beta strandi26 – 283Combined sources
Beta strandi30 – 345Combined sources
Beta strandi37 – 404Combined sources
Turni42 – 443Combined sources
Beta strandi45 – 484Combined sources
Beta strandi49 – 513Combined sources
Beta strandi54 – 563Combined sources
Helixi57 – 626Combined sources
Helixi64 – 663Combined sources
Beta strandi67 – 704Combined sources
Beta strandi72 – 743Combined sources
Helixi81 – 9313Combined sources
Turni94 – 963Combined sources
Helixi100 – 1023Combined sources
Beta strandi105 – 1095Combined sources
Helixi115 – 12713Combined sources
Beta strandi132 – 1387Combined sources
Helixi139 – 1468Combined sources
Beta strandi150 – 1578Combined sources
Beta strandi158 – 1603Combined sources
Beta strandi162 – 1687Combined sources
Helixi174 – 1763Combined sources
Beta strandi178 – 1803Combined sources
Helixi184 – 19613Combined sources
Turni197 – 1993Combined sources
Helixi205 – 21814Combined sources
Helixi225 – 23410Combined sources
Beta strandi236 – 2383Combined sources
Beta strandi240 – 2434Combined sources
Beta strandi245 – 2473Combined sources
Beta strandi249 – 2535Combined sources
Helixi255 – 26410Combined sources
Helixi266 – 2694Combined sources
Helixi276 – 28510Combined sources
Helixi289 – 2913Combined sources
Helixi292 – 2965Combined sources
Beta strandi299 – 3035Combined sources
Helixi304 – 3063Combined sources
Beta strandi308 – 3103Combined sources
Helixi311 – 32212Combined sources
Helixi324 – 3263Combined sources
Helixi337 – 3393Combined sources
Helixi340 – 35011Combined sources
Helixi352 – 3576Combined sources
Beta strandi358 – 3603Combined sources
Helixi361 – 3677Combined sources
Helixi368 – 3703Combined sources
Helixi371 – 3755Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-V/W/X/Y/Z3-374[»]
1ATNX-ray2.80A3-374[»]
1EQYX-ray2.30A1-377[»]
1ESVX-ray2.00A1-377[»]
1H1VX-ray3.00A3-377[»]
1IJJX-ray2.85A/B1-377[»]
1J6ZX-ray1.54A3-377[»]
1KXPX-ray2.10A3-377[»]
1LCUX-ray3.50A/B7-377[»]
1LOTX-ray2.50B3-377[»]
1M8Qelectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1MA9X-ray2.40B3-377[»]
1MVWelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1NWKX-ray1.85A3-377[»]
1O18electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O19electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Aelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Belectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Celectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Delectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Eelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Felectron microscopy70.000/1/2/3/4/5/6/7/8/V/W/X/Y/Z3-377[»]
1O1Gelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1P8ZX-ray2.60A1-377[»]
1QZ5X-ray1.45A3-377[»]
1QZ6X-ray1.60A3-377[»]
1RDWX-ray2.30X3-377[»]
1RFQX-ray3.00A/B3-377[»]
1RGIX-ray3.00A1-377[»]
1S22X-ray1.60A3-377[»]
1SQKX-ray2.50A1-377[»]
1T44X-ray2.00A8-377[»]
1UY5model-A3-374[»]
1WUAX-ray1.45A3-377[»]
1Y64X-ray3.05A3-377[»]
1YXQX-ray2.01A/B3-377[»]
2A3ZX-ray2.08A3-377[»]
2A40X-ray1.80A/D3-377[»]
2A41X-ray2.60A3-377[»]
2A42X-ray1.85A3-377[»]
2A5XX-ray2.49A3-377[»]
2ASMX-ray1.60A3-377[»]
2ASOX-ray1.70A3-377[»]
2ASPX-ray1.64A3-377[»]
2D1KX-ray2.50A3-377[»]
2FF3X-ray2.00B3-377[»]
2FF6X-ray2.05A3-377[»]
2FXUX-ray1.35A3-377[»]
2GWJX-ray1.90A7-377[»]
2GWKX-ray2.00A/B7-377[»]
2HMPX-ray1.90A/B3-377[»]
2PAVX-ray1.80A3-377[»]
2PBDX-ray1.50A1-377[»]
2Q0RX-ray1.70A3-377[»]
2Q0UX-ray1.45A3-377[»]
2Q1NX-ray2.70A/B3-377[»]
2Q31X-ray2.70A/B3-377[»]
2Q36X-ray2.50A3-377[»]
2Q97X-ray2.50A3-377[»]
2V51X-ray2.35B/D1-377[»]
2V52X-ray1.45B1-377[»]
2VCPX-ray3.20A/B3-377[»]
2VYPX-ray2.35A/B1-377[»]
2W49electron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2W4Uelectron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2Y83electron microscopy22.90O/P/Q/R/S/T3-377[»]
2YJEX-ray3.10A/B/C1-377[»]
2YJFX-ray3.50A/B/C/D/E1-377[»]
2ZWHfiber diffraction3.30A3-377[»]
3B5Uelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L/M/N1-377[»]
3BUZX-ray2.81B3-377[»]
3CJBX-ray3.21A1-377[»]
3CJCX-ray3.90A1-377[»]
3DAWX-ray2.55A1-377[»]
3FFKX-ray3.00B/E1-377[»]
3G37electron microscopy-O/P/Q/R/S/T/U/V/W/X/Y/Z3-377[»]
3HBTX-ray2.70A3-377[»]
3J4Kelectron microscopy8.00A/B/C/D/E3-377[»]
3J8Aelectron microscopy3.70A/B/C/D/E3-377[»]
3J8Ielectron microscopy4.70D/E/F/G/H1-377[»]
3J8Jelectron microscopy12.00A/B/C/D/E/F/G/H/I/J/K1-377[»]
3J8Kelectron microscopy12.00A/B/C/D/E/F/G/H/I/J1-377[»]
3M1FX-ray2.89A3-377[»]
3M3NX-ray7.00A/B3-377[»]
3M6GX-ray2.00A/B3-373[»]
3MFPelectron microscopy-A3-377[»]
3MN5X-ray1.50A3-377[»]
3SJHX-ray1.75A3-377[»]
3TPQX-ray3.45A/B/C/D/E3-377[»]
3TU5X-ray3.00A1-377[»]
3U8XX-ray2.00A/C3-377[»]
3U9ZX-ray2.09A3-377[»]
3UE5X-ray2.76A3-377[»]
4A7Felectron microscopy7.70A/D/E/F/I3-377[»]
4A7Helectron microscopy7.80A/D/E/F/G3-377[»]
4A7Lelectron microscopy8.10A/D/E/F/I3-377[»]
4A7Nelectron microscopy8.90A/B/C/D/E3-377[»]
4B1VX-ray1.75A/B2-377[»]
4B1WX-ray1.95B2-377[»]
4B1XX-ray1.80B2-377[»]
4B1YX-ray1.29B2-377[»]
4B1ZX-ray3.30A/B/C/D/E/F2-377[»]
4EAHX-ray3.40D/F/G/H1-377[»]
4GY2X-ray2.71B3-377[»]
4H03X-ray1.75B3-377[»]
4H0TX-ray2.20B3-377[»]
4H0VX-ray2.03B3-377[»]
4H0XX-ray2.33B3-377[»]
4H0YX-ray1.94B3-377[»]
4K41X-ray1.40A3-377[»]
4K42X-ray2.90A/B/C/D3-377[»]
4K43X-ray2.90A/B3-377[»]
4PKGX-ray1.80A1-377[»]
4PKHX-ray2.15A/D/F/I1-377[»]
4PKIX-ray2.30A1-377[»]
4PL8X-ray2.00A/B3-377[»]
4V0UX-ray7.88A/B/C/L/M3-377[»]
ProteinModelPortaliP68135.
SMRiP68135. Positions 6-377.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP68135.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiCOG5277.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68135.

Family and domain databases

InterProiIPR004000. Actin.
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.

P68135-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG
60 70 80 90 100
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP
110 120 130 140 150
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT
160 170 180 190 200
TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY
210 220 230 240 250
SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI
260 270 280 290 300
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV
310 320 330 340 350
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS
360 370
LSTFQQMWIT KQEYDEAGPS IVHRKCF
Length:377
Mass (Da):42,051
Last modified:July 21, 1986 - v1
Checksum:iDF2A3A046346A179
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00872 mRNA. Translation: CAA24241.1.
V00873 mRNA. Translation: CAA24242.1.
V00874 mRNA. Translation: CAA24243.1.
PIRiA92182. ATRB.
I46471.
I46472.
I46473.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
V00872 mRNA. Translation: CAA24241.1.
V00873 mRNA. Translation: CAA24242.1.
V00874 mRNA. Translation: CAA24243.1.
PIRiA92182. ATRB.
I46471.
I46472.
I46473.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ALMmodel-V/W/X/Y/Z3-374[»]
1ATNX-ray2.80A3-374[»]
1EQYX-ray2.30A1-377[»]
1ESVX-ray2.00A1-377[»]
1H1VX-ray3.00A3-377[»]
1IJJX-ray2.85A/B1-377[»]
1J6ZX-ray1.54A3-377[»]
1KXPX-ray2.10A3-377[»]
1LCUX-ray3.50A/B7-377[»]
1LOTX-ray2.50B3-377[»]
1M8Qelectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1MA9X-ray2.40B3-377[»]
1MVWelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1NWKX-ray1.85A3-377[»]
1O18electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O19electron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Aelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Belectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Celectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Delectron microscopy70.000/1/2/3/4/5/7/8/9/V/W/X/Y/Z3-377[»]
1O1Eelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1O1Felectron microscopy70.000/1/2/3/4/5/6/7/8/V/W/X/Y/Z3-377[»]
1O1Gelectron microscopy70.001/2/3/4/5/6/7/8/9/V/W/X/Y/Z3-377[»]
1P8ZX-ray2.60A1-377[»]
1QZ5X-ray1.45A3-377[»]
1QZ6X-ray1.60A3-377[»]
1RDWX-ray2.30X3-377[»]
1RFQX-ray3.00A/B3-377[»]
1RGIX-ray3.00A1-377[»]
1S22X-ray1.60A3-377[»]
1SQKX-ray2.50A1-377[»]
1T44X-ray2.00A8-377[»]
1UY5model-A3-374[»]
1WUAX-ray1.45A3-377[»]
1Y64X-ray3.05A3-377[»]
1YXQX-ray2.01A/B3-377[»]
2A3ZX-ray2.08A3-377[»]
2A40X-ray1.80A/D3-377[»]
2A41X-ray2.60A3-377[»]
2A42X-ray1.85A3-377[»]
2A5XX-ray2.49A3-377[»]
2ASMX-ray1.60A3-377[»]
2ASOX-ray1.70A3-377[»]
2ASPX-ray1.64A3-377[»]
2D1KX-ray2.50A3-377[»]
2FF3X-ray2.00B3-377[»]
2FF6X-ray2.05A3-377[»]
2FXUX-ray1.35A3-377[»]
2GWJX-ray1.90A7-377[»]
2GWKX-ray2.00A/B7-377[»]
2HMPX-ray1.90A/B3-377[»]
2PAVX-ray1.80A3-377[»]
2PBDX-ray1.50A1-377[»]
2Q0RX-ray1.70A3-377[»]
2Q0UX-ray1.45A3-377[»]
2Q1NX-ray2.70A/B3-377[»]
2Q31X-ray2.70A/B3-377[»]
2Q36X-ray2.50A3-377[»]
2Q97X-ray2.50A3-377[»]
2V51X-ray2.35B/D1-377[»]
2V52X-ray1.45B1-377[»]
2VCPX-ray3.20A/B3-377[»]
2VYPX-ray2.35A/B1-377[»]
2W49electron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2W4Uelectron microscopy35.00D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S3-374[»]
2Y83electron microscopy22.90O/P/Q/R/S/T3-377[»]
2YJEX-ray3.10A/B/C1-377[»]
2YJFX-ray3.50A/B/C/D/E1-377[»]
2ZWHfiber diffraction3.30A3-377[»]
3B5Uelectron microscopy-A/B/C/D/E/F/G/H/I/J/K/L/M/N1-377[»]
3BUZX-ray2.81B3-377[»]
3CJBX-ray3.21A1-377[»]
3CJCX-ray3.90A1-377[»]
3DAWX-ray2.55A1-377[»]
3FFKX-ray3.00B/E1-377[»]
3G37electron microscopy-O/P/Q/R/S/T/U/V/W/X/Y/Z3-377[»]
3HBTX-ray2.70A3-377[»]
3J4Kelectron microscopy8.00A/B/C/D/E3-377[»]
3J8Aelectron microscopy3.70A/B/C/D/E3-377[»]
3J8Ielectron microscopy4.70D/E/F/G/H1-377[»]
3J8Jelectron microscopy12.00A/B/C/D/E/F/G/H/I/J/K1-377[»]
3J8Kelectron microscopy12.00A/B/C/D/E/F/G/H/I/J1-377[»]
3M1FX-ray2.89A3-377[»]
3M3NX-ray7.00A/B3-377[»]
3M6GX-ray2.00A/B3-373[»]
3MFPelectron microscopy-A3-377[»]
3MN5X-ray1.50A3-377[»]
3SJHX-ray1.75A3-377[»]
3TPQX-ray3.45A/B/C/D/E3-377[»]
3TU5X-ray3.00A1-377[»]
3U8XX-ray2.00A/C3-377[»]
3U9ZX-ray2.09A3-377[»]
3UE5X-ray2.76A3-377[»]
4A7Felectron microscopy7.70A/D/E/F/I3-377[»]
4A7Helectron microscopy7.80A/D/E/F/G3-377[»]
4A7Lelectron microscopy8.10A/D/E/F/I3-377[»]
4A7Nelectron microscopy8.90A/B/C/D/E3-377[»]
4B1VX-ray1.75A/B2-377[»]
4B1WX-ray1.95B2-377[»]
4B1XX-ray1.80B2-377[»]
4B1YX-ray1.29B2-377[»]
4B1ZX-ray3.30A/B/C/D/E/F2-377[»]
4EAHX-ray3.40D/F/G/H1-377[»]
4GY2X-ray2.71B3-377[»]
4H03X-ray1.75B3-377[»]
4H0TX-ray2.20B3-377[»]
4H0VX-ray2.03B3-377[»]
4H0XX-ray2.33B3-377[»]
4H0YX-ray1.94B3-377[»]
4K41X-ray1.40A3-377[»]
4K42X-ray2.90A/B/C/D3-377[»]
4K43X-ray2.90A/B3-377[»]
4PKGX-ray1.80A1-377[»]
4PKHX-ray2.15A/D/F/I1-377[»]
4PKIX-ray2.30A1-377[»]
4PL8X-ray2.00A/B3-377[»]
4V0UX-ray7.88A/B/C/L/M3-377[»]
ProteinModelPortaliP68135.
SMRiP68135. Positions 6-377.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-29021N.
IntActiP68135. 29 interactions.
MINTiMINT-1489367.
STRINGi9986.ENSOCUP00000006542.

Proteomic databases

PRIDEiP68135.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

eggNOGiCOG5277.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiP68135.

Miscellaneous databases

EvolutionaryTraceiP68135.

Family and domain databases

InterProiIPR004000. Actin.
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]
ProtoNetiSearch...

Publicationsi

  1. "The primary structure of actin from rabbit skeletal muscle. Completion and analysis of the amino acid sequence."
    Collins J.H., Elzinga M.
    J. Biol. Chem. 250:5915-5920(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-377.
    Tissue: Skeletal muscle.
  2. "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: SEQUENCE REVISION TO 5; 7; 14 AND 75-81.
  3. "Partial amino acid sequence of brain actin and its homology with muscle actin."
    Lu R.C., Elzinga M.
    Biochemistry 16:5801-5806(1977) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  4. "A new troponin T and cDNA clones for 13 different muscle proteins, found by shotgun sequencing."
    Putney S.D., Herlihy W.C., Schimmel P.R.
    Nature 302:718-721(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 74-147; 194-283 AND 311-377.
  5. "The complete amino acid sequence of actins from bovine aorta, bovine heart, bovine fast skeletal muscle, and rabbit slow skeletal muscle. A protein-chemical analysis of muscle actin differentiation."
    Vandekerckhove J., Weber K.
    Differentiation 14:123-133(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 3-377.
    Tissue: Skeletal muscle.
  6. "Atomic structure of the actin:DNase I complex."
    Kabsch W., Mannherz H.G., Suck D., Pai E.F., Holmes K.C.
    Nature 347:37-44(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
  7. "Crystal structure of monomeric actin in the ATP state. Structural basis of nucleotide-dependent actin dynamics."
    Graceffa P., Dominguez R.
    J. Biol. Chem. 278:34172-34180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
  8. "Actin crystal dynamics: structural implications for F-actin nucleation, polymerization, and branching mediated by the anti-parallel dimer."
    Reutzel R., Yoshioka C., Govindasamy L., Yarmola E.G., Agbandje-McKenna M., Bubb M.R., McKenna R.
    J. Struct. Biol. 146:291-301(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 3-377 IN COMPLEX WITH ATP.
  9. "A steric antagonism of actin polymerization by a Salmonella virulence protein."
    Margarit S.M., Davidson W., Frego L., Stebbins C.E.
    Structure 14:1219-1229(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 7-377, ADP-RIBOSYLATION AT ARG-179 BY SPVB.
  10. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) IN COMPLEX WITH COBL; GSN AND TMSB4X, SUBUNIT.

Entry informationi

Entry nameiACTS_RABIT
AccessioniPrimary (citable) accession number: P68135
Secondary accession number(s): P02568, P99020
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: June 24, 2015
This is version 99 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.