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P68135

- ACTS_RABIT

UniProt

P68135 - ACTS_RABIT

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Protein

Actin, alpha skeletal muscle

Gene
ACTA1, ACTA
Organism
Oryctolagus cuniculus (Rabbit)
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. calcium-dependent protein binding Source: AgBase
  3. identical protein binding Source: IntAct
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. skeletal muscle fiber development Source: UniProtKB
  2. skeletal muscle thin filament assembly Source: UniProtKB
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: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. actin filament Source: UniProtKB
  2. stress fiber Source: UniProtKB
  3. striated muscle thin filament Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 22Removed in mature formPRO_0000000850
Chaini3 – 377375Actin, alpha skeletal musclePRO_0000000851Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei3 – 31N-acetylaspartate
Modified residuei63 – 631N6-malonyllysine By similarity
Modified residuei75 – 751Tele-methylhistidine
Modified residuei86 – 861N6-methyllysine By similarity
Modified residuei179 – 1791ADP-ribosylarginine; by SpvB Inferred

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.

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.1 Publication

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 – 85
Beta strandi10 – 145
Beta strandi16 – 238
Beta strandi26 – 283
Beta strandi30 – 345
Beta strandi37 – 404
Turni42 – 443
Beta strandi48 – 503
Beta strandi54 – 563
Helixi57 – 626
Helixi64 – 663
Beta strandi67 – 704
Beta strandi72 – 743
Helixi81 – 9313
Turni94 – 963
Helixi100 – 1023
Beta strandi105 – 1095
Helixi115 – 12713
Beta strandi132 – 1387
Helixi139 – 1468
Beta strandi150 – 1578
Beta strandi158 – 1603
Beta strandi162 – 1687
Helixi174 – 1763
Beta strandi178 – 1803
Helixi184 – 19613
Turni197 – 1993
Helixi205 – 21814
Helixi225 – 23410
Beta strandi236 – 2383
Beta strandi240 – 2434
Beta strandi245 – 2473
Beta strandi249 – 2535
Helixi255 – 26410
Helixi266 – 2694
Helixi276 – 28510
Helixi289 – 2913
Helixi292 – 2965
Beta strandi299 – 3035
Helixi304 – 3063
Beta strandi308 – 3103
Helixi311 – 32212
Helixi324 – 3263
Helixi337 – 3393
Helixi340 – 35011
Helixi352 – 3576
Beta strandi358 – 3603
Helixi361 – 3677
Helixi368 – 3703
Helixi371 – 3755

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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[»]
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[»]
ProteinModelPortaliP68135.
SMRiP68135. Positions 6-377.

Miscellaneous databases

EvolutionaryTraceiP68135.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.

Phylogenomic databases

eggNOGiCOG5277.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.

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.

P68135-1 [UniParc]FASTAAdd to Basket

« Hide

MCDEDETTAL VCDNGSGLVK AGFAGDDAPR AVFPSIVGRP RHQGVMVGMG    50
QKDSYVGDEA QSKRGILTLK YPIEHGIITN WDDMEKIWHH TFYNELRVAP 100
EEHPTLLTEA PLNPKANREK MTQIMFETFN VPAMYVAIQA VLSLYASGRT 150
TGIVLDSGDG VTHNVPIYEG YALPHAIMRL DLAGRDLTDY LMKILTERGY 200
SFVTTAEREI VRDIKEKLCY VALDFENEMA TAASSSSLEK SYELPDGQVI 250
TIGNERFRCP ETLFQPSFIG MESAGIHETT YNSIMKCDID IRKDLYANNV 300
MSGGTTMYPG IADRMQKEIT ALAPSTMKIK IIAPPERKYS VWIGGSILAS 350
LSTFQQMWIT KQEYDEAGPS IVHRKCF 377
Length:377
Mass (Da):42,051
Last modified:July 21, 1986 - v1
Checksum:iDF2A3A046346A179
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
V00872 mRNA. Translation: CAA24241.1 .
V00873 mRNA. Translation: CAA24242.1 .
V00874 mRNA. Translation: CAA24243.1 .
PIRi A92182. ATRB.
I46471.
I46472.
I46473.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1ALM model - V/W/X/Y/Z 3-374 [» ]
1ATN X-ray 2.80 A 3-374 [» ]
1EQY X-ray 2.30 A 1-377 [» ]
1ESV X-ray 2.00 A 1-377 [» ]
1H1V X-ray 3.00 A 3-377 [» ]
1IJJ X-ray 2.85 A/B 1-377 [» ]
1J6Z X-ray 1.54 A 3-377 [» ]
1KXP X-ray 2.10 A 3-377 [» ]
1LCU X-ray 3.50 A/B 7-377 [» ]
1LOT X-ray 2.50 B 3-377 [» ]
1M8Q electron microscopy 70.00 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z 3-377 [» ]
1MA9 X-ray 2.40 B 3-377 [» ]
1MVW electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1NWK X-ray 1.85 A 3-377 [» ]
1O18 electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O19 electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1A electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1B electron microscopy 70.00 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1C electron microscopy 70.00 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1D electron microscopy 70.00 0/1/2/3/4/5/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1E electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1O1F electron microscopy 70.00 0/1/2/3/4/5/6/7/8/V/W/X/Y/Z 3-377 [» ]
1O1G electron microscopy 70.00 1/2/3/4/5/6/7/8/9/V/W/X/Y/Z 3-377 [» ]
1P8Z X-ray 2.60 A 1-377 [» ]
1QZ5 X-ray 1.45 A 3-377 [» ]
1QZ6 X-ray 1.60 A 3-377 [» ]
1RDW X-ray 2.30 X 3-377 [» ]
1RFQ X-ray 3.00 A/B 3-377 [» ]
1RGI X-ray 3.00 A 1-377 [» ]
1S22 X-ray 1.60 A 3-377 [» ]
1SQK X-ray 2.50 A 1-377 [» ]
1T44 X-ray 2.00 A 8-377 [» ]
1UY5 model - A 3-374 [» ]
1WUA X-ray 1.45 A 3-377 [» ]
1Y64 X-ray 3.05 A 3-377 [» ]
1YXQ X-ray 2.01 A/B 3-377 [» ]
2A3Z X-ray 2.08 A 3-377 [» ]
2A40 X-ray 1.80 A/D 3-377 [» ]
2A41 X-ray 2.60 A 3-377 [» ]
2A42 X-ray 1.85 A 3-377 [» ]
2A5X X-ray 2.49 A 3-377 [» ]
2ASM X-ray 1.60 A 3-377 [» ]
2ASO X-ray 1.70 A 3-377 [» ]
2ASP X-ray 1.64 A 3-377 [» ]
2D1K X-ray 2.50 A 3-377 [» ]
2FF3 X-ray 2.00 B 3-377 [» ]
2FF6 X-ray 2.05 A 3-377 [» ]
2FXU X-ray 1.35 A 3-377 [» ]
2GWJ X-ray 1.90 A 7-377 [» ]
2GWK X-ray 2.00 A/B 7-377 [» ]
2HMP X-ray 1.90 A/B 3-377 [» ]
2PAV X-ray 1.80 A 3-377 [» ]
2PBD X-ray 1.50 A 1-377 [» ]
2Q0R X-ray 1.70 A 3-377 [» ]
2Q0U X-ray 1.45 A 3-377 [» ]
2Q1N X-ray 2.70 A/B 3-377 [» ]
2Q31 X-ray 2.70 A/B 3-377 [» ]
2Q36 X-ray 2.50 A 3-377 [» ]
2Q97 X-ray 2.50 A 3-377 [» ]
2V51 X-ray 2.35 B/D 1-377 [» ]
2V52 X-ray 1.45 B 1-377 [» ]
2VCP X-ray 3.20 A/B 3-377 [» ]
2VYP X-ray 2.35 A/B 1-377 [» ]
2W49 electron microscopy 35.00 D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S 3-374 [» ]
2W4U electron microscopy 35.00 D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S 3-374 [» ]
2Y83 electron microscopy 22.90 O/P/Q/R/S/T 3-377 [» ]
2YJE X-ray 3.10 A/B/C 1-377 [» ]
2YJF X-ray 3.50 A/B/C/D/E 1-377 [» ]
2ZWH fiber diffraction 3.30 A 3-377 [» ]
3B5U electron microscopy - A/B/C/D/E/F/G/H/I/J/K/L/M/N 1-377 [» ]
3BUZ X-ray 2.81 B 3-377 [» ]
3CJB X-ray 3.21 A 1-377 [» ]
3CJC X-ray 3.90 A 1-377 [» ]
3DAW X-ray 2.55 A 1-377 [» ]
3FFK X-ray 3.00 B/E 1-377 [» ]
3G37 electron microscopy - O/P/Q/R/S/T/U/V/W/X/Y/Z 3-377 [» ]
3HBT X-ray 2.70 A 3-377 [» ]
3J4K electron microscopy 8.00 A/B/C/D/E 3-377 [» ]
3M1F X-ray 2.89 A 3-377 [» ]
3M3N X-ray 7.00 A/B 3-377 [» ]
3M6G X-ray 2.00 A/B 3-373 [» ]
3MFP electron microscopy - A 3-377 [» ]
3MN5 X-ray 1.50 A 3-377 [» ]
3SJH X-ray 1.75 A 3-377 [» ]
3TPQ X-ray 3.45 A/B/C/D/E 3-377 [» ]
3TU5 X-ray 3.00 A 1-377 [» ]
3U8X X-ray 2.00 A/C 3-377 [» ]
3U9Z X-ray 2.09 A 3-377 [» ]
3UE5 X-ray 2.76 A 3-377 [» ]
4A7F electron microscopy 7.70 A/D/E/F/I 3-377 [» ]
4A7H electron microscopy 7.80 A/D/E/F/G 3-377 [» ]
4A7L electron microscopy 8.10 A/D/E/F/I 3-377 [» ]
4A7N electron microscopy 8.90 A/B/C/D/E 3-377 [» ]
4B1V X-ray 1.75 A/B 2-377 [» ]
4B1W X-ray 1.95 B 2-377 [» ]
4B1X X-ray 1.80 B 2-377 [» ]
4B1Y X-ray 1.29 B 2-377 [» ]
4B1Z X-ray 3.30 A/B/C/D/E/F 2-377 [» ]
4EAH X-ray 3.40 D/F/G/H 1-377 [» ]
4GY2 X-ray 2.71 B 3-377 [» ]
4H03 X-ray 1.75 B 3-377 [» ]
4H0T X-ray 2.20 B 3-377 [» ]
4H0V X-ray 2.03 B 3-377 [» ]
4H0X X-ray 2.33 B 3-377 [» ]
4H0Y X-ray 1.94 B 3-377 [» ]
ProteinModelPortali P68135.
SMRi P68135. Positions 6-377.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-29021N.
IntActi P68135. 29 interactions.
MINTi MINT-1489367.
STRINGi 9986.ENSOCUP00000006542.

Proteomic databases

PRIDEi P68135.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Phylogenomic databases

eggNOGi COG5277.
HOGENOMi HOG000233340.
HOVERGENi HBG003771.

Miscellaneous databases

EvolutionaryTracei P68135.

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

  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: July 9, 2014
This is version 91 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

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