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P68135

- ACTS_RABIT

UniProt

P68135 - ACTS_RABIT

Protein

Actin, alpha skeletal muscle

Gene

ACTA1

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 92 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    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

    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

    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-methylhistidine
    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP68135.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the actin family.Curated

    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: October 1, 2014
    This is version 92 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