UniProtKB - P68135 (ACTS_RABIT)
Protein
Actin, alpha skeletal muscle
Gene
ACTA1
Organism
Oryctolagus cuniculus (Rabbit)
Status
Functioni
Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
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.
GO - Molecular functioni
- actin monomer binding Source: CAFA
- ATP binding Source: UniProtKB-KW
- calcium-dependent protein binding Source: AgBase
- calcium ion binding Source: CAFA
- identical protein binding Source: IntAct
- magnesium ion binding Source: CAFA
- myosin heavy chain binding Source: CAFA
- protein domain specific binding Source: CAFA
- titin binding Source: CAFA
- tropomyosin binding Source: CAFA
- troponin I binding Source: CAFA
GO - Biological processi
- actin filament bundle assembly Source: CAFA
- actin filament polymerization Source: CAFA
- mesenchyme migration Source: AgBase
- positive regulation of actin-dependent ATPase activity Source: CAFA
- positive regulation of gene expression Source: AgBase
- skeletal muscle fiber development Source: UniProtKB
- skeletal muscle thin filament assembly Source: UniProtKB
Keywordsi
Molecular function | Muscle protein |
Ligand | ATP-binding, Nucleotide-binding |
Enzyme and pathway databases
SABIO-RKi | P68135 |
Names & Taxonomyi
Protein namesi | Recommended name: Actin, alpha skeletal muscleAlternative name(s): Alpha-actin-1 Cleaved into the following chain: |
Gene namesi | Name:ACTA1 Synonyms:ACTA |
Organismi | Oryctolagus cuniculus (Rabbit) |
Taxonomic identifieri | 9986 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Lagomorpha › Leporidae › Oryctolagus |
Proteomesi |
|
Subcellular locationi
Cytoskeleton
Cytoskeleton
- actin filament Source: CAFA
- actin filament bundle Source: CAFA
- filamentous actin Source: CAFA
- stress fiber Source: UniProtKB
- striated muscle thin filament Source: UniProtKB
Other locations
- cell body Source: AgBase
- cytoplasm Source: AgBase
- filopodium Source: AgBase
- lamellipodium Source: AgBase
- skeletal muscle myofibril Source: CAFA
Keywords - Cellular componenti
Cytoplasm, CytoskeletonPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed | |||
ChainiPRO_0000442811 | 2 – 377 | Actin, alpha skeletal muscle, intermediate formBy similarityAdd BLAST | 376 | |
ChainiPRO_0000442812 | 3 – 377 | Actin, alpha skeletal muscle2 PublicationsAdd BLAST | 375 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylcysteine; in intermediate formBy similarity | 1 | |
Modified residuei | 3 | N-acetylaspartate; in Actin, alpha skeletal muscle1 Publication | 1 | |
Modified residuei | 46 | Methionine (R)-sulfoxideBy similarity | 1 | |
Modified residuei | 49 | Methionine (R)-sulfoxideBy similarity | 1 | |
Modified residuei | 63 | N6-malonyllysineBy similarity | 1 | |
Modified residuei | 75 | Tele-methylhistidineCombined sources5 Publications | 1 | |
Modified residuei | 86 | N6-methyllysineBy similarity | 1 | |
Modified residuei | 179 | ADP-ribosylarginine; by SpvB1 Publication | 1 |
Post-translational modificationi
Oxidation of Met-46 and Met-49 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 promotes actin repolymerization.By similarity
Can be mono-ADP-ribosylated on Arg-179 by SpvB of Salmonella spp. This modification blocks subsequent polymerization and leads to cell death.1 Publication
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
Methylated at His-75 by SETD3.By similarity
Keywords - PTMi
Acetylation, ADP-ribosylation, Methylation, OxidationPTM databases
CarbonylDBi | P68135 |
iPTMneti | P68135 |
MetOSitei | P68135 |
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 alpha-actinin (PubMed:8449927).
Identified in a complex composed of ACTA1, COBL, GSN AND TMSB4X (PubMed:23009842).
Interacts with TTID (By similarity).
Interacts (via its C-terminus) with USP25 (By similarity).
By similarity3 PublicationsBinary interactionsi
Hide detailsP68135
GO - Molecular functioni
- actin monomer binding Source: CAFA
- calcium-dependent protein binding Source: AgBase
- identical protein binding Source: IntAct
- myosin heavy chain binding Source: CAFA
- protein domain specific binding Source: CAFA
- titin binding Source: CAFA
- tropomyosin binding Source: CAFA
- troponin I binding Source: CAFA
Protein-protein interaction databases
DIPi | DIP-29021N |
ELMi | P68135 |
IntActi | P68135, 88 interactors |
MINTi | P68135 |
STRINGi | 9986.ENSOCUP00000006542 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P68135 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P68135 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 112 – 125 | Interaction with alpha-actinin1 PublicationAdd BLAST | 14 | |
Regioni | 360 – 372 | Interaction with alpha-actinin1 PublicationAdd BLAST | 13 |
Sequence similaritiesi
Belongs to the actin family.Curated
Phylogenomic databases
eggNOGi | KOG0676, Eukaryota |
InParanoidi | P68135 |
Family and domain databases
IDEALi | IID50082 |
InterProi | View protein in InterPro IPR004000, Actin IPR020902, Actin/actin-like_CS IPR004001, Actin_CS IPR043129, ATPase_NBD |
PANTHERi | PTHR11937, PTHR11937, 1 hit |
Pfami | View protein in Pfam PF00022, Actin, 1 hit |
PRINTSi | PR00190, ACTIN |
SMARTi | View protein in SMART SM00268, ACTIN, 1 hit |
SUPFAMi | SSF53067, SSF53067, 2 hits |
PROSITEi | View protein in PROSITE PS00406, ACTINS_1, 1 hit PS00432, ACTINS_2, 1 hit PS01132, ACTINS_ACT_LIKE, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P68135-1 [UniParc]FASTAAdd to basket
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
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 |
PIRi | A92182, ATRB I46471 I46472 I46473 |
Similar proteinsi
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 |
PIRi | A92182, ATRB I46471 I46472 I46473 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB 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 | [»] | |
3J8A | electron microscopy | 3.70 | A/B/C/D/E | 3-377 | [»] | |
3J8I | electron microscopy | 4.70 | D/E/F/G/H | 1-377 | [»] | |
3J8J | electron microscopy | 12.00 | A/B/C/D/E/F/G/H/I/J/K | 1-377 | [»] | |
3J8K | electron microscopy | 12.00 | A/B/C/D/E/F/G/H/I/J | 1-377 | [»] | |
3JBI | electron microscopy | 8.50 | A/B | 3-377 | [»] | |
3JBJ | electron microscopy | 7.60 | A/B | 3-377 | [»] | |
3JBK | electron microscopy | 8.20 | A/B | 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 | [»] | |
4K41 | X-ray | 1.40 | A | 3-377 | [»] | |
4K42 | X-ray | 2.90 | A/B/C/D | 3-377 | [»] | |
4K43 | X-ray | 2.90 | A/B | 3-377 | [»] | |
4PKG | X-ray | 1.80 | A | 1-377 | [»] | |
4PKH | X-ray | 2.15 | A/D/F/I | 1-377 | [»] | |
4PKI | X-ray | 2.30 | A | 1-377 | [»] | |
4PL8 | X-ray | 2.00 | A/B | 3-377 | [»] | |
4V0U | X-ray | 7.88 | A/B/C/L/M | 3-377 | [»] | |
4WYB | X-ray | 3.49 | A/C/E/G/I/K/M/O/Q/S/U/X | 1-377 | [»] | |
4Z94 | X-ray | 2.40 | A | 1-377 | [»] | |
5H53 | electron microscopy | 5.20 | D/E | 3-377 | [»] | |
5JLF | electron microscopy | 3.60 | A/B/C/D/E | 3-377 | [»] | |
5KG8 | electron microscopy | 9.10 | B/C/D | 3-377 | [»] | |
5MVA | electron microscopy | 27.70 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W | 3-377 | [»] | |
5MVY | electron microscopy | 28.40 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W | 3-377 | [»] | |
5ONV | electron microscopy | 4.10 | A/B/C/D/E | 3-377 | [»] | |
5OOC | electron microscopy | 3.60 | A/B/C/D/E | 3-377 | [»] | |
5OOD | electron microscopy | 3.70 | A/B/C/D/E | 3-377 | [»] | |
5OOE | electron microscopy | 3.60 | A/B/C/D/E | 3-377 | [»] | |
5OOF | electron microscopy | 3.40 | A/B/C/D/E | 3-377 | [»] | |
5UBO | X-ray | 2.39 | A | 1-377 | [»] | |
5YEE | X-ray | 1.81 | B | 1-377 | [»] | |
5YPU | X-ray | 2.00 | A/C | 7-374 | [»] | |
5ZZA | X-ray | 1.53 | A | 5-377 | [»] | |
5ZZB | X-ray | 2.30 | B/D | 7-377 | [»] | |
6AV9 | electron microscopy | 3.90 | A/B/C | 1-377 | [»] | |
6AVB | electron microscopy | 3.90 | A/B/C | 1-377 | [»] | |
6BIH | electron microscopy | 6.00 | C | 1-377 | [»] | |
6BNO | electron microscopy | 5.50 | A/B/C/D/E/F/G/H | 1-373 | [»] | |
6BNP | electron microscopy | 4.60 | A/B/C/D/E/F/G/H | 1-373 | [»] | |
6BNQ | electron microscopy | 5.50 | A/B/C/D/E/F/G/H | 1-373 | [»] | |
6BNU | electron microscopy | 7.50 | A/B/C/D/E/F/G/H | 1-373 | [»] | |
6BNV | electron microscopy | 4.60 | A/B/C/D/E/F/G/H | 1-373 | [»] | |
6BNW | electron microscopy | 5.50 | A/B/C/D/E/F/G/H | 1-373 | [»] | |
6C1D | electron microscopy | 3.20 | A/B/C/D/E | 3-377 | [»] | |
6C1G | electron microscopy | 3.80 | A/B/C/D/E | 3-377 | [»] | |
6C1H | electron microscopy | 3.90 | A/B/C/D/E | 3-377 | [»] | |
6FHL | electron microscopy | 3.30 | A/B/C/D/E | 3-377 | [»] | |
6FM2 | X-ray | 2.80 | A | 3-377 | [»] | |
6GVC | X-ray | 2.60 | A/B/C/D | 1-377 | [»] | |
6JBK | X-ray | 2.45 | A/C/E/G | 1-377 | [»] | |
6JCU | X-ray | 2.30 | A/C | 1-377 | [»] | |
6JH8 | X-ray | 2.15 | A | 1-377 | [»] | |
6JH9 | X-ray | 1.74 | A | 1-377 | [»] | |
6KN7 | electron microscopy | 6.60 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O | 3-377 | [»] | |
6KN8 | electron microscopy | 4.80 | A/B/C/D/E/F/G/H/I/J/K/L/M/N/O | 3-377 | [»] | |
6MGO | X-ray | 2.20 | A | 1-377 | [»] | |
6NAS | X-ray | 2.90 | A | 3-377 | [»] | |
6NBE | X-ray | 2.00 | A | 3-377 | [»] | |
6QRI | X-ray | 2.40 | A/B | 1-377 | [»] | |
6RSW | X-ray | 1.95 | A | 3-377 | [»] | |
6T1Y | electron microscopy | 3.30 | A/B/C/D/E | 3-377 | [»] | |
6T20 | electron microscopy | 3.70 | A/B/C/D/E | 3-377 | [»] | |
6T23 | electron microscopy | 3.10 | A/B/C/D/E | 3-377 | [»] | |
6T24 | electron microscopy | 3.70 | A/B/C/D/E | 3-377 | [»] | |
6T25 | electron microscopy | 3.60 | A/B/C/D/E | 3-377 | [»] | |
6U96 | electron microscopy | 3.80 | A/B/C/D/E | 1-377 | [»] | |
6UBY | electron microscopy | 7.50 | A/B/C/D/E/F/G/H | 1-377 | [»] | |
6UC0 | electron microscopy | 7.50 | A/B/C/D/E/F/G | 1-377 | [»] | |
6UC4 | electron microscopy | 9.20 | A/B/C/D/E/F/G/H/J/K/L | 1-377 | [»] | |
6VAO | electron microscopy | 3.40 | A/B/C/D/E | 1-377 | [»] | |
6VAU | electron microscopy | 3.50 | A/B/C/D/E | 1-377 | [»] | |
6W17 | electron microscopy | 3.90 | I/J/K/L | 1-377 | [»] | |
6W7V | X-ray | 1.70 | A | 1-377 | [»] | |
6WVT | electron microscopy | 3.56 | B/D/E/F/H/I | 1-377 | [»] | |
7AD9 | electron microscopy | 3.50 | B/D/F/H/I | 1-377 | [»] | |
7C2F | X-ray | 2.03 | A/C | 3-377 | [»] | |
7C2G | X-ray | 1.71 | A | 1-377 | [»] | |
7C2H | X-ray | 2.35 | A | 1-377 | [»] | |
SMRi | P68135 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
DIPi | DIP-29021N |
ELMi | P68135 |
IntActi | P68135, 88 interactors |
MINTi | P68135 |
STRINGi | 9986.ENSOCUP00000006542 |
PTM databases
CarbonylDBi | P68135 |
iPTMneti | P68135 |
MetOSitei | P68135 |
Phylogenomic databases
eggNOGi | KOG0676, Eukaryota |
InParanoidi | P68135 |
Enzyme and pathway databases
SABIO-RKi | P68135 |
Miscellaneous databases
EvolutionaryTracei | P68135 |
Family and domain databases
IDEALi | IID50082 |
InterProi | View protein in InterPro IPR004000, Actin IPR020902, Actin/actin-like_CS IPR004001, Actin_CS IPR043129, ATPase_NBD |
PANTHERi | PTHR11937, PTHR11937, 1 hit |
Pfami | View protein in Pfam PF00022, Actin, 1 hit |
PRINTSi | PR00190, ACTIN |
SMARTi | View protein in SMART SM00268, ACTIN, 1 hit |
SUPFAMi | SSF53067, SSF53067, 2 hits |
PROSITEi | View protein in PROSITE PS00406, ACTINS_1, 1 hit PS00432, ACTINS_2, 1 hit PS01132, ACTINS_ACT_LIKE, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | ACTS_RABIT | |
Accessioni | P68135Primary (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: | February 10, 2021 | |
This is version 135 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families