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P29751

- ACTB_RABIT

UniProt

P29751 - ACTB_RABIT

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Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism
Oryctolagus cuniculus (Rabbit)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript 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
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_197541. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:ACTB
OrganismiOryctolagus cuniculus (Rabbit)
Taxonomic identifieri9986 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresLagomorphaLeporidaeOryctolagus
ProteomesiUP000001811: Unplaced

Subcellular locationi

Cytoplasmcytoskeleton
Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs.By similarity

GO - Cellular componenti

  1. cytoskeleton Source: UniProtKB-KW
  2. cytosol Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 375375Actin, cytoplasmic 1PRO_0000367080Add
BLAST
Initiator methioninei1 – 11Removed; alternateBy similarity
Chaini2 – 375374Actin, cytoplasmic 1, N-terminally processedPRO_0000000779Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedBy similarity
Modified residuei44 – 441Methionine (R)-sulfoxideBy similarity
Modified residuei47 – 471Methionine (R)-sulfoxideBy similarity
Modified residuei73 – 731Tele-methylhistidineBy similarity
Modified residuei84 – 841N6-methyllysineBy similarity

Post-translational modificationi

ISGylated.By similarity
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 (By similarity).By similarity
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, Ubl conjugation

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. Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Found in a complex with XPO6, Ran, ACTB and PFN1. Component of the MLL5-L complex, at least composed of KMT2E/MLL5, STK38, PPP1CA, PPP1CB, PPP1CC, HCFC1, ACTB and OGT. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM (By similarity).By similarity

Protein-protein interaction databases

BioGridi1172293. 2 interactions.
DIPiDIP-2197N.
IntActiP29751. 5 interactions.
MINTiMINT-1788815.
STRINGi9986.ENSOCUP00000007086.

Structurei

3D structure databases

ProteinModelPortaliP29751.
SMRiP29751. Positions 2-375.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiCOG5277.
HOVERGENiHBG003771.
InParanoidiP29751.

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.

P29751-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK
60 70 80 90 100
DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHTF YNELRVAPEE
110 120 130 140 150
RPVLLTEAPL 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):41,756
Last modified:April 1, 1993 - v1
Checksum:iCB1D01AFBF036B99
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60733 mRNA. Translation: CAA43140.1.
PIRiJH0637. ATRBB.
RefSeqiNP_001095153.1. NM_001101683.1.
UniGeneiOcu.734.

Genome annotation databases

GeneIDi100009272.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X60733 mRNA. Translation: CAA43140.1 .
PIRi JH0637. ATRBB.
RefSeqi NP_001095153.1. NM_001101683.1.
UniGenei Ocu.734.

3D structure databases

ProteinModelPortali P29751.
SMRi P29751. Positions 2-375.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 1172293. 2 interactions.
DIPi DIP-2197N.
IntActi P29751. 5 interactions.
MINTi MINT-1788815.
STRINGi 9986.ENSOCUP00000007086.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100009272.

Organism-specific databases

CTDi 60.

Phylogenomic databases

eggNOGi COG5277.
HOVERGENi HBG003771.
InParanoidi P29751.

Enzyme and pathway databases

Reactomei REACT_197541. Factors involved in megakaryocyte development and platelet production.

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. "Nucleotide sequences of the rabbit alpha-smooth-muscle and beta-non-muscle actin mRNAs."
    Harris D.E., Warshaw D.M., Periasamy M.
    Gene 112:265-266(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: New Zealand white.
    Tissue: Uterus.

Entry informationi

Entry nameiACTB_RABIT
AccessioniPrimary (citable) accession number: P29751
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: April 1, 1993
Last modified: October 29, 2014
This is version 109 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3