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Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism
Homo sapiens (Human)
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.

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

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: IntAct
  • kinesin binding Source: UniProtKB
  • nitric-oxide synthase binding Source: BHF-UCL
  • structural constituent of cytoskeleton Source: UniProtKB
  • structural constituent of postsynaptic actin cytoskeleton Source: SynGO
  • Tat protein binding Source: BHF-UCL

GO - Biological processi

  • ATP-dependent chromatin remodeling Source: UniProtKB
  • cell junction assembly Source: Reactome
  • ephrin receptor signaling pathway Source: Reactome
  • Fc-gamma receptor signaling pathway involved in phagocytosis Source: Reactome
  • membrane organization Source: Reactome
  • movement of cell or subcellular component Source: UniProtKB
  • platelet aggregation Source: UniProtKB
  • positive regulation of gene expression, epigenetic Source: Reactome
  • postsynaptic actin cytoskeleton organization Source: SynGO
  • protein deubiquitination Source: Reactome
  • retina homeostasis Source: UniProtKB
  • substantia nigra development Source: UniProtKB
  • vascular endothelial growth factor receptor signaling pathway Source: Reactome

Keywordsi

LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190873. Gap junction degradation.
R-HSA-196025. Formation of annular gap junctions.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-3214847. HATs acetylate histones.
R-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-418990. Adherens junctions interactions.
R-HSA-437239. Recycling pathway of L1.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-446353. Cell-extracellular matrix interactions.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5689603. UCH proteinases.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP60709.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin, cytoplasmic 1
Alternative name(s):
Beta-actin
Cleaved into the following chain:
Gene namesi
Name:ACTB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:132. ACTB.

Subcellular locationi

GO - Cellular componenti

  • blood microparticle Source: UniProtKB
  • cortical cytoskeleton Source: Ensembl
  • cytoplasm Source: UniProtKB
  • cytoplasmic ribonucleoprotein granule Source: ParkinsonsUK-UCL
  • cytoskeleton Source: AgBase
  • cytosol Source: Reactome
  • dense body Source: AgBase
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • intracellular ribonucleoprotein complex Source: UniProtKB
  • membrane Source: UniProtKB
  • myelin sheath Source: Ensembl
  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: Reactome
  • plasma membrane Source: AgBase
  • protein complex Source: UniProtKB
  • vesicle Source: UniProtKB

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Involvement in diseasei

Dystonia, juvenile-onset (DJO)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA form of dystonia with juvenile onset. Dystonia is defined by the presence of sustained involuntary muscle contraction, often leading to abnormal postures. Patients with juvenile-onset dystonia manifest progressive, generalized, dopa-unresponsive dystonia, developmental malformations and sensory hearing loss.
See also OMIM:607371
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030026183R → W in DJO; modifies cell response to latrunculin A. 1 PublicationCorresponds to variant dbSNP:rs104894003Ensembl.1
Baraitser-Winter syndrome 1 (BRWS1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA rare developmental disorder characterized by the combination of congenital ptosis, high-arched eyebrows, hypertelorism, ocular colobomata, and a brain malformation consisting of anterior-predominant lissencephaly. Other typical features include postnatal short stature and microcephaly, intellectual disability, seizures, and hearing loss.
See also OMIM:243310
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06781012N → D in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875331Ensembl.1
Natural variantiVAR_06781165L → V in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875332Ensembl.1
Natural variantiVAR_067812196R → C in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875333Ensembl.1
Natural variantiVAR_067813196R → H in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875334Ensembl.1

Keywords - Diseasei

Deafness, Disease mutation, Dystonia, Mental retardation

Organism-specific databases

DisGeNETi60.
MalaCardsiACTB.
MIMi243310. phenotype.
607371. phenotype.
OpenTargetsiENSG00000075624.
Orphaneti2995. Baraitser-Winter syndrome.
79107. Developmental malformations - deafness - dystonia.
PharmGKBiPA24457.

Chemistry databases

ChEMBLiCHEMBL2062353.

Polymorphism and mutation databases

BioMutaiACTB.
DMDMi46397333.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003670731 – 375Actin, cytoplasmic 1Add BLAST375
Initiator methionineiRemoved; alternateCombined sources2 Publications
ChainiPRO_00000007712 – 375Actin, cytoplasmic 1, N-terminally processedAdd BLAST374

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei2N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedCombined sources1 Publication1
Modified residuei44Methionine (R)-sulfoxideBy similarity1
Modified residuei47Methionine (R)-sulfoxideBy similarity1
Cross-linki50Isoglutamyl lysine isopeptide (Lys-Glu) (interchain with E-270); by Vibrio toxins RtxA and VgrG11 Publication
Modified residuei73Tele-methylhistidineBy similarity1
Modified residuei84N6-methyllysine1 Publication1
Cross-linki270Isoglutamyl lysine isopeptide (Glu-Lys) (interchain with K-50); by Vibrio toxins RtxA and VgrG11 Publication

Post-translational modificationi

ISGylated.1 Publication
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.1 Publication
(Microbial infection) Monomeric actin is cross-linked by V.cholerae toxins RtxA and VgrG1 in case of infection: bacterial toxins mediate the cross-link between Lys-50 of one monomer and Glu-270 of another actin monomer, resulting in formation of highly toxic actin oligomers that cause cell rounding (PubMed:19015515). The toxin can be highly efficient at very low concentrations by acting on formin homology family proteins: toxic actin oligomers bind with high affinity to formins and adversely affect both nucleation and elongation abilities of formins, causing their potent inhibition in both profilin-dependent and independent manners (PubMed:26228148).2 Publications

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Oxidation, Ubl conjugation

Proteomic databases

EPDiP60709.
PaxDbiP60709.
PeptideAtlasiP60709.
PRIDEiP60709.
TopDownProteomicsiP60709.

2D gel databases

DOSAC-COBS-2DPAGEiP60709.
REPRODUCTION-2DPAGEiP60709.
SWISS-2DPAGEiP60709.
UCD-2DPAGEiP60709.

PTM databases

iPTMnetiP60709.
PhosphoSitePlusiP60709.
SwissPalmiP60709.

Expressioni

Gene expression databases

BgeeiENSG00000075624.
CleanExiHS_ACTB.
ExpressionAtlasiP60709. baseline and differential.
GenevisibleiP60709. HS.

Organism-specific databases

HPAiCAB002621.
HPA041264.
HPA041271.

Interactioni

Subunit structurei

Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). 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. Interacts with TBC1D21 (By similarity).By similarity7 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • kinesin binding Source: UniProtKB
  • nitric-oxide synthase binding Source: BHF-UCL
  • Tat protein binding Source: BHF-UCL

Protein-protein interaction databases

BioGridi106575. 283 interactors.
DIPiDIP-29686N.
IntActiP60709. 198 interactors.
MINTiMINT-220312.
STRINGi9606.ENSP00000349960.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BYHelectron microscopy12.00A2-375[»]
3D2UX-ray2.21C/G170-178[»]
3J82electron microscopy7.70B/C/D2-375[»]
3LUEelectron microscopy-A/B/C/D/E/F/G/H/I/J2-375[»]
ProteinModelPortaliP60709.
SMRiP60709.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP60709.

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiP60709.
KOiK05692.
OMAiPFHTTAE.
OrthoDBiEOG091G08LD.
PhylomeDBiP60709.
TreeFamiTF354237.

Family and domain databases

InterProiView protein in InterPro
IPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiView protein in Pfam
PF00022. Actin. 1 hit.
PRINTSiPR00190. ACTIN.
SMARTiView protein in SMART
SM00268. ACTIN. 1 hit.
PROSITEiView protein in PROSITE
PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P60709-1 [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
HPVLLTEAPL 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):41,737
Last modified:April 1, 1988 - v1
Checksum:i6AFD05CA94E360E2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti97A → P in AAH16045 (PubMed:15489334).Curated1
Sequence conflicti116R → L in AAH12854 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06781012N → D in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875331Ensembl.1
Natural variantiVAR_06781165L → V in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875332Ensembl.1
Natural variantiVAR_030026183R → W in DJO; modifies cell response to latrunculin A. 1 PublicationCorresponds to variant dbSNP:rs104894003Ensembl.1
Natural variantiVAR_067812196R → C in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875333Ensembl.1
Natural variantiVAR_067813196R → H in BRWS1. 1 PublicationCorresponds to variant dbSNP:rs281875334Ensembl.1
Natural variantiVAR_048185243P → L. Corresponds to variant dbSNP:rs11546899Ensembl.1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00351 mRNA. Translation: CAA25099.1.
M10277 Genomic DNA. Translation: AAA51567.1.
X63432 mRNA. Translation: CAA45026.1.
AY582799 Genomic DNA. Translation: AAS79319.1.
AC006483 Genomic DNA. Translation: AAP22343.1.
BC001301 mRNA. Translation: AAH01301.1.
BC002409 mRNA. Translation: AAH02409.1.
BC004251 mRNA. Translation: AAH04251.1.
BC008633 mRNA. Translation: AAH08633.1.
BC012854 mRNA. Translation: AAH12854.1.
BC013380 mRNA. Translation: AAH13380.1.
BC014861 mRNA. Translation: AAH14861.1.
BC016045 mRNA. Translation: AAH16045.1.
V00478 mRNA. Translation: CAA23745.1.
CCDSiCCDS5341.1.
PIRiA25168. ATHUB.
RefSeqiNP_001092.1. NM_001101.3.
UniGeneiHs.520640.

Genome annotation databases

EnsembliENST00000331789; ENSP00000349960; ENSG00000075624.
GeneIDi60.
KEGGihsa:60.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs
Mendelian genes actin, beta (ACTB)

Leiden Open Variation Database (LOVD)

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00351 mRNA. Translation: CAA25099.1.
M10277 Genomic DNA. Translation: AAA51567.1.
X63432 mRNA. Translation: CAA45026.1.
AY582799 Genomic DNA. Translation: AAS79319.1.
AC006483 Genomic DNA. Translation: AAP22343.1.
BC001301 mRNA. Translation: AAH01301.1.
BC002409 mRNA. Translation: AAH02409.1.
BC004251 mRNA. Translation: AAH04251.1.
BC008633 mRNA. Translation: AAH08633.1.
BC012854 mRNA. Translation: AAH12854.1.
BC013380 mRNA. Translation: AAH13380.1.
BC014861 mRNA. Translation: AAH14861.1.
BC016045 mRNA. Translation: AAH16045.1.
V00478 mRNA. Translation: CAA23745.1.
CCDSiCCDS5341.1.
PIRiA25168. ATHUB.
RefSeqiNP_001092.1. NM_001101.3.
UniGeneiHs.520640.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3BYHelectron microscopy12.00A2-375[»]
3D2UX-ray2.21C/G170-178[»]
3J82electron microscopy7.70B/C/D2-375[»]
3LUEelectron microscopy-A/B/C/D/E/F/G/H/I/J2-375[»]
ProteinModelPortaliP60709.
SMRiP60709.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106575. 283 interactors.
DIPiDIP-29686N.
IntActiP60709. 198 interactors.
MINTiMINT-220312.
STRINGi9606.ENSP00000349960.

Chemistry databases

ChEMBLiCHEMBL2062353.

PTM databases

iPTMnetiP60709.
PhosphoSitePlusiP60709.
SwissPalmiP60709.

Polymorphism and mutation databases

BioMutaiACTB.
DMDMi46397333.

2D gel databases

DOSAC-COBS-2DPAGEiP60709.
REPRODUCTION-2DPAGEiP60709.
SWISS-2DPAGEiP60709.
UCD-2DPAGEiP60709.

Proteomic databases

EPDiP60709.
PaxDbiP60709.
PeptideAtlasiP60709.
PRIDEiP60709.
TopDownProteomicsiP60709.

Protocols and materials databases

DNASUi60.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000331789; ENSP00000349960; ENSG00000075624.
GeneIDi60.
KEGGihsa:60.

Organism-specific databases

CTDi60.
DisGeNETi60.
GeneCardsiACTB.
HGNCiHGNC:132. ACTB.
HPAiCAB002621.
HPA041264.
HPA041271.
MalaCardsiACTB.
MIMi102630. gene.
243310. phenotype.
607371. phenotype.
neXtProtiNX_P60709.
OpenTargetsiENSG00000075624.
Orphaneti2995. Baraitser-Winter syndrome.
79107. Developmental malformations - deafness - dystonia.
PharmGKBiPA24457.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0676. Eukaryota.
COG5277. LUCA.
GeneTreeiENSGT00760000118957.
HOVERGENiHBG003771.
InParanoidiP60709.
KOiK05692.
OMAiPFHTTAE.
OrthoDBiEOG091G08LD.
PhylomeDBiP60709.
TreeFamiTF354237.

Enzyme and pathway databases

ReactomeiR-HSA-1445148. Translocation of GLUT4 to the plasma membrane.
R-HSA-190873. Gap junction degradation.
R-HSA-196025. Formation of annular gap junctions.
R-HSA-2029482. Regulation of actin dynamics for phagocytic cup formation.
R-HSA-3214847. HATs acetylate histones.
R-HSA-389957. Prefoldin mediated transfer of substrate to CCT/TriC.
R-HSA-390450. Folding of actin by CCT/TriC.
R-HSA-3928662. EPHB-mediated forward signaling.
R-HSA-3928665. EPH-ephrin mediated repulsion of cells.
R-HSA-418990. Adherens junctions interactions.
R-HSA-437239. Recycling pathway of L1.
R-HSA-4420097. VEGFA-VEGFR2 Pathway.
R-HSA-445095. Interaction between L1 and Ankyrins.
R-HSA-446353. Cell-extracellular matrix interactions.
R-HSA-5250924. B-WICH complex positively regulates rRNA expression.
R-HSA-5626467. RHO GTPases activate IQGAPs.
R-HSA-5663213. RHO GTPases Activate WASPs and WAVEs.
R-HSA-5663220. RHO GTPases Activate Formins.
R-HSA-5674135. MAP2K and MAPK activation.
R-HSA-5689603. UCH proteinases.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-6802946. Signaling by moderate kinase activity BRAF mutants.
R-HSA-6802948. Signaling by high-kinase activity BRAF mutants.
R-HSA-6802949. Signaling by RAS mutants.
R-HSA-6802952. Signaling by BRAF and RAF fusions.
R-HSA-6802955. Paradoxical activation of RAF signaling by kinase inactive BRAF.
R-HSA-8856828. Clathrin-mediated endocytosis.
R-HSA-983231. Factors involved in megakaryocyte development and platelet production.
SignaLinkiP60709.

Miscellaneous databases

ChiTaRSiACTB. human.
EvolutionaryTraceiP60709.
GeneWikiiBeta-actin.
GenomeRNAii60.
PROiPR:P60709.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000075624.
CleanExiHS_ACTB.
ExpressionAtlasiP60709. baseline and differential.
GenevisibleiP60709. HS.

Family and domain databases

InterProiView protein in InterPro
IPR004000. Actin.
IPR020902. Actin/actin-like_CS.
IPR004001. Actin_CS.
PANTHERiPTHR11937. PTHR11937. 1 hit.
PfamiView protein in Pfam
PF00022. Actin. 1 hit.
PRINTSiPR00190. ACTIN.
SMARTiView protein in SMART
SM00268. ACTIN. 1 hit.
PROSITEiView protein in PROSITE
PS00406. ACTINS_1. 1 hit.
PS00432. ACTINS_2. 1 hit.
PS01132. ACTINS_ACT_LIKE. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiACTB_HUMAN
AccessioniPrimary (citable) accession number: P60709
Secondary accession number(s): P02570
, P70514, P99021, Q11211, Q64316, Q75MN2, Q96B34, Q96HG5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: April 1, 1988
Last modified: May 10, 2017
This is version 162 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.