UniProtKB - P60712 (ACTB_BOVIN)

BLAST

>sp|P60712|ACTB_BOVIN Actin, cytoplasmic 1 OS=Bos taurus OX=9913 GN=ACTB PE=1 SV=1
MDDDIAALVVDNGSGMCKAGFAGDDAPRAVFPSIVGRPRHQGVMVGMGQKDSYVGDEAQS
KRGILTLKYPIEHGIVTNWDDMEKIWHHTFYNELRVAPEEHPVLLTEAPLNPKANREKMT
QIMFETFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHTVPIYEGYALPHAILRLDL
AGRDLTDYLMKILTERGYSFTTTAEREIVRDIKEKLCYVALDFEQEMATAASSSSLEKSY
ELPDGQVITIGNERFRCPEALFQPSFLGMESCGIHETTFNSIMKCDVDIRKDLYANTVLS
GGTTMYPGIADRMQKEITALAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQ
EYDESGPSIVHRKCF

Align
Format
Add to basket Added to basket
History
Entry version 130 (10 Oct 2018)
Sequence version 1 (01 Apr 1988)
Previous versions | rss
Other tutorials and videos
Help video
Feedback

Protein

Actin, cytoplasmic 1

Gene

ACTB

Organism

Bos taurus (Bovine)

Status

Reviewed-Annotation score: -Experimental evidence at protein levelⁱ

Functionⁱ

Actin is a highly conserved protein that polymerizes to produce filaments that form cross-linked networks in the cytoplasm of cells. Actin exists in both monomeric (G-actin) and polymeric (F-actin) forms, both forms playing key functions, such as cell motility and contraction. In addition to their role in the cytoplasmic cytoskeleton, G- and F-actin also localize in the nucleus, and regulate gene transcription and motility and repair of damaged DNA.By similarity

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.By similarity

GO - Molecular functionⁱ

ATP binding Source: UniProtKB-KW

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Ligand	ATP-binding, Nucleotide-binding

Ligand

ATP-binding, Nucleotide-binding

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Actin, cytoplasmic 1 Alternative name(s): Beta-actin Cleaved into the following chain: Actin, cytoplasmic 1, N-terminally processed
Gene namesⁱ	Name:ACTB
Organismⁱ	Bos taurus (Bovine)
Taxonomic identifierⁱ	9913 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Laurasiatheria › Cetartiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos
Proteomesⁱ	UP000009136 Componentⁱ: Unplaced

Keywords - Cellular componentⁱ

Cytoplasm, Cytoskeleton, Nucleus

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Length
ChainⁱPRO_0000000757	1 – 375	Actin, cytoplasmic 1Add BLAST	375
Initiator methionineⁱ		Removed; alternateBy similarity
ChainⁱPRO_0000367066	2 – 375	Actin, cytoplasmic 1, N-terminally processedAdd BLAST	374

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Length
Modified residueⁱ	1	N-acetylmethionineBy similarity	1
Modified residueⁱ	2	N-acetylaspartate; in Actin, cytoplasmic 1, N-terminally processedBy similarity	1
Modified residueⁱ	44	Methionine (R)-sulfoxideBy similarity	1
Modified residueⁱ	47	Methionine (R)-sulfoxideBy similarity	1
Modified residueⁱ	73	Tele-methylhistidineBy similarity	1
Modified residueⁱ	84	N6-methyllysineBy similarity	1

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

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

Actin, cytoplasmic 1, N-terminally processed: N-terminal acetylation by NAA80 affects actin filament depolymerization and elongation, including elongation driven by formins. In contrast, filament nucleation by the Arp2/3 complex is not affected.By similarity

Keywords - PTMⁱ

Acetylation, Methylation, Oxidation, Ubl conjugation

Proteomic databases

PeptideAtlas More...PeptideAtlasⁱ	P60712
PRIDEⁱ	P60712

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. Interacts with XPO6 and EMD. Interacts with ERBB2. Interacts with GCSAM (By similarity). Interacts with TBC1D21. Interacts with CPNE1 (via VWFA domain) and CPNE4 (via VWFA domain) (By similarity). Interacts with DHX9 (via C-terminus); this interaction is direct and mediates the attachment to nuclear ribonucleoprotein complexes. Interacts with FAM107A (By similarity).By similarity

Protein-protein interaction databases

CORUMⁱ	P60712
Database of interacting proteins More...DIPⁱ	DIP-57682N
IntActⁱ	P60712, 5 interactors
Molecular INTeraction database More...MINTⁱ	P60712

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Beta strandⁱ	4 – 6	Combined sources	3
Beta strandⁱ	8 – 12	Combined sources	5
Beta strandⁱ	14 – 21	Combined sources	8
Beta strandⁱ	24 – 26	Combined sources	3
Beta strandⁱ	30 – 32	Combined sources	3
Beta strandⁱ	35 – 38	Combined sources	4
Beta strandⁱ	45 – 47	Combined sources	3
Beta strandⁱ	51 – 54	Combined sources	4
Helixⁱ	56 – 60	Combined sources	5
Helixⁱ	62 – 64	Combined sources	3
Beta strandⁱ	65 – 68	Combined sources	4
Beta strandⁱ	70 – 72	Combined sources	3
Helixⁱ	79 – 91	Combined sources	13
Turnⁱ	92 – 94	Combined sources	3
Helixⁱ	98 – 100	Combined sources	3
Beta strandⁱ	103 – 107	Combined sources	5
Helixⁱ	113 – 125	Combined sources	13
Beta strandⁱ	130 – 136	Combined sources	7
Helixⁱ	137 – 144	Combined sources	8
Beta strandⁱ	148 – 155	Combined sources	8
Beta strandⁱ	160 – 166	Combined sources	7
Helixⁱ	172 – 174	Combined sources	3
Beta strandⁱ	176 – 179	Combined sources	4
Helixⁱ	182 – 196	Combined sources	15
Helixⁱ	203 – 216	Combined sources	14
Helixⁱ	223 – 231	Combined sources	9
Beta strandⁱ	234 – 236	Combined sources	3
Beta strandⁱ	238 – 241	Combined sources	4
Beta strandⁱ	243 – 245	Combined sources	3
Beta strandⁱ	247 – 251	Combined sources	5
Helixⁱ	253 – 256	Combined sources	4
Helixⁱ	259 – 262	Combined sources	4
Helixⁱ	264 – 267	Combined sources	4
Helixⁱ	274 – 282	Combined sources	9
Helixⁱ	287 – 294	Combined sources	8
Beta strandⁱ	297 – 301	Combined sources	5
Helixⁱ	302 – 304	Combined sources	3
Helixⁱ	309 – 320	Combined sources	12
Turnⁱ	333 – 336	Combined sources	4
Helixⁱ	338 – 347	Combined sources	10
Helixⁱ	350 – 354	Combined sources	5
Beta strandⁱ	356 – 358	Combined sources	3
Helixⁱ	359 – 365	Combined sources	7
Helixⁱ	369 – 373	Combined sources	5

Show more details

3D structure databases

ProteinModelPortalⁱ	P60712
SMRⁱ	P60712
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Miscellaneous databases

EvolutionaryTraceⁱ	P60712

EvolutionaryTraceⁱ

P60712

Family & Domainsⁱ

Sequence similaritiesⁱ

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGⁱ	KOG0676 Eukaryota COG5277 LUCA
HOVERGENⁱ	HBG003771
InParanoidⁱ	P60712
KEGG Orthology (KO) More...KOⁱ	K05692

Family and domain databases

InterProⁱ	View protein in InterPro IPR004000 Actin IPR020902 Actin/actin-like_CS IPR004001 Actin_CS
PANTHERⁱ	PTHR11937 PTHR11937, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF00022 Actin, 1 hit
PRINTSⁱ	PR00190 ACTIN
SMARTⁱ	View protein in SMART SM00268 ACTIN, 1 hit
PROSITEⁱ	View 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.

P60712-1 [UniParc]FASTA Add 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

Experimental Info

Feature key	Position(s)	DescriptionActions	Length
Sequence conflictⁱ	126	T → A in AAI42414 (Ref. 3) Curated	1
Sequence conflictⁱ	204 – 206	AER → GRA in AAM98378 (PubMed:14559974).Curated	3
Sequence conflictⁱ	281	S → F in AAM98378 (PubMed:14559974).Curated	1

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY141970 mRNA Translation: AAM98378.1 BT030480 mRNA Translation: ABQ12920.1 BC102948 mRNA Translation: AAI02949.1 BC142413 mRNA Translation: AAI42414.1 K00622 mRNA Translation: AAA30352.1 K00623 mRNA Translation: AAA30353.1
PIRⁱ	E14185 ATBOB
NCBI Reference Sequences More...RefSeqⁱ	NP_776404.2, NM_173979.3
UniGeneⁱ	Bt.14186 Bt.38667

Genome annotation databases

GeneIDⁱ	280979
KEGGⁱ	bta:280979

Similar proteinsⁱ

100% Identity
90% Identity
50% Identity

Protein	Similar proteins		Species	Score	Length	Source
P60712	Actin, cytoplasmic 1	)	HUMAN		375	UniRef100_P60709
Actin, cytoplasmic 1		CANLF		375
Actin, cytoplasmic 1		CAVPO		375
Actin, cytoplasmic 1	)	CHICK		375
Actin, cytoplasmic 1		CHLAE		375
+94

Protein	Similar proteins		Species	Score	Length	Source
P60712	Actin, cytoplasmic 1	)	HUMAN		375	UniRef90_P60709
Actin, cytoplasmic 1		CANLF		375
Actin, cytoplasmic 1		CAVPO		375
Actin, cytoplasmic 1	)	CHICK		375
Actin, cytoplasmic 1		CHLAE		375
+114

Protein	Similar proteins		Species	Score	Length	Source
P60712	Actin, cytoplasmic 1	)	HUMAN		375	UniRef50_P60709
Actin, cytoplasmic 1		CANLF		375
Actin, cytoplasmic 1		CAVPO		375
Actin, cytoplasmic 1	)	CHICK		375
Actin, cytoplasmic 1		CHLAE		375
+626

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY141970 mRNA Translation: AAM98378.1 BT030480 mRNA Translation: ABQ12920.1 BC102948 mRNA Translation: AAI02949.1 BC142413 mRNA Translation: AAI42414.1 K00622 mRNA Translation: AAA30352.1 K00623 mRNA Translation: AAA30353.1
PIRⁱ	E14185 ATBOB
RefSeqⁱ	NP_776404.2, NM_173979.3
UniGeneⁱ	Bt.14186 Bt.38667

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	1HLU	X-ray	2.65	A	2-375	[»]
	2BTF	X-ray	2.55	A	2-375	[»]
	2OAN	X-ray	2.61	A/B/C/D	1-375	[»]
	3U4L	X-ray	2.40	A	1-375	[»]
	3UB5	X-ray	2.20	A	2-375	[»]
ProteinModelPortalⁱ	P60712
SMRⁱ	P60712
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

CORUMⁱ	P60712
DIPⁱ	DIP-57682N
IntActⁱ	P60712, 5 interactors
MINTⁱ	P60712

Proteomic databases

PeptideAtlasⁱ	P60712
PRIDEⁱ	P60712

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

GeneIDⁱ	280979
KEGGⁱ	bta:280979

Organism-specific databases

CTDⁱ	60

CTDⁱ

Phylogenomic databases

eggNOGⁱ	KOG0676 Eukaryota COG5277 LUCA
HOVERGENⁱ	HBG003771
InParanoidⁱ	P60712
KOⁱ	K05692

Miscellaneous databases

EvolutionaryTraceⁱ	P60712

EvolutionaryTraceⁱ

P60712

Family and domain databases

InterProⁱ	View protein in InterPro IPR004000 Actin IPR020902 Actin/actin-like_CS IPR004001 Actin_CS
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
PROSITEⁱ	View protein in PROSITE PS00406 ACTINS_1, 1 hit PS00432 ACTINS_2, 1 hit PS01132 ACTINS_ACT_LIKE, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	ACTB_BOVIN
Accessionⁱ	P60712Primary (citable) accession number: P60712 Secondary accession number(s): A5D961 Q8MIJ0
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
	Last sequence update:	April 1, 1988
	Last modified:	October 10, 2018
	This is version 130 of the entry and version 1 of the sequence. See complete history.
Entry statusⁱ	Reviewed (UniProtKB/Swiss-Prot)
Annotation program	Chordata Protein Annotation Program

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - P60712 (ACTB_BOVIN)

Your basket is currently empty. i <p>When browsing through different UniProt proteins, you can use the ‘basket’ to save them, so that you can back to find or analyse them later.<p><a href='/help/basket' target='_top'>More...</a></p>

Actin, cytoplasmic 1

ACTB

Select a section on the left to see content.

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Miscellaneous

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Cytoskeleton

Nucleus

Cytoskeleton

Cytosol

Nucleus

Plasma Membrane

Other locations

Keywords - Cellular componenti

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Keywords - PTMi

Proteomic databases

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

3D structure databases

Miscellaneous databases

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

Experimental Info

Sequence databases

Genome annotation databases

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Family and domain databases

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Documents

UniProt is an ELIXIR core data resource

Your basket is currently empty. ⁱ

Functionⁱ

GO - Molecular functionⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ

Keywords - Technical termⁱ