HUMAN:ACTB

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	ACTB
Protein Name(s)	Actin, cytoplasmic 1 Beta-actin Actin, cytoplasmic 1, N-terminally processed
External Links
UniProt	P60709
EMBL	X00351 M10277 X63432 AY582799 AC006483 BC001301 BC002409 BC004251 BC008633 BC012854 BC013380 BC014861 BC016045 V00478
CCDS	CCDS5341.1
PIR	A25168
RefSeq	NP_001092.1
UniGene	Hs.520640
PDB	3BYH 3D2U 3LUE
PDBsum	3BYH 3D2U 3LUE
ProteinModelPortal	P60709
SMR	P60709
BioGrid	106575
DIP	DIP-29686N
IntAct	P60709
MINT	MINT-220312
ChEMBL	CHEMBL2062353
PhosphoSite	P60709
DMDM	46397333
DOSAC-COBS-2DPAGE	P60709 P60709_OR_P63261
REPRODUCTION-2DPAGE	P60709
SWISS-2DPAGE	P60709
UCD-2DPAGE	P60709
MaxQB	P60709
PaxDb	P60709
PeptideAtlas	P60709
PRIDE	P60709
DNASU	60
Ensembl	ENST00000331789
GeneID	60
KEGG	hsa:60
UCSC	uc003soq.4
CTD	60
GeneCards	GC07M005566
HGNC	HGNC:132
HPA	CAB002621 HPA041264 HPA041271
MIM	102630 243310 607371
neXtProt	NX_P60709
Orphanet	2995 79107
PharmGKB	PA24457
eggNOG	COG5277
HOVERGEN	HBG003771
InParanoid	P60709
KO	K05692
OMA	ASMLQMW
OrthoDB	EOG72RMZ1
PhylomeDB	P60709
TreeFam	TF354237
Reactome	REACT_11035 REACT_11049 REACT_147867 REACT_160086 REACT_16936 REACT_17050 REACT_172610 REACT_19195 REACT_20649 REACT_22266 REACT_22365 REACT_228085 REACT_228166 REACT_228189 REACT_24970
SignaLink	P60709
ChiTaRS	ACTB
EvolutionaryTrace	P60709
GeneWiki	Beta-actin
GenomeRNAi	60
NextBio	253
PRO	PR:P60709
Proteomes	UP000005640
Bgee	P60709
CleanEx	HS_ACTB
ExpressionAtlas	P60709
Genevestigator	P60709
GO	GO:0030424 GO:0072562 GO:0030863 GO:0005737 GO:0036464 GO:0005856 GO:0005829 GO:0005615 GO:0070062 GO:0005925 GO:0016020 GO:0070688 GO:0035267 GO:0000790 GO:0005654 GO:0014069 GO:0043234 GO:0030529 GO:0005524 GO:0019894 GO:0050998 GO:0005200 GO:0030957 GO:0051084 GO:0034332 GO:0043044 GO:0007411 GO:0007596 GO:0034329 GO:0045216 GO:0006928 GO:0044267 GO:0006325 GO:0038096 GO:0045087 GO:0061024 GO:0070527 GO:0006457 GO:0001895 GO:0021762
InterPro	IPR004000 IPR020902 IPR004001
PANTHER	PTHR11937
Pfam	PF00022
PRINTS	PR00190
SMART	SM00268
PROSITE	PS00406 PS00432 PS01132

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0051621	regulation of norepinephrine uptake	PMID:18331289^[1]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60711	P	part_of:(GO:0022898) occurs_in:(CL:0000540) occurs_in:(UBERON:0001870)	Seeded From UniProt	complete
involved_in	GO:0051621	regulation of norepinephrine uptake	PMID:18331289^[1]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60711	P	part_of:(GO:0022898) occurs_in:(CL:0000540) occurs_in:(UBERON:0002148)	Seeded From UniProt	complete
involved_in	GO:0022898	regulation of transmembrane transporter activity	PMID:18331289^[1]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60711	P	has_regulation_target:(UniProtKB:P23975) regulates_transport_of:(CHEBI:33569) occurs_in:(CL:0000540) occurs_in:(UBERON:0001870)	Seeded From UniProt	complete
involved_in	GO:0022898	regulation of transmembrane transporter activity	PMID:18331289^[1]	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60711	P	has_regulation_target:(UniProtKB:P23975) regulates_transport_of:(CHEBI:33569) occurs_in:(CL:0000540) occurs_in:(UBERON:0002148)	Seeded From UniProt	complete
involved_in	GO:0051621	regulation of norepinephrine uptake	PMID:18331289^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P37840	P	part_of:(GO:0022898)	Seeded From UniProt	complete
involved_in	GO:0022898	regulation of transmembrane transporter activity	PMID:18331289^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P37840	P	has_regulation_target:(UniProtKB:P23975) regulates_transport_of:(CHEBI:33569)	Seeded From UniProt	complete
involved_in	GO:1903076	regulation of protein localization to plasma membrane	PMID:18331289^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	has_regulation_target:(UniProtKB:P23975) regulates:(GO:0015874)	Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:24327345^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13627-2	F		Seeded From UniProt	complete
involved_in	GO:0072749	cellular response to cytochalasin B	PMID:6202424^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60711	C	part_of:(UBERON:0000955)	Seeded From UniProt	complete
involved_in	GO:0000079	regulation of cyclin-dependent protein serine/threonine kinase activity	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60711	P	has_regulation_target:(UniProtKB:Q00535) happens_during:(GO:0031532)	Seeded From UniProt	complete
enables	GO:0048156	tau protein binding	PMID:28386764^[4]	ECO:0000303	author statement without traceable support used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0098974	postsynaptic actin cytoskeleton organization	PMID:18341992^[5]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0098973	structural constituent of postsynaptic actin cytoskeleton	PMID:18341992^[5]	ECO:0000314	direct assay evidence used in manual assertion		F	occurs_in:(GO:0043197) occurs_in:(CL:0002608)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:11687588^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0015629	actin cytoskeleton	PMID:11687588^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:11687588^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60706	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60706	C		Seeded From UniProt	complete
part_of	GO:0097433	dense body	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60706	C		Seeded From UniProt	complete
involved_in	GO:0032091	negative regulation of protein binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:P60710	P	has_regulation_target:(UniProtKB:Q15078) has_regulation_target:(UniProtKB:Q00535)	Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:G1NS52	C		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:Q58J72	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:24327345^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	PMID:24327345^[2]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:23533145^[7]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0031982	vesicle	PMID:19190083^[8]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002202)	Seeded From UniProt	complete
involved_in	GO:0070527	platelet aggregation	PMID:23382103^[9]	ECO:0007001	high throughput mutant phenotypic evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005925	focal adhesion	PMID:21423176^[10]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000057)	Seeded From UniProt	complete
part_of	GO:0036464	cytoplasmic ribonucleoprotein granule	PMID:15121898^[11]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0016020	membrane	PMID:19946888^[12]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0072562	blood microparticle	PMID:22516433^[13]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19199708^[14]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001831)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:11487543^[15]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	produced_by:(CL:0002563)	Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:20458337^[16]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0000639)	Seeded From UniProt	complete
part_of	GO:0032991	protein-containing complex	PMID:16217013^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0043044	ATP-dependent chromatin remodeling	PMID:16217013^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
contributes_to	GO:0031492	nucleosomal DNA binding	PMID:16217013^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0021762	substantia nigra development	PMID:22926577^[18]	ECO:0007007	high throughput expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:16502470^[19]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001914)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:23580065^[20]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
part_of	GO:0005615	extracellular space	PMID:22664934^[21]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001827)	Seeded From UniProt	complete
involved_in	GO:0001895	retina homeostasis	PMID:23580065^[20]	ECO:0007007	high throughput expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
contributes_to	GO:0000980	RNA polymerase II distal enhancer sequence-specific DNA binding	PMID:16217013^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
contributes_to	GO:0000978	RNA polymerase II proximal promoter sequence-specific DNA binding	PMID:16217013^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0000790	nuclear chromatin	PMID:16217013^[17]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0050998	nitric-oxide synthase binding	PMID:17502619^[22]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P29474	F		Seeded From UniProt	complete
enables	GO:0030957	Tat protein binding	PMID:16687403^[23]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P04608	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:21362503^[24]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(CL:0002367)	Seeded From UniProt	complete
part_of	GO:0035267	NuA4 histone acetyltransferase complex	PMID:10966108^[25]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:1990904	ribonucleoprotein complex	PMID:17289661^[26]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019894	kinesin binding	PMID:18680169^[27]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8NI77	F		Seeded From UniProt	complete
involved_in	GO:0048870	cell motility	PMID:6202424^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:18341992^[5]	ECO:0006063	over expression analysis evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:18341992^[5]	ECO:0006054	pharmacological assay evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:18341992^[5]	ECO:0006039	genetically encoded fluorescent electrophysiology assay evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098978	glutamatergic synapse	PMID:18341992^[5]	ECO:0005589	confocal microscopy evidence used in manual assertion		C	part_of:(UBERON:0002421)	Seeded From UniProt	complete
	GO:0005634	nucleus	PMID:28334682^[28]	ECO:0000314			C		Organism: Homo sapiens. Paper’s Protein Name: β-actin. UniProt Protein Name: Actin, cytoplasmic 1 or Beta-actin. Notes: Figure 3F is used. MCF-7 cells (which are human) have their nuclei stained blue and are also immunostained so that β-actin will appear green. As can be seen in the micrographs, there is significant overlap between these colors. Thus a non-transient link is established between β-actin and the nucleus.	complete CACAO 12740
enables	GO:0098973	structural constituent of postsynaptic actin cytoskeleton	PMID:18341992^[5]	ECO:0006063	over expression analysis evidence used in manual assertion		F	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002421)	Seeded From UniProt	complete
enables	GO:0098973	structural constituent of postsynaptic actin cytoskeleton	PMID:18341992^[5]	ECO:0006054	pharmacological assay evidence used in manual assertion		F	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002421)	Seeded From UniProt	complete
enables	GO:0098973	structural constituent of postsynaptic actin cytoskeleton	PMID:18341992^[5]	ECO:0006039	genetically encoded fluorescent electrophysiology assay evidence used in manual assertion		F	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002421)	Seeded From UniProt	complete
enables	GO:0098973	structural constituent of postsynaptic actin cytoskeleton	PMID:18341992^[5]	ECO:0005589	confocal microscopy evidence used in manual assertion		F	occurs_in:(GO:0098978) occurs_in:(UBERON:0000061) occurs_in:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098871	postsynaptic actin cytoskeleton	PMID:18341992^[5]	ECO:0006063	over expression analysis evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0002421)	Seeded From UniProt	complete
part_of	GO:0098871	postsynaptic actin cytoskeleton	PMID:18341992^[5]	ECO:0005589	confocal microscopy evidence used in manual assertion		C	part_of:(GO:0098978) part_of:(UBERON:0000061) part_of:(UBERON:0002421)	Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25910212^[29]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:25416956^[30]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21516116^[31]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:20383143^[32]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19000816^[33]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18234857^[34]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:17404223^[35]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16189514^[36]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P60709	F		Seeded From UniProt	complete
part_of	GO:0098685	Schaffer collateral - CA1 synapse	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P60710 ensembl:ENSMUSP00000098066	C		Seeded From UniProt	complete
involved_in	GO:0048488	synaptic vesicle endocytosis	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P60710 ensembl:ENSMUSP00000098066	P		Seeded From UniProt	complete
part_of	GO:0044305	calyx of Held	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P60710 ensembl:ENSMUSP00000098066	C		Seeded From UniProt	complete
involved_in	GO:0032091	negative regulation of protein binding	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P60710 ensembl:ENSMUSP00000098066	P		Seeded From UniProt	complete
part_of	GO:0030863	cortical cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P60710 ensembl:ENSMUSP00000098066	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P60710 ensembl:ENSMUSP00000098066	C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P60710 ensembl:ENSMUSP00000098066	C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000107	ECO:0000265	sequence orthology evidence used in automatic assertion	UniProtKB:P60710 ensembl:ENSMUSP00000098066	C		Seeded From UniProt	complete
involved_in	GO:0051623	positive regulation of norepinephrine uptake	PMID:18331289^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0098793	presynapse	PMID:18331289^[1]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	PMID:16130169^[37]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	PMID:16130169^[37]	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0005200	structural constituent of cytoskeleton	PMID:6202424^[3]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0061024	membrane organization	Reactome:R-HSA-199991	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048013	ephrin receptor signaling pathway	Reactome:R-HSA-2682334	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045815	positive regulation of gene expression, epigenetic	Reactome:R-HSA-5250924	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0038096	Fc-gamma receptor signaling pathway involved in phagocytosis	Reactome:R-HSA-2029480	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0034329	cell junction assembly	Reactome:R-HSA-446728	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0016579	protein deubiquitination	Reactome:R-HSA-5688426	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005886	plasma membrane	Reactome:R-HSA-8871194 Reactome:R-HSA-8871193 Reactome:R-HSA-8869438 Reactome:R-HSA-8868661 Reactome:R-HSA-8868660 Reactome:R-HSA-8868659 Reactome:R-HSA-8868658 Reactome:R-HSA-8868651 Reactome:R-HSA-8868648 Reactome:R-HSA-8868236 Reactome:R-HSA-8868230 Reactome:R-HSA-3928654	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-5666001 Reactome:R-HSA-5665982 Reactome:R-HSA-5665809 Reactome:R-HSA-5665802 Reactome:R-HSA-5665767 Reactome:R-HSA-5665751 Reactome:R-HSA-5626507 Reactome:R-HSA-5218916 Reactome:R-HSA-445089 Reactome:R-HSA-443779 Reactome:R-HSA-430347 Reactome:R-HSA-3928595 Reactome:R-HSA-392751 Reactome:R-HSA-2197690 Reactome:R-HSA-203070 Reactome:R-HSA-2029476 Reactome:R-HSA-2029473 Reactome:R-HSA-2029466 Reactome:R-HSA-1861595	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005654	nucleoplasm	Reactome:R-NUL-4551334 Reactome:R-HSA-5689544 Reactome:R-HSA-5250947	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963	C		Seeded From UniProt	complete
part_of	GO:0005856	cytoskeleton	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0206 UniProtKB-SubCell:SL-0090	C		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 ^1.8 Jeannotte, AM & Sidhu, A (2008) Regulated interactions of the norepineprhine transporter by the actin and microtubule cytoskeletons. J. Neurochem. 105 1668-82 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 Kaczmarski, W et al. (2014) Intracellular distribution of differentially phosphorylated dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A). J. Neurosci. Res. 92 162-73 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 Toyama, S & Toyama, S (1984) A variant form of beta-actin in a mutant of KB cells resistant to cytochalasin B. Cell 37 609-14 PubMed GONUTS page
↑ Guo, T et al. (2017) Roles of tau protein in health and disease. Acta Neuropathol. 133 665-704 PubMed GONUTS page
↑ ^5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 Honkura, N et al. (2008) The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines. Neuron 57 719-29 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Zhang, S et al. (2002) Nuclear DNA helicase II/RNA helicase A binds to filamentous actin. J. Biol. Chem. 277 843-53 PubMed GONUTS page
↑ Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page
↑ Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page
↑ Fröbel, J et al. (2013) Platelet proteome analysis reveals integrin-dependent aggregation defects in patients with myelodysplastic syndromes. Mol. Cell Proteomics 12 1272-80 PubMed GONUTS page
↑ Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page
↑ Villacé, P et al. (2004) The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 2411-20 PubMed GONUTS page
↑ Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page
↑ Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page
↑ Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page
↑ van Niel, G et al. (2001) Intestinal epithelial cells secrete exosome-like vesicles. Gastroenterology 121 337-49 PubMed GONUTS page
↑ Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page
↑ ^17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 Mahajan, MC et al. (2005) Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF form a chromatin remodeling complex at the beta-globin locus control region. Proc. Natl. Acad. Sci. U.S.A. 102 15012-7 PubMed GONUTS page
↑ Chen, S et al. (2012) Quantitative proteomic analysis of human substantia nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis. Neurochem. Res. 37 2805-13 PubMed GONUTS page
↑ Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page
↑ ^20.0 ^20.1 Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page
↑ Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page
↑ Ji, Y et al. (2007) beta-Actin regulates platelet nitric oxide synthase 3 activity through interaction with heat shock protein 90. Proc. Natl. Acad. Sci. U.S.A. 104 8839-44 PubMed GONUTS page
↑ Mahmoudi, T et al. (2006) The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation of the HIV promoter. J. Biol. Chem. 281 19960-8 PubMed GONUTS page
↑ Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page
↑ Ikura, T et al. (2000) Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 102 463-73 PubMed GONUTS page
↑ Jønson, L et al. (2007) Molecular composition of IMP1 ribonucleoprotein granules. Mol. Cell Proteomics 6 798-811 PubMed GONUTS page
↑ Zusev, M & Benayahu, D (2008) New insights on cellular distribution, microtubule interactions and post-translational modifications of MS-KIF18A. J. Cell. Physiol. 217 618-25 PubMed GONUTS page
↑ Lewinska, A et al. (2017) Phytochemical-induced nucleolar stress results in the inhibition of breast cancer cell proliferation. Redox Biol 12 469-482 PubMed GONUTS page
↑ Sahni, N et al. (2015) Widespread macromolecular interaction perturbations in human genetic disorders. Cell 161 647-660 PubMed GONUTS page
↑ Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page
↑ Yu, H et al. (2011) Next-generation sequencing to generate interactome datasets. Nat. Methods 8 478-80 PubMed GONUTS page
↑ Galkin, VE et al. (2010) Opening of tandem calponin homology domains regulates their affinity for F-actin. Nat. Struct. Mol. Biol. 17 614-6 PubMed GONUTS page
↑ Kursula, I et al. (2008) Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum. Structure 16 1638-48 PubMed GONUTS page
↑ Galkin, VE et al. (2008) High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex. Proc. Natl. Acad. Sci. U.S.A. 105 1494-8 PubMed GONUTS page
↑ Okamoto, K et al. (2007) The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure. Proc. Natl. Acad. Sci. U.S.A. 104 6418-23 PubMed GONUTS page
↑ Rual, JF et al. (2005) Towards a proteome-scale map of the human protein-protein interaction network. Nature 437 1173-8 PubMed GONUTS page
↑ ^37.0 ^37.1 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

[PMID:18331289-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 ^1.5 ^1.6 ^1.7 ^1.8 Jeannotte, AM & Sidhu, A (2008) Regulated interactions of the norepineprhine transporter by the actin and microtubule cytoskeletons. J. Neurochem. 105 1668-82 PubMed GONUTS page

[PMID:24327345-2] 2.0 ^2.1 ^2.2 Kaczmarski, W et al. (2014) Intracellular distribution of differentially phosphorylated dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A). J. Neurosci. Res. 92 162-73 PubMed GONUTS page

[PMID:6202424-3] 3.0 ^3.1 ^3.2 Toyama, S & Toyama, S (1984) A variant form of beta-actin in a mutant of KB cells resistant to cytochalasin B. Cell 37 609-14 PubMed GONUTS page

[PMID:28386764-4] Guo, T et al. (2017) Roles of tau protein in health and disease. Acta Neuropathol. 133 665-704 PubMed GONUTS page

[PMID:18341992-5] 5.00 ^5.01 ^5.02 ^5.03 ^5.04 ^5.05 ^5.06 ^5.07 ^5.08 ^5.09 ^5.10 ^5.11 Honkura, N et al. (2008) The subspine organization of actin fibers regulates the structure and plasticity of dendritic spines. Neuron 57 719-29 PubMed GONUTS page

[PMID:11687588-6] 6.0 ^6.1 ^6.2 Zhang, S et al. (2002) Nuclear DNA helicase II/RNA helicase A binds to filamentous actin. J. Biol. Chem. 277 843-53 PubMed GONUTS page

[PMID:23533145-7] Principe, S et al. (2013) In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. Proteomics 13 1667-71 PubMed GONUTS page

[PMID:19190083-8] Kesimer, M et al. (2009) Characterization of exosome-like vesicles released from human tracheobronchial ciliated epithelium: a possible role in innate defense. FASEB J. 23 1858-68 PubMed GONUTS page

[PMID:23382103-9] Fröbel, J et al. (2013) Platelet proteome analysis reveals integrin-dependent aggregation defects in patients with myelodysplastic syndromes. Mol. Cell Proteomics 12 1272-80 PubMed GONUTS page

[PMID:21423176-10] Kuo, JC et al. (2011) Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 13 383-93 PubMed GONUTS page

[PMID:15121898-11] Villacé, P et al. (2004) The composition of Staufen-containing RNA granules from human cells indicates their role in the regulated transport and translation of messenger RNAs. Nucleic Acids Res. 32 2411-20 PubMed GONUTS page

[PMID:19946888-12] Ghosh, D et al. (2010) Defining the membrane proteome of NK cells. J Mass Spectrom 45 1-25 PubMed GONUTS page

[PMID:22516433-13] Bastos-Amador, P et al. (2012) Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. J Proteomics 75 3574-84 PubMed GONUTS page

[PMID:19199708-14] Gonzalez-Begne, M et al. (2009) Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). J. Proteome Res. 8 1304-14 PubMed GONUTS page

[PMID:11487543-15] van Niel, G et al. (2001) Intestinal epithelial cells secrete exosome-like vesicles. Gastroenterology 121 337-49 PubMed GONUTS page

[PMID:20458337-16] Buschow, SI et al. () MHC class II-associated proteins in B-cell exosomes and potential functional implications for exosome biogenesis. Immunol. Cell Biol. 88 851-6 PubMed GONUTS page

[PMID:16217013-17] 17.0 ^17.1 ^17.2 ^17.3 ^17.4 ^17.5 Mahajan, MC et al. (2005) Heterogeneous nuclear ribonucleoprotein C1/C2, MeCP1, and SWI/SNF form a chromatin remodeling complex at the beta-globin locus control region. Proc. Natl. Acad. Sci. U.S.A. 102 15012-7 PubMed GONUTS page

[PMID:22926577-18] Chen, S et al. (2012) Quantitative proteomic analysis of human substantia nigra in Alzheimer's disease, Huntington's disease and Multiple sclerosis. Neurochem. Res. 37 2805-13 PubMed GONUTS page

[PMID:16502470-19] Palmer, DJ et al. (2006) Human colostrum: identification of minor proteins in the aqueous phase by proteomics. Proteomics 6 2208-16 PubMed GONUTS page

[PMID:23580065-20] 20.0 ^20.1 Pieragostino, D et al. (2013) Shotgun proteomics reveals specific modulated protein patterns in tears of patients with primary open angle glaucoma naïve to therapy. Mol Biosyst 9 1108-16 PubMed GONUTS page

[PMID:22664934-21] Böhm, D et al. (2012) Comparison of tear protein levels in breast cancer patients and healthy controls using a de novo proteomic approach. Oncol. Rep. 28 429-38 PubMed GONUTS page

[PMID:17502619-22] Ji, Y et al. (2007) beta-Actin regulates platelet nitric oxide synthase 3 activity through interaction with heat shock protein 90. Proc. Natl. Acad. Sci. U.S.A. 104 8839-44 PubMed GONUTS page

[PMID:16687403-23] Mahmoudi, T et al. (2006) The SWI/SNF chromatin-remodeling complex is a cofactor for Tat transactivation of the HIV promoter. J. Biol. Chem. 281 19960-8 PubMed GONUTS page

[PMID:21362503-24] Stamer, WD et al. (2011) Protein profile of exosomes from trabecular meshwork cells. J Proteomics 74 796-804 PubMed GONUTS page

[PMID:10966108-25] Ikura, T et al. (2000) Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis. Cell 102 463-73 PubMed GONUTS page

[PMID:17289661-26] Jønson, L et al. (2007) Molecular composition of IMP1 ribonucleoprotein granules. Mol. Cell Proteomics 6 798-811 PubMed GONUTS page

[PMID:18680169-27] Zusev, M & Benayahu, D (2008) New insights on cellular distribution, microtubule interactions and post-translational modifications of MS-KIF18A. J. Cell. Physiol. 217 618-25 PubMed GONUTS page

[PMID:28334682-28] Lewinska, A et al. (2017) Phytochemical-induced nucleolar stress results in the inhibition of breast cancer cell proliferation. Redox Biol 12 469-482 PubMed GONUTS page

[PMID:25910212-29] Sahni, N et al. (2015) Widespread macromolecular interaction perturbations in human genetic disorders. Cell 161 647-660 PubMed GONUTS page

[PMID:25416956-30] Rolland, T et al. (2014) A proteome-scale map of the human interactome network. Cell 159 1212-26 PubMed GONUTS page

[PMID:21516116-31] Yu, H et al. (2011) Next-generation sequencing to generate interactome datasets. Nat. Methods 8 478-80 PubMed GONUTS page

[PMID:20383143-32] Galkin, VE et al. (2010) Opening of tandem calponin homology domains regulates their affinity for F-actin. Nat. Struct. Mol. Biol. 17 614-6 PubMed GONUTS page

[PMID:19000816-33] Kursula, I et al. (2008) Structural basis for parasite-specific functions of the divergent profilin of Plasmodium falciparum. Structure 16 1638-48 PubMed GONUTS page

[PMID:18234857-34] Galkin, VE et al. (2008) High-resolution cryo-EM structure of the F-actin-fimbrin/plastin ABD2 complex. Proc. Natl. Acad. Sci. U.S.A. 105 1494-8 PubMed GONUTS page

[PMID:17404223-35] Okamoto, K et al. (2007) The role of CaMKII as an F-actin-bundling protein crucial for maintenance of dendritic spine structure. Proc. Natl. Acad. Sci. U.S.A. 104 6418-23 PubMed GONUTS page

[PMID:16189514-36] Rual, JF et al. (2005) Towards a proteome-scale map of the human protein-protein interaction network. Nature 437 1173-8 PubMed GONUTS page

[PMID:16130169-37] 37.0 ^37.1 Bruneel, A et al. (2005) Proteomics of human umbilical vein endothelial cells applied to etoposide-induced apoptosis. Proteomics 5 3876-84 PubMed GONUTS page

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