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Protein

Alpha-actinin-4

Gene

ACTN4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein (Probable). Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (PubMed:15772161). Involved in tight junction assembly in epithelial cells probably through interaction with MICALL2. Links MICALL2 to the actin cytoskeleton and recruits it to the tight junctions (By similarity). May also function as a transcriptional coactivator, stimulating transcription mediated by the nuclear hormone receptors PPARG and RARA (PubMed:22351778).By similarity1 Publication2 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Calcium bindingi778 – 7891PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi819 – 8302PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • calcium ion binding Source: InterPro
  • chromatin DNA binding Source: UniProtKB
  • integrin binding Source: UniProtKB
  • ion channel binding Source: UniProtKB
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • nucleoside binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB
  • RNA binding Source: UniProtKB
  • RNA polymerase II regulatory region sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • actin filament bundle assembly Source: Ensembl
  • bicellular tight junction assembly Source: Ensembl
  • negative regulation of cellular component movement Source: Ensembl
  • negative regulation of substrate adhesion-dependent cell spreading Source: UniProtKB
  • peroxisome proliferator activated receptor signaling pathway Source: UniProtKB
  • platelet degranulation Source: Reactome
  • positive regulation of cell migration Source: UniProtKB
  • positive regulation of cellular component movement Source: UniProtKB
  • positive regulation of NIK/NF-kappaB signaling Source: UniProtKB
  • positive regulation of pinocytosis Source: Ensembl
  • positive regulation of sodium:proton antiporter activity Source: UniProtKB
  • protein localization to bicellular tight junction Source: Ensembl
  • protein transport Source: UniProtKB-KW
  • regulation of apoptotic process Source: UniProtKB
  • regulation of nucleic acid-templated transcription Source: UniProtKB
  • response to hypoxia Source: Ensembl
  • retinoic acid receptor signaling pathway Source: UniProtKB
  • vesicle transport along actin filament Source: UniProtKB

Keywordsi

Molecular functionActin-binding
Biological processProtein transport, Transport
LigandCalcium, Metal-binding

Enzyme and pathway databases

ReactomeiR-HSA-114608 Platelet degranulation
R-HSA-373753 Nephrin family interactions
SIGNORiO43707

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin-4Curated
Alternative name(s):
Non-muscle alpha-actinin 41 Publication
Gene namesi
Name:ACTN4Imported
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

EuPathDBiHostDB:ENSG00000130402.11
HGNCiHGNC:166 ACTN4
MIMi604638 gene
neXtProtiNX_O43707

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Focal segmental glomerulosclerosis 1 (FSGS1)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA renal pathology defined by the presence of segmental sclerosis in glomeruli and resulting in proteinuria, reduced glomerular filtration rate and progressive decline in renal function. Renal insufficiency often progresses to end-stage renal disease, a highly morbid state requiring either dialysis therapy or kidney transplantation.
See also OMIM:603278
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07979759W → R in FSGS1. 1 Publication1
Natural variantiVAR_07979872E → Q in FSGS1. 1 Publication1
Natural variantiVAR_079799153F → L in FSGS1; unknown pathological significance. 1 Publication1
Natural variantiVAR_010378255K → E in FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity. 4 PublicationsCorresponds to variant dbSNP:rs121908415EnsemblClinVar.1
Natural variantiVAR_010379259T → I in FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity. 4 PublicationsCorresponds to variant dbSNP:rs121908416EnsemblClinVar.1
Natural variantiVAR_072115262S → F in FSGS1. 1 Publication1
Natural variantiVAR_010380262S → P in FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity. 4 PublicationsCorresponds to variant dbSNP:rs121908417EnsemblClinVar.1
Natural variantiVAR_079800310R → Q in FSGS1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs112545413EnsemblClinVar.1
Natural variantiVAR_072116427A → T in FSGS1. 1 PublicationCorresponds to variant dbSNP:rs201128110Ensembl.1
Natural variantiVAR_072117748N → D in FSGS1. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi87 – 88LL → AA: Reduced interaction with RARA. Loss of the transcriptional coac tivator activity toward RARA. 1 Publication2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi81
MalaCardsiACTN4
MIMi603278 phenotype
OpenTargetsiENSG00000130402
Orphaneti93213 Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis
PharmGKBiPA23

Polymorphism and mutation databases

BioMutaiACTN4

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000734401 – 911Alpha-actinin-4Add BLAST911

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei114N6-acetyllysineCombined sources1
Modified residuei249PhosphothreonineCombined sources1
Modified residuei592N6-acetyllysineCombined sources1
Modified residuei625N6-acetyllysineCombined sources1
Modified residuei779N6-acetyllysineBy similarity1
Modified residuei859N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiO43707
MaxQBiO43707
PaxDbiO43707
PeptideAtlasiO43707
PRIDEiO43707

2D gel databases

REPRODUCTION-2DPAGEO43707

PTM databases

CarbonylDBiO43707
iPTMnetiO43707
PhosphoSitePlusiO43707
SwissPalmiO43707

Miscellaneous databases

PMAP-CutDBO43707

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiENSG00000130402
CleanExiHS_ACTN4
ExpressionAtlasiO43707 baseline and differential
GenevisibleiO43707 HS

Organism-specific databases

HPAiHPA001873
HPA006035

Interactioni

Subunit structurei

Homodimer; antiparallel (By similarity). Binds TRIM3 at the N-terminus (By similarity). Interacts with MICALL2 (preferentially in opened conformation); stimulated by RAB13 activation (By similarity). Identified in a complex with CASK, IQGAP1, MAGI2, NPHS1, SPTAN1 and SPTBN1 (By similarity). Identified in a IGF2BP1-dependent mRNP granule complex containing untranslated mRNAs. Component of the CART complex, at least composed of ACTN4, HGS/HRS, MYO5B and TRIM3. Interacts with BAIAP1 and PDLIM2. Interacts with PPARG and RARA. Binds to VCL; this interaction triggers VCL conformational changes (PubMed:15988023).By similarity5 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • actin binding Source: UniProtKB
  • actin filament binding Source: UniProtKB
  • integrin binding Source: UniProtKB
  • ion channel binding Source: UniProtKB
  • nuclear hormone receptor binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • retinoic acid receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106596, 134 interactors
CORUMiO43707
DIPiDIP-33179N
IntActiO43707, 87 interactors
MINTiO43707
STRINGi9606.ENSP00000252699

Structurei

Secondary structure

1911
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi47 – 64Combined sources18
Helixi65 – 67Combined sources3
Turni74 – 80Combined sources7
Helixi82 – 92Combined sources11
Helixi105 – 120Combined sources16
Turni121 – 123Combined sources3
Helixi131 – 135Combined sources5
Helixi139 – 153Combined sources15
Turni154 – 157Combined sources4
Helixi165 – 177Combined sources13
Beta strandi187 – 189Combined sources3
Helixi190 – 192Combined sources3
Helixi196 – 205Combined sources10
Helixi207 – 209Combined sources3
Helixi212 – 214Combined sources3
Helixi220 – 234Combined sources15
Helixi243 – 248Combined sources6
Beta strandi249 – 251Combined sources3
Helixi254 – 267Combined sources14
Helixi519 – 552Combined sources34
Helixi560 – 600Combined sources41
Beta strandi606 – 608Combined sources3
Helixi616 – 641Combined sources26
Helixi736 – 756Combined sources21

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1WLXNMR-A519-645[»]
1YDIX-ray1.80B734-757[»]
2R0OX-ray2.20A/B47-271[»]
ProteinModelPortaliO43707
SMRiO43707
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43707

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini50 – 154Calponin-homology (CH) 1PROSITE-ProRule annotationAdd BLAST105
Domaini163 – 269Calponin-homology (CH) 2PROSITE-ProRule annotationAdd BLAST107
Repeati293 – 403Spectrin 1Sequence analysisAdd BLAST111
Repeati413 – 518Spectrin 2Sequence analysisAdd BLAST106
Repeati528 – 639Spectrin 3Sequence analysisAdd BLAST112
Repeati649 – 752Spectrin 4Sequence analysisAdd BLAST104
Domaini765 – 800EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini806 – 841EF-hand 2PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 269Actin-bindingAdd BLAST269
Regioni12 – 26Interaction with VCLCombined sources1 PublicationAdd BLAST15
Regioni40 – 61Interaction with VCLCombined sources1 PublicationAdd BLAST22
Regioni108 – 126Interaction with VCLCombined sources1 PublicationAdd BLAST19
Regioni177 – 192Polyphosphoinositide (PIP2)-bindingSequence analysisAdd BLAST16
Regioni736 – 911Mediates interaction with MICALL2By similarityAdd BLAST176

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi84 – 88LXXLL motif1 Publication5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi19 – 26Poly-GlySequence analysis8

Domaini

Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif that mediates interaction with nuclear receptors.1 Publication

Sequence similaritiesi

Belongs to the alpha-actinin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0035 Eukaryota
COG5069 LUCA
GeneTreeiENSGT00760000118813
HOGENOMiHOG000263418
HOVERGENiHBG050453
InParanoidiO43707
KOiK05699
OMAiQANIVGP
OrthoDBiEOG091G020R
PhylomeDBiO43707
TreeFamiTF352676

Family and domain databases

CDDicd00014 CH, 2 hits
cd00051 EFh, 1 hit
Gene3Di1.10.418.10, 2 hits
InterProiView protein in InterPro
IPR001589 Actinin_actin-bd_CS
IPR029637 ACTN4
IPR001715 CH-domain
IPR036872 CH_dom_sf
IPR011992 EF-hand-dom_pair
IPR014837 EF-hand_Ca_insen
IPR018247 EF_Hand_1_Ca_BS
IPR002048 EF_hand_dom
IPR018159 Spectrin/alpha-actinin
IPR002017 Spectrin_repeat
PANTHERiPTHR43947:SF7 PTHR43947:SF7, 1 hit
PfamiView protein in Pfam
PF00307 CH, 2 hits
PF08726 EFhand_Ca_insen, 1 hit
PF00435 Spectrin, 4 hits
SMARTiView protein in SMART
SM00033 CH, 2 hits
SM00054 EFh, 2 hits
SM00150 SPEC, 4 hits
SUPFAMiSSF47473 SSF47473, 1 hit
SSF47576 SSF47576, 1 hit
PROSITEiView protein in PROSITE
PS00019 ACTININ_1, 1 hit
PS00020 ACTININ_2, 1 hit
PS50021 CH, 2 hits
PS00018 EF_HAND_1, 1 hit
PS50222 EF_HAND_2, 2 hits

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43707-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MVDYHAANQS YQYGPSSAGN GAGGGGSMGD YMAQEDDWDR DLLLDPAWEK
60 70 80 90 100
QQRKTFTAWC NSHLRKAGTQ IENIDEDFRD GLKLMLLLEV ISGERLPKPE
110 120 130 140 150
RGKMRVHKIN NVNKALDFIA SKGVKLVSIG AEEIVDGNAK MTLGMIWTII
160 170 180 190 200
LRFAIQDISV EETSAKEGLL LWCQRKTAPY KNVNVQNFHI SWKDGLAFNA
210 220 230 240 250
LIHRHRPELI EYDKLRKDDP VTNLNNAFEV AEKYLDIPKM LDAEDIVNTA
260 270 280 290 300
RPDEKAIMTY VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEHLMEDYEK
310 320 330 340 350
LASDLLEWIR RTIPWLEDRV PQKTIQEMQQ KLEDFRDYRR VHKPPKVQEK
360 370 380 390 400
CQLEINFNTL QTKLRLSNRP AFMPSEGKMV SDINNGWQHL EQAEKGYEEW
410 420 430 440 450
LLNEIRRLER LDHLAEKFRQ KASIHEAWTD GKEAMLKHRD YETATLSDIK
460 470 480 490 500
ALIRKHEAFE SDLAAHQDRV EQIAAIAQEL NELDYYDSHN VNTRCQKICD
510 520 530 540 550
QWDALGSLTH SRREALEKTE KQLEAIDQLH LEYAKRAAPF NNWMESAMED
560 570 580 590 600
LQDMFIVHTI EEIEGLISAH DQFKSTLPDA DREREAILAI HKEAQRIAES
610 620 630 640 650
NHIKLSGSNP YTTVTPQIIN SKWEKVQQLV PKRDHALLEE QSKQQSNEHL
660 670 680 690 700
RRQFASQANV VGPWIQTKME EIGRISIEMN GTLEDQLSHL KQYERSIVDY
710 720 730 740 750
KPNLDLLEQQ HQLIQEALIF DNKHTNYTME HIRVGWEQLL TTIARTINEV
760 770 780 790 800
ENQILTRDAK GISQEQMQEF RASFNHFDKD HGGALGPEEF KACLISLGYD
810 820 830 840 850
VENDRQGEAE FNRIMSLVDP NHSGLVTFQA FIDFMSRETT DTDTADQVIA
860 870 880 890 900
SFKVLAGDKN FITAEELRRE LPPDQAEYCI ARMAPYQGPD AVPGALDYKS
910
FSTALYGESD L
Length:911
Mass (Da):104,854
Last modified:February 21, 2001 - v2
Checksum:i461580C3F22937D1
GO
Isoform ACTN4ISO (identifier: O43707-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     54-272: Missing.

Note: Does not colocalize with actin cytoskeleton structures.1 Publication
Show »
Length:692
Mass (Da):79,913
Checksum:i34C43B1217B8AA25
GO
Isoform 3 (identifier: O43707-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     89-478: Missing.

Show »
Length:521
Mass (Da):59,579
Checksum:i66A7C97A6AF6C87D
GO

Sequence cautioni

The sequence AAC17470 differs from that shown. Reason: Frameshift at positions 19, 26, 124, 130, 589, 594, 787 and 806.Curated
The sequence BAA24447 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti60C → S in AAC17470 (PubMed:10656685).Curated1
Sequence conflicti164S → L in AL047603 (PubMed:17974005).Curated1
Sequence conflicti221V → F in AU118403 (PubMed:16344560).Curated1
Sequence conflicti276T → TET in AAC17470 (PubMed:10656685).Curated1
Sequence conflicti292 – 294EHL → CSTS in AAC17470 (PubMed:10656685).Curated3
Sequence conflicti359 – 360TL → SV in AAC17470 (PubMed:10656685).Curated2
Sequence conflicti476I → S in AAC17470 (PubMed:10656685).Curated1
Sequence conflicti526I → II in AAC17470 (PubMed:10656685).Curated1
Sequence conflicti536R → P in AAC17470 (PubMed:10656685).Curated1
Sequence conflicti645Q → QQ in AAC17470 (PubMed:10656685).Curated1
Sequence conflicti673 – 674GR → A in AAC17470 (PubMed:10656685).Curated2
Sequence conflicti850A → T in AAC17470 (PubMed:10656685).Curated1
Sequence conflicti891 – 893AVP → GVR in AAC17470 (PubMed:10656685).Curated3

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_07979759W → R in FSGS1. 1 Publication1
Natural variantiVAR_07979872E → Q in FSGS1. 1 Publication1
Natural variantiVAR_079799153F → L in FSGS1; unknown pathological significance. 1 Publication1
Natural variantiVAR_010378255K → E in FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity. 4 PublicationsCorresponds to variant dbSNP:rs121908415EnsemblClinVar.1
Natural variantiVAR_010379259T → I in FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity. 4 PublicationsCorresponds to variant dbSNP:rs121908416EnsemblClinVar.1
Natural variantiVAR_072115262S → F in FSGS1. 1 Publication1
Natural variantiVAR_010380262S → P in FSGS1; no effect on protein abundance; no effect on homodimerization; loss of localization to the nucleus; prevents nuclear localization of the wild-type protein; decreased interaction with PPARG and RARA; loss of transcriptional coactivator activity; dominant negative effect on nuclear receptors-mediated transcription; increased actin-binding affinity. 4 PublicationsCorresponds to variant dbSNP:rs121908417EnsemblClinVar.1
Natural variantiVAR_079800310R → Q in FSGS1; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs112545413EnsemblClinVar.1
Natural variantiVAR_072116427A → T in FSGS1. 1 PublicationCorresponds to variant dbSNP:rs201128110Ensembl.1
Natural variantiVAR_072117748N → D in FSGS1. 1 Publication1
Natural variantiVAR_072118784A → V Rare variant found in patients with IgA nephropathy; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs771421233Ensembl.1
Natural variantiVAR_072119786G → R1 Publication1
Natural variantiVAR_072120787P → L1 Publication1
Natural variantiVAR_072121787P → S1 Publication1
Natural variantiVAR_072122793C → Y Rare variant found in patients with IgA nephropathy; unknown pathological significance. 1 Publication1
Natural variantiVAR_072123798G → D Rare variant found in patients with IgA nephropathy; unknown pathological significance. 1 Publication1
Natural variantiVAR_072124801V → M1 PublicationCorresponds to variant dbSNP:rs141727248EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_04773354 – 272Missing in isoform ACTN4ISO. 1 PublicationAdd BLAST219
Alternative sequenceiVSP_05340189 – 478Missing in isoform 3. 1 PublicationAdd BLAST390

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U48734 mRNA Translation: AAC17470.1 Frameshift.
GU987085 mRNA Translation: ADG03678.1
DQ431186 mRNA Translation: ABD96103.1
AC008649 Genomic DNA No translation available.
AC022144 Genomic DNA No translation available.
BC005033 mRNA Translation: AAH05033.1
AL047603 mRNA No translation available.
AU118403 mRNA No translation available.
D89980 mRNA Translation: BAA24447.1 Different initiation.
CCDSiCCDS12518.1 [O43707-1]
RefSeqiNP_004915.2, NM_004924.5 [O43707-1]
UniGeneiHs.270291

Genome annotation databases

EnsembliENST00000252699; ENSP00000252699; ENSG00000130402 [O43707-1]
ENST00000390009; ENSP00000439497; ENSG00000130402 [O43707-2]
ENST00000634692; ENSP00000488962; ENSG00000282844 [O43707-2]
ENST00000634960; ENSP00000489220; ENSG00000282844 [O43707-1]
GeneIDi81
KEGGihsa:81
UCSCiuc002oja.3 human [O43707-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Entry informationi

Entry nameiACTN4_HUMAN
AccessioniPrimary (citable) accession number: O43707
Secondary accession number(s): A4K467, D6PXK4, O76048
Entry historyiIntegrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: May 23, 2018
This is version 213 of the entry and version 2 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, Reference proteome

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