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O43707 (ACTN4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 168. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-actinin-4
Alternative name(s):
F-actin cross-linking protein
Non-muscle alpha-actinin 4
Gene names
Name:ACTN4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length911 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. 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. 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.

Subunit structure

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. Ref.10 Ref.11 Ref.12

Subcellular location

Nucleus. Cytoplasm. Cell junction By similarity. Note: Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Colocalizes with actin stress fibers. Nuclear translocation can be induced by the PI3 kinase inhibitor wortmannin or by cytochalasin D. Exclusively localized in the nucleus in a limited number of cell lines (breast cancer cell line MCF-7, oral floor cancer IMC-2, and bladder cancer KU-7). Ref.4 Ref.12

Tissue specificity

Widely expressed.

Involvement in disease

Focal segmental glomerulosclerosis 1 (FSGS1) [MIM:603278]: A 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Belongs to the alpha-actinin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 2 EF-hand domains.

Contains 4 spectrin repeats.

Sequence caution

The sequence AAC17470.1 differs from that shown. Reason: Frameshift at positions 19, 26, 124, 130, 589, 594, 787 and 806.

The sequence BAA24447.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell junction
Cytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseDisease mutation
   DomainRepeat
   LigandActin-binding
Calcium
Metal-binding
   PTMAcetylation
Isopeptide bond
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament bundle assembly

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

negative regulation of cellular component movement

Inferred from electronic annotation. Source: Ensembl

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of cellular component movement

Inferred from direct assay Ref.1. Source: UniProtKB

positive regulation of pinocytosis

Inferred from electronic annotation. Source: Ensembl

positive regulation of sodium:hydrogen antiporter activity

Non-traceable author statement PubMed 11948184. Source: UniProtKB

protein transport

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of apoptotic process

Non-traceable author statement PubMed 16807302. Source: UniProtKB

response to hypoxia

Inferred from electronic annotation. Source: Ensembl

tight junction assembly

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentZ disc

Inferred from electronic annotation. Source: Ensembl

cell-cell junction

Inferred from electronic annotation. Source: Ensembl

cortical cytoskeleton

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from direct assay Ref.1. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

neuron projection

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay Ref.1. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay PubMed 15619032. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

protein complex

Inferred from direct assay PubMed 11948184. Source: UniProtKB

pseudopodium

Traceable author statement PubMed 1629252. Source: UniProtKB

ribonucleoprotein complex

Inferred from direct assay Ref.12. Source: UniProtKB

stress fiber

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionactin binding

Traceable author statement PubMed 8104223. Source: UniProtKB

actin filament binding

Inferred from direct assay PubMed 12411747. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

integrin binding

Traceable author statement PubMed 8104223. Source: UniProtKB

nucleoside binding

Inferred from direct assay PubMed 12411747. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

protein homodimerization activity

Traceable author statement PubMed 15841212. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O43707-1)

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.
Isoform ACTN4ISO (identifier: O43707-2)

The sequence of this isoform differs from the canonical sequence as follows:
     54-272: Missing.
Note: Does not colocalize with actin cytoskeleton structures.
Isoform 3 (identifier: O43707-3)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 911911Alpha-actinin-4
PRO_0000073440

Regions

Domain1 – 269269Actin-binding
Domain50 – 154105CH 1
Domain163 – 269107CH 2
Repeat293 – 403111Spectrin 1
Repeat413 – 518106Spectrin 2
Repeat528 – 639112Spectrin 3
Repeat649 – 752104Spectrin 4
Domain765 – 80036EF-hand 1
Domain806 – 84136EF-hand 2
Calcium binding778 – 789121 Potential
Calcium binding819 – 830122 Potential
Region177 – 19216Polyphosphoinositide (PIP2)-binding Potential
Region736 – 911176Mediates interaction with MICALL2 By similarity
Compositional bias19 – 268Poly-Gly

Amino acid modifications

Modified residue1141N6-acetyllysine Ref.14
Modified residue5921N6-acetyllysine Ref.14
Modified residue6251N6-acetyllysine Ref.14
Modified residue7791N6-acetyllysine By similarity
Modified residue8591N6-acetyllysine By similarity
Cross-link378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) Ref.13

Natural variations

Alternative sequence54 – 272219Missing in isoform ACTN4ISO.
VSP_047733
Alternative sequence89 – 478390Missing in isoform 3.
VSP_053401
Natural variant2551K → E in FSGS1. Ref.16
Corresponds to variant rs28939374 [ dbSNP | Ensembl ].
VAR_010378
Natural variant2591T → I in FSGS1. Ref.16
Corresponds to variant rs28939375 [ dbSNP | Ensembl ].
VAR_010379
Natural variant2621S → P in FSGS1. Ref.16
Corresponds to variant rs28939376 [ dbSNP | Ensembl ].
VAR_010380

Experimental info

Sequence conflict601C → S in AAC17470. Ref.3
Sequence conflict1641S → L in AL047603. Ref.7
Sequence conflict1641S → L in AU118403. Ref.7
Sequence conflict2761T → TET in AAC17470. Ref.3
Sequence conflict292 – 2943EHL → CSTS in AAC17470. Ref.3
Sequence conflict359 – 3602TL → SV in AAC17470. Ref.3
Sequence conflict4761I → S in AAC17470. Ref.3
Sequence conflict5261I → II in AAC17470. Ref.3
Sequence conflict5361R → P in AAC17470. Ref.3
Sequence conflict6451Q → QQ in AAC17470. Ref.3
Sequence conflict673 – 6742GR → A in AAC17470. Ref.3
Sequence conflict8501A → T in AAC17470. Ref.3
Sequence conflict891 – 8933AVP → GVR in AAC17470. Ref.3

Secondary structure

............................................ 911
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified February 21, 2001. Version 2.
Checksum: 461580C3F22937D1

FASTA911104,854
        10         20         30         40         50         60 
MVDYHAANQS YQYGPSSAGN GAGGGGSMGD YMAQEDDWDR DLLLDPAWEK QQRKTFTAWC 

        70         80         90        100        110        120 
NSHLRKAGTQ IENIDEDFRD GLKLMLLLEV ISGERLPKPE RGKMRVHKIN NVNKALDFIA 

       130        140        150        160        170        180 
SKGVKLVSIG AEEIVDGNAK MTLGMIWTII LRFAIQDISV EETSAKEGLL LWCQRKTAPY 

       190        200        210        220        230        240 
KNVNVQNFHI SWKDGLAFNA LIHRHRPELI EYDKLRKDDP VTNLNNAFEV AEKYLDIPKM 

       250        260        270        280        290        300 
LDAEDIVNTA RPDEKAIMTY VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEHLMEDYEK 

       310        320        330        340        350        360 
LASDLLEWIR RTIPWLEDRV PQKTIQEMQQ KLEDFRDYRR VHKPPKVQEK CQLEINFNTL 

       370        380        390        400        410        420 
QTKLRLSNRP AFMPSEGKMV SDINNGWQHL EQAEKGYEEW LLNEIRRLER LDHLAEKFRQ 

       430        440        450        460        470        480 
KASIHEAWTD GKEAMLKHRD YETATLSDIK ALIRKHEAFE SDLAAHQDRV EQIAAIAQEL 

       490        500        510        520        530        540 
NELDYYDSHN VNTRCQKICD QWDALGSLTH SRREALEKTE KQLEAIDQLH LEYAKRAAPF 

       550        560        570        580        590        600 
NNWMESAMED LQDMFIVHTI EEIEGLISAH DQFKSTLPDA DREREAILAI HKEAQRIAES 

       610        620        630        640        650        660 
NHIKLSGSNP YTTVTPQIIN SKWEKVQQLV PKRDHALLEE QSKQQSNEHL RRQFASQANV 

       670        680        690        700        710        720 
VGPWIQTKME EIGRISIEMN GTLEDQLSHL KQYERSIVDY KPNLDLLEQQ HQLIQEALIF 

       730        740        750        760        770        780 
DNKHTNYTME HIRVGWEQLL TTIARTINEV ENQILTRDAK GISQEQMQEF RASFNHFDKD 

       790        800        810        820        830        840 
HGGALGPEEF KACLISLGYD VENDRQGEAE FNRIMSLVDP NHSGLVTFQA FIDFMSRETT 

       850        860        870        880        890        900 
DTDTADQVIA SFKVLAGDKN FITAEELRRE LPPDQAEYCI ARMAPYQGPD AVPGALDYKS 

       910 
FSTALYGESD L 

« Hide

Isoform ACTN4ISO [UniParc].

Checksum: 34C43B1217B8AA25
Show »

FASTA69279,913
Isoform 3 [UniParc].

Checksum: 66A7C97A6AF6C87D
Show »

FASTA52159,579

References

« Hide 'large scale' references
[1]"Actinin-4, a novel actin-bundling protein associated with cell motility and cancer invasion."
Honda K., Yamada T., Endo R., Ino Y., Gotoh M., Tsuda H., Yamada Y., Chiba H., Hirohashi S.
J. Cell Biol. 140:1383-1393(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-911 (ISOFORM 1).
[2]Erratum
Honda K., Yamada T., Endo R., Ino Y., Gotoh M., Tsuda H., Yamada Y., Chiba H., Hirohashi S.
J. Cell Biol. 143:276-276(1998)
[3]"The human non-muscle alpha-actinin protein encoded by the ACTN4 gene suppresses tumorigenicity of human neuroblastoma cells."
Nikolopoulos S.N., Spengler B.A., Kisselbach K., Evans A.E., Biedler J.L., Ross R.A.
Oncogene 19:380-386(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Neuroblastoma.
[4]"Novel splicing isoform of actin-binding protein alpha-actinin 4 in epidermoid carcinoma cells A431."
Aksenova V.I.U., Khotin M.G., Turoverova L.V., Iudintseva N.M., Magnusson K.E., Pinaev G.P., Tentler D.G.
Tsitologiia 54:25-32(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ACTN4ISO), SUBCELLULAR LOCATION, ALTERNATIVE SPLICING.
[5]"Actinin alpha4, an actin binding protein, is a transcriptional coactivator that antagonizes class II HDAC activity."
Chakraborty S., Cheng X., Lam M., Reineke E.L., Li X., Liu Y., Gao C., Khurana S., Kao H.-Y.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[6]"The DNA sequence and biology of human chromosome 19."
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. expand/collapse author list , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Placenta.
[8]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-170 (ISOFORM 1).
Tissue: Uterus.
[9]"Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes."
Kimura K., Wakamatsu A., Suzuki Y., Ota T., Nishikawa T., Yamashita R., Yamamoto J., Sekine M., Tsuritani K., Wakaguri H., Ishii S., Sugiyama T., Saito K., Isono Y., Irie R., Kushida N., Yoneyama T., Otsuka R. expand/collapse author list , Kanda K., Yokoi T., Kondo H., Wagatsuma M., Murakawa K., Ishida S., Ishibashi T., Takahashi-Fujii A., Tanase T., Nagai K., Kikuchi H., Nakai K., Isogai T., Sugano S.
Genome Res. 16:55-65(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-218 (ISOFORM 1).
[10]"Interaction of two actin-binding proteins, synaptopodin and alpha-actinin-4, with the tight junction protein MAGI-1."
Patrie K.M., Drescher A.J., Welihinda A., Mundel P., Margolis B.
J. Biol. Chem. 277:30183-30190(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH BAIAP1.
[11]"CART: an Hrs/actinin-4/BERP/myosin V protein complex required for efficient receptor recycling."
Yan Q., Sun W., Kujala P., Lotfi Y., Vida T.A., Bean A.J.
Mol. Biol. Cell 16:2470-2482(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE CART COMPLEX.
[12]"Molecular composition of IMP1 ribonucleoprotein granules."
Joeson L., Vikesaa J., Krogh A., Nielsen L.K., Hansen T., Borup R., Johnsen A.H., Christiansen J., Nielsen F.C.
Mol. Cell. Proteomics 6:798-811(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN A MRNP GRANULE COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
[13]"Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-378.
Tissue: Mammary cancer.
[14]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114; LYS-592 AND LYS-625, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis."
Kaplan J.M., Kim S.H., North K.N., Rennke H., Correia L.A., Tong H.-Q., Mathis B.J., Rodriguez-Perez J.-C., Allen P.G., Beggs A.H., Pollak M.R.
Nat. Genet. 24:251-256(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS FSGS1 GLU-255; ILE-259 AND PRO-262.
Tissue: Lymphocyte.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D89980 mRNA. Translation: BAA24447.1. Different initiation.
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.
RefSeqNP_004915.2. NM_004924.4.
UniGeneHs.270291.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLXNMR-A519-645[»]
1YDIX-ray1.80B734-757[»]
2R0OX-ray2.20A/B47-271[»]
ProteinModelPortalO43707.
SMRO43707. Positions 47-271, 286-911.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106596. 59 interactions.
DIPDIP-33179N.
IntActO43707. 26 interactions.
MINTMINT-4998602.
STRING9606.ENSP00000252699.

PTM databases

PhosphoSiteO43707.

2D gel databases

REPRODUCTION-2DPAGEO43707.

Proteomic databases

PaxDbO43707.
PeptideAtlasO43707.
PRIDEO43707.

Protocols and materials databases

DNASU81.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000252699; ENSP00000252699; ENSG00000130402. [O43707-1]
ENST00000390009; ENSP00000439497; ENSG00000130402. [O43707-2]
GeneID81.
KEGGhsa:81.
UCSCuc002oja.2. human. [O43707-1]

Organism-specific databases

CTD81.
GeneCardsGC19P039138.
HGNCHGNC:166. ACTN4.
HPAHPA001873.
HPA006035.
MIM603278. phenotype.
604638. gene.
neXtProtNX_O43707.
Orphanet93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBPA23.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000263418.
HOVERGENHBG050453.
InParanoidO43707.
KOK05699.
OMAQANIVGP.
OrthoDBEOG72C4ZJ.
PhylomeDBO43707.
TreeFamTF352676.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressO43707.
BgeeO43707.
CleanExHS_ACTN4.
GenevestigatorO43707.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
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.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. 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.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACTN4. human.
EvolutionaryTraceO43707.
GeneWikiActinin_alpha_4.
GenomeRNAi81.
NextBio303.
PMAP-CutDBO43707.
PROO43707.
SOURCESearch...

Entry information

Entry nameACTN4_HUMAN
AccessionPrimary (citable) accession number: O43707
Secondary accession number(s): A4K467, D6PXK4, O76048
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: April 16, 2014
This is version 168 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM