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O43707

- ACTN4_HUMAN

UniProt

O43707 - ACTN4_HUMAN

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Protein

Alpha-actinin-4

Gene
ACTN4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - 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. 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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi778 – 789121 Reviewed predictionAdd
BLAST
Calcium bindingi819 – 830122 Reviewed predictionAdd
BLAST

GO - Molecular functioni

  1. actin binding Source: UniProtKB
  2. actin filament binding Source: UniProtKB
  3. calcium ion binding Source: InterPro
  4. integrin binding Source: UniProtKB
  5. nucleoside binding Source: UniProtKB
  6. poly(A) RNA binding Source: UniProtKB
  7. protein binding Source: UniProtKB
  8. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. actin filament bundle assembly Source: Ensembl
  2. blood coagulation Source: Reactome
  3. negative regulation of cellular component movement Source: Ensembl
  4. platelet activation Source: Reactome
  5. platelet degranulation Source: Reactome
  6. positive regulation of cellular component movement Source: UniProtKB
  7. positive regulation of pinocytosis Source: Ensembl
  8. positive regulation of sodium:proton antiporter activity Source: UniProtKB
  9. protein transport Source: UniProtKB-KW
  10. regulation of apoptotic process Source: UniProtKB
  11. response to hypoxia Source: Ensembl
  12. tight junction assembly Source: Ensembl
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_23832. Nephrin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin-4
Alternative name(s):
F-actin cross-linking protein
Non-muscle alpha-actinin 4
Gene namesi
Name:ACTN4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:166. ACTN4.

Subcellular locationi

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).2 Publications

GO - Cellular componenti

  1. cell-cell junction Source: Ensembl
  2. cortical cytoskeleton Source: Ensembl
  3. cytoplasm Source: UniProtKB
  4. extracellular region Source: Reactome
  5. extracellular space Source: UniProt
  6. extracellular vesicular exosome Source: UniProtKB
  7. neuron projection Source: Ensembl
  8. nucleus Source: UniProtKB
  9. perinuclear region of cytoplasm Source: UniProtKB
  10. platelet alpha granule lumen Source: Reactome
  11. protein complex Source: UniProtKB
  12. pseudopodium Source: UniProtKB
  13. ribonucleoprotein complex Source: UniProtKB
  14. stress fiber Source: Ensembl
  15. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti255 – 2551K → E in FSGS1. 1 Publication
Corresponds to variant rs28939374 [ dbSNP | Ensembl ].
VAR_010378
Natural varianti259 – 2591T → I in FSGS1. 1 Publication
Corresponds to variant rs28939375 [ dbSNP | Ensembl ].
VAR_010379
Natural varianti262 – 2621S → P in FSGS1. 1 Publication
Corresponds to variant rs28939376 [ dbSNP | Ensembl ].
VAR_010380

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi603278. phenotype.
Orphaneti93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBiPA23.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 911911Alpha-actinin-4PRO_0000073440Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei114 – 1141N6-acetyllysine1 Publication
Cross-linki378 – 378Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei592 – 5921N6-acetyllysine1 Publication
Modified residuei625 – 6251N6-acetyllysine1 Publication
Modified residuei779 – 7791N6-acetyllysine By similarity
Modified residuei859 – 8591N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiO43707.
PaxDbiO43707.
PeptideAtlasiO43707.
PRIDEiO43707.

2D gel databases

REPRODUCTION-2DPAGEO43707.

PTM databases

PhosphoSiteiO43707.

Miscellaneous databases

PMAP-CutDBO43707.

Expressioni

Tissue specificityi

Widely expressed.

Gene expression databases

ArrayExpressiO43707.
BgeeiO43707.
CleanExiHS_ACTN4.
GenevestigatoriO43707.

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 PDLIM2.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CTNNB1P352226EBI-351526,EBI-491549
IQGAP1P469403EBI-351526,EBI-297509
NPP034662EBI-351526,EBI-2547640From a different organism.
NPQ5L4H45EBI-351526,EBI-9512099From a different organism.
TJP1Q071574EBI-351526,EBI-79553

Protein-protein interaction databases

BioGridi106596. 62 interactions.
DIPiDIP-33179N.
IntActiO43707. 34 interactions.
MINTiMINT-4998602.
STRINGi9606.ENSP00000252699.

Structurei

Secondary structure

1
911
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 6418
Helixi65 – 673
Turni74 – 807
Helixi82 – 9211
Helixi105 – 12016
Turni121 – 1233
Helixi131 – 1355
Helixi139 – 15315
Turni154 – 1574
Helixi165 – 17713
Beta strandi187 – 1893
Helixi190 – 1923
Helixi196 – 20510
Helixi207 – 2093
Helixi212 – 2143
Helixi220 – 23415
Helixi243 – 2486
Beta strandi249 – 2513
Helixi254 – 26714
Helixi519 – 55234
Helixi560 – 60041
Beta strandi606 – 6083
Helixi616 – 64126
Helixi736 – 75621

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WLXNMR-A519-645[»]
1YDIX-ray1.80B734-757[»]
2R0OX-ray2.20A/B47-271[»]
ProteinModelPortaliO43707.
SMRiO43707. Positions 47-271, 286-911.

Miscellaneous databases

EvolutionaryTraceiO43707.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 269269Actin-bindingAdd
BLAST
Domaini50 – 154105CH 1Add
BLAST
Domaini163 – 269107CH 2Add
BLAST
Repeati293 – 403111Spectrin 1Add
BLAST
Repeati413 – 518106Spectrin 2Add
BLAST
Repeati528 – 639112Spectrin 3Add
BLAST
Repeati649 – 752104Spectrin 4Add
BLAST
Domaini765 – 80036EF-hand 1Add
BLAST
Domaini806 – 84136EF-hand 2Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni177 – 19216Polyphosphoinositide (PIP2)-binding Reviewed predictionAdd
BLAST
Regioni736 – 911176Mediates interaction with MICALL2 By similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi19 – 268Poly-Gly

Sequence similaritiesi

Belongs to the alpha-actinin family.
Contains 2 EF-hand domains.
Contains 4 spectrin repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiO43707.
KOiK05699.
OMAiQANIVGP.
OrthoDBiEOG72C4ZJ.
PhylomeDBiO43707.
TreeFamiTF352676.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR029637. ACTN4.
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]
PANTHERiPTHR11915:SF271. PTHR11915:SF271. 1 hit.
PfamiPF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. 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]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

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

MVDYHAANQS YQYGPSSAGN GAGGGGSMGD YMAQEDDWDR DLLLDPAWEK    50
QQRKTFTAWC NSHLRKAGTQ IENIDEDFRD GLKLMLLLEV ISGERLPKPE 100
RGKMRVHKIN NVNKALDFIA SKGVKLVSIG AEEIVDGNAK MTLGMIWTII 150
LRFAIQDISV EETSAKEGLL LWCQRKTAPY KNVNVQNFHI SWKDGLAFNA 200
LIHRHRPELI EYDKLRKDDP VTNLNNAFEV AEKYLDIPKM LDAEDIVNTA 250
RPDEKAIMTY VSSFYHAFSG AQKAETAANR ICKVLAVNQE NEHLMEDYEK 300
LASDLLEWIR RTIPWLEDRV PQKTIQEMQQ KLEDFRDYRR VHKPPKVQEK 350
CQLEINFNTL QTKLRLSNRP AFMPSEGKMV SDINNGWQHL EQAEKGYEEW 400
LLNEIRRLER LDHLAEKFRQ KASIHEAWTD GKEAMLKHRD YETATLSDIK 450
ALIRKHEAFE SDLAAHQDRV EQIAAIAQEL NELDYYDSHN VNTRCQKICD 500
QWDALGSLTH SRREALEKTE KQLEAIDQLH LEYAKRAAPF NNWMESAMED 550
LQDMFIVHTI EEIEGLISAH DQFKSTLPDA DREREAILAI HKEAQRIAES 600
NHIKLSGSNP YTTVTPQIIN SKWEKVQQLV PKRDHALLEE QSKQQSNEHL 650
RRQFASQANV VGPWIQTKME EIGRISIEMN GTLEDQLSHL KQYERSIVDY 700
KPNLDLLEQQ HQLIQEALIF DNKHTNYTME HIRVGWEQLL TTIARTINEV 750
ENQILTRDAK GISQEQMQEF RASFNHFDKD HGGALGPEEF KACLISLGYD 800
VENDRQGEAE FNRIMSLVDP NHSGLVTFQA FIDFMSRETT DTDTADQVIA 850
SFKVLAGDKN FITAEELRRE LPPDQAEYCI ARMAPYQGPD AVPGALDYKS 900
FSTALYGESD L 911
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.

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 AAC17470.1 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.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti255 – 2551K → E in FSGS1. 1 Publication
Corresponds to variant rs28939374 [ dbSNP | Ensembl ].
VAR_010378
Natural varianti259 – 2591T → I in FSGS1. 1 Publication
Corresponds to variant rs28939375 [ dbSNP | Ensembl ].
VAR_010379
Natural varianti262 – 2621S → P in FSGS1. 1 Publication
Corresponds to variant rs28939376 [ dbSNP | Ensembl ].
VAR_010380

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei54 – 272219Missing in isoform ACTN4ISO. VSP_047733Add
BLAST
Alternative sequencei89 – 478390Missing in isoform 3. VSP_053401Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti60 – 601C → S in AAC17470. 1 Publication
Sequence conflicti164 – 1641S → L in AL047603. 1 Publication
Sequence conflicti164 – 1641S → L in AU118403. 1 Publication
Sequence conflicti276 – 2761T → TET in AAC17470. 1 Publication
Sequence conflicti292 – 2943EHL → CSTS in AAC17470. 1 Publication
Sequence conflicti359 – 3602TL → SV in AAC17470. 1 Publication
Sequence conflicti476 – 4761I → S in AAC17470. 1 Publication
Sequence conflicti526 – 5261I → II in AAC17470. 1 Publication
Sequence conflicti536 – 5361R → P in AAC17470. 1 Publication
Sequence conflicti645 – 6451Q → QQ in AAC17470. 1 Publication
Sequence conflicti673 – 6742GR → A in AAC17470. 1 Publication
Sequence conflicti850 – 8501A → T in AAC17470. 1 Publication
Sequence conflicti891 – 8933AVP → GVR in AAC17470. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS12518.1. [O43707-1]
RefSeqiNP_004915.2. NM_004924.4. [O43707-1]
UniGeneiHs.270291.

Genome annotation databases

EnsembliENST00000252699; ENSP00000252699; ENSG00000130402. [O43707-1]
ENST00000390009; ENSP00000439497; ENSG00000130402. [O43707-2]
GeneIDi81.
KEGGihsa:81.
UCSCiuc002oja.2. human. [O43707-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSi CCDS12518.1. [O43707-1 ]
RefSeqi NP_004915.2. NM_004924.4. [O43707-1 ]
UniGenei Hs.270291.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WLX NMR - A 519-645 [» ]
1YDI X-ray 1.80 B 734-757 [» ]
2R0O X-ray 2.20 A/B 47-271 [» ]
ProteinModelPortali O43707.
SMRi O43707. Positions 47-271, 286-911.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106596. 62 interactions.
DIPi DIP-33179N.
IntActi O43707. 34 interactions.
MINTi MINT-4998602.
STRINGi 9606.ENSP00000252699.

PTM databases

PhosphoSitei O43707.

2D gel databases

REPRODUCTION-2DPAGE O43707.

Proteomic databases

MaxQBi O43707.
PaxDbi O43707.
PeptideAtlasi O43707.
PRIDEi O43707.

Protocols and materials databases

DNASUi 81.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000252699 ; ENSP00000252699 ; ENSG00000130402 . [O43707-1 ]
ENST00000390009 ; ENSP00000439497 ; ENSG00000130402 . [O43707-2 ]
GeneIDi 81.
KEGGi hsa:81.
UCSCi uc002oja.2. human. [O43707-1 ]

Organism-specific databases

CTDi 81.
GeneCardsi GC19P039138.
HGNCi HGNC:166. ACTN4.
HPAi HPA001873.
HPA006035.
MIMi 603278. phenotype.
604638. gene.
neXtProti NX_O43707.
Orphaneti 93213. Familial idiopathic steroid-resistant nephrotic syndrome with focal segmental hyalinosis.
PharmGKBi PA23.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
HOGENOMi HOG000263418.
HOVERGENi HBG050453.
InParanoidi O43707.
KOi K05699.
OMAi QANIVGP.
OrthoDBi EOG72C4ZJ.
PhylomeDBi O43707.
TreeFami TF352676.

Enzyme and pathway databases

Reactomei REACT_23832. Nephrin interactions.

Miscellaneous databases

ChiTaRSi ACTN4. human.
EvolutionaryTracei O43707.
GeneWikii Actinin_alpha_4.
GenomeRNAii 81.
NextBioi 303.
PMAP-CutDB O43707.
PROi O43707.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43707.
Bgeei O43707.
CleanExi HS_ACTN4.
Genevestigatori O43707.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR029637. ACTN4.
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 ]
PANTHERi PTHR11915:SF271. PTHR11915:SF271. 1 hit.
Pfami PF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 4 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
PROSITEi 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.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-170 (ISOFORM 1).
    Tissue: Uterus.
  9. 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. 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. 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.

Entry informationi

Entry nameiACTN4_HUMAN
AccessioniPrimary (citable) accession number: O43707
Secondary accession number(s): A4K467, D6PXK4, O76048
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: February 21, 2001
Last modified: September 3, 2014
This is version 172 of the entry and version 2 of the sequence. [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

Documents

  1. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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