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O43707

- ACTN4_HUMAN

UniProt

O43707 - ACTN4_HUMAN

Protein

Alpha-actinin-4

Gene

ACTN4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 173 (01 Oct 2014)
      Sequence version 2 (21 Feb 2001)
      Previous versions | rss
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    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 – 789121PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi819 – 830122PROSITE-ProRule annotationAdd
    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

    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).

    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

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    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-acetyllysineBy similarity
    Modified residuei859 – 8591N6-acetyllysineBy 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.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CTNNB1P352227EBI-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. 36 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO43707.

    Family & Domainsi

    Domains and Repeats

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

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni177 – 19216Polyphosphoinositide (PIP2)-bindingSequence AnalysisAdd
    BLAST
    Regioni736 – 911176Mediates interaction with MICALL2By similarityAdd
    BLAST

    Compositional bias

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

    Sequence similaritiesi

    Belongs to the alpha-actinin family.Curated
    Contains 1 actin-binding domain.Curated
    Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
    Contains 2 EF-hand domains.PROSITE-ProRule annotation
    Contains 4 spectrin repeats.Curated

    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.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti60 – 601C → S in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti164 – 1641S → L in AL047603. (PubMed:15489334)Curated
    Sequence conflicti164 – 1641S → L in AU118403. (PubMed:15489334)Curated
    Sequence conflicti276 – 2761T → TET in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti292 – 2943EHL → CSTS in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti359 – 3602TL → SV in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti476 – 4761I → S in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti526 – 5261I → II in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti536 – 5361R → P in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti645 – 6451Q → QQ in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti673 – 6742GR → A in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti850 – 8501A → T in AAC17470. (PubMed:10656685)Curated
    Sequence conflicti891 – 8933AVP → GVR in AAC17470. (PubMed:10656685)Curated

    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. 1 PublicationVSP_047733Add
    BLAST
    Alternative sequencei89 – 478390Missing in isoform 3. 1 PublicationVSP_053401Add
    BLAST

    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. 36 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

    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: October 1, 2014
    This is version 173 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