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P12814

- ACTN1_HUMAN

UniProt

P12814 - ACTN1_HUMAN

Protein

Alpha-actinin-1

Gene

ACTN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 180 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      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.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Calcium bindingi759 – 77012PROSITE-ProRule annotationAdd
    BLAST
    Calcium bindingi800 – 81112PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. double-stranded RNA binding Source: MGI
    3. integrin binding Source: UniProtKB
    4. ion channel binding Source: BHF-UCL
    5. protein binding Source: UniProtKB
    6. vinculin binding Source: UniProtKB

    GO - Biological processi

    1. actin crosslink formation Source: InterPro
    2. actin filament bundle assembly Source: Ensembl
    3. blood coagulation Source: Reactome
    4. cell junction assembly Source: Reactome
    5. extracellular matrix organization Source: Reactome
    6. focal adhesion assembly Source: UniProtKB
    7. negative regulation of cellular component movement Source: UniProtKB
    8. platelet activation Source: Reactome
    9. platelet degranulation Source: Reactome
    10. regulation of apoptotic process Source: UniProtKB

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_163942. Syndecan interactions.
    REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    REACT_23832. Nephrin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-actinin-1
    Alternative name(s):
    Alpha-actinin cytoskeletal isoform
    F-actin cross-linking protein
    Non-muscle alpha-actinin-1
    Gene namesi
    Name:ACTN1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:163. ACTN1.

    Subcellular locationi

    Cytoplasmcytoskeleton 1 Publication. CytoplasmmyofibrilsarcomereZ line 1 Publication. Cell membrane By similarity. Cell junction By similarity. Cell projectionruffle By similarity
    Note: Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures By similarity.By similarity

    GO - Cellular componenti

    1. cell projection Source: UniProtKB
    2. cytoplasm Source: UniProtKB
    3. cytoskeleton Source: UniProtKB-SubCell
    4. cytosol Source: Reactome
    5. dendritic spine Source: Ensembl
    6. extracellular region Source: Reactome
    7. extracellular space Source: UniProt
    8. extracellular vesicular exosome Source: UniProtKB
    9. fascia adherens Source: Ensembl
    10. focal adhesion Source: UniProtKB
    11. nucleus Source: Ensembl
    12. plasma membrane Source: UniProtKB-SubCell
    13. platelet alpha granule lumen Source: Reactome
    14. pseudopodium Source: UniProtKB
    15. ruffle Source: UniProtKB-SubCell
    16. Z disc Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Bleeding disorder, platelet-type 15 (BDPLT15) [MIM:615193]: An autosomal dominant form of macrothrombocytopenia. Affected individuals usually have no or only mild bleeding tendency, such as epistaxis. Laboratory studies show decreased numbers of large platelets and anisocytosis, but the platelets show no in vitro functional abnormalities.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321Q → K in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 Publication
    VAR_069910
    Natural varianti46 – 461R → Q in BDPLT15. 1 Publication
    VAR_069911
    Natural varianti105 – 1051V → I in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 Publication
    VAR_069912
    Natural varianti225 – 2251E → K in BDPLT15. 1 Publication
    VAR_069914
    Natural varianti738 – 7381R → W in BDPLT15. 1 Publication
    VAR_069915
    Natural varianti752 – 7521R → Q in BDPLT15. 1 Publication
    VAR_069916

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615193. phenotype.
    Orphaneti140957. Autosomal dominant macrothrombocytopenia.
    PharmGKBiPA24.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 892892Alpha-actinin-1PRO_0000073431Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei6 – 61Phosphoserine1 Publication
    Modified residuei12 – 121Phosphotyrosine; by FAK11 Publication
    Modified residuei95 – 951N6-acetyllysine1 Publication
    Modified residuei195 – 1951N6-acetyllysine1 Publication
    Modified residuei676 – 6761N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP12814.
    PaxDbiP12814.
    PeptideAtlasiP12814.
    PRIDEiP12814.

    2D gel databases

    OGPiP12814.

    PTM databases

    PhosphoSiteiP12814.

    Expressioni

    Gene expression databases

    ArrayExpressiP12814.
    BgeeiP12814.
    CleanExiHS_ACTN1.
    GenevestigatoriP12814.

    Organism-specific databases

    HPAiCAB004303.
    HPA006035.

    Interactioni

    Subunit structurei

    Homodimer; antiparallel. Interacts with DDN, MYOZ2, PDLIM2, TTID and LPP. Interacts with PSD. Interacts with MICALL2 By similarity.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    P279587EBI-351710,EBI-6904388From a different organism.
    SRCP129312EBI-351710,EBI-621482
    Ssx2ipQ8VC663EBI-351710,EBI-6654049From a different organism.
    TTNQ8WZ422EBI-351710,EBI-681210

    Protein-protein interaction databases

    BioGridi106602. 89 interactions.
    DIPiDIP-33184N.
    IntActiP12814. 40 interactions.
    MINTiMINT-215335.
    STRINGi9606.ENSP00000377941.

    Structurei

    Secondary structure

    1
    892
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 4516
    Helixi46 – 483
    Turni55 – 617
    Helixi63 – 7311
    Helixi86 – 10217
    Helixi112 – 1165
    Helixi120 – 13516
    Turni136 – 1383
    Helixi146 – 15813
    Beta strandi168 – 1703
    Helixi171 – 1733
    Helixi177 – 18610
    Helixi188 – 1903
    Helixi193 – 1953
    Helixi201 – 21515
    Helixi224 – 2296
    Beta strandi230 – 2323
    Helixi235 – 24915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2EYIX-ray1.70A30-253[»]
    2EYNX-ray1.80A30-253[»]
    ProteinModelPortaliP12814.
    SMRiP12814. Positions 30-254, 267-892.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP12814.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 247247Actin-bindingAdd
    BLAST
    Domaini31 – 135105CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini144 – 247104CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati274 – 384111Spectrin 1Add
    BLAST
    Repeati394 – 499106Spectrin 2Add
    BLAST
    Repeati509 – 620112Spectrin 3Add
    BLAST
    Repeati630 – 733104Spectrin 4Add
    BLAST
    Domaini746 – 78136EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini787 – 82236EF-hand 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni274 – 733460Interaction with DDNAdd
    BLAST

    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.
    KOiK05699.
    OMAiWIRRTMP.
    OrthoDBiEOG72C4ZJ.
    PhylomeDBiP12814.
    TreeFamiTF352676.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR026921. Alpha-actinin_1.
    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:SF241. PTHR11915:SF241. 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. 3 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 (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P12814-1) [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

    MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT    50
    QIENIEEDFR DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI 100
    ASKGVKLVSI GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL 150
    LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC ALIHRHRPEL IDYGKLRKDD 200
    PLTNLNTAFD VAEKYLDIPK MLDAEDIVGT ARPDEKAIMT YVSSFYHAFS 250
    GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR 300
    VPENTMHAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR 350
    PAFMPSEGRM VSDINNAWGC LEQVEKGYEE WLLNEIRRLE RLDHLAEKFR 400
    QKASIHEAWT DGKEAMLRQK DYETATLSEI KALLKKHEAF ESDLAAHQDR 450
    VEQIAAIAQE LNELDYYDSP SVNARCQKIC DQWDNLGALT QKRREALERT 500
    EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT IEEIQGLTTA 550
    HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI 600
    NGKWDHVRQL VPRRDQALTE EHARQQHNER LRKQFGAQAN VIGPWIQTKM 650
    EEIGRISIEM HGTLEDQLSH LRQYEKSIVN YKPKIDQLEG DHQLIQEALI 700
    FDNKHTNYTM EHIRVGWEQL LTTIARTINE VENQILTRDA KGISQEQMNE 750
    FRASFNHFDR DHSGTLGPEE FKACLISLGY DIGNDPQGEA EFARIMSIVD 800
    PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK NYITMDELRR 850
    ELPPDQAEYC IARMAPYTGP DSVPGALDYM SFSTALYGES DL 892
    Length:892
    Mass (Da):103,058
    Last modified:April 13, 2004 - v2
    Checksum:i6DA3E4D1A0289519
    GO
    Isoform 2 (identifier: P12814-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         761-787: DHSGTLGPEEFKACLISLGYDIGNDPQ → KKTGMMDTDDFRACLISMGYNM

    Show »
    Length:887
    Mass (Da):102,709
    Checksum:iC478EDE4C896789A
    GO
    Isoform 3 (identifier: P12814-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         787-787: Q → QKKTGMMDTDDFRACLISMGYNM

    Show »
    Length:914
    Mass (Da):105,569
    Checksum:i4E2865FA0CA56DC5
    GO
    Isoform 4 (identifier: P12814-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         761-787: DHSGTLGPEEFKACLISLGYDIGNDPQ → KKTGMMDTDDFRACLISMGYNM
         840-840: K → KLQEGGKMQTAHAAFTPPGFAAVSGRAALRLLDFAAFLTTLSSQ

    Show »
    Length:930
    Mass (Da):107,141
    Checksum:iC8E56D242D05FFFC
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti317 – 3171R → L in CAA38970. (PubMed:2169343)Curated
    Sequence conflicti321 – 3211R → H in BAG58135. (PubMed:14702039)Curated
    Sequence conflicti424 – 4241T → A in BAG58135. (PubMed:14702039)Curated
    Sequence conflicti477 – 4771Q → L in CAA38970. (PubMed:2169343)Curated
    Sequence conflicti630 – 6312RL → SV in CAA33803. (PubMed:2780298)Curated
    Sequence conflicti654 – 6563GRI → ARF in CAA38970. (PubMed:2169343)Curated
    Sequence conflicti674 – 6741Y → D in CAA38970. (PubMed:2169343)Curated
    Sequence conflicti778 – 7781L → S in CAA38970. (PubMed:2169343)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti32 – 321Q → K in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 Publication
    VAR_069910
    Natural varianti46 – 461R → Q in BDPLT15. 1 Publication
    VAR_069911
    Natural varianti105 – 1051V → I in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 Publication
    VAR_069912
    Natural varianti197 – 1971R → W.1 Publication
    VAR_069913
    Natural varianti225 – 2251E → K in BDPLT15. 1 Publication
    VAR_069914
    Natural varianti707 – 7071N → T.
    Corresponds to variant rs7157661 [ dbSNP | Ensembl ].
    VAR_053883
    Natural varianti738 – 7381R → W in BDPLT15. 1 Publication
    VAR_069915
    Natural varianti752 – 7521R → Q in BDPLT15. 1 Publication
    VAR_069916
    Natural varianti868 – 8681T → S.
    Corresponds to variant rs11557769 [ dbSNP | Ensembl ].
    VAR_053884

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei761 – 78727DHSGT…GNDPQ → KKTGMMDTDDFRACLISMGY NM in isoform 2 and isoform 4. 3 PublicationsVSP_041264Add
    BLAST
    Alternative sequencei787 – 7871Q → QKKTGMMDTDDFRACLISMG YNM in isoform 3. 1 PublicationVSP_043525
    Alternative sequencei840 – 8401K → KLQEGGKMQTAHAAFTPPGF AAVSGRAALRLLDFAAFLTT LSSQ in isoform 4. 1 PublicationVSP_047763

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15804 mRNA. Translation: CAA33803.1.
    M95178 mRNA. Translation: AAA51582.1.
    EU716325 mRNA. Translation: ACE62922.1.
    DQ496098 mRNA. Translation: ABF50047.1.
    FJ410030 mRNA. Translation: ACJ24535.1.
    BT007207 mRNA. Translation: AAP35871.1.
    AK295099 mRNA. Translation: BAG58135.1.
    AL117694 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW80975.1.
    BC003576 mRNA. Translation: AAH03576.1.
    BC015766 mRNA. Translation: AAH15766.1.
    X55187 mRNA. Translation: CAA38970.1.
    CCDSiCCDS45129.1. [P12814-2]
    CCDS45130.1. [P12814-3]
    CCDS9792.1. [P12814-1]
    PIRiS05503. FAHUAA.
    RefSeqiNP_001093.1. NM_001102.3. [P12814-1]
    NP_001123476.1. NM_001130004.1. [P12814-3]
    NP_001123477.1. NM_001130005.1. [P12814-2]
    UniGeneiHs.509765.

    Genome annotation databases

    EnsembliENST00000193403; ENSP00000193403; ENSG00000072110. [P12814-1]
    ENST00000394419; ENSP00000377941; ENSG00000072110. [P12814-3]
    ENST00000438964; ENSP00000414272; ENSG00000072110. [P12814-2]
    ENST00000538545; ENSP00000439828; ENSG00000072110. [P12814-4]
    GeneIDi87.
    KEGGihsa:87.
    UCSCiuc001xkk.3. human. [P12814-1]
    uc001xkm.3. human. [P12814-3]
    uc001xkn.3. human. [P12814-2]

    Polymorphism databases

    DMDMi46397817.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X15804 mRNA. Translation: CAA33803.1 .
    M95178 mRNA. Translation: AAA51582.1 .
    EU716325 mRNA. Translation: ACE62922.1 .
    DQ496098 mRNA. Translation: ABF50047.1 .
    FJ410030 mRNA. Translation: ACJ24535.1 .
    BT007207 mRNA. Translation: AAP35871.1 .
    AK295099 mRNA. Translation: BAG58135.1 .
    AL117694 Genomic DNA. No translation available.
    CH471061 Genomic DNA. Translation: EAW80975.1 .
    BC003576 mRNA. Translation: AAH03576.1 .
    BC015766 mRNA. Translation: AAH15766.1 .
    X55187 mRNA. Translation: CAA38970.1 .
    CCDSi CCDS45129.1. [P12814-2 ]
    CCDS45130.1. [P12814-3 ]
    CCDS9792.1. [P12814-1 ]
    PIRi S05503. FAHUAA.
    RefSeqi NP_001093.1. NM_001102.3. [P12814-1 ]
    NP_001123476.1. NM_001130004.1. [P12814-3 ]
    NP_001123477.1. NM_001130005.1. [P12814-2 ]
    UniGenei Hs.509765.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2EYI X-ray 1.70 A 30-253 [» ]
    2EYN X-ray 1.80 A 30-253 [» ]
    ProteinModelPortali P12814.
    SMRi P12814. Positions 30-254, 267-892.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106602. 89 interactions.
    DIPi DIP-33184N.
    IntActi P12814. 40 interactions.
    MINTi MINT-215335.
    STRINGi 9606.ENSP00000377941.

    PTM databases

    PhosphoSitei P12814.

    Polymorphism databases

    DMDMi 46397817.

    2D gel databases

    OGPi P12814.

    Proteomic databases

    MaxQBi P12814.
    PaxDbi P12814.
    PeptideAtlasi P12814.
    PRIDEi P12814.

    Protocols and materials databases

    DNASUi 87.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000193403 ; ENSP00000193403 ; ENSG00000072110 . [P12814-1 ]
    ENST00000394419 ; ENSP00000377941 ; ENSG00000072110 . [P12814-3 ]
    ENST00000438964 ; ENSP00000414272 ; ENSG00000072110 . [P12814-2 ]
    ENST00000538545 ; ENSP00000439828 ; ENSG00000072110 . [P12814-4 ]
    GeneIDi 87.
    KEGGi hsa:87.
    UCSCi uc001xkk.3. human. [P12814-1 ]
    uc001xkm.3. human. [P12814-3 ]
    uc001xkn.3. human. [P12814-2 ]

    Organism-specific databases

    CTDi 87.
    GeneCardsi GC14M069341.
    HGNCi HGNC:163. ACTN1.
    HPAi CAB004303.
    HPA006035.
    MIMi 102575. gene.
    615193. phenotype.
    neXtProti NX_P12814.
    Orphaneti 140957. Autosomal dominant macrothrombocytopenia.
    PharmGKBi PA24.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000263418.
    HOVERGENi HBG050453.
    KOi K05699.
    OMAi WIRRTMP.
    OrthoDBi EOG72C4ZJ.
    PhylomeDBi P12814.
    TreeFami TF352676.

    Enzyme and pathway databases

    Reactomei REACT_163942. Syndecan interactions.
    REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
    REACT_23832. Nephrin interactions.

    Miscellaneous databases

    ChiTaRSi ACTN1. human.
    EvolutionaryTracei P12814.
    GeneWikii Actinin,_alpha_1.
    GenomeRNAii 87.
    NextBioi 323.
    PROi P12814.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P12814.
    Bgeei P12814.
    CleanExi HS_ACTN1.
    Genevestigatori P12814.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR026921. Alpha-actinin_1.
    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:SF241. PTHR11915:SF241. 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. 3 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. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Placenta.
    2. "Cloning and chromosomal localization of the human cytoskeletal alpha-actinin gene reveals linkage to the beta-spectrin gene."
      Youssoufian H., McAfee M., Kwiatkowski D.J.
      Am. J. Hum. Genet. 47:62-71(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    4. "A new mRNA isoform from ACTN1 gene."
      Mancini U.M., Tajara E.H.
      Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
      Tissue: Tongue.
    5. "Actinin alpha 1 alternative splicing variant."
      Mansilla F., Orntoft T.F., Birkenkamp-Demtroeder K.
      Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    7. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Brain.
    8. "The DNA sequence and analysis of human chromosome 14."
      Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
      , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
      Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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].
      Tissue: Colon and Skin.
    11. "Expression of human alpha-actinin in human hepatocellular carcinoma."
      Nishiyama M., Ozturk M., Frohlich M., Mafune K., Steele G. Jr., Wands J.R.
      Cancer Res. 50:6291-6294(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 297-892 (ISOFORM 1).
    12. "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
      Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
      Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-21.
      Tissue: Platelet.
    13. "Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes."
      Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J.
      Biochem. Biophys. Res. Commun. 224:666-674(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 134-146.
    14. "Identification of the cytoskeletal protein alpha-actinin as a platelet thrombospondin-binding protein."
      Dubernard V., Faucher D., Launay J.-M., Legrand C.
      FEBS Lett. 364:109-114(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 566-577; 727-738 AND 835-863, SUBCELLULAR LOCATION.
    15. "Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy."
      Salmikangas P., Mykkaenen O.M., Groenholm M., Heiska L., Kere J., Carpen O.
      Hum. Mol. Genet. 8:1329-1336(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TTID.
    16. "Calsarcins, a novel family of sarcomeric calcineurin-binding proteins."
      Frey N., Richardson J.A., Olson E.N.
      Proc. Natl. Acad. Sci. U.S.A. 97:14632-14637(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYOZ2.
    17. "The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase."
      Izaguirre G., Aguirre L., Hu Y.P., Lee H.Y., Schlaepfer D.D., Aneskievich B.J., Haimovich B.
      J. Biol. Chem. 276:28676-28685(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT TYR-12.
    18. "The lipoma preferred partner LPP interacts with alpha-actinin."
      Li B., Zhuang L., Reinhard M., Trueb B.
      J. Cell Sci. 116:1359-1366(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LPP.
    19. "Postsynaptic recruitment of Dendrin depends on both dendritic mRNA transport and synaptic anchoring."
      Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A.
      J. Neurochem. 96:1659-1666(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DDN.
    20. "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-95; LYS-195 AND LYS-676, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    23. "Crystal structure of the actin-binding domain of alpha-actinin 1: evaluating two competing actin-binding models."
      Borrego-Diaz E., Kerff F., Lee S.H., Ferron F., Li Y., Dominguez R.
      J. Struct. Biol. 155:230-238(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 30-253.
    24. Cited for: VARIANTS BDPLT15 LYS-32; GLN-46; ILE-105; LYS-225; TRP-738 AND GLN-752, VARIANT TRP-197, CHARACTERIZATION OF VARIANTS BDPLT15 LYS-32 AND ILE-105.

    Entry informationi

    Entry nameiACTN1_HUMAN
    AccessioniPrimary (citable) accession number: P12814
    Secondary accession number(s): B3V8S3
    , B4DHH3, B7TY16, Q1HE25, Q9BTN1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1989
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 180 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 14
      Human chromosome 14: 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