Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P35609

- ACTN2_HUMAN

UniProt

P35609 - ACTN2_HUMAN

Protein

Alpha-actinin-2

Gene

ACTN2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    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 bindingi766 – 777121; possibly ancestralAdd
    BLAST
    Calcium bindingi802 – 813122; possibly ancestralAdd
    BLAST

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. cytoskeletal protein binding Source: UniProtKB
    3. FATZ binding Source: UniProtKB
    4. identical protein binding Source: IntAct
    5. integrin binding Source: UniProtKB
    6. ion channel binding Source: BHF-UCL
    7. protein binding Source: UniProtKB
    8. protein dimerization activity Source: UniProtKB
    9. structural constituent of muscle Source: ProtInc
    10. thyroid hormone receptor coactivator activity Source: Ensembl
    11. titin binding Source: BHF-UCL
    12. titin Z domain binding Source: BHF-UCL

    GO - Biological processi

    1. blood coagulation Source: Reactome
    2. cell adhesion Source: UniProtKB
    3. focal adhesion assembly Source: UniProtKB
    4. microspike assembly Source: UniProtKB
    5. muscle filament sliding Source: Reactome
    6. negative regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
    7. negative regulation of potassium ion transport Source: BHF-UCL
    8. negative regulation of protein localization to cell surface Source: BHF-UCL
    9. platelet activation Source: Reactome
    10. platelet degranulation Source: Reactome
    11. positive regulation of potassium ion transmembrane transporter activity Source: BHF-UCL
    12. positive regulation of potassium ion transport Source: BHF-UCL
    13. protein homotetramerization Source: UniProtKB
    14. regulation of apoptotic process Source: UniProtKB
    15. regulation of membrane potential Source: BHF-UCL
    16. synaptic transmission Source: Reactome

    Keywords - Ligandi

    Actin-binding, Calcium, Metal-binding

    Enzyme and pathway databases

    ReactomeiREACT_16969. Striated Muscle Contraction.
    REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
    REACT_20642. CREB phosphorylation through the activation of CaMKII.
    REACT_23832. Nephrin interactions.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-actinin-2
    Alternative name(s):
    Alpha-actinin skeletal muscle isoform 2
    F-actin cross-linking protein
    Gene namesi
    Name:ACTN2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:164. ACTN2.

    Subcellular locationi

    CytoplasmmyofibrilsarcomereZ line 2 Publications
    Note: Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle.

    GO - Cellular componenti

    1. actin filament Source: ProtInc
    2. cytoskeleton Source: UniProtKB
    3. cytosol Source: Reactome
    4. dendritic spine Source: UniProtKB
    5. extracellular region Source: Reactome
    6. extracellular vesicular exosome Source: UniProt
    7. filopodium Source: UniProtKB
    8. focal adhesion Source: UniProtKB
    9. platelet alpha granule lumen Source: Reactome
    10. pseudopodium Source: UniProtKB
    11. Z disc Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Involvement in diseasei

    Cardiomyopathy, dilated 1AA (CMD1AA) [MIM:612158]: A disorder characterized by ventricular dilation and impaired systolic function, resulting in congestive heart failure and arrhythmia. Patients are at risk of premature death.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91Q → R in CMD1AA. 1 Publication
    Corresponds to variant rs121434525 [ dbSNP | Ensembl ].
    VAR_054628

    Keywords - Diseasei

    Cardiomyopathy, Disease mutation

    Organism-specific databases

    MIMi612158. phenotype.
    Orphaneti154. Familial isolated dilated cardiomyopathy.
    PharmGKBiPA25.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 894894Alpha-actinin-2PRO_0000073435Add
    BLAST

    Post-translational modificationi

    Ubiquitinated by FBXL22, leading to proteasomal degradation.1 Publication

    Keywords - PTMi

    Ubl conjugation

    Proteomic databases

    MaxQBiP35609.
    PaxDbiP35609.
    PeptideAtlasiP35609.
    PRIDEiP35609.

    PTM databases

    PhosphoSiteiP35609.

    Expressioni

    Tissue specificityi

    Expressed in both skeletal and cardiac muscle.

    Gene expression databases

    ArrayExpressiP35609.
    BgeeiP35609.
    CleanExiHS_ACTN2.
    GenevestigatoriP35609.

    Organism-specific databases

    HPAiHPA006035.
    HPA008315.

    Interactioni

    Subunit structurei

    Homodimer; antiparallel. Also forms heterodimers with ACTN3. Interacts with ADAM12, MYOZ1, MYOZ2 and MYOZ3. Interacts via its C-terminal region with the LDB3 PDZ domain. Interacts with XIRP2. Interacts with DST isoform 1 (via N-terminus). Interacts with PARVB.8 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself8EBI-77797,EBI-77797
    Adam12Q618243EBI-77797,EBI-77785From a different organism.
    ANGP039504EBI-77797,EBI-525291
    APPL1Q9UKG12EBI-77797,EBI-741243
    DISC1Q9NRI53EBI-77797,EBI-529989
    DYSFO759232EBI-77797,EBI-2799016
    KCNA5P224606EBI-77797,EBI-6426121
    MYOM2P542962EBI-77797,EBI-5357134
    TTNQ8WZ4216EBI-77797,EBI-681210

    Protein-protein interaction databases

    BioGridi106603. 39 interactions.
    DIPiDIP-383N.
    IntActiP35609. 29 interactions.
    MINTiMINT-145583.
    STRINGi9606.ENSP00000355537.

    Structurei

    Secondary structure

    1
    894
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi275 – 29420
    Helixi296 – 3038
    Beta strandi311 – 3133
    Turni314 – 3174
    Helixi318 – 32912
    Helixi331 – 34010
    Turni341 – 3433
    Helixi344 – 3474
    Turni351 – 3566
    Helixi364 – 3663
    Beta strandi368 – 3703
    Helixi371 – 38212
    Helixi393 – 41624
    Turni417 – 4193
    Helixi420 – 4256
    Helixi428 – 4303
    Helixi434 – 47037
    Helixi476 – 53661
    Turni537 – 5404
    Turni548 – 5503
    Helixi551 – 56212
    Helixi564 – 58825
    Helixi604 – 63229
    Turni666 – 6694
    Helixi672 – 70433
    Helixi716 – 74126
    Helixi828 – 83811
    Beta strandi843 – 8453
    Helixi847 – 8537
    Helixi856 – 86510
    Helixi881 – 8888

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1H8BNMR-A822-894[»]
    1HCIX-ray2.80A/B274-746[»]
    1QUUX-ray2.50A391-637[»]
    ProteinModelPortaliP35609.
    SMRiP35609. Positions 35-261, 274-894.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP35609.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 254254Actin-bindingAdd
    BLAST
    Domaini38 – 142105CH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini151 – 254104CH 2PROSITE-ProRule annotationAdd
    BLAST
    Repeati281 – 391111Spectrin 1Add
    BLAST
    Repeati401 – 506106Spectrin 2Add
    BLAST
    Repeati516 – 627112Spectrin 3Add
    BLAST
    Repeati637 – 740104Spectrin 4Add
    BLAST
    Domaini753 – 78836EF-hand 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini789 – 82436EF-hand 2PROSITE-ProRule annotationAdd
    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.
    InParanoidiP35609.
    KOiK05699.
    OrthoDBiEOG72C4ZJ.
    PhylomeDBiP35609.
    TreeFamiTF352676.

    Family and domain databases

    Gene3Di1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProiIPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR002048. EF_hand_dom.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view]
    PfamiPF00307. CH. 2 hits.
    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.
    PS50222. EF_HAND_2. 2 hits.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P35609-1) [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

    MNQIEPGVQY NYVYDEDEYM IQEEEWDRDL LLDPAWEKQQ RKTFTAWCNS    50
    HLRKAGTQIE NIEEDFRNGL KLMLLLEVIS GERLPKPDRG KMRFHKIANV 100
    NKALDYIASK GVKLVSIGAE EIVDGNVKMT LGMIWTIILR FAIQDISVEE 150
    TSAKEGLLLW CQRKTAPYRN VNIQNFHTSW KDGLGLCALI HRHRPDLIDY 200
    SKLNKDDPIG NINLAMEIAE KHLDIPKMLD AEDIVNTPKP DERAIMTYVS 250
    CFYHAFAGAE QAETAANRIC KVLAVNQENE RLMEEYERLA SELLEWIRRT 300
    IPWLENRTPE KTMQAMQKKL EDFRDYRRKH KPPKVQEKCQ LEINFNTLQT 350
    KLRISNRPAF MPSEGKMVSD IAGAWQRLEQ AEKGYEEWLL NEIRRLERLE 400
    HLAEKFRQKA STHETWAYGK EQILLQKDYE SASLTEVRAL LRKHEAFESD 450
    LAAHQDRVEQ IAAIAQELNE LDYHDAVNVN DRCQKICDQW DRLGTLTQKR 500
    REALERMEKL LETIDQLHLE FAKRAAPFNN WMEGAMEDLQ DMFIVHSIEE 550
    IQSLITAHEQ FKATLPEADG ERQSIMAIQN EVEKVIQSYN IRISSSNPYS 600
    TVTMDELRTK WDKVKQLVPI RDQSLQEELA RQHANERLRR QFAAQANAIG 650
    PWIQNKMEEI ARSSIQITGA LEDQMNQLKQ YEHNIINYKN NIDKLEGDHQ 700
    LIQEALVFDN KHTNYTMEHI RVGWELLLTT IARTINEVET QILTRDAKGI 750
    TQEQMNEFRA SFNHFDRRKN GLMDHEDFRA CLISMGYDLG EAEFARIMTL 800
    VDPNGQGTVT FQSFIDFMTR ETADTDTAEQ VIASFRILAS DKPYILAEEL 850
    RRELPPDQAQ YCIKRMPAYS GPGSVPGALD YAAFSSALYG ESDL 894
    Length:894
    Mass (Da):103,854
    Last modified:June 1, 1994 - v1
    Checksum:i7F612C1C3B3E2299
    GO
    Isoform 2 (identifier: P35609-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         234-261: IVNTPKPDERAIMTYVSCFYHAFAGAEQ → LVYTARPDERAIMTYVSCYYHAFAGAQK

    Note: No experimental confirmation available.

    Show »
    Length:894
    Mass (Da):103,920
    Checksum:iBA180F6305E25A8D
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti9 – 91Q → R in CMD1AA. 1 Publication
    Corresponds to variant rs121434525 [ dbSNP | Ensembl ].
    VAR_054628
    Natural varianti604 – 6041M → V.1 Publication
    Corresponds to variant rs35997569 [ dbSNP | Ensembl ].
    VAR_033487

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei234 – 26128IVNTP…AGAEQ → LVYTARPDERAIMTYVSCYY HAFAGAQK in isoform 2. 1 PublicationVSP_054923Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86406 mRNA. Translation: AAA51583.1.
    M86804 Genomic DNA. Translation: AAA51584.1.
    AJ249756
    , AJ249757, AJ249758, AJ249759, AJ249760, AJ249761, AJ249762, AJ249763, AJ249764, AJ249765, AJ249766, AJ249767, AJ249768, AJ249769, AJ249770, AJ249771, AJ249772, AJ249773, AJ249774, AJ249775, AJ249776 Genomic DNA. Translation: CAB61269.1.
    AK315250 mRNA. Translation: BAG37672.1.
    AL359185, AL359921 Genomic DNA. Translation: CAH73201.1.
    AL359921, AL359185 Genomic DNA. Translation: CAI13778.1.
    CH471098 Genomic DNA. Translation: EAW70064.1.
    CH471098 Genomic DNA. Translation: EAW70065.1.
    BC047901 mRNA. Translation: AAH47901.2.
    BC051770 mRNA. Translation: AAH51770.2.
    CCDSiCCDS1613.1. [P35609-1]
    CCDS60455.1. [P35609-2]
    PIRiA40199. FAHUA2.
    RefSeqiNP_001094.1. NM_001103.3. [P35609-1]
    NP_001265272.1. NM_001278343.1. [P35609-2]
    NP_001265273.1. NM_001278344.1.
    UniGeneiHs.498178.

    Genome annotation databases

    EnsembliENST00000366578; ENSP00000355537; ENSG00000077522. [P35609-1]
    ENST00000542672; ENSP00000443495; ENSG00000077522. [P35609-2]
    GeneIDi88.
    KEGGihsa:88.
    UCSCiuc001hyf.2. human. [P35609-1]
    uc009xgi.1. human.

    Polymorphism databases

    DMDMi543742.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M86406 mRNA. Translation: AAA51583.1 .
    M86804 Genomic DNA. Translation: AAA51584.1 .
    AJ249756
    , AJ249757 , AJ249758 , AJ249759 , AJ249760 , AJ249761 , AJ249762 , AJ249763 , AJ249764 , AJ249765 , AJ249766 , AJ249767 , AJ249768 , AJ249769 , AJ249770 , AJ249771 , AJ249772 , AJ249773 , AJ249774 , AJ249775 , AJ249776 Genomic DNA. Translation: CAB61269.1 .
    AK315250 mRNA. Translation: BAG37672.1 .
    AL359185 , AL359921 Genomic DNA. Translation: CAH73201.1 .
    AL359921 , AL359185 Genomic DNA. Translation: CAI13778.1 .
    CH471098 Genomic DNA. Translation: EAW70064.1 .
    CH471098 Genomic DNA. Translation: EAW70065.1 .
    BC047901 mRNA. Translation: AAH47901.2 .
    BC051770 mRNA. Translation: AAH51770.2 .
    CCDSi CCDS1613.1. [P35609-1 ]
    CCDS60455.1. [P35609-2 ]
    PIRi A40199. FAHUA2.
    RefSeqi NP_001094.1. NM_001103.3. [P35609-1 ]
    NP_001265272.1. NM_001278343.1. [P35609-2 ]
    NP_001265273.1. NM_001278344.1.
    UniGenei Hs.498178.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1H8B NMR - A 822-894 [» ]
    1HCI X-ray 2.80 A/B 274-746 [» ]
    1QUU X-ray 2.50 A 391-637 [» ]
    ProteinModelPortali P35609.
    SMRi P35609. Positions 35-261, 274-894.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106603. 39 interactions.
    DIPi DIP-383N.
    IntActi P35609. 29 interactions.
    MINTi MINT-145583.
    STRINGi 9606.ENSP00000355537.

    PTM databases

    PhosphoSitei P35609.

    Polymorphism databases

    DMDMi 543742.

    Proteomic databases

    MaxQBi P35609.
    PaxDbi P35609.
    PeptideAtlasi P35609.
    PRIDEi P35609.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366578 ; ENSP00000355537 ; ENSG00000077522 . [P35609-1 ]
    ENST00000542672 ; ENSP00000443495 ; ENSG00000077522 . [P35609-2 ]
    GeneIDi 88.
    KEGGi hsa:88.
    UCSCi uc001hyf.2. human. [P35609-1 ]
    uc009xgi.1. human.

    Organism-specific databases

    CTDi 88.
    GeneCardsi GC01P236849.
    GeneReviewsi ACTN2.
    HGNCi HGNC:164. ACTN2.
    HPAi HPA006035.
    HPA008315.
    MIMi 102573. gene.
    612158. phenotype.
    neXtProti NX_P35609.
    Orphaneti 154. Familial isolated dilated cardiomyopathy.
    PharmGKBi PA25.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5069.
    HOGENOMi HOG000263418.
    HOVERGENi HBG050453.
    InParanoidi P35609.
    KOi K05699.
    OrthoDBi EOG72C4ZJ.
    PhylomeDBi P35609.
    TreeFami TF352676.

    Enzyme and pathway databases

    Reactomei REACT_16969. Striated Muscle Contraction.
    REACT_20546. Ras activation uopn Ca2+ infux through NMDA receptor.
    REACT_20594. Unblocking of NMDA receptor, glutamate binding and activation.
    REACT_20642. CREB phosphorylation through the activation of CaMKII.
    REACT_23832. Nephrin interactions.

    Miscellaneous databases

    EvolutionaryTracei P35609.
    GeneWikii Actinin,_alpha_2.
    GenomeRNAii 88.
    NextBioi 327.
    PROi P35609.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P35609.
    Bgeei P35609.
    CleanExi HS_ACTN2.
    Genevestigatori P35609.

    Family and domain databases

    Gene3Di 1.10.238.10. 2 hits.
    1.10.418.10. 2 hits.
    InterProi IPR001589. Actinin_actin-bd_CS.
    IPR001715. CH-domain.
    IPR011992. EF-hand-dom_pair.
    IPR014837. EF-hand_Ca_insen.
    IPR002048. EF_hand_dom.
    IPR018159. Spectrin/alpha-actinin.
    IPR002017. Spectrin_repeat.
    [Graphical view ]
    Pfami PF00307. CH. 2 hits.
    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.
    PS50222. EF_HAND_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of two human skeletal muscle alpha-actinin genes located on chromosomes 1 and 11."
      Beggs A.H., Byers T.J., Knoll J.H.M., Boyce F.M., Bruns G.A.P., Kunkel L.M.
      J. Biol. Chem. 267:9281-9288(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1).
      Tissue: Skeletal muscle.
    2. "Fine mapping and genomic structure of ACTN2, the human gene coding for the sarcomeric isoform of alpha-actinin-2, expressed in skeletal and cardiac muscle."
      Tiso N., Majetti M., Stanchi F., Rampazzo A., Zimbello R., Nava A., Danieli G.A.
      Biochem. Biophys. Res. Commun. 265:256-259(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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.
    4. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: PNS.
    7. Cited for: INTERACTION WITH LDB3.
    8. Cited for: INTERACTION WITH MYOZ1.
    9. "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 MYOZ1 AND MYOZ2.
    10. "Myozenin: an alpha-actinin- and gamma-filamin-binding protein of skeletal muscle Z lines."
      Takada F., Vander Woude D.L., Tong H.-Q., Thompson T.G., Watkins S.C., Kunkel L.M., Beggs A.H.
      Proc. Natl. Acad. Sci. U.S.A. 98:1595-1600(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYOZ1, SUBCELLULAR LOCATION.
    11. "Calsarcin-3, a novel skeletal muscle-specific member of the calsarcin family, interacts with multiple Z-disc proteins."
      Frey N., Olson E.N.
      J. Biol. Chem. 277:13998-14004(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MYOZ3.
    12. "Affixin interacts with alpha-actinin and mediates integrin signaling for reorganization of F-actin induced by initial cell-substrate interaction."
      Yamaji S., Suzuki A., Kanamori H., Mishima W., Yoshimi R., Takasaki H., Takabayashi M., Fujimaki K., Fujisawa S., Ohno S., Ishigatsubo Y.
      J. Cell Biol. 165:539-551(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH PARVB.
    13. "Myomaxin is a novel transcriptional target of MEF2A that encodes a Xin-related alpha-actinin-interacting protein."
      Huang H.-T., Brand O.M., Mathew M., Ignatiou C., Ewen E.P., McCalmon S.A., Naya F.J.
      J. Biol. Chem. 281:39370-39379(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH XIRP2.
    14. "BPAG1 isoform-b: complex distribution pattern in striated and heart muscle and association with plectin and alpha-actinin."
      Steiner-Champliaud M.F., Schneider Y., Favre B., Paulhe F., Praetzel-Wunder S., Faulkner G., Konieczny P., Raith M., Wiche G., Adebola A., Liem R.K., Langbein L., Sonnenberg A., Fontao L., Borradori L.
      Exp. Cell Res. 316:297-313(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DST, SUBCELLULAR LOCATION.
    15. "F-box and leucine-rich repeat protein 22 is a cardiac-enriched F-box protein that regulates sarcomeric protein turnover and is essential for maintenance of contractile function in vivo."
      Spaich S., Will R.D., Just S., Spaich S., Kuhn C., Frank D., Berger I.M., Wiemann S., Korn B., Koegl M., Backs J., Katus H.A., Rottbauer W., Frey N.
      Circ. Res. 111:1504-1516(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY FBXL22.
    16. "Structure of the alpha-actinin rod: molecular basis for cross-linking of actin filaments."
      Djinovic-Carugo K., Young P., Gautel M., Saraste M.
      Cell 98:537-546(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 391-637.
    17. "Ca2+-independent binding of an EF-hand domain to a novel motif in the alpha-actinin-titin complex."
      Atkinson R.A., Joseph C., Kelly G., Muskett F.W., Frenkiel T.A., Nietlispach D., Pastore A.
      Nat. Struct. Biol. 8:853-857(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 823-894 IN COMPLEX WITH A TITIN Z-REPEAT.
    18. "Crystal structure of the alpha-actinin rod reveals an extensive torsional twist."
      Ylanne J., Scheffzek K., Young P., Saraste M.
      Structure 9:597-604(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 274-746.
    19. "Mutations in the muscle LIM protein and alpha-actinin-2 genes in dilated cardiomyopathy and endocardial fibroelastosis."
      Mohapatra B., Jimenez S., Lin J.H., Bowles K.R., Coveler K.J., Marx J.G., Chrisco M.A., Murphy R.T., Lurie P.R., Schwartz R.J., Elliott P.M., Vatta M., McKenna W., Towbin J.A., Bowles N.E.
      Mol. Genet. Metab. 80:207-215(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT CMD1AA ARG-9, VARIANT VAL-604.

    Entry informationi

    Entry nameiACTN2_HUMAN
    AccessioniPrimary (citable) accession number: P35609
    Secondary accession number(s): B1ANE4
    , B2RCS5, Q86TF4, Q86TI8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 164 of the entry and version 1 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 1
      Human chromosome 1: 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