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P35609

- ACTN2_HUMAN

UniProt

P35609 - ACTN2_HUMAN

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Protein

Alpha-actinin-2

Gene

ACTN2

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.

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 dimerization activity Source: UniProtKB
  8. structural constituent of muscle Source: ProtInc
  9. thyroid hormone receptor coactivator activity Source: Ensembl
  10. titin binding Source: BHF-UCL
  11. 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
Complete GO annotation...

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: UniProtKB
  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
Complete GO annotation...

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

BgeeiP35609.
CleanExiHS_ACTN2.
ExpressionAtlasiP35609. baseline and differential.
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. 40 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.
GeneTreeiENSGT00760000118813.
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

        10         20         30         40         50
MNQIEPGVQY NYVYDEDEYM IQEEEWDRDL LLDPAWEKQQ RKTFTAWCNS
60 70 80 90 100
HLRKAGTQIE NIEEDFRNGL KLMLLLEVIS GERLPKPDRG KMRFHKIANV
110 120 130 140 150
NKALDYIASK GVKLVSIGAE EIVDGNVKMT LGMIWTIILR FAIQDISVEE
160 170 180 190 200
TSAKEGLLLW CQRKTAPYRN VNIQNFHTSW KDGLGLCALI HRHRPDLIDY
210 220 230 240 250
SKLNKDDPIG NINLAMEIAE KHLDIPKMLD AEDIVNTPKP DERAIMTYVS
260 270 280 290 300
CFYHAFAGAE QAETAANRIC KVLAVNQENE RLMEEYERLA SELLEWIRRT
310 320 330 340 350
IPWLENRTPE KTMQAMQKKL EDFRDYRRKH KPPKVQEKCQ LEINFNTLQT
360 370 380 390 400
KLRISNRPAF MPSEGKMVSD IAGAWQRLEQ AEKGYEEWLL NEIRRLERLE
410 420 430 440 450
HLAEKFRQKA STHETWAYGK EQILLQKDYE SASLTEVRAL LRKHEAFESD
460 470 480 490 500
LAAHQDRVEQ IAAIAQELNE LDYHDAVNVN DRCQKICDQW DRLGTLTQKR
510 520 530 540 550
REALERMEKL LETIDQLHLE FAKRAAPFNN WMEGAMEDLQ DMFIVHSIEE
560 570 580 590 600
IQSLITAHEQ FKATLPEADG ERQSIMAIQN EVEKVIQSYN IRISSSNPYS
610 620 630 640 650
TVTMDELRTK WDKVKQLVPI RDQSLQEELA RQHANERLRR QFAAQANAIG
660 670 680 690 700
PWIQNKMEEI ARSSIQITGA LEDQMNQLKQ YEHNIINYKN NIDKLEGDHQ
710 720 730 740 750
LIQEALVFDN KHTNYTMEHI RVGWELLLTT IARTINEVET QILTRDAKGI
760 770 780 790 800
TQEQMNEFRA SFNHFDRRKN GLMDHEDFRA CLISMGYDLG EAEFARIMTL
810 820 830 840 850
VDPNGQGTVT FQSFIDFMTR ETADTDTAEQ VIASFRILAS DKPYILAEEL
860 870 880 890
RRELPPDQAQ YCIKRMPAYS GPGSVPGALD YAAFSSALYG ESDL
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. 40 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.
GeneTreei ENSGT00760000118813.
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

Bgeei P35609.
CleanExi HS_ACTN2.
ExpressionAtlasi P35609. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 165 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