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P35609 (ACTN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-actinin-2
Alternative name(s):
Alpha-actinin skeletal muscle isoform 2
F-actin cross-linking protein
Gene names
Name:ACTN2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length894 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.

Subunit structure

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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13

Subcellular location

CytoplasmmyofibrilsarcomereZ line. Note: Colocalizes with MYOZ1 and FLNC at the Z-lines of skeletal muscle. Ref.9 Ref.13

Tissue specificity

Expressed in both skeletal and cardiac muscle.

Post-translational modification

Ubiquitinated by FBXL22, leading to proteasomal degradation. Ref.14

Involvement in disease

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.18

Sequence similarities

Belongs to the alpha-actinin family.

Contains 1 actin-binding domain.

Contains 2 CH (calponin-homology) domains.

Contains 2 EF-hand domains.

Contains 4 spectrin repeats.

Ontologies

Keywords
   Cellular componentCytoplasm
   Coding sequence diversityPolymorphism
   DiseaseCardiomyopathy
Disease mutation
   DomainRepeat
   LigandActin-binding
Calcium
Metal-binding
   PTMUbl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Traceable author statement. Source: Reactome

cell adhesion

Traceable author statement PubMed 10656685. Source: UniProtKB

focal adhesion assembly

Inferred from mutant phenotype PubMed 16807302. Source: UniProtKB

microspike assembly

Inferred from direct assay PubMed 12356918. Source: UniProtKB

muscle filament sliding

Traceable author statement. Source: Reactome

negative regulation of potassium ion transmembrane transporter activity

Inferred from mutant phenotype PubMed 10812072. Source: BHF-UCL

negative regulation of potassium ion transport

Inferred from mutant phenotype PubMed 10812072. Source: BHF-UCL

negative regulation of protein localization to cell surface

Inferred from mutant phenotype PubMed 10812072. Source: BHF-UCL

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

positive regulation of potassium ion transmembrane transporter activity

Inferred from direct assay PubMed 17110593. Source: BHF-UCL

positive regulation of potassium ion transport

Inferred from direct assay PubMed 17110593. Source: BHF-UCL

protein homotetramerization

Inferred from direct assay PubMed 9501083. Source: UniProtKB

regulation of apoptotic process

Non-traceable author statement PubMed 16807302. Source: UniProtKB

regulation of membrane potential

Inferred from mutant phenotype PubMed 10812072. Source: BHF-UCL

synaptic transmission

Traceable author statement. Source: Reactome

   Cellular_componentZ disc

Inferred from direct assay Ref.13. Source: UniProtKB

actin filament

Traceable author statement Ref.1. Source: ProtInc

cytoskeleton

Non-traceable author statement PubMed 12809483. Source: UniProtKB

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Traceable author statement PubMed 15841212. Source: UniProtKB

extracellular region

Traceable author statement. Source: Reactome

filopodium

Inferred from direct assay PubMed 12356918. Source: UniProtKB

focal adhesion

Inferred from mutant phenotype PubMed 16807302. Source: UniProtKB

platelet alpha granule lumen

Traceable author statement. Source: Reactome

pseudopodium

Traceable author statement PubMed 1629252. Source: UniProtKB

   Molecular_functionFATZ binding

Inferred from direct assay PubMed 11699871. Source: UniProtKB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

cytoskeletal protein binding

Inferred from direct assay Ref.6PubMed 11699871. Source: UniProtKB

identical protein binding

Inferred from physical interaction PubMed 11101506PubMed 9501083. Source: IntAct

integrin binding

Traceable author statement PubMed 8104223. Source: UniProtKB

ion channel binding

Inferred from physical interaction PubMed 10812072PubMed 17110593PubMed 17944866. Source: BHF-UCL

protein dimerization activity

Inferred from direct assay PubMed 9501083. Source: UniProtKB

structural constituent of muscle

Traceable author statement Ref.1. Source: ProtInc

thyroid hormone receptor coactivator activity

Inferred from electronic annotation. Source: Ensembl

titin Z domain binding

Inferred from physical interaction PubMed 11846417. Source: BHF-UCL

titin binding

Inferred from physical interaction PubMed 11846417PubMed 9501083. Source: BHF-UCL

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 894894Alpha-actinin-2
PRO_0000073435

Regions

Domain1 – 254254Actin-binding
Domain38 – 142105CH 1
Domain151 – 254104CH 2
Repeat281 – 391111Spectrin 1
Repeat401 – 506106Spectrin 2
Repeat516 – 627112Spectrin 3
Repeat637 – 740104Spectrin 4
Domain753 – 78836EF-hand 1
Domain789 – 82436EF-hand 2
Calcium binding766 – 777121; possibly ancestral
Calcium binding802 – 813122; possibly ancestral

Natural variations

Natural variant91Q → R in CMD1AA. Ref.18
Corresponds to variant rs121434525 [ dbSNP | Ensembl ].
VAR_054628
Natural variant6041M → V. Ref.18
Corresponds to variant rs35997569 [ dbSNP | Ensembl ].
VAR_033487

Secondary structure

...................................................... 894
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P35609 [UniParc].

Last modified June 1, 1994. Version 1.
Checksum: 7F612C1C3B3E2299

FASTA894103,854
        10         20         30         40         50         60 
MNQIEPGVQY NYVYDEDEYM IQEEEWDRDL LLDPAWEKQQ RKTFTAWCNS HLRKAGTQIE 

        70         80         90        100        110        120 
NIEEDFRNGL KLMLLLEVIS GERLPKPDRG KMRFHKIANV NKALDYIASK GVKLVSIGAE 

       130        140        150        160        170        180 
EIVDGNVKMT LGMIWTIILR FAIQDISVEE TSAKEGLLLW CQRKTAPYRN VNIQNFHTSW 

       190        200        210        220        230        240 
KDGLGLCALI HRHRPDLIDY SKLNKDDPIG NINLAMEIAE KHLDIPKMLD AEDIVNTPKP 

       250        260        270        280        290        300 
DERAIMTYVS CFYHAFAGAE QAETAANRIC KVLAVNQENE RLMEEYERLA SELLEWIRRT 

       310        320        330        340        350        360 
IPWLENRTPE KTMQAMQKKL EDFRDYRRKH KPPKVQEKCQ LEINFNTLQT KLRISNRPAF 

       370        380        390        400        410        420 
MPSEGKMVSD IAGAWQRLEQ AEKGYEEWLL NEIRRLERLE HLAEKFRQKA STHETWAYGK 

       430        440        450        460        470        480 
EQILLQKDYE SASLTEVRAL LRKHEAFESD LAAHQDRVEQ IAAIAQELNE LDYHDAVNVN 

       490        500        510        520        530        540 
DRCQKICDQW DRLGTLTQKR REALERMEKL LETIDQLHLE FAKRAAPFNN WMEGAMEDLQ 

       550        560        570        580        590        600 
DMFIVHSIEE IQSLITAHEQ FKATLPEADG ERQSIMAIQN EVEKVIQSYN IRISSSNPYS 

       610        620        630        640        650        660 
TVTMDELRTK WDKVKQLVPI RDQSLQEELA RQHANERLRR QFAAQANAIG PWIQNKMEEI 

       670        680        690        700        710        720 
ARSSIQITGA LEDQMNQLKQ YEHNIINYKN NIDKLEGDHQ LIQEALVFDN KHTNYTMEHI 

       730        740        750        760        770        780 
RVGWELLLTT IARTINEVET QILTRDAKGI TQEQMNEFRA SFNHFDRRKN GLMDHEDFRA 

       790        800        810        820        830        840 
CLISMGYDLG EAEFARIMTL VDPNGQGTVT FQSFIDFMTR ETADTDTAEQ VIASFRILAS 

       850        860        870        880        890 
DKPYILAEEL RRELPPDQAQ YCIKRMPAYS GPGSVPGALD YAAFSSALYG ESDL 

« Hide

References

« Hide 'large scale' references
[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].
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]"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. expand/collapse author list , 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].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"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: PNS.
[6]"ZASP: a new Z-band alternatively spliced PDZ-motif protein."
Faulkner G., Pallavicini A., Formentin E., Comelli A., Ievolella C., Trevisan S., Bortoletto G., Scannapieco P., Salamon M., Mouly V., Valle G., Lanfranchi G.
J. Cell Biol. 146:465-475(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LDB3.
[7]"FATZ, a filamin-, actinin-, and telethonin-binding protein of the Z-disc of skeletal muscle."
Faulkner G., Pallavicini A., Comelli A., Salamon M., Bortoletto G., Ievolella C., Trevisan S., Kojic' S., Dalla Vecchia F., Laveder P., Valle G., Lanfranchi G.
J. Biol. Chem. 275:41234-41242(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MYOZ1.
[8]"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.
[9]"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.
[10]"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.
[11]"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.
[12]"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.
[13]"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.
[14]"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.
[15]"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.
[16]"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.
[17]"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.
[18]"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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M86406 mRNA. Translation: AAA51583.1.
M86804 Genomic DNA. Translation: AAA51584.1.
AJ249756 expand/collapse EMBL AC list , 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.
AL359185, AL359921 Genomic DNA. Translation: CAH73201.1.
AL359921, AL359185 Genomic DNA. Translation: CAI13778.1.
CH471098 Genomic DNA. Translation: EAW70064.1.
BC047901 mRNA. Translation: AAH47901.2.
BC051770 mRNA. Translation: AAH51770.2.
PIRFAHUA2. A40199.
RefSeqNP_001094.1. NM_001103.3.
UniGeneHs.498178.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1H8BNMR-A823-894[»]
1HCIX-ray2.80A/B274-746[»]
1QUUX-ray2.50A391-637[»]
ProteinModelPortalP35609.
SMRP35609. Positions 35-261, 274-746, 751-894.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106603. 39 interactions.
DIPDIP-383N.
IntActP35609. 28 interactions.
MINTMINT-145583.
STRING9606.ENSP00000355537.

PTM databases

PhosphoSiteP35609.

Polymorphism databases

DMDM543742.

Proteomic databases

PaxDbP35609.
PeptideAtlasP35609.
PRIDEP35609.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000366578; ENSP00000355537; ENSG00000077522.
GeneID88.
KEGGhsa:88.
UCSCuc001hyf.2. human.

Organism-specific databases

CTD88.
GeneCardsGC01P236849.
HGNCHGNC:164. ACTN2.
HPAHPA006035.
HPA008315.
MIM102573. gene.
612158. phenotype.
neXtProtNX_P35609.
Orphanet154. Familial isolated dilated cardiomyopathy.
PharmGKBPA25.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000263418.
HOVERGENHBG050453.
InParanoidP35609.
KOK05699.
OrthoDBEOG72C4ZJ.
PhylomeDBP35609.
TreeFamTF352676.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_13685. Neuronal System.
REACT_17044. Muscle contraction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP35609.
BgeeP35609.
CleanExHS_ACTN2.
GenevestigatorP35609.

Family and domain databases

Gene3D1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProIPR001589. 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]
PfamPF00307. CH. 2 hits.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
SUPFAMSSF47576. SSF47576. 1 hit.
PROSITEPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP35609.
GeneWikiActinin,_alpha_2.
GenomeRNAi88.
NextBio327.
PROP35609.
SOURCESearch...

Entry information

Entry nameACTN2_HUMAN
AccessionPrimary (citable) accession number: P35609
Secondary accession number(s): B1ANE4, Q86TF4, Q86TI8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 1, 1994
Last sequence update: June 1, 1994
Last modified: April 16, 2014
This is version 159 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM