P35609 (ACTN2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Alpha-actinin-2

Alternative name(s):
Alpha-actinin skeletal muscle isoform 2
F-actin cross-linking protein

Gene names

Name:

ACTN2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	894 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › myofibril › sarcomere › Z 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.15
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.19
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 component	Cytoplasm
Coding sequence diversity	Polymorphism
Disease	Cardiomyopathy Disease mutation
Domain	Repeat
Ligand	Actin-binding Calcium Metal-binding
PTM	Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	actin crosslink formation Inferred from electronic annotation. Source: InterPro actin filament bundle assembly Inferred from electronic annotation. Source: InterPro 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_component	Z disc Inferred from direct assay Ref.13. Source: UniProtKB actin filament Traceable author statement Ref.1. Source: ProtInc 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_function	FATZ binding Inferred from direct assay PubMed 11699871. Source: UniProtKB calcium ion binding Inferred from electronic annotation. Source: InterPro integrin binding Traceable author statement PubMed 8104223. Source: UniProtKB 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: Compara
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		8	EBI-77797,EBI-77797
Adam12	Q61824	3	EBI-77797,EBI-77785	From a different organism.
ANG	P03950	4	EBI-77797,EBI-525291
APPL1	Q9UKG1	2	EBI-77797,EBI-741243
DISC1	Q9NRI5	3	EBI-77797,EBI-529989
DYSF	O75923	2	EBI-77797,EBI-2799016
MYOM2	P54296	2	EBI-77797,EBI-5357134
TTN	Q8WZ42	14	EBI-77797,EBI-681210

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 894

894

Alpha-actinin-2

PRO_0000073435

Regions

Domain

1 – 254

254

Actin-binding

Domain

38 – 142

105

CH 1

Domain

151 – 254

104

CH 2

Repeat

281 – 391

111

Spectrin 1

Repeat

401 – 506

106

Spectrin 2

Repeat

516 – 627

112

Spectrin 3

Repeat

637 – 740

104

Spectrin 4

Domain

753 – 788

36

EF-hand 1

Domain

789 – 824

36

EF-hand 2

Calcium binding

766 – 777

12

1; possibly ancestral

Calcium binding

802 – 813

12

2; possibly ancestral

Amino acid modifications

Modified residue

237

1

Phosphothreonine By similarity

Natural variations

Natural variant

9

1

Q → R in CMD1AA. Ref.19

VAR_054628

Natural variant

604

1

M → V. Ref.19
Corresponds to variant rs35997569 [ dbSNP | Ensembl ].

VAR_033487

Secondary structure

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894

Helix Strand Turn

Details...

Helix

275 – 294

20

Helix

296 – 303

8

Beta strand

311 – 313

3

Turn

314 – 317

4

Helix

318 – 329

12

Helix

331 – 340

10

Turn

341 – 343

3

Helix

344 – 347

4

Turn

351 – 356

6

Helix

364 – 366

3

Beta strand

368 – 370

3

Helix

371 – 382

12

Helix

393 – 416

24

Turn

417 – 419

3

Helix

420 – 425

6

Helix

428 – 430

3

Helix

434 – 470

37

Helix

476 – 536

61

Turn

537 – 540

4

Turn

548 – 550

3

Helix

551 – 562

12

Helix

564 – 588

25

Helix

604 – 632

29

Turn

666 – 669

4

Helix

672 – 704

33

Helix

716 – 741

26

Helix

828 – 838

11

Beta strand

843 – 845

3

Helix

847 – 853

7

Helix

856 – 865

10

Helix

881 – 888

8

Sequences

	Sequence		Length	Mass (Da)
	P35609 [UniParc]. Last modified June 1, 1994. Version 1. Checksum: 7F612C1C3B3E2299	FASTA	894	103,854
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
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.

IPI

IPI00019884.

PIR

FAHUA2. A40199.

RefSeq

NP_001094.1. NM_001103.2.

UniGene

Hs.498178.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1H8B	NMR	-	A	823-894	[»]
1HCI	X-ray	2.80	A/B	274-746	[»]
1QUU	X-ray	2.50	A	391-637	[»]

ProteinModelPortal

P35609.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-383N.

IntAct

P35609. 24 interactions.

MINT

MINT-145583.

STRING

9606.ENSP00000355537.

PTM databases

PhosphoSite

P35609.

Polymorphism databases

DMDM

543742.

Proteomic databases

PaxDb

P35609.

PeptideAtlas

P35609.

PRIDE

P35609.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366578; ENSP00000355537; ENSG00000077522.

GeneID

88.

KEGG

hsa:88.

UCSC

uc001hyf.2. human.

Organism-specific databases

CTD

88.

GeneCards

GC01P236849.

HGNC

HGNC:164. ACTN2.

HPA

HPA006035.
HPA008315.

MIM

102573. gene.
612158. phenotype.

neXtProt

NX_P35609.

Orphanet

154. Familial isolated dilated cardiomyopathy.

PharmGKB

PA25.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5069.

HOGENOM

HOG000263418.

HOVERGEN

HBG050453.

InParanoid

P35609.

KO

K05699.

OMA

ELRTKWD.

OrthoDB

EOG44F68D.

Enzyme and pathway databases

Reactome

REACT_111155. Cell-Cell communication.
REACT_13685. Neuronal System.
REACT_17044. Muscle contraction.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P35609.

Bgee

P35609.

CleanEx

HS_ACTN2.

Genevestigator

P35609.

GermOnline

ENSG00000077522. Homo sapiens.

Family and domain databases

Gene3D

1.10.238.10. 2 hits.
1.10.418.10. 2 hits.

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR026921. Alpha-actinin.
IPR001715. CH-domain.
IPR011992. EF-hand-like_dom.
IPR014837. EF-hand_Ca_insen.
IPR002048. EF_hand_dom.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]

PANTHER

PTHR11915:SF47. PTHR11915:SF47. 1 hit.

Pfam

PF00307. CH. 2 hits.
PF08726. efhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]

SMART

SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view]

SUPFAM

SSF47576. Calponin-homology. 1 hit.

PROSITE

PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P35609.

GenomeRNAi

88.

NextBio

327.

SOURCE

Search...

Entry information

Entry name

ACTN2_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 150 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.