Alpha-actinin-1 - Homo sapiens (Human)

Names and origin

Protein names

Recommended name:
    Alpha-actinin-1
Alternative name(s):
    Alpha-actinin cytoskeletal isoform
    Non-muscle alpha-actinin-1
    F-actin cross-linking protein

Gene names

Name:

ACTN1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	892 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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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. Interacts with MYOZ2, PDLIM2 and TTID and LPP.
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › myofibril › sarcomere › Z-disk. Note= Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle.
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.

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Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Domain	Repeat
Ligand	Actin-binding Calcium
PTM	Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	focal adhesion formation Inferred from mutant phenotype. Source: UniProtKB negative regulation of cell motion Inferred from mutant phenotype. Source: UniProtKB regulation of apoptosis Non-traceable author statement. Source: UniProtKB
Cellular component	focal adhesion Inferred from mutant phenotype. Source: UniProtKB pseudopodium Traceable author statement. Source: UniProtKB
Molecular function	integrin binding Inferred from direct assay. Source: UniProtKB vinculin binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
PTPN1	P18031	1	EBI-351710,EBI-968788
SRC	P12931	2	EBI-351710,EBI-621482

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Chain

1 – 892

892

Alpha-actinin-1

Regions

Domain

1 – 247

247

Actin-binding

Domain

31 – 135

105

CH 1

Domain

144 – 247

104

CH 2

Repeat

274 – 384

111

Spectrin 1

Repeat

394 – 499

106

Spectrin 2

Repeat

509 – 620

112

Spectrin 3

Repeat

630 – 733

104

Spectrin 4

Domain

746 – 781

36

EF-hand 1

Domain

787 – 822

36

EF-hand 2

Calcium binding

759 – 770

12

Potential

Calcium binding

800 – 811

12

Potential

Amino acid modifications

Modified residue

12

1

Phosphotyrosine; by FAK1

Modified residue

50

1

Phosphothreonine

Modified residue

140

1

Phosphoserine

Modified residue

193

1

Phosphotyrosine

Experimental info

Sequence conflict

317

1

R → L in CAA38970. Ref.5

Sequence conflict

477

1

Q → L in CAA38970. Ref.5

Sequence conflict

630 – 631

2

RL → SV in CAA33803. Ref.1

Sequence conflict

654 – 656

3

GRI → ARF in CAA38970. Ref.5

Sequence conflict

674

1

Y → D in CAA38970. Ref.5

Sequence conflict

778

1

L → S in CAA38970. Ref.5

Secondary structure

1

.

892

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P12814-1 [UniParc].

Last modified April 13, 2004. Version 2.
Checksum: 6DA3E4D1A0289519
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FASTA

892

103,058

        10         20         30         40         50         60 
MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT QIENIEEDFR 

        70         80         90        100        110        120 
DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI ASKGVKLVSI GAEEIVDGNV 

       130        140        150        160        170        180 
KMTLGMIWTI ILRFAIQDIS VEETSAKEGL LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC 

       190        200        210        220        230        240 
ALIHRHRPEL IDYGKLRKDD PLTNLNTAFD VAEKYLDIPK MLDAEDIVGT ARPDEKAIMT 

       250        260        270        280        290        300 
YVSSFYHAFS GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR 

       310        320        330        340        350        360 
VPENTMHAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR PAFMPSEGRM 

       370        380        390        400        410        420 
VSDINNAWGC LEQVEKGYEE WLLNEIRRLE RLDHLAEKFR QKASIHEAWT DGKEAMLRQK 

       430        440        450        460        470        480 
DYETATLSEI KALLKKHEAF ESDLAAHQDR VEQIAAIAQE LNELDYYDSP SVNARCQKIC 

       490        500        510        520        530        540 
DQWDNLGALT QKRREALERT EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT 

       550        560        570        580        590        600 
IEEIQGLTTA HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI 

       610        620        630        640        650        660 
NGKWDHVRQL VPRRDQALTE EHARQQHNER LRKQFGAQAN VIGPWIQTKM EEIGRISIEM 

       670        680        690        700        710        720 
HGTLEDQLSH LRQYEKSIVN YKPKIDQLEG DHQLIQEALI FDNKHTNYTM EHIRVGWEQL 

       730        740        750        760        770        780 
LTTIARTINE VENQILTRDA KGISQEQMNE FRASFNHFDR DHSGTLGPEE FKACLISLGY 

       790        800        810        820        830        840 
DIGNDPQGEA EFARIMSIVD PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK 

       850        860        870        880        890 
NYITMDELRR ELPPDQAEYC IARMAPYTGP DSVPGALDYM SFSTALYGES DL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The cDNA sequence of a human placental alpha-actinin." Millake D.B., Blanchard A.D., Patel B., Critchley D.R. Nucleic Acids Res. 17:6725-6725(1989) [PubMed: 2780298] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Cloning and chromosomal localization of the human cytoskeletal alpha-actinin gene reveals linkage to the beta-spectrin gene." Youssoufian H., McAfee M., Kwiatkowski D.J. Am. J. Hum. Genet. 47:62-71(1990) [PubMed: 2349951] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Colon and Skin.
[5]	"Expression of human alpha-actinin in human hepatocellular carcinoma." Nishiyama M., Ozturk M., Frohlich M., Mafune K., Steele G. Jr., Wands J.R. Cancer Res. 50:6291-6294(1990) [PubMed: 2169343] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 297-892.
[6]	"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides." Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J. Nat. Biotechnol. 21:566-569(2003) [PubMed: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-21. Tissue: Platelet.
[7]	"Identification of the 70kD heat shock cognate protein (Hsc70) and alpha-actinin-1 as novel phosphotyrosine-containing proteins in T lymphocytes." Egerton M., Moritz R.L., Druker B., Kelso A., Simpson R.J. Biochem. Biophys. Res. Commun. 224:666-674(1996) [PubMed: 8713105] [Abstract] Cited for: PROTEIN SEQUENCE OF 134-146.
[8]	"Identification of the cytoskeletal protein alpha-actinin as a platelet thrombospondin-binding protein." Dubernard V., Faucher D., Launay J.-M., Legrand C. FEBS Lett. 364:109-114(1995) [PubMed: 7750553] [Abstract] Cited for: PROTEIN SEQUENCE OF 566-577; 727-738 AND 835-863, SUBCELLULAR LOCATION.
[9]	"Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy." Salmikangas P., Mykkaenen O.M., Groenholm M., Heiska L., Kere J., Carpen O. Hum. Mol. Genet. 8:1329-1336(1999) [PubMed: 10369880] [Abstract] Cited for: INTERACTION WITH TTID.
[10]	"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: 11114196] [Abstract] Cited for: INTERACTION WITH MYOZ2.
[11]	"The cytoskeletal/non-muscle isoform of alpha-actinin is phosphorylated on its actin-binding domain by the focal adhesion kinase." Izaguirre G., Aguirre L., Hu Y.P., Lee H.Y., Schlaepfer D.D., Aneskievich B.J., Haimovich B. J. Biol. Chem. 276:28676-28685(2001) [PubMed: 11369769] [Abstract] Cited for: PHOSPHORYLATION AT TYR-12.
[12]	"The lipoma preferred partner LPP interacts with alpha-actinin." Li B., Zhuang L., Reinhard M., Trueb B. J. Cell Sci. 116:1359-1366(2003) [PubMed: 12615977] [Abstract] Cited for: INTERACTION WITH LPP.
[13]	"Global phosphoproteome analysis on human HepG2 hepatocytes using reversed-phase diagonal LC." Gevaert K., Staes A., Van Damme J., De Groot S., Hugelier K., Demol H., Martens L., Goethals M., Vandekerckhove J. Proteomics 5:3589-3599(2005) [PubMed: 16097034] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-50, MASS SPECTROMETRY. Tissue: Hepatocyte.
[14]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, MASS SPECTROMETRY. Tissue: Epithelium.
[15]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-193, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

X15804 mRNA. Translation: CAA33803.1.
M95178 mRNA. Translation: AAA51582.1.
BT007207 mRNA. Translation: AAP35871.1.
BC003576 mRNA. Translation: AAH03576.1.
BC015766 mRNA. Translation: AAH15766.1.
X55187 mRNA. Translation: CAA38970.1.

PIR

FAHUAA. S05503.

RefSeq

NP_001093.1.

UniGene

Hs.509765

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EYI	X-ray	1.70	A	30-254	[»]
2EYN	X-ray	1.80	A	30-254	[»]

SMR

P12814. Positions 25-892.

ModBase

Search...

Protein-protein interaction databases

IntAct

P12814.

PTM databases

PhosphoSite

P12814.

2-D gel databases

OGP

P12814.

Proteomic databases

PeptideAtlas

P12814.

Genome annotation databases

Ensembl

ENSG00000072110. Homo sapiens. [Contig view]

GeneID

87.

KEGG

hsa:87.

Organism-specific databases

H-InvDB

HIX0011761.
HIX0055478.

HGNC

HGNC:163. ACTN1.

HPA

CAB004303.
HPA006035.

MIM

102575. gene.

PharmGKB

PA24.

GenAtlas

Search...

GeneCards

Search...

Phylogenomic databases

HOVERGEN

P12814.

Gene expression databases

ArrayExpress

P12814.

CleanEx

HS_ACTN1.

GermOnline

ENSG00000072110. Homo sapiens.

Family and domain databases

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR016146. Calponin-homology.
IPR001715. Calponin_act_bd.
IPR014837. EF-hand_Ca_insen.
IPR011992. EF-Hand_type.
IPR002048. EF_hand_Ca_bd.
IPR002017. Spectrin_repeat.
[Graphical view]

Gene3D

G3DSA:1.10.418.10. Calponin-homology. 2 hits.
G3DSA:1.10.238.10. EF-Hand_type. 2 hits.

Pfam

PF00307. CH. 2 hits.
PF00036. efhand. 2 hits.
PF08726. efhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]

ProDom

PD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]

SMART

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

PROSITE

PS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 2 hits.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

BLOCKS

Search...

Other Resources

LinkHub

P12814.

SOURCE

Search...

ProtoNet

Search...

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Entry information

Entry name

ACTN1_HUMAN

Accession

Primary (citable) accession number: P12814
Secondary accession number(s): Q9BTN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	April 13, 2004
Last modified:	September 2, 2008
This is version 112 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 14<

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents