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Reviewed, UniProtKB/Swiss-Prot P12814 (ACTN1_HUMAN)

Last modified November 3, 2009. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length892 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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. Interacts with DDN, MYOZ2, PDLIM2, TTID and LPP. Ref.9 Ref.10 Ref.12 Ref.15

Subcellular location

Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ-disk. Note: Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Ref.8

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.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 892892Alpha-actinin-1
PRO_0000073431

Regions

Domain1 – 247247Actin-binding
Domain31 – 135105CH 1
Domain144 – 247104CH 2
Repeat274 – 384111Spectrin 1
Repeat394 – 499106Spectrin 2
Repeat509 – 620112Spectrin 3
Repeat630 – 733104Spectrin 4
Domain746 – 78136EF-hand 1
Domain787 – 82236EF-hand 2
Calcium binding759 – 77012 Potential
Calcium binding800 – 81112 Potential
Region274 – 733460Interaction with DDN

Amino acid modifications

Modified residue121Phosphotyrosine; by FAK1 Ref.11
Modified residue501Phosphothreonine Ref.13
Modified residue951N6-acetyllysine Ref.20
Modified residue1401Phosphoserine Ref.14 Ref.17
Modified residue1931Phosphotyrosine Ref.16
Modified residue1951N6-acetyllysine Ref.20
Modified residue2461Phosphotyrosine Ref.19
Modified residue6761N6-acetyllysine Ref.20

Natural variations

Natural variant7071N → T: dbSNP rs7157661.
VAR_053883
Natural variant8681T → S: dbSNP rs11557769.
VAR_053884

Experimental info

Sequence conflict3171R → L in CAA38970. Ref.5
Sequence conflict4771Q → L in CAA38970. Ref.5
Sequence conflict630 – 6312RL → SV in CAA33803. Ref.1
Sequence conflict654 – 6563GRI → ARF in CAA38970. Ref.5
Sequence conflict6741Y → D in CAA38970. Ref.5
Sequence conflict7781L → S in CAA38970. Ref.5

Secondary structure

................................. 892
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P12814-1 [UniParc].

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

FASTA892103,058
        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 

« Hide

References

« Hide '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]"Postsynaptic recruitment of Dendrin depends on both dendritic mRNA transport and synaptic anchoring."
Kremerskothen J., Kindler S., Finger I., Veltel S., Barnekow A.
J. Neurochem. 96:1659-1666(2006) [PubMed: 16464232] [Abstract]
Cited for: INTERACTION WITH DDN.
[16]"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. expand/collapse author list , Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.
Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-193, MASS SPECTROMETRY.
[17]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-140, MASS SPECTROMETRY.
[18]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells."
Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J.
J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-246, MASS SPECTROMETRY.
Tissue: Mammary epithelium.
[20]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed: 19608861] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-195 AND LYS-676, MASS SPECTROMETRY.
[21]"Crystal structure of the actin-binding domain of alpha-actinin 1: evaluating two competing actin-binding models."
Borrego-Diaz E., Kerff F., Lee S.H., Ferron F., Li Y., Dominguez R.
J. Struct. Biol. 155:230-238(2006) [PubMed: 16698282] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 30-253.
+Additional computationally mapped references.

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.
IPIIPI00013508.
PIRFAHUAA. S05503.
RefSeqNP_001093.1.
NP_001123477.1.
UniGeneHs.509765

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2EYIX-ray1.70A30-253[»]
2EYNX-ray1.80A30-253[»]
SMRP12814. Positions 25-892.
ModBaseSearch...

Protein-protein interaction databases

IntActP12814. 11 interactions.
STRINGP12814.

PTM databases

PhosphoSiteP12814.

2-D gel databases

OGPP12814.

Proteomic databases

PeptideAtlasP12814.
PRIDEP12814.

Genome annotation databases

EnsemblENST00000193403; ENSP00000193403; ENSG00000072110; Homo sapiens. [Genome view]
ENST00000376839; ENSP00000366035; ENSG00000072110; Homo sapiens. [Genome view]
ENST00000394419; ENSP00000377941; ENSG00000072110; Homo sapiens. [Genome view]
ENST00000438964; ENSP00000414272; ENSG00000072110; Homo sapiens. [Genome view]
GeneID87.
KEGGhsa:87.
UCSCuc001xkl.1. human.

Organism-specific databases

CTD87.
GeneCardsGC14M068410.
H-InvDBHIX0011761.
HIX0055478.
HGNCHGNC:163. ACTN1.
HPACAB004303.
HPA006035.
MIM102575. gene.
PharmGKBPA24.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP12814.

Enzyme and pathway databases

Pathway_Interaction_DBsyndecan_4_pathway. Syndecan-4-mediated signaling events.
ReactomeREACT_604. Hemostasis.

Gene expression databases

ArrayExpressP12814.
BgeeP12814.
CleanExHS_ACTN1.
GenevestigatorP12814.
GermOnlineENSG00000072110. Homo sapiens.

Family and domain databases

InterProIPR001589. Actinin_actin-bd_CS.
IPR001715. Calponin_act_bd.
IPR014837. EF-hand_Ca_insen.
IPR011992. EF-Hand_type.
IPR018248. EF_hand.
IPR018247. EF_HAND_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca_bd.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
Gene3DG3DSA:1.10.418.10. Calponin-homology. 2 hits.
G3DSA:1.10.238.10. EF-Hand_type. 2 hits.
PfamPF00307. CH. 2 hits.
PF00036. efhand. 1 hit.
PF08726. efhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
ProDomPD000012. EF-hand. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
PROSITEPS00019. 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]
ProtoNetSearch...

Other Resources

NextBio323.
SOURCESearch...

Entry information

Entry nameACTN1_HUMAN
AccessionPrimary (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: November 3, 2009
This is version 128 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM

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List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents