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P12814 (ACTN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 175. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Alpha-actinin-1
Alternative name(s):
Alpha-actinin cytoskeletal isoform
F-actin cross-linking protein
Non-muscle alpha-actinin-1
Gene names
Name:ACTN1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length892 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. Interacts with DDN, MYOZ2, PDLIM2, TTID and LPP. Interacts with PSD. Interacts with MICALL2 By similarity. Ref.15 Ref.16 Ref.18 Ref.19

Subcellular location

Cytoplasmcytoskeleton. CytoplasmmyofibrilsarcomereZ line. Cell membrane By similarity. Cell junction By similarity. Cell projectionruffle By similarity. Note: Colocalizes with MYOZ2 and PPP3CA at the Z-line of heart and skeletal muscle. Colocalizes with PSD in membrane ruffles and central reticular structures By similarity. Ref.14

Involvement in disease

Bleeding disorder, platelet-type 15 (BDPLT15) [MIM:615193]: An autosomal dominant form of macrothrombocytopenia. Affected individuals usually have no or only mild bleeding tendency, such as epistaxis. Laboratory studies show decreased numbers of large platelets and anisocytosis, but the platelets show no in vitro functional abnormalities.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.24

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 componentCell junction
Cell membrane
Cell projection
Cytoplasm
Cytoskeleton
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainRepeat
   LigandActin-binding
Calcium
Metal-binding
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processactin filament bundle assembly

Inferred from electronic annotation. Source: Ensembl

blood coagulation

Traceable author statement. Source: Reactome

cell junction assembly

Traceable author statement. Source: Reactome

extracellular matrix organization

Traceable author statement. Source: Reactome

focal adhesion assembly

Inferred from mutant phenotype PubMed 16807302. Source: UniProtKB

negative regulation of cellular component movement

Inferred from mutant phenotype PubMed 7983147. Source: UniProtKB

platelet activation

Traceable author statement. Source: Reactome

platelet degranulation

Traceable author statement. Source: Reactome

regulation of apoptotic process

Non-traceable author statement PubMed 16807302. Source: UniProtKB

   Cellular_componentZ disc

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell projection

Inferred from direct assay Ref.19. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.19. Source: UniProtKB

cytoskeleton

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Traceable author statement. Source: Reactome

dendritic spine

Inferred from electronic annotation. Source: Ensembl

extracellular region

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

fascia adherens

Inferred from electronic annotation. Source: Ensembl

focal adhesion

Inferred from mutant phenotype PubMed 16807302. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

platelet alpha granule lumen

Traceable author statement. Source: Reactome

pseudopodium

Traceable author statement PubMed 1629252. Source: UniProtKB

ruffle

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

double-stranded RNA binding

Inferred from direct assay PubMed 21266579. Source: MGI

integrin binding

Inferred from direct assay PubMed 7983147. Source: UniProtKB

ion channel binding

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

vinculin binding

Inferred from physical interaction PubMed 15988023. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P279587EBI-351710,EBI-6904388From a different organism.
SRCP129312EBI-351710,EBI-621482
Ssx2ipQ8VC663EBI-351710,EBI-6654049From a different organism.
TTNQ8WZ422EBI-351710,EBI-681210

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P12814-1)

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.
Isoform 2 (identifier: P12814-2)

The sequence of this isoform differs from the canonical sequence as follows:
     761-787: DHSGTLGPEEFKACLISLGYDIGNDPQ → KKTGMMDTDDFRACLISMGYNM
Isoform 3 (identifier: P12814-3)

The sequence of this isoform differs from the canonical sequence as follows:
     787-787: Q → QKKTGMMDTDDFRACLISMGYNM
Isoform 4 (identifier: P12814-4)

The sequence of this isoform differs from the canonical sequence as follows:
     761-787: DHSGTLGPEEFKACLISLGYDIGNDPQ → KKTGMMDTDDFRACLISMGYNM
     840-840: K → KLQEGGKMQTAHAAFTPPGFAAVSGRAALRLLDFAAFLTTLSSQ

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 residue11N-acetylmethionine Ref.22
Modified residue61Phosphoserine Ref.22
Modified residue121Phosphotyrosine; by FAK1 Ref.17
Modified residue951N6-acetyllysine Ref.20
Modified residue1951N6-acetyllysine Ref.20
Modified residue6761N6-acetyllysine Ref.20

Natural variations

Alternative sequence761 – 78727DHSGT…GNDPQ → KKTGMMDTDDFRACLISMGY NM in isoform 2 and isoform 4.
VSP_041264
Alternative sequence7871Q → QKKTGMMDTDDFRACLISMG YNM in isoform 3.
VSP_043525
Alternative sequence8401K → KLQEGGKMQTAHAAFTPPGF AAVSGRAALRLLDFAAFLTT LSSQ in isoform 4.
VSP_047763
Natural variant321Q → K in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. Ref.24
VAR_069910
Natural variant461R → Q in BDPLT15. Ref.24
VAR_069911
Natural variant1051V → I in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. Ref.24
VAR_069912
Natural variant1971R → W. Ref.24
VAR_069913
Natural variant2251E → K in BDPLT15. Ref.24
VAR_069914
Natural variant7071N → T.
Corresponds to variant rs7157661 [ dbSNP | Ensembl ].
VAR_053883
Natural variant7381R → W in BDPLT15. Ref.24
VAR_069915
Natural variant7521R → Q in BDPLT15. Ref.24
VAR_069916
Natural variant8681T → S.
Corresponds to variant rs11557769 [ dbSNP | Ensembl ].
VAR_053884

Experimental info

Sequence conflict3171R → L in CAA38970. Ref.11
Sequence conflict3211R → H in BAG58135. Ref.7
Sequence conflict4241T → A in BAG58135. Ref.7
Sequence conflict4771Q → L in CAA38970. Ref.11
Sequence conflict630 – 6312RL → SV in CAA33803. Ref.1
Sequence conflict654 – 6563GRI → ARF in CAA38970. Ref.11
Sequence conflict6741Y → D in CAA38970. Ref.11
Sequence conflict7781L → S in CAA38970. Ref.11

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 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

Isoform 2 [UniParc].

Checksum: C478EDE4C896789A
Show »

FASTA887102,709
Isoform 3 [UniParc].

Checksum: 4E2865FA0CA56DC5
Show »

FASTA914105,569
Isoform 4 [UniParc].

Checksum: C8E56D242D05FFFC
Show »

FASTA930107,141

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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Alternative splicing in colon, bladder, and prostate cancer identified by exon array analysis."
Thorsen K., Sorensen K.D., Brems-Eskildsen A.S., Modin C., Gaustadnes M., Hein A.M., Kruhoffer M., Laurberg S., Borre M., Wang K., Brunak S., Krainer A.R., Torring N., Dyrskjot L., Andersen C.L., Orntoft T.F.
Mol. Cell. Proteomics 7:1214-1224(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"A new mRNA isoform from ACTN1 gene."
Mancini U.M., Tajara E.H.
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Tongue.
[5]"Actinin alpha 1 alternative splicing variant."
Mansilla F., Orntoft T.F., Birkenkamp-Demtroeder K.
Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
[6]"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] (ISOFORM 1).
[7]"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. expand/collapse author list , 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.
[8]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]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].
[10]"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: Colon and Skin.
[11]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 297-892 (ISOFORM 1).
[12]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-21.
Tissue: Platelet.
[13]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 134-146.
[14]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 566-577; 727-738 AND 835-863, SUBCELLULAR LOCATION.
[15]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TTID.
[16]"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 MYOZ2.
[17]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-12.
[18]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH LPP.
[19]"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] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH DDN.
[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.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-95; LYS-195 AND LYS-676, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]"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].
[22]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 30-253.
[24]"ACTN1 mutations cause congenital macrothrombocytopenia."
Kunishima S., Okuno Y., Yoshida K., Shiraishi Y., Sanada M., Muramatsu H., Chiba K., Tanaka H., Miyazaki K., Sakai M., Ohtake M., Kobayashi R., Iguchi A., Niimi G., Otsu M., Takahashi Y., Miyano S., Saito H., Kojima S., Ogawa S.
Am. J. Hum. Genet. 92:431-438(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BDPLT15 LYS-32; GLN-46; ILE-105; LYS-225; TRP-738 AND GLN-752, VARIANT TRP-197, CHARACTERIZATION OF VARIANTS BDPLT15 LYS-32 AND ILE-105.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X15804 mRNA. Translation: CAA33803.1.
M95178 mRNA. Translation: AAA51582.1.
EU716325 mRNA. Translation: ACE62922.1.
DQ496098 mRNA. Translation: ABF50047.1.
FJ410030 mRNA. Translation: ACJ24535.1.
BT007207 mRNA. Translation: AAP35871.1.
AK295099 mRNA. Translation: BAG58135.1.
AL117694 Genomic DNA. No translation available.
CH471061 Genomic DNA. Translation: EAW80975.1.
BC003576 mRNA. Translation: AAH03576.1.
BC015766 mRNA. Translation: AAH15766.1.
X55187 mRNA. Translation: CAA38970.1.
PIRFAHUAA. S05503.
RefSeqNP_001093.1. NM_001102.3.
NP_001123476.1. NM_001130004.1.
NP_001123477.1. NM_001130005.1.
UniGeneHs.509765.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2EYIX-ray1.70A30-253[»]
2EYNX-ray1.80A30-253[»]
ProteinModelPortalP12814.
SMRP12814. Positions 30-254, 267-892.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106602. 86 interactions.
DIPDIP-33184N.
IntActP12814. 36 interactions.
MINTMINT-215335.
STRING9606.ENSP00000377941.

PTM databases

PhosphoSiteP12814.

Polymorphism databases

DMDM46397817.

2D gel databases

OGPP12814.

Proteomic databases

PaxDbP12814.
PeptideAtlasP12814.
PRIDEP12814.

Protocols and materials databases

DNASU87.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000193403; ENSP00000193403; ENSG00000072110. [P12814-1]
ENST00000394419; ENSP00000377941; ENSG00000072110. [P12814-3]
ENST00000438964; ENSP00000414272; ENSG00000072110. [P12814-2]
ENST00000538545; ENSP00000439828; ENSG00000072110. [P12814-4]
GeneID87.
KEGGhsa:87.
UCSCuc001xkk.3. human. [P12814-1]
uc001xkm.3. human. [P12814-3]
uc001xkn.3. human. [P12814-2]

Organism-specific databases

CTD87.
GeneCardsGC14M069341.
HGNCHGNC:163. ACTN1.
HPACAB004303.
HPA006035.
MIM102575. gene.
615193. phenotype.
neXtProtNX_P12814.
Orphanet140957. Autosomal dominant macrothrombocytopenia.
PharmGKBPA24.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5069.
HOGENOMHOG000263418.
HOVERGENHBG050453.
KOK05699.
OMAWIRRTMP.
OrthoDBEOG72C4ZJ.
PhylomeDBP12814.
TreeFamTF352676.

Enzyme and pathway databases

ReactomeREACT_111155. Cell-Cell communication.
REACT_118779. Extracellular matrix organization.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpressP12814.
BgeeP12814.
CleanExHS_ACTN1.
GenevestigatorP12814.

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.
IPR018247. EF_Hand_1_Ca_BS.
IPR002048. EF_hand_dom.
IPR018159. Spectrin/alpha-actinin.
IPR002017. Spectrin_repeat.
[Graphical view]
PfamPF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
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.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSACTN1. human.
EvolutionaryTraceP12814.
GeneWikiActinin,_alpha_1.
GenomeRNAi87.
NextBio323.
PROP12814.
SOURCESearch...

Entry information

Entry nameACTN1_HUMAN
AccessionPrimary (citable) accession number: P12814
Secondary accession number(s): B3V8S3 expand/collapse secondary AC list , B4DHH3, B7TY16, Q1HE25, Q9BTN1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: April 13, 2004
Last modified: April 16, 2014
This is version 175 of the entry and version 2 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 14

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