P12814 (ACTN1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	892 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. Interacts with DDN, MYOZ2, PDLIM2, TTID and LPP. Interacts with PSD By similarity. Ref.12 Ref.13 Ref.15 Ref.18
Subcellular location	Cytoplasm › cytoskeleton. Cytoplasm › myofibril › sarcomere › Z line. Cell membrane By similarity. Cell projection › ruffle 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.11
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	Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat
Ligand	Actin-binding Calcium
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	focal adhesion assembly Inferred from mutant phenotype. Source: UniProtKB negative regulation of cellular component movement Inferred from mutant phenotype. Source: UniProtKB platelet activation Traceable author statement. Source: Reactome platelet degranulation Traceable author statement. Source: Reactome regulation of apoptotic process Non-traceable author statement. Source: UniProtKB
Cellular component	Z disc Inferred from electronic annotation. Source: UniProtKB-SubCell cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Traceable author statement. Source: Reactome extracellular region Traceable author statement. Source: Reactome focal adhesion Inferred from mutant phenotype. Source: UniProtKB platelet alpha granule lumen Traceable author statement. Source: Reactome pseudopodium Traceable author statement. Source: UniProtKB ruffle Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	actin binding Inferred from electronic annotation. Source: UniProtKB-KW calcium ion binding Inferred from electronic annotation. Source: InterPro integrin binding Inferred from direct assay. Source: UniProtKB vinculin binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SRC	P12931	2	EBI-351710,EBI-621482

Alternative products

This entry describes 2 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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 892

892

Alpha-actinin-1

PRO_0000073431

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

Region

274 – 733

460

Interaction with DDN

Amino acid modifications

Modified residue

12

1

Phosphotyrosine; by FAK1 Ref.14

Modified residue

50

1

Phosphothreonine Ref.16

Modified residue

95

1

N6-acetyllysine Ref.22

Modified residue

140

1

Phosphoserine Ref.17 Ref.20

Modified residue

193

1

Phosphotyrosine Ref.19

Modified residue

195

1

N6-acetyllysine Ref.22

Modified residue

246

1

Phosphotyrosine Ref.21

Modified residue

676

1

N6-acetyllysine Ref.22

Natural variations

Alternative sequence

761 – 787

27

DHSGT…GNDPQ → KKTGMMDTDDFRACLISMGY NM in isoform 2.

VSP_041264

Natural variant

707

1

N → T.
Corresponds to variant rs7157661 [ dbSNP | Ensembl ].

VAR_053883

Natural variant

868

1

T → S.
Corresponds to variant rs11557769 [ dbSNP | Ensembl ].

VAR_053884

Experimental info

Sequence conflict

317

1

R → L in CAA38970. Ref.8

Sequence conflict

321

1

R → H in BAG58135. Ref.5

Sequence conflict

424

1

T → A in BAG58135. Ref.5

Sequence conflict

477

1

Q → L in CAA38970. Ref.8

Sequence conflict

630 – 631

2

RL → SV in CAA33803. Ref.1

Sequence conflict

654 – 656

3

GRI → ARF in CAA38970. Ref.8

Sequence conflict

674

1

Y → D in CAA38970. Ref.8

Sequence conflict

778

1

L → S in CAA38970. Ref.8

Secondary structure

1

.

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892

Helix Strand Turn

Details...

Helix

30 – 45

16

Helix

46 – 48

3

Turn

55 – 61

7

Helix

63 – 73

11

Helix

86 – 102

17

Helix

112 – 116

5

Helix

120 – 135

16

Turn

136 – 138

3

Helix

146 – 158

13

Beta strand

168 – 170

3

Helix

171 – 173

3

Helix

177 – 186

10

Helix

188 – 190

3

Helix

193 – 195

3

Helix

201 – 215

15

Helix

224 – 229

6

Beta strand

230 – 232

3

Helix

235 – 249

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 13, 2004. Version 2. Checksum: 6DA3E4D1A0289519	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
	Isoform 2 [UniParc]. Checksum: C478EDE4C896789A	FASTA	887	102,709
	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 KKTGMMDTDD FRACLISMGY 790 800 810 820 830 840 NMGEAEFARI MSIVDPNRLG VVTFQAFIDF MSRETADTDT ADQVMASFKI LAGDKNYITM 850 860 870 880 DELRRELPPD QAEYCIARMA PYTGPDSVPG ALDYMSFSTA LYGESDL

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] (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: 2349951] [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: 18353764] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]	"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).
[5]	"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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain.
[6]	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].
[7]	"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.
[8]	"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 (ISOFORM 1).
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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: Hepatoma.
[17]	"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: Cervix carcinoma.
[18]	"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.
[19]	"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. , 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. Tissue: Lung carcinoma.
[20]	"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. Tissue: Cervix carcinoma.
[21]	"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.
[22]	"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.
[23]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"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

EMBL
GenBank
DDBJ

X15804 mRNA. Translation: CAA33803.1.
M95178 mRNA. Translation: AAA51582.1.
EU716325 mRNA. Translation: ACE62922.1.
BT007207 mRNA. Translation: AAP35871.1.
AK295099 mRNA. Translation: BAG58135.1.
CH471061 Genomic DNA. Translation: EAW80975.1.
BC003576 mRNA. Translation: AAH03576.1.
BC015766 mRNA. Translation: AAH15766.1.
X55187 mRNA. Translation: CAA38970.1.

IPI

IPI00013508.
IPI00909239.

PIR

FAHUAA. S05503.

RefSeq

NP_001093.1. NM_001102.3.
NP_001123477.1. NM_001130005.1.

UniGene

Hs.509765.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2EYI	X-ray	1.70	A	30-253	[»]
2EYN	X-ray	1.80	A	30-253	[»]

ProteinModelPortal

P12814.

SMR

P12814. Positions 30-254, 267-739, 742-892.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-33184N.

IntAct

P12814. 28 interactions.

MINT

MINT-215335.

STRING

P12814.

PTM databases

PhosphoSite

P12814.

Polymorphism databases

DMDM

46397817.

2D gel databases

OGP

P12814.

Proteomic databases

PeptideAtlas

P12814.

PRIDE

P12814.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000193403; ENSP00000193403; ENSG00000072110.

GeneID

87.

KEGG

hsa:87.

UCSC

uc001xkl.1. human.

Organism-specific databases

CTD

87.

GeneCards

GC14M069341.

H-InvDB

HIX0011761.

HGNC

HGNC:163. ACTN1.

HPA

CAB004303.
HPA006035.

MIM

102575. gene.

neXtProt

NX_P12814.

PharmGKB

PA24.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

HBG050453.

OrthoDB

EOG49P9XR.

PhylomeDB

P12814.

Enzyme and pathway databases

Pathway_Interaction_DB

syndecan_4_pathway. Syndecan-4-mediated signaling events.

Reactome

REACT_111155. Cell-Cell communication.
REACT_604. Hemostasis.

Gene expression databases

ArrayExpress

P12814.

Bgee

P12814.

CleanEx

HS_ACTN1.

Genevestigator

P12814.

GermOnline

ENSG00000072110. Homo sapiens.

Family and domain databases

InterPro

IPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-like_dom.
IPR014837. EF-hand_Ca_insen.
IPR018247. EF_Hand_1_Ca_BS.
IPR018249. EF_HAND_2.
IPR002048. EF_hand_Ca-bd.
IPR018159. Spectrin/alpha-actinin.
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.

KO

K05699.

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.
PS00018. EF_HAND_1. 1 hit.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

ProtoNet

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Other

NextBio

323.

SOURCE

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Entry information

Entry name

ACTN1_HUMAN

Accession

Primary (citable) accession number: P12814
Secondary accession number(s): B3V8S3, B4DHH3, Q9BTN1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1989
Last sequence update:	April 13, 2004
Last modified:	January 25, 2012
This is version 152 of the entry and version 2 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.