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P12814

- ACTN1_HUMAN

UniProt

P12814 - ACTN1_HUMAN

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Protein

Alpha-actinin-1

Gene

ACTN1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi759 – 77012PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi800 – 81112PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. double-stranded RNA binding Source: MGI
  3. integrin binding Source: UniProtKB
  4. ion channel binding Source: BHF-UCL
  5. vinculin binding Source: UniProtKB

GO - Biological processi

  1. actin crosslink formation Source: InterPro
  2. actin filament bundle assembly Source: Ensembl
  3. blood coagulation Source: Reactome
  4. cell junction assembly Source: Reactome
  5. extracellular matrix organization Source: Reactome
  6. focal adhesion assembly Source: UniProtKB
  7. negative regulation of cellular component movement Source: UniProtKB
  8. platelet activation Source: Reactome
  9. platelet degranulation Source: Reactome
  10. regulation of apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_163942. Syndecan interactions.
REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_23832. Nephrin interactions.

Names & Taxonomyi

Protein namesi
Recommended name:
Alpha-actinin-1
Alternative name(s):
Alpha-actinin cytoskeletal isoform
F-actin cross-linking protein
Non-muscle alpha-actinin-1
Gene namesi
Name:ACTN1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:163. ACTN1.

Subcellular locationi

Cytoplasmcytoskeleton 1 Publication. CytoplasmmyofibrilsarcomereZ line 1 Publication. 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).By similarity

GO - Cellular componenti

  1. cell projection Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. cytoskeleton Source: UniProtKB-KW
  4. cytosol Source: Reactome
  5. dendritic spine Source: Ensembl
  6. extracellular region Source: Reactome
  7. extracellular space Source: UniProt
  8. extracellular vesicular exosome Source: UniProtKB
  9. fascia adherens Source: Ensembl
  10. focal adhesion Source: UniProtKB
  11. nucleus Source: Ensembl
  12. plasma membrane Source: UniProtKB-KW
  13. platelet alpha granule lumen Source: Reactome
  14. pseudopodium Source: UniProtKB
  15. Z disc Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321Q → K in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 Publication
VAR_069910
Natural varianti46 – 461R → Q in BDPLT15. 1 Publication
VAR_069911
Natural varianti105 – 1051V → I in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 Publication
VAR_069912
Natural varianti225 – 2251E → K in BDPLT15. 1 Publication
VAR_069914
Natural varianti738 – 7381R → W in BDPLT15. 1 Publication
VAR_069915
Natural varianti752 – 7521R → Q in BDPLT15. 1 Publication
VAR_069916

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615193. phenotype.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
PharmGKBiPA24.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 892892Alpha-actinin-1PRO_0000073431Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei6 – 61Phosphoserine1 Publication
Modified residuei12 – 121Phosphotyrosine; by FAK11 Publication
Modified residuei95 – 951N6-acetyllysine1 Publication
Modified residuei195 – 1951N6-acetyllysine1 Publication
Modified residuei676 – 6761N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP12814.
PaxDbiP12814.
PeptideAtlasiP12814.
PRIDEiP12814.

2D gel databases

OGPiP12814.

PTM databases

PhosphoSiteiP12814.

Expressioni

Gene expression databases

BgeeiP12814.
CleanExiHS_ACTN1.
ExpressionAtlasiP12814. baseline and differential.
GenevestigatoriP12814.

Organism-specific databases

HPAiCAB004303.
HPA006035.

Interactioni

Subunit structurei

Homodimer; antiparallel. Interacts with DDN, MYOZ2, PDLIM2, TTID and LPP. Interacts with PSD. Interacts with MICALL2 (By similarity).By similarity

Binary interactionsi

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

Protein-protein interaction databases

BioGridi106602. 90 interactions.
DIPiDIP-33184N.
IntActiP12814. 41 interactions.
MINTiMINT-215335.
STRINGi9606.ENSP00000377941.

Structurei

Secondary structure

1
892
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi30 – 4516Combined sources
Helixi46 – 483Combined sources
Turni55 – 617Combined sources
Helixi63 – 7311Combined sources
Helixi86 – 10217Combined sources
Helixi112 – 1165Combined sources
Helixi120 – 13516Combined sources
Turni136 – 1383Combined sources
Helixi146 – 15813Combined sources
Beta strandi168 – 1703Combined sources
Helixi171 – 1733Combined sources
Helixi177 – 18610Combined sources
Helixi188 – 1903Combined sources
Helixi193 – 1953Combined sources
Helixi201 – 21515Combined sources
Helixi224 – 2296Combined sources
Beta strandi230 – 2323Combined sources
Helixi235 – 24915Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2EYIX-ray1.70A30-253[»]
2EYNX-ray1.80A30-253[»]
ProteinModelPortaliP12814.
SMRiP12814. Positions 30-254, 267-892.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12814.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 247247Actin-bindingAdd
BLAST
Domaini31 – 135105CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini144 – 247104CH 2PROSITE-ProRule annotationAdd
BLAST
Repeati274 – 384111Spectrin 1Add
BLAST
Repeati394 – 499106Spectrin 2Add
BLAST
Repeati509 – 620112Spectrin 3Add
BLAST
Repeati630 – 733104Spectrin 4Add
BLAST
Domaini746 – 78136EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini787 – 82236EF-hand 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni274 – 733460Interaction with DDNAdd
BLAST

Sequence similaritiesi

Belongs to the alpha-actinin family.Curated
Contains 1 actin-binding domain.Curated
Contains 2 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation
Contains 4 spectrin repeats.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiCOG5069.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiP12814.
KOiK05699.
OMAiWIRRTMP.
OrthoDBiEOG72C4ZJ.
PhylomeDBiP12814.
TreeFamiTF352676.

Family and domain databases

Gene3Di1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR026921. Alpha-actinin_1.
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]
PANTHERiPTHR11915:SF241. PTHR11915:SF241. 1 hit.
PfamiPF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view]
SUPFAMiSSF47576. SSF47576. 1 hit.
PROSITEiPS00019. 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]

Sequences (4)i

Sequence statusi: Complete.

This entry describes 4 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P12814-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDHYDSQQTN DYMQPEEDWD RDLLLDPAWE KQQRKTFTAW CNSHLRKAGT
60 70 80 90 100
QIENIEEDFR DGLKLMLLLE VISGERLAKP ERGKMRVHKI SNVNKALDFI
110 120 130 140 150
ASKGVKLVSI GAEEIVDGNV KMTLGMIWTI ILRFAIQDIS VEETSAKEGL
160 170 180 190 200
LLWCQRKTAP YKNVNIQNFH ISWKDGLGFC ALIHRHRPEL IDYGKLRKDD
210 220 230 240 250
PLTNLNTAFD VAEKYLDIPK MLDAEDIVGT ARPDEKAIMT YVSSFYHAFS
260 270 280 290 300
GAQKAETAAN RICKVLAVNQ ENEQLMEDYE KLASDLLEWI RRTIPWLENR
310 320 330 340 350
VPENTMHAMQ QKLEDFRDYR RLHKPPKVQE KCQLEINFNT LQTKLRLSNR
360 370 380 390 400
PAFMPSEGRM VSDINNAWGC LEQVEKGYEE WLLNEIRRLE RLDHLAEKFR
410 420 430 440 450
QKASIHEAWT DGKEAMLRQK DYETATLSEI KALLKKHEAF ESDLAAHQDR
460 470 480 490 500
VEQIAAIAQE LNELDYYDSP SVNARCQKIC DQWDNLGALT QKRREALERT
510 520 530 540 550
EKLLETIDQL YLEYAKRAAP FNNWMEGAME DLQDTFIVHT IEEIQGLTTA
560 570 580 590 600
HEQFKATLPD ADKERLAILG IHNEVSKIVQ TYHVNMAGTN PYTTITPQEI
610 620 630 640 650
NGKWDHVRQL VPRRDQALTE EHARQQHNER LRKQFGAQAN VIGPWIQTKM
660 670 680 690 700
EEIGRISIEM HGTLEDQLSH LRQYEKSIVN YKPKIDQLEG DHQLIQEALI
710 720 730 740 750
FDNKHTNYTM EHIRVGWEQL LTTIARTINE VENQILTRDA KGISQEQMNE
760 770 780 790 800
FRASFNHFDR DHSGTLGPEE FKACLISLGY DIGNDPQGEA EFARIMSIVD
810 820 830 840 850
PNRLGVVTFQ AFIDFMSRET ADTDTADQVM ASFKILAGDK NYITMDELRR
860 870 880 890
ELPPDQAEYC IARMAPYTGP DSVPGALDYM SFSTALYGES DL
Length:892
Mass (Da):103,058
Last modified:April 13, 2004 - v2
Checksum:i6DA3E4D1A0289519
GO
Isoform 2 (identifier: P12814-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:887
Mass (Da):102,709
Checksum:iC478EDE4C896789A
GO
Isoform 3 (identifier: P12814-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     787-787: Q → QKKTGMMDTDDFRACLISMGYNM

Show »
Length:914
Mass (Da):105,569
Checksum:i4E2865FA0CA56DC5
GO
Isoform 4 (identifier: P12814-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:930
Mass (Da):107,141
Checksum:iC8E56D242D05FFFC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti317 – 3171R → L in CAA38970. (PubMed:2169343)Curated
Sequence conflicti321 – 3211R → H in BAG58135. (PubMed:14702039)Curated
Sequence conflicti424 – 4241T → A in BAG58135. (PubMed:14702039)Curated
Sequence conflicti477 – 4771Q → L in CAA38970. (PubMed:2169343)Curated
Sequence conflicti630 – 6312RL → SV in CAA33803. (PubMed:2780298)Curated
Sequence conflicti654 – 6563GRI → ARF in CAA38970. (PubMed:2169343)Curated
Sequence conflicti674 – 6741Y → D in CAA38970. (PubMed:2169343)Curated
Sequence conflicti778 – 7781L → S in CAA38970. (PubMed:2169343)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti32 – 321Q → K in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 Publication
VAR_069910
Natural varianti46 – 461R → Q in BDPLT15. 1 Publication
VAR_069911
Natural varianti105 – 1051V → I in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 Publication
VAR_069912
Natural varianti197 – 1971R → W.1 Publication
VAR_069913
Natural varianti225 – 2251E → K in BDPLT15. 1 Publication
VAR_069914
Natural varianti707 – 7071N → T.
Corresponds to variant rs7157661 [ dbSNP | Ensembl ].
VAR_053883
Natural varianti738 – 7381R → W in BDPLT15. 1 Publication
VAR_069915
Natural varianti752 – 7521R → Q in BDPLT15. 1 Publication
VAR_069916
Natural varianti868 – 8681T → S.
Corresponds to variant rs11557769 [ dbSNP | Ensembl ].
VAR_053884

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei761 – 78727DHSGT…GNDPQ → KKTGMMDTDDFRACLISMGY NM in isoform 2 and isoform 4. 3 PublicationsVSP_041264Add
BLAST
Alternative sequencei787 – 7871Q → QKKTGMMDTDDFRACLISMG YNM in isoform 3. 1 PublicationVSP_043525
Alternative sequencei840 – 8401K → KLQEGGKMQTAHAAFTPPGF AAVSGRAALRLLDFAAFLTT LSSQ in isoform 4. 1 PublicationVSP_047763

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS45129.1. [P12814-2]
CCDS45130.1. [P12814-3]
CCDS9792.1. [P12814-1]
PIRiS05503. FAHUAA.
RefSeqiNP_001093.1. NM_001102.3. [P12814-1]
NP_001123476.1. NM_001130004.1. [P12814-3]
NP_001123477.1. NM_001130005.1. [P12814-2]
UniGeneiHs.509765.

Genome annotation databases

EnsembliENST00000193403; ENSP00000193403; ENSG00000072110. [P12814-1]
ENST00000394419; ENSP00000377941; ENSG00000072110. [P12814-3]
ENST00000438964; ENSP00000414272; ENSG00000072110. [P12814-2]
ENST00000538545; ENSP00000439828; ENSG00000072110. [P12814-4]
GeneIDi87.
KEGGihsa:87.
UCSCiuc001xkk.3. human. [P12814-1]
uc001xkm.3. human. [P12814-3]
uc001xkn.3. human. [P12814-2]

Polymorphism databases

DMDMi46397817.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS45129.1. [P12814-2 ]
CCDS45130.1. [P12814-3 ]
CCDS9792.1. [P12814-1 ]
PIRi S05503. FAHUAA.
RefSeqi NP_001093.1. NM_001102.3. [P12814-1 ]
NP_001123476.1. NM_001130004.1. [P12814-3 ]
NP_001123477.1. NM_001130005.1. [P12814-2 ]
UniGenei Hs.509765.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2EYI X-ray 1.70 A 30-253 [» ]
2EYN X-ray 1.80 A 30-253 [» ]
ProteinModelPortali P12814.
SMRi P12814. Positions 30-254, 267-892.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106602. 90 interactions.
DIPi DIP-33184N.
IntActi P12814. 41 interactions.
MINTi MINT-215335.
STRINGi 9606.ENSP00000377941.

PTM databases

PhosphoSitei P12814.

Polymorphism databases

DMDMi 46397817.

2D gel databases

OGPi P12814.

Proteomic databases

MaxQBi P12814.
PaxDbi P12814.
PeptideAtlasi P12814.
PRIDEi P12814.

Protocols and materials databases

DNASUi 87.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000193403 ; ENSP00000193403 ; ENSG00000072110 . [P12814-1 ]
ENST00000394419 ; ENSP00000377941 ; ENSG00000072110 . [P12814-3 ]
ENST00000438964 ; ENSP00000414272 ; ENSG00000072110 . [P12814-2 ]
ENST00000538545 ; ENSP00000439828 ; ENSG00000072110 . [P12814-4 ]
GeneIDi 87.
KEGGi hsa:87.
UCSCi uc001xkk.3. human. [P12814-1 ]
uc001xkm.3. human. [P12814-3 ]
uc001xkn.3. human. [P12814-2 ]

Organism-specific databases

CTDi 87.
GeneCardsi GC14M069341.
HGNCi HGNC:163. ACTN1.
HPAi CAB004303.
HPA006035.
MIMi 102575. gene.
615193. phenotype.
neXtProti NX_P12814.
Orphaneti 140957. Autosomal dominant macrothrombocytopenia.
PharmGKBi PA24.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5069.
GeneTreei ENSGT00760000118813.
HOGENOMi HOG000263418.
HOVERGENi HBG050453.
InParanoidi P12814.
KOi K05699.
OMAi WIRRTMP.
OrthoDBi EOG72C4ZJ.
PhylomeDBi P12814.
TreeFami TF352676.

Enzyme and pathway databases

Reactomei REACT_163942. Syndecan interactions.
REACT_20580. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
REACT_23832. Nephrin interactions.

Miscellaneous databases

ChiTaRSi ACTN1. human.
EvolutionaryTracei P12814.
GeneWikii Actinin,_alpha_1.
GenomeRNAii 87.
NextBioi 323.
PROi P12814.
SOURCEi Search...

Gene expression databases

Bgeei P12814.
CleanExi HS_ACTN1.
ExpressionAtlasi P12814. baseline and differential.
Genevestigatori P12814.

Family and domain databases

Gene3Di 1.10.238.10. 2 hits.
1.10.418.10. 2 hits.
InterProi IPR001589. Actinin_actin-bd_CS.
IPR026921. Alpha-actinin_1.
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 ]
PANTHERi PTHR11915:SF241. PTHR11915:SF241. 1 hit.
Pfami PF00307. CH. 2 hits.
PF13405. EF-hand_6. 1 hit.
PF08726. EFhand_Ca_insen. 1 hit.
PF00435. Spectrin. 4 hits.
[Graphical view ]
SMARTi SM00033. CH. 2 hits.
SM00054. EFh. 2 hits.
SM00150. SPEC. 3 hits.
[Graphical view ]
SUPFAMi SSF47576. SSF47576. 1 hit.
PROSITEi 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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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. 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.
    , 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.
    , 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. 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. 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. 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.

Entry informationi

Entry nameiACTN1_HUMAN
AccessioniPrimary (citable) accession number: P12814
Secondary accession number(s): B3V8S3
, B4DHH3, B7TY16, Q1HE25, Q9BTN1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: April 13, 2004
Last modified: November 26, 2014
This is version 182 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3