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Protein

Alpha-actinin-1

Gene

ACTN1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
Calcium bindingi759 – 770PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi800 – 811PROSITE-ProRule annotationAdd BLAST12

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • calcium ion binding Source: InterPro
  • double-stranded RNA binding Source: MGI
  • integrin binding Source: UniProtKB
  • ion channel binding Source: UniProtKB
  • ligand-dependent nuclear receptor transcription coactivator activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • vinculin binding Source: UniProtKB

GO - Biological processi

  • actin crosslink formation Source: InterPro
  • actin filament bundle assembly Source: Ensembl
  • actin filament network formation Source: UniProtKB
  • actin filament organization Source: UniProtKB
  • focal adhesion assembly Source: UniProtKB
  • negative regulation of cellular component movement Source: UniProtKB
  • platelet degranulation Source: Reactome
  • platelet formation Source: UniProtKB
  • platelet morphogenesis Source: UniProtKB
  • regulation of apoptotic process Source: UniProtKB
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000072110-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-3000170. Syndecan interactions.
R-HSA-373753. Nephrin interactions.
R-HSA-446388. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
SIGNORiP12814.

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
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:163. ACTN1.

Subcellular locationi

GO - Cellular componenti

  • brush border Source: Ensembl
  • cell-cell junction Source: UniProtKB
  • cell projection Source: UniProtKB
  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular region Source: Reactome
  • extracellular space Source: UniProtKB
  • fascia adherens Source: Ensembl
  • focal adhesion Source: UniProtKB
  • intracellular Source: UniProtKB
  • plasma membrane Source: UniProtKB-SubCell
  • platelet alpha granule lumen Source: Reactome
  • pseudopodium Source: UniProtKB
  • ruffle Source: UniProtKB
  • stress fiber Source: UniProtKB
  • Z disc Source: UniProtKB-SubCell
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)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:615193
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06991032Q → K in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 PublicationCorresponds to variant rs387907346dbSNPEnsembl.1
Natural variantiVAR_06991146R → Q in BDPLT15; disorganization of the actin and alpha-actinin 1 filaments. 2 PublicationsCorresponds to variant rs387907348dbSNPEnsembl.1
Natural variantiVAR_069912105V → I in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 PublicationCorresponds to variant rs387907345dbSNPEnsembl.1
Natural variantiVAR_069914225E → K in BDPLT15. 1 PublicationCorresponds to variant rs387907350dbSNPEnsembl.1
Natural variantiVAR_069915738R → W in BDPLT15. 1 PublicationCorresponds to variant rs387907349dbSNPEnsembl.1
Natural variantiVAR_069916752R → Q in BDPLT15. 1 PublicationCorresponds to variant rs387907347dbSNPEnsembl.1

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi87.
MalaCardsiACTN1.
MIMi615193. phenotype.
OpenTargetsiENSG00000072110.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
PharmGKBiPA24.

Polymorphism and mutation databases

BioMutaiACTN1.
DMDMi46397817.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000734311 – 892Alpha-actinin-1Add BLAST892

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1
Modified residuei6PhosphoserineCombined sources1
Modified residuei12Phosphotyrosine; by FAK11 Publication1
Modified residuei95N6-acetyllysineCombined sources1
Modified residuei195N6-acetyllysineCombined sources1
Modified residuei471PhosphoserineCombined sources1
Modified residuei676N6-acetyllysineCombined sources1
Modified residuei677PhosphoserineCombined sources1
Modified residuei890PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP12814.
MaxQBiP12814.
PaxDbiP12814.
PeptideAtlasiP12814.
PRIDEiP12814.

2D gel databases

OGPiP12814.

PTM databases

iPTMnetiP12814.
PhosphoSitePlusiP12814.
SwissPalmiP12814.

Expressioni

Gene expression databases

BgeeiENSG00000072110.
CleanExiHS_ACTN1.
ExpressionAtlasiP12814. baseline and differential.
GenevisibleiP12814. HS.

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). Interacts with DNM2 and CTTN (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
B2R8Y43EBI-351710,EBI-10175581
P279587EBI-351710,EBI-6904388From a different organism.
ACTN3Q080434EBI-351710,EBI-2880652
EIF2S1P051984EBI-351710,EBI-1056162
EPM2AIP1Q7L7755EBI-351710,EBI-6255981
KCTD6Q8NC693EBI-351710,EBI-2511344
MICALL2Q8IY335EBI-351710,EBI-2555563
MYOZ1Q9NP983EBI-351710,EBI-744402
MYOZ2Q9NPC67EBI-351710,EBI-746712
OAS1P009733EBI-351710,EBI-3932815
SPERTQ8NA613EBI-351710,EBI-741724
SRCP129312EBI-351710,EBI-621482
Ssx2ipQ8VC663EBI-351710,EBI-6654049From a different organism.
TTNQ8WZ422EBI-351710,EBI-681210

GO - Molecular functioni

  • actin filament binding Source: UniProtKB
  • integrin binding Source: UniProtKB
  • ion channel binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • vinculin binding Source: UniProtKB

Protein-protein interaction databases

BioGridi106602. 126 interactors.
DIPiDIP-33184N.
IntActiP12814. 77 interactors.
MINTiMINT-215335.
STRINGi9606.ENSP00000377941.

Structurei

Secondary structure

1892
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi30 – 45Combined sources16
Helixi46 – 48Combined sources3
Turni55 – 61Combined sources7
Helixi63 – 73Combined sources11
Helixi86 – 102Combined sources17
Helixi112 – 116Combined sources5
Helixi120 – 135Combined sources16
Turni136 – 138Combined sources3
Helixi146 – 158Combined sources13
Beta strandi168 – 170Combined sources3
Helixi171 – 173Combined sources3
Helixi177 – 186Combined sources10
Helixi188 – 190Combined sources3
Helixi193 – 195Combined sources3
Helixi201 – 215Combined sources15
Helixi224 – 229Combined sources6
Beta strandi230 – 232Combined sources3
Helixi235 – 249Combined sources15
Helixi745 – 751Combined sources7
Helixi754 – 757Combined sources4
Beta strandi763 – 766Combined sources4
Helixi768 – 774Combined sources7
Helixi775 – 778Combined sources4
Helixi788 – 798Combined sources11
Beta strandi803 – 807Combined sources5
Helixi809 – 816Combined sources8
Helixi818 – 820Combined sources3
Helixi826 – 830Combined sources5
Helixi832 – 837Combined sources6
Beta strandi841 – 844Combined sources4
Helixi845 – 851Combined sources7
Helixi855 – 863Combined sources9
Beta strandi864 – 867Combined sources4
Beta strandi869 – 872Combined sources4
Beta strandi876 – 881Combined sources6
Turni884 – 888Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EYIX-ray1.70A30-253[»]
2EYNX-ray1.80A30-253[»]
2N8YNMR-A743-892[»]
2N8ZNMR-A743-892[»]
ProteinModelPortaliP12814.
SMRiP12814.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP12814.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 247Actin-bindingAdd BLAST247
Domaini31 – 135CH 1PROSITE-ProRule annotationAdd BLAST105
Domaini144 – 247CH 2PROSITE-ProRule annotationAdd BLAST104
Repeati274 – 384Spectrin 1Add BLAST111
Repeati394 – 499Spectrin 2Add BLAST106
Repeati509 – 620Spectrin 3Add BLAST112
Repeati630 – 733Spectrin 4Add BLAST104
Domaini746 – 781EF-hand 1PROSITE-ProRule annotationAdd BLAST36
Domaini787 – 822EF-hand 2PROSITE-ProRule annotationAdd BLAST36

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni274 – 733Interaction with DDN1 PublicationAdd BLAST460

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

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiP12814.
KOiK05699.
OMAiNDMTRKW.
OrthoDBiEOG091G020R.
PhylomeDBiP12814.
TreeFamiTF352676.

Family and domain databases

CDDicd00014. CH. 2 hits.
cd00051. EFh. 1 hit.
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.
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]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti317R → L in CAA38970 (PubMed:2169343).Curated1
Sequence conflicti321R → H in BAG58135 (PubMed:14702039).Curated1
Sequence conflicti424T → A in BAG58135 (PubMed:14702039).Curated1
Sequence conflicti477Q → L in CAA38970 (PubMed:2169343).Curated1
Sequence conflicti630 – 631RL → SV in CAA33803 (PubMed:2780298).Curated2
Sequence conflicti654 – 656GRI → ARF in CAA38970 (PubMed:2169343).Curated3
Sequence conflicti674Y → D in CAA38970 (PubMed:2169343).Curated1
Sequence conflicti778L → S in CAA38970 (PubMed:2169343).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_06991032Q → K in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 PublicationCorresponds to variant rs387907346dbSNPEnsembl.1
Natural variantiVAR_06991146R → Q in BDPLT15; disorganization of the actin and alpha-actinin 1 filaments. 2 PublicationsCorresponds to variant rs387907348dbSNPEnsembl.1
Natural variantiVAR_069912105V → I in BDPLT15; the mutation dominantly affects the actin filament assembly likely resulting in abnormal cytoskeletal organization. 1 PublicationCorresponds to variant rs387907345dbSNPEnsembl.1
Natural variantiVAR_069913197R → W.1 Publication1
Natural variantiVAR_069914225E → K in BDPLT15. 1 PublicationCorresponds to variant rs387907350dbSNPEnsembl.1
Natural variantiVAR_053883707N → T.Corresponds to variant rs7157661dbSNPEnsembl.1
Natural variantiVAR_069915738R → W in BDPLT15. 1 PublicationCorresponds to variant rs387907349dbSNPEnsembl.1
Natural variantiVAR_069916752R → Q in BDPLT15. 1 PublicationCorresponds to variant rs387907347dbSNPEnsembl.1
Natural variantiVAR_053884868T → S.Corresponds to variant rs11557769dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_041264761 – 787DHSGT…GNDPQ → KKTGMMDTDDFRACLISMGY NM in isoform 2 and isoform 4. 3 PublicationsAdd BLAST27
Alternative sequenceiVSP_043525787Q → QKKTGMMDTDDFRACLISMG YNM in isoform 3. 1 Publication1
Alternative sequenceiVSP_047763840K → KLQEGGKMQTAHAAFTPPGF AAVSGRAALRLLDFAAFLTT LSSQ in isoform 4. 1 Publication1

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.235750.
Hs.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.
UCSCiuc001xkl.4. human. [P12814-1]

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.
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.235750.
Hs.509765.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2EYIX-ray1.70A30-253[»]
2EYNX-ray1.80A30-253[»]
2N8YNMR-A743-892[»]
2N8ZNMR-A743-892[»]
ProteinModelPortaliP12814.
SMRiP12814.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106602. 126 interactors.
DIPiDIP-33184N.
IntActiP12814. 77 interactors.
MINTiMINT-215335.
STRINGi9606.ENSP00000377941.

PTM databases

iPTMnetiP12814.
PhosphoSitePlusiP12814.
SwissPalmiP12814.

Polymorphism and mutation databases

BioMutaiACTN1.
DMDMi46397817.

2D gel databases

OGPiP12814.

Proteomic databases

EPDiP12814.
MaxQBiP12814.
PaxDbiP12814.
PeptideAtlasiP12814.
PRIDEiP12814.

Protocols and materials databases

DNASUi87.
Structural Biology KnowledgebaseSearch...

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.
UCSCiuc001xkl.4. human. [P12814-1]

Organism-specific databases

CTDi87.
DisGeNETi87.
GeneCardsiACTN1.
HGNCiHGNC:163. ACTN1.
HPAiCAB004303.
HPA006035.
MalaCardsiACTN1.
MIMi102575. gene.
615193. phenotype.
neXtProtiNX_P12814.
OpenTargetsiENSG00000072110.
Orphaneti140957. Autosomal dominant macrothrombocytopenia.
PharmGKBiPA24.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0035. Eukaryota.
COG5069. LUCA.
GeneTreeiENSGT00760000118813.
HOGENOMiHOG000263418.
HOVERGENiHBG050453.
InParanoidiP12814.
KOiK05699.
OMAiNDMTRKW.
OrthoDBiEOG091G020R.
PhylomeDBiP12814.
TreeFamiTF352676.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000072110-MONOMER.
ReactomeiR-HSA-114608. Platelet degranulation.
R-HSA-3000170. Syndecan interactions.
R-HSA-373753. Nephrin interactions.
R-HSA-446388. Regulation of cytoskeletal remodeling and cell spreading by IPP complex components.
SIGNORiP12814.

Miscellaneous databases

ChiTaRSiACTN1. human.
EvolutionaryTraceiP12814.
GeneWikiiActinin,_alpha_1.
GenomeRNAii87.
PROiP12814.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000072110.
CleanExiHS_ACTN1.
ExpressionAtlasiP12814. baseline and differential.
GenevisibleiP12814. HS.

Family and domain databases

CDDicd00014. CH. 2 hits.
cd00051. EFh. 1 hit.
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.
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]
SUPFAMiSSF47473. SSF47473. 1 hit.
SSF47576. 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]
ProtoNetiSearch...

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 30, 2016
This is version 205 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.