H9KV75 · H9KV75_HUMAN

  • Protein
    Alpha-actinin-1
  • Gene
    ACTN1
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    3/5

Function

function

F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. Association with IGSF8 regulates the immune synapse formation and is required for efficient T-cell activation.

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentactin cytoskeleton
Cellular Componentanchoring junction
Cellular Componentplasma membrane
Cellular Componentruffle
Cellular ComponentZ disc
Molecular Functionactin binding
Molecular Functioncalcium ion binding

Keywords

Names & Taxonomy

Protein names

  • Recommended name
    Alpha-actinin-1
  • Alternative names
    • Alpha-actinin cytoskeletal isoform
    • F-actin cross-linking protein
    • Non-muscle alpha-actinin-1

Gene names

    • Name
      ACTN1

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    H9KV75

Proteomes

Organism-specific databases

Subcellular Location

Keywords

Disease & Variants

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 249 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Genetic variation databases

PTM/Processing

Features

Showing features for modified residue (large scale data).

TypeIDPosition(s)SourceDescription
Modified residue (large scale data)26PRIDEPhosphoserine
Modified residue (large scale data)37PRIDEPhosphoserine
Modified residue (large scale data)75PRIDEPhosphoserine
Modified residue (large scale data)107PRIDEPhosphoserine
Modified residue (large scale data)128PRIDEPhosphotyrosine
Modified residue (large scale data)165PRIDEPhosphothreonine
Modified residue (large scale data)181PRIDEPhosphotyrosine
Modified residue (large scale data)185PRIDEPhosphoserine
Modified residue (large scale data)275PRIDEPhosphothreonine
Modified residue (large scale data)283PRIDEPhosphoserine
Modified residue (large scale data)291PRIDEPhosphoserine
Modified residue (large scale data)339PRIDEPhosphoserine
Modified residue (large scale data)357PRIDEPhosphotyrosine
Modified residue (large scale data)359PRIDEPhosphothreonine
Modified residue (large scale data)361PRIDEPhosphothreonine
Modified residue (large scale data)363PRIDEPhosphoserine
Modified residue (large scale data)377PRIDEPhosphoserine
Modified residue (large scale data)406PRIDEPhosphoserine
Modified residue (large scale data)643PRIDEPhosphotyrosine
Modified residue (large scale data)644PRIDEPhosphothreonine
Modified residue (large scale data)689PRIDEPhosphoserine
Modified residue (large scale data)820PRIDEPhosphoserine

Expression

Gene expression databases

Interaction

Subunit

Homodimer; antiparallel. Interacts with MYOZ2, TTID and LPP. Interacts with DDN. Interacts with PSD. Interacts with MICALL2. Interacts with DNM2 and CTTN. Interacts with PDLIM1. Interacts with PDLIM2. Interacts with PDLIM4 (via PDZ domain). Interacts with IGSF8.

Family & Domains

Features

Showing features for domain, coiled coil.

TypeIDPosition(s)Description
Domain1-70Calponin-homology (CH)
Domain79-185Calponin-homology (CH)
Coiled coil200-227
Coiled coil365-399
Domain681-716EF-hand
Domain717-752EF-hand

Sequence similarities

Belongs to the alpha-actinin family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    822
  • Mass (Da)
    94,826
  • Last updated
    2012-05-16 v1
  • Checksum
    B50C56784497E8BE
MLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFAIQDISVEETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFSGAQKAETAANRICKVLAVNQENEQLMEDYEKLASDLLEWIRRTIPWLENRVPENTMHAMQQKLEDFRDYRRLHKPPKVQEKCQLEINFNTLQTKLRLSNRPAFMPSEGRMVSDINNAWGCLEQVEKGYEEWLLNEIRRLERLDHLAEKFRQKASIHEAWTDGKEAMLRQKDYETATLSEIKALLKKHEAFESDLAAHQDRVEQIAAIAQELNELDYYDSPSVNARCQKICDQWDNLGALTQKRREALERTEKLLETIDQLYLEYAKRAAPFNNWMEGAMEDLQDTFIVHTIEEIQGLTTAHEQFKATLPDADKERLAILGIHNEVSKIVQTYHVNMAGTNPYTTITPQEINGKWDHVRQLVPRRDQALTEEHARQQHNERLRKQFGAQANVIGPWIQTKMEEIGRISIEMHGTLEDQLSHLRQYEKSIVNYKPKIDQLEGDHQLIQEALIFDNKHTNYTMEHIRVGWEQLLTTIARTINEVENQILTRDAKGISQEQMNEFRASFNHFDRKKTGMMDTDDFRACLISMGYNMGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETADTDTADQVMASFKILAGDKNYITMDELRRELPPDQAEYCIARMAPYTGPDSVPGALDYMSFSTALYGESDL

Computationally mapped potential isoform sequences

There are 22 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
P12814ACTN1_HUMANACTN1892
H0YJW3H0YJW3_HUMANACTN1251
H0YJ11H0YJ11_HUMANACTN1207
G3V5M4G3V5M4_HUMANACTN1126
G3V2N5G3V2N5_HUMANACTN1260
G3V2W4G3V2W4_HUMANACTN1238
G3V2X9G3V2X9_HUMANACTN1144
G3V380G3V380_HUMANACTN172
G3V2E8G3V2E8_HUMANACTN185
A0A804HIN7A0A804HIN7_HUMANACTN1883
A0A804HIY0A0A804HIY0_HUMANACTN1152
A0A804HII9A0A804HII9_HUMANACTN1913
A0A804HLD0A0A804HLD0_HUMANACTN1903
A0A804HLF4A0A804HLF4_HUMANACTN1826
A0A804HJU8A0A804HJU8_HUMANACTN1874
A0A804HK61A0A804HK61_HUMANACTN1886
A0A804HJQ9A0A804HJQ9_HUMANACTN1268
A0A804HJN7A0A804HJN7_HUMANACTN1210
A0A804HL31A0A804HL31_HUMANACTN1827
H7C5W8H7C5W8_HUMANACTN1297
A0A804HKE2A0A804HKE2_HUMANACTN1922
A0A7I2V4Y4A0A7I2V4Y4_HUMANACTN1895

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL117694
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.

Genome annotation databases

Similar Proteins

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. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp