H9KV75 · H9KV75_HUMAN
- ProteinAlpha-actinin-1
- GeneACTN1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids822 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score3/5
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | actin cytoskeleton | |
Cellular Component | anchoring junction | |
Cellular Component | plasma membrane | |
Cellular Component | ruffle | |
Cellular Component | Z disc | |
Molecular Function | actin binding | |
Molecular Function | calcium ion binding |
Keywords
- Molecular function
- Ligand
Names & Taxonomy
Protein names
- Recommended nameAlpha-actinin-1
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionH9KV75
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
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.
Genetic variation databases
PTM/Processing
Features
Showing features for modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Modified residue (large scale data) | 26 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 107 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 128 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 165 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 181 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 185 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 275 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 283 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 291 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 339 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 357 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 359 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 361 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 363 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 377 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 406 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 643 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue (large scale data) | 644 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 689 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 820 | PRIDE | Phosphoserine | ||||
Sequence: S |
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.
Structure
Family & Domains
Features
Showing features for domain, coiled coil.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 1-70 | Calponin-homology (CH) | ||||
Sequence: MLLLEVISGERLAKPERGKMRVHKISNVNKALDFIASKGVKLVSIGAEEIVDGNVKMTLGMIWTIILRFA | ||||||
Domain | 79-185 | Calponin-homology (CH) | ||||
Sequence: TSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDVAEKYLDIPKMLDAEDIVGTARPDEKAIMTYVSSFYHAFS | ||||||
Coiled coil | 200-227 | |||||
Sequence: VLAVNQENEQLMEDYEKLASDLLEWIRR | ||||||
Coiled coil | 365-399 | |||||
Sequence: IKALLKKHEAFESDLAAHQDRVEQIAAIAQELNEL | ||||||
Domain | 681-716 | EF-hand | ||||
Sequence: EQMNEFRASFNHFDRKKTGMMDTDDFRACLISMGYN | ||||||
Domain | 717-752 | EF-hand | ||||
Sequence: MGEAEFARIMSIVDPNRLGVVTFQAFIDFMSRETAD |
Sequence similarities
Belongs to the alpha-actinin family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length822
- Mass (Da)94,826
- Last updated2012-05-16 v1
- ChecksumB50C56784497E8BE
Computationally mapped potential isoform sequences
There are 22 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
P12814 | ACTN1_HUMAN | ACTN1 | 892 | ||
H0YJW3 | H0YJW3_HUMAN | ACTN1 | 251 | ||
H0YJ11 | H0YJ11_HUMAN | ACTN1 | 207 | ||
G3V5M4 | G3V5M4_HUMAN | ACTN1 | 126 | ||
G3V2N5 | G3V2N5_HUMAN | ACTN1 | 260 | ||
G3V2W4 | G3V2W4_HUMAN | ACTN1 | 238 | ||
G3V2X9 | G3V2X9_HUMAN | ACTN1 | 144 | ||
G3V380 | G3V380_HUMAN | ACTN1 | 72 | ||
G3V2E8 | G3V2E8_HUMAN | ACTN1 | 85 | ||
A0A804HIN7 | A0A804HIN7_HUMAN | ACTN1 | 883 | ||
A0A804HIY0 | A0A804HIY0_HUMAN | ACTN1 | 152 | ||
A0A804HII9 | A0A804HII9_HUMAN | ACTN1 | 913 | ||
A0A804HLD0 | A0A804HLD0_HUMAN | ACTN1 | 903 | ||
A0A804HLF4 | A0A804HLF4_HUMAN | ACTN1 | 826 | ||
A0A804HJU8 | A0A804HJU8_HUMAN | ACTN1 | 874 | ||
A0A804HK61 | A0A804HK61_HUMAN | ACTN1 | 886 | ||
A0A804HJQ9 | A0A804HJQ9_HUMAN | ACTN1 | 268 | ||
A0A804HJN7 | A0A804HJN7_HUMAN | ACTN1 | 210 | ||
A0A804HL31 | A0A804HL31_HUMAN | ACTN1 | 827 | ||
H7C5W8 | H7C5W8_HUMAN | ACTN1 | 297 | ||
A0A804HKE2 | A0A804HKE2_HUMAN | ACTN1 | 922 | ||
A0A7I2V4Y4 | A0A7I2V4Y4_HUMAN | ACTN1 | 895 |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AL117694 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. |