P01252 · PTMA_BOVIN
- ProteinProthymosin alpha
- GenePTMA
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids110 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Prothymosin alpha may mediate immune function by conferring resistance to certain opportunistic infections.
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 | |||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | nucleoplasm | |
Cellular Component | nucleus | |
Molecular Function | DNA-binding transcription factor binding | |
Molecular Function | histone binding | |
Biological Process | negative regulation of apoptotic process | |
Biological Process | positive regulation of transcription by RNA polymerase II |
Names & Taxonomy
Protein names
- Recommended nameProthymosin alpha
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Laurasiatheria > Artiodactyla > Ruminantia > Pecora > Bovidae > Bovinae > Bos
Accessions
- Primary accessionP01252
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for initiator methionine, modified residue, chain, peptide, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Initiator methionine | 1 | Removed; alternate | ||||
Sequence: M | ||||||
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000423254 | 1-110 | Prothymosin alpha | |||
Sequence: MSDAAVDTSSEITTKDLKEKKEVVEEAENGREAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAATGKRAAEDDEDDDVDTKKQKTDEDD | ||||||
Modified residue | 2 | N-acetylserine; in Prothymosin alpha, N-terminally processed | ||||
Sequence: S | ||||||
Modified residue | 2 | Phosphoserine | ||||
Sequence: S | ||||||
Peptide | PRO_0000029864 | 2-29 | Thymosin alpha-1 | |||
Sequence: SDAAVDTSSEITTKDLKEKKEVVEEAEN | ||||||
Chain | PRO_0000299249 | 2-110 | Prothymosin alpha, N-terminally processed | |||
Sequence: SDAAVDTSSEITTKDLKEKKEVVEEAENGREAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAATGKRAAEDDEDDDVDTKKQKTDEDD | ||||||
Modified residue | 8 | Phosphothreonine; by CK2 | ||||
Sequence: T | ||||||
Modified residue | 9 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 10 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 13 | Phosphothreonine; by CK2 | ||||
Sequence: T | ||||||
Modified residue | 14 | Phosphothreonine; by CK2 | ||||
Sequence: T | ||||||
Modified residue | 15 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 15 | N6-succinyllysine; alternate | ||||
Sequence: K | ||||||
Modified residue | 101 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 102 | N6-acetyllysine; alternate | ||||
Sequence: K | ||||||
Cross-link | 102 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternate | ||||
Sequence: K | ||||||
Modified residue | 106 | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Covalently linked to a small RNA of about 20 nucleotides.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Gene expression databases
Interaction
Subunit
Interacts with NUPR1; regulates apoptotic process.
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-110 | Disordered | ||||
Sequence: MSDAAVDTSSEITTKDLKEKKEVVEEAENGREAPANGNANEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAATGKRAAEDDEDDDVDTKKQKTDEDD | ||||||
Compositional bias | 12-29 | Basic and acidic residues | ||||
Sequence: ITTKDLKEKKEVVEEAEN | ||||||
Compositional bias | 44-81 | Acidic residues | ||||
Sequence: GEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEE | ||||||
Compositional bias | 82-110 | Basic and acidic residues | ||||
Sequence: AEAATGKRAAEDDEDDDVDTKKQKTDEDD |
Sequence similarities
Belongs to the pro/parathymosin family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length110
- Mass (Da)12,072
- Last updated2007-09-11 v2
- Checksum51078AE43B9308D7
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 12-29 | Basic and acidic residues | ||||
Sequence: ITTKDLKEKKEVVEEAEN | ||||||
Compositional bias | 44-81 | Acidic residues | ||||
Sequence: GEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEE | ||||||
Compositional bias | 82-110 | Basic and acidic residues | ||||
Sequence: AEAATGKRAAEDDEDDDVDTKKQKTDEDD |
Keywords
- Technical term