Q6PGN9 · PSRC1_HUMAN
- ProteinProline/serine-rich coiled-coil protein 1
- GenePSRC1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids363 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Required for normal progression through mitosis. Required for normal congress of chromosomes at the metaphase plate, and for normal rate of chromosomal segregation during anaphase. Plays a role in the regulation of mitotic spindle dynamics. Increases the rate of turnover of microtubules on metaphase spindles, and contributes to the generation of normal tension across sister kinetochores. Recruits KIF2A and ANKRD53 to the mitotic spindle and spindle poles. May participate in p53/TP53-regulated growth suppression.
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 | cytoplasm | |
Cellular Component | cytosol | |
Cellular Component | microtubule cytoskeleton | |
Cellular Component | midbody | |
Cellular Component | nucleoplasm | |
Cellular Component | spindle | |
Cellular Component | spindle pole | |
Molecular Function | microtubule binding | |
Biological Process | cell division | |
Biological Process | microtubule bundle formation | |
Biological Process | mitotic metaphase chromosome alignment | |
Biological Process | negative regulation of cell growth | |
Biological Process | positive regulation of cyclin-dependent protein serine/threonine kinase activity | |
Biological Process | positive regulation of DNA-templated transcription | |
Biological Process | positive regulation of microtubule polymerization | |
Biological Process | regulation of mitotic spindle organization |
Keywords
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameProline/serine-rich coiled-coil protein 1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ6PGN9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Detected at the mitotic spindle and spindle poles. Diffusely distributed throughout the cell during interphase.
Keywords
- Cellular component
Disease & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_051288 | 312 | in dbSNP:rs34863121 | |||
Sequence: R → Q |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 437 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data).
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000273728 | 1-363 | UniProt | Proline/serine-rich coiled-coil protein 1 | |||
Sequence: MEDLEEDVRFIVDETLDFGGLSPSDSREEEDITVLVTPEKPLRRGLSHRSDPNAVAPAPQGVRLSLGPLSPEKLEEILDEANRLAAQLEQCALQDRESAGEGLGPRRVKPSPRRETFVLKDSPVRDLLPTVNSLTRSTPSPSSLTPRLRSNDRKGSVRALRATSGKRPSNMKRESPTCNLFPASKSPASSPLTRSTPPVRGRAGPSGRAAASEETRAAKLRVSGSGEFVGLTLKFLHPSPPGPPTPIRSVLAPQPSTSNSQRLPRPQGAAAKSSSQLPIPSAIPRPASRMPLTSRSVPPGRGALPPDSLSTRKGLPRPSTAGHRVRESGHKVPVSQRLNLPVMGATRSNLQPPRKVAVPGPTR | |||||||
Modified residue | 22 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 22 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 42 | UniProt | In isoform Q6PGN9-4; Phosphoserine | ||||
Sequence: L | |||||||
Modified residue | 45 | UniProt | In isoform Q6PGN9-4; Phosphothreonine | ||||
Sequence: G | |||||||
Modified residue | 47 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 47 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 50 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 65 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 70 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 70 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 98 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 98 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 122 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 122 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 133 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 140 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 145 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 175 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 186 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 186 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 190 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 190 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 212 | UniProt | In isoform Q6PGN9-2; Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 215 | UniProt | In isoform Q6PGN9-2; Phosphothreonine | ||||
Sequence: T |
Post-translational modification
Phosphorylated during mitosis.
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Widely expressed in adult and fetal tissues, with highest expression in the adult brain and fetal thymus. Not detected in adult skeletal muscle.
Gene expression databases
Organism-specific databases
Interaction
Subunit
Interacts with APC2 (By similarity).
Interacts with KIF2A (PubMed:18411309).
Interacts with ANKRD53; recruits ANKRD53 to the spindle during mitosis (PubMed:26820536).
Interacts with KIF2A (PubMed:18411309).
Interacts with ANKRD53; recruits ANKRD53 to the spindle during mitosis (PubMed:26820536).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q6PGN9 | MAPRE3 Q9UPY8 | 3 | EBI-7392664, EBI-726739 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for repeat, region, coiled coil, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Repeat | 38-41 | 1 | ||||
Sequence: PEKP | ||||||
Region | 39-67 | Disordered | ||||
Sequence: EKPLRRGLSHRSDPNAVAPAPQGVRLSLG | ||||||
Repeat | 68-71 | 2 | ||||
Sequence: PLSP | ||||||
Coiled coil | 70-94 | |||||
Sequence: SPEKLEEILDEANRLAAQLEQCALQ | ||||||
Region | 95-363 | Disordered | ||||
Sequence: DRESAGEGLGPRRVKPSPRRETFVLKDSPVRDLLPTVNSLTRSTPSPSSLTPRLRSNDRKGSVRALRATSGKRPSNMKRESPTCNLFPASKSPASSPLTRSTPPVRGRAGPSGRAAASEETRAAKLRVSGSGEFVGLTLKFLHPSPPGPPTPIRSVLAPQPSTSNSQRLPRPQGAAAKSSSQLPIPSAIPRPASRMPLTSRSVPPGRGALPPDSLSTRKGLPRPSTAGHRVRESGHKVPVSQRLNLPVMGATRSNLQPPRKVAVPGPTR | ||||||
Compositional bias | 100-121 | Basic and acidic residues | ||||
Sequence: GEGLGPRRVKPSPRRETFVLKD | ||||||
Region | 103-246 | 4 X 4 AA repeats of P-X-X-P | ||||
Sequence: LGPRRVKPSPRRETFVLKDSPVRDLLPTVNSLTRSTPSPSSLTPRLRSNDRKGSVRALRATSGKRPSNMKRESPTCNLFPASKSPASSPLTRSTPPVRGRAGPSGRAAASEETRAAKLRVSGSGEFVGLTLKFLHPSPPGPPTP | ||||||
Compositional bias | 128-150 | Polar residues | ||||
Sequence: LPTVNSLTRSTPSPSSLTPRLRS | ||||||
Compositional bias | 169-196 | Polar residues | ||||
Sequence: SNMKRESPTCNLFPASKSPASSPLTRST | ||||||
Repeat | 238-241 | 3 | ||||
Sequence: PSPP | ||||||
Repeat | 243-246 | 4 | ||||
Sequence: PPTP | ||||||
Compositional bias | 251-281 | Polar residues | ||||
Sequence: LAPQPSTSNSQRLPRPQGAAAKSSSQLPIPS |
Sequence similarities
Belongs to the PSRC1 family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 4 isoforms produced by Alternative splicing.
Q6PGN9-1
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.
- NameC
- Length363
- Mass (Da)38,796
- Last updated2004-07-05 v1
- Checksum4B59C01EB74F3B72
Q6PGN9-2
- NameA
- Differences from canonical
- 213-242: Missing
Q6PGN9-3
- NameB
Q6PGN9-4
- NameD
Computationally mapped potential isoform sequences
There are 3 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_022602 | 1-170 | in isoform D | |||
Sequence: Missing | ||||||
Compositional bias | 100-121 | Basic and acidic residues | ||||
Sequence: GEGLGPRRVKPSPRRETFVLKD | ||||||
Compositional bias | 128-150 | Polar residues | ||||
Sequence: LPTVNSLTRSTPSPSSLTPRLRS | ||||||
Compositional bias | 169-196 | Polar residues | ||||
Sequence: SNMKRESPTCNLFPASKSPASSPLTRST | ||||||
Alternative sequence | VSP_022591 | 213-242 | in isoform A and isoform D | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_022592 | 222-310 | in isoform B | |||
Sequence: VSGSGEFVGLTLKFLHPSPPGPPTPIRSVLAPQPSTSNSQRLPRPQGAAAKSSSQLPIPSAIPRPASRMPLTSRSVPPGRGALPPDSLS → ACQPNATHQPECATWQRCPTSGFSVNSKRASKTKHCRTQSAGKWTQGSCFPATKSSCHGCHSQQSAAPQESGSPRTYQVKRSGQQARLQ | ||||||
Compositional bias | 251-281 | Polar residues | ||||
Sequence: LAPQPSTSNSQRLPRPQGAAAKSSSQLPIPS | ||||||
Alternative sequence | VSP_022593 | 311-363 | in isoform B | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF223000 EMBL· GenBank· DDBJ | AAN73431.1 EMBL· GenBank· DDBJ | mRNA | ||
AF322891 EMBL· GenBank· DDBJ | AAN73434.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AK126567 EMBL· GenBank· DDBJ | BAC86599.1 EMBL· GenBank· DDBJ | mRNA | ||
AF447874 EMBL· GenBank· DDBJ | AAQ04649.1 EMBL· GenBank· DDBJ | mRNA | ||
AL390252 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471122 EMBL· GenBank· DDBJ | EAW56373.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC056909 EMBL· GenBank· DDBJ | AAH56909.1 EMBL· GenBank· DDBJ | mRNA |