Q99575 · POP1_HUMAN
- ProteinRibonucleases P/MRP protein subunit POP1
- GenePOP1
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1024 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
Component of ribonuclease P, a ribonucleoprotein complex that generates mature tRNA molecules by cleaving their 5'-ends (PubMed:30454648, PubMed:8918471).
Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465).
Also a component of the MRP ribonuclease complex, which cleaves pre-rRNA sequences (PubMed:28115465).
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 | extracellular space | |
Cellular Component | multimeric ribonuclease P complex | |
Cellular Component | nucleolar ribonuclease P complex | |
Cellular Component | nucleolus | |
Cellular Component | nucleoplasm | |
Cellular Component | ribonuclease MRP complex | |
Molecular Function | ribonuclease P activity | |
Molecular Function | ribonuclease P RNA binding | |
Molecular Function | RNA binding | |
Biological Process | tRNA 5'-leader removal | |
Biological Process | tRNA decay | |
Biological Process | tRNA processing |
Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameRibonucleases P/MRP protein subunit POP1
- Short nameshPOP1
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ99575
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Involvement in disease
Anauxetic dysplasia 2 (ANXD2)
- Note
- DescriptionAn autosomal recessive spondyloepimetaphyseal dysplasia characterized by severe short stature of prenatal onset, very short adult height (less than 1 meter), hypodontia, midface hypoplasia, and mild intellectual disability.
- See alsoMIM:617396
Natural variants in ANXD2
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_078770 | 511 | D>Y | in ANXD2; dbSNP:rs1060505025 | |
VAR_078771 | 582 | P>S | in ANXD2; dbSNP:rs1060505023 | |
VAR_067755 | 583 | G>E | in ANXD2; dbSNP:rs374828868 |
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | VAR_057746 | 127 | in dbSNP:rs3824145 | |||
Sequence: S → L | ||||||
Natural variant | VAR_057747 | 460 | in dbSNP:rs2306131 | |||
Sequence: E → A | ||||||
Natural variant | VAR_078770 | 511 | in ANXD2; dbSNP:rs1060505025 | |||
Sequence: D → Y | ||||||
Natural variant | VAR_057748 | 522 | in dbSNP:rs17184326 | |||
Sequence: K → N | ||||||
Natural variant | VAR_078771 | 582 | in ANXD2; dbSNP:rs1060505023 | |||
Sequence: P → S | ||||||
Natural variant | VAR_067755 | 583 | in ANXD2; dbSNP:rs374828868 | |||
Sequence: G → E | ||||||
Natural variant | VAR_036232 | 675 | in a breast cancer sample; somatic mutation | |||
Sequence: E → Q | ||||||
Natural variant | VAR_057749 | 994 | in dbSNP:rs17856355 | |||
Sequence: L → V |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1,216 variants from UniProt as well as other sources including ClinVar and dbSNP.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000058513 | 1-1024 | UniProt | Ribonucleases P/MRP protein subunit POP1 | |||
Sequence: MSNAKERKHAKKMRNQPTNVTLSSGFVADRGVKHHSGGEKPFQAQKQEPHPGTSRQRQTRVNPHSLPDPEVNEQSSSKGMFRKKGGWKAGPEGTSQEIPKYITASTFAQARAAEISAMLKAVTQKSSNSLVFQTLPRHMRRRAMSHNVKRLPRRLQEIAQKEAEKAVHQKKEHSKNKCHKARRCHMNRTLEFNRRQKKNIWLETHIWHAKRFHMVKKWGYCLGERPTVKSHRACYRAMTNRCLLQDLSYYCCLELKGKEEEILKALSGMCNIDTGLTFAAVHCLSGKRQGSLVLYRVNKYPREMLGPVTFIWKSQRTPGDPSESRQLWIWLHPTLKQDILEEIKAACQCVEPIKSAVCIADPLPTPSQEKSQTELPDEKIGKKRKRKDDGENAKPIKKIIGDGTRDPCLPYSWISPTTGIIISDLTMEMNRFRLIGPLSHSILTEAIKAASVHTVGEDTEETPHRWWIETCKKPDSVSLHCRQEAIFELLGGITSPAEIPAGTILGLTVGDPRINLPQKKSKALPNPEKCQDNEKVRQLLLEGVPVECTHSFIWNQDICKSVTENKISDQDLNRMRSELLVPGSQLILGPHESKIPILLIQQPGKVTGEDRLGWGSGWDVLLPKGWGMAFWIPFIYRGVRVGGLKESAVHSQYKRSPNVPGDFPDCPAGMLFAEEQAKNLLEKYKRRPPAKRPNYVKLGTLAPFCCPWEQLTQDWESRVQAYEEPSVASSPNGKESDLRRSEVPCAPMPKKTHQPSDEVGTSIEHPREAEEVMDAGCQESAGPERITDQEASENHVAATGSHLCVLRSRKLLKQLSAWCGPSSEDSRGGRRAPGRGQQGLTREACLSILGHFPRALVWVSLSLLSKGSPEPHTMICVPAKEDFLQLHEDWHYCGPQESKHSDPFRSKILKQKEKKKREKRQKPGRASSDGPAGEEPVAGQEALTLGLWSGPLPRVTLHCSRTLLGFVTQGDFSMAVGCGEALGFVSLTGLLDMLSSQPAAQRGLVLLRPPASLQYRFARIAIEV | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 65 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 75 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 95 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 365 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 367 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 367 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 371 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 373 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 584 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 584 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 726 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 729 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 729 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 730 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 730 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 736 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 761 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 762 | PRIDE | Phosphoserine | ||||
Sequence: S |
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Interaction
Subunit
Component of nuclear RNase P and RNase MRP ribonucleoproteins (PubMed:16723659, PubMed:8918471).
RNase P consists of a catalytic RNA moiety and 10 different protein chains; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and RPP40 (PubMed:16723659, PubMed:30454648).
Within the RNase P complex, POP1, POP7 and RPP25 form the 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form the 'palm' subcomplex, and RPP21, POP4 and RPP38 form the 'wrist' subcomplex. All subunits of the RNase P complex interact with the catalytic RNA (PubMed:30454648).
Several subunits of RNase P are also part of the RNase MRP complex. RNase MRP consists of a catalytic RNA moiety and about 8 protein subunits; POP1, POP7, RPP25, RPP30, RPP38, RPP40 and possibly also POP4 and POP5 (PubMed:16723659, PubMed:28115465).
RNase P consists of a catalytic RNA moiety and 10 different protein chains; POP1, POP4, POP5, POP7, RPP14, RPP21, RPP25, RPP30, RPP38 and RPP40 (PubMed:16723659, PubMed:30454648).
Within the RNase P complex, POP1, POP7 and RPP25 form the 'finger' subcomplex, POP5, RPP14, RPP40 and homodimeric RPP30 form the 'palm' subcomplex, and RPP21, POP4 and RPP38 form the 'wrist' subcomplex. All subunits of the RNase P complex interact with the catalytic RNA (PubMed:30454648).
Several subunits of RNase P are also part of the RNase MRP complex. RNase MRP consists of a catalytic RNA moiety and about 8 protein subunits; POP1, POP7, RPP25, RPP30, RPP38, RPP40 and possibly also POP4 and POP5 (PubMed:16723659, PubMed:28115465).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | Q99575 | POP4 O95707 | 5 | EBI-366741, EBI-366477 | |
BINARY | Q99575 | POP5 Q969H6 | 3 | EBI-366741, EBI-366525 | |
BINARY | Q99575 | RPP25 Q9BUL9 | 4 | EBI-366741, EBI-366570 |
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-95 | Disordered | ||||
Sequence: MSNAKERKHAKKMRNQPTNVTLSSGFVADRGVKHHSGGEKPFQAQKQEPHPGTSRQRQTRVNPHSLPDPEVNEQSSSKGMFRKKGGWKAGPEGTS | ||||||
Compositional bias | 47-79 | Polar residues | ||||
Sequence: QEPHPGTSRQRQTRVNPHSLPDPEVNEQSSSKG | ||||||
Region | 365-399 | Disordered | ||||
Sequence: TPSQEKSQTELPDEKIGKKRKRKDDGENAKPIKKI | ||||||
Compositional bias | 372-399 | Basic and acidic residues | ||||
Sequence: QTELPDEKIGKKRKRKDDGENAKPIKKI | ||||||
Region | 722-762 | Disordered | ||||
Sequence: YEEPSVASSPNGKESDLRRSEVPCAPMPKKTHQPSDEVGTS | ||||||
Region | 773-792 | Disordered | ||||
Sequence: MDAGCQESAGPERITDQEAS | ||||||
Region | 819-838 | Disordered | ||||
Sequence: CGPSSEDSRGGRRAPGRGQQ | ||||||
Region | 911-936 | Disordered | ||||
Sequence: QKEKKKREKRQKPGRASSDGPAGEEP |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,024
- Mass (Da)114,709
- Last updated2001-02-21 v2
- ChecksumA1DB872F3B940C02
Computationally mapped potential isoform sequences
There is 1 potential isoform mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E5RK39 | E5RK39_HUMAN | POP1 | 183 |
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 47-79 | Polar residues | ||||
Sequence: QEPHPGTSRQRQTRVNPHSLPDPEVNEQSSSKG | ||||||
Compositional bias | 372-399 | Basic and acidic residues | ||||
Sequence: QTELPDEKIGKKRKRKDDGENAKPIKKI |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK291434 EMBL· GenBank· DDBJ | BAF84123.1 EMBL· GenBank· DDBJ | mRNA | ||
CH471060 EMBL· GenBank· DDBJ | EAW91776.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X99302 EMBL· GenBank· DDBJ | CAA67684.1 EMBL· GenBank· DDBJ | mRNA | ||
D31765 EMBL· GenBank· DDBJ | BAA06543.1 EMBL· GenBank· DDBJ | mRNA |