Q99575 (POP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 107.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Ribonucleases P/MRP protein subunit POP1 Short name=hPOP1 EC=3.1.26.5 | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1024 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP. |
| Catalytic activity | Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor. |
| Subunit structure | RNase P consists of a RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. |
| Subcellular location | |
| Post-translational modification | Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 |
Ontologies
| Keywords | |
|---|---|
| Biological process | tRNA processing |
| Cellular component | Nucleus |
| Coding sequence diversity | Polymorphism |
| Molecular function | Hydrolase |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | tRNA 5'-leader removal Inferred from electronic annotation. Source: InterPro tRNA catabolic processInferred from direct assay Ref.3. Source: UniProtKB |
| Cellular component | nucleolar ribonuclease P complex Inferred from direct assay Ref.3. Source: UniProtKB ribonuclease MRP complexInferred from direct assay Ref.3. Source: UniProtKB |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct ribonuclease MRP activityInferred from direct assay Ref.3. Source: UniProtKB ribonuclease P activityInferred from direct assay Ref.3. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| POP4 | O95707 | 2 | EBI-366741,EBI-366477 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 1024 | 1024 | Ribonucleases P/MRP protein subunit POP1 | PRO_0000058513 | |||||
Amino acid modifications | |||||||||
| Modified residue | 40 | 1 | N6-acetyllysine Ref.13 | ||||||
| Modified residue | 46 | 1 | N6-acetyllysine Ref.13 | ||||||
| Modified residue | 365 | 1 | Phosphothreonine Ref.7 | ||||||
| Modified residue | 367 | 1 | Phosphoserine Ref.5 Ref.7 Ref.10 | ||||||
| Modified residue | 371 | 1 | Phosphoserine Ref.7 Ref.8 | ||||||
| Modified residue | 404 | 1 | Phosphothreonine Ref.6 | ||||||
| Modified residue | 584 | 1 | Phosphoserine Ref.7 | ||||||
| Modified residue | 730 | 1 | Phosphoserine Ref.5 Ref.9 Ref.10 Ref.11 Ref.12 | ||||||
Natural variations | |||||||||
| Natural variant | 127 | 1 | S → L. Corresponds to variant rs3824145 [ dbSNP | Ensembl ]. | VAR_057746 | |||||
| Natural variant | 460 | 1 | E → A. Corresponds to variant rs2306131 [ dbSNP | Ensembl ]. | VAR_057747 | |||||
| Natural variant | 522 | 1 | K → N. Corresponds to variant rs17184326 [ dbSNP | Ensembl ]. | VAR_057748 | |||||
| Natural variant | 675 | 1 | E → Q in a breast cancer sample; somatic mutation. Ref.15 | VAR_036232 | |||||
| Natural variant | 994 | 1 | L → V. Corresponds to variant rs17856355 [ dbSNP | Ensembl ]. | VAR_057749 | |||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. Sugano S.Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain. |
| [2] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | "hPop1: an autoantigenic protein subunit shared by the human RNase P and RNase MRP ribonucleoproteins." Lygerou Z., Pluk H., Van Venrooij W.J., Seraphin B. EMBO J. 15:5936-5948(1996) [PubMed: 8918471] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-126. |
| [4] | "Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed: 7584044] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-1024. Tissue: Bone marrow. |
| [5] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-730, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [6] | "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-404, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [7] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-365; SER-367; SER-371 AND SER-584, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [8] | "Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [9] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [10] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-367 AND SER-730, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [11] | "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [12] | "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [13] | "Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-40 AND LYS-46, MASS SPECTROMETRY. |
| [14] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| [15] | "The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. Velculescu V.E.Science 314:268-274(2006) [PubMed: 16959974] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-675. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AK291434 mRNA. Translation: BAF84123.1. CH471060 Genomic DNA. Translation: EAW91776.1. X99302 mRNA. Translation: CAA67684.1. D31765 mRNA. Translation: BAA06543.1. |
| IPI | IPI00293331. |
| RefSeq | NP_001139332.1. NM_001145860.1. NP_001139333.1. NM_001145861.1. NP_055844.2. NM_015029.2. |
| UniGene | Hs.252828. |
3D structure databases | |
| ProteinModelPortal | Q99575. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q99575. 10 interactions. |
| STRING | Q99575. |
PTM databases | |
| PhosphoSite | Q99575. |
Polymorphism databases | |
| DMDM | 13124451. |
Proteomic databases | |
| PeptideAtlas | Q99575. |
| PRIDE | Q99575. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000349693; ENSP00000339529; ENSG00000104356. ENST00000401707; ENSP00000385787; ENSG00000104356. |
| GeneID | 10940. |
| KEGG | hsa:10940. |
| NMPDR | fig|9606.3.peg.30577. |
| UCSC | uc003yij.2. human. |
Organism-specific databases | |
| CTD | 10940. |
| GeneCards | GC08P099129. |
| H-InvDB | HIX0007674. |
| HGNC | HGNC:30129. POP1. |
| MIM | 602486. gene. |
| neXtProt | NX_Q99575. |
| Orphanet | 93347. Anauxetic dysplasia. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG08782. |
| GeneTree | ENSGT00390000017478. |
| HOGENOM | HBG715929. |
| HOVERGEN | HBG008232. |
| InParanoid | Q99575. |
| OMA | AVGCGEA. |
| OrthoDB | EOG4F4S9F. |
| PhylomeDB | Q99575. |
Gene expression databases | |
| Bgee | Q99575. |
| CleanEx | HS_POP1. |
| Genevestigator | Q99575. |
| GermOnline | ENSG00000104356. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR012590. POPLD. IPR009723. RNase_P/MRP_POP1. [Graphical view] |
| KO | K01164. |
| Pfam | PF06978. POP1. 1 hit. PF08170. POPLD. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| SOURCE | Search... |
Entry information
| Entry name | POP1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q99575 Secondary accession number(s): A8K5W9, Q15037 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| 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. | ||||||||
Relevant documents
| Human chromosome 8 Human chromosome 8: entries, gene names and cross-references to MIM |
| Human entries with polymorphisms or disease mutations List of human entries with polymorphisms or disease mutations |
| Human polymorphisms and disease mutations Index of human polymorphisms and disease mutations |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |

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