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Q969H6

- POP5_HUMAN

UniProt

Q969H6 - POP5_HUMAN

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Protein

Ribonuclease P/MRP protein subunit POP5

Gene
POP5, AD-008, HSPC004, x0003
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP.1 Publication

Catalytic activityi

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.1 Publication

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. ribonuclease P activity Source: UniProtKB-EC

GO - Biological processi

  1. tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P/MRP protein subunit POP5 (EC:3.1.26.5)
Short name:
hPop5
Gene namesi
Name:POP5
ORF Names:AD-008, HSPC004, x0003
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:17689. POP5.

Subcellular locationi

GO - Cellular componenti

  1. nucleolar ribonuclease P complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA128394660.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 163163Ribonuclease P/MRP protein subunit POP5PRO_0000239007Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei154 – 1541Phosphoserine4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ969H6.
PaxDbiQ969H6.
PRIDEiQ969H6.

PTM databases

PhosphoSiteiQ969H6.

Expressioni

Gene expression databases

BgeeiQ969H6.
CleanExiHS_POP5.
GenevestigatoriQ969H6.

Organism-specific databases

HPAiHPA047598.

Interactioni

Subunit structurei

Component of nuclear RNase P and RNase MRP ribonucleoproteins. RNase P consists of an RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RNase MRP consists of an RNA moiety and at least 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38, RPP40, POP5 and RPP21.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
POP4O957072EBI-366525,EBI-366477

Protein-protein interaction databases

BioGridi119502. 4 interactions.
IntActiQ969H6. 4 interactions.
STRINGi9606.ENSP00000350098.

Structurei

3D structure databases

ProteinModelPortaliQ969H6.
SMRiQ969H6. Positions 1-119.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG284693.
HOGENOMiHOG000293345.
HOVERGENiHBG082157.
InParanoidiQ969H6.
KOiK03537.
OMAiCEVVSDD.
OrthoDBiEOG7GTT69.
PhylomeDBiQ969H6.
TreeFamiTF317496.

Family and domain databases

InterProiIPR016819. RNase_P/MRP_POP5.
IPR002759. RNase_P/MRP_subunit.
[Graphical view]
PfamiPF01900. RNase_P_Rpp14. 1 hit.
[Graphical view]
PIRSFiPIRSF023803. Ribonuclease_P_prd. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q969H6-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MVRFKHRYLL CELVSDDPRC RLSLDDRVLS SLVRDTIARV HGTFGAAACS    50
IGFAVRYLNA YTGIVLLRCR KEFYQLVWSA LPFITYLENK GHRYPCFFNT 100
LHVGGTIRTC QKFLIQYNRR QLLILLQNCT DEGEREAIQK SVTRSCLLEE 150
EEESGEEAAE AME 163
Length:163
Mass (Da):18,820
Last modified:December 1, 2001 - v1
Checksum:iDF436E60B3DD50C1
GO
Isoform 2 (identifier: Q969H6-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     55-104: Missing.

Note: No experimental confirmation available.

Show »
Length:113
Mass (Da):12,826
Checksum:i1004F004EBE8E949
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei55 – 10450Missing in isoform 2. VSP_042733Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 482AA → P in AAF17213. 1 Publication
Sequence conflicti47 – 482AA → P in AAD20966. 1 Publication
Sequence conflicti99 – 991N → D in BAD96926. 1 Publication
Sequence conflicti102 – 1021H → R in BAD96926. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ306296 mRNA. Translation: CAC59822.1.
AF117232 mRNA. Translation: AAF17213.1.
AF070660 mRNA. Translation: AAD20966.1.
AK303144 mRNA. Translation: BAG64248.1.
AK223206 mRNA. Translation: BAD96926.1.
AC063943 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98206.1.
BC012505 mRNA. Translation: AAH12505.1.
CCDSiCCDS9202.1. [Q969H6-1]
CCDS9203.1. [Q969H6-2]
RefSeqiNP_057002.2. NM_015918.3. [Q969H6-1]
NP_937845.1. NM_198202.1. [Q969H6-2]
UniGeneiHs.279913.

Genome annotation databases

EnsembliENST00000341039; ENSP00000341791; ENSG00000167272. [Q969H6-2]
ENST00000357500; ENSP00000350098; ENSG00000167272. [Q969H6-1]
GeneIDi51367.
KEGGihsa:51367.
UCSCiuc001tys.3. human. [Q969H6-1]
uc001tyt.3. human. [Q969H6-2]

Polymorphism databases

DMDMi74731042.

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ306296 mRNA. Translation: CAC59822.1 .
AF117232 mRNA. Translation: AAF17213.1 .
AF070660 mRNA. Translation: AAD20966.1 .
AK303144 mRNA. Translation: BAG64248.1 .
AK223206 mRNA. Translation: BAD96926.1 .
AC063943 Genomic DNA. No translation available.
CH471054 Genomic DNA. Translation: EAW98206.1 .
BC012505 mRNA. Translation: AAH12505.1 .
CCDSi CCDS9202.1. [Q969H6-1 ]
CCDS9203.1. [Q969H6-2 ]
RefSeqi NP_057002.2. NM_015918.3. [Q969H6-1 ]
NP_937845.1. NM_198202.1. [Q969H6-2 ]
UniGenei Hs.279913.

3D structure databases

ProteinModelPortali Q969H6.
SMRi Q969H6. Positions 1-119.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119502. 4 interactions.
IntActi Q969H6. 4 interactions.
STRINGi 9606.ENSP00000350098.

PTM databases

PhosphoSitei Q969H6.

Polymorphism databases

DMDMi 74731042.

Proteomic databases

MaxQBi Q969H6.
PaxDbi Q969H6.
PRIDEi Q969H6.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341039 ; ENSP00000341791 ; ENSG00000167272 . [Q969H6-2 ]
ENST00000357500 ; ENSP00000350098 ; ENSG00000167272 . [Q969H6-1 ]
GeneIDi 51367.
KEGGi hsa:51367.
UCSCi uc001tys.3. human. [Q969H6-1 ]
uc001tyt.3. human. [Q969H6-2 ]

Organism-specific databases

CTDi 51367.
GeneCardsi GC12M121016.
HGNCi HGNC:17689. POP5.
HPAi HPA047598.
MIMi 609992. gene.
neXtProti NX_Q969H6.
PharmGKBi PA128394660.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG284693.
HOGENOMi HOG000293345.
HOVERGENi HBG082157.
InParanoidi Q969H6.
KOi K03537.
OMAi CEVVSDD.
OrthoDBi EOG7GTT69.
PhylomeDBi Q969H6.
TreeFami TF317496.

Miscellaneous databases

GeneWikii POP5.
GenomeRNAii 51367.
NextBioi 54841.
PROi Q969H6.
SOURCEi Search...

Gene expression databases

Bgeei Q969H6.
CleanExi HS_POP5.
Genevestigatori Q969H6.

Family and domain databases

InterProi IPR016819. RNase_P/MRP_POP5.
IPR002759. RNase_P/MRP_subunit.
[Graphical view ]
Pfami PF01900. RNase_P_Rpp14. 1 hit.
[Graphical view ]
PIRSFi PIRSF023803. Ribonuclease_P_prd. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "hPop5, a protein subunit of the human RNase MRP and RNase P endoribonucleases."
    van Eenennaam H., Lugtenberg D., Vogelzangs J.H.P., van Venrooij W.J., Pruijn G.J.M.
    J. Biol. Chem. 276:31635-31641(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, SUBUNIT.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  3. "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells."
    Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G., Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W., Tao J., Huang Q.-H., Zhou J., Hu G.-X.
    , Gu J., Chen S.-J., Chen Z.
    Genome Res. 10:1546-1560(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Umbilical cord blood.
  4. "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.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Thymus.
  5. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney proximal tubule.
  6. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Mammary gland.
  9. "Mutual interactions between subunits of the human RNase MRP ribonucleoprotein complex."
    Welting T.J., van Venrooij W.J., Pruijn G.J.
    Nucleic Acids Res. 32:2138-2146(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POP4 AND RPP14.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPOP5_HUMAN
AccessioniPrimary (citable) accession number: Q969H6
Secondary accession number(s): A6NL80, Q53FS5, Q9Y2Q6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: December 1, 2001
Last modified: July 9, 2014
This is version 95 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Miscellaneous

The last C-terminal 19 amino acids are not required for complex association and RNase activity.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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