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O95707

- RPP29_HUMAN

UniProt

O95707 - RPP29_HUMAN

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Protein
Ribonuclease P protein subunit p29
Gene
POP4, RPP29
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Part of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. May function with RPP38 to coordinate the nucleolar targeting and/or assembly of RNase P.

Catalytic activityi

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

GO - Molecular functioni

  1. RNA binding Source: ProtInc
  2. protein binding Source: IntAct
  3. ribonuclease P activity Source: ProtInc

GO - Biological processi

  1. RNA phosphodiester bond hydrolysis Source: GOC
  2. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  3. mRNA cleavage Source: InterPro
  4. rRNA processing Source: ProtInc
  5. tRNA processing Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein subunit p29 (EC:3.1.26.5)
Short name:
hPOP4
Gene namesi
Name:POP4
Synonyms:RPP29
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:30081. POP4.

Subcellular locationi

Nucleusnucleolus 1 Publication

GO - Cellular componenti

  1. nucleolar ribonuclease P complex Source: InterPro
  2. ribonuclease MRP complex Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134987921.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 220220Ribonuclease P protein subunit p29
PRO_0000128418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei10 – 101Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiO95707.
PaxDbiO95707.
PRIDEiO95707.

PTM databases

PhosphoSiteiO95707.

Expressioni

Gene expression databases

ArrayExpressiO95707.
BgeeiO95707.
CleanExiHS_POP4.
GenevestigatoriO95707.

Organism-specific databases

HPAiHPA042748.

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. Interacts with RPP25 and POP5.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
POP1Q995752EBI-366477,EBI-366741
POP5Q969H62EBI-366477,EBI-366525
RPP25Q9BUL92EBI-366477,EBI-366570
RPP38P783452EBI-366477,EBI-366493

Protein-protein interaction databases

BioGridi115993. 8 interactions.
IntActiO95707. 7 interactions.
MINTiMINT-2799029.
STRINGi9606.ENSP00000221770.

Structurei

3D structure databases

ProteinModelPortaliO95707.
SMRiO95707. Positions 107-213.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi65 – 7410Poly-Lys

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG255667.
HOGENOMiHOG000007746.
HOVERGENiHBG002676.
InParanoidiO95707.
KOiK03538.
OMAiMSQQACE.
OrthoDBiEOG786H4B.
PhylomeDBiO95707.

Family and domain databases

Gene3Di2.30.30.210. 1 hit.
InterProiIPR002730. RNase_P/MRP_p29.
IPR016848. RNase_P/MRP_p29-subunit.
IPR023534. Rof/RNase_P-like.
[Graphical view]
PfamiPF01868. UPF0086. 1 hit.
[Graphical view]
PIRSFiPIRSF027081. RNase_P/MRP_p29_subunit. 1 hit.
SMARTiSM00538. POP4. 1 hit.
[Graphical view]
SUPFAMiSSF101744. SSF101744. 1 hit.

Sequencei

Sequence statusi: Complete.

O95707-1 [UniParc]FASTAAdd to Basket

« Hide

MKSVIYHALS QKEANDSDVQ PSGAQRAEAF VRAFLKRSTP RMSPQAREDQ    50
LQRKAVVLEY FTRHKRKEKK KKAKGLSARQ RRELRLFDIK PEQQRYSLFL 100
PLHELWKQYI RDLCSGLKPD TQPQMIQAKL LKADLHGAII SVTKSKCPSY 150
VGITGILLQE TKHIFKIITK EDRLKVIPKL NCVFTVETDG FISYIYGSKF 200
QLRSSERSAK KFKAKGTIDL 220
Length:220
Mass (Da):25,425
Last modified:April 3, 2002 - v2
Checksum:i26141947E9F5C61E
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 392ST → TS in AAD00893. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF001176 mRNA. Translation: AAD00893.2.
Y18863 mRNA. Translation: CAB39167.1.
CR536569 mRNA. Translation: CAG38806.1.
AK314790 mRNA. Translation: BAG37321.1.
BC004438 mRNA. Translation: AAH04438.1.
BC006098 mRNA. Translation: AAH06098.1.
CCDSiCCDS12416.1.
RefSeqiNP_006618.1. NM_006627.2.
UniGeneiHs.412870.

Genome annotation databases

EnsembliENST00000585603; ENSP00000465213; ENSG00000105171.
GeneIDi10775.
KEGGihsa:10775.
UCSCiuc002nsf.2. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF001176 mRNA. Translation: AAD00893.2 .
Y18863 mRNA. Translation: CAB39167.1 .
CR536569 mRNA. Translation: CAG38806.1 .
AK314790 mRNA. Translation: BAG37321.1 .
BC004438 mRNA. Translation: AAH04438.1 .
BC006098 mRNA. Translation: AAH06098.1 .
CCDSi CCDS12416.1.
RefSeqi NP_006618.1. NM_006627.2.
UniGenei Hs.412870.

3D structure databases

ProteinModelPortali O95707.
SMRi O95707. Positions 107-213.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115993. 8 interactions.
IntActi O95707. 7 interactions.
MINTi MINT-2799029.
STRINGi 9606.ENSP00000221770.

PTM databases

PhosphoSitei O95707.

Proteomic databases

MaxQBi O95707.
PaxDbi O95707.
PRIDEi O95707.

Protocols and materials databases

DNASUi 10775.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000585603 ; ENSP00000465213 ; ENSG00000105171 .
GeneIDi 10775.
KEGGi hsa:10775.
UCSCi uc002nsf.2. human.

Organism-specific databases

CTDi 10775.
GeneCardsi GC19P030097.
HGNCi HGNC:30081. POP4.
HPAi HPA042748.
MIMi 606114. gene.
neXtProti NX_O95707.
PharmGKBi PA134987921.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG255667.
HOGENOMi HOG000007746.
HOVERGENi HBG002676.
InParanoidi O95707.
KOi K03538.
OMAi MSQQACE.
OrthoDBi EOG786H4B.
PhylomeDBi O95707.

Miscellaneous databases

GenomeRNAii 10775.
NextBioi 40914.
PROi O95707.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95707.
Bgeei O95707.
CleanExi HS_POP4.
Genevestigatori O95707.

Family and domain databases

Gene3Di 2.30.30.210. 1 hit.
InterProi IPR002730. RNase_P/MRP_p29.
IPR016848. RNase_P/MRP_p29-subunit.
IPR023534. Rof/RNase_P-like.
[Graphical view ]
Pfami PF01868. UPF0086. 1 hit.
[Graphical view ]
PIRSFi PIRSF027081. RNase_P/MRP_p29_subunit. 1 hit.
SMARTi SM00538. POP4. 1 hit.
[Graphical view ]
SUPFAMi SSF101744. SSF101744. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Rpp14 and Rpp29, two protein subunits of human ribonuclease P."
    Jarrous N., Eder P.S., Wesolowski D., Altman S.
    RNA 5:153-157(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 86-95.
  2. "hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes."
    van Eenennaam H., Pruijn G.J.M., van Venrooij W.J.
    Nucleic Acids Res. 27:2465-2472(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
  3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  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].
    Tissue: Brain.
  5. "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].
    Tissue: Lung and Lymph.
  6. "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 RPP25 AND POP5.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRPP29_HUMAN
AccessioniPrimary (citable) accession number: O95707
Secondary accession number(s): Q5XKL7, Q6FHW9, Q9UQQ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 3, 2002
Last modified: July 9, 2014
This is version 128 of the entry and version 2 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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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