Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O95707 (RPP29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 128. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Ribonuclease P protein subunit p29

Short name=hPOP4
EC=3.1.26.5
Gene names
Name:POP4
Synonyms:RPP29
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length220 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 activity

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

Subunit structure

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. Ref.6

Subcellular location

Nucleusnucleolus Ref.2.

Sequence similarities

Belongs to the eukaryotic/archaeal RNase P protein component 1 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 220220Ribonuclease P protein subunit p29
PRO_0000128418

Regions

Compositional bias65 – 7410Poly-Lys

Amino acid modifications

Modified residue101Phosphoserine Ref.7

Experimental info

Sequence conflict38 – 392ST → TS in AAD00893. Ref.1

Sequences

Sequence LengthMass (Da)Tools
O95707 [UniParc].

Last modified April 3, 2002. Version 2.
Checksum: 26141947E9F5C61E

FASTA22025,425
        10         20         30         40         50         60 
MKSVIYHALS QKEANDSDVQ PSGAQRAEAF VRAFLKRSTP RMSPQAREDQ LQRKAVVLEY 

        70         80         90        100        110        120 
FTRHKRKEKK KKAKGLSARQ RRELRLFDIK PEQQRYSLFL PLHELWKQYI RDLCSGLKPD 

       130        140        150        160        170        180 
TQPQMIQAKL LKADLHGAII SVTKSKCPSY VGITGILLQE TKHIFKIITK EDRLKVIPKL 

       190        200        210        220 
NCVFTVETDG FISYIYGSKF QLRSSERSAK KFKAKGTIDL 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-10, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS12416.1.
RefSeqNP_006618.1. NM_006627.2.
UniGeneHs.412870.

3D structure databases

ProteinModelPortalO95707.
SMRO95707. Positions 107-213.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115993. 8 interactions.
IntActO95707. 7 interactions.
MINTMINT-2799029.
STRING9606.ENSP00000221770.

PTM databases

PhosphoSiteO95707.

Proteomic databases

MaxQBO95707.
PaxDbO95707.
PRIDEO95707.

Protocols and materials databases

DNASU10775.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000585603; ENSP00000465213; ENSG00000105171.
GeneID10775.
KEGGhsa:10775.
UCSCuc002nsf.2. human.

Organism-specific databases

CTD10775.
GeneCardsGC19P030097.
HGNCHGNC:30081. POP4.
HPAHPA042748.
MIM606114. gene.
neXtProtNX_O95707.
PharmGKBPA134987921.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG255667.
HOGENOMHOG000007746.
HOVERGENHBG002676.
InParanoidO95707.
KOK03538.
OMAMSQQACE.
OrthoDBEOG786H4B.
PhylomeDBO95707.

Gene expression databases

ArrayExpressO95707.
BgeeO95707.
CleanExHS_POP4.
GenevestigatorO95707.

Family and domain databases

Gene3D2.30.30.210. 1 hit.
InterProIPR002730. RNase_P/MRP_p29.
IPR016848. RNase_P/MRP_p29-subunit.
IPR023534. Rof/RNase_P-like.
[Graphical view]
PfamPF01868. UPF0086. 1 hit.
[Graphical view]
PIRSFPIRSF027081. RNase_P/MRP_p29_subunit. 1 hit.
SMARTSM00538. POP4. 1 hit.
[Graphical view]
SUPFAMSSF101744. SSF101744. 1 hit.
ProtoNetSearch...

Other

GenomeRNAi10775.
NextBio40914.
PROO95707.
SOURCESearch...

Entry information

Entry nameRPP29_HUMAN
AccessionPrimary (citable) accession number: O95707
Secondary accession number(s): Q5XKL7, Q6FHW9, Q9UQQ3
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM