O95707 (RPP29_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease P protein subunit p29
Short name=hPOP4
EC=3.1.26.5

Gene names

Name:	POP4
Synonyms:	RPP29

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	220 AA.
Sequence status	Complete.
Protein existence	Evidence 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 a RNA moiety and at least 8 protein subunits; POP1, RPP14, RPP20/POP7, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40. RNase MRP consists of a 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	Nucleus › nucleolus Ref.2.
Sequence similarities	Belongs to the eukaryotic/archaeal RNase P protein component 1 family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	mRNA cleavage Inferred from electronic annotation. Source: InterPro rRNA processing Traceable author statement Ref.2. Source: ProtInc tRNA processing Traceable author statement Ref.2. Source: ProtInc
Cellular_component	nucleolar ribonuclease P complex Inferred from electronic annotation. Source: InterPro ribonuclease MRP complex Traceable author statement Ref.2. Source: ProtInc
Molecular_function	RNA binding Traceable author statement Ref.2. Source: ProtInc ribonuclease P activity Traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
POP1	Q99575	2	EBI-366477,EBI-366741
POP5	Q969H6	2	EBI-366477,EBI-366525
RPP25	Q9BUL9	2	EBI-366477,EBI-366570
RPP38	P78345	2	EBI-366477,EBI-366493

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 220	220	Ribonuclease P protein subunit p29		PRO_0000128418
Regions
	Compositional bias	65 – 74	10	Poly-Lys
Amino acid modifications
	Modified residue	10	1	Phosphoserine Ref.7
Experimental info
	Sequence conflict	38 – 39	2	ST → TS in AAD00893. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O95707 [UniParc]. Last modified April 3, 2002. Version 2. Checksum: 26141947E9F5C61E	FASTA	220	25,425
	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

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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].

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.
IPI	IPI00032791.
RefSeq	NP_006618.1. NM_006627.2.
UniGene	Hs.412870.
3D structure databases
ProteinModelPortal	O95707.
SMR	O95707. Positions 107-213.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95707. 7 interactions.
STRING	9606.ENSP00000221770.
PTM databases
PhosphoSite	O95707.
Proteomic databases
PaxDb	O95707.
PRIDE	O95707.
Protocols and materials databases
DNASU	10775.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000585603; ENSP00000465213; ENSG00000105171.
GeneID	10775.
KEGG	hsa:10775.
UCSC	uc002nsf.2. human.
Organism-specific databases
CTD	10775.
GeneCards	GC19P030097.
HGNC	HGNC:30081. POP4.
HPA	HPA042748.
MIM	606114. gene.
neXtProt	NX_O95707.
PharmGKB	PA134987921.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG255667.
HOGENOM	HOG000007746.
HOVERGEN	HBG002676.
InParanoid	O95707.
KO	K03538.
OMA	RSKCPSY.
OrthoDB	EOG4TXBT7.
PhylomeDB	O95707.
Gene expression databases
ArrayExpress	O95707.
Bgee	O95707.
CleanEx	HS_POP4.
Genevestigator	O95707.
GermOnline	ENSG00000105171. Homo sapiens.
Family and domain databases
Gene3D	2.30.30.210. 1 hit.
InterPro	IPR002730. RNase_P/MRP_p29. IPR016848. RNase_P/MRP_p29-subunit. IPR023534. Rof/RNase_P-like. [Graphical view]
Pfam	PF01868. UPF0086. 1 hit. [Graphical view]
PIRSF	PIRSF027081. RNase_P/MRP_p29_subunit. 1 hit.
SMART	SM00538. POP4. 1 hit. [Graphical view]
SUPFAM	SSF101744. RNase_P_Rpp29. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	10775.
NextBio	40914.
SOURCE	Search...

Entry information

Entry name

RPP29_HUMAN

Accession

Primary (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:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

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.