P78345 (RPP38_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease P protein subunit p38
Short name=RNaseP protein p38
EC=3.1.26.5

Gene names

Name:

RPP38

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	283 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. RPP38 may associate transiently with RNase P RNA as a factor involved in the transport of H1 RNA to the putative site of its assembly in the cell, the nucleolus.
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. RPP38 is probably a dimer.
Subcellular location	Nucleus › nucleolus Potential.
Miscellaneous	Autoantibodies against RPP38 are found in sera from scleroderma patients.
Sequence similarities	Belongs to the ribosomal protein L7Ae family.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolar ribonuclease P complex Traceable author statement PubMed 9630247. Source: ProtInc
Molecular_function	ribonuclease P activity Traceable author statement PubMed 9630247. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
NCK1	P16333	2	EBI-366493,EBI-389883
POP4	O95707	2	EBI-366493,EBI-366477

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 283	283	Ribonuclease P protein subunit p38		PRO_0000136783
Regions
	Compositional bias	63 – 68	6	Poly-Lys
Amino acid modifications
	Modified residue	226	1	Phosphoserine Ref.12
	Modified residue	235	1	Phosphoserine Ref.8 Ref.10
Natural variations
	Natural variant	86	1	I → V. Corresponds to variant rs3814171 [ dbSNP | Ensembl ].		VAR_051811
	Natural variant	88	1	E → D. Corresponds to variant rs1052157 [ dbSNP | Ensembl ].		VAR_023960
	Natural variant	114	1	A → V. Ref.1 Corresponds to variant rs1132078 [ dbSNP | Ensembl ].		VAR_023961
	Natural variant	181	1	A → G. Ref.2 Ref.4 Corresponds to variant rs15772 [ dbSNP | Ensembl ].		VAR_023962
	Natural variant	202	1	S → R. Corresponds to variant rs12249258 [ dbSNP | Ensembl ].		VAR_051812
	Natural variant	212	1	I → T. Corresponds to variant rs10242 [ dbSNP | Ensembl ].		VAR_029298
	Natural variant	250	1	R → G. Corresponds to variant rs34040166 [ dbSNP | Ensembl ].		VAR_051813
Experimental info
	Sequence conflict	24	1	S → A AA sequence Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P78345 [UniParc]. Last modified December 6, 2005. Version 2. Checksum: 233F3397DBDE4F18	FASTA	283	31,834
	10 20 30 40 50 60 MAAAPQAPGR GSLRKTRPLV VKTSLNNPYI IRWSALESED MHFILQTLED RLKAIGLQKI 70 80 90 100 110 120 EDKKKKNKTP FLKKESREKC SIAVDISENL KEKKTDAKQQ VSGWTPAHVR KQLAIGVNEV 130 140 150 160 170 180 TRALERRELL LVLVCKSVKP AMITSHLIQL SLSRSVPACQ VPRLSERIAP VIGLKCVLAL 190 200 210 220 230 240 AFKKNTTDFV DEVRAIIPRV PSLSVPWLQD RIEDSGENLE TEPLESQDRE LLDTSFEDLS 250 260 270 280 KPKRKLADGR QASVTLQPLK IKKLIPNPNK IRKPPKSKKA TPK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Characterization of two scleroderma autoimmune antigens that copurify with human ribonuclease P." Eder P.S., Kekuda R., Stolc V., Altman S. Proc. Natl. Acad. Sci. U.S.A. 94:1101-1106(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 24-32; 113-122 AND 212-228, VARIANT VAL-114.
[2]	"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], VARIANT GLY-181. Tissue: Skeletal muscle.
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	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], VARIANT GLY-181.
[5]	"The DNA sequence and comparative analysis of human chromosome 10." Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J. Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"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: Testis.
[8]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
[10]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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].
[12]	"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-226, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U77664 mRNA. Translation: AAC51142.1. AK057006 mRNA. Translation: BAG51842.1. CR541816 mRNA. Translation: CAG46615.1. AK223418 mRNA. Translation: BAD97138.1. AL590365 Genomic DNA. Translation: CAH73968.1. CH471072 Genomic DNA. Translation: EAW86240.1. CH471072 Genomic DNA. Translation: EAW86241.1. BC029494 mRNA. Translation: AAH29494.1.
IPI	IPI00019195.
RefSeq	NP_001091059.1. NM_001097590.2. NP_001252530.1. NM_001265601.1. NP_006405.2. NM_006414.4. NP_892117.1. NM_183005.4.
UniGene	Hs.94986.
3D structure databases
ProteinModelPortal	P78345.
ModBase	Search...
Protein-protein interaction databases
IntAct	P78345. 8 interactions.
MINT	MINT-5009179.
STRING	9606.ENSP00000367439.
PTM databases
PhosphoSite	P78345.
Polymorphism databases
DMDM	83305638.
Proteomic databases
PaxDb	P78345.
PRIDE	P78345.
Protocols and materials databases
DNASU	10557.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000378197; ENSP00000367439; ENSG00000152464. ENST00000378202; ENSP00000367444; ENSG00000152464. ENST00000378203; ENSP00000367445; ENSG00000152464.
GeneID	10557.
KEGG	hsa:10557.
UCSC	uc001inx.4. human.
Organism-specific databases
CTD	10557.
GeneCards	GC10P015140.
HGNC	HGNC:30329. RPP38.
HPA	HPA045128.
MIM	606116. gene.
neXtProt	NX_P78345.
PharmGKB	PA134957031.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG308103.
HOGENOM	HOG000231566.
HOVERGEN	HBG060241.
InParanoid	P78345.
KO	K14523.
OMA	KIRKPPK.
OrthoDB	EOG4Q84ZM.
PhylomeDB	P78345.
Gene expression databases
ArrayExpress	P78345.
Bgee	P78345.
CleanEx	HS_RPP38.
Genevestigator	P78345.
GermOnline	ENSG00000152464. Homo sapiens.
Family and domain databases
InterPro	IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45. [Graphical view]
Pfam	PF01248. Ribosomal_L7Ae. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10557.
NextBio	40059.
SOURCE	Search...

Entry information

Entry name

RPP38_HUMAN

Accession

Primary (citable) accession number: P78345
Secondary accession number(s): B3KPY0 , D3DRT8, Q53F71, Q8NHS8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	December 6, 2005
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.