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P78345 (RPP38_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 p38

Short name=RNaseP protein p38
EC=3.1.26.5
Gene names
Name:RPP38
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length283 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 an 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

Nucleusnucleolus Potential.

Miscellaneous

Autoantibodies against RPP38 are found in sera from scleroderma patients.

Sequence similarities

Belongs to the ribosomal protein L7Ae family.

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.9
Chain2 – 283282Ribonuclease P protein subunit p38
PRO_0000136783

Regions

Compositional bias63 – 686Poly-Lys

Amino acid modifications

Modified residue21N-acetylalanine Ref.9 Ref.14
Modified residue2261Phosphoserine Ref.13
Modified residue2351Phosphoserine Ref.8 Ref.11

Natural variations

Natural variant861I → V.
Corresponds to variant rs3814171 [ dbSNP | Ensembl ].
VAR_051811
Natural variant881E → D.
Corresponds to variant rs1052157 [ dbSNP | Ensembl ].
VAR_023960
Natural variant1141A → V. Ref.1
Corresponds to variant rs1132078 [ dbSNP | Ensembl ].
VAR_023961
Natural variant1811A → G. Ref.2 Ref.4
Corresponds to variant rs15772 [ dbSNP | Ensembl ].
VAR_023962
Natural variant2021S → R.
Corresponds to variant rs12249258 [ dbSNP | Ensembl ].
VAR_051812
Natural variant2121I → T.
Corresponds to variant rs10242 [ dbSNP | Ensembl ].
VAR_029298
Natural variant2501R → G.
Corresponds to variant rs34040166 [ dbSNP | Ensembl ].
VAR_051813

Experimental info

Sequence conflict241S → A AA sequence Ref.1

Sequences

Sequence LengthMass (Da)Tools
P78345 [UniParc].

Last modified December 6, 2005. Version 2.
Checksum: 233F3397DBDE4F18

FASTA28331,834
        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 

« Hide

References

« Hide '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. 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], 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[10]"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.
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_001091059.1. NM_001097590.2.
NP_001252530.1. NM_001265601.1.
NP_006405.2. NM_006414.4.
NP_892117.1. NM_183005.4.
UniGeneHs.94986.

3D structure databases

ProteinModelPortalP78345.
SMRP78345. Positions 111-200.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115808. 18 interactions.
IntActP78345. 8 interactions.
MINTMINT-5009179.
STRING9606.ENSP00000367439.

PTM databases

PhosphoSiteP78345.

Polymorphism databases

DMDM83305638.

Proteomic databases

PaxDbP78345.
PRIDEP78345.

Protocols and materials databases

DNASU10557.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378197; ENSP00000367439; ENSG00000152464.
ENST00000378202; ENSP00000367444; ENSG00000152464.
ENST00000378203; ENSP00000367445; ENSG00000152464.
GeneID10557.
KEGGhsa:10557.
UCSCuc001inx.5. human.

Organism-specific databases

CTD10557.
GeneCardsGC10P015140.
HGNCHGNC:30329. RPP38.
HPAHPA045128.
MIM606116. gene.
neXtProtNX_P78345.
PharmGKBPA134957031.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG308103.
HOGENOMHOG000231566.
HOVERGENHBG060241.
InParanoidP78345.
KOK14523.
OMAKIRKPPK.
OrthoDBEOG74BJT8.
PhylomeDBP78345.
TreeFamTF332558.

Gene expression databases

ArrayExpressP78345.
BgeeP78345.
CleanExHS_RPP38.
GenevestigatorP78345.

Family and domain databases

InterProIPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view]
PfamPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiRPP38.
GenomeRNAi10557.
NextBio40059.
PROP78345.
SOURCESearch...

Entry information

Entry nameRPP38_HUMAN
AccessionPrimary (citable) accession number: P78345
Secondary accession number(s): B3KPY0 expand/collapse secondary AC list , D3DRT8, Q53F71, Q8NHS8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: December 6, 2005
Last modified: April 16, 2014
This is version 125 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

Ribosomal proteins

Ribosomal proteins families and list of entries

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM