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Protein

Ribonuclease P protein subunit p38

Gene

RPP38

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 activityi

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

GO - Molecular functioni

  1. ribonuclease P activity Source: ProtInc

GO - Biological processi

  1. RNA phosphodiester bond hydrolysis Source: GOC
  2. RNA phosphodiester bond hydrolysis, endonucleolytic Source: GOC
  3. tRNA processing Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

tRNA processing

Names & Taxonomyi

Protein namesi
Recommended name:
Ribonuclease P protein subunit p38 (EC:3.1.26.5)
Short name:
RNaseP protein p38
Gene namesi
Name:RPP38
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:30329. RPP38.

Subcellular locationi

  1. Nucleusnucleolus Curated

GO - Cellular componenti

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

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134957031.

Polymorphism and mutation databases

BioMutaiRPP38.
DMDMi83305638.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 283282Ribonuclease P protein subunit p38PRO_0000136783Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei226 – 2261Phosphoserine1 Publication
Modified residuei235 – 2351Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP78345.
PaxDbiP78345.
PRIDEiP78345.

PTM databases

PhosphoSiteiP78345.

Expressioni

Gene expression databases

BgeeiP78345.
CleanExiHS_RPP38.
ExpressionAtlasiP78345. baseline and differential.
GenevestigatoriP78345.

Organism-specific databases

HPAiHPA045128.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
NCK1P163332EBI-366493,EBI-389883
POP4O957072EBI-366493,EBI-366477

Protein-protein interaction databases

BioGridi115808. 25 interactions.
IntActiP78345. 8 interactions.
MINTiMINT-5009179.
STRINGi9606.ENSP00000367439.

Structurei

3D structure databases

ProteinModelPortaliP78345.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi63 – 686Poly-Lys

Sequence similaritiesi

Belongs to the ribosomal protein L7Ae family.Curated

Phylogenomic databases

eggNOGiNOG308103.
GeneTreeiENSGT00390000007526.
HOGENOMiHOG000231566.
HOVERGENiHBG060241.
InParanoidiP78345.
KOiK14523.
OMAiKIRKPPK.
OrthoDBiEOG74BJT8.
PhylomeDBiP78345.
TreeFamiTF332558.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P78345-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAAPQAPGR GSLRKTRPLV VKTSLNNPYI IRWSALESED MHFILQTLED
60 70 80 90 100
RLKAIGLQKI EDKKKKNKTP FLKKESREKC SIAVDISENL KEKKTDAKQQ
110 120 130 140 150
VSGWTPAHVR KQLAIGVNEV TRALERRELL LVLVCKSVKP AMITSHLIQL
160 170 180 190 200
SLSRSVPACQ VPRLSERIAP VIGLKCVLAL AFKKNTTDFV DEVRAIIPRV
210 220 230 240 250
PSLSVPWLQD RIEDSGENLE TEPLESQDRE LLDTSFEDLS KPKRKLADGR
260 270 280
QASVTLQPLK IKKLIPNPNK IRKPPKSKKA TPK
Length:283
Mass (Da):31,834
Last modified:December 6, 2005 - v2
Checksum:i233F3397DBDE4F18
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti24 – 241S → A AA sequence (PubMed:9037013).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti86 – 861I → V.
Corresponds to variant rs3814171 [ dbSNP | Ensembl ].
VAR_051811
Natural varianti88 – 881E → D.
Corresponds to variant rs1052157 [ dbSNP | Ensembl ].
VAR_023960
Natural varianti114 – 1141A → V.1 Publication
Corresponds to variant rs1132078 [ dbSNP | Ensembl ].
VAR_023961
Natural varianti181 – 1811A → G.2 Publications
Corresponds to variant rs15772 [ dbSNP | Ensembl ].
VAR_023962
Natural varianti202 – 2021S → R.
Corresponds to variant rs12249258 [ dbSNP | Ensembl ].
VAR_051812
Natural varianti212 – 2121I → T.
Corresponds to variant rs10242 [ dbSNP | Ensembl ].
VAR_029298
Natural varianti250 – 2501R → G.
Corresponds to variant rs34040166 [ dbSNP | Ensembl ].
VAR_051813

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7108.1.
RefSeqiNP_001091059.1. NM_001097590.2.
NP_001252530.1. NM_001265601.1.
NP_006405.2. NM_006414.4.
NP_892117.1. NM_183005.4.
XP_006717426.1. XM_006717363.1.
XP_006717427.1. XM_006717364.2.
UniGeneiHs.94986.

Genome annotation databases

EnsembliENST00000378197; ENSP00000367439; ENSG00000152464.
ENST00000378202; ENSP00000367444; ENSG00000152464.
ENST00000378203; ENSP00000367445; ENSG00000152464.
ENST00000616640; ENSP00000478982; ENSG00000152464.
GeneIDi10557.
KEGGihsa:10557.
UCSCiuc001inx.5. human.

Polymorphism and mutation databases

BioMutaiRPP38.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS7108.1.
RefSeqiNP_001091059.1. NM_001097590.2.
NP_001252530.1. NM_001265601.1.
NP_006405.2. NM_006414.4.
NP_892117.1. NM_183005.4.
XP_006717426.1. XM_006717363.1.
XP_006717427.1. XM_006717364.2.
UniGeneiHs.94986.

3D structure databases

ProteinModelPortaliP78345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115808. 25 interactions.
IntActiP78345. 8 interactions.
MINTiMINT-5009179.
STRINGi9606.ENSP00000367439.

PTM databases

PhosphoSiteiP78345.

Polymorphism and mutation databases

BioMutaiRPP38.
DMDMi83305638.

Proteomic databases

MaxQBiP78345.
PaxDbiP78345.
PRIDEiP78345.

Protocols and materials databases

DNASUi10557.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378197; ENSP00000367439; ENSG00000152464.
ENST00000378202; ENSP00000367444; ENSG00000152464.
ENST00000378203; ENSP00000367445; ENSG00000152464.
ENST00000616640; ENSP00000478982; ENSG00000152464.
GeneIDi10557.
KEGGihsa:10557.
UCSCiuc001inx.5. human.

Organism-specific databases

CTDi10557.
GeneCardsiGC10P015140.
HGNCiHGNC:30329. RPP38.
HPAiHPA045128.
MIMi606116. gene.
neXtProtiNX_P78345.
PharmGKBiPA134957031.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG308103.
GeneTreeiENSGT00390000007526.
HOGENOMiHOG000231566.
HOVERGENiHBG060241.
InParanoidiP78345.
KOiK14523.
OMAiKIRKPPK.
OrthoDBiEOG74BJT8.
PhylomeDBiP78345.
TreeFamiTF332558.

Miscellaneous databases

GeneWikiiRPP38.
GenomeRNAii10557.
NextBioi40059.
PROiP78345.
SOURCEiSearch...

Gene expression databases

BgeeiP78345.
CleanExiHS_RPP38.
ExpressionAtlasiP78345. baseline and differential.
GenevestigatoriP78345.

Family and domain databases

Gene3Di3.30.1330.30. 1 hit.
InterProiIPR029064. L30e-like.
IPR004038. Ribosomal_L7Ae/L30e/S12e/Gad45.
[Graphical view]
PfamiPF01248. Ribosomal_L7Ae. 1 hit.
[Graphical view]
SUPFAMiSSF55315. SSF55315. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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. 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. 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. 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. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRPP38_HUMAN
AccessioniPrimary (citable) accession number: P78345
Secondary accession number(s): B3KPY0
, D3DRT8, Q53F71, Q8NHS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: December 6, 2005
Last modified: April 29, 2015
This is version 133 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

Miscellaneous

Autoantibodies against RPP38 are found in sera from scleroderma patients.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Ribosomal proteins
    Ribosomal proteins families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.