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O75818

- RPP40_HUMAN

UniProt

O75818 - RPP40_HUMAN

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Protein

Ribonuclease P protein subunit p40

Gene

RPP40

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 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.

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 p40 (EC:3.1.26.5)
Short name:
RNaseP protein p40
Alternative name(s):
RNase P subunit 1
Gene namesi
Name:RPP40
Synonyms:RNASEP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:20992. RPP40.

Subcellular locationi

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

PharmGKBiPA134911809.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 363363Ribonuclease P protein subunit p40PRO_0000097434Add
BLAST

Proteomic databases

MaxQBiO75818.
PaxDbiO75818.
PRIDEiO75818.

PTM databases

PhosphoSiteiO75818.

Expressioni

Gene expression databases

BgeeiO75818.
CleanExiHS_RPP40.
ExpressionAtlasiO75818. baseline and differential.
GenevestigatoriO75818.

Organism-specific databases

HPAiHPA035686.

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.

Protein-protein interaction databases

BioGridi116013. 13 interactions.
IntActiO75818. 3 interactions.
MINTiMINT-4527266.
STRINGi9606.ENSP00000369391.

Structurei

3D structure databases

ProteinModelPortaliO75818.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiNOG42164.
GeneTreeiENSGT00390000014167.
HOGENOMiHOG000006875.
HOVERGENiHBG055018.
InParanoidiO75818.
KOiK14530.
OMAiKGSCYAL.
OrthoDBiEOG7ZPNK2.
PhylomeDBiO75818.
TreeFamiTF330967.

Family and domain databases

InterProiIPR013893. RNase_P_Rpp40.
[Graphical view]
PfamiPF08584. Ribonuc_P_40. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: O75818-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATLRRLREA PRHLLVCEKS NFGNHKSRHR HLVQTHYYNY RVSFLIPECG
60 70 80 90 100
ILSEELKNLV MNTGPYYFVK NLPLHELITP EFISTFIKKG SCYALTYNTH
110 120 130 140 150
IDEDNTVALL PNGKLILSLD KDTYEETGLQ GHPSQFSGRK IMKFIVSIDL
160 170 180 190 200
MELSLNLDSK KYERISWSFK EKKPLKFDFL LAWHKTGSEE STMMSYFSKY
210 220 230 240 250
QIQEHQPKVA LSTLRDLQCP VLQSSELEGT PEVSCRALEL FDWLGAVFSN
260 270 280 290 300
VDLNNEPNNF ISTYCCPEPS TVVAKAYLCT ITGFILPEKI CLLLEHLCHY
310 320 330 340 350
FDEPKLAPWV TLSVQGFADS PVSWEKNEHG FRKGGEHLYN FVIFNNQDYW
360
LQMAVGANDH CPP
Length:363
Mass (Da):41,834
Last modified:May 26, 2009 - v3
Checksum:i9B4495BA6CD40E79
GO
Isoform 2 (identifier: O75818-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     90-112: Missing.

Note: No experimental confirmation available.

Show »
Length:340
Mass (Da):39,327
Checksum:iBBA05462D4E02FE2
GO

Sequence cautioni

The sequence AAC24114.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence AAH17871.1 differs from that shown. Reason: Frameshift at position 327. Curated
The sequence CAH73740.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti255 – 2551Missing in AAC24114. (PubMed:9630247)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti314 – 3141V → I.
Corresponds to variant rs12332997 [ dbSNP | Ensembl ].
VAR_055405

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei90 – 11223Missing in isoform 2. 1 PublicationVSP_037346Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL359643 Genomic DNA. Translation: CAH73740.1. Different initiation.
BC017871 mRNA. Translation: AAH17871.1. Sequence problems.
U94317 Genomic DNA. Translation: AAC24114.1. Different initiation.
CCDSiCCDS34333.1. [O75818-1]
CCDS69040.1. [O75818-2]
RefSeqiNP_001273061.1. NM_001286132.1. [O75818-2]
NP_001273062.1. NM_001286133.1.
NP_006629.2. NM_006638.3. [O75818-1]
UniGeneiHs.511756.

Genome annotation databases

EnsembliENST00000319533; ENSP00000317998; ENSG00000124787. [O75818-2]
ENST00000380051; ENSP00000369391; ENSG00000124787. [O75818-1]
GeneIDi10799.
KEGGihsa:10799.
UCSCiuc003mwl.3. human. [O75818-1]
uc003mwm.3. human. [O75818-2]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL359643 Genomic DNA. Translation: CAH73740.1 . Different initiation.
BC017871 mRNA. Translation: AAH17871.1 . Sequence problems.
U94317 Genomic DNA. Translation: AAC24114.1 . Different initiation.
CCDSi CCDS34333.1. [O75818-1 ]
CCDS69040.1. [O75818-2 ]
RefSeqi NP_001273061.1. NM_001286132.1. [O75818-2 ]
NP_001273062.1. NM_001286133.1.
NP_006629.2. NM_006638.3. [O75818-1 ]
UniGenei Hs.511756.

3D structure databases

ProteinModelPortali O75818.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 116013. 13 interactions.
IntActi O75818. 3 interactions.
MINTi MINT-4527266.
STRINGi 9606.ENSP00000369391.

PTM databases

PhosphoSitei O75818.

Proteomic databases

MaxQBi O75818.
PaxDbi O75818.
PRIDEi O75818.

Protocols and materials databases

DNASUi 10799.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000319533 ; ENSP00000317998 ; ENSG00000124787 . [O75818-2 ]
ENST00000380051 ; ENSP00000369391 ; ENSG00000124787 . [O75818-1 ]
GeneIDi 10799.
KEGGi hsa:10799.
UCSCi uc003mwl.3. human. [O75818-1 ]
uc003mwm.3. human. [O75818-2 ]

Organism-specific databases

CTDi 10799.
GeneCardsi GC06M004942.
H-InvDB HIX0005551.
HIX0005552.
HGNCi HGNC:20992. RPP40.
HPAi HPA035686.
MIMi 606117. gene.
neXtProti NX_O75818.
PharmGKBi PA134911809.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG42164.
GeneTreei ENSGT00390000014167.
HOGENOMi HOG000006875.
HOVERGENi HBG055018.
InParanoidi O75818.
KOi K14530.
OMAi KGSCYAL.
OrthoDBi EOG7ZPNK2.
PhylomeDBi O75818.
TreeFami TF330967.

Miscellaneous databases

GeneWikii RPP40.
GenomeRNAii 10799.
NextBioi 41013.
PROi O75818.
SOURCEi Search...

Gene expression databases

Bgeei O75818.
CleanExi HS_RPP40.
ExpressionAtlasi O75818. baseline and differential.
Genevestigatori O75818.

Family and domain databases

InterProi IPR013893. RNase_P_Rpp40.
[Graphical view ]
Pfami PF08584. Ribonuc_P_40. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  2. "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] (ISOFORM 2).
    Tissue: Brain.
  3. "Autoantigenic properties of some protein subunits of catalytically active complexes of human ribonuclease P."
    Jarrous N., Eder P.S., Guerrier-Takada C., Hoog C., Altman S.
    RNA 4:407-417(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 41-363, PROTEIN SEQUENCE OF 73-87; 116-125 AND 202-208 (ISOFORM 1).

Entry informationi

Entry nameiRPP40_HUMAN
AccessioniPrimary (citable) accession number: O75818
Secondary accession number(s): Q5VX97, Q8WVK8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: May 26, 2009
Last modified: October 29, 2014
This is version 119 of the entry and version 3 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

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: 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

External Data

Dasty 3