O75818 (RPP40_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease P protein subunit p40
Short name=RNaseP protein p40
EC=3.1.26.5

Alternative name(s):
RNase P subunit 1

Gene names

Name:	RPP40
Synonyms:	RNASEP1

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	363 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.
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.
Subcellular location	Nucleus › nucleolus Potential.
Sequence caution	The sequence AAC24114.1 differs from that shown. Reason: Erroneous initiation. The sequence AAH17871.1 differs from that shown. Reason: Frameshift at position 327. The sequence CAH73740.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase
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 Ref.3. Source: ProtInc
Molecular_function	ribonuclease P activity Traceable author statement Ref.3. Source: ProtInc
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O75818-1)

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.

Isoform 2 (identifier: O75818-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 363	363	Ribonuclease P protein subunit p40		PRO_0000097434
Natural variations
	Alternative sequence	90 – 112	23	Missing in isoform 2.		VSP_037346
	Natural variant	314	1	V → I. Corresponds to variant rs12332997 [ dbSNP | Ensembl ].		VAR_055405
Experimental info
	Sequence conflict	255	1	Missing in AAC24114. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 26, 2009. Version 3. Checksum: 9B4495BA6CD40E79	FASTA	363	41,834
	10 20 30 40 50 60 MATLRRLREA PRHLLVCEKS NFGNHKSRHR HLVQTHYYNY RVSFLIPECG ILSEELKNLV 70 80 90 100 110 120 MNTGPYYFVK NLPLHELITP EFISTFIKKG SCYALTYNTH IDEDNTVALL PNGKLILSLD 130 140 150 160 170 180 KDTYEETGLQ GHPSQFSGRK IMKFIVSIDL MELSLNLDSK KYERISWSFK EKKPLKFDFL 190 200 210 220 230 240 LAWHKTGSEE STMMSYFSKY QIQEHQPKVA LSTLRDLQCP VLQSSELEGT PEVSCRALEL 250 260 270 280 290 300 FDWLGAVFSN VDLNNEPNNF ISTYCCPEPS TVVAKAYLCT ITGFILPEKI CLLLEHLCHY 310 320 330 340 350 360 FDEPKLAPWV TLSVQGFADS PVSWEKNEHG FRKGGEHLYN FVIFNNQDYW LQMAVGANDH CPP
	Isoform 2 [UniParc]. Checksum: BBA05462D4E02FE2	FASTA	340	39,327
	10 20 30 40 50 60 MATLRRLREA PRHLLVCEKS NFGNHKSRHR HLVQTHYYNY RVSFLIPECG ILSEELKNLV 70 80 90 100 110 120 MNTGPYYFVK NLPLHELITP EFISTFIKKG KLILSLDKDT YEETGLQGHP SQFSGRKIMK 130 140 150 160 170 180 FIVSIDLMEL SLNLDSKKYE RISWSFKEKK PLKFDFLLAW HKTGSEESTM MSYFSKYQIQ 190 200 210 220 230 240 EHQPKVALST LRDLQCPVLQ SSELEGTPEV SCRALELFDW LGAVFSNVDL NNEPNNFIST 250 260 270 280 290 300 YCCPEPSTVV AKAYLCTITG FILPEKICLL LEHLCHYFDE PKLAPWVTLS VQGFADSPVS 310 320 330 340 WEKNEHGFRK GGEHLYNFVI FNNQDYWLQM AVGANDHCPP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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).
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL359643 Genomic DNA. Translation: CAH73740.1. Different initiation. BC017871 mRNA. Translation: AAH17871.1. Sequence problems. U94317 Genomic DNA. Translation: AAC24114.1. Different initiation.
IPI	IPI00332091. IPI00478496.
RefSeq	NP_006629.2. NM_006638.2.
UniGene	Hs.511756.
3D structure databases
ProteinModelPortal	O75818.
ModBase	Search...
Protein-protein interaction databases
IntAct	O75818. 3 interactions.
STRING	9606.ENSP00000369391.
PTM databases
PhosphoSite	O75818.
Proteomic databases
PaxDb	O75818.
PRIDE	O75818.
Protocols and materials databases
DNASU	10799.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000319533; ENSP00000317998; ENSG00000124787. ENST00000380051; ENSP00000369391; ENSG00000124787. ENST00000464646; ENSP00000419431; ENSG00000124787.
GeneID	10799.
KEGG	hsa:10799.
UCSC	uc003mwl.3. human. uc003mwm.3. human.
Organism-specific databases
CTD	10799.
GeneCards	GC06M004942.
H-InvDB	HIX0005551. HIX0005552.
HGNC	HGNC:20992. RPP40.
HPA	HPA035686.
MIM	606117. gene.
neXtProt	NX_O75818.
PharmGKB	PA134911809.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG42164.
HOGENOM	HOG000006875.
HOVERGEN	HBG055018.
InParanoid	O75818.
KO	K14530.
OMA	FSKYQIQ.
OrthoDB	EOG4DR9CW.
Gene expression databases
ArrayExpress	O75818.
Bgee	O75818.
CleanEx	HS_RPP40.
Genevestigator	O75818.
GermOnline	ENSG00000124787. Homo sapiens.
Family and domain databases
InterPro	IPR013893. RNase_P_Rpp40. [Graphical view]
Pfam	PF08584. Ribonuc_P_40. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10799.
NextBio	41013.
SOURCE	Search...

Entry information

Entry name

RPP40_HUMAN

Accession

Primary (citable) accession number: O75818
Secondary accession number(s): Q5VX97, Q8WVK8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	May 26, 2009
Last modified:	April 3, 2013
This is version 106 of the entry and version 3 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.