Q9H633 (RPP21_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonuclease P protein subunit p21
Short name=RNaseP protein p21
EC=3.1.26.5

Alternative name(s):
Ribonuclease P/MRP 21 kDa subunit
Ribonucleoprotein V

Gene names

Name:	RPP21
Synonyms:	C6orf135, CAT60

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	154 AA.
Sequence status	Complete.
Protein existence	Evidence at transcript 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 9 protein subunits; POP1, RPP14, RPP20/POP7, RPP21, RPP25, RPP29/POP4, RPP30, RPP38 and RPP40.
Subcellular location	Nucleus › nucleolus Ref.1.
Sequence similarities	Belongs to the eukaryotic/archaeal RNase P protein component 4 family.
Sequence caution	The sequence BI598757 differs from that shown. Reason: Erroneous termination at position 155. Translated as stop.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Hydrolase
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	response to drug Inferred from expression pattern PubMed 18291362. Source: UniProtKB tRNA processing Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	ribonuclease P activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q9H633-1)

Also known as: CAT60-V1;

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: Q9H633-2)

Also known as: CAT60-V3;

The sequence of this isoform differs from the canonical sequence as follows:
     19-19: Q → QVSLRQGPHGDGARRPRVTAPLPQ

Isoform 3 (identifier: Q9H633-3)

Also known as: CAT60-V4;

The sequence of this isoform differs from the canonical sequence as follows:
     123-154: DSKPLQPLPNTAHSISDRLPEEKMQTQGSSNQ → GERFQTTTTLAKHSPLHFRPPS

Isoform 4 (identifier: Q9H633-4)

The sequence of this isoform differs from the canonical sequence as follows:
     52-52: R → RRPLSSSAP

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 154	154	Ribonuclease P protein subunit p21		PRO_0000153845
Natural variations
	Alternative sequence	19	1	Q → QVSLRQGPHGDGARRPRVTA PLPQ in isoform 2.		VSP_010695
	Alternative sequence	52	1	R → RRPLSSSAP in isoform 4.		VSP_044901
	Alternative sequence	123 – 154	32	DSKPL…GSSNQ → GERFQTTTTLAKHSPLHFRP PS in isoform 3.		VSP_010696
	Natural variant	77	1	Q → H. Ref.2 Ref.4 Ref.6 Corresponds to variant rs6986 [ dbSNP | Ensembl ].		VAR_019116
	Natural variant	149	1	Q → K. Ref.4 Corresponds to variant rs974963 [ dbSNP | Ensembl ].		VAR_045986
Experimental info
	Sequence conflict	9	1	E → K in BI598757. Ref.6
	Sequence conflict	113	1	R → Q in CAD44290. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (CAT60-V1) [UniParc]. Last modified March 1, 2001. Version 1. Checksum: F8BD15AA20AE695F	FASTA	154	17,570
	10 20 30 40 50 60 MAGPVKDREA FQRLNFLYQA AHCVLAQDPE NQALARFYCY TERTIAKRLV LRRDPSVKRT 70 80 90 100 110 120 LCRGCSSLLV PGLTCTQRQR RCRGQRWTVQ TCLTCQRSQR FLNDPGHLLW GDRPEAQLGS 130 140 150 QADSKPLQPL PNTAHSISDR LPEEKMQTQG SSNQ
	Isoform 2 (CAT60-V3) [UniParc]. Checksum: 0FE5E6F3296602FB	FASTA	177	20,018
	10 20 30 40 50 60 MAGPVKDREA FQRLNFLYQV SLRQGPHGDG ARRPRVTAPL PQAAHCVLAQ DPENQALARF 70 80 90 100 110 120 YCYTERTIAK RLVLRRDPSV KRTLCRGCSS LLVPGLTCTQ RQRRCRGQRW TVQTCLTCQR 130 140 150 160 170 SQRFLNDPGH LLWGDRPEAQ LGSQADSKPL QPLPNTAHSI SDRLPEEKMQ TQGSSNQ
	Isoform 3 (CAT60-V4) [UniParc]. Checksum: B037193A307F6F77	FASTA	144	16,544
	10 20 30 40 50 60 MAGPVKDREA FQRLNFLYQA AHCVLAQDPE NQALARFYCY TERTIAKRLV LRRDPSVKRT 70 80 90 100 110 120 LCRGCSSLLV PGLTCTQRQR RCRGQRWTVQ TCLTCQRSQR FLNDPGHLLW GDRPEAQLGS 130 140 QAGERFQTTT TLAKHSPLHF RPPS
	Isoform 4 [UniParc]. Checksum: E2CA143586B0B751	FASTA	162	18,366
	10 20 30 40 50 60 MAGPVKDREA FQRLNFLYQA AHCVLAQDPE NQALARFYCY TERTIAKRLV LRRPLSSSAP 70 80 90 100 110 120 RDPSVKRTLC RGCSSLLVPG LTCTQRQRRC RGQRWTVQTC LTCQRSQRFL NDPGHLLWGD 130 140 150 160 RPEAQLGSQA DSKPLQPLPN TAHSISDRLP EEKMQTQGSS NQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Function and subnuclear distribution of Rpp21, a protein subunit of the human ribonucleoprotein ribonuclease P." Jarrous N., Reiner R., Wesolowski D., Mann H., Guerrier-Takada C., Altman S. RNA 7:1153-1164(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION.
[2]	"Genes from major histocompatibility complex (MHC) class I region from HLA-C to HLA-A." Raha-Chowdhury R., Andrews S.R., Gruen J.R., Weissman S.M. Submitted (AUG-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), VARIANT HIS-77. Tissue: Spleen.
[3]	"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] (ISOFORM 1). Tissue: Small intestine.
[4]	"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], VARIANTS HIS-77 AND LYS-149.
[5]	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 (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] (ISOFORMS 1 AND 4), VARIANT HIS-77. Tissue: Hypothalamus and Skin.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF212152 mRNA. Translation: AAK39955.2. AJ504713 mRNA. Translation: CAD44289.1. AJ504714 mRNA. Translation: CAD44290.1. AJ504715 mRNA. Translation: CAD44291.1. AJ504716 mRNA. Translation: CAD44292.1. AK026291 mRNA. Translation: BAB15433.1. AL662832 Genomic DNA. Translation: CAI17503.2. AL662832 Genomic DNA. Translation: CAI17506.2. AL662832 Genomic DNA. Translation: CAI17507.2. AL662795 Genomic DNA. Translation: CAI18254.1. AL662795 Genomic DNA. Translation: CAI18255.2. AL773535 Genomic DNA. Translation: CAI41822.1. AL773535 Genomic DNA. Translation: CAI41824.2. AL662795 Genomic DNA. Translation: CAM25559.1. BX294158 Genomic DNA. Translation: CAM25886.1. BX294158 Genomic DNA. Translation: CAM25887.1. BX294158 Genomic DNA. Translation: CAM25888.1. BX294158 Genomic DNA. Translation: CAM25889.1. CR759928 Genomic DNA. Translation: CAQ08317.1. CR759928 Genomic DNA. Translation: CAQ08318.1. BX927214 Genomic DNA. Translation: CAQ08386.1. BX927214 Genomic DNA. Translation: CAQ08387.1. BX927214 Genomic DNA. Translation: CAQ08388.1. CR759281 Genomic DNA. Translation: CAQ09024.1. CR759281 Genomic DNA. Translation: CAQ09025.1. CH471081 Genomic DNA. Translation: EAX03287.1. CH471081 Genomic DNA. Translation: EAX03288.1. CH471081 Genomic DNA. Translation: EAX03289.1. BC011730 mRNA. Translation: AAH11730.1. BI598757 mRNA. No translation available.
IPI	IPI00304938. IPI00384602. IPI00384603. IPI00641359.
RefSeq	NP_001186049.1. NM_001199120.1. NP_001186050.1. NM_001199121.1. NP_079115.1. NM_024839.2.
UniGene	Hs.183232.
3D structure databases
ProteinModelPortal	Q9H633.
SMR	Q9H633. Positions 4-103.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9H633. 1 interaction.
PTM databases
PhosphoSite	Q9H633.
Polymorphism databases
DMDM	52001252.
Proteomic databases
PaxDb	Q9H633.
PRIDE	Q9H633.
Protocols and materials databases
DNASU	79897.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000376642; ENSP00000365829; ENSG00000239927. ENST00000411784; ENSP00000412619; ENSG00000241863. ENST00000413228; ENSP00000405035; ENSG00000239865. ENST00000414187; ENSP00000398396; ENSG00000243009. ENST00000415583; ENSP00000403747; ENSG00000239927. ENST00000416977; ENSP00000404312; ENSG00000241779. ENST00000418043; ENSP00000404260; ENSG00000239865. ENST00000422320; ENSP00000391247; ENSG00000242726. ENST00000424616; ENSP00000399295; ENSG00000241863. ENST00000425575; ENSP00000405834; ENSG00000239927. ENST00000428040; ENSP00000394320; ENSG00000241370. ENST00000430900; ENSP00000415046; ENSG00000239927. ENST00000433076; ENSP00000409799; ENSG00000241370. ENST00000434282; ENSP00000414284; ENSG00000242726. ENST00000435318; ENSP00000411003; ENSG00000239865. ENST00000436442; ENSP00000397778; ENSG00000241370. ENST00000437470; ENSP00000408610; ENSG00000241863. ENST00000439624; ENSP00000389565; ENSG00000241779. ENST00000442966; ENSP00000403833; ENSG00000241370. ENST00000452262; ENSP00000388494; ENSG00000243009. ENST00000455025; ENSP00000409193; ENSG00000241863.
GeneID	79897.
KEGG	hsa:79897.
UCSC	uc003nqd.2. human. uc003nqe.2. human. uc003nqf.2. human.
Organism-specific databases
CTD	79897.
GeneCards	GC06P030312.
H-InvDB	HIX0207610. HIX0207675. HIX0207761.
HGNC	HGNC:21300. RPP21.
MIM	612524. gene.
neXtProt	NX_Q9H633.
PharmGKB	PA134960979.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG285045.
HOVERGEN	HBG055987.
KO	K03540.
OMA	DPKHLLW.
Gene expression databases
ArrayExpress	Q9H633.
Bgee	Q9H633.
CleanEx	HS_RPP21.
Genevestigator	Q9H633.
GermOnline	ENSG00000204596. Homo sapiens.
Family and domain databases
InterPro	IPR007175. Rpr2. [Graphical view]
PANTHER	PTHR14742. PTHR14742. 1 hit.
Pfam	PF04032. Rpr2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	79897.
NextBio	69734.
SOURCE	Search...

Entry information

Entry name

RPP21_HUMAN

Accession

Primary (citable) accession number: Q9H633
Secondary accession number(s): A2AAZ8 , B0S834, B0S835, Q5JPL9, Q5JPM1, Q5STF8, Q5STF9, Q5STG2, Q5SU41, Q5SU42, Q86Y49, Q86Y50, Q86Y51, Q96F16

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 5, 2004
Last sequence update:	March 1, 2001
Last modified:	May 1, 2013
This is version 90 of the entry and version 1 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.