Q99575 (POP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribonucleases P/MRP protein subunit POP1
Short name=hPOP1
EC=3.1.26.5

Gene names

Name:	POP1
Synonyms:	KIAA0061

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	1024 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. Also a component of RNase MRP.
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.
Involvement in disease	Defects in POP1 may be the cause of a severe skeletal dysplasia reminiscent of anauxetic dysplasia. Affected individuals show severe growth retardation of prenatal onset, a bone dysplasia affecting the epiphyses and metaphyses of the long bones particularly in the lower limbs, and abnormalities of the spine including irregularly shaped vertebral bodies and marked cervical spine instability.

Ontologies

Keywords
Biological process	tRNA processing
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Dwarfism
Molecular function	Hydrolase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	tRNA 5'-leader removal Inferred from electronic annotation. Source: InterPro tRNA catabolic process Inferred from direct assay Ref.3. Source: UniProtKB
Cellular_component	nucleolar ribonuclease P complex Inferred from direct assay Ref.3. Source: UniProtKB ribonuclease MRP complex Inferred from direct assay Ref.3. Source: UniProtKB
Molecular_function	ribonuclease MRP activity Inferred from direct assay Ref.3. Source: UniProtKB ribonuclease P activity Inferred from direct assay Ref.3. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
POP4	O95707	2	EBI-366741,EBI-366477

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1024	1024	Ribonucleases P/MRP protein subunit POP1		PRO_0000058513
Amino acid modifications
	Modified residue	367	1	Phosphoserine Ref.7
	Modified residue	584	1	Phosphoserine Ref.6
	Modified residue	729	1	Phosphoserine Ref.12
	Modified residue	730	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.12
Natural variations
	Natural variant	127	1	S → L. Corresponds to variant rs3824145 [ dbSNP | Ensembl ].		VAR_057746
	Natural variant	460	1	E → A. Corresponds to variant rs2306131 [ dbSNP | Ensembl ].		VAR_057747
	Natural variant	522	1	K → N. Corresponds to variant rs17184326 [ dbSNP | Ensembl ].		VAR_057748
	Natural variant	583	1	G → E Probable disease associated mutation found in a patient with a skeletal dysplasia reminiscent of anauxetic dysplasia. Ref.11		VAR_067755
	Natural variant	675	1	E → Q in a breast cancer sample; somatic mutation. Ref.13		VAR_036232
	Natural variant	994	1	L → V. Corresponds to variant rs17856355 [ dbSNP | Ensembl ].		VAR_057749

Sequences

	Sequence		Length	Mass (Da)
	Q99575 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: A1DB872F3B940C02	FASTA	1,024	114,709
	10 20 30 40 50 60 MSNAKERKHA KKMRNQPTNV TLSSGFVADR GVKHHSGGEK PFQAQKQEPH PGTSRQRQTR 70 80 90 100 110 120 VNPHSLPDPE VNEQSSSKGM FRKKGGWKAG PEGTSQEIPK YITASTFAQA RAAEISAMLK 130 140 150 160 170 180 AVTQKSSNSL VFQTLPRHMR RRAMSHNVKR LPRRLQEIAQ KEAEKAVHQK KEHSKNKCHK 190 200 210 220 230 240 ARRCHMNRTL EFNRRQKKNI WLETHIWHAK RFHMVKKWGY CLGERPTVKS HRACYRAMTN 250 260 270 280 290 300 RCLLQDLSYY CCLELKGKEE EILKALSGMC NIDTGLTFAA VHCLSGKRQG SLVLYRVNKY 310 320 330 340 350 360 PREMLGPVTF IWKSQRTPGD PSESRQLWIW LHPTLKQDIL EEIKAACQCV EPIKSAVCIA 370 380 390 400 410 420 DPLPTPSQEK SQTELPDEKI GKKRKRKDDG ENAKPIKKII GDGTRDPCLP YSWISPTTGI 430 440 450 460 470 480 IISDLTMEMN RFRLIGPLSH SILTEAIKAA SVHTVGEDTE ETPHRWWIET CKKPDSVSLH 490 500 510 520 530 540 CRQEAIFELL GGITSPAEIP AGTILGLTVG DPRINLPQKK SKALPNPEKC QDNEKVRQLL 550 560 570 580 590 600 LEGVPVECTH SFIWNQDICK SVTENKISDQ DLNRMRSELL VPGSQLILGP HESKIPILLI 610 620 630 640 650 660 QQPGKVTGED RLGWGSGWDV LLPKGWGMAF WIPFIYRGVR VGGLKESAVH SQYKRSPNVP 670 680 690 700 710 720 GDFPDCPAGM LFAEEQAKNL LEKYKRRPPA KRPNYVKLGT LAPFCCPWEQ LTQDWESRVQ 730 740 750 760 770 780 AYEEPSVASS PNGKESDLRR SEVPCAPMPK KTHQPSDEVG TSIEHPREAE EVMDAGCQES 790 800 810 820 830 840 AGPERITDQE ASENHVAATG SHLCVLRSRK LLKQLSAWCG PSSEDSRGGR RAPGRGQQGL 850 860 870 880 890 900 TREACLSILG HFPRALVWVS LSLLSKGSPE PHTMICVPAK EDFLQLHEDW HYCGPQESKH 910 920 930 940 950 960 SDPFRSKILK QKEKKKREKR QKPGRASSDG PAGEEPVAGQ EALTLGLWSG PLPRVTLHCS 970 980 990 1000 1010 1020 RTLLGFVTQG DFSMAVGCGE ALGFVSLTGL LDMLSSQPAA QRGLVLLRPP ASLQYRFARI AIEV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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]. Tissue: Brain.
[2]	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].
[3]	"hPop1: an autoantigenic protein subunit shared by the human RNase P and RNase MRP ribonucleoproteins." Lygerou Z., Pluk H., Van Venrooij W.J., Seraphin B. EMBO J. 15:5936-5948(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-126.
[4]	"Prediction of the coding sequences of unidentified human genes. II. The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by analysis of cDNA clones from human cell line KG-1." Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., Seki N., Kawarabayasi Y., Ishikawa K., Tabata S. DNA Res. 1:223-229(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 122-1024. Tissue: Bone marrow.
[5]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[6]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-584, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"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-367 AND SER-730, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[9]	"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-730, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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].
[11]	"Whole-exome re-sequencing in a family quartet identifies POP1 mutations as the cause of a novel skeletal dysplasia." Glazov E.A., Zankl A., Donskoi M., Kenna T.J., Thomas G.P., Clark G.R., Duncan E.L., Brown M.A. PLoS Genet. 7:E1002027-E1002027(2011) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN SKELETAL DYSPLASIA, VARIANT GLU-583.
[12]	"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-729 AND SER-730, MASS SPECTROMETRY.
[13]	"The consensus coding sequences of human breast and colorectal cancers." Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E. Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT [LARGE SCALE ANALYSIS] GLN-675.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK291434 mRNA. Translation: BAF84123.1. CH471060 Genomic DNA. Translation: EAW91776.1. X99302 mRNA. Translation: CAA67684.1. D31765 mRNA. Translation: BAA06543.1.
IPI	IPI00293331.
RefSeq	NP_001139332.1. NM_001145860.1. NP_001139333.1. NM_001145861.1. NP_055844.2. NM_015029.2.
UniGene	Hs.252828.
3D structure databases
ProteinModelPortal	Q99575.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q99575. 8 interactions.
MINT	MINT-4537563.
STRING	9606.ENSP00000339529.
PTM databases
PhosphoSite	Q99575.
Polymorphism databases
DMDM	13124451.
Proteomic databases
PaxDb	Q99575.
PeptideAtlas	Q99575.
PRIDE	Q99575.
Protocols and materials databases
DNASU	10940.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000349693; ENSP00000339529; ENSG00000104356. ENST00000401707; ENSP00000385787; ENSG00000104356.
GeneID	10940.
KEGG	hsa:10940.
UCSC	uc003yij.4. human.
Organism-specific databases
CTD	10940.
GeneCards	GC08P099129.
H-InvDB	HIX0007674.
HGNC	HGNC:30129. POP1.
MIM	602486. gene.
neXtProt	NX_Q99575.
Orphanet	93347. Anauxetic dysplasia.
PharmGKB	PA134907403.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG297409.
HOGENOM	HOG000013102.
HOVERGEN	HBG008232.
InParanoid	Q99575.
KO	K01164.
OMA	KKMRNQP.
OrthoDB	EOG4F4S9F.
PhylomeDB	Q99575.
Gene expression databases
ArrayExpress	Q99575.
Bgee	Q99575.
CleanEx	HS_POP1.
Genevestigator	Q99575.
GermOnline	ENSG00000104356. Homo sapiens.
Family and domain databases
InterPro	IPR012590. POPLD. IPR009723. RNase_P/MRP_POP1. [Graphical view]
Pfam	PF06978. POP1. 1 hit. PF08170. POPLD. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	10940.
NextBio	41555.
SOURCE	Search...

Entry information

Entry name

POP1_HUMAN

Accession

Primary (citable) accession number: Q99575
Secondary accession number(s): A8K5W9, Q15037

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2001
Last sequence update:	February 21, 2001
Last modified:	May 29, 2013
This is version 120 of the entry and version 2 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.