KIAA0391

Functionⁱ

Catalytic ribonuclease component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP3, which cleaves tRNA molecules in their 5'-ends (PubMed:18984158, PubMed:25953853). The presence of TRMT10C/MRPP1, HSD17B10/MRPP2 is required to catalyze tRNA molecules in their 5'-ends (PubMed:25953853).2 Publications

Catalytic activityⁱ

Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.1 Publication

Cofactorⁱ

Mg²⁺1 Publication, Mn²⁺1 PublicationNote: Binds 2 Mg²⁺ or Mg²⁺ ions per subunit.1 Publication

Sites

Feature key	Position(s)	DescriptionActions	Length
Metal bindingⁱ	348	ZincCombined sources1 Publication	1
Metal bindingⁱ	351	ZincCombined sources1 Publication	1
Metal bindingⁱ	409	Magnesium or manganese 1; catalytic1 Publication	1
Metal bindingⁱ	478	Magnesium or manganese 1; catalytic1 Publication	1
Metal bindingⁱ	479	Magnesium or manganese 2; catalytic1 Publication	1
Metal bindingⁱ	499	Magnesium or manganese 2; catalytic1 Publication	1
Metal bindingⁱ	557	Zinc; via tele nitrogenCombined sources1 Publication	1
Metal bindingⁱ	578	ZincCombined sources1 Publication	1

GO - Molecular functionⁱ

metal ion binding Source: UniProtKB-KW
ribonuclease P activity
Source: UniProtKB
Inferred from direct assayⁱ
- 25953853

View the complete GO annotation on QuickGO ...

GO - Biological processⁱ

mitochondrial tRNA 5'-end processing
Source: UniProtKB
Inferred from direct assayⁱ
- 25953853
mitochondrial tRNA processing Source: Reactome
tRNA 5'-leader removal
Source: GO_Central
Inferred from biological aspect of ancestorⁱ
- 21873635

View the complete GO annotation on QuickGO ...

Keywordsⁱ

Molecular function	Hydrolase, Nuclease
Biological process	tRNA processing
Ligand	Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

Reactomeⁱ	R-HSA-6785470 tRNA processing in the mitochondrion R-HSA-6787450 tRNA modification in the mitochondrion R-HSA-8868766 rRNA processing in the mitochondrion

Reactomeⁱ

R-HSA-6785470 tRNA processing in the mitochondrion
R-HSA-6787450 tRNA modification in the mitochondrion
R-HSA-8868766 rRNA processing in the mitochondrion

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Mitochondrial ribonuclease P catalytic subunit (EC:3.1.26.51 Publication) Alternative name(s): Mitochondrial ribonuclease P protein 31 Publication Short name: Mitochondrial RNase P protein 31 Publication
Gene namesⁱ	Name:KIAA0391Imported Synonyms:MRPP31 Publication
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 14

Organism-specific databases

EuPathDBⁱ	HostDB:ENSG00000100890.15
Human Gene Nomenclature Database More...HGNCⁱ	HGNC:19958 KIAA0391
MIMⁱ	609947 gene
neXtProtⁱ	NX_O15091

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Mitochondrion

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	DescriptionActions	Length
Mutagenesisⁱ	409	D → N: Abolishes ribonuclease activity. 1 Publication	1
Mutagenesisⁱ	478	D → N: Abolishes ribonuclease activity. 1 Publication	1
Mutagenesisⁱ	479	D → N: Abolishes ribonuclease activity. 1 Publication	1
Mutagenesisⁱ	480	P → G: Does not affect ribonuclease activity. 1 Publication	1
Mutagenesisⁱ	498	R → D or N: Does not affect ribonuclease activity. 1 Publication	1
Mutagenesisⁱ	499	D → N: Abolishes ribonuclease activity. 1 Publication	1
Mutagenesisⁱ	569	S → A: Does not affect ribonuclease activity. 1 Publication	1

Organism-specific databases

DisGeNET More...DisGeNETⁱ	9692
Open Targets More...OpenTargetsⁱ	ENSG00000100890
PharmGKBⁱ	PA134879499

Polymorphism and mutation databases

BioMutaⁱ	KIAA0391

BioMutaⁱ

KIAA0391

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Transit peptideⁱ	1 – 45	MitochondrionSequence analysisAdd BLAST		45
ChainⁱPRO_0000050749	46 – 583	Mitochondrial ribonuclease P catalytic subunitAdd BLAST		538

Amino acid modifications

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Modified residueⁱ	98	PhosphoserineCombined sources		1

Post-translational modificationⁱ

Degraded by LONP1 following mitochondrial unfolded protein response, probably leading to inhibit translation in mitochondrion.1 Publication

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	O15091
MaxQB - The MaxQuant DataBase More...MaxQBⁱ	O15091
PaxDbⁱ	O15091
PeptideAtlas More...PeptideAtlasⁱ	O15091
PRIDEⁱ	O15091
ProteomicsDBⁱ	48444 48445 [O15091-2] 48446 [O15091-3] 48447 [O15091-4]

PTM databases

iPTMnetⁱ	O15091
PhosphoSitePlusⁱ	O15091

Expressionⁱ

Inductionⁱ

Down-regulated following mitochondrial unfolded protein response.1 Publication

Gene expression databases

Bgeeⁱ	ENSG00000100890 Expressed in 107 organ(s), highest expression level in leukocyte
CleanExⁱ	HS_KIAA0391
ExpressionAtlasⁱ	O15091 baseline and differential
Genevisibleⁱ	O15091 HS

Organism-specific databases

Human Protein Atlas More...HPAⁱ	HPA020459

HPAⁱ

HPA020459

Interactionⁱ

Subunit structureⁱ

Catalytic component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and MRPP31 (PubMed:18984158).1 Publication

Protein-protein interaction databases

BioGridⁱ	115044, 31 interactors
IntActⁱ	O15091, 6 interactors
Molecular INTeraction database More...MINTⁱ	O15091
STRINGⁱ	9606.ENSP00000454657

Structureⁱ

Secondary structure

Legend: HelixTurnBeta strandPDB Structure known for this area

Feature key	Position(s)	DescriptionActions	Length
Helixⁱ	213 – 220	Combined sources	8
Turnⁱ	224 – 226	Combined sources	3
Helixⁱ	227 – 237	Combined sources	11
Helixⁱ	244 – 256	Combined sources	13
Helixⁱ	260 – 272	Combined sources	13
Helixⁱ	279 – 289	Combined sources	11
Helixⁱ	295 – 310	Combined sources	16
Helixⁱ	317 – 329	Combined sources	13
Beta strandⁱ	335 – 340	Combined sources	6
Beta strandⁱ	346 – 348	Combined sources	3
Turnⁱ	349 – 351	Combined sources	3
Beta strandⁱ	357 – 359	Combined sources	3
Helixⁱ	362 – 376	Combined sources	15
Helixⁱ	388 – 399	Combined sources	12
Beta strandⁱ	405 – 409	Combined sources	5
Helixⁱ	410 – 413	Combined sources	4
Helixⁱ	423 – 433	Combined sources	11
Helixⁱ	434 – 436	Combined sources	3
Beta strandⁱ	440 – 445	Combined sources	6
Helixⁱ	446 – 449	Combined sources	4
Helixⁱ	460 – 466	Combined sources	7
Beta strandⁱ	467 – 472	Combined sources	6
Helixⁱ	481 – 489	Combined sources	9
Beta strandⁱ	494 – 498	Combined sources	5
Helixⁱ	511 – 524	Combined sources	14
Beta strandⁱ	553 – 561	Combined sources	9
Beta strandⁱ	575 – 581	Combined sources	7

Show more details

3D structure databases

ProteinModelPortalⁱ	O15091
SMRⁱ	O15091
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Domainⁱ	342 – 578	PRORPAdd BLAST		237

Domainⁱ

Displays a distorted and non-productive active site that probably switches to a fully productive state only upon association with TRMT10C/MRPP1, HSD17B10/MRPP2 and pre-tRNA substrate.1 Publication

Sequence similaritiesⁱ

Belongs to the PPR family. P subfamily.Curated

Keywords - Domainⁱ

Transit peptide

Phylogenomic databases

eggNOGⁱ	ENOG410IE4T Eukaryota ENOG4111GT9 LUCA
Ensembl GeneTree More...GeneTreeⁱ	ENSGT00390000002201
HOVERGENⁱ	HBG099441
InParanoidⁱ	O15091
KEGG Orthology (KO) More...KOⁱ	K17655
OMAⁱ	HDDPFLL
Database of Orthologous Groups More...OrthoDBⁱ	EOG091G0JTR
PhylomeDBⁱ	O15091
TreeFamⁱ	TF324726

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR033495 MRPP3 IPR031595 PRORP_C IPR011990 TPR-like_helical_dom_sf
PANTHERⁱ	PTHR13547:SF1 PTHR13547:SF1, 1 hit
Pfam protein domain database More...Pfamⁱ	View protein in Pfam PF16953 PRORP, 1 hit

Sequences (4+)ⁱ

Sequence statusⁱ: Complete.

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

This entry describes 4 isoformsⁱ produced by alternative splicing. Align Add to basket

This entry has 4 described isoforms and 4 potential isoforms that are computationally mapped.Show all Align All

Isoform 1 (identifier: O15091-1) [UniParc]FASTA Add 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
MTFYLFGIRS FPKLWKSPYL GLGPGHSYVS LFLADRCGIR NQQRLFSLKT 
        60         70         80         90        100
MSPQNTKATN LIAKARYLRK DEGSNKQVYS VPHFFLAGAA KERSQMNSQT 
       110        120        130        140        150
EDHALAPVRN TIQLPTQPLN SEEWDKLKED LKENTGKTSF ESWIISQMAG 
       160        170        180        190        200
CHSSIDVAKS LLAWVAAKNN GIVSYDLLVK YLYLCVFHMQ TSEVIDVFEI 
       210        220        230        240        250
MKARYKTLEP RGYSLLIRGL IHSDRWREAL LLLEDIKKVI TPSKKNYNDC 
       260        270        280        290        300
IQGALLHQDV NTAWNLYQEL LGHDIVPMLE TLKAFFDFGK DIKDDNYSNK 
       310        320        330        340        350
LLDILSYLRN NQLYPGESFA HSIKTWFESV PGKQWKGQFT TVRKSGQCSG 
       360        370        380        390        400
CGKTIESIQL SPEEYECLKG KIMRDVIDGG DQYRKTTPQE LKRFENFIKS 
       410        420        430        440        450
RPPFDVVIDG LNVAKMFPKV RESQLLLNVV SQLAKRNLRL LVLGRKHMLR 
       460        470        480        490        500
RSSQWSRDEM EEVQKQASCF FADDISEDDP FLLYATLHSG NHCRFITRDL 
       510        520        530        540        550
MRDHKACLPD AKTQRLFFKW QQGHQLAIVN RFPGSKLTFQ RILSYDTVVQ 
       560        570        580 
TTGDSWHIPY DEDLVERCSC EVPTKWLCLH QKT

Length:583

Mass (Da):67,315

Last modified:January 20, 2009 - v2

Checksum:ⁱ6AB17E7E8820D818

GO

Isoform 2 (identifier: O15091-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
329-344: Missing.

« Hide

        10         20         30         40         50
MTFYLFGIRS FPKLWKSPYL GLGPGHSYVS LFLADRCGIR NQQRLFSLKT 
        60         70         80         90        100
MSPQNTKATN LIAKARYLRK DEGSNKQVYS VPHFFLAGAA KERSQMNSQT 
       110        120        130        140        150
EDHALAPVRN TIQLPTQPLN SEEWDKLKED LKENTGKTSF ESWIISQMAG 
       160        170        180        190        200
CHSSIDVAKS LLAWVAAKNN GIVSYDLLVK YLYLCVFHMQ TSEVIDVFEI 
       210        220        230        240        250
MKARYKTLEP RGYSLLIRGL IHSDRWREAL LLLEDIKKVI TPSKKNYNDC 
       260        270        280        290        300
IQGALLHQDV NTAWNLYQEL LGHDIVPMLE TLKAFFDFGK DIKDDNYSNK 
       310        320        330        340        350
LLDILSYLRN NQLYPGESFA HSIKTWFESG QCSGCGKTIE SIQLSPEEYE 
       360        370        380        390        400
CLKGKIMRDV IDGGDQYRKT TPQELKRFEN FIKSRPPFDV VIDGLNVAKM 
       410        420        430        440        450
FPKVRESQLL LNVVSQLAKR NLRLLVLGRK HMLRRSSQWS RDEMEEVQKQ 
       460        470        480        490        500
ASCFFADDIS EDDPFLLYAT LHSGNHCRFI TRDLMRDHKA CLPDAKTQRL 
       510        520        530        540        550
FFKWQQGHQL AIVNRFPGSK LTFQRILSYD TVVQTTGDSW HIPYDEDLVE 
       560 
RCSCEVPTKW LCLHQKT

Show »

Length:567

Mass (Da):65,486

Checksum:ⁱ67B870DEBE05F5CC

GO

Isoform 3 (identifier: O15091-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-372: Missing.

« Hide

        10         20         30         40         50
MRDVIDGGDQ YRKTTPQELK RFENFIKSRP PFDVVIDGLN VAKMFPKVRE 
        60         70         80         90        100
SQLLLNVVSQ LAKRNLRLLV LGRKHMLRRS SQWSRDEMEE VQKQASCFFA 
       110        120        130        140        150
DDISEDDPFL LYATLHSGNH CRFITRDLMR DHKACLPDAK TQRLFFKWQQ 
       160        170        180        190        200
GHQLAIVNRF PGSKLTFQRI LSYDTVVQTT GDSWHIPYDE DLVERCSCEV 
       210 
PTKWLCLHQK T

Show »

Length:211

Mass (Da):24,787

Checksum:ⁱD8B8A46D9244A3BD

GO

Isoform 4 (identifier: O15091-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1-95: Missing.

« Hide

        10         20         30         40         50
MNSQTEDHAL APVRNTIQLP TQPLNSEEWD KLKEDLKENT GKTSFESWII 
        60         70         80         90        100
SQMAGCHSSI DVAKSLLAWV AAKNNGIVSY DLLVKYLYLC VFHMQTSEVI 
       110        120        130        140        150
DVFEIMKARY KTLEPRGYSL LIRGLIHSDR WREALLLLED IKKVITPSKK 
       160        170        180        190        200
NYNDCIQGAL LHQDVNTAWN LYQELLGHDI VPMLETLKAF FDFGKDIKDD 
       210        220        230        240        250
NYSNKLLDIL SYLRNNQLYP GESFAHSIKT WFESVPGKQW KGQFTTVRKS 
       260        270        280        290        300
GQCSGCGKTI ESIQLSPEEY ECLKGKIMRD VIDGGDQYRK TTPQELKRFE 
       310        320        330        340        350
NFIKSRPPFD VVIDGLNVAK MFPKVRESQL LLNVVSQLAK RNLRLLVLGR 
       360        370        380        390        400
KHMLRRSSQW SRDEMEEVQK QASCFFADDI SEDDPFLLYA TLHSGNHCRF 
       410        420        430        440        450
ITRDLMRDHK ACLPDAKTQR LFFKWQQGHQ LAIVNRFPGS KLTFQRILSY 
       460        470        480 
DTVVQTTGDS WHIPYDEDLV ERCSCEVPTK WLCLHQKT

Note: No experimental confirmation available.

Show »

Length:488

Mass (Da):56,487

Checksum:ⁱEF0D334CD9099547

GO

Computationally mapped potential isoform sequencesⁱ

There are 4 potential isoforms mapped to this entry.BLAST Align Show all Add to basket

Entry	Entry name	Protein names	Gene names	Length	Annotation

A0A0A0MTQ0	A0A0A0MTQ0_HUMAN	Mitochondrial ribonuclease P cataly... Mitochondrial ribonuclease P catalytic subunit	KIAA0391	185	Annotation score:
S4R3T4	S4R3T4_HUMAN	Mitochondrial ribonuclease P cataly... Mitochondrial ribonuclease P catalytic subunit	KIAA0391	23	Annotation score:
S4R416	S4R416_HUMAN	Mitochondrial ribonuclease P cataly... Mitochondrial ribonuclease P catalytic subunit	KIAA0391	34	Annotation score:
S4R3S1	S4R3S1_HUMAN	Mitochondrial ribonuclease P cataly... Mitochondrial ribonuclease P catalytic subunit	KIAA0391	19	Annotation score:

Sequence cautionⁱ

The sequence BAA20845 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Sequence conflictⁱ	315	P → L in BAG63351 (PubMed:14702039).Curated		1
Sequence conflictⁱ	453	S → F in BAG64540 (PubMed:14702039).Curated		1

Natural variant

Feature key	Position(s)	DescriptionActions	Graphical view	Length
Natural variantⁱVAR_054212	437	N → S2 PublicationsCorresponds to variant dbSNP:rs11156878Ensembl.		1

Alternative sequence

Feature key	Position(s)	DescriptionActions	Length
Alternative sequenceⁱVSP_036201	1 – 372	Missing in isoform 3. 2 PublicationsAdd BLAST	372
Alternative sequenceⁱVSP_036202	1 – 95	Missing in isoform 4. 1 PublicationAdd BLAST	95
Alternative sequenceⁱVSP_036203	329 – 344	Missing in isoform 2. 2 PublicationsAdd BLAST	16

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB002389 mRNA Translation: BAA20845.2 Different initiation. BX161394 mRNA Translation: CAD61881.1 BX161487 mRNA Translation: CAD61937.1 AK301931 mRNA Translation: BAG63351.1 AK303508 mRNA Translation: BAG64540.1 AK304066 mRNA Translation: BAG64973.1 AL121594 Genomic DNA No translation available. CH471078 Genomic DNA Translation: EAW65878.1 CH471078 Genomic DNA Translation: EAW65882.1 CH471078 Genomic DNA Translation: EAW65879.1 CH471078 Genomic DNA Translation: EAW65880.1 CH471078 Genomic DNA Translation: EAW65881.1 CH471078 Genomic DNA Translation: EAW65883.1 CH471078 Genomic DNA Translation: EAW65884.1 BC032221 mRNA Translation: AAH32221.1 BC044580 mRNA Translation: AAH44580.1
The Consensus CDS (CCDS) project More...CCDSⁱ	CCDS32063.1 [O15091-1] CCDS58312.1 [O15091-2] CCDS58313.1 [O15091-4] CCDS58314.1 [O15091-3]
NCBI Reference Sequences More...RefSeqⁱ	NP_001243607.1, NM_001256678.1 [O15091-2] NP_001243608.1, NM_001256679.1 [O15091-4] NP_001243609.1, NM_001256680.1 [O15091-3] NP_001243610.1, NM_001256681.1 [O15091-3] NP_055487.2, NM_014672.3 [O15091-1] XP_005268294.1, XM_005268237.3 [O15091-1] XP_011535711.1, XM_011537409.2 XP_011535712.1, XM_011537410.2 [O15091-1] XP_016877324.1, XM_017021835.1 XP_016877325.1, XM_017021836.1 [O15091-2] XP_016877326.1, XM_017021837.1
UniGeneⁱ	Hs.458487 Hs.739309

Genome annotation databases

Ensemblⁱ	ENST00000250377; ENSP00000250377; ENSG00000100890 [O15091-2] ENST00000321130; ENSP00000324697; ENSG00000100890 [O15091-3] ENST00000534898; ENSP00000440915; ENSG00000100890 [O15091-1] ENST00000603544; ENSP00000473856; ENSG00000100890 [O15091-2] ENST00000604948; ENSP00000474620; ENSG00000100890 [O15091-4] ENST00000605870; ENSP00000474299; ENSG00000100890 [O15091-3]
GeneIDⁱ	9692
KEGGⁱ	hsa:9692
UCSC genome browser More...UCSCⁱ	uc001wsy.3 human [O15091-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Protein	Similar proteins		Species	Score	Length	Source
O15091	Mitochondrial ribonuclease P catalytic subunit (Fragment)		HUMAN		34	UniRef100_O15091
KIAA0391 isoform 1 (Fragment)		PANTR		34
Mitochondrial ribonuclease P catalytic subunit (Fragment)		HUMAN		19
Mitochondrial ribonuclease P catalytic subunit (Fragment)		HUMAN		23
Isoform 4 of Mitochondrial ribonuclease P catalytic subunit		HUMAN		488
+3

Protein	Similar proteins		Species	Score	Length	Source
O15091	Mitochondrial ribonuclease P catalytic subunit		MACFA		581	UniRef90_O15091
Mitochondrial ribonuclease P catalytic subunit (Fragment)		HUMAN		34
KIAA0391 isoform 1 (Fragment)		PANTR		34
T0122578 isoform 1		PONAB		583
Uncharacterized protein		PANPA		583
+58

Protein	Similar proteins		Species	Score	Length	Source
O15091	Mitochondrial ribonuclease P catalytic subunit		MACFA		581	UniRef50_O15091
Mitochondrial ribonuclease P catalytic subunit		MOUSE		584
Mitochondrial ribonuclease P catalytic subunit		RAT		587
Mitochondrial ribonuclease P catalytic subunit (Fragment)		HUMAN		34
KIAA0391 isoform 1 (Fragment)		PANTR		34
+237

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB002389 mRNA Translation: BAA20845.2 Different initiation. BX161394 mRNA Translation: CAD61881.1 BX161487 mRNA Translation: CAD61937.1 AK301931 mRNA Translation: BAG63351.1 AK303508 mRNA Translation: BAG64540.1 AK304066 mRNA Translation: BAG64973.1 AL121594 Genomic DNA No translation available. CH471078 Genomic DNA Translation: EAW65878.1 CH471078 Genomic DNA Translation: EAW65882.1 CH471078 Genomic DNA Translation: EAW65879.1 CH471078 Genomic DNA Translation: EAW65880.1 CH471078 Genomic DNA Translation: EAW65881.1 CH471078 Genomic DNA Translation: EAW65883.1 CH471078 Genomic DNA Translation: EAW65884.1 BC032221 mRNA Translation: AAH32221.1 BC044580 mRNA Translation: AAH44580.1
CCDSⁱ	CCDS32063.1 [O15091-1] CCDS58312.1 [O15091-2] CCDS58313.1 [O15091-4] CCDS58314.1 [O15091-3]
RefSeqⁱ	NP_001243607.1, NM_001256678.1 [O15091-2] NP_001243608.1, NM_001256679.1 [O15091-4] NP_001243609.1, NM_001256680.1 [O15091-3] NP_001243610.1, NM_001256681.1 [O15091-3] NP_055487.2, NM_014672.3 [O15091-1] XP_005268294.1, XM_005268237.3 [O15091-1] XP_011535711.1, XM_011537409.2 XP_011535712.1, XM_011537410.2 [O15091-1] XP_016877324.1, XM_017021835.1 XP_016877325.1, XM_017021836.1 [O15091-2] XP_016877326.1, XM_017021837.1
UniGeneⁱ	Hs.458487 Hs.739309

3D structure databases

Select the link destinations: Protein Data Bank Europe More...PDBeⁱ Protein Data Bank RCSB More...RCSB PDBⁱ Protein Data Bank Japan More...PDBjⁱ Links Updated	PDB entry	Method	Resolution (Å)	Chain	Positions	PDBsum
	4ROU	X-ray	2.71	A/B	274-583	[»]
	4XGL	X-ray	1.80	A	207-583	[»]
	4XGM	X-ray	1.98	A	207-583	[»]
ProteinModelPortalⁱ	O15091
SMRⁱ	O15091
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115044, 31 interactors
IntActⁱ	O15091, 6 interactors
MINTⁱ	O15091
STRINGⁱ	9606.ENSP00000454657

PTM databases

iPTMnetⁱ	O15091
PhosphoSitePlusⁱ	O15091

Polymorphism and mutation databases

BioMutaⁱ	KIAA0391

BioMutaⁱ

KIAA0391

Proteomic databases

EPDⁱ	O15091
MaxQBⁱ	O15091
PaxDbⁱ	O15091
PeptideAtlasⁱ	O15091
PRIDEⁱ	O15091
ProteomicsDBⁱ	48444 48445 [O15091-2] 48446 [O15091-3] 48447 [O15091-4]

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000250377; ENSP00000250377; ENSG00000100890 [O15091-2] ENST00000321130; ENSP00000324697; ENSG00000100890 [O15091-3] ENST00000534898; ENSP00000440915; ENSG00000100890 [O15091-1] ENST00000603544; ENSP00000473856; ENSG00000100890 [O15091-2] ENST00000604948; ENSP00000474620; ENSG00000100890 [O15091-4] ENST00000605870; ENSP00000474299; ENSG00000100890 [O15091-3]
GeneIDⁱ	9692
KEGGⁱ	hsa:9692
UCSCⁱ	uc001wsy.3 human [O15091-1]

Organism-specific databases

CTDⁱ	9692
DisGeNETⁱ	9692
EuPathDBⁱ	HostDB:ENSG00000100890.15
GeneCardsⁱ	KIAA0391
H-InvDBⁱ	HIX0018405 HIX0079614
HGNCⁱ	HGNC:19958 KIAA0391
HPAⁱ	HPA020459
MIMⁱ	609947 gene
neXtProtⁱ	NX_O15091
OpenTargetsⁱ	ENSG00000100890
PharmGKBⁱ	PA134879499
HUGEⁱ	Search...
GenAtlas: human gene database More...GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IE4T Eukaryota ENOG4111GT9 LUCA
GeneTreeⁱ	ENSGT00390000002201
HOVERGENⁱ	HBG099441
InParanoidⁱ	O15091
KOⁱ	K17655
OMAⁱ	HDDPFLL
OrthoDBⁱ	EOG091G0JTR
PhylomeDBⁱ	O15091
TreeFamⁱ	TF324726

Enzyme and pathway databases

Reactomeⁱ	R-HSA-6785470 tRNA processing in the mitochondrion R-HSA-6787450 tRNA modification in the mitochondrion R-HSA-8868766 rRNA processing in the mitochondrion

Reactomeⁱ

R-HSA-6785470 tRNA processing in the mitochondrion
R-HSA-6787450 tRNA modification in the mitochondrion
R-HSA-8868766 rRNA processing in the mitochondrion

Miscellaneous databases

ChiTaRSⁱ	KIAA0391 human
GenomeRNAiⁱ	9692
Protein Ontology More...PROⁱ	PR:O15091
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000100890 Expressed in 107 organ(s), highest expression level in leukocyte
CleanExⁱ	HS_KIAA0391
ExpressionAtlasⁱ	O15091 baseline and differential
Genevisibleⁱ	O15091 HS

Family and domain databases

Gene3Dⁱ	1.25.40.10, 1 hit
InterProⁱ	View protein in InterPro IPR033495 MRPP3 IPR031595 PRORP_C IPR011990 TPR-like_helical_dom_sf
PANTHERⁱ	PTHR13547:SF1 PTHR13547:SF1, 1 hit
Pfamⁱ	View protein in Pfam PF16953 PRORP, 1 hit
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ	MRPP3_HUMAN
Accessionⁱ	O15091Primary (citable) accession number: O15091 Secondary accession number(s): B4DXD9 Q8N5L5
Entry historyⁱ	Integrated into UniProtKB/Swiss-Prot:	July 15, 1998
	Last sequence update:	January 20, 2009
	Last modified:	November 7, 2018
	This is version 138 of the entry and version 2 of the sequence. See complete history.
Entry statusⁱ	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.

Miscellaneousⁱ

Keywords - Technical termⁱ

3D-structure, Complete proteome, Reference proteome

Documents

SIMILARITY comments
Index of protein domains and families
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
PDB cross-references
Index of Protein Data Bank (PDB) cross-references
Human chromosome 14
Human chromosome 14: entries, gene names and cross-references to MIM

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UniProtKB - O15091 (MRPP3_HUMAN)

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Mitochondrial ribonuclease P catalytic subunit

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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

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Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

Keywords - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Keywords - PTMⁱ

Expressionⁱ

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Family & Domainsⁱ

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Keywords - Domainⁱ

Sequence cautionⁱ

Keywords - Coding sequence diversityⁱ

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Keywords - Technical termⁱ