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Protein

39S ribosomal protein L19, mitochondrial

Gene

MRPL19

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

  1. structural constituent of ribosome Source: InterPro

GO - Biological processi

  1. mitochondrial translation Source: Reactome
  2. mitochondrial translational elongation Source: Reactome
  3. mitochondrial translational initiation Source: Reactome
  4. mitochondrial translational termination Source: Reactome
  5. organelle organization Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Ribonucleoprotein, Ribosomal protein

Enzyme and pathway databases

ReactomeiREACT_267602. Mitochondrial translation termination.
REACT_267677. Mitochondrial translation elongation.
REACT_267680. Mitochondrial translation initiation.

Names & Taxonomyi

Protein namesi
Recommended name:
39S ribosomal protein L19, mitochondrial
Short name:
L19mt
Short name:
MRP-L19
Alternative name(s):
39S ribosomal protein L15, mitochondrial
Short name:
L15mt
Short name:
MRP-L15
Gene namesi
Name:MRPL19
Synonyms:KIAA0104, MRPL15
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:14052. MRPL19.

Subcellular locationi

Mitochondrion 2 Publications

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. nuclear membrane Source: UniProtKB
  3. nucleus Source: UniProtKB
  4. ribosome Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30948.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 29239S ribosomal protein L19, mitochondrialPRO_0000030473
Transit peptidei1 – ?MitochondrionSequence Analysis

Proteomic databases

MaxQBiP49406.
PaxDbiP49406.
PRIDEiP49406.

PTM databases

PhosphoSiteiP49406.

Expressioni

Gene expression databases

BgeeiP49406.
CleanExiHS_MRPL15.
HS_MRPL19.
ExpressionAtlasiP49406. baseline and differential.
GenevestigatoriP49406.

Organism-specific databases

HPAiHPA056622.

Interactioni

Protein-protein interaction databases

BioGridi115142. 41 interactions.
IntActiP49406. 7 interactions.
MINTiMINT-6492165.
STRINGi9606.ENSP00000377486.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40Q1-292[»]
ProteinModelPortaliP49406.
SMRiP49406. Positions 71-292.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L19P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0335.
GeneTreeiENSGT00390000009415.
HOGENOMiHOG000020439.
HOVERGENiHBG023932.
InParanoidiP49406.
KOiK02884.
OMAiICIQRGG.
OrthoDBiEOG7GXPCC.
PhylomeDBiP49406.
TreeFamiTF320270.

Family and domain databases

InterProiIPR001857. Ribosomal_L19.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR15680. PTHR15680. 1 hit.
PfamiPF01245. Ribosomal_L19. 1 hit.
[Graphical view]
PRINTSiPR00061. RIBOSOMALL19.
SUPFAMiSSF50104. SSF50104. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P49406-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAACIAAGHW AAMGLGRSFQ AARTLLPPPA SIACRVHAGP VRQQSTGPSE
60 70 80 90 100
PGAFQPPPKP VIVDKHRPVE PERRFLSPEF IPRRGRTDPL KFQIERKDML
110 120 130 140 150
ERRKVLHIPE FYVGSILRVT TADPYASGKI SQFLGICIQR SGRGLGATFI
160 170 180 190 200
LRNVIEGQGV EICFELYNPR VQEIQVVKLE KRLDDSLLYL RDALPEYSTF
210 220 230 240 250
DVNMKPVVQE PNQKVPVNEL KVKMKPKPWS KRWERPNFNI KGIRFDLCLT
260 270 280 290
EQQMKEAQKW NQPWLEFDMM REYDTSKIEA AIWKEIEASK RS
Length:292
Mass (Da):33,535
Last modified:April 4, 2006 - v2
Checksum:i4056F39694284A9F
GO

Sequence cautioni

The sequence AAY14972.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA03494.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005034 Genomic DNA. Translation: AAY14972.1. Different initiation.
BC030144 mRNA. Translation: AAH30144.2.
D14660 mRNA. Translation: BAA03494.1. Different initiation.
AB051621 Genomic DNA. Translation: BAB54949.1.
CCDSiCCDS1960.2.
RefSeqiNP_055578.2. NM_014763.3.
UniGeneiHs.44024.

Genome annotation databases

EnsembliENST00000393909; ENSP00000377486; ENSG00000115364.
ENST00000409374; ENSP00000387284; ENSG00000115364.
GeneIDi9801.
KEGGihsa:9801.
UCSCiuc002snl.3. human.

Polymorphism databases

DMDMi92090636.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC005034 Genomic DNA. Translation: AAY14972.1. Different initiation.
BC030144 mRNA. Translation: AAH30144.2.
D14660 mRNA. Translation: BAA03494.1. Different initiation.
AB051621 Genomic DNA. Translation: BAB54949.1.
CCDSiCCDS1960.2.
RefSeqiNP_055578.2. NM_014763.3.
UniGeneiHs.44024.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3J7Yelectron microscopy3.40Q1-292[»]
ProteinModelPortaliP49406.
SMRiP49406. Positions 71-292.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115142. 41 interactions.
IntActiP49406. 7 interactions.
MINTiMINT-6492165.
STRINGi9606.ENSP00000377486.

PTM databases

PhosphoSiteiP49406.

Polymorphism databases

DMDMi92090636.

Proteomic databases

MaxQBiP49406.
PaxDbiP49406.
PRIDEiP49406.

Protocols and materials databases

DNASUi9801.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000393909; ENSP00000377486; ENSG00000115364.
ENST00000409374; ENSP00000387284; ENSG00000115364.
GeneIDi9801.
KEGGihsa:9801.
UCSCiuc002snl.3. human.

Organism-specific databases

CTDi9801.
GeneCardsiGC02P075873.
HGNCiHGNC:14052. MRPL19.
HPAiHPA056622.
MIMi611832. gene.
neXtProtiNX_P49406.
PharmGKBiPA30948.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0335.
GeneTreeiENSGT00390000009415.
HOGENOMiHOG000020439.
HOVERGENiHBG023932.
InParanoidiP49406.
KOiK02884.
OMAiICIQRGG.
OrthoDBiEOG7GXPCC.
PhylomeDBiP49406.
TreeFamiTF320270.

Enzyme and pathway databases

ReactomeiREACT_267602. Mitochondrial translation termination.
REACT_267677. Mitochondrial translation elongation.
REACT_267680. Mitochondrial translation initiation.

Miscellaneous databases

ChiTaRSiMRPL19. human.
GeneWikiiMRPL19.
GenomeRNAii9801.
NextBioi36904.
PROiP49406.
SOURCEiSearch...

Gene expression databases

BgeeiP49406.
CleanExiHS_MRPL15.
HS_MRPL19.
ExpressionAtlasiP49406. baseline and differential.
GenevestigatoriP49406.

Family and domain databases

InterProiIPR001857. Ribosomal_L19.
IPR008991. Translation_prot_SH3-like.
[Graphical view]
PANTHERiPTHR15680. PTHR15680. 1 hit.
PfamiPF01245. Ribosomal_L19. 1 hit.
[Graphical view]
PRINTSiPR00061. RIBOSOMALL19.
SUPFAMiSSF50104. SSF50104. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [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].
    Tissue: B-cell.
  3. "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1."
    Nagase T., Miyajima N., Tanaka A., Sazuka T., Seki N., Sato S., Tabata S., Ishikawa K., Kawarabayasi Y., Kotani H., Nomura N.
    DNA Res. 2:37-43(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2-292.
    Tissue: Bone marrow.
  4. "The human mitochondrial ribosomal protein genes: mapping of 54 genes to the chromosomes and implications for human disorders."
    Kenmochi N., Suzuki T., Uechi T., Magoori M., Kuniba M., Higa S., Watanabe K., Tanaka T.
    Genomics 77:65-70(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 257-292, SUBCELLULAR LOCATION.
  5. "Identification of mammalian mitochondrial ribosomal proteins (MRPs) by N-terminal sequencing of purified bovine MRPs and comparison to data bank sequences: the large subribosomal particle."
    Graack H.R., Bryant M.L., O'Brien T.W.
    Biochemistry 38:16569-16577(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION AS A RIBOSOMAL PROTEIN, SUBCELLULAR LOCATION.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiRM19_HUMAN
AccessioniPrimary (citable) accession number: P49406
Secondary accession number(s): Q53TX9, Q96Q52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1996
Last sequence update: April 4, 2006
Last modified: March 4, 2015
This is version 130 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Ribosomal proteins
    Ribosomal proteins families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.