Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

39S ribosomal protein L17, mitochondrial

Gene

MRPL17

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

Functioni

GO - Molecular functioni

  1. protein domain specific binding Source: UniProtKB
  2. structural constituent of ribosome Source: GO_Central

GO - Biological processi

  1. mitochondrial genome maintenance Source: GO_Central
  2. mitochondrial translation Source: Reactome
  3. mitochondrial translational elongation Source: Reactome
  4. mitochondrial translational initiation Source: Reactome
  5. mitochondrial translational termination Source: Reactome
  6. 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 L17, mitochondrial
Short name:
L17mt
Short name:
MRP-L17
Alternative name(s):
LYST-interacting protein 2
Gene namesi
Name:MRPL17
Synonyms:LIP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 11

Organism-specific databases

HGNCiHGNC:14053. MRPL17.

Subcellular locationi

GO - Cellular componenti

  1. mitochondrial inner membrane Source: Reactome
  2. mitochondrial large ribosomal subunit Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30946.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 88MitochondrionBy similarity
Chaini9 – 17516739S ribosomal protein L17, mitochondrialPRO_0000237331Add
BLAST

Proteomic databases

MaxQBiQ9NRX2.
PaxDbiQ9NRX2.
PeptideAtlasiQ9NRX2.
PRIDEiQ9NRX2.

PTM databases

PhosphoSiteiQ9NRX2.

Expressioni

Tissue specificityi

Detected in adrenal gland, mammary gland and adipose tissue.1 Publication

Gene expression databases

BgeeiQ9NRX2.
CleanExiHS_MRPL17.
ExpressionAtlasiQ9NRX2. baseline and differential.
GenevestigatoriQ9NRX2.

Organism-specific databases

HPAiHPA043666.
HPA050552.

Interactioni

Protein-protein interaction databases

BioGridi121968. 20 interactions.
IntActiQ9NRX2. 2 interactions.
MINTiMINT-3064942.
STRINGi9606.ENSP00000288937.

Structurei

Secondary structure

1
175
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi28 – 3811Combined sources
Beta strandi41 – 455Combined sources
Helixi46 – 6520Combined sources
Helixi70 – 7910Combined sources
Helixi85 – 906Combined sources
Helixi93 – 997Combined sources
Beta strandi105 – 1106Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi120 – 1278Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQMNMR-A28-136[»]
3J7Yelectron microscopy3.40O1-175[»]
ProteinModelPortaliQ9NRX2.
SMRiQ9NRX2. Positions 28-129.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NRX2.

Family & Domainsi

Sequence similaritiesi

Belongs to the ribosomal protein L17P family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiCOG0203.
GeneTreeiENSGT00390000010698.
HOGENOMiHOG000019780.
HOVERGENiHBG056029.
InParanoidiQ9NRX2.
KOiK02879.
OMAiRYEDRQG.
OrthoDBiEOG74TX11.
PhylomeDBiQ9NRX2.
TreeFamiTF105844.

Family and domain databases

Gene3Di3.90.1030.10. 1 hit.
InterProiIPR000456. Ribosomal_L17.
[Graphical view]
PANTHERiPTHR14413. PTHR14413. 1 hit.
PfamiPF01196. Ribosomal_L17. 1 hit.
[Graphical view]
SUPFAMiSSF64263. SSF64263. 1 hit.
TIGRFAMsiTIGR00059. L17. 1 hit.

Sequencei

Sequence statusi: Complete.

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

Q9NRX2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRLSVAAAIS HGRVFRRMGL GPESRIHLLR NLLTGLVRHE RIEAPWARVD
60 70 80 90 100
EMRGYAEKLI DYGKLGDTNE RAMRMADFWL TEKDLIPKLF QVLAPRYKDQ
110 120 130 140 150
TGGYTRMLQI PNRSLDRAKM AVIEYKGNCL PPLPLPRRDS HLTLLNQLLQ
160 170
GLRQDLRQSQ EASNHSSHTA QTPGI
Length:175
Mass (Da):20,050
Last modified:October 1, 2000 - v1
Checksum:i48C73425104200EA
GO

Sequence cautioni

The sequence AAG49441.1 differs from that shown. Reason: Frameshift at position 8. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti105 – 1051T → A in CAG33458 (PubMed:11984006).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164797 mRNA. Translation: AAF80761.1.
AF141338 mRNA. Translation: AAG49441.1. Frameshift.
AK026857 mRNA. Translation: BAB15575.1.
CR457177 mRNA. Translation: CAG33458.1.
CH471064 Genomic DNA. Translation: EAW68681.1.
CH471064 Genomic DNA. Translation: EAW68682.1.
BC012306 mRNA. Translation: AAH12306.1.
AB051620 Genomic DNA. Translation: BAB54948.1.
CCDSiCCDS31412.1.
RefSeqiNP_071344.1. NM_022061.3.
UniGeneiHs.523456.
Hs.708782.

Genome annotation databases

EnsembliENST00000288937; ENSP00000288937; ENSG00000158042.
GeneIDi63875.
KEGGihsa:63875.
UCSCiuc001men.2. human.

Polymorphism databases

DMDMi74752931.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164797 mRNA. Translation: AAF80761.1.
AF141338 mRNA. Translation: AAG49441.1. Frameshift.
AK026857 mRNA. Translation: BAB15575.1.
CR457177 mRNA. Translation: CAG33458.1.
CH471064 Genomic DNA. Translation: EAW68681.1.
CH471064 Genomic DNA. Translation: EAW68682.1.
BC012306 mRNA. Translation: AAH12306.1.
AB051620 Genomic DNA. Translation: BAB54948.1.
CCDSiCCDS31412.1.
RefSeqiNP_071344.1. NM_022061.3.
UniGeneiHs.523456.
Hs.708782.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2CQMNMR-A28-136[»]
3J7Yelectron microscopy3.40O1-175[»]
ProteinModelPortaliQ9NRX2.
SMRiQ9NRX2. Positions 28-129.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121968. 20 interactions.
IntActiQ9NRX2. 2 interactions.
MINTiMINT-3064942.
STRINGi9606.ENSP00000288937.

PTM databases

PhosphoSiteiQ9NRX2.

Polymorphism databases

DMDMi74752931.

Proteomic databases

MaxQBiQ9NRX2.
PaxDbiQ9NRX2.
PeptideAtlasiQ9NRX2.
PRIDEiQ9NRX2.

Protocols and materials databases

DNASUi63875.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000288937; ENSP00000288937; ENSG00000158042.
GeneIDi63875.
KEGGihsa:63875.
UCSCiuc001men.2. human.

Organism-specific databases

CTDi63875.
GeneCardsiGC11M006659.
HGNCiHGNC:14053. MRPL17.
HPAiHPA043666.
HPA050552.
MIMi611830. gene.
neXtProtiNX_Q9NRX2.
PharmGKBiPA30946.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0203.
GeneTreeiENSGT00390000010698.
HOGENOMiHOG000019780.
HOVERGENiHBG056029.
InParanoidiQ9NRX2.
KOiK02879.
OMAiRYEDRQG.
OrthoDBiEOG74TX11.
PhylomeDBiQ9NRX2.
TreeFamiTF105844.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTraceiQ9NRX2.
GeneWikiiMRPL17.
GenomeRNAii63875.
NextBioi65556.
PROiQ9NRX2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9NRX2.
CleanExiHS_MRPL17.
ExpressionAtlasiQ9NRX2. baseline and differential.
GenevestigatoriQ9NRX2.

Family and domain databases

Gene3Di3.90.1030.10. 1 hit.
InterProiIPR000456. Ribosomal_L17.
[Graphical view]
PANTHERiPTHR14413. PTHR14413. 1 hit.
PfamiPF01196. Ribosomal_L17. 1 hit.
[Graphical view]
SUPFAMiSSF64263. SSF64263. 1 hit.
TIGRFAMsiTIGR00059. L17. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], TISSUE SPECIFICITY.
    Tissue: Adrenal gland.
  2. "The Chediak-Higashi protein interacts with SNARE complex and signal transduction proteins."
    Tchernev V.T., Mansfield T.A., Giot L., Kumar A.M., Nandabalan K., Li Y., Mishra V.S., Detter J.C., Rothberg J.M., Wallace M.R., Southwick F.S., Kingsmore S.F.
    Mol. Med. 8:56-64(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  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].
    Tissue: Adipose tissue.
  4. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. 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].
    Tissue: Mammary gland.
  7. "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 144-175.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. "Solution structure of the mitochondrial ribosomal protein L17 isolog."
    RIKEN structural genomics initiative (RSGI)
    Submitted (NOV-2005) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 28-136.

Entry informationi

Entry nameiRM17_HUMAN
AccessioniPrimary (citable) accession number: Q9NRX2
Secondary accession number(s): D3DQU3
, Q6IAH8, Q96Q53, Q9C066
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: October 1, 2000
Last modified: March 4, 2015
This is version 109 of the entry and version 1 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 11
    Human chromosome 11: 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.