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P42704

- LPPRC_HUMAN

UniProt

P42704 - LPPRC_HUMAN

Protein

Leucine-rich PPR motif-containing protein, mitochondrial

Gene

LRPPRC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 138 (01 Oct 2014)
      Sequence version 3 (24 Jul 2007)
      Previous versions | rss
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    Functioni

    May play a role in RNA metabolism in both nuclei and mitochondria. In the nucleus binds to HNRPA1-associated poly(A) mRNAs and is part of nmRNP complexes at late stages of mRNA maturation which are possibly associated with nuclear mRNA export. May bind mature mRNA in the nucleus outer membrane. In mitochondria binds to poly(A) mRNA. Plays a role in translation or stability of mitochondrially encoded cytochrome c oxidase (COX) subunits. May be involved in transcription regulation. Cooperates with PPARGC1A to regulate certain mitochondrially encoded genes and gluconeogenic genes and may regulate docking of PPARGC1A to transcription factors. Seems to be involved in the transcription regulation of the multidrug-related genes MDR1 and MVP. Part of a nuclear factor that binds to the invMED1 element of MDR1 and MVP gene promoters. Binds single-stranded DNA By similarity.By similarity

    GO - Molecular functioni

    1. beta-tubulin binding Source: HGNC
    2. microtubule binding Source: HGNC
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: IntAct
    5. RNA binding Source: UniProtKB
    6. single-stranded DNA binding Source: Ensembl

    GO - Biological processi

    1. mitochondrion transport along microtubule Source: HGNC
    2. mRNA transport Source: UniProtKB-KW
    3. negative regulation of mitochondrial RNA catabolic process Source: Ensembl
    4. regulation of mitochondrial translation Source: Ensembl
    5. regulation of transcription, DNA-templated Source: UniProtKB-KW
    6. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Biological processi

    mRNA transport, Transcription, Transcription regulation, Transport

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Leucine-rich PPR motif-containing protein, mitochondrial
    Alternative name(s):
    130 kDa leucine-rich protein
    Short name:
    LRP 130
    GP130
    Gene namesi
    Name:LRPPRC
    Synonyms:LRP130
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 2

    Organism-specific databases

    HGNCiHGNC:15714. LRPPRC.

    Subcellular locationi

    Mitochondrion. Nucleusnucleoplasm. Nucleus inner membrane. Nucleus outer membrane
    Note: Seems to be predominantly mitochondrial.

    GO - Cellular componenti

    1. condensed nuclear chromosome Source: HGNC
    2. cytoskeleton Source: HGNC
    3. membrane Source: UniProtKB
    4. microtubule Source: UniProtKB
    5. mitochondrial nucleoid Source: BHF-UCL
    6. mitochondrion Source: UniProtKB
    7. nuclear inner membrane Source: UniProtKB-SubCell
    8. nuclear outer membrane Source: UniProtKB-SubCell
    9. nucleoplasm Source: UniProtKB-SubCell
    10. nucleus Source: UniProtKB
    11. perinuclear region of cytoplasm Source: HGNC
    12. ribonucleoprotein complex Source: Ensembl

    Keywords - Cellular componenti

    Membrane, Mitochondrion, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Leigh syndrome French-Canadian type (LSFC) [MIM:220111]: Severe neurological disorder characterized by bilaterally symmetrical necrotic lesions in subcortical brain regions that is commonly associated with systemic cytochrome c oxidase (COX) deficiency. In the Saguenay-Lac Saint Jean region of Quebec province in Canada, a biochemically distinct form of Leigh syndrome with COX deficiency has been described. Patients have been observed to have a developmental delay, hypotonia, mild facial dysmorphism, chronic well-compensated metabolic acidosis, and high mortality due to episodes of severe acidosis and coma. Enzyme activity was close to normal in kidney and heart, 50% of normal in fibroblasts and skeletal muscle, and nearly absent in brain and liver. LSFC patients show reduced (<30%) levels of LRPPRC in both fibroblast and liver mitochondria and a specifically reduced translation of COX subunits MT-CO1/COXI and MT-CO3 (COXIII).1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti354 – 3541A → V in LSFC. 1 Publication
    VAR_018656

    Keywords - Diseasei

    Disease mutation, Leigh syndrome

    Organism-specific databases

    MIMi220111. phenotype.
    Orphaneti70472. Congenital lactic acidosis, Saguenay-Lac-St. Jean type.
    PharmGKBiPA30459.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 5959MitochondrionSequence AnalysisAdd
    BLAST
    Chaini60 – 13941335Leucine-rich PPR motif-containing protein, mitochondrialPRO_0000084467Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei155 – 1551N6-acetyllysine1 Publication
    Modified residuei187 – 1871N6-acetyllysine1 Publication
    Modified residuei226 – 2261N6-acetyllysineBy similarity
    Modified residuei292 – 2921N6-acetyllysine1 Publication
    Modified residuei463 – 4631N6-acetyllysineBy similarity
    Modified residuei613 – 6131N6-acetyllysine1 Publication
    Modified residuei726 – 7261N6-acetyllysine1 Publication
    Modified residuei750 – 7501N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    MaxQBiP42704.
    PaxDbiP42704.
    PRIDEiP42704.

    Expressioni

    Tissue specificityi

    Expressed ubiquitously. Expression is highest in heart, skeletal muscle, kidney and liver, intermediate in brain, non-mucosal colon, spleen and placenta, and lowest in small intestine, thymus, lung and peripheral blood leukocytes.2 Publications

    Gene expression databases

    ArrayExpressiP42704.
    BgeeiP42704.
    CleanExiHS_LRPPRC.
    GenevestigatoriP42704.

    Organism-specific databases

    HPAiHPA036408.
    HPA036409.

    Interactioni

    Subunit structurei

    Interacts with CECR2, HEBP2, MAP1S and UXT. Interacts with PPARGC1A. Interacts with FOXO1 By similarity. Component of mRNP complexes associated with HNRPA1.By similarity4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    EIF4EP067306EBI-1050853,EBI-73440
    PPARGC1AQ9UBK22EBI-1050853,EBI-765486

    Protein-protein interaction databases

    BioGridi115432. 58 interactions.
    DIPiDIP-27543N.
    IntActiP42704. 28 interactions.
    MINTiMINT-205076.
    STRINGi9606.ENSP00000260665.

    Structurei

    3D structure databases

    ProteinModelPortaliP42704.
    SMRiP42704. Positions 72-326.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati126 – 16035PPR 1Add
    BLAST
    Repeati161 – 19535PPR 2Add
    BLAST
    Repeati196 – 23035PPR 3Add
    BLAST
    Repeati231 – 26535PPR 4Add
    BLAST
    Repeati266 – 30035PPR 5Add
    BLAST
    Repeati301 – 33535PPR 6Add
    BLAST
    Repeati403 – 43735PPR 7Add
    BLAST
    Repeati438 – 47235PPR 8Add
    BLAST
    Repeati678 – 70932PPR 9Add
    BLAST
    Repeati710 – 74637PPR 10Add
    BLAST
    Repeati747 – 78438PPR 11Add
    BLAST
    Repeati785 – 82036PPR 12Add
    BLAST
    Repeati821 – 85636PPR 13Add
    BLAST
    Repeati954 – 98835PPR 14Add
    BLAST
    Repeati1031 – 106535PPR 15Add
    BLAST
    Repeati1066 – 110237PPR 16Add
    BLAST
    Repeati1103 – 113735PPR 17Add
    BLAST
    Repeati1138 – 117538PPR 18Add
    BLAST
    Repeati1176 – 121035PPR 19Add
    BLAST
    Repeati1317 – 135135PPR 20Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1121 – 1394274RNA-bindingAdd
    BLAST

    Sequence similaritiesi

    Contains 20 PPR (pentatricopeptide) repeats.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Transit peptide

    Phylogenomic databases

    eggNOGiNOG292283.
    HOVERGENiHBG097314.
    InParanoidiP42704.
    KOiK17964.
    OMAiWNKMQEE.
    OrthoDBiEOG72JWG1.
    PhylomeDBiP42704.
    TreeFamiTF323626.

    Family and domain databases

    Gene3Di1.25.40.10. 4 hits.
    InterProiIPR002885. Pentatricopeptide_repeat.
    IPR011990. TPR-like_helical.
    [Graphical view]
    PfamiPF01535. PPR. 6 hits.
    [Graphical view]
    TIGRFAMsiTIGR00756. PPR. 2 hits.
    PROSITEiPS51375. PPR. 11 hits.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P42704-1 [UniParc]FASTAAdd to Basket

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    MAALLRSARW LLRAGAAPRL PLSLRLLPGG PGRLHAASYL PAARAGPVAG     50
    GLLSPARLYA IAAKEKDIQE ESTFSSRKIS NQFDWALMRL DLSVRRTGRI 100
    PKKLLQKVFN DTCRSGGLGG SHALLLLRSC GSLLPELKLE ERTEFAHRIW 150
    DTLQKLGAVY DVSHYNALLK VYLQNEYKFS PTDFLAKMEE ANIQPNRVTY 200
    QRLIASYCNV GDIEGASKIL GFMKTKDLPV TEAVFSALVT GHARAGDMEN 250
    AENILTVMRD AGIEPGPDTY LALLNAYAEK GDIDHVKQTL EKVEKSELHL 300
    MDRDLLQIIF SFSKAGYPQY VSEILEKVTC ERRYIPDAMN LILLLVTEKL 350
    EDVALQILLA CPVSKEDGPS VFGSFFLQHC VTMNTPVEKL TDYCKKLKEV 400
    QMHSFPLQFT LHCALLANKT DLAKALMKAV KEEGFPIRPH YFWPLLVGRR 450
    KEKNVQGIIE ILKGMQELGV HPDQETYTDY VIPCFDSVNS ARAILQENGC 500
    LSDSDMFSQA GLRSEAANGN LDFVLSFLKS NTLPISLQSI RSSLLLGFRR 550
    SMNINLWSEI TELLYKDGRY CQEPRGPTEA VGYFLYNLID SMSDSEVQAK 600
    EEHLRQYFHQ LEKMNVKIPE NIYRGIRNLL ESYHVPELIK DAHLLVESKN 650
    LDFQKTVQLT SSELESTLET LKAENQPIRD VLKQLILVLC SEENMQKALE 700
    LKAKYESDMV TGGYAALINL CCRHDKVEDA LNLKEEFDRL DSSAVLDTGK 750
    YVGLVRVLAK HGKLQDAINI LKEMKEKDVL IKDTTALSFF HMLNGAALRG 800
    EIETVKQLHE AIVTLGLAEP STNISFPLVT VHLEKGDLST ALEVAIDCYE 850
    KYKVLPRIHD VLCKLVEKGE TDLIQKAMDF VSQEQGEMVM LYDLFFAFLQ 900
    TGNYKEAKKI IETPGIRARS ARLQWFCDRC VANNQVETLE KLVELTQKLF 950
    ECDRDQMYYN LLKLYKINGD WQRADAVWNK IQEENVIPRE KTLRLLAEIL 1000
    REGNQEVPFD VPELWYEDEK HSLNSSSAST TEPDFQKDIL IACRLNQKKG 1050
    AYDIFLNAKE QNIVFNAETY SNLIKLLMSE DYFTQAMEVK AFAETHIKGF 1100
    TLNDAANSRL IITQVRRDYL KEAVTTLKTV LDQQQTPSRL AVTRVIQALA 1150
    MKGDVENIEV VQKMLNGLED SIGLSKMVFI NNIALAQIKN NNIDAAIENI 1200
    ENMLTSENKV IEPQYFGLAY LFRKVIEEQL EPAVEKISIM AERLANQFAI 1250
    YKPVTDFFLQ LVDAGKVDDA RALLQRCGAI AEQTPILLLF LLRNSRKQGK 1300
    ASTVKSVLEL IPELNEKEEA YNSLMKSYVS EKDVTSAKAL YEHLTAKNTK 1350
    LDDLFLKRYA SLLKYAGEPV PFIEPPESFE FYAQQLRKLR ENSS 1394
    Length:1,394
    Mass (Da):157,905
    Last modified:July 24, 2007 - v3
    Checksum:i61AB0C8BF8A972E6
    GO

    Sequence cautioni

    The sequence AAA67549.1 differs from that shown. Reason: Frameshift at several positions.
    The sequence AAA67549.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti54 – 541S → G in BAF82705. (PubMed:14702039)Curated
    Sequence conflicti296 – 2961S → F in AAA67549. (PubMed:8012652)Curated
    Sequence conflicti528 – 5314LKSN → YFPI in AAH26034. (PubMed:15489334)Curated
    Sequence conflicti556 – 5561L → V in AAA67549. (PubMed:8012652)Curated
    Sequence conflicti583 – 5831Y → N in AAA67549. (PubMed:8012652)Curated
    Sequence conflicti648 – 6481S → R in AAA67549. (PubMed:8012652)Curated
    Sequence conflicti676 – 6761Q → R in BAC86287. (PubMed:14702039)Curated
    Sequence conflicti702 – 7021K → R in BAC86287. (PubMed:14702039)Curated
    Sequence conflicti750 – 7523KYV → NYL in AAA67549. (PubMed:8012652)Curated
    Sequence conflicti769 – 7691N → K in AAA67549. (PubMed:8012652)Curated
    Sequence conflicti1192 – 11921N → D in BAC86287. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti354 – 3541A → V in LSFC. 1 Publication
    VAR_018656
    Natural varianti478 – 4781T → A.
    Corresponds to variant rs35035668 [ dbSNP | Ensembl ].
    VAR_052935

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY289212 mRNA. Translation: AAP41922.1.
    AK125781 mRNA. Translation: BAC86287.1.
    AK290016 mRNA. Translation: BAF82705.1.
    AC108476 Genomic DNA. Translation: AAY24012.1.
    AC127379 Genomic DNA. Translation: AAY24043.1.
    BC010282 mRNA. Translation: AAH10282.1.
    BC026034 mRNA. Translation: AAH26034.1.
    BC050311 mRNA. Translation: AAH50311.1.
    BC130285 mRNA. Translation: AAI30286.1.
    M92439 mRNA. Translation: AAA67549.1. Sequence problems.
    CCDSiCCDS33189.1.
    PIRiS27954.
    RefSeqiNP_573566.2. NM_133259.3.
    UniGeneiHs.368084.

    Genome annotation databases

    EnsembliENST00000260665; ENSP00000260665; ENSG00000138095.
    ENST00000409946; ENSP00000386234; ENSG00000138095.
    GeneIDi10128.
    KEGGihsa:10128.
    UCSCiuc002rtr.2. human.

    Polymorphism databases

    DMDMi156632706.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AY289212 mRNA. Translation: AAP41922.1 .
    AK125781 mRNA. Translation: BAC86287.1 .
    AK290016 mRNA. Translation: BAF82705.1 .
    AC108476 Genomic DNA. Translation: AAY24012.1 .
    AC127379 Genomic DNA. Translation: AAY24043.1 .
    BC010282 mRNA. Translation: AAH10282.1 .
    BC026034 mRNA. Translation: AAH26034.1 .
    BC050311 mRNA. Translation: AAH50311.1 .
    BC130285 mRNA. Translation: AAI30286.1 .
    M92439 mRNA. Translation: AAA67549.1 . Sequence problems.
    CCDSi CCDS33189.1.
    PIRi S27954.
    RefSeqi NP_573566.2. NM_133259.3.
    UniGenei Hs.368084.

    3D structure databases

    ProteinModelPortali P42704.
    SMRi P42704. Positions 72-326.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115432. 58 interactions.
    DIPi DIP-27543N.
    IntActi P42704. 28 interactions.
    MINTi MINT-205076.
    STRINGi 9606.ENSP00000260665.

    Polymorphism databases

    DMDMi 156632706.

    Proteomic databases

    MaxQBi P42704.
    PaxDbi P42704.
    PRIDEi P42704.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000260665 ; ENSP00000260665 ; ENSG00000138095 .
    ENST00000409946 ; ENSP00000386234 ; ENSG00000138095 .
    GeneIDi 10128.
    KEGGi hsa:10128.
    UCSCi uc002rtr.2. human.

    Organism-specific databases

    CTDi 10128.
    GeneCardsi GC02M044113.
    H-InvDB HIX0023918.
    HGNCi HGNC:15714. LRPPRC.
    HPAi HPA036408.
    HPA036409.
    MIMi 220111. phenotype.
    607544. gene.
    neXtProti NX_P42704.
    Orphaneti 70472. Congenital lactic acidosis, Saguenay-Lac-St. Jean type.
    PharmGKBi PA30459.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG292283.
    HOVERGENi HBG097314.
    InParanoidi P42704.
    KOi K17964.
    OMAi WNKMQEE.
    OrthoDBi EOG72JWG1.
    PhylomeDBi P42704.
    TreeFami TF323626.

    Miscellaneous databases

    ChiTaRSi LRPPRC. human.
    GeneWikii LRPPRC.
    GenomeRNAii 10128.
    NextBioi 38311.
    PROi P42704.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P42704.
    Bgeei P42704.
    CleanExi HS_LRPPRC.
    Genevestigatori P42704.

    Family and domain databases

    Gene3Di 1.25.40.10. 4 hits.
    InterProi IPR002885. Pentatricopeptide_repeat.
    IPR011990. TPR-like_helical.
    [Graphical view ]
    Pfami PF01535. PPR. 6 hits.
    [Graphical view ]
    TIGRFAMsi TIGR00756. PPR. 2 hits.
    PROSITEi PS51375. PPR. 11 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The role of the LRPPRC (leucine-rich pentatricopeptide repeat cassette) gene in cytochrome oxidase assembly: mutation causes lowered levels of COX (cytochrome c oxidase) I and COX III mRNA."
      Xu F., Morin C., Mitchell G., Ackerley C., Robinson B.H.
      Biochem. J. 382:331-336(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION IN COX ASSEMBLY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    2. "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: Hippocampus and Testis.
    3. "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].
    4. "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: Brain, Muscle, Placenta and Testis.
    5. "Molecular cloning and expression of the gene for a major leucine-rich protein from human hepatoblastoma cells (HepG2)."
      Hou J., Wang F., McKeehan W.L.
      In Vitro Cell. Dev. Biol. Anim. 30A:111-114(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 108-1394.
      Tissue: Liver.
    6. Bienvenut W.V., Heiserich L., Boulahbel H., Gottlieb E.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 156-170; 260-280; 304-314; 454-463; 530-541; 656-672; 740-750; 764-772; 1050-1059; 1091-1098; 1177-1189 AND 1339-1347, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: B-cell lymphoma and Colon carcinoma.
    7. "Distinct RNP complexes of shuttling hnRNP proteins with pre-mRNA and mRNA: candidate intermediates in formation and export of mRNA."
      Mili S., Shu H.J., Zhao Y., Pinol-Roma S.
      Mol. Cell. Biol. 21:7307-7319(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA EXPORT, IDENTIFICATION IN NMRNP COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY.
    8. "Sequence analysis of LRPPRC and its SEC1 domain interaction partners suggests roles in cytoskeletal organization, vesicular trafficking, nucleocytosolic shuttling, and chromosome activity."
      Liu L., McKeehan W.L.
      Genomics 79:124-136(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY, INTERACTION WITH CECR2; HEBP2; MAP1S AND UXT.
    9. "LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, is bound in vivo to mitochondrial and nuclear RNAs."
      Mili S., Pinol-Roma S.
      Mol. Cell. Biol. 23:4972-4982(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: RNA-BINDING, FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION.
    10. "LRP130, a single-stranded DNA/RNA-binding protein, localizes at the outer nuclear and endoplasmic reticulum membrane, and interacts with mRNA in vivo."
      Tsuchiya N., Fukuda H., Nakashima K., Nagao M., Sugimura T., Nakagama H.
      Biochem. Biophys. Res. Commun. 317:736-743(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN MRNA EXPORT, SUBCELLULAR LOCATION.
    11. "New invMED1 element cis-activates human multidrug-related MDR1 and MVP genes, involving the LRP130 protein."
      Labialle S., Dayan G., Gayet L., Rigal D., Gambrelle J., Baggetto L.G.
      Nucleic Acids Res. 32:3864-3876(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION REGULATION, IDENTIFICATION BY MASS SPECTROMETRY, SUBCELLULAR LOCATION.
    12. "Putative tumor suppressor RASSF1 interactive protein and cell death inducer C19ORF5 is a DNA binding protein."
      Liu L., Vo A., Liu G., McKeehan W.L.
      Biochem. Biophys. Res. Commun. 332:670-676(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH MAP1S.
    13. "Defects in energy homeostasis in Leigh syndrome French Canadian variant through PGC-1alpha/LRP130 complex."
      Cooper M.P., Qu L., Rohas L.M., Lin J., Yang W., Erdjument-Bromage H., Tempst P., Spiegelman B.M.
      Genes Dev. 20:2996-3009(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTION REGULATION, INTERACTION WITH PPARGC1A.
    14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-155; LYS-187; LYS-292; LYS-613; LYS-726 AND LYS-750, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. Cited for: VARIANT LSFC VAL-354.

    Entry informationi

    Entry nameiLPPRC_HUMAN
    AccessioniPrimary (citable) accession number: P42704
    Secondary accession number(s): A0PJE3
    , A8K1V1, Q53PC0, Q53QN7, Q6ZUD8, Q7Z7A6, Q96D84
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1995
    Last sequence update: July 24, 2007
    Last modified: October 1, 2014
    This is version 138 of the entry and version 3 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 2
      Human chromosome 2: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3