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P42704

- LPPRC_HUMAN

UniProt

P42704 - LPPRC_HUMAN

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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

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. RNA binding Source: UniProtKB
  5. 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
Complete GO annotation...

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. nucleus Source: UniProtKB
  8. perinuclear region of cytoplasm Source: HGNC
  9. ribonucleoprotein complex Source: Ensembl
Complete GO annotation...

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-Saint-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

BgeeiP42704.
CleanExiHS_LRPPRC.
ExpressionAtlasiP42704. baseline and differential.
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. 69 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.
GeneTreeiENSGT00390000016775.
HOVERGENiHBG097314.
InParanoidiP42704.
KOiK17964.
OMAiWNKMQEE.
OrthoDBiEOG72JWG1.
PhylomeDBiP42704.
TreeFamiTF323626.

Family and domain databases

Gene3Di1.25.40.10. 4 hits.
InterProiIPR002885. Pentatricopeptide_repeat.
IPR011990. TPR-like_helical_dom.
[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

« Hide

        10         20         30         40         50
MAALLRSARW LLRAGAAPRL PLSLRLLPGG PGRLHAASYL PAARAGPVAG
60 70 80 90 100
GLLSPARLYA IAAKEKDIQE ESTFSSRKIS NQFDWALMRL DLSVRRTGRI
110 120 130 140 150
PKKLLQKVFN DTCRSGGLGG SHALLLLRSC GSLLPELKLE ERTEFAHRIW
160 170 180 190 200
DTLQKLGAVY DVSHYNALLK VYLQNEYKFS PTDFLAKMEE ANIQPNRVTY
210 220 230 240 250
QRLIASYCNV GDIEGASKIL GFMKTKDLPV TEAVFSALVT GHARAGDMEN
260 270 280 290 300
AENILTVMRD AGIEPGPDTY LALLNAYAEK GDIDHVKQTL EKVEKSELHL
310 320 330 340 350
MDRDLLQIIF SFSKAGYPQY VSEILEKVTC ERRYIPDAMN LILLLVTEKL
360 370 380 390 400
EDVALQILLA CPVSKEDGPS VFGSFFLQHC VTMNTPVEKL TDYCKKLKEV
410 420 430 440 450
QMHSFPLQFT LHCALLANKT DLAKALMKAV KEEGFPIRPH YFWPLLVGRR
460 470 480 490 500
KEKNVQGIIE ILKGMQELGV HPDQETYTDY VIPCFDSVNS ARAILQENGC
510 520 530 540 550
LSDSDMFSQA GLRSEAANGN LDFVLSFLKS NTLPISLQSI RSSLLLGFRR
560 570 580 590 600
SMNINLWSEI TELLYKDGRY CQEPRGPTEA VGYFLYNLID SMSDSEVQAK
610 620 630 640 650
EEHLRQYFHQ LEKMNVKIPE NIYRGIRNLL ESYHVPELIK DAHLLVESKN
660 670 680 690 700
LDFQKTVQLT SSELESTLET LKAENQPIRD VLKQLILVLC SEENMQKALE
710 720 730 740 750
LKAKYESDMV TGGYAALINL CCRHDKVEDA LNLKEEFDRL DSSAVLDTGK
760 770 780 790 800
YVGLVRVLAK HGKLQDAINI LKEMKEKDVL IKDTTALSFF HMLNGAALRG
810 820 830 840 850
EIETVKQLHE AIVTLGLAEP STNISFPLVT VHLEKGDLST ALEVAIDCYE
860 870 880 890 900
KYKVLPRIHD VLCKLVEKGE TDLIQKAMDF VSQEQGEMVM LYDLFFAFLQ
910 920 930 940 950
TGNYKEAKKI IETPGIRARS ARLQWFCDRC VANNQVETLE KLVELTQKLF
960 970 980 990 1000
ECDRDQMYYN LLKLYKINGD WQRADAVWNK IQEENVIPRE KTLRLLAEIL
1010 1020 1030 1040 1050
REGNQEVPFD VPELWYEDEK HSLNSSSAST TEPDFQKDIL IACRLNQKKG
1060 1070 1080 1090 1100
AYDIFLNAKE QNIVFNAETY SNLIKLLMSE DYFTQAMEVK AFAETHIKGF
1110 1120 1130 1140 1150
TLNDAANSRL IITQVRRDYL KEAVTTLKTV LDQQQTPSRL AVTRVIQALA
1160 1170 1180 1190 1200
MKGDVENIEV VQKMLNGLED SIGLSKMVFI NNIALAQIKN NNIDAAIENI
1210 1220 1230 1240 1250
ENMLTSENKV IEPQYFGLAY LFRKVIEEQL EPAVEKISIM AERLANQFAI
1260 1270 1280 1290 1300
YKPVTDFFLQ LVDAGKVDDA RALLQRCGAI AEQTPILLLF LLRNSRKQGK
1310 1320 1330 1340 1350
ASTVKSVLEL IPELNEKEEA YNSLMKSYVS EKDVTSAKAL YEHLTAKNTK
1360 1370 1380 1390
LDDLFLKRYA SLLKYAGEPV PFIEPPESFE FYAQQLRKLR ENSS
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. 69 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-Saint-Jean type.
PharmGKBi PA30459.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG292283.
GeneTreei ENSGT00390000016775.
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

Bgeei P42704.
CleanExi HS_LRPPRC.
ExpressionAtlasi P42704. baseline and differential.
Genevestigatori P42704.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  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 29, 2014
This is version 139 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