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P42704 (LPPRC_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Leucine-rich PPR motif-containing protein, mitochondrial
Alternative name(s):
130 kDa leucine-rich protein
Short name=LRP 130
GP130
Gene names
Name:LRPPRC
Synonyms:LRP130
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1394 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.7 Ref.9 Ref.10 Ref.11 Ref.13

Subunit structure

Interacts with CECR2, HEBP2, MAP1S and UXT. Interacts with PPARGC1A. Interacts with FOXO1 By similarity. Component of mRNP complexes associated with HNRPA1. Ref.7 Ref.8 Ref.12 Ref.13

Subcellular location

Mitochondrion. Nucleusnucleoplasm. Nucleus inner membrane. Nucleus outer membrane. Note: Seems to be predominantly mitochondrial. Ref.1 Ref.9 Ref.10 Ref.11

Tissue specificity

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. Ref.1 Ref.8

Involvement in disease

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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.16

Sequence similarities

Contains 20 PPR (pentatricopeptide) repeats.

Sequence caution

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

The sequence AAA67549.1 differs from that shown. Reason: Frameshift at several positions.

Ontologies

Keywords
   Biological processmRNA transport
Transcription
Transcription regulation
Transport
   Cellular componentMembrane
Mitochondrion
Nucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Leigh syndrome
   DomainRepeat
Transit peptide
   LigandDNA-binding
RNA-binding
   PTMAcetylation
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processmRNA transport

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion transport along microtubule

Traceable author statement PubMed 12762840. Source: HGNC

negative regulation of mitochondrial RNA catabolic process

Inferred from electronic annotation. Source: Ensembl

regulation of mitochondrial translation

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcondensed nuclear chromosome

Inferred from direct assay PubMed 12762840. Source: HGNC

microtubule

Inferred from direct assay PubMed 21525035. Source: UniProtKB

mitochondrial nucleoid

Inferred from direct assay PubMed 18063578. Source: BHF-UCL

nuclear inner membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from direct assay PubMed 12762840. Source: HGNC

ribonucleoprotein complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRNA binding

Non-traceable author statement Ref.9. Source: UniProtKB

beta-tubulin binding

Inferred from direct assay PubMed 12762840. Source: HGNC

microtubule binding

Traceable author statement PubMed 12762840. Source: HGNC

single-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

EIF4EP067306EBI-1050853,EBI-73440
PPARGC1AQ9UBK22EBI-1050853,EBI-765486

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 5959Mitochondrion Potential
Chain60 – 13941335Leucine-rich PPR motif-containing protein, mitochondrial
PRO_0000084467

Regions

Repeat126 – 16035PPR 1
Repeat161 – 19535PPR 2
Repeat196 – 23035PPR 3
Repeat231 – 26535PPR 4
Repeat266 – 30035PPR 5
Repeat301 – 33535PPR 6
Repeat403 – 43735PPR 7
Repeat438 – 47235PPR 8
Repeat678 – 70932PPR 9
Repeat710 – 74637PPR 10
Repeat747 – 78438PPR 11
Repeat785 – 82036PPR 12
Repeat821 – 85636PPR 13
Repeat954 – 98835PPR 14
Repeat1031 – 106535PPR 15
Repeat1066 – 110237PPR 16
Repeat1103 – 113735PPR 17
Repeat1138 – 117538PPR 18
Repeat1176 – 121035PPR 19
Repeat1317 – 135135PPR 20
Region1121 – 1394274RNA-binding

Amino acid modifications

Modified residue1551N6-acetyllysine Ref.14
Modified residue1871N6-acetyllysine Ref.14
Modified residue2261N6-acetyllysine By similarity
Modified residue2921N6-acetyllysine Ref.14
Modified residue4631N6-acetyllysine By similarity
Modified residue6131N6-acetyllysine Ref.14
Modified residue7261N6-acetyllysine Ref.14
Modified residue7501N6-acetyllysine Ref.14

Natural variations

Natural variant3541A → V in LSFC. Ref.16
VAR_018656
Natural variant4781T → A.
Corresponds to variant rs35035668 [ dbSNP | Ensembl ].
VAR_052935

Experimental info

Sequence conflict541S → G in BAF82705. Ref.2
Sequence conflict2961S → F in AAA67549. Ref.5
Sequence conflict528 – 5314LKSN → YFPI in AAH26034. Ref.4
Sequence conflict5561L → V in AAA67549. Ref.5
Sequence conflict5831Y → N in AAA67549. Ref.5
Sequence conflict6481S → R in AAA67549. Ref.5
Sequence conflict6761Q → R in BAC86287. Ref.2
Sequence conflict7021K → R in BAC86287. Ref.2
Sequence conflict750 – 7523KYV → NYL in AAA67549. Ref.5
Sequence conflict7691N → K in AAA67549. Ref.5
Sequence conflict11921N → D in BAC86287. Ref.2

Sequences

Sequence LengthMass (Da)Tools
P42704 [UniParc].

Last modified July 24, 2007. Version 3.
Checksum: 61AB0C8BF8A972E6

FASTA1,394157,905
        10         20         30         40         50         60 
MAALLRSARW LLRAGAAPRL PLSLRLLPGG PGRLHAASYL PAARAGPVAG GLLSPARLYA 

        70         80         90        100        110        120 
IAAKEKDIQE ESTFSSRKIS NQFDWALMRL DLSVRRTGRI PKKLLQKVFN DTCRSGGLGG 

       130        140        150        160        170        180 
SHALLLLRSC GSLLPELKLE ERTEFAHRIW DTLQKLGAVY DVSHYNALLK VYLQNEYKFS 

       190        200        210        220        230        240 
PTDFLAKMEE ANIQPNRVTY QRLIASYCNV GDIEGASKIL GFMKTKDLPV TEAVFSALVT 

       250        260        270        280        290        300 
GHARAGDMEN AENILTVMRD AGIEPGPDTY LALLNAYAEK GDIDHVKQTL EKVEKSELHL 

       310        320        330        340        350        360 
MDRDLLQIIF SFSKAGYPQY VSEILEKVTC ERRYIPDAMN LILLLVTEKL EDVALQILLA 

       370        380        390        400        410        420 
CPVSKEDGPS VFGSFFLQHC VTMNTPVEKL TDYCKKLKEV QMHSFPLQFT LHCALLANKT 

       430        440        450        460        470        480 
DLAKALMKAV KEEGFPIRPH YFWPLLVGRR KEKNVQGIIE ILKGMQELGV HPDQETYTDY 

       490        500        510        520        530        540 
VIPCFDSVNS ARAILQENGC LSDSDMFSQA GLRSEAANGN LDFVLSFLKS NTLPISLQSI 

       550        560        570        580        590        600 
RSSLLLGFRR SMNINLWSEI TELLYKDGRY CQEPRGPTEA VGYFLYNLID SMSDSEVQAK 

       610        620        630        640        650        660 
EEHLRQYFHQ LEKMNVKIPE NIYRGIRNLL ESYHVPELIK DAHLLVESKN LDFQKTVQLT 

       670        680        690        700        710        720 
SSELESTLET LKAENQPIRD VLKQLILVLC SEENMQKALE LKAKYESDMV TGGYAALINL 

       730        740        750        760        770        780 
CCRHDKVEDA LNLKEEFDRL DSSAVLDTGK YVGLVRVLAK HGKLQDAINI LKEMKEKDVL 

       790        800        810        820        830        840 
IKDTTALSFF HMLNGAALRG EIETVKQLHE AIVTLGLAEP STNISFPLVT VHLEKGDLST 

       850        860        870        880        890        900 
ALEVAIDCYE KYKVLPRIHD VLCKLVEKGE TDLIQKAMDF VSQEQGEMVM LYDLFFAFLQ 

       910        920        930        940        950        960 
TGNYKEAKKI IETPGIRARS ARLQWFCDRC VANNQVETLE KLVELTQKLF ECDRDQMYYN 

       970        980        990       1000       1010       1020 
LLKLYKINGD WQRADAVWNK IQEENVIPRE KTLRLLAEIL REGNQEVPFD VPELWYEDEK 

      1030       1040       1050       1060       1070       1080 
HSLNSSSAST TEPDFQKDIL IACRLNQKKG AYDIFLNAKE QNIVFNAETY SNLIKLLMSE 

      1090       1100       1110       1120       1130       1140 
DYFTQAMEVK AFAETHIKGF TLNDAANSRL IITQVRRDYL KEAVTTLKTV LDQQQTPSRL 

      1150       1160       1170       1180       1190       1200 
AVTRVIQALA MKGDVENIEV VQKMLNGLED SIGLSKMVFI NNIALAQIKN NNIDAAIENI 

      1210       1220       1230       1240       1250       1260 
ENMLTSENKV IEPQYFGLAY LFRKVIEEQL EPAVEKISIM AERLANQFAI YKPVTDFFLQ 

      1270       1280       1290       1300       1310       1320 
LVDAGKVDDA RALLQRCGAI AEQTPILLLF LLRNSRKQGK ASTVKSVLEL IPELNEKEEA 

      1330       1340       1350       1360       1370       1380 
YNSLMKSYVS EKDVTSAKAL YEHLTAKNTK LDDLFLKRYA SLLKYAGEPV PFIEPPESFE 

      1390 
FYAQQLRKLR ENSS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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, 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, 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, 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[16]"Identification of a gene causing human cytochrome c oxidase deficiency by integrative genomics."
Mootha V.K., Lepage P., Miller K., Bunkenborg J., Reich M., Hjerrild M., Delmonte T., Villeneuve A., Sladek R., Xu F., Mitchell G.A., Morin C., Mann M., Hudson T.J., Robinson B., Rioux J.D., Lander E.S.
Proc. Natl. Acad. Sci. U.S.A. 100:605-610(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LSFC VAL-354.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS27954.
RefSeqNP_573566.2. NM_133259.3.
UniGeneHs.368084.

3D structure databases

ProteinModelPortalP42704.
SMRP42704. Positions 72-326, 714-762, 1179-1204.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115432. 53 interactions.
DIPDIP-27543N.
IntActP42704. 28 interactions.
MINTMINT-205076.
STRING9606.ENSP00000260665.

Polymorphism databases

DMDM156632706.

Proteomic databases

PaxDbP42704.
PRIDEP42704.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260665; ENSP00000260665; ENSG00000138095.
ENST00000409946; ENSP00000386234; ENSG00000138095.
GeneID10128.
KEGGhsa:10128.
UCSCuc002rtr.2. human.

Organism-specific databases

CTD10128.
GeneCardsGC02M044113.
H-InvDBHIX0023918.
HGNCHGNC:15714. LRPPRC.
HPAHPA036408.
HPA036409.
MIM220111. phenotype.
607544. gene.
neXtProtNX_P42704.
Orphanet70472. Congenital lactic acidosis, Saguenay-Lac-St. Jean type.
PharmGKBPA30459.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG292283.
HOVERGENHBG097314.
InParanoidP42704.
OMAWNKMQEE.
OrthoDBEOG72JWG1.
TreeFamTF323626.

Gene expression databases

ArrayExpressP42704.
BgeeP42704.
CleanExHS_LRPPRC.
GenevestigatorP42704.

Family and domain databases

Gene3D1.25.40.10. 4 hits.
InterProIPR002885. Pentatricopeptide_repeat.
IPR011990. TPR-like_helical.
[Graphical view]
PfamPF01535. PPR. 6 hits.
[Graphical view]
TIGRFAMsTIGR00756. PPR. 2 hits.
PROSITEPS51375. PPR. 11 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLRPPRC. human.
GeneWikiLRPPRC.
GenomeRNAi10128.
NextBio38311.
PROP42704.
SOURCESearch...

Entry information

Entry nameLPPRC_HUMAN
AccessionPrimary (citable) accession number: P42704
Secondary accession number(s): A0PJE3 expand/collapse secondary AC list , A8K1V1, Q53PC0, Q53QN7, Q6ZUD8, Q7Z7A6, Q96D84
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: July 24, 2007
Last modified: March 19, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM