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Protein

La-related protein 1

Gene

LARP1

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

Functioni

RNA-binding protein that promotes translation of specific classes of mRNAs downstream of the mTORC1 complex. Associates with the mRNA 5'cap in an MTOR-dependent manner and associates with mRNAs containing a 5' terminal oligopyrimidine (5'TOP) motif, which is present in mRNAs encoding for ribosomal proteins and several components of the translation machinery. Associates with actively translating ribosomes via interaction with PABPC1/PABP and stimulates translation of mRNAs containing a 5'TOP, thereby regulating cell growth and proliferation. Positively regulates the replication of dengue virus (DENV) (PubMed:26735137).4 Publications

GO - Molecular functioni

  • eukaryotic initiation factor 4E binding Source: UniProtKB
  • mRNA 3'-UTR binding Source: UniProtKB
  • mRNA 5'-UTR binding Source: UniProtKB
  • poly(A) RNA binding Source: UniProtKB
  • RNA cap binding Source: UniProtKB
  • translation activator activity Source: UniProtKB
  • translation initiation factor binding Source: UniProtKB

GO - Biological processi

  • cell proliferation Source: UniProtKB
  • positive regulation of macroautophagy Source: BHF-UCL
  • positive regulation of viral genome replication Source: UniProtKB
  • TOR signaling Source: UniProtKB
  • translational initiation Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Protein biosynthesis

Keywords - Ligandi

RNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
La-related protein 1
Alternative name(s):
La ribonucleoprotein domain family member 1
Gene namesi
Name:LARP1
Synonyms:KIAA0731, LARP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 5

Organism-specific databases

HGNCiHGNC:29531. LARP1.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA142671564.

Polymorphism and mutation databases

DMDMi73621135.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 10961095La-related protein 1PRO_0000207609Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei75 – 751PhosphoserineCombined sources
Modified residuei90 – 901PhosphoserineCombined sources
Modified residuei143 – 1431PhosphoserineCombined sources
Modified residuei165 – 1651PhosphoserineCombined sources
Modified residuei215 – 2151PhosphoserineCombined sources
Modified residuei220 – 2201PhosphoserineCombined sources
Modified residuei223 – 2231PhosphothreonineBy similarity
Modified residuei225 – 2251PhosphoserineBy similarity
Modified residuei228 – 2281PhosphoserineBy similarity
Cross-linki311 – 311Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Modified residuei324 – 3241PhosphoserineBy similarity
Modified residuei327 – 3271PhosphoserineBy similarity
Modified residuei376 – 3761PhosphothreonineCombined sources
Modified residuei517 – 5171PhosphoserineCombined sources
Modified residuei521 – 5211PhosphoserineCombined sources
Modified residuei526 – 5261PhosphothreonineCombined sources1 Publication
Modified residuei548 – 5481PhosphoserineCombined sources
Modified residuei591 – 5911PhosphoserineCombined sources
Modified residuei627 – 6271PhosphoserineCombined sources
Modified residuei631 – 6311PhosphoserineCombined sources
Modified residuei649 – 6491PhosphothreonineCombined sources
Modified residuei724 – 7241PhosphothreonineCombined sources
Modified residuei766 – 7661PhosphoserineCombined sources
Modified residuei774 – 7741PhosphoserineCombined sources1 Publication
Modified residuei777 – 7771PhosphotyrosineCombined sources
Modified residuei785 – 7851PhosphothreonineCombined sources
Modified residuei788 – 7881PhosphothreonineCombined sources
Modified residuei824 – 8241PhosphoserineCombined sources
Modified residuei845 – 8451PhosphothreonineCombined sources
Modified residuei851 – 8511PhosphoserineCombined sources
Modified residuei853 – 8531PhosphoserineBy similarity
Modified residuei865 – 8651PhosphothreonineBy similarity
Modified residuei868 – 8681PhosphoserineBy similarity
Modified residuei892 – 8921N6-acetyllysineCombined sources
Modified residuei1017 – 10171N6-acetyllysineCombined sources
Modified residuei1040 – 10401PhosphoserineCombined sources
Modified residuei1089 – 10891PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6PKG0.
MaxQBiQ6PKG0.
PaxDbiQ6PKG0.
PeptideAtlasiQ6PKG0.
PRIDEiQ6PKG0.

PTM databases

iPTMnetiQ6PKG0.
PhosphoSiteiQ6PKG0.
SwissPalmiQ6PKG0.

Miscellaneous databases

PMAP-CutDBQ6PKG0.

Expressioni

Inductioni

Up-regulated in a number of hepatocellular carcinoma cell lines and liver cancer lesions, as well as in patients with hepatocellular carcinoma with a lower survival rate (at protein level).1 Publication

Gene expression databases

BgeeiQ6PKG0.
CleanExiHS_LARP1.
ExpressionAtlasiQ6PKG0. baseline and differential.
GenevisibleiQ6PKG0. HS.

Organism-specific databases

HPAiCAB015222.
HPA051397.

Interactioni

Subunit structurei

Interacts with PABPC1/PABP. Associates with the mTORC1 complex. Interacts with EIF4E. Found in a complex with PABPC1 and RYDEN (PubMed:26735137).3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC155Q8N6L03EBI-1052114,EBI-749265

GO - Molecular functioni

  • eukaryotic initiation factor 4E binding Source: UniProtKB
  • translation initiation factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116947. 104 interactions.
IntActiQ6PKG0. 46 interactions.
MINTiMINT-1631511.
STRINGi9606.ENSP00000336721.

Structurei

Secondary structure

1
1096
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi875 – 8806Combined sources
Helixi887 – 90418Combined sources
Helixi910 – 92213Combined sources
Turni923 – 9253Combined sources
Helixi929 – 94416Combined sources
Helixi949 – 96416Combined sources
Helixi968 – 98316Combined sources
Helixi988 – 99912Combined sources
Helixi1001 – 10044Combined sources
Helixi1009 – 101810Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZC4X-ray1.86A/B/C/D873-1023[»]
5C0VX-ray2.20A/B/C/D873-1023[»]
ProteinModelPortaliQ6PKG0.
SMRiQ6PKG0. Positions 873-1023.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini397 – 48791HTH La-type RNA-bindingPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1044 – 10507Poly-Gly

Sequence similaritiesi

Belongs to the LARP family.Curated
Contains 1 HTH La-type RNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2590. Eukaryota.
COG5193. LUCA.
GeneTreeiENSGT00390000000523.
HOGENOMiHOG000113283.
HOVERGENiHBG054322.
InParanoidiQ6PKG0.
KOiK18757.
OMAiQHSDTQT.
OrthoDBiEOG7HB59K.
PhylomeDBiQ6PKG0.
TreeFamiTF314516.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006607. DM15.
IPR006630. Lupus_La_RNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
[Graphical view]
SMARTiSM00684. DM15. 3 hits.
SM00715. LA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q6PKG0-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MATQVEPLLP GGATLLQAEE HGGLVRKKPP PAPEGKGEPG PNDVRGGEPD
60 70 80 90 100
GSARRPRPPC AKPHKEGTGQ QERESPRPLQ LPGAEGPAIS DGEEGGGEPG
110 120 130 140 150
AGGGAAGAAG AGRRDFVEAP PPKVNPWTKN ALPPVLTTVN GQSPPEHSAP
160 170 180 190 200
AKVVRAAVPK QRKGSKVGDF GDAINWPTPG EIAHKSVQPQ SHKPQPTRKL
210 220 230 240 250
PPKKDMKEQE KGEGSDSKES PKTKSDESGE EKNGDEDCQR GGQKKKGNKH
260 270 280 290 300
KWVPLQIDMK PEVPREKLAS RPTRPPEPRH IPANRGEIKG SESATYVPVA
310 320 330 340 350
PPTPAWQPEI KPEPAWHDQD ETSSVKSDGA GGARASFRGR GRGRGRGRGR
360 370 380 390 400
GRGGTRTHFD YQFGYRKFDG VEGPRTPKYM NNITYYFDNV SSTELYSVDQ
410 420 430 440 450
ELLKDYIKRQ IEYYFSVDNL ERDFFLRRKM DADGFLPITL IASFHRVQAL
460 470 480 490 500
TTDISLIFAA LKDSKVVEIV DEKVRRREEP EKWPLPPIVD YSQTDFSQLL
510 520 530 540 550
NCPEFVPRQH YQKETESAPG SPRAVTPVPT KTEEVSNLKT LPKGLSASLP
560 570 580 590 600
DLDSENWIEV KKRPRPSPAR PKKSEESRFS HLTSLPQQLP SQQLMSKDQD
610 620 630 640 650
EQEELDFLFD EEMEQMDGRK NTFTAWSDEE SDYEIDDRDV NKILIVTQTP
660 670 680 690 700
HYMRRHPGGD RTGNHTSRAK MSAELAKVIN DGLFYYEQDL WAEKFEPEYS
710 720 730 740 750
QIKQEVENFK KVNMISREQF DTLTPEPPVD PNQEVPPGPP RFQQVPTDAL
760 770 780 790 800
ANKLFGAPEP STIARSLPTT VPESPNYRNT RTPRTPRTPQ LKDSSQTSRF
810 820 830 840 850
YPVVKEGRTL DAKMPRKRKT RHSSNPPLES HVGWVMDSRE HRPRTASISS
860 870 880 890 900
SPSEGTPTVG SYGCTPQSLP KFQHPSHELL KENGFTQHVY HKYRRRCLNE
910 920 930 940 950
RKRLGIGQSQ EMNTLFRFWS FFLRDHFNKK MYEEFKQLAL EDAKEGYRYG
960 970 980 990 1000
LECLFRYYSY GLEKKFRLDI FKDFQEETVK DYEAGQLYGL EKFWAFLKYS
1010 1020 1030 1040 1050
KAKNLDIDPK LQEYLGKFRR LEDFRVDPPM GEEGNHKRHS VVAGGGGGEG
1060 1070 1080 1090
RKRCPSQSSS RPAAMISQPP TPPTGQPVRE DAKWTSQHSN TQTLGK
Length:1,096
Mass (Da):123,510
Last modified:August 16, 2005 - v2
Checksum:iCA3E9D30BBC101B7
GO
Isoform 2 (identifier: Q6PKG0-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-77: Missing.
     78-144: PLQLPGAEGP...VLTTVNGQSP → MLWRVLLSKR...PFPVLAPFSN

Show »
Length:1,019
Mass (Da):116,465
Checksum:i64982CA22171B0E6
GO

Sequence cautioni

The sequence AAH33856.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAA34451.1 differs from that shown.Aberrant splicing.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti778 – 7803RNT → TRP in AAH33856 (PubMed:15489334).Curated
Sequence conflicti979 – 9791V → L in CAB61364 (PubMed:17974005).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7777Missing in isoform 2. 1 PublicationVSP_015114Add
BLAST
Alternative sequencei78 – 14467PLQLP…NGQSP → MLWRVLLSKRPPFPHPELDF QEAPIPSCPGRLPGRKNSVA LAAAPRKEPTGDREKPLPFP VLAPFSN in isoform 2. 1 PublicationVSP_015115Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC001460 mRNA. Translation: AAH01460.2.
BC033856 mRNA. Translation: AAH33856.1. Different initiation.
AK091465 mRNA. Translation: BAC03668.1.
AB018274 mRNA. Translation: BAA34451.1. Sequence problems.
AL133034 mRNA. Translation: CAB61364.1.
CCDSiCCDS4328.1. [Q6PKG0-3]
PIRiT42646.
RefSeqiNP_056130.2. NM_015315.4. [Q6PKG0-3]
XP_005268461.1. XM_005268404.3. [Q6PKG0-1]
UniGeneiHs.292078.

Genome annotation databases

EnsembliENST00000336314; ENSP00000336721; ENSG00000155506. [Q6PKG0-3]
GeneIDi23367.
KEGGihsa:23367.
UCSCiuc003lvo.4. human. [Q6PKG0-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC001460 mRNA. Translation: AAH01460.2.
BC033856 mRNA. Translation: AAH33856.1. Different initiation.
AK091465 mRNA. Translation: BAC03668.1.
AB018274 mRNA. Translation: BAA34451.1. Sequence problems.
AL133034 mRNA. Translation: CAB61364.1.
CCDSiCCDS4328.1. [Q6PKG0-3]
PIRiT42646.
RefSeqiNP_056130.2. NM_015315.4. [Q6PKG0-3]
XP_005268461.1. XM_005268404.3. [Q6PKG0-1]
UniGeneiHs.292078.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4ZC4X-ray1.86A/B/C/D873-1023[»]
5C0VX-ray2.20A/B/C/D873-1023[»]
ProteinModelPortaliQ6PKG0.
SMRiQ6PKG0. Positions 873-1023.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116947. 104 interactions.
IntActiQ6PKG0. 46 interactions.
MINTiMINT-1631511.
STRINGi9606.ENSP00000336721.

PTM databases

iPTMnetiQ6PKG0.
PhosphoSiteiQ6PKG0.
SwissPalmiQ6PKG0.

Polymorphism and mutation databases

DMDMi73621135.

Proteomic databases

EPDiQ6PKG0.
MaxQBiQ6PKG0.
PaxDbiQ6PKG0.
PeptideAtlasiQ6PKG0.
PRIDEiQ6PKG0.

Protocols and materials databases

DNASUi23367.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000336314; ENSP00000336721; ENSG00000155506. [Q6PKG0-3]
GeneIDi23367.
KEGGihsa:23367.
UCSCiuc003lvo.4. human. [Q6PKG0-1]

Organism-specific databases

CTDi23367.
GeneCardsiLARP1.
HGNCiHGNC:29531. LARP1.
HPAiCAB015222.
HPA051397.
MIMi612059. gene.
neXtProtiNX_Q6PKG0.
PharmGKBiPA142671564.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2590. Eukaryota.
COG5193. LUCA.
GeneTreeiENSGT00390000000523.
HOGENOMiHOG000113283.
HOVERGENiHBG054322.
InParanoidiQ6PKG0.
KOiK18757.
OMAiQHSDTQT.
OrthoDBiEOG7HB59K.
PhylomeDBiQ6PKG0.
TreeFamiTF314516.

Miscellaneous databases

ChiTaRSiLARP1. human.
GeneWikiiLARP1.
GenomeRNAii23367.
PMAP-CutDBQ6PKG0.
PROiQ6PKG0.
SOURCEiSearch...

Gene expression databases

BgeeiQ6PKG0.
CleanExiHS_LARP1.
ExpressionAtlasiQ6PKG0. baseline and differential.
GenevisibleiQ6PKG0. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR006607. DM15.
IPR006630. Lupus_La_RNA-bd.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF05383. La. 1 hit.
[Graphical view]
SMARTiSM00684. DM15. 3 hits.
SM00715. LA. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS50961. HTH_LA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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] (ISOFORM 2).
    Tissue: Cervix and Placenta.
  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] OF 1-816 (ISOFORM 1).
    Tissue: Brain.
  3. Cited for: PROTEIN SEQUENCE OF 2-26; 115-123; 167-185; 252-265; 357-366; 410-422; 429-473; 524-539; 579-597; 643-654; 695-703; 718-778; 904-924; 937-944; 949-964 AND 1004-1017, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, PHOSPHORYLATION AT THR-526 AND SER-774, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Cervix carcinoma, Colon carcinoma and Mammary carcinoma.
  4. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 123-1096 (ISOFORM 1).
    Tissue: Brain.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1096.
    Tissue: Mammary cancer.
  6. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-521; THR-526; SER-627; SER-766 AND SER-774, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-845, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
    Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
    Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75 AND SER-90, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-627, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-165; SER-517; SER-521; THR-526; SER-627; SER-631; THR-649; THR-724; SER-774; SER-824 AND SER-851, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; THR-526 AND SER-774, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-627; SER-631; THR-724 AND SER-824, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  17. "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-892 AND LYS-1017, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. Cited for: RNA-BINDING, FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH EIF4E AND PABPC1.
  19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143; SER-220; THR-376; SER-521; THR-526; SER-548; SER-627; SER-631; THR-649; SER-766 AND SER-774, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; SER-215; SER-220; SER-521; THR-526; SER-548; SER-627; SER-631; SER-766; SER-774 AND TYR-777, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  23. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "LARP1 specifically recognizes the 3' terminus of poly(A) mRNA."
    Aoki K., Adachi S., Homoto M., Kusano H., Koike K., Natsume T.
    FEBS Lett. 587:2173-2178(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: RNA-BINDING, FUNCTION.
  25. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-143; THR-376; SER-517; SER-521; THR-526; SER-548; SER-591; SER-627; THR-649; SER-766; SER-774; THR-785; THR-788; SER-824 AND SER-1089, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  26. "LARP1 predict the prognosis for early-stage and AFP-normal hepatocellular carcinoma."
    Xie C., Huang L., Xie S., Xie D., Zhang G., Wang P., Peng L., Gao Z.
    J. Transl. Med. 11:272-272(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  27. "Proteomic analysis of cap-dependent translation identifies LARP1 as a key regulator of 5'TOP mRNA translation."
    Tcherkezian J., Cargnello M., Romeo Y., Huttlin E.L., Lavoie G., Gygi S.P., Roux P.P.
    Genes Dev. 28:357-371(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, RNA-BINDING, INTERACTION WITH PABPC1, SUBCELLULAR LOCATION.
  28. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-627; SER-631; THR-649; SER-766 AND SER-1040, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  29. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-311, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, IDENTIFICATION IN A COMPLEX WITH PABPC1 AND RYDEN.

Entry informationi

Entry nameiLARP1_HUMAN
AccessioniPrimary (citable) accession number: Q6PKG0
Secondary accession number(s): O94836
, Q8N4M2, Q8NB73, Q9UFD7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 16, 2005
Last sequence update: August 16, 2005
Last modified: July 6, 2016
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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: 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. SIMILARITY comments
    Index of protein domains and families

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 one 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.