Q6PKG0 (LARP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 97.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: La-related protein 1 Alternative name(s): La ribonucleoprotein domain family member 1 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 1096 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Sequence similarities | Belongs to the LARP family. Contains 1 HTH La-type RNA-binding domain. |
| Sequence caution | The sequence AAH33856.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA34451.1 differs from that shown. Reason: Aberrant splicing. |
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing |
| Ligand | RNA-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | positive regulation of macroautophagy Inferred from mutant phenotype PubMed 22354037. Source: BHF-UCL |
| Molecular_function | RNA binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: Q6PKG0-1) 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. | ||||||
| Isoform 2 (identifier: Q6PKG0-3) The sequence of this isoform differs from the canonical sequence as follows: 1-77: Missing. 78-144: PLQLPGAEGP...VLTTVNGQSP → MLWRVLLSKR...PFPVLAPFSN |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.3 | ||||||
| Chain | 2 – 1096 | 1095 | La-related protein 1 | PRO_0000207609 | |||||
Regions | |||||||||
| Domain | 397 – 487 | 91 | HTH La-type RNA-binding | ||||||
| Compositional bias | 1044 – 1050 | 7 | Poly-Gly | ||||||
Amino acid modifications | |||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.3 | ||||||
| Modified residue | 75 | 1 | Phosphoserine Ref.11 Ref.15 | ||||||
| Modified residue | 90 | 1 | Phosphoserine Ref.6 Ref.9 Ref.11 Ref.13 Ref.14 Ref.15 Ref.19 | ||||||
| Modified residue | 143 | 1 | Phosphoserine Ref.13 Ref.17 Ref.19 | ||||||
| Modified residue | 165 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 215 | 1 | Phosphoserine Ref.19 | ||||||
| Modified residue | 220 | 1 | Phosphoserine Ref.17 Ref.19 | ||||||
| Modified residue | 228 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 324 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 327 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 376 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 517 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 521 | 1 | Phosphoserine Ref.6 Ref.13 Ref.17 Ref.19 | ||||||
| Modified residue | 526 | 1 | Phosphothreonine Ref.3 Ref.6 Ref.13 Ref.14 Ref.17 Ref.19 | ||||||
| Modified residue | 548 | 1 | Phosphoserine Ref.17 Ref.19 | ||||||
| Modified residue | 627 | 1 | Phosphoserine Ref.6 Ref.12 Ref.13 Ref.15 Ref.17 Ref.19 | ||||||
| Modified residue | 631 | 1 | Phosphoserine Ref.13 Ref.15 Ref.17 Ref.19 | ||||||
| Modified residue | 649 | 1 | Phosphothreonine Ref.13 Ref.17 | ||||||
| Modified residue | 724 | 1 | Phosphothreonine Ref.13 Ref.15 | ||||||
| Modified residue | 766 | 1 | Phosphoserine Ref.6 Ref.17 Ref.19 | ||||||
| Modified residue | 774 | 1 | Phosphoserine Ref.3 Ref.6 Ref.13 Ref.14 Ref.17 Ref.19 | ||||||
| Modified residue | 777 | 1 | Phosphotyrosine Ref.19 | ||||||
| Modified residue | 824 | 1 | Phosphoserine Ref.13 Ref.15 | ||||||
| Modified residue | 845 | 1 | Phosphothreonine Ref.7 | ||||||
| Modified residue | 851 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 865 | 1 | Phosphothreonine Ref.15 | ||||||
| Modified residue | 868 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 892 | 1 | N6-acetyllysine Ref.16 | ||||||
| Modified residue | 1017 | 1 | N6-acetyllysine Ref.16 | ||||||
| Modified residue | 1056 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 77 | 77 | Missing in isoform 2. | VSP_015114 | |||||
| Alternative sequence | 78 – 144 | 67 | PLQLP…NGQSP → MLWRVLLSKRPPFPHPELDF QEAPIPSCPGRLPGRKNSVA LAAAPRKEPTGDREKPLPFP VLAPFSN in isoform 2. | VSP_015115 | |||||
Experimental info | |||||||||
| Sequence conflict | 778 – 780 | 3 | RNT → TRP in AAH33856. Ref.1 | ||||||
| Sequence conflict | 979 | 1 | V → L in CAB61364. Ref.5 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. 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] | Bienvenut W.V., Calvo F., Matallanas D., Cooper W.N., Kolch W., Heiserich L., Boulahbel H., Gottlieb E. Submitted (FEB-2008) to UniProtKB 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, 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] | "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [10] | "ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [14] | "Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; THR-526 AND SER-774, MASS SPECTROMETRY. |
| [15] | "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; SER-824; THR-865 AND SER-868, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [16] | "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, MASS SPECTROMETRY. |
| [17] | "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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [18] | "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]. |
| [19] | "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, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | 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. |
| IPI | IPI00185919. IPI00411690. |
| PIR | T42646. |
| RefSeq | NP_056130.2. NM_015315.3. |
| UniGene | Hs.292078. |
3D structure databases | |
| ProteinModelPortal | Q6PKG0. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q6PKG0. 12 interactions. |
| MINT | MINT-1631511. |
| STRING | 9606.ENSP00000366871. |
PTM databases | |
| PhosphoSite | Q6PKG0. |
Polymorphism databases | |
| DMDM | 73621135. |
Proteomic databases | |
| PaxDb | Q6PKG0. |
| PRIDE | Q6PKG0. |
Protocols and materials databases | |
| DNASU | 23367. |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000336314; ENSP00000336721; ENSG00000155506. ENST00000518297; ENSP00000428589; ENSG00000155506. |
| GeneID | 23367. |
| KEGG | hsa:23367. |
| UCSC | uc003lvo.3. human. uc010jie.1. human. |
Organism-specific databases | |
| CTD | 23367. |
| GeneCards | GC05P154092. |
| HGNC | HGNC:29531. LARP1. |
| HPA | CAB015222. |
| MIM | 612059. gene. |
| neXtProt | NX_Q6PKG0. |
| PharmGKB | PA142671564. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | COG5193. |
| HOGENOM | HOG000113283. |
| HOVERGEN | HBG054322. |
| InParanoid | Q6PKG0. |
| OMA | GSEPATY. |
Gene expression databases | |
| ArrayExpress | Q6PKG0. |
| Bgee | Q6PKG0. |
| CleanEx | HS_LARP1. |
| Genevestigator | Q6PKG0. |
| GermOnline | ENSG00000155506. Homo sapiens. |
Family and domain databases | |
| Gene3D | 1.10.10.10. 1 hit. |
| InterPro | IPR006607. DM15. IPR006630. Lupus_La_RNA-bd. IPR011991. WHTH_DNA-bd_dom. [Graphical view] |
| Pfam | PF05383. La. 1 hit. [Graphical view] |
| SMART | SM00684. DM15. 3 hits. SM00715. LA. 1 hit. [Graphical view] |
| PROSITE | PS50961. HTH_LA. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| ChiTaRS | LARP1. human. |
| GenomeRNAi | 23367. |
| NextBio | 45430. |
| PMAP-CutDB | Q6PKG0. |
| SOURCE | Search... |
Entry information
| Entry name | LARP1_HUMAN | ||||||||
| Accession | Primary (citable) accession number: Q6PKG0 Secondary accession number(s): O94836 Q9UFD7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Chordata Protein Annotation Program | ||||||||
| Disclaimer | Any 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
| Human chromosome 5 Human chromosome 5: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| SIMILARITY comments Index of protein domains and families |

Clusters with
