Reviewed,
UniProtKB/Swiss-Prot Q6PKG0 (LARP1_HUMAN)
Last modified
July 7, 2009.
Version 60.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
Customize display | text xml rdf/xml gff fasta |
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names 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) [Complete 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)
Ontologies
| Keywords | |
|---|---|
| Coding sequence diversity | Alternative splicing |
| Ligand | RNA-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Direct protein sequencing |
| Gene Ontology (GO) | |
| Molecular function | RNA binding Inferred from electronic annotation. Source: UniProtKB-KW protein bindingInferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| YWHAB | P31946 | 1 | EBI-1052114,EBI-359815 | |
| YWHAG | P61981 | 1 | EBI-1052114,EBI-359832 | |
| YWHAQ | P27348 | 1 | EBI-1052114,EBI-359854 | |
| YWHAZ | P63104 | 1 | EBI-1052114,EBI-347088 |
Alternative products
| This entry describes 3 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: Q6PKG0-2) The sequence of this isoform differs from the canonical sequence as follows: 1-122: MATQVEPLLP...RRDFVEAPPP → AADRVVCLAR...EEGVAGALLA | ||||||
| Note: Incomplete sequence. No experimental confirmation available. | ||||||
| Isoform 3 (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.4 | ||||||
| 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.4 | ||||||
| Modified residue | 75 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 90 | 1 | Phosphoserine Ref.7 Ref.10 Ref.15 Ref.17 | ||||||
| Modified residue | 143 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 165 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 324 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 327 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 517 | 1 | Phosphoserine Ref.7 Ref.11 Ref.17 | ||||||
| Modified residue | 521 | 1 | Phosphoserine Ref.7 Ref.11 Ref.14 Ref.17 | ||||||
| Modified residue | 526 | 1 | Phosphothreonine Ref.4 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.17 | ||||||
| Modified residue | 548 | 1 | Phosphoserine Ref.6 Ref.16 | ||||||
| Modified residue | 622 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 624 | 1 | Phosphothreonine Ref.11 | ||||||
| Modified residue | 627 | 1 | Phosphoserine Ref.6 Ref.7 Ref.11 Ref.17 | ||||||
| Modified residue | 631 | 1 | Phosphoserine Ref.7 Ref.17 | ||||||
| Modified residue | 649 | 1 | Phosphothreonine Ref.9 Ref.17 | ||||||
| Modified residue | 724 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 766 | 1 | Phosphoserine Ref.7 Ref.15 Ref.17 | ||||||
| Modified residue | 774 | 1 | Phosphoserine Ref.4 Ref.6 Ref.7 Ref.13 Ref.15 Ref.17 | ||||||
| Modified residue | 785 | 1 | Phosphothreonine Ref.8 Ref.11 | ||||||
| Modified residue | 788 | 1 | Phosphothreonine Ref.8 Ref.11 | ||||||
| Modified residue | 823 | 1 | Phosphoserine Ref.15 | ||||||
| Modified residue | 824 | 1 | Phosphoserine Ref.7 Ref.15 Ref.17 | ||||||
| Modified residue | 845 | 1 | Phosphothreonine Ref.17 | ||||||
| Modified residue | 851 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 853 | 1 | Phosphoserine Ref.17 | ||||||
| Modified residue | 1056 | 1 | Phosphoserine Ref.12 | ||||||
| Modified residue | 1071 | 1 | Phosphothreonine Ref.7 Ref.12 | ||||||
Natural variations | |||||||||
| Alternative sequence | 1 – 122 | 122 | MATQV…EAPPP → AADRVVCLARRASPPSVHIA AAPEPGSPGRPGGGGEGGTG LEACRARGGGVLRGTGGGGR TPRRPGLQSGGPSSPPAPLV GLGFTAAASNWEGAAPRVNP DPSLQGLGPSAPEEGVAGAL LA in isoform 2. | VSP_015113 | |||||
| Alternative sequence | 1 – 77 | 77 | Missing in isoform 3. | VSP_015114 | |||||
| Alternative sequence | 78 – 144 | 67 | PLQLP…NGQSP → MLWRVLLSKRPPFPHPELDF QEAPIPSCPGRLPGRKNSVA LAAAPRKEPTGDREKPLPFP VLAPFSN in isoform 3. | VSP_015115 | |||||
Experimental info | |||||||||
| Sequence conflict | 778 – 780 | 3 | RNT → TRP in AAH33856. Ref.1 | ||||||
| Sequence conflict | 979 | 1 | V → L Ref.5 | ||||||
Sequences
| ||||||||||||||||||||||||||||||
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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). Tissue: Cervix and Placenta. |
| [2] | "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: 9872452] [Abstract] Cited for: PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). Tissue: Brain. |
| [3] | "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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-816 (ISOFORM 1). Tissue: Brain. |
| [4] | 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. |
| [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., Blocker H., Heubner D., Hoerlein A., Michel G., Wedler H., Kohrer K., Ottenwalder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed: 17974005] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 538-1096. Tissue: Mammary cancer. |
| [6] | "Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526; SER-548; SER-627 AND SER-774, MASS SPECTROMETRY. Tissue: Epithelium. |
| [7] | "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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90; SER-517; SER-521; THR-526; SER-627; SER-631; SER-766; SER-774; SER-824 AND THR-1071, MASS SPECTROMETRY. Tissue: Epithelium. |
| [8] | "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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526; THR-785 AND THR-788, MASS SPECTROMETRY. Tissue: Epithelium. |
| [9] | "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: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526 AND THR-649, MASS SPECTROMETRY. Tissue: Epithelium. |
| [10] | "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: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-90 AND THR-526, MASS SPECTROMETRY. |
| [11] | "Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-517; SER-521; THR-526; THR-622; THR-624; SER-627; THR-785 AND THR-788, MASS SPECTROMETRY. |
| [12] | "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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1056 AND THR-1071, MASS SPECTROMETRY. |
| [13] | "Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column." Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y. Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-526 AND SER-774, MASS SPECTROMETRY. |
| [14] | "Phosphoproteome of resting human platelets." Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., Schuetz C., Walter U., Gambaryan S., Sickmann A. J. Proteome Res. 7:526-534(2008) [PubMed: 18088087] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-521, MASS SPECTROMETRY. Tissue: Platelet. |
| [15] | "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: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-90; SER-766; SER-774; SER-823 AND SER-824, MASS SPECTROMETRY. |
| [16] | "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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-548, MASS SPECTROMETRY. |
| [17] | "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: 18669648] [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-766; SER-774; SER-824; THR-845; SER-851 AND SER-853, MASS SPECTROMETRY. |
| [18] | Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| BC001460 mRNA. Translation: AAH01460.2. BC033856 mRNA. Translation: AAH33856.1. Different initiation. AB018274 mRNA. Translation: BAA34451.1. AK091465 mRNA. Translation: BAC03668.1. AL133034 mRNA. Translation: CAB61364.1. | |
| IPI | IPI00185919. IPI00411690. IPI00643027. |
| PIR | T42646. |
| RefSeq | NP_056130.2. NP_291029.2. |
| UniGene | Hs.292078 |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q6PKG0. 6 interactions. |
PTM databases | |
| PhosphoSite | Q6PKG0. |
Proteomic databases | |
| PRIDE | Q6PKG0. |
Genome annotation databases | |
| Ensembl | ENSG00000155506. Homo sapiens. [Contig view] |
| GeneID | 23367. |
| KEGG | hsa:23367. |
| UCSC | uc003lvo.1. human. uc003lvp.1. human. |
Organism-specific databases | |
| GeneCards | GC05P154073. |
| H-InvDB | HIX0005343. |
| HGNC | HGNC:29531. LARP1. |
| HPA | CAB015222. |
| MIM | 612059. gene. |
| PharmGKB | PA142671564. |
| HUGE | Search... |
| GenAtlas | Search... |
Phylogenomic databases | |
| HOGENOM | Q6PKG0. |
| HOVERGEN | Q6PKG0. |
Gene expression databases | |
| ArrayExpress | Q6PKG0. |
| Bgee | Q6PKG0. |
| CleanEx | HS_LARP1. |
| GermOnline | ENSG00000155506. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR006607. DM15. IPR006630. Lupus_La_RNA_bd. IPR011991. Wing_hlx_DNA_bd. [Graphical view] |
| Gene3D | G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit. |
| 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 Resources | |
| 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 project | HPI (Human Proteome Initiative) | ||||||||
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


