O95232 (LC7L3_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 78.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Luc7-like protein 3 Alternative name(s): Cisplatin resistance-associated-overexpressed protein Luc7A Okadaic acid-inducible phosphoprotein OA48-18 cAMP regulatory element-associated protein 1 Short name=CRE-associated protein 1 Short name=CREAP-1 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 432 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing. Ref.2 |
| Subunit structure | May interact with SFRS1 and form homodimers. Interacts with JMJD6 and RBM25. Interacts with RSRC1 (via Arg/Ser-rich domain). Ref.7 Ref.8 Ref.11 Ref.15 |
| Subcellular location | Nucleus speckle. Note: The subnuclear localization is affected by cisplatin. Ref.1 Ref.7 |
| Tissue specificity | Widely expressed. Highest levels in heart, brain, pancreas, thymus, ovary, small intestine and peripheral blood leukocytes, as well as cerebellum, putamen and pituitary gland. Lowest levels in lung, liver and kidney. Also expressed in fetal tissues, including brain, heart, kidney, thymus and lung. Ref.1 Ref.2 |
| Post-translational modification | Phosphorylated in vitro by SRPK1, SRPK2 and CLK1. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.7 Ref.9 Ref.10 Ref.12 Ref.13 Ref.14 |
| Sequence similarities | Belongs to the Luc7 family. |
| Sequence caution | The sequence AAC79807.1 differs from that shown. Reason: Erroneous translation. Erroneous CDS prediction. |
Ontologies
| Keywords | |
|---|---|
| Biological process | mRNA processing mRNA splicing |
| Cellular component | Nucleus |
| Coding sequence diversity | Alternative splicing |
| Domain | Coiled coil |
| Ligand | DNA-binding |
| PTM | Acetylation Phosphoprotein |
| Technical term | Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | RNA splicing Inferred from mutant phenotype Ref.1. Source: UniProtKB apoptotic processInferred from mutant phenotype Ref.6. Source: UniProtKB mRNA processingInferred from electronic annotation. Source: UniProtKB-KW response to stressInferred from mutant phenotype Ref.6. Source: UniProtKB |
| Cellular component | focal adhesion Inferred from direct assay. Source: HPA nuclear speckInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | DNA binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA bindingInferred from mutant phenotype Ref.1. Source: UniProtKB protein bindingInferred from physical interaction Ref.8Ref.11Ref.15. Source: UniProtKB |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| RNPS1 | Q15287 | 1 | EBI-395671,EBI-395959 |
Alternative products
| This entry describes 2 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (identifier: O95232-1) 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: O95232-2) The sequence of this isoform differs from the canonical sequence as follows: 56-79: GPCEKIHDENLRKQYEKSSRFMKV → DVFGRGDNISDVSKFLEDDKWMEE 80-432: Missing. | ||||||
| Note: No experimental confirmation available. |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 432 | 432 | Luc7-like protein 3 | PRO_0000058013 | |||||
Regions | |||||||||
| Coiled coil | 124 – 181 | 58 | Potential | ||||||
| Compositional bias | 228 – 282 | 55 | Glu-rich | ||||||
| Compositional bias | 235 – 395 | 161 | Arg/Ser-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.13 | ||||||
| Modified residue | 78 | 1 | N6-acetyllysine Ref.16 | ||||||
| Modified residue | 110 | 1 | Phosphoserine Ref.10 | ||||||
| Modified residue | 115 | 1 | Phosphoserine Ref.13 | ||||||
| Modified residue | 166 | 1 | N6-acetyllysine Ref.16 | ||||||
| Modified residue | 231 | 1 | N6-acetyllysine Ref.16 | ||||||
| Modified residue | 333 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 335 | 1 | Phosphoserine Ref.9 | ||||||
| Modified residue | 425 | 1 | Phosphoserine Ref.10 Ref.12 Ref.13 Ref.14 | ||||||
| Modified residue | 429 | 1 | Phosphothreonine Ref.10 | ||||||
| Modified residue | 431 | 1 | Phosphoserine Ref.12 Ref.13 Ref.14 | ||||||
Natural variations | |||||||||
| Alternative sequence | 56 – 79 | 24 | GPCEK…RFMKV → DVFGRGDNISDVSKFLEDDK WMEE in isoform 2. | VSP_018136 | |||||
| Alternative sequence | 80 – 432 | 353 | Missing in isoform 2. | VSP_018137 | |||||
Experimental info | |||||||||
| Sequence conflict | 217 | 1 | H → Y in BAA91981. Ref.3 | ||||||
| Sequence conflict | 378 – 379 | 2 | EK → HE Ref.3 | ||||||
Sequences
| ||||||||||||||||||||||||
References
| « Hide 'large scale' references | |
| [1] | "CROP/Luc7A, a novel serine/arginine-rich nuclear protein, isolated from cisplatin-resistant cell line." Nishii Y., Morishima M., Kakehi Y., Umehara K., Kioka N., Terano Y., Amachi T., Ueda K. FEBS Lett. 465:153-156(2000) [PubMed: 10631324] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY. |
| [2] | "Identification of a family of DNA-binding proteins with homology to RNA splicing factors." Shipman K.L., Robinson P.J., King B.R., Smith R., Nicholson R.C. Biochem. Cell Biol. 84:9-19(2006) [PubMed: 16462885] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY. Tissue: Placenta. |
| [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] (ISOFORM 1). Tissue: Placenta. |
| [4] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | "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 2). Tissue: PNS. |
| [6] | "Identification of okadaic-acid-induced genes by mRNA differential display in glioma cells." Chin L.S., Singh S.K., Wang Q., Murray S.F. J. Biomed. Sci. 7:152-159(2000) [PubMed: 10754390] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 378-432. Tissue: Fetal brain. |
| [7] | "Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A." Umehara H., Nishii Y., Morishima M., Kakehi Y., Kioka N., Amachi T., Koizumi J., Hagiwara M., Ueda K. Biochem. Biophys. Res. Commun. 301:324-329(2003) [PubMed: 12565863] [Abstract] Cited for: INTERACTION WITH SFRS1, PHOSPHORYLATION, SUBCELLULAR LOCATION. |
| [8] | "A novel SR-related protein is required for the second step of pre-mRNA splicing." Cazalla D., Newton K., Caceres J.F. Mol. Cell. Biol. 25:2969-2980(2005) [PubMed: 15798186] [Abstract] Cited for: INTERACTION WITH RSRC1. |
| [9] | "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-333 AND SER-335, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [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: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-425 AND THR-429, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [11] | "Novel splicing factor RBM25 modulates Bcl-x pre-mRNA 5' splice site selection." Zhou A., Ou A.C., Cho A., Benz E.J. Jr., Huang S.C. Mol. Cell. Biol. 28:5924-5936(2008) [PubMed: 18663000] [Abstract] Cited for: INTERACTION WITH RBM25. |
| [12] | "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-425 AND SER-431, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-425 AND SER-431, MASS SPECTROMETRY. Tissue: Embryonic kidney. |
| [14] | "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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-431, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [15] | "Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing." Webby C.J., Wolf A., Gromak N., Dreger M., Kramer H., Kessler B., Nielsen M.L., Schmitz C., Butler D.S., Yates J.R. III, Delahunty C.M., Hahn P., Lengeling A., Mann M., Proudfoot N.J., Schofield C.J., Boettger A. Science 325:90-93(2009) [PubMed: 19574390] [Abstract] Cited for: INTERACTION WITH JMJD6. |
| [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., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-166 AND LYS-231, MASS SPECTROMETRY. |
| [17] | "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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB034205 mRNA. Translation: BAA90542.1. DQ013876 mRNA. Translation: AAY26238.1. AK001925 mRNA. Translation: BAA91981.1. AK023672 mRNA. Translation: BAG51216.1. CH471109 Genomic DNA. Translation: EAW94583.1. CH471109 Genomic DNA. Translation: EAW94585.1. CH471109 Genomic DNA. Translation: EAW94587.1. BC056409 mRNA. Translation: AAH56409.1. AF069250 mRNA. Translation: AAC79807.1. Sequence problems. |
| IPI | IPI00107745. IPI00448519. |
| RefSeq | NP_006098.2. NM_006107.3. NP_057508.2. NM_016424.4. |
| UniGene | Hs.130293. |
3D structure databases | |
| ProteinModelPortal | O95232. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | O95232. 6 interactions. |
| MINT | MINT-1683180. |
| STRING | O95232. |
PTM databases | |
| PhosphoSite | O95232. |
Proteomic databases | |
| PeptideAtlas | O95232. |
| PRIDE | O95232. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| Ensembl | ENST00000240304; ENSP00000240304; ENSG00000108848. ENST00000393227; ENSP00000376919; ENSG00000108848. |
| GeneID | 51747. |
| KEGG | hsa:51747. |
| UCSC | uc002isq.2. human. |
Organism-specific databases | |
| CTD | 51747. |
| GeneCards | GC17P048796. |
| H-InvDB | HIX0013986. |
| HGNC | HGNC:24309. LUC7L3. |
| HPA | HPA018475. HPA018484. HPA020017. |
| MIM | 609434. gene. |
| neXtProt | NX_O95232. |
| GenAtlas | Search... |
Phylogenomic databases | |
| eggNOG | prNOG04463. |
| HOGENOM | HBG714380. |
| HOVERGEN | HBG062167. |
| InParanoid | O95232. |
| OMA | ISVPLWK. |
| OrthoDB | EOG4QJRNZ. |
| PhylomeDB | O95232. |
Gene expression databases | |
| ArrayExpress | O95232. |
| Bgee | O95232. |
| Genevestigator | O95232. |
| GermOnline | ENSG00000108848. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR004882. LUC7-rel. [Graphical view] |
| PANTHER | PTHR12375. LUC7_rel. 1 hit. |
| Pfam | PF03194. LUC7. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Other | |
| NextBio | 55830. |
| SOURCE | Search... |
Entry information
| Entry name | LC7L3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O95232 Secondary accession number(s): B3KN54 Q9P2S7 | ||||||||
| 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 17 Human chromosome 17: 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