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O95232

- LC7L3_HUMAN

UniProt

O95232 - LC7L3_HUMAN

Protein

Luc7-like protein 3

Gene

LUC7L3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 105 (01 Oct 2014)
      Sequence version 2 (02 May 2006)
      Previous versions | rss
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    Functioni

    Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing.1 Publication

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. mRNA binding Source: UniProtKB
    3. poly(A) RNA binding Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. mRNA splice site selection Source: InterPro
    2. RNA splicing Source: UniProtKB

    Keywords - Biological processi

    mRNA processing, mRNA splicing

    Keywords - Ligandi

    DNA-binding

    Names & Taxonomyi

    Protein namesi
    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 namesi
    Name:LUC7L3
    Synonyms:CREAP1, CROP, O48
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:24309. LUC7L3.

    Subcellular locationi

    Nucleus speckle 2 Publications
    Note: The subnuclear localization is affected by cisplatin.

    GO - Cellular componenti

    1. focal adhesion Source: HPA
    2. nuclear speck Source: UniProtKB-SubCell
    3. nucleus Source: UniProtKB
    4. plasma membrane Source: HPA
    5. U1 snRNP Source: InterPro

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA165432062.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 432432Luc7-like protein 3PRO_0000058013Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei3 – 31Phosphoserine2 Publications
    Modified residuei110 – 1101Phosphoserine2 Publications
    Modified residuei231 – 2311N6-acetyllysine1 Publication
    Modified residuei420 – 4201Phosphoserine2 Publications
    Modified residuei425 – 4251Phosphoserine5 Publications
    Modified residuei431 – 4311Phosphoserine3 Publications

    Post-translational modificationi

    Phosphorylated in vitro by SRPK1, SRPK2 and CLK1.6 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO95232.
    PaxDbiO95232.
    PeptideAtlasiO95232.
    PRIDEiO95232.

    PTM databases

    PhosphoSiteiO95232.

    Expressioni

    Tissue specificityi

    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.2 Publications

    Gene expression databases

    ArrayExpressiO95232.
    BgeeiO95232.
    GenevestigatoriO95232.

    Organism-specific databases

    HPAiHPA018475.
    HPA018484.
    HPA020017.

    Interactioni

    Subunit structurei

    May interact with SFRS1 and form homodimers. Interacts with JMJD6 and RBM25. Interacts with RSRC1 (via Arg/Ser-rich domain).4 Publications

    Protein-protein interaction databases

    BioGridi119710. 38 interactions.
    IntActiO95232. 6 interactions.
    MINTiMINT-1683180.
    STRINGi9606.ENSP00000240304.

    Structurei

    3D structure databases

    ProteinModelPortaliO95232.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili124 – 18158Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi228 – 28255Glu-richAdd
    BLAST
    Compositional biasi235 – 395161Arg/Ser-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the Luc7 family.Curated

    Keywords - Domaini

    Coiled coil

    Phylogenomic databases

    eggNOGiCOG5200.
    HOGENOMiHOG000215956.
    HOVERGENiHBG062167.
    InParanoidiO95232.
    OrthoDBiEOG78H3TX.
    PhylomeDBiO95232.
    TreeFamiTF354312.

    Family and domain databases

    InterProiIPR004882. Luc7-rel.
    [Graphical view]
    PANTHERiPTHR12375. PTHR12375. 1 hit.
    PfamiPF03194. LUC7. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95232-1) [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

    MISAAQLLDE LMGRDRNLAP DEKRSNVRWD HESVCKYYLC GFCPAELFTN    50
    TRSDLGPCEK IHDENLRKQY EKSSRFMKVG YERDFLRYLQ SLLAEVERRI 100
    RRGHARLALS QNQQSSGAAG PTGKNEEKIQ VLTDKIDVLL QQIEELGSEG 150
    KVEEAQGMMK LVEQLKEERE LLRSTTSTIE SFAAQEKQME VCEVCGAFLI 200
    VGDAQSRVDD HLMGKQHMGY AKIKATVEEL KEKLRKRTEE PDRDERLKKE 250
    KQEREEREKE REREREERER KRRREEEERE KERARDRERR KRSRSRSRHS 300
    SRTSDRRCSR SRDHKRSRSR ERRRSRSRDR RRSRSHDRSE RKHRSRSRDR 350
    RRSKSRDRKS YKHRSKSRDR EQDRKSKEKE KRGSDDKKSS VKSGSREKQS 400
    EDTNTESKES DTKNEVNGTS EDIKSEGDTQ SN 432
    Length:432
    Mass (Da):51,466
    Last modified:May 2, 2006 - v2
    Checksum:iE75F55EC0137310C
    GO
    Isoform 2 (identifier: O95232-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         56-79: GPCEKIHDENLRKQYEKSSRFMKV → DVFGRGDNISDVSKFLEDDKWMEE
         80-432: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay. No experimental confirmation available.

    Show »
    Length:79
    Mass (Da):9,194
    Checksum:iD204FE4F76DF2FD2
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti217 – 2171H → Y in BAA91981. (PubMed:14702039)Curated
    Sequence conflicti378 – 3792EK → HE in AAC79807. (PubMed:10754390)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei56 – 7924GPCEK…RFMKV → DVFGRGDNISDVSKFLEDDK WMEE in isoform 2. 1 PublicationVSP_018136Add
    BLAST
    Alternative sequencei80 – 432353Missing in isoform 2. 1 PublicationVSP_018137Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS11573.1. [O95232-1]
    RefSeqiNP_006098.2. NM_006107.3. [O95232-1]
    NP_057508.2. NM_016424.4. [O95232-1]
    UniGeneiHs.130293.

    Genome annotation databases

    EnsembliENST00000240304; ENSP00000240304; ENSG00000108848. [O95232-1]
    ENST00000505658; ENSP00000425092; ENSG00000108848. [O95232-1]
    GeneIDi51747.
    KEGGihsa:51747.
    UCSCiuc002isr.3. human. [O95232-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSi CCDS11573.1. [O95232-1 ]
    RefSeqi NP_006098.2. NM_006107.3. [O95232-1 ]
    NP_057508.2. NM_016424.4. [O95232-1 ]
    UniGenei Hs.130293.

    3D structure databases

    ProteinModelPortali O95232.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119710. 38 interactions.
    IntActi O95232. 6 interactions.
    MINTi MINT-1683180.
    STRINGi 9606.ENSP00000240304.

    PTM databases

    PhosphoSitei O95232.

    Proteomic databases

    MaxQBi O95232.
    PaxDbi O95232.
    PeptideAtlasi O95232.
    PRIDEi O95232.

    Protocols and materials databases

    DNASUi 51747.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000240304 ; ENSP00000240304 ; ENSG00000108848 . [O95232-1 ]
    ENST00000505658 ; ENSP00000425092 ; ENSG00000108848 . [O95232-1 ]
    GeneIDi 51747.
    KEGGi hsa:51747.
    UCSCi uc002isr.3. human. [O95232-1 ]

    Organism-specific databases

    CTDi 51747.
    GeneCardsi GC17P048796.
    HGNCi HGNC:24309. LUC7L3.
    HPAi HPA018475.
    HPA018484.
    HPA020017.
    MIMi 609434. gene.
    neXtProti NX_O95232.
    PharmGKBi PA165432062.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5200.
    HOGENOMi HOG000215956.
    HOVERGENi HBG062167.
    InParanoidi O95232.
    OrthoDBi EOG78H3TX.
    PhylomeDBi O95232.
    TreeFami TF354312.

    Miscellaneous databases

    ChiTaRSi LUC7L3. human.
    GeneWikii CROP_(gene).
    GenomeRNAii 51747.
    NextBioi 55830.
    PROi O95232.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95232.
    Bgeei O95232.
    Genevestigatori O95232.

    Family and domain databases

    InterProi IPR004882. Luc7-rel.
    [Graphical view ]
    PANTHERi PTHR12375. PTHR12375. 1 hit.
    Pfami PF03194. LUC7. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [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.
      , 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] (ISOFORM 1).
      Tissue: Placenta.
    4. 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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RSRC1.
    9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    10. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RBM25.
    11. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425 AND SER-431, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    12. "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 MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "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-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    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-231, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: INTERACTION WITH JMJD6.
    16. "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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-3; SER-425 AND SER-431, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "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-420 AND SER-425, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    20. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiLC7L3_HUMAN
    AccessioniPrimary (citable) accession number: O95232
    Secondary accession number(s): B3KN54
    , D3DTY1, Q6PHR9, Q9NUY0, Q9P2S7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2000
    Last sequence update: May 2, 2006
    Last modified: October 1, 2014
    This is version 105 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3