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O95232 (LC7L3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:LUC7L3
Synonyms:CREAP1, CROP, O48
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length432 AA.
Sequence statusComplete.
Protein existenceEvidence 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.10 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. Ref.7

Sequence similarities

Belongs to the Luc7 family.

Sequence caution

The sequence AAC79807.1 differs from that shown. Reason: Erroneous translation. Erroneous CDS prediction.

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: 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 432432Luc7-like protein 3
PRO_0000058013

Regions

Coiled coil124 – 18158 Potential
Compositional bias228 – 28255Glu-rich
Compositional bias235 – 395161Arg/Ser-rich

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12 Ref.16 Ref.20
Modified residue31Phosphoserine Ref.16
Modified residue1101Phosphoserine Ref.9
Modified residue2311N6-acetyllysine Ref.14
Modified residue4201Phosphoserine Ref.18
Modified residue4251Phosphoserine Ref.11 Ref.13 Ref.16 Ref.18
Modified residue4311Phosphoserine Ref.11 Ref.16

Natural variations

Alternative sequence56 – 7924GPCEK…RFMKV → DVFGRGDNISDVSKFLEDDK WMEE in isoform 2.
VSP_018136
Alternative sequence80 – 432353Missing in isoform 2.
VSP_018137

Experimental info

Sequence conflict2171H → Y in BAA91981. Ref.3
Sequence conflict378 – 3792EK → HE in AAC79807. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 2, 2006. Version 2.
Checksum: E75F55EC0137310C

FASTA43251,466
        10         20         30         40         50         60 
MISAAQLLDE LMGRDRNLAP DEKRSNVRWD HESVCKYYLC GFCPAELFTN TRSDLGPCEK 

        70         80         90        100        110        120 
IHDENLRKQY EKSSRFMKVG YERDFLRYLQ SLLAEVERRI RRGHARLALS QNQQSSGAAG 

       130        140        150        160        170        180 
PTGKNEEKIQ VLTDKIDVLL QQIEELGSEG KVEEAQGMMK LVEQLKEERE LLRSTTSTIE 

       190        200        210        220        230        240 
SFAAQEKQME VCEVCGAFLI VGDAQSRVDD HLMGKQHMGY AKIKATVEEL KEKLRKRTEE 

       250        260        270        280        290        300 
PDRDERLKKE KQEREEREKE REREREERER KRRREEEERE KERARDRERR KRSRSRSRHS 

       310        320        330        340        350        360 
SRTSDRRCSR SRDHKRSRSR ERRRSRSRDR RRSRSHDRSE RKHRSRSRDR RRSKSRDRKS 

       370        380        390        400        410        420 
YKHRSKSRDR EQDRKSKEKE KRGSDDKKSS VKSGSREKQS EDTNTESKES DTKNEVNGTS 

       430 
EDIKSEGDTQ SN 

« Hide

Isoform 2 [UniParc].

Checksum: D204FE4F76DF2FD2
Show »

FASTA799,194

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] [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. expand/collapse author list , 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]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. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., 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] [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]"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: 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]"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-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]"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] [Europe PMC] [Abstract]
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]"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].
[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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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.
RefSeqNP_006098.2. NM_006107.3.
NP_057508.2. NM_016424.4.
UniGeneHs.130293.

3D structure databases

ProteinModelPortalO95232.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119710. 33 interactions.
IntActO95232. 6 interactions.
MINTMINT-1683180.
STRING9606.ENSP00000240304.

PTM databases

PhosphoSiteO95232.

Proteomic databases

PaxDbO95232.
PeptideAtlasO95232.
PRIDEO95232.

Protocols and materials databases

DNASU51747.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000240304; ENSP00000240304; ENSG00000108848. [O95232-1]
ENST00000505658; ENSP00000425092; ENSG00000108848. [O95232-1]
GeneID51747.
KEGGhsa:51747.
UCSCuc002isr.3. human. [O95232-1]

Organism-specific databases

CTD51747.
GeneCardsGC17P048796.
HGNCHGNC:24309. LUC7L3.
HPAHPA018475.
HPA018484.
HPA020017.
MIM609434. gene.
neXtProtNX_O95232.
PharmGKBPA165432062.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5200.
HOGENOMHOG000215956.
HOVERGENHBG062167.
InParanoidO95232.
OrthoDBEOG78H3TX.
PhylomeDBO95232.
TreeFamTF354312.

Gene expression databases

ArrayExpressO95232.
BgeeO95232.
GenevestigatorO95232.

Family and domain databases

InterProIPR004882. Luc7-rel.
[Graphical view]
PANTHERPTHR12375. PTHR12375. 1 hit.
PfamPF03194. LUC7. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSLUC7L3. human.
GeneWikiCROP_(gene).
GenomeRNAi51747.
NextBio55830.
PROO95232.
SOURCESearch...

Entry information

Entry nameLC7L3_HUMAN
AccessionPrimary (citable) accession number: O95232
Secondary accession number(s): B3KN54 expand/collapse secondary AC list , D3DTY1, Q6PHR9, Q9NUY0, Q9P2S7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 2, 2006
Last modified: April 16, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM