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UniProtKB/Swiss-Prot entry O95232


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CROP_HUMAN
Primary accession number O95232
Secondary accession numbers Q6PHR9 Q9NUY0 Q9P2S7
Integrated into Swiss-Prot on May 30, 2000
Sequence was last modified on May 2, 2006 (Sequence version 2)
Annotations were last modified on    November 25, 2008 (Entry version 48)
Name and origin of the protein
Protein name Cisplatin resistance-associated overexpressed protein
Synonyms cAMP regulatory element-associated protein 1
CRE-associated protein 1
CREAP-1
Luc7A
Okadaic acid-inducible phosphoprotein OA48-18
Gene name
Name: CROP
Synonyms: CREAP1, O48
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
DOI=10.1016/S0014-5793(99)01744-5; PubMed=10631324 [NCBI, ExPASy, EBI, Israel, Japan]
Nishii Y., Morishima M., Kakehi Y., Umehara K., Kioka N., Terano Y., Amachi T., Ueda K.;
"CROP/Luc7A, a novel serine/arginine-rich nuclear protein, isolated from cisplatin-resistant cell line.";
FEBS Lett. 465:153-156(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
TISSUE=Placenta;
DOI=10.1139/o05-139; PubMed=16462885 [NCBI, ExPASy, EBI, Israel, Japan]
Shipman K.L., Robinson P.J., King B.R., Smith R., Nicholson R.C.;
"Identification of a family of DNA-binding proteins with homology to RNA splicing factors.";
Biochem. Cell Biol. 84:9-19(2006).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Placenta;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=PNS;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 378-432.
TISSUE=Fetal brain;
DOI=10.1159/000025441; PubMed=10754390 [NCBI, ExPASy, EBI, Israel, Japan]
Chin L.S., Singh S.K., Wang Q., Murray S.F.;
"Identification of okadaic-acid-induced genes by mRNA differential display in glioma cells.";
J. Biomed. Sci. 7:152-159(2000).
[6]
INTERACTION WITH SFRS1, PHOSPHORYLATION, AND SUBCELLULAR LOCATION.
DOI=10.1016/S0006-291X(02)03017-6; PubMed=12565863 [NCBI, ExPASy, EBI, Israel, Japan]
Umehara H., Nishii Y., Morishima M., Kakehi Y., Kioka N., Amachi T., Koizumi J., Hagiwara M., Ueda K.;
"Effect of cisplatin treatment on speckled distribution of a serine/arginine-rich nuclear protein CROP/Luc7A.";
Biochem. Biophys. Res. Commun. 301:324-329(2003).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-333 AND SER-335, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-110; SER-425 AND THR-429, AND MASS SPECTROMETRY.
DOI=10.1126/science.1140321; PubMed=17525332 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage.";
Science 316:1160-1166(2007).
Comments
  • FUNCTION: Binds cAMP regulatory element DNA sequence. May play a role in RNA splicing.
  • SUBUNIT: May interact with SFRS1 and form homodimers.
  • INTERACTION:
    Q15287:RNPS1; NbExp=1; IntAct=EBI-395671, EBI-395959;
  • SUBCELLULAR LOCATION: Nucleus speckle. Note=The subnuclear localization is affected by cisplatin.
  • ALTERNATIVE PRODUCTS: 2 named isoforms [FASTA] produced by alternative splicing.
    Name1
    Isoform IDO95232-1
    This is the isoform sequence displayed in this entry.
    Name2
    Isoform IDO95232-2
    Note: No experimental confirmation available.
    Features which should be applied to build the isoform sequence: VSP_018136, VSP_018137.
  • 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.
  • PTM: Phosphorylated in vitro by SRPK1, SRPK2 and CLK1. Phosphorylated upon DNA damage, probably by ATM or ATR.
  • SIMILARITY: Belongs to the Luc7 family.
  • SEQUENCE CAUTION:
    • Sequence=AAC79807.1; Type=Erroneous translation; Note=Erroneous CDS prediction
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB034205; BAA90542.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ013876; AAY26238.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001925; BAA91981.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC056409; AAH56409.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF069250; AAC79807.1; ALT_SEQ; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_006098.2; -.
NP_057508.2; -.
UniGene Hs.130293
3D structure databases
ModBase O95232.
Protein-protein interaction databases
IntAct O95232; -.
PTM databases
PhosphoSite O95232; -.
Organism-specific databases
H-InvDB HIX0013986; -.
HIX0039603; -.
MIM 609434; gene. [NCBI / EBI]
GeneCards O95232.
Gene expression databases
ArrayExpress O95232; -.
GermOnline ENSG00000108848; Homo sapiens.
Ontologies
GO
GO:0016607; Cellular component: nuclear speck (inferred from electronic annotation from UniProtKB-SubCell).
GO:0003677; Molecular function: DNA binding (inferred from electronic annotation from UniProtKB-KW).
GO:0003729; Molecular function: mRNA binding (inferred from mutant phenotype from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006915; Biological process: apoptosis (inferred from mutant phenotype from UniProtKB).
GO:0006397; Biological process: mRNA processing (inferred from electronic annotation from UniProtKB-KW).
GO:0006950; Biological process: response to stress (inferred from mutant phenotype from UniProtKB).
GO:0008380; Biological process: RNA splicing (inferred from mutant phenotype from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR004882; LUC7_rel.
Graphical view of domain structure.
PANTHER PTHR12375; LUC7_rel; 1.
Pfam PF03194; LUC7; 1.
Pfam graphical view of domain structure.
ProtoNet O95232.
Proteomic databases
PeptideAtlas O95232; -.
Genome annotation databases
Ensembl ENSG00000108848; Homo sapiens. [Contig view]
GeneID 51747; -.
KEGG hsa:51747; -.
Phylogenomic databases
HOGENOM O95232; -.
HOVERGEN O95232; -.
Other
NextBio 55830; -.
SOURCE CROP; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Coiled coil; DNA-binding; mRNA processing; mRNA splicing; Nucleus; Phosphoprotein.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   432  432     Cisplatin resistance-associated overexpressed protein. PRO_0000058013
COILED   124   181  58     Potential. 
COMPBIAS   228   282  55     Glu-rich. 
COMPBIAS   235   395  161     Arg/Ser-rich. 
MOD_RES   110   110        Phosphoserine. 
MOD_RES   333   333        Phosphoserine. 
MOD_RES   335   335        Phosphoserine. 
MOD_RES   425   425        Phosphoserine. 
MOD_RES   429   429        Phosphothreonine. 
MOD_RES   431   431        Phosphoserine (By similarity). 
VAR_SEQ   56    79        GPCEKIHDENLRKQYEKSSRFMKV -> DVFGRGDNISDVSKFLEDDKWMEE (in isoform 2). VSP_018136
VAR_SEQ   80   432        Missing (in isoform 2). VSP_018137
CONFLICT   217   217        H -> Y (in Ref. 3; BAA91981). 
CONFLICT   378   379        EK -> HE (in Ref. 3). 
Sequence information
Length: 432 AA [This is the length of the unprocessed precursor] Molecular weight: 51466 Da [This is the MW of the unprocessed precursor] CRC64: E75F55EC0137310C [This is a checksum on the sequence]
        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 

O95232 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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