Reviewed, UniProtKB/Swiss-Prot O95232 (CROP_HUMAN)

Names and origin

Protein names

Recommended name:
    Cisplatin resistance-associated overexpressed protein
Alternative name(s):
    cAMP regulatory element-associated protein 1
      Short name=CRE-associated protein 1
      Short name=CREAP-1
    Luc7A
    Okadaic acid-inducible phosphoprotein OA48-18

Gene names

Name:	CROP
Synonyms:	CREAP1, O48

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	432 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
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.
Subcellular location	Nucleus speckle. Note: The subnuclear localization is affected by cisplatin. Ref.1 Ref.6
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.2 Ref.1
Post-translational modification	Phosphorylated in vitro by SRPK1, SRPK2 and CLK1. Phosphorylated upon DNA damage, probably by ATM or ATR. Ref.6 Ref.7 Ref.8 Ref.9
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	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	RNA splicing Ref.1 Inferred from mutant phenotype. Source: UniProtKB apoptosis Ref.5 Inferred from mutant phenotype. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW response to stress Ref.5 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA binding Ref.1 Inferred from mutant phenotype. Source: UniProtKB protein binding Inferred from physical interaction. Source: IntAct
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	Cisplatin resistance-associated overexpressed protein		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	110	1	Phosphoserine Ref.8
	Modified residue	333	1	Phosphoserine Ref.7
	Modified residue	335	1	Phosphoserine Ref.7
	Modified residue	425	1	Phosphoserine Ref.8 Ref.9
	Modified residue	429	1	Phosphothreonine Ref.8
	Modified residue	431	1	Phosphoserine Ref.9
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

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 2, 2006. Version 2. Checksum: E75F55EC0137310C	FASTA	432	51,466
	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
	Isoform 2. Checksum: D204FE4F76DF2FD2	FASTA	79	9,194
	10 20 30 40 50 60 MISAAQLLDE LMGRDRNLAP DEKRSNVRWD HESVCKYYLC GFCPAELFTN TRSDLDVFGR 70 GDNISDVSKF LEDDKWMEE

References

	« Hide 'large scale' referencesShow '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. , 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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Placenta.
[4]	"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.
[5]	"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.
[6]	"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.
[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-333 AND SER-335, MASS SPECTROMETRY. Tissue: Epithelium.
[8]	"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.
[9]	"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.
[10]	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
EMBLGenBankDDBJ	AB034205 mRNA. Translation: BAA90542.1. DQ013876 mRNA. Translation: AAY26238.1. AK001925 mRNA. Translation: BAA91981.1. BC056409 mRNA. Translation: AAH56409.1. AF069250 mRNA. Translation: AAC79807.1. Sequence problems.
IPI	IPI00107745. IPI00448519.
RefSeq	NP_006098.2. NP_057508.2.
UniGene	Hs.130293
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O95232. 6 interactions.
PTM databases
PhosphoSite	O95232.
Proteomic databases
PeptideAtlas	O95232.
PRIDE	O95232.
Genome annotation databases
Ensembl	ENSG00000108848. Homo sapiens. [Contig view]
GeneID	51747.
KEGG	hsa:51747.
UCSC	uc002isq.2. human.
Organism-specific databases
GeneCards	GC17P046151.
H-InvDB	HIX0013986. HIX0039603.
MIM	609434. gene.
Phylogenomic databases
HOGENOM	O95232.
HOVERGEN	O95232.
OMA	O95232. RTQSHVT.
Gene expression databases
ArrayExpress	O95232.
Bgee	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 Resources
NextBio	55830.
SOURCE	Search...

Entry information

Entry name

CROP_HUMAN

Accession

Primary (citable) accession number: O95232
Secondary accession number(s): Q6PHR9, Q9NUY0, Q9P2S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 2, 2006
Last modified:	July 7, 2009
This is version 54 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)