O95232 (LC7L3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names 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

Name:	LUC7L3
Synonyms:	CREAP1, CROP, O48

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 process Inferred from mutant phenotype Ref.6. Source: UniProtKB mRNA processing Inferred from electronic annotation. Source: UniProtKB-KW response to stress Inferred from mutant phenotype Ref.6. Source: UniProtKB
Cellular component	focal adhesion Inferred from direct assay. Source: HPA nuclear speck Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA binding Inferred from mutant phenotype Ref.1. Source: UniProtKB protein binding Inferred 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

	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 [UniParc]. 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]	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. , 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: 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 , D3DTY1, Q6PHR9, Q9NUY0, Q9P2S7

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2000
Last sequence update:	May 2, 2006
Last modified:	January 25, 2012
This is version 78 of the entry and version 2 of the sequence. [Complete 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.