O95391 (SLU7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Pre-mRNA-splicing factor SLU7
Short name=hSlu7

Gene names

Name:

SLU7

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	586 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Participates in the second catalytic step of pre-mRNA splicing, when the free hydroxyl group of exon I attacks the 3'-splice site to generate spliced mRNA and the excised lariat intron. Required for holding exon 1 properly in the spliceosome and for correct AG identification when more than one possible AG exists in 3'-splicing site region. May be involved in the activation of proximal AG. Probably also involved in alternative splicing regulation. Ref.1 Ref.6 Ref.7 Ref.9
Subunit structure	Component of late spliceosomal complexes. Associates with the spliceosome prior to recognition of the 3'-splice site for step II, probably during catalysis of step I.
Subcellular location	Nucleus. Cytoplasm. Note: Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. Upon UV-C stress stimulus, the nuclear concentration of the protein decreases, affecting alternative splicing. Translocates from the nucleus to the cytoplasm after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules. Ref.1 Ref.8 Ref.9 Ref.15
Domain	The CCHC-type zinc finger is required to retain the protein within the nucleus and prevent its shuttle back to the cytoplasm via the CRM1 pathway. Ref.8
Sequence similarities	Belongs to the SLU7 family. Contains 1 CCHC-type zinc finger.

Ontologies

Keywords
Biological process	mRNA processing mRNA splicing
Cellular component	Cytoplasm Nucleus Spliceosome
Coding sequence diversity	Polymorphism
Domain	Zinc-finger
Ligand	Metal-binding Zinc
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	alternative mRNA splicing, via spliceosome Inferred from direct assay Ref.9. Source: HGNC cellular response to stress Inferred from direct assay PubMed 19369195. Source: UniProtKB intracellular protein transport Inferred from direct assay PubMed 19369195. Source: UniProtKB mRNA 3'-splice site recognition Inferred from direct assay Ref.9. Source: HGNC
Cellular_component	catalytic step 2 spliceosome Inferred from direct assay PubMed 11991638. Source: UniProtKB cytoplasm Inferred from direct assay PubMed 19369195. Source: UniProtKB nuclear speck Inferred from direct assay Ref.9. Source: HGNC small nuclear ribonucleoprotein complex Inferred from direct assay Ref.8. Source: HGNC
Molecular_function	pre-mRNA 3'-splice site binding Inferred from direct assay Ref.9. Source: HGNC second spliceosomal transesterification activity Inferred from direct assay Ref.1. Source: HGNC zinc ion binding Inferred from direct assay Ref.8. Source: HGNC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 586	586	Pre-mRNA-splicing factor SLU7		PRO_0000289194
Regions
	Zinc finger	118 – 135	18	CCHC-type
	Motif	129 – 169	41	Bipartite nuclear localization signal
Amino acid modifications
	Modified residue	215	1	Phosphoserine Ref.11 Ref.12 Ref.13 Ref.14 Ref.16
	Modified residue	227	1	Phosphoserine Ref.14
	Modified residue	235	1	Phosphoserine Ref.14 Ref.16
Natural variations
	Natural variant	111	1	I → V. Ref.4 Corresponds to variant rs17856338 [ dbSNP | Ensembl ].		VAR_032598
	Natural variant	229	1	M → T. Ref.1 Ref.3 Ref.4 Ref.11 Ref.14 Corresponds to variant rs2961944 [ dbSNP | Ensembl ].		VAR_032599
Experimental info
	Mutagenesis	116	1	R → N: Abolishes nuclear localization. Ref.8
	Mutagenesis	117	1	K → N: Abolishes nuclear localization. Ref.8
	Mutagenesis	120	1	C → S: Induces a cytoplasmic localization; when associated with S-123; G-128 and S-133. Ref.8
	Mutagenesis	123	1	C → S: Induces a cytoplasmic localization; when associated with S-120; G-128 and S-133. Ref.8
	Mutagenesis	125 – 126	2	AM → VP: Does not affect nuclear localization.
	Mutagenesis	128	1	H → G: Induces a cytoplasmic localization; when associated with S-120; S-123 and S-133. Ref.8
	Mutagenesis	129	1	K → N: Abolishes nuclear localization. Ref.8
	Mutagenesis	133	1	C → S: Induces a cytoplasmic localization; when associated with S-120; S-123 and G-128. Ref.8
	Mutagenesis	136	1	R → N: Abolishes nuclear localization.
	Mutagenesis	166	1	K → N: Abolishes nuclear localization. Ref.8

Sequences

	Sequence		Length	Mass (Da)
	O95391 [UniParc]. Last modified November 3, 2009. Version 2. Checksum: 237B8C8014EEAB6E	FASTA	586	68,387
	10 20 30 40 50 60 MSATVVDAVN AAPLSGSKEM SLEEPKKMTR EDWRKKKELE EQRKLGNAPA EVDEEGKDIN 70 80 90 100 110 120 PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE WYKRGVKENS IITKYRKGAC 130 140 150 160 170 180 ENCGAMTHKK KDCFERPRRV GAKFTGTNIA PDEHVQPQLM FDYDGKRDRW NGYNPEEHMK 190 200 210 220 230 240 IVEEYAKVDL AKRTLKAQKL QEELASGKLV EQANSPKHQW GEEEPNSQME KDHNSEDEDE 250 260 270 280 290 300 DKYADDIDMP GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA 310 320 330 340 350 360 GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDKGSE VHLQADPTKL ELLYKSFKVK 370 380 390 400 410 420 KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY SRHGTVIKGQ ERAVACSKYE 430 440 450 460 470 480 EDVKIHNHTH IWGSYWKEGR WGYKCCHSFF KYSYCTGEAG KEIVNSEECI INEITGEESV 490 500 510 520 530 540 KKPQTLMELH QEKLKEEKKK KKKKKKKHRK SSSDSDDEEK KHEKLKKALN AEEARLLHVK 550 560 570 580 ETMQIDERKR PYNSMYETRE PTEEEMEAYR MKRQRPDDPM ASFLGQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Human step II splicing factor hSlu7 functions in restructuring the spliceosome between the catalytic steps of splicing." Chua K., Reed R. Genes Dev. 13:841-850(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH LATE SPLICEOSOMAL COMPLEX, VARIANT THR-229.
[2]	"The DNA sequence and comparative analysis of human chromosome 5." Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S. , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M. Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	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], VARIANT THR-229.
[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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS VAL-111 AND THR-229. Tissue: Eye.
[5]	Holste D., Shomron N., Burge C.B. Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-102. Tissue: Colon.
[6]	"The RNA splicing factor hSlu7 is required for correct 3' splice-site choice." Chua K., Reed R. Nature 402:207-210(1999) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[7]	"The birth of an alternatively spliced exon: 3' splice-site selection in Alu exons." Lev-Maor G., Sorek R., Shomron N., Ast G. Science 300:1288-1291(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION.
[8]	"Splicing factor hSlu7 contains a unique functional domain required to retain the protein within the nucleus." Shomron N., Reznik M., Ast G. Mol. Biol. Cell 15:3782-3795(2004) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION, DOMAIN CCHC-TYPE ZINC FINGER, ZINC-BINDING, MUTAGENESIS OF ARG-116; LYS-117; CYS-120; CYS-123; 125-ALA-MET-126; HIS-128; LYS-129; CYS-133 AND LYS-166.
[9]	"Stress alters the subcellular distribution of hSlu7 and thus modulates alternative splicing." Shomron N., Alberstein M., Reznik M., Ast G. J. Cell Sci. 118:1151-1159(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION.
[10]	Erratum Shomron N., Alberstein M., Reznik M., Ast G. J. Cell Sci. 118:1331-1331(2005)
[11]	"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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, VARIANT [LARGE SCALE ANALYSIS] THR-229, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-215; SER-227 AND SER-235, VARIANT [LARGE SCALE ANALYSIS] THR-229, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Stress induced subcellular distribution of ALG-2, RBM22 and hSlu7." Janowicz A., Michalak M., Krebs J. Biochim. Biophys. Acta 1813:1045-1049(2011) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION.
[16]	"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-215 AND SER-235, MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF101074 mRNA. Translation: AAD13774.1. AC091842 Genomic DNA. No translation available. CH471062 Genomic DNA. Translation: EAW61554.1. CH471062 Genomic DNA. Translation: EAW61555.1. BC010634 mRNA. Translation: AAH10634.1. AY486334 mRNA. Translation: AAS59410.1. DQ174516 mRNA. Translation: ABA08382.1. DQ174517 mRNA. Translation: ABA08383.1.
IPI	IPI00294435.
RefSeq	NP_006416.3. NM_006425.4.
UniGene	Hs.435342.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O95391. 5 interactions.
MINT	MINT-1467161.
STRING	9606.ENSP00000297151.
PTM databases
PhosphoSite	O95391.
Proteomic databases
PaxDb	O95391.
PRIDE	O95391.
Protocols and materials databases
DNASU	10569.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000297151; ENSP00000297151; ENSG00000164609. ENST00000520664; ENSP00000428362; ENSG00000164609.
GeneID	10569.
KEGG	hsa:10569.
UCSC	uc003lyg.3. human.
Organism-specific databases
CTD	10569.
GeneCards	GC05M159762.
HGNC	HGNC:16939. SLU7.
HPA	HPA035907.
MIM	605974. gene.
neXtProt	NX_O95391.
PharmGKB	PA128394574.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG251791.
HOGENOM	HOG000194391.
HOVERGEN	HBG053287.
InParanoid	O95391.
KO	K12819.
OMA	PQTLMEM.
OrthoDB	EOG42RD76.
PhylomeDB	O95391.
Gene expression databases
ArrayExpress	O95391.
Bgee	O95391.
CleanEx	HS_SLU7.
Genevestigator	O95391.
Family and domain databases
InterPro	IPR021715. Slu7. IPR001878. Znf_CCHC. [Graphical view]
Pfam	PF11708. Slu7. 1 hit. [Graphical view]
SMART	SM00343. ZnF_C2HC. 1 hit. [Graphical view]
PROSITE	PS50158. ZF_CCHC. False negative. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	SLU7. human.
GenomeRNAi	10569.
NextBio	40113.
PMAP-CutDB	O95391.
SOURCE	Search...

Entry information

Entry name

SLU7_HUMAN

Accession

Primary (citable) accession number: O95391
Secondary accession number(s): D3DQK2 , Q3LUJ0, Q3LUJ1, Q6RXQ5, Q96FM9

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 29, 2007
Last sequence update:	November 3, 2009
Last modified:	April 3, 2013
This is version 86 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.