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O95391 (SLU7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 93. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Pre-mRNA-splicing factor SLU7

Short name=hSlu7
Gene names
Name:SLU7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length586 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.16

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 processmRNA processing
mRNA splicing
   Cellular componentCytoplasm
Nucleus
Spliceosome
   Coding sequence diversityPolymorphism
   DomainZinc-finger
   LigandMetal-binding
Zinc
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA splicing, via transesterification reactions

Inferred from direct assay Ref.1. Source: HGNC

alternative mRNA splicing, via spliceosome

Inferred from direct assay Ref.9. Source: HGNC

cellular response to heat

Inferred from direct assay Ref.16. Source: UniProtKB

intracellular protein transport

Inferred from direct assay Ref.16. Source: UniProtKB

mRNA 3'-splice site recognition

Inferred from direct assay Ref.9. Source: HGNC

mRNA splicing, via spliceosome

Inferred by curator PubMed 11991638. Source: UniProtKB

   Cellular_componentcatalytic step 2 spliceosome

Inferred from direct assay PubMed 11991638. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.16. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

nuclear speck

Inferred from direct assay Ref.9. Source: HGNC

nucleus

Inferred from direct assay Ref.16. Source: UniProtKB

small nuclear ribonucleoprotein complex

Inferred from direct assay Ref.8. Source: HGNC

spliceosomal complex

Inferred from direct assay Ref.1. Source: HGNC

   Molecular_functionpre-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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.14
Chain2 – 586585Pre-mRNA-splicing factor SLU7
PRO_0000289194

Regions

Zinc finger118 – 13518CCHC-type
Motif129 – 16941Bipartite nuclear localization signal

Amino acid modifications

Modified residue21N-acetylserine Ref.14
Modified residue2151Phosphoserine Ref.11 Ref.12 Ref.13 Ref.15 Ref.17
Modified residue2271Phosphoserine Ref.15
Modified residue2351Phosphoserine Ref.15 Ref.17

Natural variations

Natural variant1111I → V. Ref.4
Corresponds to variant rs17856338 [ dbSNP | Ensembl ].
VAR_032598
Natural variant2291M → T. Ref.1 Ref.3 Ref.4 Ref.11 Ref.15
Corresponds to variant rs2961944 [ dbSNP | Ensembl ].
VAR_032599

Experimental info

Mutagenesis1161R → N: Abolishes nuclear localization. Ref.8
Mutagenesis1171K → N: Abolishes nuclear localization. Ref.8
Mutagenesis1201C → S: Induces a cytoplasmic localization; when associated with S-123; G-128 and S-133. Ref.8
Mutagenesis1231C → S: Induces a cytoplasmic localization; when associated with S-120; G-128 and S-133. Ref.8
Mutagenesis125 – 1262AM → VP: Does not affect nuclear localization.
Mutagenesis1281H → G: Induces a cytoplasmic localization; when associated with S-120; S-123 and S-133. Ref.8
Mutagenesis1291K → N: Abolishes nuclear localization. Ref.8
Mutagenesis1331C → S: Induces a cytoplasmic localization; when associated with S-120; S-123 and G-128. Ref.8
Mutagenesis1361R → N: Abolishes nuclear localization.
Mutagenesis1661K → N: Abolishes nuclear localization. Ref.8

Sequences

Sequence LengthMass (Da)Tools
O95391 [UniParc].

Last modified November 3, 2009. Version 2.
Checksum: 237B8C8014EEAB6E

FASTA58668,387
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. 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], 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[15]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[16]"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.
[17]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+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.
RefSeqNP_006416.3. NM_006425.4.
UniGeneHs.435342.

3D structure databases

ProteinModelPortalO95391.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115820. 22 interactions.
IntActO95391. 17 interactions.
MINTMINT-1467161.
STRING9606.ENSP00000297151.

PTM databases

PhosphoSiteO95391.

Proteomic databases

PaxDbO95391.
PRIDEO95391.

Protocols and materials databases

DNASU10569.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000297151; ENSP00000297151; ENSG00000164609.
ENST00000520664; ENSP00000428362; ENSG00000164609.
GeneID10569.
KEGGhsa:10569.
UCSCuc003lyg.3. human.

Organism-specific databases

CTD10569.
GeneCardsGC05M159762.
HGNCHGNC:16939. SLU7.
HPAHPA035907.
MIM605974. gene.
neXtProtNX_O95391.
PharmGKBPA128394574.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG251791.
HOGENOMHOG000194391.
HOVERGENHBG053287.
InParanoidO95391.
KOK12819.
OMAPQTLMEM.
OrthoDBEOG7GQXV9.
PhylomeDBO95391.
TreeFamTF105691.

Gene expression databases

ArrayExpressO95391.
BgeeO95391.
CleanExHS_SLU7.
GenevestigatorO95391.

Family and domain databases

InterProIPR021715. Slu7.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF11708. Slu7. 1 hit.
[Graphical view]
SMARTSM00343. ZnF_C2HC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSSLU7. human.
GeneWikiSLU7.
GenomeRNAi10569.
NextBio40113.
PMAP-CutDBO95391.
PROO95391.
SOURCESearch...

Entry information

Entry nameSLU7_HUMAN
AccessionPrimary (citable) accession number: O95391
Secondary accession number(s): D3DQK2 expand/collapse secondary AC list , Q3LUJ0, Q3LUJ1, Q6RXQ5, Q96FM9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: November 3, 2009
Last modified: April 16, 2014
This is version 93 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 5

Human chromosome 5: entries, gene names and cross-references to MIM