SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O95391

- SLU7_HUMAN

UniProt

O95391 - SLU7_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Pre-mRNA-splicing factor SLU7

Gene
SLU7
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri118 – 13518CCHC-typeAdd
BLAST

GO - Molecular functioni

  1. pre-mRNA 3'-splice site binding Source: HGNC
  2. protein binding Source: IntAct
  3. second spliceosomal transesterification activity Source: HGNC
  4. zinc ion binding Source: HGNC

GO - Biological processi

  1. alternative mRNA splicing, via spliceosome Source: HGNC
  2. cellular response to heat Source: UniProtKB
  3. intracellular protein transport Source: UniProtKB
  4. mRNA 3'-splice site recognition Source: HGNC
  5. mRNA splicing, via spliceosome Source: UniProtKB
  6. RNA splicing, via transesterification reactions Source: HGNC
Complete GO annotation...

Keywords - Biological processi

mRNA processing, mRNA splicing

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Pre-mRNA-splicing factor SLU7
Short name:
hSlu7
Gene namesi
Name:SLU7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:16939. SLU7.

Subcellular locationi

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.4 Publications

GO - Cellular componenti

  1. catalytic step 2 spliceosome Source: UniProtKB
  2. cytoplasm Source: UniProtKB
  3. intracellular membrane-bounded organelle Source: HPA
  4. nuclear speck Source: HGNC
  5. nucleus Source: UniProtKB
  6. small nuclear ribonucleoprotein complex Source: HGNC
  7. spliceosomal complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi116 – 1161R → N: Abolishes nuclear localization. 1 Publication
Mutagenesisi117 – 1171K → N: Abolishes nuclear localization. 1 Publication
Mutagenesisi120 – 1201C → S: Induces a cytoplasmic localization; when associated with S-123; G-128 and S-133. 1 Publication
Mutagenesisi123 – 1231C → S: Induces a cytoplasmic localization; when associated with S-120; G-128 and S-133. 1 Publication
Mutagenesisi125 – 1262AM → VP: Does not affect nuclear localization.
Mutagenesisi128 – 1281H → G: Induces a cytoplasmic localization; when associated with S-120; S-123 and S-133. 1 Publication
Mutagenesisi129 – 1291K → N: Abolishes nuclear localization. 1 Publication
Mutagenesisi133 – 1331C → S: Induces a cytoplasmic localization; when associated with S-120; S-123 and G-128. 1 Publication
Mutagenesisi136 – 1361R → N: Abolishes nuclear localization.
Mutagenesisi166 – 1661K → N: Abolishes nuclear localization. 1 Publication

Organism-specific databases

PharmGKBiPA128394574.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 586585Pre-mRNA-splicing factor SLU7PRO_0000289194Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine1 Publication
Modified residuei215 – 2151Phosphoserine5 Publications
Modified residuei227 – 2271Phosphoserine1 Publication
Modified residuei235 – 2351Phosphoserine2 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO95391.
PaxDbiO95391.
PRIDEiO95391.

PTM databases

PhosphoSiteiO95391.

Miscellaneous databases

PMAP-CutDBO95391.

Expressioni

Gene expression databases

ArrayExpressiO95391.
BgeeiO95391.
CleanExiHS_SLU7.
GenevestigatoriO95391.

Organism-specific databases

HPAiHPA035907.

Interactioni

Subunit structurei

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.

Binary interactionsi

WithEntry#Exp.IntActNotes
PRPF3O433952EBI-750559,EBI-744322
PRPF8Q6P2Q92EBI-750559,EBI-538479
SF3B2Q134352EBI-750559,EBI-749111
WHSC1L1Q9BZ952EBI-750559,EBI-3390132

Protein-protein interaction databases

BioGridi115820. 22 interactions.
IntActiO95391. 17 interactions.
MINTiMINT-1467161.
STRINGi9606.ENSP00000297151.

Structurei

3D structure databases

ProteinModelPortaliO95391.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi129 – 16941Bipartite nuclear localization signalAdd
BLAST

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the SLU7 family.

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG251791.
HOGENOMiHOG000194391.
HOVERGENiHBG053287.
InParanoidiO95391.
KOiK12819.
OMAiEECIIND.
OrthoDBiEOG7GQXV9.
PhylomeDBiO95391.
TreeFamiTF105691.

Family and domain databases

InterProiIPR021715. Slu7.
IPR001878. Znf_CCHC.
[Graphical view]
PfamiPF11708. Slu7. 1 hit.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O95391-1 [UniParc]FASTAAdd to Basket

« Hide

MSATVVDAVN AAPLSGSKEM SLEEPKKMTR EDWRKKKELE EQRKLGNAPA    50
EVDEEGKDIN PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE 100
WYKRGVKENS IITKYRKGAC ENCGAMTHKK KDCFERPRRV GAKFTGTNIA 150
PDEHVQPQLM FDYDGKRDRW NGYNPEEHMK IVEEYAKVDL AKRTLKAQKL 200
QEELASGKLV EQANSPKHQW GEEEPNSQME KDHNSEDEDE DKYADDIDMP 250
GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA 300
GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDKGSE VHLQADPTKL 350
ELLYKSFKVK KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY 400
SRHGTVIKGQ ERAVACSKYE EDVKIHNHTH IWGSYWKEGR WGYKCCHSFF 450
KYSYCTGEAG KEIVNSEECI INEITGEESV KKPQTLMELH QEKLKEEKKK 500
KKKKKKKHRK SSSDSDDEEK KHEKLKKALN AEEARLLHVK ETMQIDERKR 550
PYNSMYETRE PTEEEMEAYR MKRQRPDDPM ASFLGQ 586
Length:586
Mass (Da):68,387
Last modified:November 3, 2009 - v2
Checksum:i237B8C8014EEAB6E
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti111 – 1111I → V.1 Publication
Corresponds to variant rs17856338 [ dbSNP | Ensembl ].
VAR_032598
Natural varianti229 – 2291M → T.5 Publications
Corresponds to variant rs2961944 [ dbSNP | Ensembl ].
VAR_032599

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
CCDSiCCDS4352.1.
RefSeqiNP_006416.3. NM_006425.4.
UniGeneiHs.435342.

Genome annotation databases

EnsembliENST00000297151; ENSP00000297151; ENSG00000164609.
ENST00000520664; ENSP00000428362; ENSG00000164609.
GeneIDi10569.
KEGGihsa:10569.
UCSCiuc003lyg.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
CCDSi CCDS4352.1.
RefSeqi NP_006416.3. NM_006425.4.
UniGenei Hs.435342.

3D structure databases

ProteinModelPortali O95391.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115820. 22 interactions.
IntActi O95391. 17 interactions.
MINTi MINT-1467161.
STRINGi 9606.ENSP00000297151.

PTM databases

PhosphoSitei O95391.

Proteomic databases

MaxQBi O95391.
PaxDbi O95391.
PRIDEi O95391.

Protocols and materials databases

DNASUi 10569.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000297151 ; ENSP00000297151 ; ENSG00000164609 .
ENST00000520664 ; ENSP00000428362 ; ENSG00000164609 .
GeneIDi 10569.
KEGGi hsa:10569.
UCSCi uc003lyg.3. human.

Organism-specific databases

CTDi 10569.
GeneCardsi GC05M159762.
HGNCi HGNC:16939. SLU7.
HPAi HPA035907.
MIMi 605974. gene.
neXtProti NX_O95391.
PharmGKBi PA128394574.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG251791.
HOGENOMi HOG000194391.
HOVERGENi HBG053287.
InParanoidi O95391.
KOi K12819.
OMAi EECIIND.
OrthoDBi EOG7GQXV9.
PhylomeDBi O95391.
TreeFami TF105691.

Miscellaneous databases

ChiTaRSi SLU7. human.
GeneWikii SLU7.
GenomeRNAii 10569.
NextBioi 40113.
PMAP-CutDB O95391.
PROi O95391.
SOURCEi Search...

Gene expression databases

ArrayExpressi O95391.
Bgeei O95391.
CleanExi HS_SLU7.
Genevestigatori O95391.

Family and domain databases

InterProi IPR021715. Slu7.
IPR001878. Znf_CCHC.
[Graphical view ]
Pfami PF11708. Slu7. 1 hit.
[Graphical view ]
SMARTi SM00343. ZnF_C2HC. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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].

Entry informationi

Entry nameiSLU7_HUMAN
AccessioniPrimary (citable) accession number: O95391
Secondary accession number(s): D3DQK2
, Q3LUJ0, Q3LUJ1, Q6RXQ5, Q96FM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: November 3, 2009
Last modified: July 9, 2014
This is version 96 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi