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Protein

Pre-mRNA-splicing factor SLU7

Gene

Slu7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 (By similarity).By similarity

Regions

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

GO - Molecular functioni

  • pre-mRNA 3'-splice site binding Source: HGNC
  • second spliceosomal transesterification activity Source: HGNC
  • zinc ion binding Source: HGNC

GO - Biological processi

  • alternative mRNA splicing, via spliceosome Source: HGNC
  • cellular response to heat Source: UniProtKB
  • intracellular protein transport Source: UniProtKB
  • mRNA 3'-splice site recognition Source: HGNC
  • 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
Gene namesi
Name:Slu7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 10

Organism-specific databases

RGDi631432. Slu7.

Subcellular locationi

  • Nucleus By similarity
  • Cytoplasm By similarity

  • Note: Predominantly nuclear. Shuttling between the nucleus and the cytoplasm is regulated by the CCHC-type zinc finger. 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 (By similarity).By similarity

GO - Cellular componenti

  • catalytic step 2 spliceosome Source: Ensembl
  • cytoplasm Source: UniProtKB
  • membrane Source: Ensembl
  • nuclear speck Source: HGNC
  • nucleus Source: UniProtKB
  • small nuclear ribonucleoprotein complex Source: HGNC
  • spliceosomal complex Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Spliceosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 586585Pre-mRNA-splicing factor SLU7PRO_0000289197Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei215 – 2151PhosphoserineCombined sources
Modified residuei227 – 2271PhosphoserineBy similarity
Modified residuei235 – 2351PhosphoserineCombined sources

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ80ZG5.
PRIDEiQ80ZG5.

PTM databases

PhosphoSiteiQ80ZG5.

Expressioni

Gene expression databases

ExpressionAtlasiQ80ZG5. baseline and differential.
GenevisibleiQ80ZG5. RN.

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 (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005132.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi129 – 16941Bipartite nuclear localization signalBy similarityAdd
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.By similarity

Sequence similaritiesi

Belongs to the SLU7 family.Curated
Contains 1 CCHC-type zinc finger.Curated

Zinc finger

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG2560. Eukaryota.
ENOG410XPPP. LUCA.
GeneTreeiENSGT00390000002292.
HOGENOMiHOG000194391.
HOVERGENiHBG053287.
InParanoidiQ80ZG5.
KOiK12819.
OMAiIANSEEC.
OrthoDBiEOG7GQXV9.
PhylomeDBiQ80ZG5.
TreeFamiTF105691.

Family and domain databases

InterProiIPR021715. Slu7.
[Graphical view]
PfamiPF11708. Slu7. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q80ZG5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAAAVDPVS ATPMTGSKEM NLEEPKKMTR EDWRKKKELE EQRKLGNAPA
60 70 80 90 100
EVDEEGKDIN PHIPQYISSV PWYIDPSKRP TLKHQRPQPE KQKQFSSSGE
110 120 130 140 150
WYKRGVKENS ITTKYRKGAC ENCGAMTHKR KDCFERPRRV GAKFTGTNIA
160 170 180 190 200
PDEHIQPQLM FDYDGKRDRW NGYNPEEHMK IVEEYAKVDL AKRTLKAQKL
210 220 230 240 250
QEELASGKLV EQANSPKHQW GEEEPNSQME KDHNSEDEDE DKYADDIDMP
260 270 280 290 300
GQNFDSKRRI TVRNLRIRED IAKYLRNLDP NSAYYDPKTR AMRENPYANA
310 320 330 340 350
GKNPDEVSYA GDNFVRYTGD TISMAQTQLF AWEAYDKGSE VHLQADPTKL
360 370 380 390 400
ELLYKSFKVK KEDFKEQQKE SILEKYGGQE HLDAPPAELL LAQTEDYVEY
410 420 430 440 450
SRHGTVIKGQ ERAVACSKYE EDVKINNHTH IWGSYWKEGR WGYKCCHSFF
460 470 480 490 500
KYSYCTGEAG KESVNSEECI INDATGEEPV KKPQTLMELH QEKLKEEKKK
510 520 530 540 550
KKKKKKHRKS SSDSDDDEER KQEKLKKALN AEEARLLHVK EIMQVDERKR
560 570 580
PYNSIYETRE PTEEEMEAYR MKRQRPDDPM ASFLGQ
Length:586
Mass (Da):68,337
Last modified:May 29, 2007 - v2
Checksum:iDBDBFBCDE5DC571A
GO

Sequence cautioni

The sequence AAO17154.2 differs from that shown.Many sequencing errors.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY207315 mRNA. Translation: AAO17154.2. Sequence problems.
AABR03074285 Genomic DNA. No translation available.
AABR03076495 Genomic DNA. No translation available.
BC062243 mRNA. Translation: AAH62243.1. Different termination.
RefSeqiNP_001094020.1. NM_001100550.1.
XP_008765862.1. XM_008767640.1.
XP_008765863.1. XM_008767641.1.
XP_008765864.1. XM_008767642.1.
UniGeneiRn.137183.

Genome annotation databases

EnsembliENSRNOT00000005132; ENSRNOP00000005132; ENSRNOG00000003822.
GeneIDi303057.
KEGGirno:303057.
UCSCiRGD:631432. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY207315 mRNA. Translation: AAO17154.2. Sequence problems.
AABR03074285 Genomic DNA. No translation available.
AABR03076495 Genomic DNA. No translation available.
BC062243 mRNA. Translation: AAH62243.1. Different termination.
RefSeqiNP_001094020.1. NM_001100550.1.
XP_008765862.1. XM_008767640.1.
XP_008765863.1. XM_008767641.1.
XP_008765864.1. XM_008767642.1.
UniGeneiRn.137183.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000005132.

PTM databases

PhosphoSiteiQ80ZG5.

Proteomic databases

PaxDbiQ80ZG5.
PRIDEiQ80ZG5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005132; ENSRNOP00000005132; ENSRNOG00000003822.
GeneIDi303057.
KEGGirno:303057.
UCSCiRGD:631432. rat.

Organism-specific databases

CTDi10569.
RGDi631432. Slu7.

Phylogenomic databases

eggNOGiKOG2560. Eukaryota.
ENOG410XPPP. LUCA.
GeneTreeiENSGT00390000002292.
HOGENOMiHOG000194391.
HOVERGENiHBG053287.
InParanoidiQ80ZG5.
KOiK12819.
OMAiIANSEEC.
OrthoDBiEOG7GQXV9.
PhylomeDBiQ80ZG5.
TreeFamiTF105691.

Miscellaneous databases

NextBioi650615.
PROiQ80ZG5.

Gene expression databases

ExpressionAtlasiQ80ZG5. baseline and differential.
GenevisibleiQ80ZG5. RN.

Family and domain databases

InterProiIPR021715. Slu7.
[Graphical view]
PfamiPF11708. Slu7. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  3. "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] OF 1-493.
    Tissue: Pituitary.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [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_RAT
AccessioniPrimary (citable) accession number: Q80ZG5
Secondary accession number(s): Q6P6G1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: May 29, 2007
Last modified: May 11, 2016
This is version 91 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.