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O88453 (SAFB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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:
Scaffold attachment factor B1

Short name=SAF-B
Short name=SAF-B1
Gene names
Name:Safb
Synonyms:Safb1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length931 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing. When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter By similarity.

Subunit structure

Monomer. Can form homodimers By similarity. Interacts with KHDRBS3, POLR2A, SAFB2 or SFRS1, SFRS9 and TRA2B/SFRS10. Interacts with SRPK1 and inhibits its activity By similarity. Interacts with RBMX By similarity. Ref.1 Ref.2

Subcellular location

Nucleus.

Post-translational modification

Phosphorylated by CDC-like kinase 2 (CLK2).

Sumoylated by PIAS1 with SUMO1 and SUMO2/3, desumoylated by SENP1. Sumoylation is required for transcriptional repressor activity By similarity.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Contains 1 SAP domain.

Sequence caution

The sequence AAC29479.1 differs from that shown. Reason: Frameshift at position 50.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SRPK1Q96SB42EBI-539530,EBI-539478From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 931930Scaffold attachment factor B1
PRO_0000081906

Regions

Domain31 – 6535SAP
Domain428 – 50679RRM
Region550 – 816267Interacts with POLR2A; SFRS1; SFRS9 and TRA2B
Motif621 – 63818Nuclear localization signal Potential
Compositional bias66 – 285220Glu-rich
Compositional bias634 – 855222Arg-rich
Compositional bias640 – 72889Glu-rich

Amino acid modifications

Modified residue21N-acetylalanine By similarity
Modified residue551Phosphoserine By similarity
Modified residue4051Phosphoserine By similarity
Modified residue4061Phosphoserine By similarity
Modified residue4371Phosphoserine By similarity
Modified residue6021Phosphoserine By similarity
Modified residue6041Phosphoserine By similarity
Modified residue6231Phosphoserine By similarity
Modified residue6261Phosphoserine By similarity
Modified residue6291N6-acetyllysine By similarity
Cross-link230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link316Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence LengthMass (Da)Tools
O88453 [UniParc].

Last modified November 14, 2003. Version 2.
Checksum: A5E3FD7AB33341F6

FASTA931104,567
        10         20         30         40         50         60 
MAETLSGLGD SGAASAAAVS SAASETGTRR LSDLRVIDLR AELRKRNLTS SGNKSVLMER 

        70         80         90        100        110        120 
LKKAIEEEGG NPDEIEVISE GNKKMPKRPS KGKKPEDEGV EDNGLEENSG DGQEDVETSL 

       130        140        150        160        170        180 
ENLQDMDMMD ISVLDEADID NGSVADCVEE EEEATLPEGL GLLRIGRLQS KGLPEQLQEL 

       190        200        210        220        230        240 
AIDDKEAINN VDTSSSDFTI LQEMEEASLE PENEKILDIL GETCKSEPVK EEGSELEQPF 

       250        260        270        280        290        300 
AQATSSVGPD RKLAEEEDLF ESCGHPEEEE EEEEEEEQEE EQEEEGDLAL ASSSKSESSS 

       310        320        330        340        350        360 
TRCQWSEADA LLAVVKREPA EAPGGGTGMD REPVGLEEPV EQSSTAAQLP ETTSQELVRA 

       370        380        390        400        410        420 
PTAAPSPEPR DSKDDVKKFA FDACNDVPAA PKESSASEGA DQKMSSVEDD SDTKRLSREE 

       430        440        450        460        470        480 
KGRSSCGRNF WVSGLSSTTR ATDLKNLFSR YGKVVGAKVV TNARSPGARC YGFVTMSTAE 

       490        500        510        520        530        540 
EATKCINHLH KTELHGKMIS VEKAKSEPAG KRVPDRRDGD SKKEKTSTSD RSANLKREEK 

       550        560        570        580        590        600 
GDRKDDAKKT DDGSTEKSKD ADDQKPGPSE RSRTTKSGSR GTERTVVMDK SKGVPVISVK 

       610        620        630        640        650        660 
TSGSKERASK SQDRKSVSRE KRSVVSFDKV KESRKSRDSE SRRERERERS EREQRLQAQW 

       670        680        690        700        710        720 
EREERERLEI ARERLAFHRH RLERERMERE RLERERMHVE QERRREQERI HREREELRRQ 

       730        740        750        760        770        780 
QELRYEQERR PAVRRPYEVD GRRDDAYWPE AKRAALDDRY HSDFSRQDRF HDFDHRDRGR 

       790        800        810        820        830        840 
YPNHSVDRRE GSRSMMGDRE GQHYPERHGG PERHGRDSRD GWGYGSNKRL SEGRGLPLLP 

       850        860        870        880        890        900 
RRDWGEHARR LEDDRAWQGT ADGGMMERDQ QRWQGGERSM SGHSGPGHMM NRGGMSGRGS 

       910        920        930 
FAPGGASRRH VIPRGGMQAG FGGTEPGQQT Q 

« Hide

References

[1]"SAF-B couples transcription and pre-mRNA splicing to SAR/MAR elements."
Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L., Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S.
Nucleic Acids Res. 26:3542-3549(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, INTERACTION WITH POLR2A; SFRS1; SFRS9 AND TRA2B.
[2]"The STAR/GSG family protein rSLM-2 regulates the selection of alternative splice sites."
Stoss O., Olbrich M., Hartmann A.M., Koenig H., Memmott J., Andreadis A., Stamm S.
J. Biol. Chem. 276:8665-8673(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KHDRBS3.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF056324 mRNA. Translation: AAC29479.1. Frameshift.
RefSeqNP_071789.1. NM_022394.1.
UniGeneRn.88640.

3D structure databases

ProteinModelPortalO88453.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid249003. 8 interactions.
IntActO88453. 1 interaction.

PTM databases

PhosphoSiteO88453.

Proteomic databases

PRIDEO88453.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID64196.
KEGGrno:64196.

Organism-specific databases

CTD6294.
RGD620613. Safb.

Phylogenomic databases

HOVERGENHBG078408.
PhylomeDBO88453.

Gene expression databases

GenevestigatorO88453.

Family and domain databases

Gene3D1.10.720.30. 1 hit.
3.30.70.330. 1 hit.
InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003034. SAP_dom.
[Graphical view]
PfamPF02037. SAP. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio612872.
PROO88453.

Entry information

Entry nameSAFB1_RAT
AccessionPrimary (citable) accession number: O88453
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 14, 2003
Last modified: April 16, 2014
This is version 105 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families