Scaffold attachment factor B1 - Rattus norvegicus (Rat)

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O88453 (SAFB1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 100. History...

Clusters with 100%, 90%, 50% identity |

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Scaffold attachment factor B1
Short name=SAF-B
Short name=SAF-B1

Gene names

Name:	Safb
Synonyms:	Safb1

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	931 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding RNA-binding
Molecular function	Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	regulation of mRNA processing Inferred from direct assay Ref.1. Source: RGD regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.1. Source: RGD transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	nucleus Inferred from direct assay Ref.1. Source: RGD
Molecular_function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro sequence-specific DNA binding Inferred from direct assay Ref.1. Source: RGD
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SRPK1	Q96SB4	2	EBI-539530,EBI-539478	From a different organism.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 931

930

Scaffold attachment factor B1

PRO_0000081906

Regions

Domain

31 – 65

SAP

Domain

428 – 506

RRM

Region

550 – 816

267

Interacts with POLR2A; SFRS1; SFRS9 and TRA2B

Motif

621 – 638

Nuclear localization signal Potential

Compositional bias

66 – 285

220

Glu-rich

Compositional bias

634 – 855

222

Arg-rich

Compositional bias

640 – 728

Glu-rich

Amino acid modifications

Modified residue

N-acetylalanine By similarity

Modified residue

Phosphoserine By similarity

Modified residue

366

Phosphoserine Ref.3

Modified residue

405

Phosphoserine By similarity

Modified residue

406

Phosphoserine By similarity

Modified residue

437

Phosphoserine By similarity

Modified residue

602

Phosphoserine By similarity

Modified residue

604

Phosphoserine By similarity

Modified residue

623

Phosphoserine By similarity

Modified residue

626

Phosphoserine By similarity

Modified residue

629

N6-acetyllysine By similarity

Modified residue

831

Phosphoserine By similarity

Cross-link

230

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

316

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

O88453 [UniParc].

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

FASTA

931

104,567

        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

	« Hide 'large scale' referencesShow 'large scale' 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.
[3]	"Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS." Moser K., White F.M. J. Proteome Res. 5:98-104(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-366, MASS SPECTROMETRY. Strain: Fischer. Tissue: Liver.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF056324 mRNA. Translation: AAC29479.1. Frameshift.
IPI	IPI00209618.
RefSeq	NP_071789.1. NM_022394.1.
UniGene	Rn.88640.
3D structure databases
ProteinModelPortal	O88453.
ModBase	Search...
Protein-protein interaction databases
IntAct	O88453. 1 interaction.
PTM databases
PhosphoSite	O88453.
Proteomic databases
PRIDE	O88453.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	64196.
KEGG	rno:64196.
Organism-specific databases
CTD	6294.
RGD	620613. Safb.
Phylogenomic databases
HOVERGEN	HBG078408.
Gene expression databases
Genevestigator	O88453.
Family and domain databases
Gene3D	1.10.720.30. 1 hit. 3.30.70.330. 1 hit.
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. IPR003034. SAP_dom. [Graphical view]
Pfam	PF02037. SAP. 1 hit. [Graphical view]
SMART	SM00360. RRM. 1 hit. SM00513. SAP. 1 hit. [Graphical view]
PROSITE	PS50102. RRM. 1 hit. PS50800. SAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	612872.

Entry information

Entry name

SAFB1_RAT

Accession

Primary (citable) accession number: O88453

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	November 14, 2003
Last modified:	April 3, 2013
This is version 100 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents