Q15424 (SAFB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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

Alternative name(s):
HSP27 estrogen response element-TATA box-binding protein
Short name=HSP27 ERE-TATA-binding protein

Gene names

Name:	SAFB
Synonyms:	HAP, HET, SAFB1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	915 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 By similarity. Can function as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription. When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter By similarity. Can inhibit cell proliferation.
Subunit structure	Monomer. Can form homodimers. Interacts with KHDRBS3, POLR2A, SAFB2 or SFRS1, SFRS9 and TRA2B/SFRS10 By similarity. Interacts with isoform 1 and isoform 2 of SRPK1 and inhibits its activity. Interacts with RBMX By similarity. Ref.6 Ref.7 Ref.15
Subcellular location	Nucleus Ref.15.
Tissue specificity	Ubiquitous. Expressed at high levels in the CNS and at low levels in the liver. Expressed in a wide number of breast cancer cell lines.
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain. Contains 1 SAP domain.
Sequence caution	The sequence BAD92017.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding RNA-binding
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	chromatin organization Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Inferred from direct assay. Source: HPA
Molecular function	RNA binding Inferred from electronic annotation. Source: UniProtKB-KW double-stranded DNA binding Traceable author statement. Source: ProtInc nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SAFB2	Q14151	3	EBI-348298,EBI-352869

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 915	914	Scaffold attachment factor B1		PRO_0000081905
Regions
	Domain	31 – 65	35	SAP
	Domain	406 – 484	79	RRM
	Region	528 – 792	265	Interaction with POLR2A
	Region	599 – 915	317	Interaction with SAFB2
	Motif	599 – 616	18	Nuclear localization signal Potential
	Compositional bias	612 – 831	220	Arg-rich
	Compositional bias	625 – 705	81	Glu-rich
	Compositional bias	785 – 903	119	Gly-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.4 Ref.14
	Modified residue	55	1	Phosphoserine Ref.13
	Modified residue	194	1	Phosphothreonine Ref.14
	Modified residue	235	1	Phosphoserine Ref.16
	Modified residue	247	1	Phosphoserine Ref.16
	Modified residue	288	1	Phosphoserine Ref.10 Ref.14 Ref.16
	Modified residue	344	1	Phosphoserine By similarity
	Modified residue	373	1	Phosphoserine Ref.13
	Modified residue	383	1	Phosphoserine Ref.13 Ref.14
	Modified residue	384	1	Phosphoserine Ref.9 Ref.13 Ref.14
	Modified residue	475	1	N6-acetyllysine Ref.17
	Modified residue	555	1	Phosphoserine Ref.12
	Modified residue	557	1	Phosphoserine Ref.12
	Modified residue	589	1	Phosphoserine Ref.9
	Modified residue	601	1	Phosphoserine Ref.10 Ref.13
	Modified residue	604	1	Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13
	Modified residue	607	1	N6-acetyllysine Ref.17
	Modified residue	808	1	Phosphoserine Ref.9
Experimental info
	Sequence conflict	16	1	A → P in AAC00056. Ref.1
	Sequence conflict	42 – 43	2	EL → DV in AAC00056. Ref.1
	Sequence conflict	621	1	Missing in BAD92017. Ref.3
	Sequence conflict	731	1	A → G in AAC00056. Ref.1
	Sequence conflict	731	1	A → G in AAC18697. Ref.5
	Sequence conflict	744	1	D → E in AAC00056. Ref.1
	Sequence conflict	744	1	D → E in AAC18697. Ref.5

Sequences

	Sequence		Length	Mass (Da)
	Q15424 [UniParc]. Last modified October 17, 2006. Version 4. Checksum: E865940BC7783C4A	FASTA	915	102,642
	10 20 30 40 50 60 MAETLSGLGD SGAAGAAALS SASSETGTRR LSDLRVIDLR AELRKRNVDS SGNKSVLMER 70 80 90 100 110 120 LKKAIEDEGG NPDEIEITSE GNKKTSKRSS KGRKPEEEGV EDNGLEENSG DGQEDVETSL 130 140 150 160 170 180 ENLQDIDIMD ISVLDEAEID NGSVADCVED DDADNLQESL SDSRELVEGE MKELPEQLQE 190 200 210 220 230 240 HAIEDKETIN NLDTSSSDFT ILQEIEEPSL EPENEKILDI LGETCKSEPV KEESSELEQP 250 260 270 280 290 300 FAQDTSSVGP DRKLAEEEDL FDSAHPEEGD LDLASESTAH AQSSKADSLL AVVKREPAEQ 310 320 330 340 350 360 PGDGERTDCE PVGLEPAVEQ SSAASELAEA SSEELAEAPT EAPSPEARDS KEDGRKFDFD 370 380 390 400 410 420 ACNEVPPAPK ESSTSEGADQ KMSSPEDDSD TKRLSKEEKG RSSCGRNFWV SGLSSTTRAT 430 440 450 460 470 480 DLKNLFSKYG KVVGAKVVTN ARSPGARCYG FVTMSTAEEA TKCINHLHKT ELHGKMISVE 490 500 510 520 530 540 KAKNEPVGKK TSDKRDSDGK KEKSSNSDRS TNLKRDDKCD RKDDAKKGDD GSGEKSKDQD 550 560 570 580 590 600 DQKPGPSERS RATKSGSRGT ERTVVMDKSK GVPVISVKTS GSKERASKSQ DRKSASREKR 610 620 630 640 650 660 SVVSFDKVKE PRKSRDSESH SRVRERSERE QRMQAQWERE ERERLEIARE RLAFQRQRLE 670 680 690 700 710 720 RERMERERLE RERMHVEHER RREQERIHRE REELRRQQEL RYEQERRPAV RRPYDLDRRD 730 740 750 760 770 780 DAYWPEAKRA ALDERYHSDF NRQDRFHDFD HRDRGRYPDH SVDRREGSRS MMGEREGQHY 790 800 810 820 830 840 PERHGGPERH GRDSRDGWGG YGSDKRMSEG RGLPPPPRRD WGDHGRREDD RSWQGTADGG 850 860 870 880 890 900 MMDRDHKRWQ GGERSMSGHS GPGHMMNRGG MSGRGSFAPG GASRGHPIPH GGMQGGFGGQ 910 SRGSRPSDAR FTRRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel nuclear matrix protein HET binds to and influences activity of the HSP27 promoter in human breast cancer cells." Oesterreich S., Lee A.V., Sullivan T.M., Samuel S.K., Davie J.R., Fuqua S.A.W. J. Cell. Biochem. 67:275-286(1997) [PubMed: 9328833] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION. Tissue: Mammary carcinoma.
[2]	"The DNA sequence and biology of human chromosome 19." Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V. , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M. Nature 428:529-535(2004) [PubMed: 15057824] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-753. Tissue: Brain.
[4]	Bienvenut W.V., Matallanas D., Kolch W. Submitted (JUL-2009) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-30; 419-428; 571-578 AND 601-612, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, MASS SPECTROMETRY. Tissue: Mammary carcinoma.
[5]	"Purification and molecular cloning of the scaffold attachment factor B (SAF-B), a novel human nuclear protein that specifically binds to S/MAR-DNA." Renz A., Fackelmayer F.O. Nucleic Acids Res. 24:843-849(1996) [PubMed: 8600450] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 52-915, CHARACTERIZATION, PHOSPHORYLATION. Tissue: Cervix carcinoma.
[6]	"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: 9671816] [Abstract] Cited for: INTERACTION WITH POLR2A.
[7]	"Cloning and characterization of an alternatively spliced form of SR protein kinase 1 that interacts specifically with scaffold attachment factor-B." Nikolakaki E., Kohen R., Hartmann A.M., Stamm S., Georgatsou E., Giannakouros T. J. Biol. Chem. 276:40175-40182(2001) [PubMed: 11509566] [Abstract] Cited for: INTERACTION WITH SRPK1.
[8]	"SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor." Townson S.M., Dobrzycka K.M., Lee A.V., Air M., Deng W., Kang K., Jiang S., Kioka N., Michaelis K., Oesterreich S. J. Biol. Chem. 278:20059-20068(2003) [PubMed: 12660241] [Abstract] Cited for: CHARACTERIZATION.
[9]	"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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-384; SER-589; SER-604 AND SER-808, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"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: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-601 AND SER-604, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-604, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-555 AND SER-557, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-55; SER-373; SER-383; SER-384; SER-601 AND SER-604, MASS SPECTROMETRY. 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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-194; SER-288; SER-383 AND SER-384, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[15]	"The enzymatic activity of SR protein kinases 1 and 1a is negatively affected by interaction with scaffold attachment factors B1 and 2." Tsianou D., Nikolakaki E., Tzitzira A., Bonanou S., Giannakouros T., Georgatsou E. FEBS J. 276:5212-5227(2009) [PubMed: 19674106] [Abstract] Cited for: INTERACTION WITH SRPK1, SUBCELLULAR LOCATION.
[16]	"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-247 AND SER-288, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[17]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-475 AND LYS-607, MASS SPECTROMETRY.
[18]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	U72355 mRNA. Translation: AAC00056.1. AC004611 Genomic DNA. Translation: AAC14667.1. AC011499 Genomic DNA. No translation available. AC134303 Genomic DNA. No translation available. AB208780 mRNA. Translation: BAD92017.1. Different initiation. L43631 mRNA. Translation: AAC18697.1.
IPI	IPI00300631.
PIR	S64732.
RefSeq	NP_002958.2. NM_002967.3.
UniGene	Hs.728802.
3D structure databases
ProteinModelPortal	Q15424.
SMR	Q15424. Positions 31-69.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15424. 9 interactions.
MINT	MINT-1033560.
STRING	Q15424.
PTM databases
PhosphoSite	Q15424.
Polymorphism databases
DMDM	116242782.
Proteomic databases
PRIDE	Q15424.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000292123; ENSP00000292123; ENSG00000160633.
GeneID	6294.
KEGG	hsa:6294.
UCSC	uc002mcf.1. human.
Organism-specific databases
CTD	6294.
GeneCards	GC19P005574.
H-InvDB	HIX0014682.
HGNC	HGNC:10520. SAFB.
HPA	CAB001969. HPA016832. HPA020076.
MIM	602895. gene.
neXtProt	NX_Q15424.
PharmGKB	PA34928.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	HBG078408.
InParanoid	Q15424.
PhylomeDB	Q15424.
Gene expression databases
ArrayExpress	Q15424.
Bgee	Q15424.
CleanEx	HS_SAFB.
Genevestigator	Q15424.
GermOnline	ENSG00000160633. Homo sapiens.
Family and domain databases
InterPro	IPR012677. Nucleotide-bd_a/b_plait. IPR000504. RRM_dom. IPR003034. SAP_DNA-bd. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit. G3DSA:1.10.720.30. G3DSA:1.10.720.30. 1 hit.
Pfam	PF00076. RRM_1. 1 hit. 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	24435.
SOURCE	Search...

Entry information

Entry name

SAFB1_HUMAN

Accession

Primary (citable) accession number: Q15424
Secondary accession number(s): O60406, Q59HH8

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 116 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.