Reviewed, UniProtKB/Swiss-Prot Q15424 (SAFB1_HUMAN)

Names and origin

Protein names

Recommended name:
    Scaffold attachment factor B1
Alternative name(s):
    SAB-B1
    SAF-B
    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 not processed.
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. Can inhibit cell proliferation.
Subunit structure	Monomer. Can form homodimers. Interacts with KHDRBS3, POLR2A, SAFB2 or SFRS1, SFRS9 and TRA2B/SFRS10 By similarity.
Subcellular location	Nucleus.
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.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding RNA-binding
Molecular function	Repressor
PTM	Phosphoprotein
Gene Ontology (GO)
Biological process	establishment or maintenance of chromatin architecture Traceable author statement. Source: ProtInc regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	nucleus Traceable author statement. Source: ProtInc
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: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
BAT5	O95870	1	EBI-348298,EBI-348517

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 915	915	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	55	1	Phosphoserine Ref.11
	Modified residue	288	1	Phosphoserine Ref.8
	Modified residue	344	1	Phosphoserine By similarity
	Modified residue	373	1	Phosphoserine Ref.11
	Modified residue	383	1	Phosphoserine Ref.11
	Modified residue	384	1	Phosphoserine Ref.11 Ref.7
	Modified residue	555	1	Phosphoserine Ref.10
	Modified residue	557	1	Phosphoserine Ref.10
	Modified residue	589	1	Phosphoserine Ref.7
	Modified residue	601	1	Phosphoserine Ref.11 Ref.8
	Modified residue	604	1	Phosphoserine Ref.11 Ref.8 Ref.7 Ref.9
	Modified residue	808	1	Phosphoserine Ref.7
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 Ref.1
	Sequence conflict	731	1	A → G Ref.4
	Sequence conflict	744	1	D → E Ref.1
	Sequence conflict	744	1	D → E Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Q15424-1 [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]	"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.
[5]	"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.
[6]	"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.
[7]	"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: Epithelium.
[8]	"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: Epithelium.
[9]	"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: Epithelium.
[10]	"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.
[11]	"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.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	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.
UniGene	Hs.23978
3D structure databases
HSSP	HSSP built from PDB template 1HD1 based on UniProtKB Q14103.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q15424. 2 interactions.
PTM databases
PhosphoSite	Q15424.
Proteomic databases
PRIDE	Q15424.
Genome annotation databases
Ensembl	ENSG00000160633. Homo sapiens. [Contig view]
GeneID	6294.
KEGG	hsa:6294.
Organism-specific databases
GeneCards	GC19P005574.
HGNC	HGNC:10520. SAFB.
HPA	CAB001969. HPA016832.
MIM	602895. gene.
PharmGKB	PA34928.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q15424.
HOVERGEN	Q15424.
OMA	Q15424. EDDRAWQ.
Gene expression databases
ArrayExpress	Q15424.
Bgee	Q15424.
CleanEx	HS_SAFB.
GermOnline	ENSG00000160633. Homo sapiens.
Family and domain databases
InterPro	IPR012677. a_b_plait_nuc_bd. IPR000504. RRM_RNP1. IPR003034. SAP_DNA_bd. [Graphical view]
Gene3D	G3DSA:3.30.70.330. a_b_plait_nuc_bd. 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 Resources
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:	June 16, 2009
This is version 87 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)