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Q15424 (SAFB1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 116. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length915 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 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.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SAFB2Q141513EBI-348298,EBI-352869

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.4
Chain2 – 915914Scaffold attachment factor B1
PRO_0000081905

Regions

Domain31 – 6535SAP
Domain406 – 48479RRM
Region528 – 792265Interaction with POLR2A
Region599 – 915317Interaction with SAFB2
Motif599 – 61618Nuclear localization signal Potential
Compositional bias612 – 831220Arg-rich
Compositional bias625 – 70581Glu-rich
Compositional bias785 – 903119Gly-rich

Amino acid modifications

Modified residue21N-acetylalanine Ref.4 Ref.14
Modified residue551Phosphoserine Ref.13
Modified residue1941Phosphothreonine Ref.14
Modified residue2351Phosphoserine Ref.16
Modified residue2471Phosphoserine Ref.16
Modified residue2881Phosphoserine Ref.10 Ref.14 Ref.16
Modified residue3441Phosphoserine By similarity
Modified residue3731Phosphoserine Ref.13
Modified residue3831Phosphoserine Ref.13 Ref.14
Modified residue3841Phosphoserine Ref.9 Ref.13 Ref.14
Modified residue4751N6-acetyllysine Ref.17
Modified residue5551Phosphoserine Ref.12
Modified residue5571Phosphoserine Ref.12
Modified residue5891Phosphoserine Ref.9
Modified residue6011Phosphoserine Ref.10 Ref.13
Modified residue6041Phosphoserine Ref.9 Ref.10 Ref.11 Ref.13
Modified residue6071N6-acetyllysine Ref.17
Modified residue8081Phosphoserine Ref.9

Experimental info

Sequence conflict161A → P in AAC00056. Ref.1
Sequence conflict42 – 432EL → DV in AAC00056. Ref.1
Sequence conflict6211Missing in BAD92017. Ref.3
Sequence conflict7311A → G in AAC00056. Ref.1
Sequence conflict7311A → G in AAC18697. Ref.5
Sequence conflict7441D → E in AAC00056. Ref.1
Sequence conflict7441D → E in AAC18697. Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q15424 [UniParc].

Last modified October 17, 2006. Version 4.
Checksum: E865940BC7783C4A

FASTA915102,642
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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.
IPIIPI00300631.
PIRS64732.
RefSeqNP_002958.2. NM_002967.3.
UniGeneHs.728802.

3D structure databases

ProteinModelPortalQ15424.
SMRQ15424. Positions 31-69.
ModBaseSearch...

Protein-protein interaction databases

IntActQ15424. 9 interactions.
MINTMINT-1033560.
STRINGQ15424.

PTM databases

PhosphoSiteQ15424.

Polymorphism databases

DMDM116242782.

Proteomic databases

PRIDEQ15424.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000292123; ENSP00000292123; ENSG00000160633.
GeneID6294.
KEGGhsa:6294.
UCSCuc002mcf.1. human.

Organism-specific databases

CTD6294.
GeneCardsGC19P005574.
H-InvDBHIX0014682.
HGNCHGNC:10520. SAFB.
HPACAB001969.
HPA016832.
HPA020076.
MIM602895. gene.
neXtProtNX_Q15424.
PharmGKBPA34928.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG078408.
InParanoidQ15424.
PhylomeDBQ15424.

Gene expression databases

ArrayExpressQ15424.
BgeeQ15424.
CleanExHS_SAFB.
GenevestigatorQ15424.
GermOnlineENSG00000160633. Homo sapiens.

Family and domain databases

InterProIPR012677. Nucleotide-bd_a/b_plait.
IPR000504. RRM_dom.
IPR003034. SAP_DNA-bd.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
G3DSA:1.10.720.30. G3DSA:1.10.720.30. 1 hit.
PfamPF00076. RRM_1. 1 hit.
PF02037. 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

NextBio24435.
SOURCESearch...

Entry information

Entry nameSAFB1_HUMAN
AccessionPrimary (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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families