Q14151 (SAFB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Scaffold attachment factor B2
Short name=SAF-B2

Gene names

Name:	SAFB2
Synonyms:	KIAA0138

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	953 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. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation.
Subunit structure	Interacts with SAFB/SAFB1 and SCAM1. Interacts with isoform 2 SRPK1 and inhibits its activity. Ref.13
Subcellular location	Cytoplasm. Nucleus.
Tissue specificity	Expressed at high levels in the CNS and at low levels in the liver. Expressed in a wide number of breast cancer cell lines.
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR By similarity. Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.12 Ref.14
Sequence similarities	Contains 1 RRM (RNA recognition motif) domain. Contains 1 SAP domain.
Sequence caution	The sequence BAA09487.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Ligand	DNA-binding RNA-binding
Molecular function	Repressor
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW transcription, DNA-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW RNA binding Inferred from electronic annotation. Source: UniProtKB-KW nucleotide binding Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction Ref.4. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESR1	P03372	2	EBI-352869,EBI-78473
GABARAPL1	Q9H0R8	2	EBI-352869,EBI-3464833
MAP1LC3B	Q9GZQ8	3	EBI-352869,EBI-373144
SAFB	Q15424	3	EBI-352869,EBI-348298
SORBS3	O60504-2	3	EBI-352869,EBI-1222956

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 953	952	Scaffold attachment factor B2		PRO_0000081907
Regions
	Domain	30 – 64	35	SAP
	Domain	407 – 485	79	RRM
	Region	600 – 953	354	Interacts with SAFB1
	Motif	713 – 730	18	Nuclear localization signal Potential
	Compositional bias	482 – 545	64	Lys-rich
	Compositional bias	619 – 724	106	Glu-rich
	Compositional bias	621 – 788	168	Arg-rich
	Compositional bias	792 – 926	135	Gly-rich
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.12
	Modified residue	31	1	Phosphoserine Ref.7
	Modified residue	109	1	Phosphoserine Ref.5 Ref.6 Ref.10
	Modified residue	195	1	Phosphoserine Ref.12 Ref.14
	Modified residue	201	1	Phosphothreonine Ref.12
	Modified residue	207	1	Phosphoserine Ref.8 Ref.11 Ref.14
	Modified residue	234	1	Phosphoserine By similarity
	Modified residue	287	1	Phosphoserine Ref.11
	Modified residue	293	1	N6-acetyllysine Ref.15
	Modified residue	331	1	Phosphoserine By similarity
	Modified residue	343	1	Phosphoserine Ref.6 Ref.9 Ref.11
	Modified residue	424	1	N6-acetyllysine Ref.15
	Modified residue	429	1	N6-acetyllysine Ref.15
	Modified residue	513	1	Phosphoserine Ref.6
	Modified residue	613	1	Phosphoserine Ref.11
	Modified residue	616	1	N6-acetyllysine Ref.15
Experimental info
	Sequence conflict	528	1	K → M in AAH25279. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q14151 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 084343934F8B3196	FASTA	953	107,473
	10 20 30 40 50 60 MAETLPGSGD SGPGTASLGP GVAETGTRRL SELRVIDLRA ELKKRNLDTG GNKSVLMERL 70 80 90 100 110 120 KKAVKEEGQD PDEIGIELEA TSKKSAKRCV KGLKMEEEGT EDNGLEDDSR DGQEDMEASL 130 140 150 160 170 180 ENLQNMGMMD MSVLDETEVA NSSAPDFGED GTDGLLDSFC DSKEYVAAQL RQLPAQPPEH 190 200 210 220 230 240 AVDGEGFKNT LETSSLNFKV TPDIEESLLE PENEKILDIL GETCKSEPVK EESSELEQPF 250 260 270 280 290 300 AQDTSSVGPD RKLAEEEDLF DSAHPEEGDL DLASESTAHA QSSKADSLLA VVKREPAEQP 310 320 330 340 350 360 GDGERTDCEP VGLEPAVEQS SAASELAEAS SEELAEAPTE APSPEARDSK EDGRKFDFDA 370 380 390 400 410 420 CNEVPPAPKE SSTSEGADQK MSSFKEEKDI KPIIKDEKGR VGSGSGRNLW VSGLSSTTRA 430 440 450 460 470 480 TDLKNLFSKY GKVVGAKVVT NARSPGARCY GFVTMSTSDE ATKCISHLHR TELHGRMISV 490 500 510 520 530 540 EKAKNEPAGK KLSDRKECEV KKEKLSSVDR HHSVEIKIEK TVIKKEEKIE KKEEKKPEDI 550 560 570 580 590 600 KKEEKDQDEL KPGPTNRSRV TKSGSRGMER TVVMDKSKGE PVISVKTTSR SKERSSKSQD 610 620 630 640 650 660 RKSESKEKRD ILSFDKIKEQ RERERQRQRE REIRETERRR EREQREREQR LEAFHERKEK 670 680 690 700 710 720 ARLQRERLQL ECQRQRLERE RMERERLERE RMRVERERRK EQERIHRERE ELRRQQEQLR 730 740 750 760 770 780 YEQERRPGRR PYDLDRRDDA YWPEGKRVAM EDRYRADFPR PDHRFHDFDH RDRGQYQDHA 790 800 810 820 830 840 IDRREGSRPM MGDHRDGQHY GDDRHGHGGP PERHGRDSRD GWGGYGSDKR LSEGRGLPPP 850 860 870 880 890 900 PRGGRDWGEH NQRLEEHQAR AWQGAMDAGA ASREHARWQG GERGLSGPSG PGHMASRGGV 910 920 930 940 950 AGRGGFAQGG HSQGHVVPGG GLEGGGVASQ DRGSRVPHPH PHPPPYPHFT RRY

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prediction of the coding sequences of unidentified human genes. IV. The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by analysis of cDNA clones from human cell line KG-1." Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N. DNA Res. 2:167-174(1995) [PubMed: 8590280] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Bone marrow.
[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]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-528. Tissue: Pancreas.
[4]	"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.
[5]	"Large-scale characterization of HeLa cell nuclear phosphoproteins." Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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-109; SER-343 AND SER-513, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[7]	"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-31, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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-207, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment." Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J. J. Proteome Res. 7:5167-5176(2008) [PubMed: 19367720] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, MASS SPECTROMETRY. Tissue: T-cell.
[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-207; SER-287; SER-343 AND SER-613, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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 SER-195 AND THR-201, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[13]	"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.
[14]	"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-195 AND SER-207, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[15]	"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-293; LYS-424; LYS-429 AND LYS-616, MASS SPECTROMETRY.
[16]	"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	D50928 mRNA. Translation: BAA09487.2. Different initiation. AC004611 Genomic DNA. Translation: AAC14666.1. BC025279 mRNA. Translation: AAH25279.1.
IPI	IPI00005648.
RefSeq	NP_055464.1. NM_014649.2.
UniGene	Hs.655392.
3D structure databases
ProteinModelPortal	Q14151.
SMR	Q14151. Positions 23-68.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q14151. 18 interactions.
MINT	MINT-5006081.
STRING	Q14151.
PTM databases
PhosphoSite	Q14151.
Polymorphism databases
DMDM	38372432.
Proteomic databases
PeptideAtlas	Q14151.
PRIDE	Q14151.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000252542; ENSP00000252542; ENSG00000130254.
GeneID	9667.
KEGG	hsa:9667.
UCSC	uc002mcd.1. human.
Organism-specific databases
CTD	9667.
GeneCards	GC19M005587.
HGNC	HGNC:21605. SAFB2.
MIM	608066. gene.
neXtProt	NX_Q14151.
PharmGKB	PA134987683.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
GeneTree	ENSGT00590000082875.
HOGENOM	HBG714637.
HOVERGEN	HBG078408.
InParanoid	Q14151.
OMA	RGQYQDH.
OrthoDB	EOG4F4S9X.
PhylomeDB	Q14151.
Gene expression databases
ArrayExpress	Q14151.
Bgee	Q14151.
CleanEx	HS_SAFB2.
Genevestigator	Q14151.
GermOnline	ENSG00000130254. 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	36299.
SOURCE	Search...

Entry information

Entry name

SAFB2_HUMAN

Accession

Primary (citable) accession number: Q14151
Secondary accession number(s): Q8TB13

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 14, 2003
Last sequence update:	November 1, 1996
Last modified:	January 25, 2012
This is version 112 of the entry and version 1 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.