Full text data of SAFB2
SAFB2
(KIAA0138)
[Confidence: low (only semi-automatic identification from reviews)]
Scaffold attachment factor B2; SAF-B2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Scaffold attachment factor B2; SAF-B2
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q14151
ID SAFB2_HUMAN Reviewed; 953 AA.
AC Q14151; Q8TB13;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Scaffold attachment factor B2;
DE Short=SAF-B2;
GN Name=SAFB2; Synonyms=KIAA0138;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-528.
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP CHARACTERIZATION.
RX PubMed=12660241; DOI=10.1074/jbc.M212988200;
RA Townson S.M., Dobrzycka K.M., Lee A.V., Air M., Deng W., Kang K.,
RA Jiang S., Kioka N., Michaelis K., Oesterreich S.;
RT "SAFB2, a new scaffold attachment factor homolog and estrogen receptor
RT corepressor.";
RL J. Biol. Chem. 278:20059-20068(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP INTERACTION WITH SRPK1.
RX PubMed=19674106; DOI=10.1111/j.1742-4658.2009.07217.x;
RA Tsianou D., Nikolakaki E., Tzitzira A., Bonanou S., Giannakouros T.,
RA Georgatsou E.;
RT "The enzymatic activity of SR protein kinases 1 and 1a is negatively
RT affected by interaction with scaffold attachment factors B1 and 2.";
RL FEBS J. 276:5212-5227(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-616, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; THR-201; SER-207
RP AND SER-513, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP SUMOYLATION AT LYS-230 AND LYS-293.
RX PubMed=21527249; DOI=10.1016/j.bbrc.2011.04.040;
RA Garee J.P., Meyer R., Oesterreich S.;
RT "Co-repressor activity of scaffold attachment factor B1 requires
RT sumoylation.";
RL Biochem. Biophys. Res. Commun. 408:516-522(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA.
CC Can function as an estrogen receptor corepressor and can also
CC inhibit cell proliferation.
CC -!- SUBUNIT: Interacts with SAFB/SAFB1 and SCAM1. Interacts with
CC isoform 2 SRPK1 and inhibits its activity.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-352869, EBI-352869;
CC P03372:ESR1; NbExp=2; IntAct=EBI-352869, EBI-78473;
CC Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-352869, EBI-746969;
CC Q9GZQ8:MAP1LC3B; NbExp=3; IntAct=EBI-352869, EBI-373144;
CC Q15424:SAFB; NbExp=3; IntAct=EBI-352869, EBI-348298;
CC O60504-2:SORBS3; NbExp=3; IntAct=EBI-352869, EBI-1222956;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the CNS and at low
CC levels in the liver. Expressed in a wide number of breast cancer
CC cell lines.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- SIMILARITY: Contains 1 SAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09487.2; Type=Erroneous initiation;
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DR EMBL; D50928; BAA09487.2; ALT_INIT; mRNA.
DR EMBL; AC004611; AAC14666.1; -; Genomic_DNA.
DR EMBL; BC025279; AAH25279.1; -; mRNA.
DR RefSeq; NP_055464.1; NM_014649.2.
DR UniGene; Hs.655392; -.
DR ProteinModelPortal; Q14151; -.
DR SMR; Q14151; 405-486.
DR IntAct; Q14151; 20.
DR MINT; MINT-5006081; -.
DR STRING; 9606.ENSP00000252542; -.
DR PhosphoSite; Q14151; -.
DR DMDM; 38372432; -.
DR PaxDb; Q14151; -.
DR PeptideAtlas; Q14151; -.
DR PRIDE; Q14151; -.
DR Ensembl; ENST00000252542; ENSP00000252542; ENSG00000130254.
DR GeneID; 9667; -.
DR KEGG; hsa:9667; -.
DR UCSC; uc002mcd.3; human.
DR CTD; 9667; -.
DR GeneCards; GC19M005587; -.
DR HGNC; HGNC:21605; SAFB2.
DR HPA; HPA050894; -.
DR MIM; 608066; gene.
DR neXtProt; NX_Q14151; -.
DR PharmGKB; PA134987683; -.
DR eggNOG; NOG248048; -.
DR HOGENOM; HOG000092533; -.
DR HOVERGEN; HBG078408; -.
DR InParanoid; Q14151; -.
DR OMA; TPDIEEP; -.
DR OrthoDB; EOG722J7Z; -.
DR PhylomeDB; Q14151; -.
DR ChiTaRS; SAFB2; human.
DR GeneWiki; SAFB2; -.
DR GenomeRNAi; 9667; -.
DR NextBio; 36299; -.
DR PRO; PR:Q14151; -.
DR ArrayExpress; Q14151; -.
DR Bgee; Q14151; -.
DR CleanEx; HS_SAFB2; -.
DR Genevestigator; Q14151; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003034; SAP_dom.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 953 Scaffold attachment factor B2.
FT /FTId=PRO_0000081907.
FT DOMAIN 30 64 SAP.
FT DOMAIN 407 485 RRM.
FT REGION 600 953 Interacts with SAFB1.
FT MOTIF 713 730 Nuclear localization signal (Potential).
FT COMPBIAS 482 545 Lys-rich.
FT COMPBIAS 619 724 Glu-rich.
FT COMPBIAS 621 788 Arg-rich.
FT COMPBIAS 792 926 Gly-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 109 109 Phosphoserine.
FT MOD_RES 201 201 Phosphothreonine.
FT MOD_RES 207 207 Phosphoserine.
FT MOD_RES 513 513 Phosphoserine.
FT MOD_RES 616 616 N6-acetyllysine.
FT CROSSLNK 230 230 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT CONFLICT 528 528 K -> M (in Ref. 3; AAH25279).
SQ SEQUENCE 953 AA; 107473 MW; 084343934F8B3196 CRC64;
MAETLPGSGD SGPGTASLGP GVAETGTRRL SELRVIDLRA ELKKRNLDTG GNKSVLMERL
KKAVKEEGQD PDEIGIELEA TSKKSAKRCV KGLKMEEEGT EDNGLEDDSR DGQEDMEASL
ENLQNMGMMD MSVLDETEVA NSSAPDFGED GTDGLLDSFC DSKEYVAAQL RQLPAQPPEH
AVDGEGFKNT LETSSLNFKV TPDIEESLLE PENEKILDIL GETCKSEPVK EESSELEQPF
AQDTSSVGPD RKLAEEEDLF DSAHPEEGDL DLASESTAHA QSSKADSLLA VVKREPAEQP
GDGERTDCEP VGLEPAVEQS SAASELAEAS SEELAEAPTE APSPEARDSK EDGRKFDFDA
CNEVPPAPKE SSTSEGADQK MSSFKEEKDI KPIIKDEKGR VGSGSGRNLW VSGLSSTTRA
TDLKNLFSKY GKVVGAKVVT NARSPGARCY GFVTMSTSDE ATKCISHLHR TELHGRMISV
EKAKNEPAGK KLSDRKECEV KKEKLSSVDR HHSVEIKIEK TVIKKEEKIE KKEEKKPEDI
KKEEKDQDEL KPGPTNRSRV TKSGSRGMER TVVMDKSKGE PVISVKTTSR SKERSSKSQD
RKSESKEKRD ILSFDKIKEQ RERERQRQRE REIRETERRR EREQREREQR LEAFHERKEK
ARLQRERLQL ECQRQRLERE RMERERLERE RMRVERERRK EQERIHRERE ELRRQQEQLR
YEQERRPGRR PYDLDRRDDA YWPEGKRVAM EDRYRADFPR PDHRFHDFDH RDRGQYQDHA
IDRREGSRPM MGDHRDGQHY GDDRHGHGGP PERHGRDSRD GWGGYGSDKR LSEGRGLPPP
PRGGRDWGEH NQRLEEHQAR AWQGAMDAGA ASREHARWQG GERGLSGPSG PGHMASRGGV
AGRGGFAQGG HSQGHVVPGG GLEGGGVASQ DRGSRVPHPH PHPPPYPHFT RRY
//
ID SAFB2_HUMAN Reviewed; 953 AA.
AC Q14151; Q8TB13;
DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1996, sequence version 1.
DT 22-JAN-2014, entry version 129.
DE RecName: Full=Scaffold attachment factor B2;
DE Short=SAF-B2;
GN Name=SAFB2; Synonyms=KIAA0138;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Bone marrow;
RX PubMed=8590280; DOI=10.1093/dnares/2.4.167;
RA Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. IV.
RT The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
RT analysis of cDNA clones from human cell line KG-1.";
RL DNA Res. 2:167-174(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
RA Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
RA Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
RA Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
RA Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
RA Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
RA Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
RA Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
RA Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
RA Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
RA Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
RA Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
RA Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
RA Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
RA Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
RA Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-528.
RC TISSUE=Pancreas;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP CHARACTERIZATION.
RX PubMed=12660241; DOI=10.1074/jbc.M212988200;
RA Townson S.M., Dobrzycka K.M., Lee A.V., Air M., Deng W., Kang K.,
RA Jiang S., Kioka N., Michaelis K., Oesterreich S.;
RT "SAFB2, a new scaffold attachment factor homolog and estrogen receptor
RT corepressor.";
RL J. Biol. Chem. 278:20059-20068(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASS
RP SPECTROMETRY.
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using
RT sequential IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY, AND
RP CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [9]
RP INTERACTION WITH SRPK1.
RX PubMed=19674106; DOI=10.1111/j.1742-4658.2009.07217.x;
RA Tsianou D., Nikolakaki E., Tzitzira A., Bonanou S., Giannakouros T.,
RA Georgatsou E.;
RT "The enzymatic activity of SR protein kinases 1 and 1a is negatively
RT affected by interaction with scaffold attachment factors B1 and 2.";
RL FEBS J. 276:5212-5227(2009).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-616, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; THR-201; SER-207
RP AND SER-513, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP SUMOYLATION AT LYS-230 AND LYS-293.
RX PubMed=21527249; DOI=10.1016/j.bbrc.2011.04.040;
RA Garee J.P., Meyer R., Oesterreich S.;
RT "Co-repressor activity of scaffold attachment factor B1 requires
RT sumoylation.";
RL Biochem. Biophys. Res. Commun. 408:516-522(2011).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Binds to scaffold/matrix attachment region (S/MAR) DNA.
CC Can function as an estrogen receptor corepressor and can also
CC inhibit cell proliferation.
CC -!- SUBUNIT: Interacts with SAFB/SAFB1 and SCAM1. Interacts with
CC isoform 2 SRPK1 and inhibits its activity.
CC -!- INTERACTION:
CC Self; NbExp=2; IntAct=EBI-352869, EBI-352869;
CC P03372:ESR1; NbExp=2; IntAct=EBI-352869, EBI-78473;
CC Q9H0R8:GABARAPL1; NbExp=2; IntAct=EBI-352869, EBI-746969;
CC Q9GZQ8:MAP1LC3B; NbExp=3; IntAct=EBI-352869, EBI-373144;
CC Q15424:SAFB; NbExp=3; IntAct=EBI-352869, EBI-348298;
CC O60504-2:SORBS3; NbExp=3; IntAct=EBI-352869, EBI-1222956;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus.
CC -!- TISSUE SPECIFICITY: Expressed at high levels in the CNS and at low
CC levels in the liver. Expressed in a wide number of breast cancer
CC cell lines.
CC -!- SIMILARITY: Contains 1 RRM (RNA recognition motif) domain.
CC -!- SIMILARITY: Contains 1 SAP domain.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA09487.2; Type=Erroneous initiation;
CC -----------------------------------------------------------------------
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DR EMBL; D50928; BAA09487.2; ALT_INIT; mRNA.
DR EMBL; AC004611; AAC14666.1; -; Genomic_DNA.
DR EMBL; BC025279; AAH25279.1; -; mRNA.
DR RefSeq; NP_055464.1; NM_014649.2.
DR UniGene; Hs.655392; -.
DR ProteinModelPortal; Q14151; -.
DR SMR; Q14151; 405-486.
DR IntAct; Q14151; 20.
DR MINT; MINT-5006081; -.
DR STRING; 9606.ENSP00000252542; -.
DR PhosphoSite; Q14151; -.
DR DMDM; 38372432; -.
DR PaxDb; Q14151; -.
DR PeptideAtlas; Q14151; -.
DR PRIDE; Q14151; -.
DR Ensembl; ENST00000252542; ENSP00000252542; ENSG00000130254.
DR GeneID; 9667; -.
DR KEGG; hsa:9667; -.
DR UCSC; uc002mcd.3; human.
DR CTD; 9667; -.
DR GeneCards; GC19M005587; -.
DR HGNC; HGNC:21605; SAFB2.
DR HPA; HPA050894; -.
DR MIM; 608066; gene.
DR neXtProt; NX_Q14151; -.
DR PharmGKB; PA134987683; -.
DR eggNOG; NOG248048; -.
DR HOGENOM; HOG000092533; -.
DR HOVERGEN; HBG078408; -.
DR InParanoid; Q14151; -.
DR OMA; TPDIEEP; -.
DR OrthoDB; EOG722J7Z; -.
DR PhylomeDB; Q14151; -.
DR ChiTaRS; SAFB2; human.
DR GeneWiki; SAFB2; -.
DR GenomeRNAi; 9667; -.
DR NextBio; 36299; -.
DR PRO; PR:Q14151; -.
DR ArrayExpress; Q14151; -.
DR Bgee; Q14151; -.
DR CleanEx; HS_SAFB2; -.
DR Genevestigator; Q14151; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW.
DR Gene3D; 1.10.720.30; -; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003034; SAP_dom.
DR Pfam; PF00076; RRM_1; 1.
DR Pfam; PF02037; SAP; 1.
DR SMART; SM00360; RRM; 1.
DR SMART; SM00513; SAP; 1.
DR PROSITE; PS50102; RRM; 1.
DR PROSITE; PS50800; SAP; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Cytoplasm; DNA-binding;
KW Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW Repressor; RNA-binding; Transcription; Transcription regulation;
KW Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 953 Scaffold attachment factor B2.
FT /FTId=PRO_0000081907.
FT DOMAIN 30 64 SAP.
FT DOMAIN 407 485 RRM.
FT REGION 600 953 Interacts with SAFB1.
FT MOTIF 713 730 Nuclear localization signal (Potential).
FT COMPBIAS 482 545 Lys-rich.
FT COMPBIAS 619 724 Glu-rich.
FT COMPBIAS 621 788 Arg-rich.
FT COMPBIAS 792 926 Gly-rich.
FT MOD_RES 2 2 N-acetylalanine.
FT MOD_RES 109 109 Phosphoserine.
FT MOD_RES 201 201 Phosphothreonine.
FT MOD_RES 207 207 Phosphoserine.
FT MOD_RES 513 513 Phosphoserine.
FT MOD_RES 616 616 N6-acetyllysine.
FT CROSSLNK 230 230 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT CROSSLNK 293 293 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT CONFLICT 528 528 K -> M (in Ref. 3; AAH25279).
SQ SEQUENCE 953 AA; 107473 MW; 084343934F8B3196 CRC64;
MAETLPGSGD SGPGTASLGP GVAETGTRRL SELRVIDLRA ELKKRNLDTG GNKSVLMERL
KKAVKEEGQD PDEIGIELEA TSKKSAKRCV KGLKMEEEGT EDNGLEDDSR DGQEDMEASL
ENLQNMGMMD MSVLDETEVA NSSAPDFGED GTDGLLDSFC DSKEYVAAQL RQLPAQPPEH
AVDGEGFKNT LETSSLNFKV TPDIEESLLE PENEKILDIL GETCKSEPVK EESSELEQPF
AQDTSSVGPD RKLAEEEDLF DSAHPEEGDL DLASESTAHA QSSKADSLLA VVKREPAEQP
GDGERTDCEP VGLEPAVEQS SAASELAEAS SEELAEAPTE APSPEARDSK EDGRKFDFDA
CNEVPPAPKE SSTSEGADQK MSSFKEEKDI KPIIKDEKGR VGSGSGRNLW VSGLSSTTRA
TDLKNLFSKY GKVVGAKVVT NARSPGARCY GFVTMSTSDE ATKCISHLHR TELHGRMISV
EKAKNEPAGK KLSDRKECEV KKEKLSSVDR HHSVEIKIEK TVIKKEEKIE KKEEKKPEDI
KKEEKDQDEL KPGPTNRSRV TKSGSRGMER TVVMDKSKGE PVISVKTTSR SKERSSKSQD
RKSESKEKRD ILSFDKIKEQ RERERQRQRE REIRETERRR EREQREREQR LEAFHERKEK
ARLQRERLQL ECQRQRLERE RMERERLERE RMRVERERRK EQERIHRERE ELRRQQEQLR
YEQERRPGRR PYDLDRRDDA YWPEGKRVAM EDRYRADFPR PDHRFHDFDH RDRGQYQDHA
IDRREGSRPM MGDHRDGQHY GDDRHGHGGP PERHGRDSRD GWGGYGSDKR LSEGRGLPPP
PRGGRDWGEH NQRLEEHQAR AWQGAMDAGA ASREHARWQG GERGLSGPSG PGHMASRGGV
AGRGGFAQGG HSQGHVVPGG GLEGGGVASQ DRGSRVPHPH PHPPPYPHFT RRY
//
MIM
608066
*RECORD*
*FIELD* NO
608066
*FIELD* TI
*608066 SCAFFOLD ATTACHMENT FACTOR B2; SAFB2
;;KIAA0138
*FIELD* TX
CLONING
By sequencing cDNAs randomly selected from a cDNA library derived from
read morethe human immature myeloid cell line KG-1, Nagase et al. (1995)
identified a partial cDNA, which they designated KIAA0138. Northern blot
analysis detected expression in all human tissues and cell lines
examined, with highest expression in kidney and lowest expression in
liver.
By database searching with the sequence of nuclear matrix
protein/scaffold attachment factor (SAFB; 602895) as query, Townson et
al. (2003) identified KIAA0138, which they renamed SAFB2, as a member of
the scaffold attachment factor family. SAFB2 encodes a deduced 953-amino
acid protein with 75% homology to SAFB. Both SAFB and SAFB2 contain a
highly conserved SAF box and RRM domain and both contain a nuclear
localization signal. Using RT-PCR with SAFB2-specific primers, Townson
et al. (2003) found that, like SAFB, SAFB2 is expressed in several
breast cancer cell lines. Using SAFB- and SAFB2-specific probes in RNase
protection assays, they found that the 2 genes are coexpressed in many
tissues.
GENE FUNCTION
As had been shown for SAFB, Townson et al. (2003) found that SAFB2
functions as an estrogen receptor corepressor and that its
overexpression results in inhibition of proliferation. SAFB and SAFB2
interact directly through a C-terminal domain, resulting in additive
repression activity. Whereas SAFB is exclusively nuclear, SAFB2 is found
in the cytoplasm as well as in the nucleus. Transfection experiments
detected interaction between SAFB2 and vinexin, a protein involved in
linking signaling to the cytoskeleton.
Using chromatin immunoprecipitation (ChIP)-on-chip and gene expression
array analyses of MCF7 human breast cancer cells, Hammerich-Hille et al.
(2010) identified 541 SAFB1- and/or SAFB2-binding sites in promoters of
known genes. Enrichment of binding sites was observed in regions of
chromosomes 1 and 6 containing histone gene clusters. Gene expression
array analysis revealed upregulation of most target genes following
knockdown of SAFB1 or SAFB2 via small interfering RNA. In general, SAFB2
regulated fewer genes than SAFB1, and there was relatively little
overlap in the genes regulated by SAFB1 and SAFB2.
GENE STRUCTURE
Townson et al. (2003) determined that the SAFB and SAFB2 genes are
adjacent and arranged in a head-to-head fashion, being separated by a
short GC-rich intergenic region that can function as a bidirectional
promoter. The bidirectional promoter contains a number of potential
transcription factor binding sites, SP1 being the most frequent.
MAPPING
By sequence analysis, Townson et al. (2003) identified the SAFB2 gene
adjacent to the SAFB gene on chromosome 19p13.3.
*FIELD* RF
1. Hammerich-Hille, S.; Kaipparettu, B. A.; Tsimelzon, A.; Creighton,
C. J.; Jiang, S.; Polo, J. M.; Melnick, A.; Meyer, R.; Oesterreich,
S.: SAFB1 mediates repression of immune regulators and apoptotic
genes in breast cancer cells. J. Biol. Chem. 285: 3608-3616, 2010.
2. Nagase, T.; Seki, N.; Tanaka, A.; Ishikawa, K.; Nomura, N.: 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. DNA Res. 2: 167-174, 1995.
3. Townson, S. M.; Dobrzycka, K. M.; Lee, A. V.; Air, M.; Deng, W.;
Kang, K.; Jiang, S.; Kioka, N.; Michaelis, K.; Oesterreich, S.: SAFB2,
a new scaffold attachment factor homolog and estrogen receptor corepressor. J.
Biol. Chem. 278: 20059-20068, 2003.
*FIELD* CN
Patricia A. Hartz - updated: 8/31/2011
*FIELD* CD
Carol A. Bocchini: 8/28/2003
*FIELD* ED
mgross: 09/08/2011
terry: 8/31/2011
tkritzer: 8/29/2003
carol: 8/29/2003
*RECORD*
*FIELD* NO
608066
*FIELD* TI
*608066 SCAFFOLD ATTACHMENT FACTOR B2; SAFB2
;;KIAA0138
*FIELD* TX
CLONING
By sequencing cDNAs randomly selected from a cDNA library derived from
read morethe human immature myeloid cell line KG-1, Nagase et al. (1995)
identified a partial cDNA, which they designated KIAA0138. Northern blot
analysis detected expression in all human tissues and cell lines
examined, with highest expression in kidney and lowest expression in
liver.
By database searching with the sequence of nuclear matrix
protein/scaffold attachment factor (SAFB; 602895) as query, Townson et
al. (2003) identified KIAA0138, which they renamed SAFB2, as a member of
the scaffold attachment factor family. SAFB2 encodes a deduced 953-amino
acid protein with 75% homology to SAFB. Both SAFB and SAFB2 contain a
highly conserved SAF box and RRM domain and both contain a nuclear
localization signal. Using RT-PCR with SAFB2-specific primers, Townson
et al. (2003) found that, like SAFB, SAFB2 is expressed in several
breast cancer cell lines. Using SAFB- and SAFB2-specific probes in RNase
protection assays, they found that the 2 genes are coexpressed in many
tissues.
GENE FUNCTION
As had been shown for SAFB, Townson et al. (2003) found that SAFB2
functions as an estrogen receptor corepressor and that its
overexpression results in inhibition of proliferation. SAFB and SAFB2
interact directly through a C-terminal domain, resulting in additive
repression activity. Whereas SAFB is exclusively nuclear, SAFB2 is found
in the cytoplasm as well as in the nucleus. Transfection experiments
detected interaction between SAFB2 and vinexin, a protein involved in
linking signaling to the cytoskeleton.
Using chromatin immunoprecipitation (ChIP)-on-chip and gene expression
array analyses of MCF7 human breast cancer cells, Hammerich-Hille et al.
(2010) identified 541 SAFB1- and/or SAFB2-binding sites in promoters of
known genes. Enrichment of binding sites was observed in regions of
chromosomes 1 and 6 containing histone gene clusters. Gene expression
array analysis revealed upregulation of most target genes following
knockdown of SAFB1 or SAFB2 via small interfering RNA. In general, SAFB2
regulated fewer genes than SAFB1, and there was relatively little
overlap in the genes regulated by SAFB1 and SAFB2.
GENE STRUCTURE
Townson et al. (2003) determined that the SAFB and SAFB2 genes are
adjacent and arranged in a head-to-head fashion, being separated by a
short GC-rich intergenic region that can function as a bidirectional
promoter. The bidirectional promoter contains a number of potential
transcription factor binding sites, SP1 being the most frequent.
MAPPING
By sequence analysis, Townson et al. (2003) identified the SAFB2 gene
adjacent to the SAFB gene on chromosome 19p13.3.
*FIELD* RF
1. Hammerich-Hille, S.; Kaipparettu, B. A.; Tsimelzon, A.; Creighton,
C. J.; Jiang, S.; Polo, J. M.; Melnick, A.; Meyer, R.; Oesterreich,
S.: SAFB1 mediates repression of immune regulators and apoptotic
genes in breast cancer cells. J. Biol. Chem. 285: 3608-3616, 2010.
2. Nagase, T.; Seki, N.; Tanaka, A.; Ishikawa, K.; Nomura, N.: 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. DNA Res. 2: 167-174, 1995.
3. Townson, S. M.; Dobrzycka, K. M.; Lee, A. V.; Air, M.; Deng, W.;
Kang, K.; Jiang, S.; Kioka, N.; Michaelis, K.; Oesterreich, S.: SAFB2,
a new scaffold attachment factor homolog and estrogen receptor corepressor. J.
Biol. Chem. 278: 20059-20068, 2003.
*FIELD* CN
Patricia A. Hartz - updated: 8/31/2011
*FIELD* CD
Carol A. Bocchini: 8/28/2003
*FIELD* ED
mgross: 09/08/2011
terry: 8/31/2011
tkritzer: 8/29/2003
carol: 8/29/2003