LOCUS       NP_055464                953 aa            linear   PRI 28-APR-2025
DEFINITION  scaffold attachment factor B2 [Homo sapiens].
ACCESSION   NP_055464 XP_375559
VERSION     NP_055464.1
DBSOURCE    REFSEQ: accession NM_014649.3
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 953)
  AUTHORS   Zhen,H., Yao,Y. and Yang,H.
  TITLE     SAFB2 Inhibits the Progression of Breast Cancer by Suppressing the
            Wnt/beta-Catenin Signaling Pathway via NFAT5
  JOURNAL   Mol Biotechnol 65 (9), 1465-1475 (2023)
   PUBMED   36652182
  REMARK    GeneRIF: SAFB2 Inhibits the Progression of Breast Cancer by
            Suppressing the Wnt/beta-Catenin Signaling Pathway via NFAT5.
REFERENCE   2  (residues 1 to 953)
  AUTHORS   Hutter,K., Lohmuller,M., Jukic,A., Eichin,F., Avci,S., Labi,V.,
            Szabo,T.G., Hoser,S.M., Huttenhofer,A., Villunger,A. and Herzog,S.
  TITLE     SAFB2 Enables the Processing of Suboptimal Stem-Loop Structures in
            Clustered Primary miRNA Transcripts
  JOURNAL   Mol Cell 78 (5), 876-889 (2020)
   PUBMED   32502422
  REMARK    GeneRIF: SAFB2 Enables the Processing of Suboptimal Stem-Loop
            Structures in Clustered Primary miRNA Transcripts.
REFERENCE   3  (residues 1 to 953)
  AUTHORS   Hong,E., Best,A., Gautrey,H., Chin,J., Razdan,A., Curk,T.,
            Elliott,D.J. and Tyson-Capper,A.J.
  TITLE     Unravelling the RNA-Binding Properties of SAFB Proteins in Breast
            Cancer Cells
  JOURNAL   Biomed Res Int 2015, 395816 (2015)
   PUBMED   26273616
  REMARK    GeneRIF: Single depletion of either SAFB1 or SAFB2 leads to an
            increase in expression of the other SAFB protein.
REFERENCE   4  (residues 1 to 953)
  AUTHORS   Hashimoto,T., Matsuda,K. and Kawata,M.
  TITLE     Scaffold attachment factor B (SAFB)1 and SAFB2 cooperatively
            inhibit the intranuclear mobility and function of ERalpha
  JOURNAL   J Cell Biochem 113 (9), 3039-3050 (2012)
   PUBMED   22566185
  REMARK    GeneRIF: Results indicate that SAFB1 and SAFB2 are crucial
            repressors for ERalpha dynamics in association with the nuclear
            matrix and that their synergistic regulation of ERalpha mobility is
            sufficient for inhibiting ERalpha function.
REFERENCE   5  (residues 1 to 953)
  AUTHORS   Hammerich-Hille,S., Bardout,V.J., Hilsenbeck,S.G., Osborne,C.K. and
            Oesterreich,S.
  TITLE     Low SAFB levels are associated with worse outcome in breast cancer
            patients
  JOURNAL   Breast Cancer Res Treat 121 (2), 503-509 (2010)
   PUBMED   19137425
  REMARK    GeneRIF: This study shows that low SAFB protein levels predict poor
            prognosis of breast cancer patients, suggesting critical functions
            of SAFB1 and SAFB2 in breast cancer cells.
REFERENCE   6  (residues 1 to 953)
  AUTHORS   Hammerich-Hille,S., Kaipparettu,B.A., Tsimelzon,A., Creighton,C.J.,
            Jiang,S., Polo,J.M., Melnick,A., Meyer,R. and Oesterreich,S.
  TITLE     SAFB1 mediates repression of immune regulators and apoptotic genes
            in breast cancer cells
  JOURNAL   J Biol Chem 285 (6), 3608-3616 (2010)
   PUBMED   19901029
  REMARK    GeneRIF: Study confirms the primary role of SAFB1/SAFB2 as
            corepressors and also uncovers a previously unknown role for SAFB1
            in the regulation of immune genes and in estrogen-mediated
            repression of genes.
REFERENCE   7  (residues 1 to 953)
  AUTHORS   Tsianou,D., Nikolakaki,E., Tzitzira,A., Bonanou,S., Giannakouros,T.
            and Georgatsou,E.
  TITLE     The enzymatic activity of SR protein kinases 1 and 1a is negatively
            affected by interaction with scaffold attachment factors B1 and 2
  JOURNAL   FEBS J 276 (18), 5212-5227 (2009)
   PUBMED   19674106
  REMARK    GeneRIF: The enzymatic activity of SR protein kinases 1 and 1a is
            negatively affected by interaction with scaffold attachment factors
            B1 and 2.
REFERENCE   8  (residues 1 to 953)
  AUTHORS   Bergman,A., Abel,F., Behboudi,A., Yhr,M., Mattsson,J.,
            Svensson,J.H., Karlsson,P. and Nordling,M.
  TITLE     No germline mutations in supposed tumour suppressor genes SAFB1 and
            SAFB2 in familial breast cancer with linkage to 19p
  JOURNAL   BMC Med Genet 9, 108 (2008)
   PUBMED   19077293
  REMARK    GeneRIF: SAFB2 is not likely to be causative of the hereditary
            breast cancer syndrome in west Swedish breast cancer families
            Publication Status: Online-Only
REFERENCE   9  (residues 1 to 953)
  AUTHORS   Oesterreich,S.
  TITLE     Scaffold attachment factors SAFB1 and SAFB2: Innocent bystanders or
            critical players in breast tumorigenesis?
  JOURNAL   J Cell Biochem 90 (4), 653-661 (2003)
   PUBMED   14587024
  REMARK    GeneRIF: REVIEW: possibility that SAFB1 and SAFB2 are novel breast
            tumor suppressor genes, and how they might function in this role,
            are discussed
            Review article
REFERENCE   10 (residues 1 to 953)
  AUTHORS   Townson,S.M., Dobrzycka,K.M., Lee,A.V., Air,M., Deng,W., Kang,K.,
            Jiang,S., Kioka,N., Michaelis,K. and Oesterreich,S.
  TITLE     SAFB2, a new scaffold attachment factor homolog and estrogen
            receptor corepressor
  JOURNAL   J Biol Chem 278 (22), 20059-20068 (2003)
   PUBMED   12660241
COMMENT     REVIEWED REFSEQ: This record has been curated by NCBI staff. The
            reference sequence was derived from DB475007.1, D50928.1 and
            AW136754.1.
            This sequence is a reference standard in the RefSeqGene project.
            
            On Aug 30, 2004 this sequence version replaced XP_375559.1.
            
            Summary: The protein encoded by this gene, along with its paralog
            (scaffold attachment factor B1), is a repressor of estrogen
            receptor alpha. The encoded protein binds scaffold/matrix
            attachment region (S/MAR) DNA and is involved in cell cycle
            regulation, apoptosis, differentiation, the stress response, and
            regulation of immune genes. [provided by RefSeq, May 2016].
            
            ##Evidence-Data-START##
            Transcript exon combination :: D50928.1, SRR1660807.108917.1
                                           [ECO:0000332]
            RNAseq introns              :: mixed sample support SAMEA1965299,
                                           SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            MANE Ensembl match     :: ENST00000252542.9/ ENSP00000252542.3
            RefSeq Select criteria :: based on conservation, expression,
                                      longest protein
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..953
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19p13.3"
     Protein         1..953
                     /product="scaffold attachment factor B2"
                     /calculated_mol_wt=107343
     Region          1..29
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Site            2
                     /site_type="acetylation"
                     /note="N-acetylalanine.
                     /evidence=ECO:0007744|PubMed:19413330,
                     ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378;
                     propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Region          30..64
                     /region_name="SAP"
                     /note="Putative DNA-binding (bihelical) motif predicted to
                     be involved in chromosomal organisation; smart00513"
                     /db_xref="CDD:128789"
     Region          31..>153
                     /region_name="PLN03124"
                     /note="poly [ADP-ribose] polymerase; Provisional"
                     /db_xref="CDD:215591"
     Site            54
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     Region          91..114
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Site            109
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:19367720,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692;
                     propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Site            158
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:24275569; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     Site            201
                     /site_type="phosphorylation"
                     /note="Phosphothreonine.
                     /evidence=ECO:0007744|PubMed:20068231; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     Site            207
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:18669648,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Region          219..404
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Region          406..481
                     /region_name="RRM_SAFB1_SAFB2"
                     /note="RNA recognition motif (RRM) found in scaffold
                     attachment factor B1 (SAFB1), scaffold attachment factor
                     B2 (SAFB2), and similar proteins; cd12679"
                     /db_xref="CDD:410080"
     Site            507
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     Site            513
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:17081983,
                     ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163;
                     propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Region          525..665
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Region          600..953
                     /region_name="Interaction with SAFB1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Site            616
                     /site_type="acetylation"
                     /note="N6-acetyllysine, alternate.
                     /evidence=ECO:0007744|PubMed:19608861; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     Region          684..953
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Region          713..730
                     /region_name="Nuclear localization signal.
                     /evidence=ECO:0000255"
                     /note="propagated from UniProtKB/Swiss-Prot (Q14151.1)"
     Region          756..>843
                     /region_name="RcnB"
                     /note="Periplasmic regulator RcnB of Ni and Co efflux
                     [Inorganic ion transport and metabolism]; COG5455"
                     /db_xref="CDD:444206"
     Site            787
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     Site            832
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     Site            886
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0007744|PubMed:23186163; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     Site            897
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     Site            903
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0007744|PubMed:24129315; propagated from
                     UniProtKB/Swiss-Prot (Q14151.1)"
     CDS             1..953
                     /gene="SAFB2"
                     /coded_by="NM_014649.3:62..2923"
                     /db_xref="CCDS:CCDS32879.1"
                     /db_xref="GeneID:9667"
                     /db_xref="HGNC:HGNC:21605"
                     /db_xref="MIM:608066"
ORIGIN      
        1 maetlpgsgd sgpgtaslgp gvaetgtrrl selrvidlra elkkrnldtg gnksvlmerl
       61 kkavkeegqd pdeigielea tskksakrcv kglkmeeegt edngleddsr dgqedmeasl
      121 enlqnmgmmd msvldeteva nssapdfged gtdglldsfc dskeyvaaql rqlpaqppeh
      181 avdgegfknt letsslnfkv tpdieeslle penekildil getcksepvk eesseleqpf
      241 aqdtssvgpd rklaeeedlf dsahpeegdl dlasestaha qsskadslla vvkrepaeqp
      301 gdgertdcep vglepaveqs saaselaeas seelaeapte apspeardsk edgrkfdfda
      361 cnevppapke sstsegadqk mssfkeekdi kpiikdekgr vgsgsgrnlw vsglssttra
      421 tdlknlfsky gkvvgakvvt narspgarcy gfvtmstsde atkcishlhr telhgrmisv
      481 ekaknepagk klsdrkecev kkeklssvdr hhsveikiek tvikkeekie kkeekkpedi
      541 kkeekdqdel kpgptnrsrv tksgsrgmer tvvmdkskge pvisvkttsr skerssksqd
      601 rkseskekrd ilsfdkikeq rererqrqre reireterrr ereqrereqr leafherkek
      661 arlqrerlql ecqrqrlere rmererlere rmrvererrk eqerihrere elrrqqeqlr
      721 yeqerrpgrr pydldrrdda ywpegkrvam edryradfpr pdhrfhdfdh rdrgqyqdha
      781 idrregsrpm mgdhrdgqhy gddrhghggp perhgrdsrd gwggygsdkr lsegrglppp
      841 prggrdwgeh nqrleehqar awqgamdaga asreharwqg gerglsgpsg pghmasrggv
      901 agrggfaqgg hsqghvvpgg glegggvasq drgsrvphph phpppyphft rry
//
