Details for: SAFB2

Gene ID: 9667

Symbol: SAFB2

Ensembl ID: ENSG00000130254

Description: scaffold attachment factor B2

Associated with

Other Information

Genular Protein ID: 3151879399

Symbol: SAFB2_HUMAN

Name: Scaffold attachment factor B2

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 8590280

Title: 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.

PubMed ID: 8590280

DOI: 10.1093/dnares/2.4.167

PubMed ID: 14702039

Title: Complete sequencing and characterization of 21,243 full-length human cDNAs.

PubMed ID: 14702039

DOI: 10.1038/ng1285

PubMed ID: 15057824

Title: The DNA sequence and biology of human chromosome 19.

PubMed ID: 15057824

DOI: 10.1038/nature02399

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 12660241

Title: SAFB2, a new scaffold attachment factor homolog and estrogen receptor corepressor.

PubMed ID: 12660241

DOI: 10.1074/jbc.m212988200

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 19367720

Title: Phosphorylation analysis of primary human T lymphocytes using sequential IMAC and titanium oxide enrichment.

PubMed ID: 19367720

DOI: 10.1021/pr800500r

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19674106

Title: The enzymatic activity of SR protein kinases 1 and 1a is negatively affected by interaction with scaffold attachment factors B1 and 2.

PubMed ID: 19674106

DOI: 10.1111/j.1742-4658.2009.07217.x

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21527249

Title: Co-repressor activity of scaffold attachment factor B1 requires sumoylation.

PubMed ID: 21527249

DOI: 10.1016/j.bbrc.2011.04.040

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 22814378

Title: N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB.

PubMed ID: 22814378

DOI: 10.1073/pnas.1210303109

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

Sequence Information:

  • Length: 953
  • Mass: 107473
  • Checksum: 084343934F8B3196
  • Sequence:
  • 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

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.