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Q14151

- SAFB2_HUMAN

UniProt

Q14151 - SAFB2_HUMAN

Protein

Scaffold attachment factor B2

Gene

SAFB2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 136 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    Functioni

    Binds to scaffold/matrix attachment region (S/MAR) DNA. Can function as an estrogen receptor corepressor and can also inhibit cell proliferation.

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. nucleotide binding Source: InterPro
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. regulation of transcription, DNA-templated Source: UniProtKB-KW
    2. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Scaffold attachment factor B2
    Short name:
    SAF-B2
    Gene namesi
    Name:SAFB2
    Synonyms:KIAA0138
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:21605. SAFB2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell
    2. intracellular membrane-bounded organelle Source: HPA
    3. nucleus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA134987683.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed3 Publications
    Chaini2 – 953952Scaffold attachment factor B2PRO_0000081907Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine3 Publications
    Modified residuei109 – 1091Phosphoserine3 Publications
    Modified residuei201 – 2011Phosphothreonine1 Publication
    Modified residuei207 – 2071Phosphoserine2 Publications
    Cross-linki230 – 230Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Cross-linki293 – 293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
    Modified residuei513 – 5131Phosphoserine2 Publications
    Modified residuei616 – 6161N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14151.
    PaxDbiQ14151.
    PeptideAtlasiQ14151.
    PRIDEiQ14151.

    PTM databases

    PhosphoSiteiQ14151.

    Expressioni

    Tissue specificityi

    Expressed at high levels in the CNS and at low levels in the liver. Expressed in a wide number of breast cancer cell lines.

    Gene expression databases

    ArrayExpressiQ14151.
    BgeeiQ14151.
    CleanExiHS_SAFB2.
    GenevestigatoriQ14151.

    Organism-specific databases

    HPAiHPA050894.

    Interactioni

    Subunit structurei

    Interacts with SAFB/SAFB1 and SCAM1. Interacts with isoform 2 SRPK1 and inhibits its activity.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself2EBI-352869,EBI-352869
    ESR1P033722EBI-352869,EBI-78473
    GABARAPL1Q9H0R82EBI-352869,EBI-746969
    MAP1LC3BQ9GZQ83EBI-352869,EBI-373144
    SAFBQ154243EBI-352869,EBI-348298
    SORBS3O60504-23EBI-352869,EBI-1222956

    Protein-protein interaction databases

    BioGridi115022. 28 interactions.
    IntActiQ14151. 20 interactions.
    MINTiMINT-5006081.
    STRINGi9606.ENSP00000252542.

    Structurei

    3D structure databases

    ProteinModelPortaliQ14151.
    SMRiQ14151. Positions 27-68, 404-484.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini30 – 6435SAPPROSITE-ProRule annotationAdd
    BLAST
    Domaini407 – 48579RRMPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni600 – 953354Interacts with SAFB1Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi713 – 73018Nuclear localization signalSequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi482 – 54564Lys-richAdd
    BLAST
    Compositional biasi619 – 724106Glu-richAdd
    BLAST
    Compositional biasi621 – 788168Arg-richAdd
    BLAST
    Compositional biasi792 – 926135Gly-richAdd
    BLAST

    Sequence similaritiesi

    Contains 1 RRM (RNA recognition motif) domain.PROSITE-ProRule annotation
    Contains 1 SAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG248048.
    HOGENOMiHOG000092533.
    HOVERGENiHBG078408.
    InParanoidiQ14151.
    OMAiTPDIEEP.
    OrthoDBiEOG722J7Z.
    PhylomeDBiQ14151.
    TreeFamiTF325240.

    Family and domain databases

    Gene3Di1.10.720.30. 1 hit.
    3.30.70.330. 1 hit.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR003034. SAP_dom.
    [Graphical view]
    PfamiPF00076. RRM_1. 1 hit.
    PF02037. SAP. 1 hit.
    [Graphical view]
    SMARTiSM00360. RRM. 1 hit.
    SM00513. SAP. 1 hit.
    [Graphical view]
    PROSITEiPS50102. RRM. 1 hit.
    PS50800. SAP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14151-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAETLPGSGD SGPGTASLGP GVAETGTRRL SELRVIDLRA ELKKRNLDTG    50
    GNKSVLMERL KKAVKEEGQD PDEIGIELEA TSKKSAKRCV KGLKMEEEGT 100
    EDNGLEDDSR DGQEDMEASL ENLQNMGMMD MSVLDETEVA NSSAPDFGED 150
    GTDGLLDSFC DSKEYVAAQL RQLPAQPPEH AVDGEGFKNT LETSSLNFKV 200
    TPDIEESLLE PENEKILDIL GETCKSEPVK EESSELEQPF AQDTSSVGPD 250
    RKLAEEEDLF DSAHPEEGDL DLASESTAHA QSSKADSLLA VVKREPAEQP 300
    GDGERTDCEP VGLEPAVEQS SAASELAEAS SEELAEAPTE APSPEARDSK 350
    EDGRKFDFDA CNEVPPAPKE SSTSEGADQK MSSFKEEKDI KPIIKDEKGR 400
    VGSGSGRNLW VSGLSSTTRA TDLKNLFSKY GKVVGAKVVT NARSPGARCY 450
    GFVTMSTSDE ATKCISHLHR TELHGRMISV EKAKNEPAGK KLSDRKECEV 500
    KKEKLSSVDR HHSVEIKIEK TVIKKEEKIE KKEEKKPEDI KKEEKDQDEL 550
    KPGPTNRSRV TKSGSRGMER TVVMDKSKGE PVISVKTTSR SKERSSKSQD 600
    RKSESKEKRD ILSFDKIKEQ RERERQRQRE REIRETERRR EREQREREQR 650
    LEAFHERKEK ARLQRERLQL ECQRQRLERE RMERERLERE RMRVERERRK 700
    EQERIHRERE ELRRQQEQLR YEQERRPGRR PYDLDRRDDA YWPEGKRVAM 750
    EDRYRADFPR PDHRFHDFDH RDRGQYQDHA IDRREGSRPM MGDHRDGQHY 800
    GDDRHGHGGP PERHGRDSRD GWGGYGSDKR LSEGRGLPPP PRGGRDWGEH 850
    NQRLEEHQAR AWQGAMDAGA ASREHARWQG GERGLSGPSG PGHMASRGGV 900
    AGRGGFAQGG HSQGHVVPGG GLEGGGVASQ DRGSRVPHPH PHPPPYPHFT 950
    RRY 953
    Length:953
    Mass (Da):107,473
    Last modified:November 1, 1996 - v1
    Checksum:i084343934F8B3196
    GO
    Isoform 2 (identifier: Q14151-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         93-115: LKMEEEGTEDNGLEDDSRDGQED → GHGSKSGEPAEYGHDGHECARRN
         116-953: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:115
    Mass (Da):12,169
    Checksum:i534B2863F1DC5B72
    GO

    Sequence cautioni

    The sequence BAA09487.2 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti528 – 5281K → M in AAH25279. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei93 – 11523LKMEE…DGQED → GHGSKSGEPAEYGHDGHECA RRN in isoform 2. 1 PublicationVSP_056404Add
    BLAST
    Alternative sequencei116 – 953838Missing in isoform 2. 1 PublicationVSP_056405Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50928 mRNA. Translation: BAA09487.2. Different initiation.
    AK296552 mRNA. Translation: BAG59175.1.
    AC004611 Genomic DNA. Translation: AAC14666.1.
    BC025279 mRNA. Translation: AAH25279.1.
    CCDSiCCDS32879.1.
    RefSeqiNP_055464.1. NM_014649.2.
    UniGeneiHs.655392.

    Genome annotation databases

    EnsembliENST00000252542; ENSP00000252542; ENSG00000130254.
    ENST00000591120; ENSP00000468505; ENSG00000130254.
    GeneIDi9667.
    KEGGihsa:9667.
    UCSCiuc002mcd.3. human.

    Polymorphism databases

    DMDMi38372432.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D50928 mRNA. Translation: BAA09487.2 . Different initiation.
    AK296552 mRNA. Translation: BAG59175.1 .
    AC004611 Genomic DNA. Translation: AAC14666.1 .
    BC025279 mRNA. Translation: AAH25279.1 .
    CCDSi CCDS32879.1.
    RefSeqi NP_055464.1. NM_014649.2.
    UniGenei Hs.655392.

    3D structure databases

    ProteinModelPortali Q14151.
    SMRi Q14151. Positions 27-68, 404-484.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115022. 28 interactions.
    IntActi Q14151. 20 interactions.
    MINTi MINT-5006081.
    STRINGi 9606.ENSP00000252542.

    PTM databases

    PhosphoSitei Q14151.

    Polymorphism databases

    DMDMi 38372432.

    Proteomic databases

    MaxQBi Q14151.
    PaxDbi Q14151.
    PeptideAtlasi Q14151.
    PRIDEi Q14151.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000252542 ; ENSP00000252542 ; ENSG00000130254 .
    ENST00000591120 ; ENSP00000468505 ; ENSG00000130254 .
    GeneIDi 9667.
    KEGGi hsa:9667.
    UCSCi uc002mcd.3. human.

    Organism-specific databases

    CTDi 9667.
    GeneCardsi GC19M005587.
    HGNCi HGNC:21605. SAFB2.
    HPAi HPA050894.
    MIMi 608066. gene.
    neXtProti NX_Q14151.
    PharmGKBi PA134987683.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG248048.
    HOGENOMi HOG000092533.
    HOVERGENi HBG078408.
    InParanoidi Q14151.
    OMAi TPDIEEP.
    OrthoDBi EOG722J7Z.
    PhylomeDBi Q14151.
    TreeFami TF325240.

    Miscellaneous databases

    ChiTaRSi SAFB2. human.
    GeneWikii SAFB2.
    GenomeRNAii 9667.
    NextBioi 36299.
    PROi Q14151.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14151.
    Bgeei Q14151.
    CleanExi HS_SAFB2.
    Genevestigatori Q14151.

    Family and domain databases

    Gene3Di 1.10.720.30. 1 hit.
    3.30.70.330. 1 hit.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR000504. RRM_dom.
    IPR003034. SAP_dom.
    [Graphical view ]
    Pfami PF00076. RRM_1. 1 hit.
    PF02037. SAP. 1 hit.
    [Graphical view ]
    SMARTi SM00360. RRM. 1 hit.
    SM00513. SAP. 1 hit.
    [Graphical view ]
    PROSITEi PS50102. RRM. 1 hit.
    PS50800. SAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Bone marrow.
    2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
      Tissue: Thalamus.
    3. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-528 (ISOFORM 1).
      Tissue: Pancreas.
    5. "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] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    7. "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] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: T-cell.
    8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    9. "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] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
    10. "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] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH SRPK1.
    11. "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] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-616, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; THR-201; SER-207 AND SER-513, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Co-repressor activity of scaffold attachment factor B1 requires sumoylation."
      Garee J.P., Meyer R., Oesterreich S.
      Biochem. Biophys. Res. Commun. 408:516-522(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-230 AND LYS-293.
    16. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiSAFB2_HUMAN
    AccessioniPrimary (citable) accession number: Q14151
    Secondary accession number(s): B4DKG3, Q8TB13
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 14, 2003
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 136 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3