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Q14151

- SAFB2_HUMAN

UniProt

Q14151 - SAFB2_HUMAN

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Protein
Scaffold attachment factor B2
Gene
SAFB2, KIAA0138
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134987683.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 953952Scaffold attachment factor B2
PRO_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)1 Publication
Cross-linki293 – 293Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication
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.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 6435SAP
Add
BLAST
Domaini407 – 48579RRM
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni600 – 953354Interacts with SAFB1
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi713 – 73018Nuclear localization signal Reviewed prediction
Add
BLAST

Compositional bias

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

Sequence similaritiesi

Contains 1 SAP domain.

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]

Sequencei

Sequence statusi: Complete.

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

Q14151-1 [UniParc]FASTAAdd to Basket

« 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

Sequence cautioni

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti528 – 5281K → M in AAH25279. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50928 mRNA. Translation: BAA09487.2. Different initiation.
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.
GeneIDi9667.
KEGGihsa:9667.
UCSCiuc002mcd.3. human.

Polymorphism databases

DMDMi38372432.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D50928 mRNA. Translation: BAA09487.2 . Different initiation.
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 .
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

« Hide 'large scale' publications
  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].
    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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
  5. "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.
  6. "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.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  8. "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].
  9. "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.
  10. "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.
  11. "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].
  12. "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.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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.
  15. "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].
  16. "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].
  17. 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): Q8TB13
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 135 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

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