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Reviewed, UniProtKB/Swiss-Prot Q14151 (SAFB2_HUMAN)

Last modified June 16, 2009. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Scaffold attachment factor B2
      Short name=SAF-B2
Gene names
Name: SAFB2
Synonyms: KIAA0138
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length953 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Subunit structure

Interacts with SAFB/SAFB1 and SCAM1.

Subcellular location

Cytoplasm. Nucleus.

Tissue specificity

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

Post-translational modification

Phosphorylated upon DNA damage, probably by ATM or ATR By similarity.

Sequence similarities

Contains 1 RRM (RNA recognition motif) domain.

Contains 1 SAP domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   LigandDNA-binding
RNA-binding
   Molecular functionRepressor
   PTMPhosphoprotein
Gene Ontology (GO)
   Biological processregulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

transcription

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionDNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotide binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 953953Scaffold attachment factor B2
PRO_0000081907

Regions

Domain30 – 6435SAP
Domain407 – 48579RRM
Region600 – 953354Interacts with SAFB1
Motif713 – 73018Nuclear localization signal Potential
Compositional bias482 – 54564Lys-rich
Compositional bias619 – 724106Glu-rich
Compositional bias621 – 788168Arg-rich
Compositional bias792 – 926135Gly-rich

Amino acid modifications

Modified residue311Phosphoserine Ref.7
Modified residue1091Phosphoserine Ref.5 Ref.6
Modified residue2071Phosphoserine Ref.8 Ref.10
Modified residue2341Phosphoserine By similarity
Modified residue2871Phosphoserine Ref.10
Modified residue3311Phosphoserine By similarity
Modified residue3431Phosphoserine Ref.6 Ref.10 Ref.9
Modified residue5131Phosphoserine Ref.6
Modified residue6131Phosphoserine Ref.10

Experimental info

Sequence conflict5281K → M in AAH25279. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q14151-1 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 084343934F8B3196

FASTA953107,473
        10         20         30         40         50         60 
MAETLPGSGD SGPGTASLGP GVAETGTRRL SELRVIDLRA ELKKRNLDTG GNKSVLMERL 

        70         80         90        100        110        120 
KKAVKEEGQD PDEIGIELEA TSKKSAKRCV KGLKMEEEGT EDNGLEDDSR DGQEDMEASL 

       130        140        150        160        170        180 
ENLQNMGMMD MSVLDETEVA NSSAPDFGED GTDGLLDSFC DSKEYVAAQL RQLPAQPPEH 

       190        200        210        220        230        240 
AVDGEGFKNT LETSSLNFKV TPDIEESLLE PENEKILDIL GETCKSEPVK EESSELEQPF 

       250        260        270        280        290        300 
AQDTSSVGPD RKLAEEEDLF DSAHPEEGDL DLASESTAHA QSSKADSLLA VVKREPAEQP 

       310        320        330        340        350        360 
GDGERTDCEP VGLEPAVEQS SAASELAEAS SEELAEAPTE APSPEARDSK EDGRKFDFDA 

       370        380        390        400        410        420 
CNEVPPAPKE SSTSEGADQK MSSFKEEKDI KPIIKDEKGR VGSGSGRNLW VSGLSSTTRA 

       430        440        450        460        470        480 
TDLKNLFSKY GKVVGAKVVT NARSPGARCY GFVTMSTSDE ATKCISHLHR TELHGRMISV 

       490        500        510        520        530        540 
EKAKNEPAGK KLSDRKECEV KKEKLSSVDR HHSVEIKIEK TVIKKEEKIE KKEEKKPEDI 

       550        560        570        580        590        600 
KKEEKDQDEL KPGPTNRSRV TKSGSRGMER TVVMDKSKGE PVISVKTTSR SKERSSKSQD 

       610        620        630        640        650        660 
RKSESKEKRD ILSFDKIKEQ RERERQRQRE REIRETERRR EREQREREQR LEAFHERKEK 

       670        680        690        700        710        720 
ARLQRERLQL ECQRQRLERE RMERERLERE RMRVERERRK EQERIHRERE ELRRQQEQLR 

       730        740        750        760        770        780 
YEQERRPGRR PYDLDRRDDA YWPEGKRVAM EDRYRADFPR PDHRFHDFDH RDRGQYQDHA 

       790        800        810        820        830        840 
IDRREGSRPM MGDHRDGQHY GDDRHGHGGP PERHGRDSRD GWGGYGSDKR LSEGRGLPPP 

       850        860        870        880        890        900 
PRGGRDWGEH NQRLEEHQAR AWQGAMDAGA ASREHARWQG GERGLSGPSG PGHMASRGGV 

       910        920        930        940        950 
AGRGGFAQGG HSQGHVVPGG GLEGGGVASQ DRGSRVPHPH PHPPPYPHFT RRY 

« Hide

References

« Hide 'large scale' references
[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: 8590280] [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. expand/collapse author list , 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: 15057824] [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: 15489334] [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: 12660241] [Abstract]
Cited for: CHARACTERIZATION.
[5]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109, MASS SPECTROMETRY.
Tissue: Epithelium.
[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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-109; SER-343 AND SER-513, MASS SPECTROMETRY.
Tissue: Epithelium.
[7]"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, MASS SPECTROMETRY.
Tissue: Epithelium.
[8]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207, MASS SPECTROMETRY.
[9]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343, MASS SPECTROMETRY.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-207; SER-287; SER-343 AND SER-613, MASS SPECTROMETRY.
[11]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

D50928 mRNA. Translation: BAA09487.2. Different initiation.
AC004611 Genomic DNA. Translation: AAC14666.1.
BC025279 mRNA. Translation: AAH25279.1.
IPIIPI00005648.
RefSeqNP_055464.1.
UniGeneHs.655392

3D structure databases

HSSPHSSP built from PDB template 2MST based on UniProtKB Q61474.
ModBaseSearch...

Protein-protein interaction databases

IntActQ14151. 3 interactions.

PTM databases

PhosphoSiteQ14151.

Proteomic databases

PeptideAtlasQ14151.
PRIDEQ14151.

Genome annotation databases

EnsemblENSG00000130254. Homo sapiens. [Contig view]
GeneID9667.
KEGGhsa:9667.

Organism-specific databases

GeneCardsGC19M005538.
H-InvDBHIX0014676.
HGNCHGNC:21605. SAFB2.
MIM608066. gene.
PharmGKBPA134987683.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMQ14151.
HOVERGENQ14151.
OMAQ14151. DRKECEV.

Gene expression databases

ArrayExpressQ14151.
BgeeQ14151.
CleanExHS_SAFB2.
GermOnlineENSG00000130254. Homo sapiens.

Family and domain databases

InterProIPR012677. a_b_plait_nuc_bd.
IPR000504. RRM_RNP1.
IPR003034. SAP_DNA_bd.
[Graphical view]
Gene3DG3DSA:3.30.70.330. a_b_plait_nuc_bd. 1 hit.
PfamPF00076. RRM_1. 1 hit.
PF02037. SAP. 1 hit.
[Graphical view]
SMARTSM00360. RRM. 1 hit.
SM00513. SAP. 1 hit.
[Graphical view]
PROSITEPS50102. RRM. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio36299.
SOURCESearch...

Entry information

Entry nameSAFB2_HUMAN
AccessionPrimary (citable) accession number: Q14151
Secondary accession number(s): Q8TB13
Entry history
Integrated into UniProtKB/Swiss-Prot: November 14, 2003
Last sequence update: November 1, 1996
Last modified: June 16, 2009
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents