Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Scaffold attachment factor B1

Gene

Safb

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to scaffold/matrix attachment region (S/MAR) DNA and forms a molecular assembly point to allow the formation of a 'transcriptosomal' complex (consisting of SR proteins and RNA polymerase II) coupling transcription and RNA processing. Can function as an estrogen receptor corepressor and can also bind to the HSP27 promoter and decrease its transcription. Can inhibit cell proliferation. When associated with RBMX, binds to and stimulates transcription from the SREBF1 promoter.1 Publication

GO - Molecular functioni

  • chromatin binding Source: UniProtKB
  • core promoter binding Source: UniProtKB
  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: MGI
  • sequence-specific DNA binding Source: Ensembl

GO - Biological processi

  • growth Source: MGI
  • hormone metabolic process Source: MGI
  • intracellular estrogen receptor signaling pathway Source: MGI
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • regulation of mRNA processing Source: Ensembl
  • 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 B1
Short name:
SAF-B1
Gene namesi
Name:Safb
Synonyms:Safb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 17

Organism-specific databases

MGIiMGI:2146974. Safb.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 937936Scaffold attachment factor B1PRO_0000413022Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity
Modified residuei24 – 241PhosphoserineBy similarity
Modified residuei55 – 551PhosphoserineBy similarity
Cross-linki172 – 172Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei188 – 1881PhosphothreonineBy similarity
Modified residuei195 – 1951PhosphoserineBy similarity
Modified residuei197 – 1971PhosphoserineBy similarity
Modified residuei209 – 2091PhosphoserineBy similarity
Cross-linki231 – 231Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki316 – 316Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei405 – 4051PhosphoserineBy similarity
Modified residuei406 – 4061PhosphoserineBy similarity
Modified residuei437 – 4371PhosphoserineBy similarity
Cross-linki505 – 505Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki565 – 565Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Cross-linki600 – 600Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity
Modified residuei602 – 6021PhosphoserineBy similarity
Modified residuei604 – 6041PhosphoserineBy similarity
Modified residuei623 – 6231PhosphoserineBy similarity
Modified residuei626 – 6261PhosphoserineCombined sources
Modified residuei629 – 6291N6-acetyllysineBy similarity

Post-translational modificationi

Sumoylated by PIAS1 with SUMO1 and SUMO2/3, desumoylated by SENP1. Sumoylation is required for transcriptional repressor activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiD3YXK2.
MaxQBiD3YXK2.
PaxDbiD3YXK2.
PRIDEiD3YXK2.

PTM databases

iPTMnetiD3YXK2.

Expressioni

Gene expression databases

BgeeiD3YXK2.
ExpressionAtlasiD3YXK2. baseline and differential.
GenevisibleiD3YXK2. MM.

Interactioni

Subunit structurei

Monomer. Can form homodimers. Interacts with KHDRBS3, POLR2A, SAFB2 or SFRS1, SFRS9 and TRA2B/SFRS10 (By similarity). Interacts with RBMX. Interacts with SRPK1 and inhibits its activity (By similarity).By similarity

Protein-protein interaction databases

BioGridi230338. 3 interactions.
IntActiD3YXK2. 1 interaction.
STRINGi10090.ENSMUSP00000092849.

Structurei

3D structure databases

ProteinModelPortaliD3YXK2.
SMRiD3YXK2. Positions 425-506.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini31 – 6535SAPPROSITE-ProRule annotationAdd
BLAST
Domaini428 – 50679RRMPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni550 – 814265Interaction with POLR2ABy similarityAdd
BLAST
Regioni621 – 937317Interaction with SAFB2By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili652 – 72675Sequence analysisAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi621 – 63818Nuclear localization signalSequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi96 – 285190Glu-richAdd
BLAST
Compositional biasi634 – 853220Arg-richAdd
BLAST
Compositional biasi640 – 72687Glu-richAdd
BLAST
Compositional biasi807 – 925119Gly-richAdd
BLAST

Sequence similaritiesi

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

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiKOG4661. Eukaryota.
ENOG4111F1G. LUCA.
GeneTreeiENSGT00730000110777.
HOGENOMiHOG000092533.
InParanoidiD3YXK2.
OrthoDBiEOG722J7Z.
PhylomeDBiD3YXK2.
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]
SUPFAMiSSF54928. SSF54928. 1 hit.
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.

D3YXK2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAETLSGLGD ASAAGAAAVS SAASETGTRR LSDLRVIDLR AELKKRNLDS
60 70 80 90 100
SGNKSVLMER LKKAIEDEGG NPDEIEVTSE CNKKMPKRPS KGRKPEDEGV
110 120 130 140 150
EDNGLEENSG DGQEDVETSL ENLQDMDMMD ISVLDEADID NGSVADCVEE
160 170 180 190 200
EEEATLPEGL ADSTELVEGD LKGLPEQLQE HAIDDKDTVN NVDTSSSDFT
210 220 230 240 250
MLQEMEEASL EPENEKILDI LGETCKSEPV KEEGSELEQP FAQATSSVGP
260 270 280 290 300
DRKLAEEEDL FESCGHPEEE EEEEEEDQEE EQEEEGDLAL ASSSKSESPS
310 320 330 340 350
TRCQWSEADA PLAVVKREPA DAPGGGTGMD REPVGLEEPV EQSSTAAQLP
360 370 380 390 400
EATSQELVRA PTAALSPEPQ DSKEDVKKFA FDACNDVPAP PKESSASEGA
410 420 430 440 450
DQKMSSVEED SDTKRLSREE KGRSSCGRNF WVSGLSSTTR ATDLKNLFSR
460 470 480 490 500
YGKVVGAKVV TNARSPGARC YGFVTMSTAE EATKCISHLH KTELHGKMIS
510 520 530 540 550
VEKAKSEPTG KRVPDRRDGD SKKEKASTSD RSANLKREEK GERKDDAKKT
560 570 580 590 600
DDGSTEKSKD ADDQKPGPSE RSRTTKSGSR GTERTVVMDK SKGVPVISVK
610 620 630 640 650
TSGSKERASK SQDRKSASRE KRSVVSFDKV KESRKSRDSE SRRERERSER
660 670 680 690 700
EQRLQAQWER EERERLEIAR ERLAFHRHRL ERERMERERL ERERMHVEQE
710 720 730 740 750
RRREQERIHR EREELRRQQE LRYEQERRPA VRRPYEVDGR RDDAYWPEAK
760 770 780 790 800
RAALDDRYHS DFSRQDRFHD FDHRDRGRYP NHSVDRREGS RSMMGDREGQ
810 820 830 840 850
HYPERHGGPE RHGRDSRDGW GYGSNKRLSE GRGLPPPPRR DWGEHGRRLE
860 870 880 890 900
DDRAWQGTAD GGMMERDHKR WQGGERSMSG HSGPGHMMNR GGMSGRGSFA
910 920 930
PGGASRGHVI PRGGMQAGFG GQSRGSRPSD ARFTRRY
Length:937
Mass (Da):105,104
Last modified:April 5, 2011 - v2
Checksum:iD246A419FA465C3D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT485788 Genomic DNA. No translation available.
CH466537 Genomic DNA. Translation: EDL38175.1.
BC018200 mRNA. No translation available.
AK087504 mRNA. No translation available.
CCDSiCCDS50152.1.
RefSeqiNP_001156772.1. NM_001163300.1.
UniGeneiMm.255066.

Genome annotation databases

EnsembliENSMUST00000095224; ENSMUSP00000092849; ENSMUSG00000071054.
GeneIDi224903.
KEGGimmu:224903.
UCSCiuc012avv.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CT485788 Genomic DNA. No translation available.
CH466537 Genomic DNA. Translation: EDL38175.1.
BC018200 mRNA. No translation available.
AK087504 mRNA. No translation available.
CCDSiCCDS50152.1.
RefSeqiNP_001156772.1. NM_001163300.1.
UniGeneiMm.255066.

3D structure databases

ProteinModelPortaliD3YXK2.
SMRiD3YXK2. Positions 425-506.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi230338. 3 interactions.
IntActiD3YXK2. 1 interaction.
STRINGi10090.ENSMUSP00000092849.

PTM databases

iPTMnetiD3YXK2.

Proteomic databases

EPDiD3YXK2.
MaxQBiD3YXK2.
PaxDbiD3YXK2.
PRIDEiD3YXK2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000095224; ENSMUSP00000092849; ENSMUSG00000071054.
GeneIDi224903.
KEGGimmu:224903.
UCSCiuc012avv.1. mouse.

Organism-specific databases

CTDi6294.
MGIiMGI:2146974. Safb.

Phylogenomic databases

eggNOGiKOG4661. Eukaryota.
ENOG4111F1G. LUCA.
GeneTreeiENSGT00730000110777.
HOGENOMiHOG000092533.
InParanoidiD3YXK2.
OrthoDBiEOG722J7Z.
PhylomeDBiD3YXK2.
TreeFamiTF325240.

Miscellaneous databases

ChiTaRSiSafb. mouse.
NextBioi377448.
PROiD3YXK2.
SOURCEiSearch...

Gene expression databases

BgeeiD3YXK2.
ExpressionAtlasiD3YXK2. baseline and differential.
GenevisibleiD3YXK2. MM.

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]
SUPFAMiSSF54928. SSF54928. 1 hit.
PROSITEiPS50102. RRM. 1 hit.
PS50800. SAP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  2. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
    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 1-203.
    Tissue: Mammary tumor.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 405-937.
    Strain: C57BL/6J.
    Tissue: Eye.
  5. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. "SAFB1, an RBMX-binding protein, is a newly identified regulator of hepatic SREBP-1c gene."
    Omura Y., Nishio Y., Takemoto T., Ikeuchi C., Sekine O., Morino K., Maeno Y., Obata T., Ugi S., Maegawa H., Kimura H., Kashiwagi A.
    BMB Rep. 42:232-237(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RBMX, ASSOCIATION WITH CHROMATIN.
  7. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-626, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brown adipose tissue, Kidney, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSAFB1_MOUSE
AccessioniPrimary (citable) accession number: D3YXK2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2011
Last sequence update: April 5, 2011
Last modified: March 16, 2016
This is version 59 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.