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Q9ER74 (SALL1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 101. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Sal-like protein 1
Alternative name(s):
Zinc finger protein Spalt-3
Short name=Sal-3
Short name=mSal-3
Gene names
Name:Sall1
Synonyms:Sal3
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length1322 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Transcriptional repressor involved in organogenesis. Essential for ureteric bud invasion in kidney development. Homozygous deletion of SALL1 results in an incomplete ureteric bud outgrowth, a failure of tubule formation in the mesenchyme and an apoptosis of the mesenchyme. Ref.3

Subunit structure

Interacts with HDAC1, HDAC2, RBBP4, RBPP7, MTA1 and MTA2. Interacts with FAM58A By similarity. Probably associates with NuRD histone deacetylase complex (HDAC).

Subcellular location

Nucleus.

Tissue specificity

Expressed in the metanephric mesenchyme surrounding ureteric bud.

Sequence similarities

Belongs to the sal C2H2-type zinc-finger protein family.

Contains 9 C2H2-type zinc fingers.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainRepeat
Zinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   Molecular functionRepressor
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processbranching involved in ureteric bud morphogenesis

Inferred from mutant phenotype PubMed 12482961. Source: UniProtKB

embryonic digit morphogenesis

Inferred from mutant phenotype PubMed 18470945. Source: UniProtKB

forelimb morphogenesis

Inferred from genetic interaction PubMed 19168674. Source: MGI

hindlimb morphogenesis

Inferred from genetic interaction PubMed 19168674. Source: MGI

histone deacetylation

Inferred from mutant phenotype PubMed 16707490. Source: GOC

inductive cell-cell signaling

Inferred from mutant phenotype Ref.2. Source: MGI

kidney epithelium development

Inferred from mutant phenotype PubMed 16839447. Source: UniProtKB

mesenchymal to epithelial transition involved in metanephros morphogenesis

Inferred from mutant phenotype Ref.2. Source: UniProtKB

negative regulation of ectoderm development

Inferred from mutant phenotype PubMed 21062744. Source: BHF-UCL

negative regulation of mesoderm development

Inferred from mutant phenotype PubMed 21062744. Source: BHF-UCL

negative regulation of smoothened signaling pathway

Inferred from genetic interaction PubMed 19168674. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 16707490. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 16707490. Source: UniProtKB

neural tube closure

Inferred from genetic interaction PubMed 16790473. Source: MGI

neural tube development

Inferred from genetic interaction PubMed 18818376. Source: MGI

olfactory bulb development

Inferred from mutant phenotype PubMed 18024993. Source: MGI

olfactory bulb interneuron differentiation

Inferred from mutant phenotype PubMed 18024993. Source: UniProtKB

olfactory nerve development

Inferred from mutant phenotype PubMed 18024993. Source: UniProtKB

positive regulation of neuron differentiation

Inferred from mutant phenotype PubMed 18024993. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 20439720. Source: MGI

regulation of neural precursor cell proliferation

Inferred from mutant phenotype PubMed 18024993. Source: MGI

ureteric bud development

Inferred from mutant phenotype Ref.2. Source: MGI

ureteric bud invasion

Inferred from mutant phenotype Ref.2PubMed 16839447. Source: UniProtKB

ventricular septum development

Inferred from mutant phenotype PubMed 18470945. Source: UniProtKB

   Cellular_componentNuRD complex

Inferred from direct assay Ref.3. Source: MGI

heterochromatin

Inferred from direct assay PubMed 17295837. Source: MGI

nucleus

Inferred by curator PubMed 21062744. Source: BHF-UCL

   Molecular_functionDNA binding

Inferred from direct assay PubMed 19168674. Source: MGI

RNA polymerase II transcription coactivator activity

Inferred from direct assay PubMed 21062744. Source: BHF-UCL

RNA polymerase II transcription factor binding

Inferred from physical interaction PubMed 21062744. Source: BHF-UCL

chromatin binding

Inferred from direct assay PubMed 20439720. Source: MGI

enhancer sequence-specific DNA binding

Inferred from direct assay PubMed 21062744. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.3. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13221322Sal-like protein 1
PRO_0000047021

Regions

Zinc finger450 – 47223C2H2-type 1
Zinc finger478 – 50023C2H2-type 2
Zinc finger705 – 72723C2H2-type 3
Zinc finger733 – 75523C2H2-type 4
Zinc finger765 – 78723C2H2-type 5
Zinc finger1000 – 102223C2H2-type 6
Zinc finger1028 – 105023C2H2-type 7
Zinc finger1133 – 115523C2H2-type 8
Zinc finger1161 – 118323C2H2-type 9
Compositional bias133 – 1397Poly-Thr
Compositional bias237 – 2404Poly-Gln
Compositional bias1143 – 11464Poly-Ser

Amino acid modifications

Modified residue5941Phosphoserine By similarity
Modified residue5961Phosphoserine By similarity
Modified residue9401Phosphoserine By similarity

Experimental info

Sequence conflict1651C → S Ref.2
Sequence conflict1671S → T Ref.2
Sequence conflict12711S → SS in BAB55673. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9ER74 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: DF4FEF7FEA0B9F5C

FASTA1,322140,230
        10         20         30         40         50         60 
MSRRKQAKPQ HFQSDPEVAS LPRRDGDTEK GQPSRPTKSK DAHVCGRCCA EFFELSDLLL 

        70         80         90        100        110        120 
HKKSCTKNQL VLIVNESPAS PAKTFPPGPS LNDPDDQMKD AANKADQEDC SDLSEPKGLD 

       130        140        150        160        170        180 
REESMEVEVP VATTTTTTTG GSGGSGGSTL SGVTNITTPS CHSGCSSGTS AITTSLPQLG 

       190        200        210        220        230        240 
DLTTLGNFSV INSNVIIENL QSTKVAVAQF SQEARCGGAS GGKLLISTLM EQLLALQQQQ 

       250        260        270        280        290        300 
IHQLQLIEQI RHQILLLASQ SADLPAAPSI PSQGTLRTSA NPLTTLSSHL SQQLAVAAGL 

       310        320        330        340        350        360 
AQSLASQSAN ISGVKQLPHV QLPQSSSGTS IVPPSGGTSP NMSIVTAAVP TPSSEKVASN 

       370        380        390        400        410        420 
AGASHVSSPA VSASSSPAFA ISSLLSPESN PLLPQPTPAN AVFPTPLPNI ATTAEDLNSL 

       430        440        450        460        470        480 
SALAQQRKSK PPNVTAFEAK STSDEAFFKH KCRFCAKVFG SDSALQIHLR SHTGERPFKC 

       490        500        510        520        530        540 
NICGNRFSTK GNLKVHFQRH KEKYPHIQMN PYPVPEHLDN VPTSTGIPYG MSIPSEKPVT 

       550        560        570        580        590        600 
SWLDTKPVLP TLTTSVGLPL PPTLPSLTPF IKTEEPAPIP ISHSAASPQG SVKSDSGAPD 

       610        620        630        640        650        660 
LATRNPSGVP EEVEGSAVPP FGGKGEESNM ASSAVPTAGN STLNSPVADG GPGGTTFTNP 

       670        680        690        700        710        720 
LLPLMSEQFK AKFPFGGLLD SAQASETSKL QQLVENIDKK ATDPNECIIC HRVLSCQSAL 

       730        740        750        760        770        780 
KMHYRTHTGE RPFKCKICGR AFTTKGNLKT HYSVHRAMPP LRVQHSCPIC QKKFTNAVVL 

       790        800        810        820        830        840 
QQHIRMHMGG QIPNTPVPDN YPESMESDTG SFDEKNFDDL DNFSDENMEE CPEGSIPDTP 

       850        860        870        880        890        900 
KSADASQDSL SSSPLPLEMS SIAALENQMK MINAGLAEQL QASLKSVENG SMEGDVLTND 

       910        920        930        940        950        960 
SSSVGGDMES QSAGSPAISE STSSMQALSP SNSTQEFHKS PGMEEKPQRV GPGEFANGLS 

       970        980        990       1000       1010       1020 
PTPVNGGALD LTSSHAEKII KEDSLGILFP FRDRGKFKNT ACDICGKTFA CQSALDIHYR 

      1030       1040       1050       1060       1070       1080 
SHTKERPFIC TVCNRGFSTK GNLKQHMLTH QMRDLPSQLF EPSSNLGPNQ NSAVIPANSL 

      1090       1100       1110       1120       1130       1140 
SSLIKTEVNG FVHVSPQDSK DAPTSHVPQG PLSSSATSPV LLPALPRRTP KQHYCNTCGK 

      1150       1160       1170       1180       1190       1200 
TFSSSSALQI HERTHTGEKP FACTICGRAF TTKGNLKVHM GTHMWNSTPA RRGRRLSVDG 

      1210       1220       1230       1240       1250       1260 
PMTFLGGNPV KFPEMFQKDL AARSGSGDPS SFWNQYTAAL SNGLAMKANE ISVIQNGGIP 

      1270       1280       1290       1300       1310       1320 
PIPGSLGSGS SPISGLTGNV EKLGNSEPSA PLAGLEKMAS SENGTNFRFT RFVEDSKEIV 


TS 

« Hide

References

[1]"Molecular cloning, chromosomal localization, and expression of the murine SALL1 ortholog Sall-1."
Buck A., Archangelo L., Dixkens C., Kohlhase J.
Cytogenet. Cell Genet. 89:150-153(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 129/Ola.
[2]"Murine homolog of SALL1 is essential for ureteric bud invasion in kidney development."
Nishinakamura R., Matsumoto Y., Nakao K., Nakamura K., Sato A., Copeland N.G., Gilbert D.J., Jenkins N.A., Scully S., Lacey D.L., Katsuki M., Asashima M., Yokota T.
Development 128:3105-3115(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Murine sall1 represses transcription by recruiting a histone deacetylase complex."
Kiefer S.M., McDill B.W., Yang J., Rauchman M.
J. Biol. Chem. 277:14869-14876(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ASSOCIATION WITH HDAC.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ271914, AJ271915 Genomic DNA. Translation: CAC09602.1.
AB051409 mRNA. Translation: BAB55673.1.
UniGeneMm.214361.

3D structure databases

ProteinModelPortalQ9ER74.
SMRQ9ER74. Positions 449-505, 707-787, 998-1183.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-54906N.
IntActQ9ER74. 6 interactions.
STRING10090.ENSMUSP00000034090.

PTM databases

PhosphoSiteQ9ER74.

Proteomic databases

PRIDEQ9ER74.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

MGIMGI:1889585. Sall1.

Phylogenomic databases

eggNOGNOG293478.
HOVERGENHBG058921.
InParanoidQ9ER74.
PhylomeDBQ9ER74.

Gene expression databases

CleanExMM_SALL1.
GenevestigatorQ9ER74.

Family and domain databases

Gene3D3.30.160.60. 9 hits.
InterProIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
SMARTSM00355. ZnF_C2H2. 9 hits.
[Graphical view]
PROSITEPS00028. ZINC_FINGER_C2H2_1. 9 hits.
PS50157. ZINC_FINGER_C2H2_2. 9 hits.
[Graphical view]
ProtoNetSearch...

Other

PROQ9ER74.
SOURCESearch...

Entry information

Entry nameSALL1_MOUSE
AccessionPrimary (citable) accession number: Q9ER74
Secondary accession number(s): Q920R5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: March 1, 2001
Last modified: June 11, 2014
This is version 101 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot