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Protein

Steroidogenic factor 1

Gene

Nr5a1

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

Functioni

Transcriptional activator. Seems to be essential for sexual differentiation and formation of the primary steroidogenic tissues. Binds to the Ad4 site found in the promoter region of steroidogenic P450 genes such as CYP11A, CYP11B and CYP21B. Also regulates the AMH/Muellerian inhibiting substance gene as well as the AHCH and STAR genes. 5'-YCAAGGYC-3' and 5'-RRAGGTCA-3' are the consensus sequences for the recognition by NR5A1. The SFPQ-NONO-NR5A1 complex binds to the CYP17 promoter and regulates basal and cAMP-dependent transcriptional avtivity (By similarity). Transcription repressor of the Moloney leukemia virus long terminal repeat in undifferentiated murine embryonal carcinoma cells. Binds phosphatidylcholine and phospholipids with a phosphatidylinositol (PI) headgroup, in particular phosphatidyl(3,4)bisphosphate, phosphatidyl(3,5)bisphosphate and phosphatidyl(3,4,5)triphosphate. Activated by the phosphorylation of NR5A1 by HIPK3 leading to increased steroidogenic gene expression upon cAMP signaling pathway stimulation.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei342 – 3421Lipid headgroup; via amide nitrogen1 Publication
Binding sitei437 – 4371Lipid headgroup1 Publication
Binding sitei441 – 4411Lipid headgroup1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi10 – 8576Nuclear receptorPROSITE-ProRule annotationAdd
BLAST
Zinc fingeri13 – 3321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri49 – 7325NR C4-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

GO - Biological processi

  • adrenal gland development Source: MGI
  • cell differentiation Source: MGI
  • hormone metabolic process Source: MGI
  • luteinization Source: MGI
  • maintenance of protein location in nucleus Source: MGI
  • male gonad development Source: MGI
  • multicellular organismal aging Source: MGI
  • negative regulation of female gonad development Source: UniProtKB
  • positive regulation of male gonad development Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: MGI
  • regulation of transcription, DNA-templated Source: MGI
  • regulation of transcription from RNA polymerase II promoter Source: MGI
  • reproductive process Source: MGI
  • tissue development Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Activator, Receptor, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Lipid-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiREACT_276696. Nuclear Receptor transcription pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Steroidogenic factor 1
Short name:
SF-1
Short name:
STF-1
Alternative name(s):
Adrenal 4-binding protein
Embryonal LTR-binding protein
Short name:
ELP
Embryonal long terminal repeat-binding protein
Fushi tarazu factor homolog 1
Nuclear receptor subfamily 5 group A member 1
Steroid hormone receptor Ad4BP
Steroid hydroxylase positive regulator
Gene namesi
Name:Nr5a1
Synonyms:Ftzf1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1346833. Nr5a1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: HGNC
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi270 – 2701A → W: Reduced lipid binding and transactivation. Abolishes ligand binding and reduces transactivation; when associated with F-345. 2 Publications
Mutagenesisi314 – 3141R → M: Strongly reduced transactivation. 1 Publication
Mutagenesisi345 – 3451L → F: Abolishes ligand binding and reduces transactivation; when associated with W-270. 2 Publications
Mutagenesisi345 – 3451L → W: Strongly reduced transactivation. 2 Publications
Mutagenesisi348 – 3481L → W: Strongly reduced transactivation. 1 Publication
Mutagenesisi349 – 3491V → W: Strongly reduced transactivation. 1 Publication
Mutagenesisi352 – 3521A → W: Strongly reduced transactivation. 1 Publication
Mutagenesisi434 – 4341A → W: Strongly reduced transactivation. 1 Publication
Mutagenesisi440 – 4401H → D: Strongly reduced transactivation; when associated with D-442.
Mutagenesisi441 – 4411K → E: Strongly reduced transactivation. 1 Publication
Mutagenesisi442 – 4421H → D: Strongly reduced transactivation; when associated with D-440.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 462462Steroidogenic factor 1PRO_0000053732Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki119 – 119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki194 – 194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Modified residuei203 – 2031Phosphoserine; by CDK7By similarity

Post-translational modificationi

Acetylation stimulates the transcriptional activity.By similarity
Sumoylation reduces CDK7-mediated phosophorylation on Ser-203.By similarity
Phosphorylated on Ser-203 by CDK7. This phosphorylation promotes transcriptional activity (By similarity).By similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiP33242.

PTM databases

PhosphoSiteiP33242.

Expressioni

Developmental stagei

Expressed during early embryonic development. Expressed only in undifferentiated embryonal carcinoma cells.

Gene expression databases

BgeeiP33242.
CleanExiMM_NR5A1.
ExpressionAtlasiP33242. baseline.
GenevisibleiP33242. MM.

Interactioni

Subunit structurei

Binds DNA as a monomer (By similarity). Part of a complex consisting of SFPQ, NONO and NR5A1. Interacts with DGKQ and CDK7 (By similarity). Interacts with NR0B2, NCOA2 and PPARGC1A. Binds to and activated by HIPK3.By similarity5 Publications

Protein-protein interaction databases

BioGridi204975. 10 interactions.
IntActiP33242. 1 interaction.
STRINGi10090.ENSMUSP00000028084.

Structurei

Secondary structure

1
462
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 163Combined sources
Beta strandi22 – 243Combined sources
Beta strandi27 – 293Combined sources
Helixi31 – 4111Combined sources
Turni42 – 443Combined sources
Helixi61 – 644Combined sources
Helixi66 – 7611Combined sources
Helixi80 – 823Combined sources
Turni94 – 974Combined sources
Helixi98 – 1069Combined sources
Beta strandi220 – 2223Combined sources
Helixi226 – 2349Combined sources
Helixi238 – 24912Combined sources
Beta strandi252 – 2543Combined sources
Turni255 – 2573Combined sources
Helixi263 – 28321Combined sources
Helixi287 – 2893Combined sources
Helixi292 – 31827Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi331 – 3333Combined sources
Helixi334 – 3407Combined sources
Helixi343 – 36119Combined sources
Helixi366 – 37712Combined sources
Helixi382 – 3843Combined sources
Helixi388 – 40922Combined sources
Turni411 – 4133Combined sources
Helixi416 – 44328Combined sources
Helixi452 – 4587Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YMTX-ray1.20A219-462[»]
1YP0X-ray1.50A223-461[»]
2FF0NMR-A10-111[»]
3F7DX-ray2.20A219-462[»]
ProteinModelPortaliP33242.
SMRiP33242. Positions 10-136, 237-461.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33242.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni263 – 34886Ligand-bindingAdd
BLAST

Sequence similaritiesi

Contains 1 nuclear receptor DNA-binding domain.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri13 – 3321NR C4-typePROSITE-ProRule annotationAdd
BLAST
Zinc fingeri49 – 7325NR C4-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG240365.
GeneTreeiENSGT00780000121906.
HOVERGENiHBG106677.
InParanoidiP33242.
KOiK08560.
OMAiLQEPAKG.
OrthoDBiEOG7BS4B9.
TreeFamiTF350737.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR016355. NR5_fam.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERiPTHR24086. PTHR24086. 1 hit.
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFiPIRSF002530. Nuc_orph_FTZ-F1. 1 hit.
PRINTSiPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 2 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P33242-1) [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

        10         20         30         40         50
MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT
60 70 80 90 100
ESQSCKIDKT QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK
110 120 130 140 150
RDRALKQQKK AQIRANGFKL ETGPPMGVPP PPPPPPDYML PPSLHAPEPK
160 170 180 190 200
ALVSGPPSGP LGDFGAPSLP MAVPGPHGPL AGYLYPAFSN RTIKSEYPEP
210 220 230 240 250
YASPPQQPGP PYSYPEPFSG GPNVPELILQ LLQLEPEEDQ VRARIVGCLQ
260 270 280 290 300
EPAKSRSDQP APFSLLCRMA DQTFISIVDW ARRCMVFKEL EVADQMTLLQ
310 320 330 340 350
NCWSELLVLD HIYRQVQYGK EDSILLVTGQ EVELSTVAVQ AGSLLHSLVL
360 370 380 390 400
RAQELVLQLH ALQLDRQEFV CLKFLILFSL DVKFLNNHSL VKDAQEKANA
410 420 430 440 450
ALLDYTLCHY PHCGDKFQQL LLCLVEVRAL SMQAKEYLYH KHLGNEMPRN
460
NLLIEMLQAK QT
Length:462
Mass (Da):52,077
Last modified:July 27, 2011 - v3
Checksum:i67045B563403CF5A
GO
Isoform 2 (identifier: P33242-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     333-462: ELSTVAVQAG...LIEMLQAKQT → TELVKPLVLH...GMVSGSSYRR

Show »
Length:388
Mass (Da):43,387
Checksum:iE9A38FD8427F5888
GO

Sequence cautioni

The sequence BAA01441.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti164 – 1641F → I in BAA01441 (PubMed:1545809).Curated
Sequence conflicti256 – 2561R → G in BAA01441 (PubMed:1545809).Curated
Sequence conflicti328 – 3281T → S in BAA01441 (PubMed:1545809).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti172 – 1721A → S in strain: C3H/HeJ and DBA/2J; does not change transcriptional activity. 1 Publication

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei333 – 462130ELSTV…QAKQT → TELVKPLVLHNPRPLRADSG HPKFQIQGHALARLLCVLGP FEEPQCGMVSGSSYRR in isoform 2. 1 PublicationVSP_003715Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10584 mRNA. Translation: BAA01441.1. Different initiation.
S65878
, S65875, S65919, S65876, S65877 Genomic DNA. Translation: AAB28338.1.
S65876, S65875, S65919 Genomic DNA. Translation: AAB28339.1.
AF511594 mRNA. Translation: AAM43952.1.
AK134378 mRNA. Translation: BAE22121.1.
AK144376 mRNA. Translation: BAE25855.1.
AL844842 Genomic DNA. Translation: CAM21930.1.
BC110476 mRNA. Translation: AAI10477.1.
BC110477 mRNA. Translation: AAI10478.1.
CCDSiCCDS16011.1. [P33242-1]
PIRiA40716.
A42128.
RefSeqiNP_620639.1. NM_139051.3. [P33242-1]
XP_006498125.1. XM_006498062.2. [P33242-1]
UniGeneiMm.31387.

Genome annotation databases

EnsembliENSMUST00000028084; ENSMUSP00000028084; ENSMUSG00000026751. [P33242-1]
ENSMUST00000112883; ENSMUSP00000108504; ENSMUSG00000026751. [P33242-1]
GeneIDi26423.
KEGGimmu:26423.
UCSCiuc008jnr.1. mouse. [P33242-1]
uc008jnt.1. mouse. [P33242-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D10584 mRNA. Translation: BAA01441.1. Different initiation.
S65878
, S65875, S65919, S65876, S65877 Genomic DNA. Translation: AAB28338.1.
S65876, S65875, S65919 Genomic DNA. Translation: AAB28339.1.
AF511594 mRNA. Translation: AAM43952.1.
AK134378 mRNA. Translation: BAE22121.1.
AK144376 mRNA. Translation: BAE25855.1.
AL844842 Genomic DNA. Translation: CAM21930.1.
BC110476 mRNA. Translation: AAI10477.1.
BC110477 mRNA. Translation: AAI10478.1.
CCDSiCCDS16011.1. [P33242-1]
PIRiA40716.
A42128.
RefSeqiNP_620639.1. NM_139051.3. [P33242-1]
XP_006498125.1. XM_006498062.2. [P33242-1]
UniGeneiMm.31387.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1YMTX-ray1.20A219-462[»]
1YP0X-ray1.50A223-461[»]
2FF0NMR-A10-111[»]
3F7DX-ray2.20A219-462[»]
ProteinModelPortaliP33242.
SMRiP33242. Positions 10-136, 237-461.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204975. 10 interactions.
IntActiP33242. 1 interaction.
STRINGi10090.ENSMUSP00000028084.

Chemistry

ChEMBLiCHEMBL1764943.

PTM databases

PhosphoSiteiP33242.

Proteomic databases

PRIDEiP33242.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000028084; ENSMUSP00000028084; ENSMUSG00000026751. [P33242-1]
ENSMUST00000112883; ENSMUSP00000108504; ENSMUSG00000026751. [P33242-1]
GeneIDi26423.
KEGGimmu:26423.
UCSCiuc008jnr.1. mouse. [P33242-1]
uc008jnt.1. mouse. [P33242-2]

Organism-specific databases

CTDi2516.
MGIiMGI:1346833. Nr5a1.

Phylogenomic databases

eggNOGiNOG240365.
GeneTreeiENSGT00780000121906.
HOVERGENiHBG106677.
InParanoidiP33242.
KOiK08560.
OMAiLQEPAKG.
OrthoDBiEOG7BS4B9.
TreeFamiTF350737.

Enzyme and pathway databases

ReactomeiREACT_276696. Nuclear Receptor transcription pathway.

Miscellaneous databases

EvolutionaryTraceiP33242.
NextBioi304449.
PROiP33242.
SOURCEiSearch...

Gene expression databases

BgeeiP33242.
CleanExiMM_NR5A1.
ExpressionAtlasiP33242. baseline.
GenevisibleiP33242. MM.

Family and domain databases

Gene3Di1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProiIPR016355. NR5_fam.
IPR008946. Nucl_hormone_rcpt_ligand-bd.
IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
IPR001723. Str_hrmn_rcpt.
IPR001628. Znf_hrmn_rcpt.
IPR013088. Znf_NHR/GATA.
[Graphical view]
PANTHERiPTHR24086. PTHR24086. 1 hit.
PfamiPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFiPIRSF002530. Nuc_orph_FTZ-F1. 1 hit.
PRINTSiPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTiSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMiSSF48508. SSF48508. 2 hits.
PROSITEiPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Embryonal long terminal repeat-binding protein is a murine homolog of FTZ-F1, a member of the steroid receptor superfamily."
    Tsukiyama T., Ueda H., Hirose S., Niwa O.
    Mol. Cell. Biol. 12:1286-1291(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Strain: DBA/2J.
  2. "Characterization of the mouse FTZ-F1 gene, which encodes a key regulator of steroid hydroxylase gene expression."
    Ikeda Y., Lala D.S., Luo X., Kim E., Moisan M.P., Parker K.L.
    Mol. Endocrinol. 7:852-860(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A polymorphic form of steroidogenic factor-1 is associated with adrenocorticotropin resistance in y1 mouse adrenocortical tumor cell mutants."
    Frigeri C., Tsao J., Cordova M., Schimmer B.P.
    Endocrinology 143:4031-4037(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-172.
    Strain: C57L/JxA/HeJF1.
  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] (ISOFORM 1).
    Strain: C57BL/6J.
    Tissue: Testis.
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  6. "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] (ISOFORM 1).
  7. "The orphan receptors NGFI-B and steroidogenic factor 1 establish monomer binding as a third paradigm of nuclear receptor-DNA interaction."
    Wilson T.E., Fahrner T.J., Milbrandt J.
    Mol. Cell. Biol. 13:5794-5804(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "Cyclic AMP stimulates SF-1-dependent CYP11A1 expression through homeodomain-interacting protein kinase 3-mediated Jun N-terminal kinase and c-Jun phosphorylation."
    Lan H.-C., Li H.-J., Lin G., Lai P.-Y., Chung B.-C.
    Mol. Cell. Biol. 27:2027-2036(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH HIPK3.
  9. Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) OF 219-462 IN COMPLEX WITH NR0B2 AND PHOSPHOLIPID, MUTAGENESIS OF ALA-270 AND ARG-314.
  10. "Crystallographic identification and functional characterization of phospholipids as ligands for the orphan nuclear receptor steroidogenic factor-1."
    Li Y., Choi M., Cavey G., Daugherty J., Suino K., Kovach A., Bingham N.C., Kliewer S.A., Xu H.E.
    Mol. Cell 17:491-502(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 223-461 IN COMPLEX WITH NR0B2 AND PHOSPHOLIPID, MUTAGENESIS OF LEU-345; LEU-348; VAL-349; ALA-352; ALA-434 AND LYS-441.
  11. "Structure of SF-1 bound by different phospholipids: evidence for regulatory ligands."
    Sablin E.P., Blind R.D., Krylova I.N., Ingraham J.G., Cai F., Williams J.D., Fletterick R.J., Ingraham H.A.
    Mol. Endocrinol. 23:25-34(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 219-462 IN COMPLEX WITH LIPID AND PPARGC1A, INTERACTION WITH NCOA2 AND PPARGC1A, FUNCTION, MUTAGENESIS OF ALA-270 AND LEU-345, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiSTF1_MOUSE
AccessioniPrimary (citable) accession number: P33242
Secondary accession number(s): Q812G5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: July 27, 2011
Last modified: June 24, 2015
This is version 142 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

External Data

Dasty 3

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 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.