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P33242

- STF1_MOUSE

UniProt

P33242 - STF1_MOUSE

Protein

Steroidogenic factor 1

Gene

Nr5a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 135 (01 Oct 2014)
      Sequence version 3 (27 Jul 2011)
      Previous versions | rss
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    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

    1. chromatin binding Source: MGI
    2. DNA binding Source: MGI
    3. double-stranded DNA binding Source: Ensembl
    4. phospholipid binding Source: Ensembl
    5. protein binding Source: MGI
    6. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
    7. sequence-specific DNA binding Source: Ensembl
    8. steroid hormone receptor activity Source: InterPro
    9. zinc ion binding Source: InterPro

    GO - Biological processi

    1. adrenal gland development Source: MGI
    2. cell differentiation Source: MGI
    3. hormone metabolic process Source: MGI
    4. luteinization Source: MGI
    5. maintenance of protein location in nucleus Source: MGI
    6. male gonad development Source: MGI
    7. multicellular organismal aging Source: MGI
    8. negative regulation of female gonad development Source: UniProtKB
    9. positive regulation of male gonad development Source: UniProtKB
    10. positive regulation of transcription, DNA-templated Source: UniProtKB
    11. positive regulation of transcription from RNA polymerase II promoter Source: MGI
    12. regulation of transcription, DNA-templated Source: MGI
    13. regulation of transcription from RNA polymerase II promoter Source: MGI
    14. reproductive process Source: MGI
    15. tissue development Source: MGI

    Keywords - Molecular functioni

    Activator, Receptor, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

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

    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: Chromosome 2

    Organism-specific databases

    MGIiMGI:1346833. Nr5a1.

    Subcellular locationi

    GO - Cellular componenti

    1. nucleus Source: HGNC

    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

    ArrayExpressiP33242.
    BgeeiP33242.
    CleanExiMM_NR5A1.
    GenevestigatoriP33242.

    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.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1YMTX-ray1.20A219-462[»]
    1YP0X-ray1.50A223-461[»]
    2FF0NMR-A10-111[»]
    3F7DX-ray2.20A219-462[»]
    ProteinModelPortaliP33242.
    SMRiP33242. Positions 9-461.
    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.
    GeneTreeiENSGT00750000117458.
    HOVERGENiHBG106677.
    InParanoidiQ812G5.
    KOiK08560.
    OMAiLQEPAKG.
    OrthoDBiEOG7BS4B9.
    TreeFamiTF350737.

    Family and domain databases

    Gene3Di1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProiIPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR016355. Steroidogenic_factor_1.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view]
    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. Align

    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

    MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT    50
    ESQSCKIDKT QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK 100
    RDRALKQQKK AQIRANGFKL ETGPPMGVPP PPPPPPDYML PPSLHAPEPK 150
    ALVSGPPSGP LGDFGAPSLP MAVPGPHGPL AGYLYPAFSN RTIKSEYPEP 200
    YASPPQQPGP PYSYPEPFSG GPNVPELILQ LLQLEPEEDQ VRARIVGCLQ 250
    EPAKSRSDQP APFSLLCRMA DQTFISIVDW ARRCMVFKEL EVADQMTLLQ 300
    NCWSELLVLD HIYRQVQYGK EDSILLVTGQ EVELSTVAVQ AGSLLHSLVL 350
    RAQELVLQLH ALQLDRQEFV CLKFLILFSL DVKFLNNHSL VKDAQEKANA 400
    ALLDYTLCHY PHCGDKFQQL LLCLVEVRAL SMQAKEYLYH KHLGNEMPRN 450
    NLLIEMLQAK QT 462
    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.

    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:
    EMBL
    GenBank
    DDBJ
    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_006498062.1. [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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS16011.1. [P33242-1 ]
    PIRi A40716.
    A42128.
    RefSeqi NP_620639.1. NM_139051.3. [P33242-1 ]
    XP_006498125.1. XM_006498062.1. [P33242-1 ]
    UniGenei Mm.31387.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1YMT X-ray 1.20 A 219-462 [» ]
    1YP0 X-ray 1.50 A 223-461 [» ]
    2FF0 NMR - A 10-111 [» ]
    3F7D X-ray 2.20 A 219-462 [» ]
    ProteinModelPortali P33242.
    SMRi P33242. Positions 9-461.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 204975. 10 interactions.

    Chemistry

    ChEMBLi CHEMBL1764943.

    PTM databases

    PhosphoSitei P33242.

    Proteomic databases

    PRIDEi P33242.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000028084 ; ENSMUSP00000028084 ; ENSMUSG00000026751 . [P33242-1 ]
    ENSMUST00000112883 ; ENSMUSP00000108504 ; ENSMUSG00000026751 . [P33242-1 ]
    GeneIDi 26423.
    KEGGi mmu:26423.
    UCSCi uc008jnr.1. mouse. [P33242-1 ]
    uc008jnt.1. mouse. [P33242-2 ]

    Organism-specific databases

    CTDi 2516.
    MGIi MGI:1346833. Nr5a1.

    Phylogenomic databases

    eggNOGi NOG240365.
    GeneTreei ENSGT00750000117458.
    HOVERGENi HBG106677.
    InParanoidi Q812G5.
    KOi K08560.
    OMAi LQEPAKG.
    OrthoDBi EOG7BS4B9.
    TreeFami TF350737.

    Miscellaneous databases

    EvolutionaryTracei P33242.
    NextBioi 304449.
    PROi P33242.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P33242.
    Bgeei P33242.
    CleanExi MM_NR5A1.
    Genevestigatori P33242.

    Family and domain databases

    Gene3Di 1.10.565.10. 1 hit.
    3.30.50.10. 1 hit.
    InterProi IPR008946. Nucl_hormone_rcpt_ligand-bd.
    IPR000536. Nucl_hrmn_rcpt_lig-bd_core.
    IPR016355. Steroidogenic_factor_1.
    IPR001723. Str_hrmn_rcpt.
    IPR001628. Znf_hrmn_rcpt.
    IPR013088. Znf_NHR/GATA.
    [Graphical view ]
    Pfami PF00104. Hormone_recep. 1 hit.
    PF00105. zf-C4. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF002530. Nuc_orph_FTZ-F1. 1 hit.
    PRINTSi PR00398. STRDHORMONER.
    PR00047. STROIDFINGER.
    SMARTi SM00430. HOLI. 1 hit.
    SM00399. ZnF_C4. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48508. SSF48508. 2 hits.
    PROSITEi PS00031. NUCLEAR_REC_DBD_1. 1 hit.
    PS51030. NUCLEAR_REC_DBD_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 135 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