P33242 (STF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	Nr5a1
Synonyms:	Ftzf1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	462 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8 Ref.11
Subunit structure	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. Ref.7 Ref.8 Ref.11
Subcellular location	Nucleus.
Developmental stage	Expressed during early embryonic development. Expressed only in undifferentiated embryonal carcinoma cells.
Post-translational modification	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.
Sequence similarities	Belongs to the nuclear hormone receptor family. NR5 subfamily. Contains 1 nuclear receptor DNA-binding domain.
Sequence caution	The sequence BAA01441.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Zinc-finger
Ligand	DNA-binding Lipid-binding Metal-binding Zinc
Molecular function	Activator Receptor Repressor
PTM	Acetylation Isopeptide bond Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	adrenal gland development Inferred from mutant phenotype PubMed 11796523PubMed 16176945PubMed 21820362. Source: MGI cell differentiation Inferred from genetic interaction PubMed 15829514. Source: MGI hormone metabolic process Inferred from mutant phenotype PubMed 21820362. Source: MGI luteinization Inferred from mutant phenotype PubMed 15118069. Source: MGI maintenance of protein location in nucleus Inferred from direct assay PubMed 12610109. Source: MGI male gonad development Inferred from mutant phenotype PubMed 15118069PubMed 21820362. Source: MGI multicellular organismal aging Inferred from mutant phenotype PubMed 21820362. Source: MGI negative regulation of female gonad development Inferred from mutant phenotype PubMed 19301398. Source: UniProtKB positive regulation of male gonad development Inferred from mutant phenotype PubMed 19301398. Source: UniProtKB positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay PubMed 10446902PubMed 12732652PubMed 15590666. Source: MGI tissue development Inferred from mutant phenotype PubMed 16176945. Source: MGI
Cellular_component	nucleus Inferred from direct assay PubMed 10848616. Source: HGNC
Molecular_function	DNA binding Inferred from direct assay PubMed 12730328PubMed 14726490PubMed 15590666. Source: MGI RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from electronic annotation. Source: Compara chromatin binding Inferred from direct assay PubMed 16109736. Source: MGI double-stranded DNA binding Inferred from electronic annotation. Source: Compara phospholipid binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding Inferred from electronic annotation. Source: Compara steroid hormone receptor activity Inferred from electronic annotation. Source: InterPro zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P33242-1)

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.

Isoform 2 (identifier: P33242-2)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 462

462

Steroidogenic factor 1

PRO_0000053732

Regions

DNA binding

10 – 85

76

Nuclear receptor

Zinc finger

13 – 33

21

NR C4-type

Zinc finger

49 – 73

25

NR C4-type

Region

263 – 348

86

Ligand-binding

Sites

Binding site

342

1

Lipid headgroup; via amide nitrogen

Binding site

437

1

Lipid headgroup

Binding site

441

1

Lipid headgroup

Amino acid modifications

Modified residue

203

1

Phosphoserine; by CDK7 By similarity

Cross-link

119

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Cross-link

194

Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence

333 – 462

130

ELSTV…QAKQT → TELVKPLVLHNPRPLRADSG HPKFQIQGHALARLLCVLGP FEEPQCGMVSGSSYRR in isoform 2.

VSP_003715

Natural variant

172

1

A → S in strain: C3H/HeJ and DBA/2J; does not change transcriptional activity. Ref.3

Experimental info

Mutagenesis

270

1

A → W: Reduced lipid binding and transactivation. Abolishes ligand binding and reduces transactivation; when associated with F-345. Ref.9 Ref.11

Mutagenesis

314

1

R → M: Strongly reduced transactivation. Ref.9

Mutagenesis

345

1

L → F: Abolishes ligand binding and reduces transactivation; when associated with W-270. Ref.10 Ref.11

Mutagenesis

345

1

L → W: Strongly reduced transactivation. Ref.10 Ref.11

Mutagenesis

348

1

L → W: Strongly reduced transactivation. Ref.10

Mutagenesis

349

1

V → W: Strongly reduced transactivation. Ref.10

Mutagenesis

352

1

A → W: Strongly reduced transactivation. Ref.10

Mutagenesis

434

1

A → W: Strongly reduced transactivation. Ref.10

Mutagenesis

440

1

H → D: Strongly reduced transactivation; when associated with D-442.

Mutagenesis

441

1

K → E: Strongly reduced transactivation. Ref.10

Mutagenesis

442

1

H → D: Strongly reduced transactivation; when associated with D-440.

Sequence conflict

164

1

F → I in BAA01441. Ref.1

Sequence conflict

256

1

R → G in BAA01441. Ref.1

Sequence conflict

328

1

T → S in BAA01441. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

462

Helix Strand Turn

Details...

Beta strand

14 – 16

3

Beta strand

22 – 24

3

Beta strand

27 – 29

3

Helix

31 – 41

11

Turn

42 – 44

3

Helix

61 – 64

4

Helix

66 – 76

11

Helix

80 – 82

3

Turn

94 – 97

4

Helix

98 – 106

9

Beta strand

220 – 222

3

Helix

226 – 234

9

Helix

238 – 249

12

Beta strand

252 – 254

3

Turn

255 – 257

3

Helix

263 – 283

21

Helix

287 – 289

3

Helix

292 – 318

27

Beta strand

323 – 325

3

Beta strand

331 – 333

3

Helix

334 – 340

7

Helix

343 – 361

19

Helix

366 – 377

12

Helix

382 – 384

3

Helix

388 – 409

22

Turn

411 – 413

3

Helix

416 – 443

28

Helix

452 – 458

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 27, 2011. Version 3. Checksum: 67045B563403CF5A	FASTA	462	52,077
	10 20 30 40 50 60 MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT ESQSCKIDKT 70 80 90 100 110 120 QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK RDRALKQQKK AQIRANGFKL 130 140 150 160 170 180 ETGPPMGVPP PPPPPPDYML PPSLHAPEPK ALVSGPPSGP LGDFGAPSLP MAVPGPHGPL 190 200 210 220 230 240 AGYLYPAFSN RTIKSEYPEP YASPPQQPGP PYSYPEPFSG GPNVPELILQ LLQLEPEEDQ 250 260 270 280 290 300 VRARIVGCLQ EPAKSRSDQP APFSLLCRMA DQTFISIVDW ARRCMVFKEL EVADQMTLLQ 310 320 330 340 350 360 NCWSELLVLD HIYRQVQYGK EDSILLVTGQ EVELSTVAVQ AGSLLHSLVL RAQELVLQLH 370 380 390 400 410 420 ALQLDRQEFV CLKFLILFSL DVKFLNNHSL VKDAQEKANA ALLDYTLCHY PHCGDKFQQL 430 440 450 460 LLCLVEVRAL SMQAKEYLYH KHLGNEMPRN NLLIEMLQAK QT
	Isoform 2 [UniParc]. Checksum: E9A38FD8427F5888	FASTA	388	43,387
	10 20 30 40 50 60 MDYSYDEDLD ELCPVCGDKV SGYHYGLLTC ESCKGFFKRT VQNNKHYTCT ESQSCKIDKT 70 80 90 100 110 120 QRKRCPFCRF QKCLTVGMRL EAVRADRMRG GRNKFGPMYK RDRALKQQKK AQIRANGFKL 130 140 150 160 170 180 ETGPPMGVPP PPPPPPDYML PPSLHAPEPK ALVSGPPSGP LGDFGAPSLP MAVPGPHGPL 190 200 210 220 230 240 AGYLYPAFSN RTIKSEYPEP YASPPQQPGP PYSYPEPFSG GPNVPELILQ LLQLEPEEDQ 250 260 270 280 290 300 VRARIVGCLQ EPAKSRSDQP APFSLLCRMA DQTFISIVDW ARRCMVFKEL EVADQMTLLQ 310 320 330 340 350 360 NCWSELLVLD HIYRQVQYGK EDSILLVTGQ EVTELVKPLV LHNPRPLRAD SGHPKFQIQG 370 380 HALARLLCVL GPFEEPQCGM VSGSSYRR

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Lineage-specific biology revealed by a finished genome assembly of the mouse." Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P. PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract] 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]	"Structural analyses reveal phosphatidyl inositols as ligands for the NR5 orphan receptors SF-1 and LRH-1." Krylova I.N., Sablin E.P., Moore J., Xu R.X., Waitt G.M., MacKay J.A., Juzumiene D., Bynum J.M., Madauss K., Montana V., Lebedeva L., Suzawa M., Williams J.D., Williams S.P., Guy R.K., Thornton J.W., Fletterick R.J., Willson T.M., Ingraham H.A. Cell 120:343-355(2005) [PubMed] [Europe PMC] [Abstract] 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, MASS SPECTROMETRY, MUTAGENESIS OF ALA-270 AND LEU-345.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00107985.
IPI00330060.

PIR

A40716.
A42128.

RefSeq

NP_620639.1. NM_139051.3.

UniGene

Mm.31387.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P33242.

SMR

P33242. Positions 10-111, 237-461.

ModBase

Search...

PTM databases

PhosphoSite

P33242.

Proteomic databases

PRIDE

P33242.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000028084; ENSMUSP00000028084; ENSMUSG00000026751.
ENSMUST00000112883; ENSMUSP00000108504; ENSMUSG00000026751.

GeneID

26423.

KEGG

mmu:26423.

Organism-specific databases

CTD

2516.

MGI

MGI:1346833. Nr5a1.

Phylogenomic databases

eggNOG

NOG240365.

GeneTree

ENSGT00670000097927.

HOVERGEN

HBG106677.

InParanoid

Q812G5.

KO

K08560.

OMA

PFGLMCK.

OrthoDB

EOG4FJ891.

Gene expression databases

ArrayExpress

P33242.

Bgee

P33242.

CleanEx

MM_NR5A1.

Genevestigator

P33242.

GermOnline

ENSMUSG00000026751. Mus musculus.

Family and domain databases

Gene3D

1.10.565.10. 1 hit.
3.30.50.10. 1 hit.

InterPro

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]

Pfam

PF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]

PIRSF

PIRSF002530. Nuc_orph_FTZ-F1. 1 hit.

PRINTS

PR00398. STRDHORMONER.
PR00047. STROIDFINGER.

SMART

SM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]

SUPFAM

SSF48508. Str_ncl_receptor. 1 hit.

PROSITE

PS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

ChEMBL

CHEMBL1764943.

EvolutionaryTrace

P33242.

NextBio

304449.

SOURCE

Search...

Entry information

Entry name

STF1_MOUSE

Accession

Primary (citable) accession number: P33242
Secondary accession number(s): Q812G5

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	July 27, 2011
Last modified:	May 1, 2013
This is version 120 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program