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P33242 (STF1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 133. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length462 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainZinc-finger
   LigandDNA-binding
Lipid-binding
Metal-binding
Zinc
   Molecular functionActivator
Receptor
Repressor
   PTMAcetylation
Isopeptide bond
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processadrenal 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 15590666PubMed 21757499. Source: MGI

positive regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 19301398. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from direct assay PubMed 12861022. Source: MGI

regulation of transcription, DNA-templated

Inferred from direct assay PubMed 12651892. Source: MGI

reproductive process

Inferred from mutant phenotype PubMed 21820362. Source: MGI

tissue development

Inferred from mutant phenotype PubMed 16176945. Source: MGI

   Cellular_componentnucleus

Inferred from direct assay PubMed 10848616. Source: HGNC

   Molecular_functionDNA 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: Ensembl

chromatin binding

Inferred from direct assay PubMed 16109736. Source: MGI

double-stranded DNA binding

Inferred from electronic annotation. Source: Ensembl

phospholipid binding

Inferred from electronic annotation. Source: Ensembl

protein binding

Inferred from physical interaction PubMed 12651892PubMed 12730328PubMed 12732652. Source: MGI

sequence-specific DNA binding

Inferred from electronic annotation. Source: Ensembl

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 462462Steroidogenic factor 1
PRO_0000053732

Regions

DNA binding10 – 8576Nuclear receptor
Zinc finger13 – 3321NR C4-type
Zinc finger49 – 7325NR C4-type
Region263 – 34886Ligand-binding

Sites

Binding site3421Lipid headgroup; via amide nitrogen
Binding site4371Lipid headgroup
Binding site4411Lipid headgroup

Amino acid modifications

Modified residue2031Phosphoserine; by CDK7 By similarity
Cross-link119Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity
Cross-link194Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) By similarity

Natural variations

Alternative sequence333 – 462130ELSTV…QAKQT → TELVKPLVLHNPRPLRADSG HPKFQIQGHALARLLCVLGP FEEPQCGMVSGSSYRR in isoform 2.
VSP_003715
Natural variant1721A → S in strain: C3H/HeJ and DBA/2J; does not change transcriptional activity. Ref.3

Experimental info

Mutagenesis2701A → W: Reduced lipid binding and transactivation. Abolishes ligand binding and reduces transactivation; when associated with F-345. Ref.9 Ref.11
Mutagenesis3141R → M: Strongly reduced transactivation. Ref.9
Mutagenesis3451L → F: Abolishes ligand binding and reduces transactivation; when associated with W-270. Ref.10 Ref.11
Mutagenesis3451L → W: Strongly reduced transactivation. Ref.10 Ref.11
Mutagenesis3481L → W: Strongly reduced transactivation. Ref.10
Mutagenesis3491V → W: Strongly reduced transactivation. Ref.10
Mutagenesis3521A → W: Strongly reduced transactivation. Ref.10
Mutagenesis4341A → W: Strongly reduced transactivation. Ref.10
Mutagenesis4401H → D: Strongly reduced transactivation; when associated with D-442.
Mutagenesis4411K → E: Strongly reduced transactivation. Ref.10
Mutagenesis4421H → D: Strongly reduced transactivation; when associated with D-440.
Sequence conflict1641F → I in BAA01441. Ref.1
Sequence conflict2561R → G in BAA01441. Ref.1
Sequence conflict3281T → S in BAA01441. Ref.1

Secondary structure

..................................................... 462
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified July 27, 2011. Version 3.
Checksum: 67045B563403CF5A

FASTA46252,077
        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 

« Hide

Isoform 2 [UniParc].

Checksum: E9A38FD8427F5888
Show »

FASTA38843,387

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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, MUTAGENESIS OF ALA-270 AND LEU-345, IDENTIFICATION BY MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D10584 mRNA. Translation: BAA01441.1. Different initiation.
S65878 expand/collapse EMBL AC list , 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.
CCDSCCDS16011.1. [P33242-1]
PIRA40716.
A42128.
RefSeqNP_620639.1. NM_139051.3. [P33242-1]
XP_006498125.1. XM_006498062.1. [P33242-1]
UniGeneMm.31387.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1YMTX-ray1.20A219-462[»]
1YP0X-ray1.50A223-461[»]
2FF0NMR-A10-111[»]
3F7DX-ray2.20A219-462[»]
ProteinModelPortalP33242.
SMRP33242. Positions 9-461.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid204975. 10 interactions.

Chemistry

ChEMBLCHEMBL1764943.

PTM databases

PhosphoSiteP33242.

Proteomic databases

PRIDEP33242.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028084; ENSMUSP00000028084; ENSMUSG00000026751. [P33242-1]
ENSMUST00000112883; ENSMUSP00000108504; ENSMUSG00000026751. [P33242-1]
GeneID26423.
KEGGmmu:26423.
UCSCuc008jnr.1. mouse. [P33242-1]
uc008jnt.1. mouse. [P33242-2]

Organism-specific databases

CTD2516.
MGIMGI:1346833. Nr5a1.

Phylogenomic databases

eggNOGNOG240365.
GeneTreeENSGT00750000117458.
HOVERGENHBG106677.
InParanoidQ812G5.
KOK08560.
OMALQEPAKG.
OrthoDBEOG7BS4B9.
TreeFamTF350737.

Gene expression databases

ArrayExpressP33242.
BgeeP33242.
CleanExMM_NR5A1.
GenevestigatorP33242.

Family and domain databases

Gene3D1.10.565.10. 1 hit.
3.30.50.10. 1 hit.
InterProIPR008946. 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]
PfamPF00104. Hormone_recep. 1 hit.
PF00105. zf-C4. 1 hit.
[Graphical view]
PIRSFPIRSF002530. Nuc_orph_FTZ-F1. 1 hit.
PRINTSPR00398. STRDHORMONER.
PR00047. STROIDFINGER.
SMARTSM00430. HOLI. 1 hit.
SM00399. ZnF_C4. 1 hit.
[Graphical view]
SUPFAMSSF48508. SSF48508. 2 hits.
PROSITEPS00031. NUCLEAR_REC_DBD_1. 1 hit.
PS51030. NUCLEAR_REC_DBD_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33242.
NextBio304449.
PROP33242.
SOURCESearch...

Entry information

Entry nameSTF1_MOUSE
AccessionPrimary (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: July 9, 2014
This is version 133 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

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