UniProtKB - P17679 (GATA1_MOUSE)
Erythroid transcription factor
Gata1
Functioni
Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcription of genes involved in erythroid differentiation of K562 erythroleukemia cells, including HBB, HBG1/2, ALAS2 and HMBS (By similarity).
By similarity5 PublicationsRegions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 204 – 228 | GATA-type 1PROSITE-ProRule annotationAdd BLAST | 25 | |
Zinc fingeri | 258 – 282 | GATA-type 2PROSITE-ProRule annotationAdd BLAST | 25 |
GO - Molecular functioni
- C2H2 zinc finger domain binding Source: MGI
- chromatin binding Source: MGI
- chromatin DNA binding Source: UniProtKB
- cis-regulatory region sequence-specific DNA binding Source: UniProtKB
- DNA binding Source: MGI
- DNA-binding transcription activator activity, RNA polymerase II-specific Source: MGI
- DNA-binding transcription factor activity Source: MGI
- DNA-binding transcription factor activity, RNA polymerase II-specific Source: GO_Central
- p53 binding Source: MGI
- RNA polymerase II cis-regulatory region sequence-specific DNA binding Source: MGI
- RNA polymerase II-specific DNA-binding transcription factor binding Source: BHF-UCL
- RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: MGI
- sequence-specific DNA binding Source: MGI
- sequence-specific double-stranded DNA binding Source: MGI
- transcription cis-regulatory region binding Source: MGI
- transcription coactivator binding Source: BHF-UCL
- transcription coregulator binding Source: BHF-UCL
- zinc ion binding Source: InterPro
GO - Biological processi
- animal organ regeneration Source: MGI
- basophil differentiation Source: Ensembl
- cell-cell signaling Source: MGI
- cell development Source: MGI
- cell fate commitment Source: GO_Central
- cellular response to cAMP Source: Ensembl
- cellular response to follicle-stimulating hormone stimulus Source: Ensembl
- cellular response to lipopolysaccharide Source: MGI
- cellular response to thyroid hormone stimulus Source: MGI
- dendritic cell differentiation Source: MGI
- embryonic hemopoiesis Source: MGI
- eosinophil fate commitment Source: MGI
- erythrocyte development Source: MGI
- erythrocyte differentiation Source: MGI
- homeostasis of number of cells within a tissue Source: MGI
- in utero embryonic development Source: MGI
- male gonad development Source: MGI
- megakaryocyte differentiation Source: MGI
- myeloid cell differentiation Source: MGI
- negative regulation of apoptotic process Source: MGI
- negative regulation of bone mineralization Source: MGI
- negative regulation of cell population proliferation Source: MGI
- negative regulation of extrinsic apoptotic signaling pathway in absence of ligand Source: MGI
- negative regulation of transcription by RNA polymerase II Source: MGI
- negative regulation of transcription regulatory region DNA binding Source: MGI
- platelet aggregation Source: BHF-UCL
- platelet formation Source: MGI
- positive regulation of cytosolic calcium ion concentration Source: MGI
- positive regulation of erythrocyte differentiation Source: MGI
- positive regulation of mast cell degranulation Source: MGI
- positive regulation of osteoblast proliferation Source: MGI
- positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
- positive regulation of transcription, DNA-templated Source: UniProtKB
- positive regulation of transcription by RNA polymerase II Source: BHF-UCL
- regulation of definitive erythrocyte differentiation Source: BHF-UCL
- regulation of glycoprotein biosynthetic process Source: BHF-UCL
- regulation of primitive erythrocyte differentiation Source: MGI
- Sertoli cell development Source: Ensembl
Keywordsi
Molecular function | Activator, DNA-binding, Repressor |
Biological process | Transcription, Transcription regulation |
Ligand | Metal-binding, Zinc |
Enzyme and pathway databases
Reactomei | R-MMU-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-MMU-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs R-MMU-983231, Factors involved in megakaryocyte development and platelet production |
Names & Taxonomyi
Protein namesi | Recommended name: Erythroid transcription factorAlternative name(s): Eryf1 GATA-binding factor 1 Short name: GATA-1 Short name: GF-1 NF-E1 DNA-binding protein |
Gene namesi | Name:Gata1 Synonyms:Gf-1 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:95661, Gata1 |
VEuPathDBi | HostDB:ENSMUSG00000031162 |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Nucleus
- nucleoplasm Source: MGI
- nucleus Source: MGI
Other locations
- protein-DNA complex Source: MGI
- transcription regulator complex Source: MGI
- transcription repressor complex Source: MGI
Keywords - Cellular componenti
NucleusPathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 26 | S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication | 1 | |
Mutagenesisi | 49 | S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication | 1 | |
Mutagenesisi | 72 | S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication | 1 | |
Mutagenesisi | 137 | K → R: Abolishes sumoylation. No change in PIAS4 binding nor on transcriptional activity. 1 Publication | 1 | |
Mutagenesisi | 142 | S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication | 1 | |
Mutagenesisi | 178 | S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication | 1 | |
Mutagenesisi | 187 | S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication | 1 | |
Mutagenesisi | 203 | E → V: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication | 1 | |
Mutagenesisi | 204 | C → R: Disrupts interaction with ZFPM1 and binding to DNA. 1 Publication | 1 | |
Mutagenesisi | 205 | V → G: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication | 1 | |
Mutagenesisi | 205 | V → M: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication | 1 | |
Mutagenesisi | 207 | C → G, R or W: Disrupts interaction with ZFPM1. 2 Publications | 1 | |
Mutagenesisi | 207 | C → P: Stability of binding to DNA reduced. 2 Publications | 1 | |
Mutagenesisi | 208 | G → E or V: Disrupts interaction with ZFPM1 and binding to DNA. 1 Publication | 1 | |
Mutagenesisi | 218 | D → G or V: No effect on interaction with ZFPM1. 1 Publication | 1 | |
Mutagenesisi | 222 | H → R: Disrupts interaction with ZFPM1. Binds normally to DNA. 1 Publication | 1 | |
Mutagenesisi | 224 | L → P: Disrupts interaction with ZFPM1 and binding to DNA. 1 Publication | 1 | |
Mutagenesisi | 225 | C → R, S or Y: Disrupts interaction with ZFPM1. 1 Publication | 1 | |
Mutagenesisi | 228 | C → R or S: Disrupts interaction with ZFPM1. 1 Publication | 1 | |
Mutagenesisi | 230 | L → F: Stability of binding to DNA reduced. 1 Publication | 1 | |
Mutagenesisi | 233 | K → E: No effect on interaction with ZFPM1. 1 Publication | 1 | |
Mutagenesisi | 245 – 246 | KK → AA: No effect on DNA binding. Reduces acetylation. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 312-A--A-316. Abrogates ability to induce erythroid differentiation; when associated with 312-A--A-316. Reduces binding to CREBBP; when associated with 312-A--A-316. Disrupts stable association with chromatin; when associated with 312-A--A-316. 2 Publications | 2 | |
Mutagenesisi | 245 – 246 | KK → RR: No effect on DNA binding. 2 Publications | 2 | |
Mutagenesisi | 261 | C → P: Abolishes DNA-binding. 1 Publication | 1 | |
Mutagenesisi | 284 | L → F: Binds to DNA with reduced affinity. 1 Publication | 1 | |
Mutagenesisi | 310 | S → A: Loss of phosphorylation of the chymotryptic peptide. 1 Publication | 1 | |
Mutagenesisi | 312 – 316 | KGKKK → AGAAA: No effect on DNA binding. Reduces acetylation. Reduces binding to CREBBP. Reduces ability to induce erythroid differentiation. Abrogates acetylation; when associated with 245-A-A-246. Abrogates ability to induce erythroid differentiation; when associated with 245-A-A-246. Reduces binding to CREBBP; when associated with 245-A-A-246. Disrupts stable association with chromatin; when associated with 245-A-A-246. 2 Publications | 5 | |
Mutagenesisi | 312 – 316 | KGKKK → RGRRR: No effect on DNA binding. 2 Publications | 5 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000083398 | 1 – 413 | Erythroid transcription factorAdd BLAST | 413 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 26 | Phosphoserine1 Publication | 1 | |
Modified residuei | 49 | Phosphoserine1 Publication | 1 | |
Modified residuei | 72 | Phosphoserine1 Publication | 1 | |
Cross-linki | 137 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication | ||
Modified residuei | 142 | Phosphoserine1 Publication | 1 | |
Modified residuei | 178 | Phosphoserine1 Publication | 1 | |
Modified residuei | 187 | Phosphoserine1 Publication | 1 | |
Modified residuei | 233 | N6-acetyllysine; by EP300By similarity | 1 | |
Modified residuei | 245 | N6-acetyllysine; by EP300By similarity | 1 | |
Modified residuei | 246 | N6-acetyllysine; by CREBBP1 Publication | 1 | |
Modified residuei | 246 | N6-acetyllysine; by EP300By similarity | 1 | |
Modified residuei | 252 | N6-acetyllysine; by CREBBP1 Publication | 1 | |
Modified residuei | 308 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 310 | Phosphoserine1 Publication | 1 | |
Modified residuei | 312 | N6-acetyllysine; by CREBBP2 Publications | 1 | |
Modified residuei | 314 | N6-acetyllysine1 Publication | 1 | |
Modified residuei | 315 | N6-acetyllysine1 Publication | 1 |
Post-translational modificationi
Keywords - PTMi
Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | P17679 |
PRIDEi | P17679 |
ProteomicsDBi | 267766 [P17679-1] 267767 [P17679-2] |
PTM databases
iPTMneti | P17679 |
PhosphoSitePlusi | P17679 |
Expressioni
Tissue specificityi
Developmental stagei
Gene expression databases
Bgeei | ENSMUSG00000031162, Expressed in bone marrow and 153 other tissues |
ExpressionAtlasi | P17679, baseline and differential |
Genevisiblei | P17679, MM |
Interactioni
Subunit structurei
May form homodimers or heterodimers with other isoforms.
Interacts (via the N-terminal zinc finger) with ZFPM1 (By similarity).
Interacts with GFI1B.
Interacts with PIAS4; the interaction enhances sumoylation and represses the transactivational activity in a sumoylation-independent manner.
Interacts with LMCD1.
Interacts with CREBBP; the interaction stimulates acetylation and transcriptional activity in vivo.
Interacts with BRD3.
Interacts with MED1, CCAR1 and CALCOCO1.
Interacts with EP300 (By similarity).
Interacts with CEBPE (By similarity).
By similarity8 PublicationsBinary interactionsi
P17679
GO - Molecular functioni
- C2H2 zinc finger domain binding Source: MGI
- p53 binding Source: MGI
- RNA polymerase II-specific DNA-binding transcription factor binding Source: BHF-UCL
- transcription coactivator binding Source: BHF-UCL
- transcription coregulator binding Source: BHF-UCL
Protein-protein interaction databases
BioGRIDi | 199838, 23 interactors |
CORUMi | P17679 |
DIPi | DIP-40883N |
IntActi | P17679, 10 interactors |
MINTi | P17679 |
STRINGi | 10090.ENSMUSP00000033502 |
Miscellaneous databases
RNActi | P17679, protein |
Structurei
Secondary structure
3D structure databases
SMRi | P17679 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P17679 |
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 29 – 49 | DisorderedSequence analysisAdd BLAST | 21 | |
Regioni | 200 – 330 | Interaction with MED1 and CCAR11 PublicationAdd BLAST | 131 | |
Regioni | 203 – 222 | Required for interaction with ZFPM1By similarityAdd BLAST | 20 | |
Regioni | 249 – 315 | Interaction with CALCOCO11 PublicationAdd BLAST | 67 | |
Regioni | 297 – 325 | DisorderedSequence analysisAdd BLAST | 29 | |
Regioni | 391 – 413 | DisorderedSequence analysisAdd BLAST | 23 |
Domaini
Zinc finger
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Zinc fingeri | 204 – 228 | GATA-type 1PROSITE-ProRule annotationAdd BLAST | 25 | |
Zinc fingeri | 258 – 282 | GATA-type 2PROSITE-ProRule annotationAdd BLAST | 25 |
Keywords - Domaini
Repeat, Zinc-fingerPhylogenomic databases
eggNOGi | KOG1601, Eukaryota |
GeneTreei | ENSGT00940000161156 |
HOGENOMi | CLU_027524_1_1_1 |
InParanoidi | P17679 |
OMAi | YSKTGLY |
OrthoDBi | 807790at2759 |
PhylomeDBi | P17679 |
TreeFami | TF315391 |
Family and domain databases
CDDi | cd00202, ZnF_GATA, 2 hits |
Gene3Di | 3.30.50.10, 2 hits |
IDEALi | IID50040 |
InterProi | View protein in InterPro IPR029524, GATA-1 IPR039355, Transcription_factor_GATA IPR000679, Znf_GATA IPR013088, Znf_NHR/GATA |
PANTHERi | PTHR10071, PTHR10071, 1 hit PTHR10071:SF190, PTHR10071:SF190, 1 hit |
Pfami | View protein in Pfam PF00320, GATA, 2 hits |
PRINTSi | PR00619, GATAZNFINGER |
SMARTi | View protein in SMART SM00401, ZnF_GATA, 2 hits |
PROSITEi | View protein in PROSITE PS00344, GATA_ZN_FINGER_1, 2 hits PS50114, GATA_ZN_FINGER_2, 2 hits |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative initiation. AlignAdd to basketThis entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All
This isoform has been chosen as the sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
10 20 30 40 50
MDFPGLGALG TSEPLPQFVD SALVSSPSDS TGFFSSGPEG LDAASSSTSP
60 70 80 90 100
NAATAAASAL AYYREAEAYR HSPVFQVYPL LNSMEGIPGG SPYASWAYGK
110 120 130 140 150
TALYPASTVC PSHEDAPSQA LEDQEGKSNN TFLDTLKTER LSPDLLTLGT
160 170 180 190 200
ALPASLPVTG SAYGGADFPS PFFSPTGSPL SSAAYSSPKF HGSLPLAPCE
210 220 230 240 250
ARECVNCGAT ATPLWRRDRT GHYLCNACGL YHKMNGQNRP LIRPKKRMIV
260 270 280 290 300
SKRAGTQCTN CQTTTTTLWR RNASGDPVCN ACGLYFKLHQ VNRPLTMRKD
310 320 330 340 350
GIQTRNRKAS GKGKKKRGSN LAGAGAAEGP AGGFMVVAGS SSSGNCGEVA
360 370 380 390 400
SGLALGTAGT AHLYQGLGPV VLSGPVSHLM PFPGPLLGSP TTSFPTGPAP
410
TTSSTSVIAP LSS
The sequence of this isoform differs from the canonical sequence as follows:
1-83: Missing.
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketB1AUB4 | B1AUB4_MOUSE | Erythroid transcription factor | Gata1 | 124 | Annotation score: | ||
B1AUB3 | B1AUB3_MOUSE | Erythroid transcription factor | Gata1 | 109 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 29 | D → G in AAH52653 (PubMed:15489334).Curated | 1 | |
Sequence conflicti | 129 | N → S in AAH52653 (PubMed:15489334).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_041452 | 1 – 83 | Missing in isoform 2. CuratedAdd BLAST | 83 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X15763 mRNA Translation: CAA33769.1 AK146915 mRNA Translation: BAE27527.1 AL670169 Genomic DNA No translation available. CH466638 Genomic DNA Translation: EDL33938.1 X57530 Genomic DNA Translation: CAA40751.1 BC052653 mRNA Translation: AAH52653.1 |
CCDSi | CCDS29981.1 [P17679-1] |
PIRi | S04655 |
RefSeqi | NP_032115.1, NM_008089.2 [P17679-1] XP_011245750.1, XM_011247448.2 [P17679-1] |
Genome annotation databases
Ensembli | ENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162 [P17679-1] |
GeneIDi | 14460 |
KEGGi | mmu:14460 |
UCSCi | uc009snl.2, mouse [P17679-1] |
Keywords - Coding sequence diversityi
Alternative initiationSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | X15763 mRNA Translation: CAA33769.1 AK146915 mRNA Translation: BAE27527.1 AL670169 Genomic DNA No translation available. CH466638 Genomic DNA Translation: EDL33938.1 X57530 Genomic DNA Translation: CAA40751.1 BC052653 mRNA Translation: AAH52653.1 |
CCDSi | CCDS29981.1 [P17679-1] |
PIRi | S04655 |
RefSeqi | NP_032115.1, NM_008089.2 [P17679-1] XP_011245750.1, XM_011247448.2 [P17679-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1GNF | NMR | - | A | 200-243 | [»] | |
1Y0J | NMR | - | A | 200-243 | [»] | |
2L5E | NMR | - | B | 308-320 | [»] | |
2L6Y | NMR | - | A | 200-238 | [»] | |
2L6Z | NMR | - | A | 200-238 | [»] | |
3VD6 | X-ray | 1.98 | C | 200-318 | [»] | |
3VEK | X-ray | 2.63 | C/F | 200-318 | [»] | |
SMRi | P17679 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 199838, 23 interactors |
CORUMi | P17679 |
DIPi | DIP-40883N |
IntActi | P17679, 10 interactors |
MINTi | P17679 |
STRINGi | 10090.ENSMUSP00000033502 |
PTM databases
iPTMneti | P17679 |
PhosphoSitePlusi | P17679 |
Proteomic databases
PaxDbi | P17679 |
PRIDEi | P17679 |
ProteomicsDBi | 267766 [P17679-1] 267767 [P17679-2] |
Protocols and materials databases
ABCDi | P17679, 35 sequenced antibodies |
Antibodypediai | 372, 982 antibodies from 47 providers |
DNASUi | 14460 |
Genome annotation databases
Ensembli | ENSMUST00000033502; ENSMUSP00000033502; ENSMUSG00000031162 [P17679-1] |
GeneIDi | 14460 |
KEGGi | mmu:14460 |
UCSCi | uc009snl.2, mouse [P17679-1] |
Organism-specific databases
CTDi | 2623 |
MGIi | MGI:95661, Gata1 |
VEuPathDBi | HostDB:ENSMUSG00000031162 |
Phylogenomic databases
eggNOGi | KOG1601, Eukaryota |
GeneTreei | ENSGT00940000161156 |
HOGENOMi | CLU_027524_1_1_1 |
InParanoidi | P17679 |
OMAi | YSKTGLY |
OrthoDBi | 807790at2759 |
PhylomeDBi | P17679 |
TreeFami | TF315391 |
Enzyme and pathway databases
Reactomei | R-MMU-8936459, RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function R-MMU-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs R-MMU-983231, Factors involved in megakaryocyte development and platelet production |
Miscellaneous databases
BioGRID-ORCSi | 14460, 1 hit in 64 CRISPR screens |
ChiTaRSi | Gata1, mouse |
EvolutionaryTracei | P17679 |
PROi | PR:P17679 |
RNActi | P17679, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000031162, Expressed in bone marrow and 153 other tissues |
ExpressionAtlasi | P17679, baseline and differential |
Genevisiblei | P17679, MM |
Family and domain databases
CDDi | cd00202, ZnF_GATA, 2 hits |
Gene3Di | 3.30.50.10, 2 hits |
IDEALi | IID50040 |
InterProi | View protein in InterPro IPR029524, GATA-1 IPR039355, Transcription_factor_GATA IPR000679, Znf_GATA IPR013088, Znf_NHR/GATA |
PANTHERi | PTHR10071, PTHR10071, 1 hit PTHR10071:SF190, PTHR10071:SF190, 1 hit |
Pfami | View protein in Pfam PF00320, GATA, 2 hits |
PRINTSi | PR00619, GATAZNFINGER |
SMARTi | View protein in SMART SM00401, ZnF_GATA, 2 hits |
PROSITEi | View protein in PROSITE PS00344, GATA_ZN_FINGER_1, 2 hits PS50114, GATA_ZN_FINGER_2, 2 hits |
MobiDBi | Search... |
Entry informationi
Entry namei | GATA1_MOUSE | |
Accessioni | P17679Primary (citable) accession number: P17679 Secondary accession number(s): Q3UIH9, Q7TMX8 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | August 1, 1990 |
Last sequence update: | August 1, 1990 | |
Last modified: | February 23, 2022 | |
This is version 198 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references