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P42230

- STA5A_MOUSE

UniProt

P42230 - STA5A_MOUSE

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Protein

Signal transducer and activator of transcription 5A

Gene

Stat5a

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

Functioni

Carries out a dual function: signal transduction and activation of transcription. Mediates cellular responses to the cytokine KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the GAS element and activates PRL-induced transcription. Regulates the expression of milk proteins during lactation.2 Publications

GO - Molecular functioni

  1. calcium ion binding Source: InterPro
  2. DNA binding Source: MGI
  3. protein phosphatase binding Source: UniProtKB
  4. RNA polymerase II core promoter sequence-specific DNA binding Source: MGI
  5. sequence-specific DNA binding transcription factor activity Source: InterPro
  6. signal transducer activity Source: MGI

GO - Biological processi

  1. 2-oxoglutarate metabolic process Source: BHF-UCL
  2. allantoin metabolic process Source: BHF-UCL
  3. cellular response to granulocyte macrophage colony-stimulating factor stimulus Source: MGI
  4. citrate metabolic process Source: BHF-UCL
  5. creatine metabolic process Source: BHF-UCL
  6. creatinine metabolic process Source: BHF-UCL
  7. cytokine-mediated signaling pathway Source: MGI
  8. development of secondary female sexual characteristics Source: MGI
  9. development of secondary male sexual characteristics Source: MGI
  10. epithelial cell differentiation involved in prostate gland development Source: MGI
  11. fatty acid metabolic process Source: BHF-UCL
  12. female pregnancy Source: MGI
  13. isoleucine metabolic process Source: BHF-UCL
  14. JAK-STAT cascade Source: MGI
  15. JAK-STAT cascade involved in growth hormone signaling pathway Source: BHF-UCL
  16. lactation Source: MGI
  17. lipid storage Source: MGI
  18. luteinization Source: MGI
  19. mammary gland development Source: MGI
  20. mammary gland epithelium development Source: MGI
  21. natural killer cell differentiation Source: MGI
  22. negative regulation of apoptotic process Source: MGI
  23. negative regulation of erythrocyte differentiation Source: MGI
  24. negative regulation of mast cell apoptotic process Source: MGI
  25. oxaloacetate metabolic process Source: BHF-UCL
  26. peptidyl-tyrosine phosphorylation Source: MGI
  27. Peyer's patch development Source: MGI
  28. positive regulation of activated T cell proliferation Source: MGI
  29. positive regulation of B cell differentiation Source: MGI
  30. positive regulation of cell proliferation Source: MGI
  31. positive regulation of gamma-delta T cell differentiation Source: MGI
  32. positive regulation of inflammatory response Source: MGI
  33. positive regulation of interleukin-2 biosynthetic process Source: MGI
  34. positive regulation of lymphocyte differentiation Source: MGI
  35. positive regulation of mast cell differentiation Source: MGI
  36. positive regulation of mast cell proliferation Source: MGI
  37. positive regulation of mitotic cell cycle Source: MGI
  38. positive regulation of multicellular organism growth Source: MGI
  39. positive regulation of natural killer cell differentiation Source: MGI
  40. positive regulation of natural killer cell mediated cytotoxicity Source: MGI
  41. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  42. prolactin signaling pathway Source: UniProtKB
  43. prostate gland epithelium morphogenesis Source: MGI
  44. regulation of cell adhesion Source: MGI
  45. regulation of epithelial cell differentiation Source: MGI
  46. regulation of multicellular organism growth Source: BHF-UCL
  47. regulation of steroid metabolic process Source: MGI
  48. regulation of transcription from RNA polymerase II promoter Source: MGI
  49. response to peptide hormone Source: MGI
  50. succinate metabolic process Source: BHF-UCL
  51. taurine metabolic process Source: BHF-UCL
  52. T cell differentiation in thymus Source: MGI
  53. T cell homeostasis Source: MGI
  54. transcription, DNA-templated Source: UniProtKB-KW
  55. valine metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Lactation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_169390. Signaling by Leptin.
REACT_188529. Signaling by Leptin.
REACT_188578. Signaling by SCF-KIT.
REACT_196460. Signaling by FGFR1 fusion mutants.
REACT_198561. Prolactin receptor signaling.
REACT_198574. Nuclear signaling by ERBB4.
REACT_198614. Growth hormone receptor signaling.
REACT_198701. Interleukin-7 signaling.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_230639. Downstream signal transduction.
REACT_261365. Interleukin-2 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Signal transducer and activator of transcription 5A
Alternative name(s):
Mammary gland factor
Gene namesi
Name:Stat5a
Synonyms:Mgf, Mpf
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 11

Organism-specific databases

MGIiMGI:103036. Stat5a.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 Publication
Note: Translocated into the nucleus in response to phosphorylation.

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 793793Signal transducer and activator of transcription 5APRO_0000182424Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei128 – 1281PhosphoserineBy similarity
Modified residuei694 – 6941Phosphotyrosine; by JAK2By similarity

Post-translational modificationi

Tyrosine phosphorylated in response to IL2, IL3, IL7, IL15, KITLG/SCF, CSF2/GMCSF, GH1, PRL, EPO and THPO. Activated KIT promotes phosphorylation on tyrosine residues and subsequent translocation to the nucleus. Tyrosine phosphorylated in response to constitutively activated FGFR1, FGFR2, FGFR3 and FGFR4. Tyrosine phosphorylated in response to signaling via activated FLT3; wild-type FLT3 results in much weaker phosphorylation than constitutively activated mutant FLT3. Alternatively, can be phosphorylated by JAK2 at Tyr-694. Tyrosine phosphorylation is required for DNA-binding activity and dimerization. Serine phosphorylation is also required for maximal transcriptional activity. Dephosphorylation on tyrosine residues by PTPN2 negatively regulates prolactin signaling pathway (By similarity).By similarity
ISGylated.1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP42230.
PaxDbiP42230.
PRIDEiP42230.

PTM databases

PhosphoSiteiP42230.

Expressioni

Tissue specificityi

In the virgin, found in most tissues except brain and muscle. During lactation, abundantly found in mammary tissue, as well as in other secretory organs such as salivary gland and seminal vesicle.

Gene expression databases

BgeeiP42230.
ExpressionAtlasiP42230. baseline and differential.
GenevestigatoriP42230.

Interactioni

Subunit structurei

Forms a homodimer or a heterodimer with a related family member. Interacts with NCOA1 and SOCS7 (By similarity). Binds NR3C1. Interacts with ERBB4.By similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGAP2Q99490-22EBI-617434,EBI-7737644From a different organism.
GHRP199413EBI-617434,EBI-7526279From a different organism.

Protein-protein interaction databases

BioGridi203525. 13 interactions.
DIPiDIP-897N.
IntActiP42230. 7 interactions.
MINTiMINT-2576471.

Structurei

Secondary structure

1
793
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi144 – 18138Combined sources
Turni182 – 1909Combined sources
Turni196 – 1983Combined sources
Helixi199 – 24951Combined sources
Helixi251 – 26212Combined sources
Turni263 – 2653Combined sources
Helixi273 – 30028Combined sources
Helixi309 – 33022Combined sources
Beta strandi332 – 3365Combined sources
Beta strandi340 – 3456Combined sources
Beta strandi348 – 3558Combined sources
Turni356 – 3616Combined sources
Beta strandi368 – 3758Combined sources
Helixi376 – 3838Combined sources
Beta strandi404 – 4063Combined sources
Turni407 – 4104Combined sources
Beta strandi411 – 4133Combined sources
Beta strandi415 – 4195Combined sources
Helixi435 – 4373Combined sources
Beta strandi439 – 44911Combined sources
Beta strandi451 – 4544Combined sources
Beta strandi456 – 4627Combined sources
Beta strandi466 – 4694Combined sources
Helixi475 – 48814Combined sources
Beta strandi500 – 5034Combined sources
Helixi504 – 51916Combined sources
Helixi527 – 53812Combined sources
Helixi545 – 5506Combined sources
Beta strandi552 – 5543Combined sources
Helixi555 – 5595Combined sources
Beta strandi566 – 5694Combined sources
Helixi570 – 58415Combined sources
Helixi586 – 5916Combined sources
Helixi600 – 6089Combined sources
Beta strandi615 – 6206Combined sources
Beta strandi626 – 6316Combined sources
Beta strandi641 – 6466Combined sources
Helixi648 – 6536Combined sources
Helixi656 – 6627Combined sources
Helixi675 – 6795Combined sources
Turni680 – 6823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1Y1UX-ray3.21A/B/C128-712[»]
ProteinModelPortaliP42230.
SMRiP42230. Positions 138-690.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP42230.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini589 – 68698SH2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the transcription factor STAT family.Curated
Contains 1 SH2 domain.PROSITE-ProRule annotation

Keywords - Domaini

SH2 domain

Phylogenomic databases

eggNOGiNOG245085.
HOGENOMiHOG000230988.
HOVERGENiHBG107486.
InParanoidiP42230.
KOiK11223.
OrthoDBiEOG73JKTT.
TreeFamiTF318648.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.532.10. 1 hit.
1.20.1050.20. 1 hit.
2.60.40.630. 1 hit.
3.30.505.10. 1 hit.
InterProiIPR011992. EF-hand-dom_pair.
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR001217. STAT.
IPR013800. STAT_TF_alpha.
IPR015988. STAT_TF_coiled-coil.
IPR013801. STAT_TF_DNA-bd.
IPR012345. STAT_TF_DNA-bd_sub.
IPR013799. STAT_TF_prot_interaction.
[Graphical view]
PANTHERiPTHR11801. PTHR11801. 1 hit.
PfamiPF00017. SH2. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view]
SMARTiSM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view]
SUPFAMiSSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEiPS50001. SH2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P42230-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAGWIQAQQL QGDALRQMQV LYGQHFPIEV RHYLAQWIES QPWDAIDLDN
60 70 80 90 100
PQDRGQATQL LEGLVQELQK KAEHQVGEDG FLLKIKLGHY ATQLQNTYDR
110 120 130 140 150
CPMELVRCIR HILYNEQRLV REANNCSSPA GVLVDAMSQK HLQINQRFEE
160 170 180 190 200
LRLITQDTEN ELKKLQQTQE YFIIQYQESL RIQAQFAQLG QLNPQERMSR
210 220 230 240 250
ETALQQKQVS LETWLQREAQ TLQQYRVELA EKHQKTLQLL RKQQTIILDD
260 270 280 290 300
ELIQWKRRQQ LAGNGGPPEG SLDVLQSWCE KLAEIIWQNR QQIRRAEHLC
310 320 330 340 350
QQLPIPGPVE EMLAEVNATI TDIISALVTS TFIIEKQPPQ VLKTQTKFAA
360 370 380 390 400
TVRLLVGGKL NVHMNPPQVK ATIISEQQAK SLLKNENTRN ECSGEILNNC
410 420 430 440 450
CVMEYHQATG TLSAHFRNMS LKRIKRADRR GAESVTEEKF TVLFESQFSV
460 470 480 490 500
GSNELVFQVK TLSLPVVVIV HGSQDHNATA TVLWDNAFAE PGRVPFAVPD
510 520 530 540 550
KVLWPQLCEA LNMKFKAEVQ SNRGLTKENL VFLAQKLFNI SSNHLEDYNS
560 570 580 590 600
MSVSWSQFNR ENLPGWNYTF WQWFDGVMEV LKKHHKPHWN DGAILGFVNK
610 620 630 640 650
QQAHDLLINK PDGTFLLRFS DSEIGGITIA WKFDSPDRNL WNLKPFTTRD
660 670 680 690 700
FSIRSLADRL GDLNYLIYVF PDRPKDEVFA KYYTPVLAKA VDGYVKPQIK
710 720 730 740 750
QVVPEFVNAS TDAGASATYM DQAPSPVVCP QPHYNMYPPN PDPVLDQDGE
760 770 780 790
FDLDESMDVA RHVEELLRRP MDSLDARLSP PAGLFTSARS SLS
Length:793
Mass (Da):90,831
Last modified:November 1, 1995 - v1
Checksum:i7C66E435C37624DD
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48538 mRNA. Translation: CAA88419.1.
U21103 mRNA. Translation: AAA80590.1.
U36502 mRNA. Translation: AAA78945.1.
CCDSiCCDS25439.1.
PIRiS54772.
RefSeqiNP_035618.1. NM_011488.3.
XP_006532784.1. XM_006532721.1.
XP_006532785.1. XM_006532722.1.
UniGeneiMm.277403.

Genome annotation databases

EnsembliENSMUST00000004145; ENSMUSP00000004145; ENSMUSG00000004043.
ENSMUST00000107356; ENSMUSP00000102979; ENSMUSG00000004043.
GeneIDi20850.
KEGGimmu:20850.
UCSCiuc007lml.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z48538 mRNA. Translation: CAA88419.1 .
U21103 mRNA. Translation: AAA80590.1 .
U36502 mRNA. Translation: AAA78945.1 .
CCDSi CCDS25439.1.
PIRi S54772.
RefSeqi NP_035618.1. NM_011488.3.
XP_006532784.1. XM_006532721.1.
XP_006532785.1. XM_006532722.1.
UniGenei Mm.277403.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1Y1U X-ray 3.21 A/B/C 128-712 [» ]
ProteinModelPortali P42230.
SMRi P42230. Positions 138-690.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 203525. 13 interactions.
DIPi DIP-897N.
IntActi P42230. 7 interactions.
MINTi MINT-2576471.

Chemistry

ChEMBLi CHEMBL5513.

PTM databases

PhosphoSitei P42230.

Proteomic databases

MaxQBi P42230.
PaxDbi P42230.
PRIDEi P42230.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000004145 ; ENSMUSP00000004145 ; ENSMUSG00000004043 .
ENSMUST00000107356 ; ENSMUSP00000102979 ; ENSMUSG00000004043 .
GeneIDi 20850.
KEGGi mmu:20850.
UCSCi uc007lml.2. mouse.

Organism-specific databases

CTDi 6776.
MGIi MGI:103036. Stat5a.

Phylogenomic databases

eggNOGi NOG245085.
HOGENOMi HOG000230988.
HOVERGENi HBG107486.
InParanoidi P42230.
KOi K11223.
OrthoDBi EOG73JKTT.
TreeFami TF318648.

Enzyme and pathway databases

Reactomei REACT_169390. Signaling by Leptin.
REACT_188529. Signaling by Leptin.
REACT_188578. Signaling by SCF-KIT.
REACT_196460. Signaling by FGFR1 fusion mutants.
REACT_198561. Prolactin receptor signaling.
REACT_198574. Nuclear signaling by ERBB4.
REACT_198614. Growth hormone receptor signaling.
REACT_198701. Interleukin-7 signaling.
REACT_225836. Interleukin-3, 5 and GM-CSF signaling.
REACT_230639. Downstream signal transduction.
REACT_261365. Interleukin-2 signaling.

Miscellaneous databases

EvolutionaryTracei P42230.
NextBioi 299635.
PROi P42230.
SOURCEi Search...

Gene expression databases

Bgeei P42230.
ExpressionAtlasi P42230. baseline and differential.
Genevestigatori P42230.

Family and domain databases

Gene3Di 1.10.238.10. 1 hit.
1.10.532.10. 1 hit.
1.20.1050.20. 1 hit.
2.60.40.630. 1 hit.
3.30.505.10. 1 hit.
InterProi IPR011992. EF-hand-dom_pair.
IPR008967. p53-like_TF_DNA-bd.
IPR000980. SH2.
IPR001217. STAT.
IPR013800. STAT_TF_alpha.
IPR015988. STAT_TF_coiled-coil.
IPR013801. STAT_TF_DNA-bd.
IPR012345. STAT_TF_DNA-bd_sub.
IPR013799. STAT_TF_prot_interaction.
[Graphical view ]
PANTHERi PTHR11801. PTHR11801. 1 hit.
Pfami PF00017. SH2. 1 hit.
PF01017. STAT_alpha. 1 hit.
PF02864. STAT_bind. 1 hit.
PF02865. STAT_int. 1 hit.
[Graphical view ]
SMARTi SM00252. SH2. 1 hit.
SM00964. STAT_int. 1 hit.
[Graphical view ]
SUPFAMi SSF47655. SSF47655. 1 hit.
SSF48092. SSF48092. 1 hit.
SSF49417. SSF49417. 1 hit.
SSF55550. SSF55550. 1 hit.
PROSITEi PS50001. SH2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Interleukin-3, granulocyte-macrophage colony stimulating factor and interleukin-5 transduce signals through two STAT5 homologs."
    Mui A.L.-F., Wakao H., O'Farrell A.-M., Harada N., Miyajima A.
    EMBO J. 14:1166-1175(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6 X A/J.
    Tissue: Liver.
  2. "Cloning and expression of Stat5 and an additional homologue (Stat5b) involved in prolactin signal transduction in mouse mammary tissue."
    Liu X., Robinson G.W., Gouilleux F., Groner B., Hennighausen L.
    Proc. Natl. Acad. Sci. U.S.A. 92:8831-8835(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6.
  3. Zhou L.X., Moore R.C., Oka T.
    Submitted (SEP-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C3H/HeN.
    Tissue: Mammary gland.
  4. "Characterization of Stat5a and Stat5b homodimers and heterodimers and their association with the glucocortiocoid receptor in mammary cells."
    Cella N., Groner B., Hynes N.E.
    Mol. Cell. Biol. 18:1783-1792(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NR3C1.
  5. "ErbB4 signaling in the mammary gland is required for lobuloalveolar development and Stat5 activation during lactation."
    Jones F.E., Welte T., Fu X.Y., Stern D.F.
    J. Cell Biol. 147:77-88(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ERBB4.
  6. "Flt3 mutations from patients with acute myeloid leukemia induce transformation of 32D cells mediated by the Ras and STAT5 pathways."
    Mizuki M., Fenski R., Halfter H., Matsumura I., Schmidt R., Muller C., Gruning W., Kratz-Albers K., Serve S., Steur C., Buchner T., Kienast J., Kanakura Y., Berdel W.E., Serve H.
    Blood 96:3907-3914(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
  7. "The intracellular domain of ErbB4 induces differentiation of mammary epithelial cells."
    Muraoka-Cook R.S., Sandahl M., Husted C., Hunter D., Miraglia L., Feng S.M., Elenius K., Earp H.S. III
    Mol. Biol. Cell 17:4118-4129(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, SUBCELLULAR LOCATION, INTERACTION WITH ERBB4.
  8. "Mechanisms of STAT protein activation by oncogenic KIT mutants in neoplastic mast cells."
    Chaix A., Lopez S., Voisset E., Gros L., Dubreuil P., De Sepulveda P.
    J. Biol. Chem. 286:5956-5966(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION IN RESPONSE TO KIT SIGNALING.
  9. Cited for: PHOSPHORYLATION IN RESPONSE TO FLT3 SIGNALING.
  10. Cited for: ISGYLATION.
  11. Cited for: X-RAY CRYSTALLOGRAPHY (3.21 ANGSTROMS) OF 128-712.

Entry informationi

Entry nameiSTA5A_MOUSE
AccessioniPrimary (citable) accession number: P42230
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 26, 2014
This is version 150 of the entry and version 1 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