Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q9Y5Q3

- MAFB_HUMAN

UniProt

Q9Y5Q3 - MAFB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Transcription factor MafB

Gene

MAFB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Acts as a transcriptional activator or repressor. Plays a pivotal role in regulating lineage-specific hematopoiesis by repressing ETS1-mediated transcription of erythroid-specific genes in myeloid cells. Required for monocytic, macrophage, podocyte and islet beta cell differentiation. Involved in renal tubule survival and F4/80 maturation. Activates the insulin and glucagon promoters. Together with PAX6, transactivates weakly the glucagon gene promoter through the G1 element. SUMO modification controls its transcriptional activity and ability to specify macrophage fate. Binds element G1 on the glucagon promoter (By similarity). Involved either as an oncogene or as a tumor suppressor, depending on the cell context.By similarity1 Publication

GO - Molecular functioni

  1. sequence-specific DNA binding Source: InterPro
  2. sequence-specific DNA binding transcription factor activity Source: InterPro
  3. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. brain segmentation Source: Ensembl
  2. inner ear morphogenesis Source: Ensembl
  3. negative regulation of erythrocyte differentiation Source: UniProtKB
  4. positive regulation of transcription from RNA polymerase II promoter Source: Ensembl
  5. respiratory gaseous exchange Source: Ensembl
  6. rhombomere 5 development Source: Ensembl
  7. rhombomere 6 development Source: Ensembl
  8. segment specification Source: Ensembl
  9. sensory organ development Source: ProtInc
  10. T cell differentiation in thymus Source: Ensembl
  11. thymus development Source: Ensembl
  12. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription factor MafB
Short name:
Maf-B
Alternative name(s):
V-maf musculoaponeurotic fibrosarcoma oncogene homolog B
Gene namesi
Name:MAFB
Synonyms:KRML
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 20

Organism-specific databases

HGNCiHGNC:6408. MAFB.

Subcellular locationi

Nucleus PROSITE-ProRule annotation

GO - Cellular componenti

  1. nucleus Source: ProtInc
  2. transcription factor complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Multicentric carpotarsal osteolysis syndrome (MCTO) [MIM:166300]: A rare skeletal disorder, usually presenting in early childhood with a clinical picture mimicking juvenile rheumatoid arthritis. Progressive destruction of the carpal and tarsal bone usually occurs and other bones may also be involved. Chronic renal failure is a frequent component of the syndrome. Mental retardation and minor facial anomalies have been noted in some patients.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541S → L in MCTO. 1 Publication
VAR_067979
Natural varianti59 – 591P → L in MCTO. 1 Publication
VAR_067980
Natural varianti62 – 621T → P in MCTO. 1 Publication
VAR_067981
Natural varianti63 – 631P → R in MCTO. 1 Publication
VAR_067982
Natural varianti66 – 661S → C in MCTO. 1 Publication
VAR_067983
Natural varianti69 – 691S → L in MCTO. 1 Publication
VAR_067984
Natural varianti70 – 701S → A in MCTO. 1 Publication
VAR_067985
Natural varianti70 – 701S → L in MCTO. 1 Publication
VAR_067986
Natural varianti71 – 711P → L in MCTO. 1 Publication
VAR_067987
Natural varianti71 – 711P → S in MCTO. 1 Publication
VAR_067988

Keywords - Diseasei

Disease mutation, Proto-oncogene, Tumor suppressor

Organism-specific databases

MIMi166300. phenotype.
Orphaneti2774. Multicentric carpo-tarsal osteolysis with or without nephropathy.
PharmGKBiPA30535.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 323323Transcription factor MafBPRO_0000076494Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki32 – 32Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity
Cross-linki297 – 297Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)By similarity

Post-translational modificationi

Phosphorylated by GSK3 and MAPK13 on serine and threonine residues.2 Publications
Sumoylated. Sumoylation on Lys-32 and Lys-297 stimulates its transcriptional repression activity and promotes macrophage differentiation from myeloid progenitors (By similarity).By similarity

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

PaxDbiQ9Y5Q3.
PRIDEiQ9Y5Q3.

PTM databases

PhosphoSiteiQ9Y5Q3.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiQ9Y5Q3.
CleanExiHS_MAFB.
GenevestigatoriQ9Y5Q3.

Organism-specific databases

HPAiHPA005653.

Interactioni

Subunit structurei

Homodimer or heterodimer with other bHLH-Zip transcription factors. Binds DNA as a homodimer or a heterodimer. Forms homodimers and heterodimers with FOS, FOSB and FOSL2, but not with JUN proteins (JUN, JUNB and JUND). Interacts with PAX6; the interaction is direct. Interacts with ETS1 and LRP1 (By similarity). Interacts with the intracellular cytoplasmic domain of LRP1 (LRPICD); the interaction results in a moderate reduction of MAFB transcriptional potential.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
IRF3Q146534EBI-3649340,EBI-2650369

Protein-protein interaction databases

BioGridi115261. 14 interactions.
IntActiQ9Y5Q3. 5 interactions.
STRINGi9606.ENSP00000362410.

Structurei

3D structure databases

ProteinModelPortaliQ9Y5Q3.
SMRiQ9Y5Q3. Positions 211-297.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini238 – 30164bZIPPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni238 – 26326Basic motifPROSITE-ProRule annotationAdd
BLAST
Regioni266 – 28722Leucine-zipperPROSITE-ProRule annotationAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi131 – 14313Poly-HisAdd
BLAST
Compositional biasi158 – 16710Poly-His

Domaini

The leucine-zipper domain is involved in the interaction with LRPICD.

Sequence similaritiesi

Belongs to the bZIP family. Maf subfamily.Curated
Contains 1 bZIP (basic-leucine zipper) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG241084.
GeneTreeiENSGT00550000074549.
HOGENOMiHOG000261683.
HOVERGENiHBG000313.
InParanoidiQ9Y5Q3.
KOiK09036.
OMAiHPHHGYP.
OrthoDBiEOG7BGHMQ.
PhylomeDBiQ9Y5Q3.
TreeFamiTF325689.

Family and domain databases

Gene3Di1.10.880.10. 1 hit.
InterProiIPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028571. MafB.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view]
PANTHERiPTHR10129. PTHR10129. 1 hit.
PTHR10129:SF10. PTHR10129:SF10. 1 hit.
PfamiPF03131. bZIP_Maf. 1 hit.
PF08383. Maf_N. 1 hit.
[Graphical view]
SMARTiSM00338. BRLZ. 1 hit.
[Graphical view]
SUPFAMiSSF47454. SSF47454. 1 hit.
PROSITEiPS50217. BZIP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9Y5Q3 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAELSMGPE LPTSPLAMEY VNDFDLLKFD VKKEPLGRAE RPGRPCTRLQ
60 70 80 90 100
PAGSVSSTPL STPCSSVPSS PSFSPTEQKT HLEDLYWMAS NYQQMNPEAL
110 120 130 140 150
NLTPEDAVEA LIGSHPVPQP LQSFDSFRGA HHHHHHHHPH PHHAYPGAGV
160 170 180 190 200
AHDELGPHAH PHHHHHHQAS PPPSSAASPA QQLPTSHPGP GPHATASATA
210 220 230 240 250
AGGNGSVEDR FSDDQLVSMS VRELNRHLRG FTKDEVIRLK QKRRTLKNRG
260 270 280 290 300
YAQSCRYKRV QQKHHLENEK TQLIQQVEQL KQEVSRLARE RDAYKVKCEK
310 320
LANSGFREAG STSDSPSSPE FFL
Length:323
Mass (Da):35,792
Last modified:July 11, 2002 - v2
Checksum:iA0F3C09F8936CB16
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti52 – 521A → V in AAD30106. (PubMed:10444328)Curated
Sequence conflicti241 – 2411Q → H in AAD30106. (PubMed:10444328)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti54 – 541S → L in MCTO. 1 Publication
VAR_067979
Natural varianti59 – 591P → L in MCTO. 1 Publication
VAR_067980
Natural varianti62 – 621T → P in MCTO. 1 Publication
VAR_067981
Natural varianti63 – 631P → R in MCTO. 1 Publication
VAR_067982
Natural varianti66 – 661S → C in MCTO. 1 Publication
VAR_067983
Natural varianti69 – 691S → L in MCTO. 1 Publication
VAR_067984
Natural varianti70 – 701S → A in MCTO. 1 Publication
VAR_067985
Natural varianti70 – 701S → L in MCTO. 1 Publication
VAR_067986
Natural varianti71 – 711P → L in MCTO. 1 Publication
VAR_067987
Natural varianti71 – 711P → S in MCTO. 1 Publication
VAR_067988

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF134157 mRNA. Translation: AAD30106.1.
AK027324 mRNA. Translation: BAG51303.1.
AL035665 Genomic DNA. Translation: CAB75863.1.
CH471077 Genomic DNA. Translation: EAW76000.1.
BC028098 mRNA. Translation: AAH28098.1.
BC036689 mRNA. Translation: AAH36689.1.
CCDSiCCDS13311.1.
RefSeqiNP_005452.2. NM_005461.4.
UniGeneiHs.169487.

Genome annotation databases

EnsembliENST00000373313; ENSP00000362410; ENSG00000204103.
GeneIDi9935.
KEGGihsa:9935.
UCSCiuc002xji.3. human.

Polymorphism databases

DMDMi21759268.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF134157 mRNA. Translation: AAD30106.1 .
AK027324 mRNA. Translation: BAG51303.1 .
AL035665 Genomic DNA. Translation: CAB75863.1 .
CH471077 Genomic DNA. Translation: EAW76000.1 .
BC028098 mRNA. Translation: AAH28098.1 .
BC036689 mRNA. Translation: AAH36689.1 .
CCDSi CCDS13311.1.
RefSeqi NP_005452.2. NM_005461.4.
UniGenei Hs.169487.

3D structure databases

ProteinModelPortali Q9Y5Q3.
SMRi Q9Y5Q3. Positions 211-297.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115261. 14 interactions.
IntActi Q9Y5Q3. 5 interactions.
STRINGi 9606.ENSP00000362410.

PTM databases

PhosphoSitei Q9Y5Q3.

Polymorphism databases

DMDMi 21759268.

Proteomic databases

PaxDbi Q9Y5Q3.
PRIDEi Q9Y5Q3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000373313 ; ENSP00000362410 ; ENSG00000204103 .
GeneIDi 9935.
KEGGi hsa:9935.
UCSCi uc002xji.3. human.

Organism-specific databases

CTDi 9935.
GeneCardsi GC20M039314.
HGNCi HGNC:6408. MAFB.
HPAi HPA005653.
MIMi 166300. phenotype.
608968. gene.
neXtProti NX_Q9Y5Q3.
Orphaneti 2774. Multicentric carpo-tarsal osteolysis with or without nephropathy.
PharmGKBi PA30535.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG241084.
GeneTreei ENSGT00550000074549.
HOGENOMi HOG000261683.
HOVERGENi HBG000313.
InParanoidi Q9Y5Q3.
KOi K09036.
OMAi HPHHGYP.
OrthoDBi EOG7BGHMQ.
PhylomeDBi Q9Y5Q3.
TreeFami TF325689.

Miscellaneous databases

ChiTaRSi MAFB. human.
GeneWikii MAFB_(gene).
GenomeRNAii 9935.
NextBioi 37480.
PROi Q9Y5Q3.
SOURCEi Search...

Gene expression databases

Bgeei Q9Y5Q3.
CleanExi HS_MAFB.
Genevestigatori Q9Y5Q3.

Family and domain databases

Gene3Di 1.10.880.10. 1 hit.
InterProi IPR004827. bZIP.
IPR004826. bZIP_Maf.
IPR013592. Maf_TF_N.
IPR028571. MafB.
IPR008917. TF_DNA-bd.
IPR024874. Transciption_factor_Maf.
[Graphical view ]
PANTHERi PTHR10129. PTHR10129. 1 hit.
PTHR10129:SF10. PTHR10129:SF10. 1 hit.
Pfami PF03131. bZIP_Maf. 1 hit.
PF08383. Maf_N. 1 hit.
[Graphical view ]
SMARTi SM00338. BRLZ. 1 hit.
[Graphical view ]
SUPFAMi SSF47454. SSF47454. 1 hit.
PROSITEi PS50217. BZIP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Human KRML (MAFB): cDNA cloning, genomic structure, and evaluation as a candidate tumor suppressor gene in myeloid leukemias."
    Wang P.W., Eisenbart J.D., Cordes S.P., Barsh G.S., Stoffel M., Le Beau M.M.
    Genomics 59:275-281(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Bone marrow.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Embryo.
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R., Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L., Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P., Bird C.P., Blakey S.E.
    , Bridgeman A.M., Brown A.J., Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P., Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E., Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J., Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D., Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S., Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D., Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A., Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T., Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I., Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Brain.
  6. "Low-density lipoprotein receptor-related protein interacts with MafB, a regulator of hindbrain development."
    Petersen H.H., Hilpert J., Jacobsen C., Lauwers A., Roebroek A.J.M., Willnow T.E.
    FEBS Lett. 565:23-27(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRP1.
  7. Cited for: PHOSPHORYLATION.
  8. Cited for: PHOSPHORYLATION.
  9. Cited for: REVIEW, FUNCTION.
  10. "Multicentric carpotarsal osteolysis is caused by mutations clustering in the amino-terminal transcriptional activation domain of MAFB."
    Zankl A., Duncan E.L., Leo P.J., Clark G.R., Glazov E.A., Addor M.C., Herlin T., Kim C.A., Leheup B.P., McGill J., McTaggart S., Mittas S., Mitchell A.L., Mortier G.R., Robertson S.P., Schroeder M., Terhal P., Brown M.A.
    Am. J. Hum. Genet. 90:494-501(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MCTO LEU-54; LEU-59; PRO-62; ARG-63; CYS-66; LEU-69; ALA-70; LEU-70; SER-71 AND LEU-71.

Entry informationi

Entry nameiMAFB_HUMAN
AccessioniPrimary (citable) accession number: Q9Y5Q3
Secondary accession number(s): B3KNE1, Q9H1F1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2002
Last sequence update: July 11, 2002
Last modified: October 29, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3