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Q8WWZ3

- EDAD_HUMAN

UniProt

Q8WWZ3 - EDAD_HUMAN

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Protein
Ectodysplasin-A receptor-associated adapter protein
Gene
EDARADD
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Adapter protein that interacts with EDAR DEATH domain and couples the receptor to EDA signaling pathway during morphogenesis of ectodermal organs. Mediates the activation of NF-kappa-B.1 Publication

GO - Biological processi

  1. cell differentiation Source: UniProtKB-KW
  2. hair follicle development Source: Ensembl
  3. odontogenesis of dentin-containing tooth Source: Ensembl
  4. signal transduction Source: InterPro
  5. trachea gland development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation

Names & Taxonomyi

Protein namesi
Recommended name:
Ectodysplasin-A receptor-associated adapter protein
Alternative name(s):
EDAR-associated death domain protein
Protein crinkled homolog
Gene namesi
Name:EDARADD
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:14341. EDARADD.

Subcellular locationi

Cytoplasm Inferred

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Involvement in diseasei

Ectodermal dysplasia 11A, hypohidrotic/hair/nail type, autosomal dominant (ECTD11A) [MIM:614940]: A form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. It is an autosomal dominant condition characterized by hypotrichosis, abnormal or missing teeth, and hypohidrosis due to the absence of sweat glands.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti114 – 1141D → Y in ECTD11A. 1 Publication
VAR_064835
Natural varianti122 – 1221L → R in ECTD11A; severely impairs NF-kappa-B activation and acted in a dominant-negative manner. 1 Publication
VAR_054510
Ectodermal dysplasia 11B, hypohidrotic/hair/tooth type, autosomal recessive (ECTD11B) [MIM:614941]: A disorder due to abnormal development of two or more ectodermal structures, and characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands.
Note: The disease is caused by mutations affecting the gene represented in this entry.3 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti135 – 1362Missing in ECTD11B; impairs the interaction with EDAR and severely inhibits NF-kappa-B activity.
VAR_064836
Natural varianti152 – 1521E → K in ECTD11B; may reduce binding to EDAR; impairs NF-kappa-B activation by about 50%. 2 Publications
VAR_013482

Keywords - Diseasei

Disease mutation, Ectodermal dysplasia

Organism-specific databases

MIMi614940. phenotype.
614941. phenotype.
Orphaneti1810. Autosomal dominant hypohidrotic ectodermal dysplasia.
248. Autosomal recessive hypohidrotic ectodermal dysplasia.
99798. Oligodontia.
PharmGKBiPA27603.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 215215Ectodysplasin-A receptor-associated adapter protein
PRO_0000086928Add
BLAST

Proteomic databases

MaxQBiQ8WWZ3.
PaxDbiQ8WWZ3.
PRIDEiQ8WWZ3.

Expressioni

Tissue specificityi

Detected in adult pancreas, placenta and fetal skin, and at lower levels in lung, thymus, prostate and testis.

Gene expression databases

ArrayExpressiQ8WWZ3.
BgeeiQ8WWZ3.
CleanExiHS_EDARADD.
GenevestigatoriQ8WWZ3.

Organism-specific databases

HPAiHPA018836.

Interactioni

Subunit structurei

Self-associates and binds EDAR, TRAF1, TRAF2 and TRAF3.

Protein-protein interaction databases

BioGridi126096. 5 interactions.
IntActiQ8WWZ3. 3 interactions.
STRINGi9606.ENSP00000335076.

Structurei

3D structure databases

ProteinModelPortaliQ8WWZ3.
SMRiQ8WWZ3. Positions 120-204.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini123 – 20280Death
Add
BLAST

Sequence similaritiesi

Contains 1 death domain.

Phylogenomic databases

eggNOGiNOG46533.
HOGENOMiHOG000013132.
HOVERGENiHBG018567.
InParanoidiQ8WWZ3.
OMAiDHMAKEP.
PhylomeDBiQ8WWZ3.
TreeFamiTF335658.

Family and domain databases

Gene3Di1.10.533.10. 1 hit.
InterProiIPR011029. DEATH-like_dom.
IPR000488. Death_domain.
[Graphical view]
PfamiPF00531. Death. 1 hit.
[Graphical view]
SUPFAMiSSF47986. SSF47986. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform A (identifier: Q8WWZ3-1) [UniParc]FASTAAdd to Basket

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.

« Hide

MGLRTTKQMG RGTKAPGHQE DHMVKEPVED TDPSTLSFNM SDKYPIQDTE    50
LPKAEECDTI TLNCPRNSDM KNQGEENGFP DSTGDPLPEI SKDNSCKENC 100
TCSSCLLRAP TISDLLNDQD LLDVIRIKLD PCHPTVKNWR NFASKWGMSY 150
DELCFLEQRP QSPTLEFLLR NSQRTVGQLM ELCRLYHRAD VEKVLRRWVD 200
EEWPKRERGD PSRHF 215
Length:215
Mass (Da):24,802
Last modified:November 4, 2008 - v3
Checksum:i25C198E3CA1F68F2
GO
Isoform B (identifier: Q8WWZ3-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-20: MGLRTTKQMGRGTKAPGHQE → MASPDDPLRA

Show »
Length:205
Mass (Da):23,690
Checksum:iA83CCC3E4F3115CF
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti9 – 91M → I.3 Publications
Corresponds to variant rs966365 [ dbSNP | Ensembl ].
VAR_050963
Natural varianti103 – 1031S → F.1 Publication
Corresponds to variant rs114632254 [ dbSNP | Ensembl ].
VAR_054509
Natural varianti114 – 1141D → Y in ECTD11A. 1 Publication
VAR_064835
Natural varianti122 – 1221L → R in ECTD11A; severely impairs NF-kappa-B activation and acted in a dominant-negative manner. 1 Publication
VAR_054510
Natural varianti135 – 1362Missing in ECTD11B; impairs the interaction with EDAR and severely inhibits NF-kappa-B activity.
VAR_064836
Natural varianti152 – 1521E → K in ECTD11B; may reduce binding to EDAR; impairs NF-kappa-B activation by about 50%. 2 Publications
VAR_013482

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2020MGLRT…PGHQE → MASPDDPLRA in isoform B.
VSP_003861Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY028914 mRNA. Translation: AAK40288.1.
AY071862 mRNA. Translation: AAL60590.1.
AY028912
, AY028906, AY028908, AY028909, AY028910, AY028911 Genomic DNA. Translation: AAK40285.1.
AY028912
, AY028907, AY028908, AY028909, AY028910, AY028911 Genomic DNA. Translation: AAK40286.1.
AY028913 mRNA. Translation: AAK40287.1.
AK290862 mRNA. Translation: BAF83551.1.
AK291930 mRNA. Translation: BAF84619.1.
AK314634 mRNA. Translation: BAG37197.1.
AL354693, AL136105 Genomic DNA. Translation: CAH70608.1.
AL354693, AL136105 Genomic DNA. Translation: CAH70609.1.
AL136105, AL354693 Genomic DNA. Translation: CAI22302.1.
AL136105, AL354693 Genomic DNA. Translation: CAI22303.1.
CH471098 Genomic DNA. Translation: EAW70052.1.
BC128082 mRNA. Translation: AAI28083.1.
CCDSiCCDS1610.1. [Q8WWZ3-1]
CCDS31065.1. [Q8WWZ3-2]
RefSeqiNP_542776.1. NM_080738.3. [Q8WWZ3-2]
NP_665860.2. NM_145861.2. [Q8WWZ3-1]
UniGeneiHs.352224.

Genome annotation databases

EnsembliENST00000334232; ENSP00000335076; ENSG00000186197. [Q8WWZ3-1]
ENST00000359362; ENSP00000352320; ENSG00000186197. [Q8WWZ3-2]
GeneIDi128178.
KEGGihsa:128178.
UCSCiuc001hxu.1. human. [Q8WWZ3-1]
uc001hxv.1. human. [Q8WWZ3-2]

Polymorphism databases

DMDMi212276512.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY028914 mRNA. Translation: AAK40288.1 .
AY071862 mRNA. Translation: AAL60590.1 .
AY028912
, AY028906 , AY028908 , AY028909 , AY028910 , AY028911 Genomic DNA. Translation: AAK40285.1 .
AY028912
, AY028907 , AY028908 , AY028909 , AY028910 , AY028911 Genomic DNA. Translation: AAK40286.1 .
AY028913 mRNA. Translation: AAK40287.1 .
AK290862 mRNA. Translation: BAF83551.1 .
AK291930 mRNA. Translation: BAF84619.1 .
AK314634 mRNA. Translation: BAG37197.1 .
AL354693 , AL136105 Genomic DNA. Translation: CAH70608.1 .
AL354693 , AL136105 Genomic DNA. Translation: CAH70609.1 .
AL136105 , AL354693 Genomic DNA. Translation: CAI22302.1 .
AL136105 , AL354693 Genomic DNA. Translation: CAI22303.1 .
CH471098 Genomic DNA. Translation: EAW70052.1 .
BC128082 mRNA. Translation: AAI28083.1 .
CCDSi CCDS1610.1. [Q8WWZ3-1 ]
CCDS31065.1. [Q8WWZ3-2 ]
RefSeqi NP_542776.1. NM_080738.3. [Q8WWZ3-2 ]
NP_665860.2. NM_145861.2. [Q8WWZ3-1 ]
UniGenei Hs.352224.

3D structure databases

ProteinModelPortali Q8WWZ3.
SMRi Q8WWZ3. Positions 120-204.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 126096. 5 interactions.
IntActi Q8WWZ3. 3 interactions.
STRINGi 9606.ENSP00000335076.

Polymorphism databases

DMDMi 212276512.

Proteomic databases

MaxQBi Q8WWZ3.
PaxDbi Q8WWZ3.
PRIDEi Q8WWZ3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000334232 ; ENSP00000335076 ; ENSG00000186197 . [Q8WWZ3-1 ]
ENST00000359362 ; ENSP00000352320 ; ENSG00000186197 . [Q8WWZ3-2 ]
GeneIDi 128178.
KEGGi hsa:128178.
UCSCi uc001hxu.1. human. [Q8WWZ3-1 ]
uc001hxv.1. human. [Q8WWZ3-2 ]

Organism-specific databases

CTDi 128178.
GeneCardsi GC01P236511.
GeneReviewsi EDARADD.
HGNCi HGNC:14341. EDARADD.
HPAi HPA018836.
MIMi 606603. gene.
614940. phenotype.
614941. phenotype.
neXtProti NX_Q8WWZ3.
Orphaneti 1810. Autosomal dominant hypohidrotic ectodermal dysplasia.
248. Autosomal recessive hypohidrotic ectodermal dysplasia.
99798. Oligodontia.
PharmGKBi PA27603.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG46533.
HOGENOMi HOG000013132.
HOVERGENi HBG018567.
InParanoidi Q8WWZ3.
OMAi DHMAKEP.
PhylomeDBi Q8WWZ3.
TreeFami TF335658.

Miscellaneous databases

GeneWikii EDARADD.
GenomeRNAii 128178.
NextBioi 82231.
PROi Q8WWZ3.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q8WWZ3.
Bgeei Q8WWZ3.
CleanExi HS_EDARADD.
Genevestigatori Q8WWZ3.

Family and domain databases

Gene3Di 1.10.533.10. 1 hit.
InterProi IPR011029. DEATH-like_dom.
IPR000488. Death_domain.
[Graphical view ]
Pfami PF00531. Death. 1 hit.
[Graphical view ]
SUPFAMi SSF47986. SSF47986. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Gene defect in ectodermal dysplasia implicates a DEATH domain adapter in development."
    Headon D.J., Emmal S.A., Ferguson B.M., Tucker A.S., Justice M.J., Sharpe P.T., Zonana J., Overbeek P.A.
    Nature 414:913-916(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), VARIANT ECTD11B LYS-152.
  2. "Identification of a novel DEATH domain-containing adaptor molecule for ectodysplasin-A receptor that is mutated in crinkled mice."
    Yan M., Zhang Z., Brady J.R., Schilbach S., Fairbrother W.J., Dixit V.M.
    Curr. Biol. 12:409-413(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B), FUNCTION.
    Tissue: Skin.
  3. "A novel death domain adapter required for ectodermal development."
    Emmal S.A., Ferguson B.M., Zonana J.
    Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM A), NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ILE-9.
  4. "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] (ISOFORMS A AND B), VARIANT ILE-9.
    Tissue: Mammary gland and Placenta.
  5. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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 A), VARIANT ILE-9.
  8. Cited for: VARIANT ECTD11A ARG-122, CHARACTERIZATION OF VARIANT ECTD11A ARG-122, CHARACTERIZATION OF VARIANT ECTD11B LYS-152.
  9. "Mutation screening of the ectodysplasin-A receptor gene EDAR in hypohidrotic ectodermal dysplasia."
    van der Hout A.H., Oudesluijs G.G., Venema A., Verheij J.B.G.M., Mol B.G.J., Rump P., Brunner H.G., Vos Y.J., van Essen A.J.
    Eur. J. Hum. Genet. 16:673-679(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT PHE-103.
  10. "Mutations in EDARADD account for a small proportion of hypohidrotic ectodermal dysplasia cases."
    Chassaing N., Cluzeau C., Bal E., Guigue P., Vincent M.C., Viot G., Ginisty D., Munnich A., Smahi A., Calvas P.
    Br. J. Dermatol. 162:1044-1048(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ECTD11B 135-THR-VAL-136 DEL, CHARACTERIZATION OF VARIANT ECTD11B 135-THR-VAL-136 DEL.
  11. Cited for: VARIANT ECTD11A TYR-114.

Entry informationi

Entry nameiEDAD_HUMAN
AccessioniPrimary (citable) accession number: Q8WWZ3
Secondary accession number(s): A2VCK5
, A8K7B5, B1AL54, B9ZVW5, Q5VYJ7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: November 4, 2008
Last modified: July 9, 2014
This is version 111 of the entry and version 3 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 1
    Human chromosome 1: 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

Similar proteinsi