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O95409

- ZIC2_HUMAN

UniProt

O95409 - ZIC2_HUMAN

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Protein
Zinc finger protein ZIC 2
Gene
ZIC2
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 important roles in the early stage of organogenesis of the CNS. Activates the transcription of the serotonin transporter SERT in uncrossed ipsilateral retinal ganglion cells (iRGCs) to refine eye-specific projections in primary visual targets. Its transcriptional activity is repressed by MDFIC. Involved in the formation of the ipsilateral retinal projection at the optic chiasm midline. Drives the expression of EPHB1 on ipsilaterally projecting growth cones. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. Associates to the basal SERT promoter region from ventrotemporal retinal segments of retinal embryos.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri256 – 29136C2H2-type 1; atypical
Add
BLAST
Zinc fingeri300 – 32728C2H2-type 2; atypical
Add
BLAST
Zinc fingeri333 – 35725C2H2-type 3
Add
BLAST
Zinc fingeri363 – 38725C2H2-type 4
Add
BLAST
Zinc fingeri393 – 41523C2H2-type 5
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. chromatin DNA binding Source: UniProtKB
  3. metal ion binding Source: UniProtKB-KW
  4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
Complete GO annotation...

GO - Biological processi

  1. brain development Source: ProtInc
  2. developmental pigmentation Source: Ensembl
  3. negative regulation of transcription, DNA-templated Source: UniProtKB
  4. neural tube closure Source: Ensembl
  5. positive regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  6. positive regulation of transcription, DNA-templated Source: UniProtKB
  7. retinal ganglion cell axon guidance Source: Ensembl
  8. transcription, DNA-templated Source: UniProtKB-KW
  9. visual perception Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Repressor

Keywords - Biological processi

Differentiation, Neurogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiO95409.

Names & Taxonomyi

Protein namesi
Recommended name:
Zinc finger protein ZIC 2
Alternative name(s):
Zinc finger protein of the cerebellum 2
Gene namesi
Name:ZIC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:12873. ZIC2.

Subcellular locationi

Nucleus. Cytoplasm By similarity
Note: Localizes in the cytoplasm in presence of MDFIC overexpression. Both phosphorylated and unphosphorylated forms are localized in the nucleus By similarity.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Holoprosencephaly 5 (HPE5) [MIM:609637]: A structural anomaly of the brain, in which the developing forebrain fails to correctly separate into right and left hemispheres. Holoprosencephaly is genetically heterogeneous and associated with several distinct facies and phenotypic variability.
Note: The disease is caused by mutations affecting the gene represented in this entry.5 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361Q → P in HPE5; 2-fold increase in luciferase activity. 2 Publications
VAR_023793
Natural varianti37 – 371D → N in HPE5. 1 Publication
VAR_058592
Natural varianti128 – 1281D → N in HPE5. 1 Publication
VAR_058593
Natural varianti152 – 1521D → F in HPE5; requires 2 nucleotide substitutions; 50% reduction of luciferase activity. 3 Publications
VAR_023794
Natural varianti272 – 2721S → N in HPE5. 1 Publication
VAR_058594
Natural varianti286 – 2861H → L in HPE5. 1 Publication
VAR_058595
Natural varianti286 – 2861H → Q in HPE5. 1 Publication
VAR_058596
Natural varianti286 – 2861H → Y in HPE5. 1 Publication
VAR_058597
Natural varianti291 – 2911H → Y in HPE5. 1 Publication
VAR_058598
Natural varianti304 – 3041W → R in HPE5. 1 Publication
VAR_058599
Natural varianti314 – 3141F → C in HPE5. 1 Publication
VAR_058600
Natural varianti325 – 3251R → L in HPE5. 1 Publication
VAR_058601
Natural varianti325 – 3251R → S in HPE5. 1 Publication
VAR_058602
Natural varianti327 – 3271H → Y in HPE5. 1 Publication
VAR_058603
Natural varianti335 – 3351C → F in HPE5. 1 Publication
VAR_058604
Natural varianti373 – 3731R → P in HPE5. 1 Publication
VAR_058605
Natural varianti402 – 4021Y → N in HPE5. 1 Publication
VAR_058606
Natural varianti403 – 4031T → K in HPE5. 1 Publication
VAR_058607
Natural varianti404 – 4041H → R in HPE5. 1 Publication
VAR_058608
Natural varianti409 – 4091R → W in HPE5. 1 Publication
VAR_058609
Natural varianti415 – 4151H → Q in HPE5. 1 Publication
VAR_058610
Natural varianti470 – 4701A → AAAAAAAAAAA in HPE5; near-complete loss of luciferase activity.
VAR_008856

Keywords - Diseasei

Disease mutation, Holoprosencephaly

Organism-specific databases

MIMi609637. phenotype.
Orphaneti93925. Alobar holoprosencephaly.
93924. Lobar holoprosencephaly.
280200. Microform holoprosencephaly.
93926. Midline interhemispheric variant of holoprosencephaly.
220386. Semilobar holoprosencephaly.
280195. Septopreoptic holoprosencephaly.
PharmGKBiPA37462.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 532532Zinc finger protein ZIC 2
PRO_0000047247Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei191 – 1911Phosphoserine By similarity
Modified residuei199 – 1991Phosphoserine By similarity

Post-translational modificationi

Phosphorylated.
Ubiquitinated by RNF180, leading to its degradation.

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO95409.
PaxDbiO95409.
PeptideAtlasiO95409.
PRIDEiO95409.

PTM databases

PhosphoSiteiO95409.

Expressioni

Gene expression databases

BgeeiO95409.
CleanExiHS_ZIC2.
GenevestigatoriO95409.

Interactioni

Subunit structurei

Interacts with RNF180. Interacts (via the C2H2-type domains 3, 4 and 5) with MDFIC (via the C2H2-type domains 3, 4 and 5); the interaction reduces its transcriptional activity. Interacts with DHX9 By similarity.

Protein-protein interaction databases

BioGridi113378. 7 interactions.
IntActiO95409. 1 interaction.
MINTiMINT-2798893.
STRINGi9606.ENSP00000365514.

Structurei

3D structure databases

ProteinModelPortaliO95409.
SMRiO95409. Positions 250-417.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni100 – 255156Necessary for interaction with MDFIC and transcriptional activation or repression By similarity
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 234Poly-His
Compositional biasi25 – 339Poly-Ala
Compositional biasi89 – 979Poly-Ala
Compositional biasi226 – 2305Poly-Ala
Compositional biasi231 – 2399Poly-His
Compositional biasi456 – 47015Poly-Ala
Add
BLAST
Compositional biasi490 – 50819Poly-Gly
Add
BLAST

Domaini

The C2H2-type 3, 4 and 5 zinc finger domains are necessary for transcription activation By similarity.

Sequence similaritiesi

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiCOG5048.
HOGENOMiHOG000232057.
HOVERGENiHBG007135.
InParanoidiO95409.
KOiK06235.
OMAiGIHDQHG.
OrthoDBiEOG76472R.
PhylomeDBiO95409.
TreeFamiTF351425.

Family and domain databases

Gene3Di3.30.160.60. 4 hits.
InterProiIPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00096. zf-C2H2. 1 hit.
[Graphical view]
SMARTiSM00355. ZnF_C2H2. 5 hits.
[Graphical view]
PROSITEiPS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O95409-1 [UniParc]FASTAAdd to Basket

« Hide

MLLDAGPQFP AIGVGSFARH HHHSAAAAAA AAAEMQDREL SLAAAQNGFV    50
DSAAAHMGAF KLNPGAHELS PGQSSAFTSQ GPGAYPGSAA AAAAAAALGP 100
HAAHVGSYSG PPFNSTRDFL FRSRGFGDSA PGGGQHGLFG PGAGGLHHAH 150
SDAQGHLLFP GLPEQHGPHG SQNVLNGQMR LGLPGEVFGR SEQYRQVASP 200
RTDPYSAAQL HNQYGPMNMN MGMNMAAAAA HHHHHHHHHP GAFFRYMRQQ 250
CIKQELICKW IDPEQLSNPK KSCNKTFSTM HELVTHVSVE HVGGPEQSNH 300
VCFWEECPRE GKPFKAKYKL VNHIRVHTGE KPFPCPFPGC GKVFARSENL 350
KIHKRTHTGE KPFQCEFEGC DRRFANSSDR KKHMHVHTSD KPYLCKMCDK 400
SYTHPSSLRK HMKVHESSPQ GSESSPAASS GYESSTPPGL VSPSAEPQSS 450
SNLSPAAAAA AAAAAAAAAA VSAVHRGGGS GSGGAGGGSG GGSGSGGGGG 500
GAGGGGGGSS GGGSGTAGGH SGLSSNFNEW YV 532
Length:532
Mass (Da):55,006
Last modified:April 16, 2002 - v2
Checksum:iBA3E6455DAF97EAC
GO

Polymorphismi

The poly-His region between amino acids 231-239 of ZIC2 is polymorphic and the number of His can vary from 8 to 12.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti36 – 361Q → P in HPE5; 2-fold increase in luciferase activity. 2 Publications
VAR_023793
Natural varianti37 – 371D → N in HPE5. 1 Publication
VAR_058592
Natural varianti128 – 1281D → N in HPE5. 1 Publication
VAR_058593
Natural varianti152 – 1521D → F in HPE5; requires 2 nucleotide substitutions; 50% reduction of luciferase activity. 3 Publications
VAR_023794
Natural varianti239 – 2391H → HH.1 Publication
VAR_023795
Natural varianti239 – 2391Missing.1 Publication
VAR_023796
Natural varianti272 – 2721S → N in HPE5. 1 Publication
VAR_058594
Natural varianti286 – 2861H → L in HPE5. 1 Publication
VAR_058595
Natural varianti286 – 2861H → Q in HPE5. 1 Publication
VAR_058596
Natural varianti286 – 2861H → Y in HPE5. 1 Publication
VAR_058597
Natural varianti291 – 2911H → Y in HPE5. 1 Publication
VAR_058598
Natural varianti304 – 3041W → R in HPE5. 1 Publication
VAR_058599
Natural varianti314 – 3141F → C in HPE5. 1 Publication
VAR_058600
Natural varianti325 – 3251R → L in HPE5. 1 Publication
VAR_058601
Natural varianti325 – 3251R → S in HPE5. 1 Publication
VAR_058602
Natural varianti327 – 3271H → Y in HPE5. 1 Publication
VAR_058603
Natural varianti335 – 3351C → F in HPE5. 1 Publication
VAR_058604
Natural varianti373 – 3731R → P in HPE5. 1 Publication
VAR_058605
Natural varianti402 – 4021Y → N in HPE5. 1 Publication
VAR_058606
Natural varianti403 – 4031T → K in HPE5. 1 Publication
VAR_058607
Natural varianti404 – 4041H → R in HPE5. 1 Publication
VAR_058608
Natural varianti409 – 4091R → W in HPE5. 1 Publication
VAR_058609
Natural varianti415 – 4151H → Q in HPE5. 1 Publication
VAR_058610
Natural varianti470 – 4701A → AAAAAAAAAAA in HPE5; near-complete loss of luciferase activity.
VAR_008856

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1285RGFGD → ARLPGT in AAC96325. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104902 mRNA. Translation: AAC96325.1.
AF193855 mRNA. Translation: AAG28409.1.
AL355338 Genomic DNA. Translation: CAH70367.1.
CCDSiCCDS9495.1.
RefSeqiNP_009060.2. NM_007129.3.
UniGeneiHs.653700.

Genome annotation databases

EnsembliENST00000376335; ENSP00000365514; ENSG00000043355.
GeneIDi7546.
KEGGihsa:7546.
UCSCiuc001von.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF104902 mRNA. Translation: AAC96325.1 .
AF193855 mRNA. Translation: AAG28409.1 .
AL355338 Genomic DNA. Translation: CAH70367.1 .
CCDSi CCDS9495.1.
RefSeqi NP_009060.2. NM_007129.3.
UniGenei Hs.653700.

3D structure databases

ProteinModelPortali O95409.
SMRi O95409. Positions 250-417.
ModBasei Search...

Protein-protein interaction databases

BioGridi 113378. 7 interactions.
IntActi O95409. 1 interaction.
MINTi MINT-2798893.
STRINGi 9606.ENSP00000365514.

PTM databases

PhosphoSitei O95409.

Proteomic databases

MaxQBi O95409.
PaxDbi O95409.
PeptideAtlasi O95409.
PRIDEi O95409.

Protocols and materials databases

DNASUi 7546.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000376335 ; ENSP00000365514 ; ENSG00000043355 .
GeneIDi 7546.
KEGGi hsa:7546.
UCSCi uc001von.3. human.

Organism-specific databases

CTDi 7546.
GeneCardsi GC13P100634.
GeneReviewsi ZIC2.
HGNCi HGNC:12873. ZIC2.
MIMi 603073. gene.
609637. phenotype.
neXtProti NX_O95409.
Orphaneti 93925. Alobar holoprosencephaly.
93924. Lobar holoprosencephaly.
280200. Microform holoprosencephaly.
93926. Midline interhemispheric variant of holoprosencephaly.
220386. Semilobar holoprosencephaly.
280195. Septopreoptic holoprosencephaly.
PharmGKBi PA37462.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5048.
HOGENOMi HOG000232057.
HOVERGENi HBG007135.
InParanoidi O95409.
KOi K06235.
OMAi GIHDQHG.
OrthoDBi EOG76472R.
PhylomeDBi O95409.
TreeFami TF351425.

Enzyme and pathway databases

SignaLinki O95409.

Miscellaneous databases

GeneWikii ZIC2.
GenomeRNAii 7546.
NextBioi 29525.
PROi O95409.
SOURCEi Search...

Gene expression databases

Bgeei O95409.
CleanExi HS_ZIC2.
Genevestigatori O95409.

Family and domain databases

Gene3Di 3.30.160.60. 4 hits.
InterProi IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view ]
Pfami PF00096. zf-C2H2. 1 hit.
[Graphical view ]
SMARTi SM00355. ZnF_C2H2. 5 hits.
[Graphical view ]
PROSITEi PS00028. ZINC_FINGER_C2H2_1. 3 hits.
PS50157. ZINC_FINGER_C2H2_2. 4 hits.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Holoprosencephaly due to mutations in ZIC2, a homologue of Drosophila odd-paired."
    Brown S.A., Warburton D., Brown L.Y., Yu C.Y., Roeder E.R., Stengel-Rutkowski S., Hennekam R.C.M., Muenke M.
    Nat. Genet. 20:180-183(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION OF VARIANT HPE5 POLY-ALA INS.
  2. "ZIC2 and Sp3 repress Sp1-induced activation of the human D1A dopamine receptor gene."
    Yang Y., Hwang C.K., Junn E., Lee G., Mouradian M.M.
    J. Biol. Chem. 275:38863-38869(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain.
  3. "The DNA sequence and analysis of human chromosome 13."
    Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.
    Nature 428:522-528(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Holoprosencephaly due to mutations in ZIC2: alanine tract expansion mutations may be caused by parental somatic recombination."
    Brown L.Y., Odent S., David V., Blayau M., Dubourg C., Apacik C., Delgado M.A., Hall B.D., Reynolds J.F., Sommer A., Wieczorek D., Brown S.A., Muenke M.
    Hum. Mol. Genet. 10:791-796(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HPE5 POLY-ALA INS AND PHE-152, POLYMORPHISM OF POLY-HIS REGION.
  5. "Molecular screening of SHH, ZIC2, SIX3, and TGIF genes in patients with features of holoprosencephaly spectrum: mutation review and genotype-phenotype correlations."
    Dubourg C., Lazaro L., Pasquier L., Bendavid C., Blayau M., Le Duff F., Durou M.-R., Odent S., David V.
    Hum. Mutat. 24:43-51(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HPE5 PRO-36 AND PHE-152, VARIANTS HIS-239 INS AND HIS-239 DEL.
  6. "In vitro analysis of partial loss-of-function ZIC2 mutations in holoprosencephaly: alanine tract expansion modulates DNA binding and transactivation."
    Brown L., Paraso M., Arkell R., Brown S.
    Hum. Mol. Genet. 14:411-420(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS HPE5 PRO-36; PHE-152 AND POLY-ALA INS.
  7. "The full spectrum of holoprosencephaly-associated mutations within the ZIC2 gene in humans predicts loss-of-function as the predominant disease mechanism."
    Roessler E., Lacbawan F., Dubourg C., Paulussen A., Herbergs J., Hehr U., Bendavid C., Zhou N., Ouspenskaia M., Bale S., Odent S., David V., Muenke M.
    Hum. Mutat. 30:E541-E554(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HPE5 ASN-37; ASN-128; ASN-272; LEU-286; GLN-286; TYR-286; TYR-291; ARG-304; CYS-314; SER-325; LEU-325; TYR-327; PHE-335; PRO-373; ASN-402; LYS-403; ARG-404; TRP-409 AND GLN-415.

Entry informationi

Entry nameiZIC2_HUMAN
AccessioniPrimary (citable) accession number: O95409
Secondary accession number(s): Q5VYA9, Q9H309
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: April 16, 2002
Last modified: July 9, 2014
This is version 135 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 13
    Human chromosome 13: 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