SubmitCancel

Skip Header

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

O00422

- SAP18_HUMAN

UniProt

O00422 - SAP18_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
Histone deacetylase complex subunit SAP18
Gene
SAP18, GIG38
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Component of the SIN3-repressing complex. Enhances the ability of SIN3-HDAC1-mediated transcriptional repression. When tethered to the promoter, it can direct the formation of a repressive complex to core histone proteins. Auxiliary component of the splicing-dependent multiprotein exon junction complex (EJC) deposited at splice junction on mRNAs. The EJC is a dynamic structure consisting of core proteins and several peripheral nuclear and cytoplasmic associated factors that join the complex only transiently either during EJC assembly or during subsequent mRNA metabolism. Component of the ASAP and PSAP complexes which bind RNA in a sequence-independent manner and are proposed to be recruited to the EJC prior to or during the splicing process and to regulate specific excision of introns in specific transcription subsets. The ASAP complex can inhibit mRNA processing during in vitro splicing reactions. The ASAP complex promotes apoptosis and is disassembled after induction of apoptosis. Involved in the splicing modulation of BCL2L1/Bcl-X (and probably other apoptotic genes); specifically inhibits the formation of proapoptotic isoforms such as Bcl-X(S); the activity is different from the established EJC assembly and function.4 Publications

GO - Molecular functioni

  1. poly(A) RNA binding Source: UniProtKB
  2. protein binding Source: IntAct
  3. transcription corepressor activity Source: ProtInc

GO - Biological processi

  1. RNA splicing Source: UniProtKB-KW
  2. mRNA processing Source: UniProtKB-KW
  3. negative regulation of mRNA splicing, via spliceosome Source: UniProtKB
  4. positive regulation of apoptotic process Source: UniProtKB
  5. regulation of alternative mRNA splicing, via spliceosome Source: UniProtKB
  6. regulation of transcription from RNA polymerase II promoter Source: ProtInc
  7. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Repressor

Keywords - Biological processi

mRNA processing, mRNA splicing, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_200856. NoRC negatively regulates rRNA expression.
SignaLinkiO00422.

Protein family/group databases

TCDBi3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Histone deacetylase complex subunit SAP18
Alternative name(s):
18 kDa Sin3-associated polypeptide
2HOR0202
Cell growth-inhibiting gene 38 protein
Sin3-associated polypeptide p18
Gene namesi
Name:SAP18
ORF Names:GIG38
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 13

Organism-specific databases

HGNCiHGNC:10530. SAP18.

Subcellular locationi

Nucleus. Cytoplasm. Nucleus speckle
Note: Shuttles between the nucleus and the cytoplasm. Colocalizes with ACIN1 and SRSF2 in nuclear speckles.2 Publications

GO - Cellular componenti

  1. ASAP complex Source: UniProtKB
  2. cytoplasm Source: HPA
  3. histone deacetylase complex Source: ProtInc
  4. nuclear speck Source: UniProtKB
  5. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi118 – 1181D → A: Abolishes splicing regulation activity and interaction with RNPS1 and ACIN1; when associated with A-121. 1 Publication
Mutagenesisi121 – 1211T → A: Abolishes splicing regulation activity and interaction with RNPS1 and ACIN1; when associated with A-118. 1 Publication
Mutagenesisi126 – 1261K → A: No effect on splicing regulation activity. 1 Publication

Organism-specific databases

PharmGKBiPA34940.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 153152Histone deacetylase complex subunit SAP18
PRO_0000220975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiO00422.
PaxDbiO00422.
PeptideAtlasiO00422.
PRIDEiO00422.

PTM databases

PhosphoSiteiO00422.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO00422.
CleanExiHS_SAP18.
GenevestigatoriO00422.

Organism-specific databases

HPAiCAB012273.
HPA011352.

Interactioni

Subunit structurei

Found in a mRNA splicing-dependent exon junction complex (EJC). Component of the heterotrimeric ASAP (apoptosis- and splicing-associated protein) and PSAP complexes consisting of RNPS1, SAP18 and either ACIN1 or PNN, respectively; the ASAP and PSAP complexes probably are formed mutually exclusive. For the ASAP complex, the association of SAP18 seems to require a preformed RNPS1:ACIN1 complex. Forms a complex with SIN3A and HDAC1. Interacts with SUFU.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC1Q135472EBI-1044156,EBI-301834

Protein-protein interaction databases

BioGridi115573. 95 interactions.
DIPiDIP-33590N.
IntActiO00422. 12 interactions.
MINTiMINT-5002140.
STRINGi9606.ENSP00000371973.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni22 – 243
Beta strandi28 – 3710
Helixi43 – 453
Turni52 – 543
Beta strandi55 – 606
Helixi66 – 7611
Helixi78 – 814
Beta strandi86 – 916
Beta strandi95 – 984
Beta strandi104 – 1129
Helixi122 – 1254
Beta strandi132 – 1387
Beta strandi144 – 1474

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2HDENMR-A6-149[»]
ProteinModelPortaliO00422.
SMRiO00422. Positions 6-149.

Miscellaneous databases

EvolutionaryTraceiO00422.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni93 – 15361Involved in splicing regulation activity
Add
BLAST

Sequence similaritiesi

Belongs to the SAP18 family.

Phylogenomic databases

eggNOGiNOG249491.
HOGENOMiHOG000238745.
HOVERGENiHBG003465.
InParanoidiO00422.
KOiK14324.
OrthoDBiEOG79SDZS.
PhylomeDBiO00422.
TreeFamiTF313032.

Family and domain databases

InterProiIPR017250. Hist_deAcase_cplx_SAP18.
IPR010516. SAP18.
[Graphical view]
PANTHERiPTHR13082. PTHR13082. 1 hit.
PfamiPF06487. SAP18. 1 hit.
[Graphical view]
PIRSFiPIRSF037637. HDAC_SAP18. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O00422-1 [UniParc]FASTAAdd to Basket

« Hide

MAVESRVTQE EIKKEPEKPI DREKTCPLLL RVFTTNNGRH HRMDEFSRGN    50
VPSSELQIYT WMDATLKELT SLVKEVYPEA RKKGTHFNFA IVFTDVKRPG 100
YRVKEIGSTM SGRKGTDDSM TLQSQKFQIG DYLDIAITPP NRAPPPSGRM 150
RPY 153
Length:153
Mass (Da):17,561
Last modified:July 1, 1997 - v1
Checksum:iC7E479FFE9CA5774
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti114 – 1141K → E in AAF21220. 1 Publication
Sequence conflicti146 – 1461P → T in AAH30836. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U96915 mRNA. Translation: AAC51322.1.
U78303 mRNA. Translation: AAF21220.1.
AF153608 mRNA. Translation: AAD41090.1.
AY550970 mRNA. Translation: AAT52216.1.
CR457035 mRNA. Translation: CAG33316.1.
AK311748 mRNA. Translation: BAG34691.1.
AL158032 Genomic DNA. Translation: CAH69949.1.
CH471075 Genomic DNA. Translation: EAX08291.1.
BC030836 mRNA. Translation: AAH30836.1.
RefSeqiNP_005861.2. NM_005870.4.
UniGeneiHs.524899.

Genome annotation databases

EnsembliENST00000607003; ENSP00000475925; ENSG00000150459.
GeneIDi10284.
KEGGihsa:10284.
UCSCiuc001uns.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U96915 mRNA. Translation: AAC51322.1 .
U78303 mRNA. Translation: AAF21220.1 .
AF153608 mRNA. Translation: AAD41090.1 .
AY550970 mRNA. Translation: AAT52216.1 .
CR457035 mRNA. Translation: CAG33316.1 .
AK311748 mRNA. Translation: BAG34691.1 .
AL158032 Genomic DNA. Translation: CAH69949.1 .
CH471075 Genomic DNA. Translation: EAX08291.1 .
BC030836 mRNA. Translation: AAH30836.1 .
RefSeqi NP_005861.2. NM_005870.4.
UniGenei Hs.524899.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2HDE NMR - A 6-149 [» ]
ProteinModelPortali O00422.
SMRi O00422. Positions 6-149.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 115573. 95 interactions.
DIPi DIP-33590N.
IntActi O00422. 12 interactions.
MINTi MINT-5002140.
STRINGi 9606.ENSP00000371973.

Protein family/group databases

TCDBi 3.A.18.1.1. the nuclear mrna exporter (mrna-e) family.

PTM databases

PhosphoSitei O00422.

Proteomic databases

MaxQBi O00422.
PaxDbi O00422.
PeptideAtlasi O00422.
PRIDEi O00422.

Protocols and materials databases

DNASUi 10284.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000607003 ; ENSP00000475925 ; ENSG00000150459 .
GeneIDi 10284.
KEGGi hsa:10284.
UCSCi uc001uns.3. human.

Organism-specific databases

CTDi 10284.
GeneCardsi GC13P021714.
H-InvDB HIX0011163.
HGNCi HGNC:10530. SAP18.
HPAi CAB012273.
HPA011352.
MIMi 602949. gene.
neXtProti NX_O00422.
PharmGKBi PA34940.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG249491.
HOGENOMi HOG000238745.
HOVERGENi HBG003465.
InParanoidi O00422.
KOi K14324.
OrthoDBi EOG79SDZS.
PhylomeDBi O00422.
TreeFami TF313032.

Enzyme and pathway databases

Reactomei REACT_200856. NoRC negatively regulates rRNA expression.
SignaLinki O00422.

Miscellaneous databases

ChiTaRSi SAP18. human.
EvolutionaryTracei O00422.
GeneWikii SAP18.
GenomeRNAii 10284.
NextBioi 38964.
PROi O00422.
SOURCEi Search...

Gene expression databases

Bgeei O00422.
CleanExi HS_SAP18.
Genevestigatori O00422.

Family and domain databases

InterProi IPR017250. Hist_deAcase_cplx_SAP18.
IPR010516. SAP18.
[Graphical view ]
PANTHERi PTHR13082. PTHR13082. 1 hit.
Pfami PF06487. SAP18. 1 hit.
[Graphical view ]
PIRSFi PIRSF037637. HDAC_SAP18. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Histone deacetylases and SAP18, a novel polypeptide, are components of a human Sin3 complex."
    Zhang Y., Iratni R., Erdjument-Bromage H., Tempst P., Reinberg D.
    Cell 89:357-364(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH SIN3A AND HDAC1.
  2. "Characterization of proteins interacting with CAMPGEF."
    Kawasaki H., Housman D.E., Graybiel A.M.
    Submitted (NOV-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "A catalogue of genes in the human dermal papilla cells as identified by expressed sequence tags."
    Kim M.K., Kim Y.H., Seo J.M., Lee H.M., Chung H.J., Sohn M.Y., Hwang S.Y., Im S.U., Jung E.J., Lee H.D., Kim J.C.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Hair follicle dermal papilla.
  4. "Identification of a human cell growth inhibiting gene."
    Kim J.W.
    Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  6. "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: Brain cortex.
  7. "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].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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: Hypothalamus.
  10. Cited for: IDENTIFICATION IN THE ASAP COMPLEX, FUNCTION OF THE ASAP COMPLEX.
  11. "Biochemical analysis of the EJC reveals two new factors and a stable tetrameric protein core."
    Tange T.O., Shibuya T., Jurica M.S., Moore M.J.
    RNA 11:1869-1883(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A MRNA SPLICING-DEPENDENT EXON JUNCTION COMPLEX, IDENTIFICATION IN THE ASAP COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  12. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  13. "Human SAP18 mediates assembly of a splicing regulatory multiprotein complex via its ubiquitin-like fold."
    Singh K.K., Erkelenz S., Rattay S., Dehof A.K., Hildebrandt A., Schulze-Osthoff K., Schaal H., Schwerk C.
    RNA 16:2442-2454(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RNPS1 AND ACIN1, MUTAGENESIS OF ASP-118; THR-121 AND LYS-126.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "Proteins associated with the exon junction complex also control the alternative splicing of apoptotic regulators."
    Michelle L., Cloutier A., Toutant J., Shkreta L., Thibault P., Durand M., Garneau D., Gendron D., Lapointe E., Couture S., Le Hir H., Klinck R., Elela S.A., Prinos P., Chabot B.
    Mol. Cell. Biol. 32:954-967(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  16. "Structure of SAP18: a ubiquitin fold in histone deacetylase complex assembly."
    McCallum S.A., Bazan J.F., Merchant M., Yin J., Pan B., de Sauvage F.J., Fairbrother W.J.
    Biochemistry 45:11974-11982(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 6-149, INTERACTION WITH SUFU.

Entry informationi

Entry nameiSAP18_HUMAN
AccessioniPrimary (citable) accession number: O00422
Secondary accession number(s): B2R494
, Q2TTR4, Q6IAW9, Q8N606, Q9UF14
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: July 1, 1997
Last modified: September 3, 2014
This is version 131 of the entry and version 1 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi