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Q8N2W9

- PIAS4_HUMAN

UniProt

Q8N2W9 - PIAS4_HUMAN

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Protein

E3 SUMO-protein ligase PIAS4

Gene

PIAS4

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

Functioni

Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation.7 Publications

Pathwayi

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri311 – 38878SP-RING-typePROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. SUMO ligase activity Source: UniProtKB
  3. ubiquitin protein ligase binding Source: BHF-UCL
  4. zinc ion binding Source: UniProtKB

GO - Biological processi

  1. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
  2. negative regulation of transcription, DNA-templated Source: UniProtKB
  3. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  4. positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage Source: Ensembl
  5. positive regulation of keratinocyte apoptotic process Source: BHF-UCL
  6. positive regulation of protein sumoylation Source: UniProtKB
  7. protein sumoylation Source: UniProtKB
  8. transcription, DNA-templated Source: UniProtKB-KW
  9. Wnt signaling pathway Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Ligase, Repressor

Keywords - Biological processi

Transcription, Transcription regulation, Ubl conjugation pathway, Wnt signaling pathway

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

SignaLinkiQ8N2W9.
UniPathwayiUPA00886.

Names & Taxonomyi

Protein namesi
Recommended name:
E3 SUMO-protein ligase PIAS4 (EC:6.3.2.-)
Alternative name(s):
PIASy
Protein inhibitor of activated STAT protein 4
Protein inhibitor of activated STAT protein gamma
Short name:
PIAS-gamma
Gene namesi
Name:PIAS4
Synonyms:PIASG
OrganismiHomo sapiens (Human)Imported
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 19

Organism-specific databases

HGNCiHGNC:17002. PIAS4.

Subcellular locationi

NucleusPML body 3 Publications
Note: Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies.

GO - Cellular componenti

  1. cytoplasm Source: BHF-UCL
  2. nuclear matrix Source: Ensembl
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi23 – 242LL → AA: Loss of repression of AR- and STAT1-induced transcription; no effect on AR- and STAT1-binding. 2 Publications
Mutagenesisi35 – 351K → R: Complete loss of sumoylation. No enhancement of TCF4 sumoylation. No effect on interaction with TCF4. Colocalizes with SUMO1 in nucleus but concentrated into nuclear granules. 2 Publications
Mutagenesisi128 – 1281K → R: Some loss of sumoylation. 2 Publications
Mutagenesisi342 – 3421C → A: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-347.
Mutagenesisi347 – 3471C → A: Inhibits TCF4 sumoylation. Inhibits beta-catenin-mediated TCF7L2/TCF4 activity. No colocalization with TCF7L2/TCF4 in nuclear punctate structures; when associated with A-342. AR- and STAT1-binding.

Organism-specific databases

PharmGKBiPA134945903.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 510509E3 SUMO-protein ligase PIAS4PRO_0000218982Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine1 Publication
Cross-linki35 – 35Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)
Modified residuei114 – 1141N6-acetyllysine1 Publication
Cross-linki128 – 128Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Sumoylated. Lys-35 is the main site of sumoylation. Sumoylation is required for TCF4 sumoylation and transcriptional activation. Represses LEF1 transcriptional activity. SUMO1 is the preferred conjugate.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ8N2W9.
PaxDbiQ8N2W9.
PRIDEiQ8N2W9.

PTM databases

PhosphoSiteiQ8N2W9.

Expressioni

Tissue specificityi

Highly expressed in testis and, at lower levels, in spleen, prostate, ovary, colon and peripheral blood leukocytes.1 Publication

Gene expression databases

BgeeiQ8N2W9.
CleanExiHS_PIAS4.
ExpressionAtlasiQ8N2W9. baseline and differential.
GenevestigatoriQ8N2W9.

Organism-specific databases

HPAiHPA010598.

Interactioni

Subunit structurei

Interacts with AR, AXIN1, GATA2, LEF1, TP53 and STAT1 (IFNG-induced). Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs) (By similarity). Interacts with TICAM1. Interacts with KLF8; the interaction results in SUMO ligation and repression of KLF8 transcriptional activity and of its cell cycle progression into G1 phase. Interacts with MTA1.By similarity8 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIF1AQ166653EBI-473160,EBI-447269
HTTP428583EBI-473160,EBI-466029
PARP1P098745EBI-473160,EBI-355676
SUMO2P619563EBI-473160,EBI-473220
TADA3O755282EBI-473160,EBI-473249
TP53P046372EBI-473160,EBI-366083

Protein-protein interaction databases

BioGridi119624. 88 interactions.
DIPiDIP-32499N.
IntActiQ8N2W9. 55 interactions.
MINTiMINT-1181821.
STRINGi9606.ENSP00000262971.

Structurei

3D structure databases

ProteinModelPortaliQ8N2W9.
SMRiQ8N2W9. Positions 3-66, 130-407.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 4635SAPCuratedPROSITE-ProRule annotationAdd
BLAST
Domaini119 – 279161PINITPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi20 – 245LXXLL motif

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi464 – 49229Asp/Glu-rich (acidic)Add
BLAST

Domaini

The LXXLL motif is a coregulator signature that is essential for transcriptional corepression.

Sequence similaritiesi

Belongs to the PIAS family.Curated
Contains 1 PINIT domain.PROSITE-ProRule annotation
Contains 1 SAP domain.PROSITE-ProRule annotation
Contains 1 SP-RING-type zinc finger.PROSITE-ProRule annotation

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri311 – 38878SP-RING-typePROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiNOG125513.
GeneTreeiENSGT00550000074410.
HOGENOMiHOG000230594.
HOVERGENiHBG053598.
InParanoidiQ8N2W9.
KOiK16065.
OMAiRICYTDT.
OrthoDBiEOG7HF1JB.
PhylomeDBiQ8N2W9.
TreeFamiTF323787.

Family and domain databases

Gene3Di1.10.720.30. 1 hit.
InterProiIPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view]
PfamiPF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view]
SMARTiSM00513. SAP. 1 hit.
[Graphical view]
PROSITEiPS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q8N2W9 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAELVEAKN MVMSFRVSDL QMLLGFVGRS KSGLKHELVT RALQLVQFDC
60 70 80 90 100
SPELFKKIKE LYETRYAKKN SEPAPQPHRP LDPLTMHSTY DRAGAVPRTP
110 120 130 140 150
LAGPNIDYPV LYGKYLNGLG RLPAKTLKPE VRLVKLPFFN MLDELLKPTE
160 170 180 190 200
LVPQNNEKLQ ESPCIFALTP RQVELIRNSR ELQPGVKAVQ VVLRICYSDT
210 220 230 240 250
SCPQEDQYPP NIAVKVNHSY CSVPGYYPSN KPGVEPKRPC RPINLTHLMY
260 270 280 290 300
LSSATNRITV TWGNYGKSYS VALYLVRQLT SSELLQRLKT IGVKHPELCK
310 320 330 340 350
ALVKEKLRLD PDSEIATTGV RVSLICPLVK MRLSVPCRAE TCAHLQCFDA
360 370 380 390 400
VFYLQMNEKK PTWMCPVCDK PAPYDQLIID GLLSKILSEC EDADEIEYLV
410 420 430 440 450
DGSWCPIRAE KERSCSPQGA ILVLGPSDAN GLLPAPSVNG SGALGSTGGG
460 470 480 490 500
GPVGSMENGK PGADVVDLTL DSSSSSEDEE EEEEEEEDED EEGPRPKRRC
510
PFQKGLVPAC
Length:510
Mass (Da):56,504
Last modified:October 1, 2002 - v1
Checksum:i26AAA18246E1ACE3
GO

Sequence cautioni

The sequence AAD45155.1 differs from that shown. Reason: Erroneous initiation.

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti178 – 1781N → K(PubMed:9724754)Curated
Sequence conflicti179 – 1824SREL → FQGM(PubMed:9724754)Curated
Sequence conflicti179 – 1824SREL → FQGM(PubMed:11388671)Curated
Sequence conflicti482 – 4821E → G in AAH66895. (PubMed:15489334)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077952 mRNA. Translation: AAC36703.1.
BC010047 mRNA. Translation: AAH10047.2.
BC029874 mRNA. Translation: AAH29874.1.
BC066895 mRNA. Translation: AAH66895.1.
AF164437 mRNA. Translation: AAD45155.1. Different initiation.
CCDSiCCDS12118.1.
RefSeqiNP_056981.2. NM_015897.2.
UniGeneiHs.105779.

Genome annotation databases

GeneIDi51588.
KEGGihsa:51588.
UCSCiuc002lzg.3. human.

Polymorphism databases

DMDMi34922831.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF077952 mRNA. Translation: AAC36703.1 .
BC010047 mRNA. Translation: AAH10047.2 .
BC029874 mRNA. Translation: AAH29874.1 .
BC066895 mRNA. Translation: AAH66895.1 .
AF164437 mRNA. Translation: AAD45155.1 . Different initiation.
CCDSi CCDS12118.1.
RefSeqi NP_056981.2. NM_015897.2.
UniGenei Hs.105779.

3D structure databases

ProteinModelPortali Q8N2W9.
SMRi Q8N2W9. Positions 3-66, 130-407.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119624. 88 interactions.
DIPi DIP-32499N.
IntActi Q8N2W9. 55 interactions.
MINTi MINT-1181821.
STRINGi 9606.ENSP00000262971.

PTM databases

PhosphoSitei Q8N2W9.

Polymorphism databases

DMDMi 34922831.

Proteomic databases

MaxQBi Q8N2W9.
PaxDbi Q8N2W9.
PRIDEi Q8N2W9.

Protocols and materials databases

DNASUi 51588.
Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 51588.
KEGGi hsa:51588.
UCSCi uc002lzg.3. human.

Organism-specific databases

CTDi 51588.
GeneCardsi GC19P004007.
HGNCi HGNC:17002. PIAS4.
HPAi HPA010598.
MIMi 605989. gene.
neXtProti NX_Q8N2W9.
PharmGKBi PA134945903.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG125513.
GeneTreei ENSGT00550000074410.
HOGENOMi HOG000230594.
HOVERGENi HBG053598.
InParanoidi Q8N2W9.
KOi K16065.
OMAi RICYTDT.
OrthoDBi EOG7HF1JB.
PhylomeDBi Q8N2W9.
TreeFami TF323787.

Enzyme and pathway databases

UniPathwayi UPA00886 .
SignaLinki Q8N2W9.

Miscellaneous databases

ChiTaRSi PIAS4. human.
GeneWikii PIAS4.
GenomeRNAii 51588.
NextBioi 55429.
PROi Q8N2W9.
SOURCEi Search...

Gene expression databases

Bgeei Q8N2W9.
CleanExi HS_PIAS4.
ExpressionAtlasi Q8N2W9. baseline and differential.
Genevestigatori Q8N2W9.

Family and domain databases

Gene3Di 1.10.720.30. 1 hit.
InterProi IPR023321. PINIT.
IPR003034. SAP_dom.
IPR004181. Znf_MIZ.
[Graphical view ]
Pfami PF14324. PINIT. 1 hit.
PF02891. zf-MIZ. 1 hit.
[Graphical view ]
SMARTi SM00513. SAP. 1 hit.
[Graphical view ]
PROSITEi PS51466. PINIT. 1 hit.
PS50800. SAP. 1 hit.
PS51044. ZF_SP_RING. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: B-cell.
  2. "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, Lung and Skin.
  3. "A putative protein inhibitor of activated STAT (PIASy) interacts with p53 and inhibits p53-mediated transactivation but not apoptosis."
    Nelson V., Davis G.E., Maxwell S.A.
    Apoptosis 6:221-234(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-510, INTERACTION WITH TP53.
  4. "A transcriptional corepressor of Stat1 with an essential LXXLL signature motif."
    Liu B., Gross M., ten Hoeve J., Shuai K.
    Proc. Natl. Acad. Sci. U.S.A. 98:3203-3207(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH STAT1, SUBCELLULAR LOCATION, MUTAGENESIS OF 23-LEU-LEU-24.
  5. "Distinct effects of PIAS proteins on androgen-mediated gene activation in prostate cancer cells."
    Gross M., Liu B., Tan J.-A., French F.S., Carey M., Shuai K.
    Oncogene 20:3880-3887(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AR, TISSUE SPECIFICITY, MUTAGENESIS OF 23-LEU-LEU-24.
  6. "SUMO-1 modification of the C-terminal KVEKVD of Axin is required for JNK activation but has no effect on Wnt signaling."
    Rui H.L., Fan E., Zhou H.M., Xu Z., Zhang Y., Lin S.C.
    J. Biol. Chem. 277:42981-42986(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AXIN1.
  7. "Modification of GATA-2 transcriptional activity in endothelial cells by the SUMO E3 ligase PIASy."
    Chun T.-H., Itoh H., Subramanian L., Iniguez-Lluhi J.A., Nakao K.
    Circ. Res. 92:1201-1208(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GATA2.
  8. "Sumoylation is involved in beta-catenin-dependent activation of Tcf-4."
    Yamamoto H., Ihara M., Matsuura Y., Kikuchi A.
    EMBO J. 22:2047-2059(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUMOYLATION OF TCF4, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-35 AND LYS-128.
  9. "Transactivation properties of c-Myb are critically dependent on two SUMO-1 acceptor sites that are conjugated in a PIASy enhanced manner."
    Dahle O., Andersen T.O., Nordgaard O., Matre V., Del Sal G., Gabrielsen O.S.
    Eur. J. Biochem. 270:1338-1348(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUMOYLATION OF MYB.
  10. "A synergy control motif within the attenuator domain of CCAAT/enhancer-binding protein alpha inhibits transcriptional synergy through its PIASy-enhanced modification by SUMO-1 or SUMO-3."
    Subramanian L., Benson M.D., Iniguez-Lluhi J.A.
    J. Biol. Chem. 278:9134-9141(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUMOYLATION OF CEBPA.
  11. "PIASy represses TRIF-induced ISRE and NF-kappaB activation but not apoptosis."
    Zhang J., Xu L.G., Han K.J., Wei X., Shu H.B.
    FEBS Lett. 570:97-101(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TICAM1.
  12. "SUMO-1 modification of PIASy, an E3 ligase, is necessary for PIASy-dependent activation of Tcf-4."
    Ihara M., Yamamoto H., Kikuchi A.
    Mol. Cell. Biol. 25:3506-3518(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-35 AND LYS-128, FUNCTION IN SUMOYLATION OF TCF4, SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-35 AND LYS-128.
  13. "Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities."
    Shinbo Y., Niki T., Taira T., Ooe H., Takahashi-Niki K., Maita C., Seino C., Iguchi-Ariga S.M.M., Ariga H.
    Cell Death Differ. 13:96-108(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUMOYLATION OF PARK7.
  14. "Sumoylation delimits KLF8 transcriptional activity associated with the cell cycle regulation."
    Wei H., Wang X., Gan B., Urvalek A.M., Melkoumian Z.K., Guan J.-L., Zhao J.
    J. Biol. Chem. 281:16664-16671(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KLF8.
  15. "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].
  16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "SUMOylation and SUMO-interacting motif (SIM) of metastasis tumor antigen 1 (MTA1) synergistically regulate its transcriptional repressor function."
    Cong L., Pakala S.B., Ohshiro K., Li D.Q., Kumar R.
    J. Biol. Chem. 286:43793-43808(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH MTA1.
  18. "DNA damage-inducible SUMOylation of HERC2 promotes RNF8 binding via a novel SUMO-binding Zinc finger."
    Danielsen J.R., Povlsen L.K., Villumsen B.H., Streicher W., Nilsson J., Wikstrom M., Bekker-Jensen S., Mailand N.
    J. Cell Biol. 197:179-187(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN SUMOYLATION OF HERC2 AND RNF168.

Entry informationi

Entry nameiPIAS4_HUMAN
AccessioniPrimary (citable) accession number: Q8N2W9
Secondary accession number(s): O75926, Q96G19, Q9UN16
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2003
Last sequence update: October 1, 2002
Last modified: October 29, 2014
This is version 126 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 19
    Human chromosome 19: 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. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3