wanglab/gogpt-training-data huggingface dataset:
Protein: U6 snRNA-associated Sm-like protein LSm1 (A0A8I6GHU0)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU365047}. Cytoplasm, P-body {ECO:0000256|RuleBase:RU365047}.
Interaction partners:
Sequence:
HCISSLKLTAFFKRSFLLSPEKHLVLLRDGRTLIGFLRSIDQFANLVLHQTVERIHVGRKYGDIPRGIFVVRGENVVLLGEIDLEKESDTPLQQVSIEEILEEQRVEQQSRLEAEKLKVQALKDRGLSIPRADTLDEY
Protein: Ferric uptake regulation protein (A3N1M0)
Organism: Actinobacillus pleuropneumoniae serotype 5b (strain L20)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364037}.
Interaction partners:
- Flavodoxin
Sequence:
MSEENAKLLKSVGLKVTEPRLTILALMQQHREQMQHFSAEDIYKILLEHGSDIGLATVYRVLNQFEEVGILLRHNFDANKAVFELNVEQEHDHIICMDCGKVFEFKDPDIERRQREISEQHGMKLATHSLYLYAKCSDISHCDSSKDKK
Protein: Single-stranded DNA cytosine deaminase (EC 3.5.4.38) (Activation-induced cytidine deaminase) (AID) (Cytidine aminohydrolase) (Q9WVE0)
Organism: Mus musculus (Mouse)
Function: Single-stranded DNA-specific cytidine deaminase. Involved in somatic hypermutation (SHM), gene conversion, and class-switch recombination (CSR) in B-lymphocytes by deaminating C to U during transcription of Ig-variable (V) and Ig-switch (S) region DNA. Required for several crucial steps of B-cell terminal differentiation necessary for efficient antibody responses. May also play a role in the epigenetic regulation of gene expression by participating in DNA demethylation.
Subcellular location: Nucleus {ECO:0000269|PubMed:20507984}. Cytoplasm {ECO:0000269|PubMed:20507984, ECO:0000269|PubMed:23803409}. Note=Predominantly cytoplasmic. In the presence of MCM3AP/GANP, relocalizes to the nucleus. {ECO:0000269|PubMed:20507984}.
Interaction partners:
- Cytochrome c oxidase subunit 5A, mitochondrial
- Uracil-DNA glycosylase
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome c oxidase subunit 7C, mitochondrial
- Cytochrome b-c1 complex subunit 7
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 8
- G/T mismatch-specific thymine DNA glycosylase
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Core-binding factor subunit beta
Sequence:
MDSLLMKQKKFLYHFKNVRWAKGRHETYLCYVVKRRDSATSCSLDFGHLRNKSGCHVELLFLRYISDWDLDPGRCYRVTWFTSWSPCYDCARHVAEFLRWNPNLSLRIFTARLYFCEDRKAEPEGLRRLHRAGVQIGIMTFKDYFYCWNTFVENRERTFKAWEGLHENSVRLTRQLRRILLPLYEVDDLRDAFRMLGF
Protein: Exocyst complex component 8 (Q8SWU0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, growth cone {ECO:0000256|ARBA:ARBA00004624}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}.
Interaction partners:
Sequence:
MKEFDDFNFSVEKYTKDLTRECVGGSDLQQRKKEIEAYNETTAATLKQTCKKNYMEFIQTAKEISHLESEMYQLSHILIEQRNILATMTDGKTSSHLKAESLEAESTTATEDLENSHATRAVKEMVQGFNGNLEGKTFLNEGALIELDSNDYRPIQRVFFFLFNDVLIVCKVKHDKRLDFLTEYDPKKIAVINIKDLDGVKNAINIITPDGSKIYQSITAAGKTEWIEKLEEAFRFDQQKKPKKGQAPQPPTRAKQQSKASTPEKETTPQSPGQPKSLEDETPEWLSTASEEIQTLVAQRHFEDAQELIKRTQDFLRNENRKKLPLADAIETKVKQQELKLINVLLKELSNSHNRNLQIALRAAKRPLKILVEMGRYRQASATLLKVCAVSLRVAQREARRNNADISELFFCDLTQVACDFLTAFEKQPACVSALVVWCNAELQYFASQLIKHYLTKGTSLESVAKCVERVRKPSTKLTEIGLDISYHLEGLLRTTLESLIEESKERLLDSVGPPRRAGSRTICRPSRT
Protein: Polyadenylate-binding protein 1 (PABP-1) (Poly(A)-binding protein 1) (P61286)
Organism: Bos taurus (Bovine)
Function: Binds the poly(A) tail of mRNA, including that of its own transcript, and regulates processes of mRNA metabolism such as pre-mRNA splicing and mRNA stability. Its function in translational initiation regulation can either be enhanced by PAIP1 or repressed by PAIP2. Can probably bind to cytoplasmic RNA sequences other than poly(A) in vivo. Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs. Involved in translationally coupled mRNA turnover. Implicated with other RNA-binding proteins in the cytoplasmic deadenylation/translational and decay interplay of the FOS mRNA mediated by the major coding-region determinant of instability (mCRD) domain. Involved in regulation of nonsense-mediated decay (NMD) of mRNAs containing premature stop codons; for the recognition of premature termination codons (PTC) and initiation of NMD a competitive interaction between UPF1 and PABPC1 with the ribosome-bound release factors is proposed. By binding to long poly(A) tails, may protect them from uridylation by ZCCHC6/ZCCHC11 and hence contribute to mRNA stability.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11940}. Cytoplasm, Stress granule {ECO:0000250|UniProtKB:P11940}. Nucleus {ECO:0000250|UniProtKB:P11940}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:P11940}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs (By similarity). Shuttles between the cytoplasm and the nucleus (By similarity). During stress and in the absence of DDX3X, localizes to the nucleus (By similarity). At the leading edge of migrating fibroblasts, colocalizes with DDX3X (By similarity). Relocalizes to cytoplasmic stress granules upon cellular stress where it colocalizes with ENDOV (By similarity). {ECO:0000250|UniProtKB:P11940}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Polyadenylate-binding protein-interacting protein 1
- Regulator of nonsense transcripts 1
- Eukaryotic translation initiation factor 4B
- Eukaryotic translation initiation factor 4 gamma 1
- Heat shock cognate 71 kDa protein
- Ataxin 2
- Nonsense-mediated mRNA decay factor
- Nonsense-mediated mRNA decay factor
- Eukaryotic initiation factor 4A-III
Sequence:
MNPSAPSYPMASLYVGDLHPDVTEAMLYEKFSPAGPILSIRVCRDMITRRSLGYAYVNFQQPADAERALDTMNFDVIKGKPVRIMWSQRDPSLRKSGVGNIFIKNLDKSIDNKALYDTFSAFGNILSCKVVCDENGSKGYGFVHFETQEAAERAIEKMNGMLLNDRKVFVGRFKSRKEREAELGARAKEFTNVYIKNFGEDMDDERLKDLFGKFGPALSVKVMTDESGKSKGFGFVSFERHEDAQKAVDEMNGKELNGKQIYVGRAQKKVERQTELKRKFEQMKQDRITRYQGVNLYVKNLDDGIDDERLRKEFSPFGTITSAKVMMEGGRSKGFGFVCFSSPEEATKAVTEMNGRIVATKPLYVALAQRKEERQAHLTNQYMQRMASVRAVPNPVINPYQPAPPSGYFMAAIPQTQNRAAYYPPSQIAQLRPSPRWTAQGARPHPFQNMPGAIRPAAPRPPFSTMRPASSQVPRVMSTQRVANTSTQTMGPRPAAAAAAATPAVRTVPQYKYAAGVRNPQQHLNAQPQVTMQQPAVHVQGQEPLTASMLASAPPQEQKQMLGERLFPLIQAMHPTLAGKITGMLLEIDNSELLHMLESPESLRSKVDEAVAVLQAHQAKEAAQKAVNSATGVPTV
Protein: Histone-lysine N-methyltransferase EZH2 (EC 2.1.1.356) (ENX-1) (Enhancer of zeste homolog 2) (Q61188)
Organism: Mus musculus (Mouse)
Function: Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Displays a preference for substrates with less methylation, loses activity when progressively more methyl groups are incorporated into H3K27, H3K27me0 > H3K27me1 > H3K27me2. Compared to EZH1-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXA7, HOXB6 and HOXC8. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA. Regulates the circadian clock via histone methylation at the promoter of the circadian genes. Essential for the CRY1/2-mediated repression of the transcriptional activation of PER1/2 by the CLOCK-BMAL1 heterodimer; involved in the di and trimethylation of 'Lys-27' of histone H3 on PER1/2 promoters which is necessary for the CRY1/2 proteins to inhibit transcription.
Subcellular location: Nucleus {ECO:0000269|PubMed:12123576}. Chromosome. Note=Localizes to the inactive X chromosome in trophoblast stem cells. {ECO:0000269|PubMed:12123576}.
Interaction partners:
- Transcriptional repressor protein YY1
- Histone-binding protein RBBP7
- Protein Jumonji
- DNA
- Zinc finger protein AEBP2
- Histone-binding protein RBBP4
- Polycomb protein EED
- Polycomb protein Suz12
- DNA
- Histone deacetylase 1
Sequence:
MGQTGKKSEKGPVCWRKRVKSEYMRLRQLKRFRRADEVKTMFSSNRQKILERTETLNQEWKQRRIQPVHIMTSVSSLRGTRECSVTSDLDFPAQVIPLKTLNAVASVPIMYSWSPLQQNFMVEDETVLHNIPYMGDEVLDQDGTFIEELIKNYDGKVHGDRECGFINDEIFVELVNALGQYNDDDDDDDGDDPDEREEKQKDLEDNRDDKETCPPRKFPADKIFEAISSMFPDKGTAEELKEKYKELTEQQLPGALPPECTPNIDGPNAKSVQREQSLHSFHTLFCRRCFKYDCFLHPFHATPNTYKRKNTETALDNKPCGPQCYQHLEGAKEFAAALTAERIKTPPKRPGGRRRGRLPNNSSRPSTPTISVLESKDTDSDREAGTETGGENNDKEEEEKKDETSSSSEANSRCQTPIKMKPNIEPPENVEWSGAEASMFRVLIGTYYDNFCAIARLIGTKTCRQVYEFRVKESSIIAPVPTEDVDTPPRKKKRKHRLWAAHCRKIQLKKDGSSNHVYNYQPCDHPRQPCDSSCPCVIAQNFCEKFCQCSSECQNRFPGCRCKAQCNTKQCPCYLAVRECDPDLCLTCGAADHWDSKNVSCKNCSIQRGSKKHLLLAPSDVAGWGIFIKDPVQKNEFISEYCGEIISQDEADRRGKVYDKYMCSFLFNLNNDFVVDATRKGNKIRFANHSVNPNCYAKVMMVNGDHRIGIFAKRAIQTGEELFFDYRYSQADALKYVGIEREMEIP
Protein: 3-oxo-5-alpha-steroid 4-dehydrogenase 2 (EC 1.3.1.22) (5 alpha-SR2) (SR type 2) (Steroid 5-alpha-reductase 2) (S5AR 2) (Q99N99)
Organism: Mus musculus (Mouse)
Function: Converts testosterone (T) into 5-alpha-dihydrotestosterone (DHT) and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology.
Subcellular location: Microsome membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- 17-beta-hydroxysteroid dehydrogenase type 3
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Aldo-keto reductase family 1 member C18
- Polyprenal reductase
- 17-beta-hydroxysteroid dehydrogenase type 6
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- Estradiol 17-beta-dehydrogenase 2
- Aromatase
- Aldo-keto reductase family 1 member D1
Sequence:
MPIVCHQVPVLAGSATLATMGTLILCFGKPASYGKHSESVSSGVPLLPARIAWFLQELPSFVVSVGMLAWQPRSLFGPPGNVLLGLFSAHYFHRTFIYSLLTRGRPLSAVIFLKATAFCIGNGLLQAYYLVYCAEYPEEWYTDMRFSVGVFFFILGMGINIHSDCMLRQLRKPGEVIYRIPQGGLFTYVSGANFLGEIIEWMGYALATWSVPAFAFAFFTLCFLGMQAFYHHRFYLKMFKDYPKSRKALIPFIF
Protein: Single-stranded DNA-binding protein (SSB) (Q9WZ73)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Interaction partners:
- Small ribosomal subunit protein bS6
- DNA polymerase III subunit alpha
- Small ribosomal subunit protein bS18
- Replication restart protein PriA
- DNA polymerase III, gamma and tau subunit
- DNA polymerase III, gamma subunit-related protein
- Large ribosomal subunit protein uL11
- Large ribosomal subunit protein uL10
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS2
Sequence:
MSFFNKIILIGRLVRDPEERYTLSGTPVTTFTIAVDRVPRKNAPDDAQTTDFFRIVTFGRLAEFARTYLTKGRLVLVEGEMRMRRWETPTGEKRVSPEVVANVVRFMDRKPAETVSETEEELEIPEEDFSSDTFSEDEPPF
Protein: Bis(5'-adenosyl)-triphosphatase (EC 3.6.1.29) (AP3A hydrolase) (AP3Aase) (Adenosine 5'-monophosphoramidase FHIT) (EC 3.9.1.-) (Adenylylsulfatase) (EC 3.6.2.1) (Adenylylsulfate-ammonia adenylyltransferase) (EC 2.7.7.51) (Diadenosine 5',5'''-P1,P3-triphosphate hydrolase) (Dinucleosidetriphosphatase) (Fragile histidine triad protein) (O89106)
Organism: Mus musculus (Mouse)
Function: Possesses dinucleoside triphosphate hydrolase activity (By similarity). Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP (By similarity). Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP (By similarity). Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate (By similarity). Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2 (By similarity). Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate (By similarity). Also catalyzes the ammonolysis of adenosine 5-phosphorofluoridate and diadenosine triphosphate (By similarity). Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5 (By similarity). Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways (By similarity). Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis (By similarity). Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity (By similarity). Functions as tumor suppressor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9699672}. Nucleus {ECO:0000250|UniProtKB:P49789}. Mitochondrion {ECO:0000250|UniProtKB:P49789}.
Interaction partners:
- Deaminated glutathione amidase
- Bis
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- WW domain-containing oxidoreductase
Sequence:
MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFRDLHPDEVADLFQVTQRVGTVVEKHFQGTSITFSMQDGPEAGQTVKHVHVHVLPRKAGDFPRNDNIYDELQKHDREEEDSPAFWRSEKEMAAEAEALRVYFQA
Protein: CheY-P phosphatase CheC (EC 3.-.-.-) (P40403)
Organism: Bacillus subtilis (strain 168)
Function: Involved in restoring normal CheY-P levels following the addition of attractant by increasing the rate of CheY-P hydrolysis. Is only 6% as active as FliY, which indicates that CheC may function after addition of an attractant to cope with increased levels of CheY-P whereas FliY may function constitutively to remove CheY-P around the flagellar switch to maintain an optimal level of CheY-P. In addition, it was shown to prevent methylation of the methyl-accepting chemotaxis proteins (MCPs). Inhibits CheD.
Interaction partners:
- Chemotaxis protein CheA
- Chemoreceptor glutamine deamidase CheD
- Flagellar motor switch phosphatase FliY
- Chemotaxis protein CheY
- Chemotaxis protein CheW
- Protein-glutamate methylesterase/protein-glutamine glutaminase
- Flagellar motor switch protein FliM
- Protein CcdB
- Flagellum site-determining protein YlxH
- Flagellar biosynthesis protein FlhF
Sequence:
MSIFNGIKEEQMDILREVGNIGAGHSASAMAQLLNRKIDMEVPFAKLLSFDELVDFFGGADVPVASIFLRMEGDLTGSMFFIMPFFQAEQFIRELIGNPDFDIEDLGEDHMSSSALHELGNILAGSYLTALADLTKLQLYPSVPEVSLDMFGAVISEGLMELSQVGEHAIVVDTSIFDQSHQQELKAHMFMLPDYDSFEKLFVALGASL
Protein: S-adenosylmethionine synthase 3 (AdoMet synthase 3) (EC 2.5.1.6) (Methionine adenosyltransferase 3) (MAT 3) (Q9SJL8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. Involved in the biosynthesis of lignin.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9LUT2}.
Interaction partners:
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 1
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 2
- Homocysteine S-methyltransferase 3
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase 3, chloroplastic
- Homocysteine S-methyltransferase 2
- Homocysteine S-methyltransferase 1
- At1g77670
- S-adenosylmethionine decarboxylase proenzyme 2
- S-adenosylmethionine decarboxylase proenzyme 1
- S-adenosylmethionine decarboxylase proenzyme 3
Sequence:
METFLFTSESVNEGHPDKLCDQISDAILDACLEQDPESKVACETCTKTNMVMVFGEITTAAKVDYEKIVRSTCREIGFISADVGLDADKCNVLVNIEQQSPDIAQGVHGHLTKKPEDIGAGDQGHMFGYATDETPELMPLTHVLATKLGAKLTEVRKNKTCPWLRPDGKTQVTVEYKNDGGAMIPIRVHTVLISTQHDETVTNDEIAADLKEHVIKPVIPAKYLDDNTIFHLNPSGRFVIGGPHGDAGLTGRKIIIDTYGGWGAHGGGAFSGKDPTKVDRSGAYIVRQAAKSVVAAGLARRCIVQVSYAIGVPEPLSVFVDTYKTGTIPDKDILVLIKEAFDFRPGMMAINLDLKRGGNFRFQKTAAYGHFGRDDPDFTWEVVKPLKPKA
Protein: Mitochondrial proton/calcium exchanger protein (Leucine zipper-EF-hand-containing transmembrane protein 1) (F4IBH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004434}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004434}.
Interaction partners:
- Uncharacterized mitochondrial protein AtMg00860
- Gamma-soluble NSF attachment protein
- TLC domain-containing protein At5g14285
- Receptor-like protein 35
- Prohibitin-4, mitochondrial
- Mitochondrial import inner membrane translocase subunit TIM23-2
- Chaperone protein dnaJ 16
Sequence:
MASRALLRRRSYDVVKSLSEHLPTVQCFSSIERQGQRGYRDFKDVKKKESSVLMEGFYRSRLLQSPSFSNGVGILELPYPLGYRLVFQSMYSSLATANKPDHDKKGEKVTSQTKEASPEECDEAVEGLSLAKAKAKAMKLEESQKSDISIMQRVRLFLLGIGPALRAIASMSREDWAKKLRHWKDEFKSTLQHYWLGTKLLWADVRISVRLLVKLANGKGLSRRERQQLTRTTADIFRLVPVAVFIIVPFMEFLLPVFLKLFPNMLPSTFQDKMKEEEALKRRLNARMEYAKFLQDTVKEMAKEVQTSRSGEIKKTAEDLDGFMTKVRRGVGVSNDEILGFAKLFNDELTLDNINRSRLVNMCKYMGISPFGTDAYLRYMLRKRLQEIKKDDKLIKAEGVESLSEAELRQACRERGMLQLGSVEEMREQLVDWLDLSLNHSVPSSLLILSRSFSMAGKLKPEEAVQATLSSLPDEVVDTVGVTALSSEDSVSERKRKLEYLEMQEELIKEEEEEEEEEMAKMKESASSQKDVALDEMMASTAKDANEQAKAKTLEKHEQLCELSRALAVLASASSVSMEREEFLKLVKKEVDLYNSMVEKGGTDDEEDARKAYLAAREDSDRSAQKAIADKTSSALLDRVETMLQKLEKEIDDVDNKIGNRWRLLDRDYDGKVSPDEVALAAMYLKDTLGKEGIQELIQNLSKDKDGKILVEDLVKLASEIEDAEAEETDEPTTKS
Protein: Enoyl-CoA-hydratase (EC 4.2.1.17) (G4V4T7)
Organism: Amycolatopsis orientalis (Nocardia orientalis)
Function: Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. Catalyzes the syn-addition of a water molecule across the double bond of a trans-2-enoyl-CoA thioester, resulting in the formation of a beta-hydroxyacyl-CoA thioester. Physiologically, DpgD could act as a dehydratase, facilitating the aromatization of the DPA-S-DgpA or DPA-S-CoA intermediate. It can use the non physiological substrates crotonyl-CoA and beta-methylcrotonyl-CoA.
Interaction partners:
- Enoyl-CoA-hydratase
- 3,5-dihydroxyphenylacetyl-CoA synthase
- 
- 3-hydroxybutyryl-CoA dehydrogenase
- 3-hydroxyacyl-CoA dehydrogenase
- 3-hydroxybutyryl-CoA dehydrogenase
- 3-hydroxyacyl-CoA dehydrogenase
- Enoyl-CoA hydratase
Sequence:
MSETRVRYEKKDHVAYVTMDRPAVLNAMDRRMHEELAGIWDDVEADDDVRAVVLTGAGDRAFSVGQDLKERARLNESGVAPTTFGSGGQAGHPRLTDRFTLSKPVVARVRGYALGGGFELVLACDIVIAAEDAVFALPEVRLGLIAGAGGVFRLPRQLPQKVAMGYLLTGRRMDAATALRHGLVNEVVPAAELDQCVADWTDSLVRAAPLSVRAIKEAALRSVDLPLEEAFTTSYHWEERRRRSADAIEGVRAFAEKRDPIWTGQ
Protein: 26.2 kDa heat shock protein, mitochondrial (OsHsp26.2) (Q67X83)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- 19.0 kDa class II heat shock protein
Sequence:
MASTVALKGRPLATLLRQLLAADAPPAATGRPVAAAPAASGKPVTAPAAATATNAASRRLYNTEGAPLRRYDVVDESGTDSGDEYDATDDGRRLTVPFFFSASDVLDPFGAPTSLGRLLALMEDAAVATAAAPGTNGLATAAARRGGWWVAKEDDDAVHLKVSMPGLGKEHVKVWAEQNSLVIKGEGEKDPEDDADAAPPRYTRRIELPADAFKMDKIKAEMKNGVLRVAVPKLKEEERKDVFQVNVE
Protein: AP2-like ethylene-responsive transcription factor TOE2 (Protein TARGET OF EAT 2) (Q9LVG2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity). Regulates negatively the transition to flowering time and confers flowering time delay.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- 1-aminocyclopropane-1-carboxylate oxidase 4
- Squamosa promoter-binding-like protein 9
- Protein TIFY 6B
- Squamosa promoter-binding-like protein 15
- Squamosa promoter-binding-like protein 10
- Squamosa promoter-binding-like protein 3
- Squamosa promoter-binding-like protein 13A
- MADS-box protein SOC1
- Agamous-like MADS-box protein AGL8
- Squamosa promoter-binding-like protein 13B
Sequence:
MLDLNLDVDSTESTQNERDSITVKGVSLNQMDESVTSNSSVVNAEASSCIDGEDELCSTRTVKFQFEILKGGGEEEEEDDDERSAVMMTKEFFPVAKGMNFMDSSAQSSRSTVDISFQRGKQGGDFIGSGSGGGDASRVMQPPSQPVKKSRRGPRSKSSQYRGVTFYRRTGRWESHIWDCGKQVYLGGFDTAHAAARAYDRAAVKFRGLEADINFVIGDYEEDLKQMANLSKEEVVQVLRRQSSGFSRNNSRYQGVALQKIGGWGAQMEQLHGNMGCDKAAVQWKGREAASLIEPHASRMIPEAANVKLDLNLGISLSLGDGPKQKDRALRLHHVPNNSVCGRNTMMENHMAAAACDTPFNFLKRGSDHLNNRHALPSAFFSPMERTPEKGLMLRSHQSFPARTWQGHDQSSGGTAVAATAPPLFSNAASSGFSLSATRPPSSTAIHHPSQPFVNLNQPGLYVIHPSDYISQHQHNLMNRPQPPP
Protein: Adenylate cyclase type 2 (EC 4.6.1.1) (ATP pyrophosphate-lyase 2) (Adenylate cyclase type II) (Adenylyl cyclase 2) (Q08462)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling. Down-stream signaling cascades mediate changes in gene expression patterns and lead to increased IL6 production. Functions in signaling cascades downstream of the muscarinic acetylcholine receptors (By similarity).
Subcellular location: Membrane {ECO:0000269|PubMed:15385642}; Multi-pass membrane protein {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:11549699, ECO:0000269|PubMed:21228062}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:11549699}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Rap guanine nucleotide exchange factor 4
- Rap guanine nucleotide exchange factor 3
- Protein kinase C delta type
- Cannabinoid receptor 1
- Ectonucleoside triphosphate diphosphohydrolase 2
- Bis
- Cancer-related nucleoside-triphosphatase
- Inosine triphosphate pyrophosphatase
Sequence:
MWQEAMRRRRYLRDRSEEAAGGGDGLPRSRDWLYESYYCMSQQHPLIVFLLLIVMGSCLALLAVFFALGLEVEDHVAFLITVPTALAIFFAIFILVCIESVFKKLLRLFSLVIWICLVAMGYLFMCFGGTVSPWDQVSFFLFIIFVVYTMLPFNMRDAIIASVLTSSSHTIVLSVCLSATPGGKEHLVWQILANVIIFICGNLAGAYHKHLMELALQQTYQDTCNCIKSRIKLEFEKRQQERLLLSLLPAHIAMEMKAEIIQRLQGPKAGQMENTNNFHNLYVKRHTNVSILYADIVGFTRLASDCSPGELVHMLNELFGKFDQIAKENECMRIKILGDCYYCVSGLPISLPNHAKNCVKMGLDMCEAIKKVRDATGVDINMRVGVHSGNVLCGVIGLQKWQYDVWSHDVTLANHMEAGGVPGRVHISSVTLEHLNGAYKVEEGDGDIRDPYLKQHLVKTYFVINPKGERRSPQHLFRPRHTLDGAKMRASVRMTRYLESWGAAKPFAHLHHRDSMTTENGKISTTDVPMGQHNFQNRTLRTKSQKKRFEEELNERMIQAIDGINAQKQWLKSEDIQRISLLFYNKVLEKEYRATALPAFKYYVTCACLIFFCIFIVQILVLPKTSVLGISFGAAFLLLAFILFVCFAGQLLQCSKKASPLLMWLLKSSGIIANRPWPRISLTIITTAIILMMAVFNMFFLSDSEETIPPTANTTNTSFSASNNQVAILRAQNLFFLPYFIYSCILGLISCSVFLRVNYELKMLIMMVALVGYNTILLHTHAHVLGDYSQVLFERPGIWKDLKTMGSVSLSIFFITLLVLGRQNEYYCRLDFLWKNKFKKEREEIETMENLNRVLLENVLPAHVAEHFLARSLKNEELYHQSYDCVCVMFASIPDFKEFYTESDVNKEGLECLRLLNEIIADFDDLLSKPKFSGVEKIKTIGSTYMAATGLSAVPSQEHSQEPERQYMHIGTMVEFAFALVGKLDAINKHSFNDFKLRVGINHGPVIAGVIGAQKPQYDIWGNTVNVASRMDSTGVLDKIQVTEETSLVLQTLGYTCTCRGIINVKGKGDLKTYFVNTEMSRSLSQSNVAS
Protein: Intelectin-like protein (Mannose-specific lectin) (P86928)
Organism: Alligator mississippiensis (American alligator)
Function: Binds mannan, mannose and, to a lesser degree, D-lactose, N-acetylgalactosamine, N-acetylglucosamine and beta-D-glucose.
Subcellular location: Secreted {ECO:0000269|PubMed:22085437}.
Interaction partners:
Sequence:
NNQLALKLAATGGSTNSLPALALQNLLNTWEDTSCCSQTSPGQQSWPRDGAQDGLYTLSTADGEIYQTFCDMSTHGGGWTLVASVHENNAHGKCTVGDRWSSQQGNSPLYPEGDGNWANNNIFGSAMGSTSDDYKNPGYYDLQAGDLSVWHVPDRAPLRKEMIESSVLLFYRTGFLSSEGGNLLRLYEKYPVKYGAGSCKVDNGPAVPIVYDFGSAEKTAAYYSPSGRGEFTAGFVQFRVFNNEKAPMALCSGLKVTGCNTEHHCIGGGGFFPEGNPRQCGDFPAFDWDGYGTHQSWSTSREMIESSVLLFYR