wanglab/gogpt-training-data huggingface dataset:
Protein: DUP240 protein DFP3 (P25354)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YCR022C
- Uncharacterized protein YIR020C
Sequence:
MQPHLDNNSNNDDVKLDTLGEQNVLSSAENITLPEDTFKSYMTYLLYEMAHYKPMIFSFLALSVSILIVVIFHNVKACDVVFGFSIFVTSILFLSTLIPFNVYISDEGFRIKLLLEVITHRPAVKGKEWRAITDNMNQYLLDNGLWSTRYYFYSSERCYKFFRFLVKEKPPGVNVNSSVKDATSTQIDAPANEASNEVIKCFSFSSDPIFEAYFVKAVEVEKQAQQEYWRKQYPDADIP
Protein: Alanine dehydrogenase (EC 1.4.1.1) (A0QVQ8)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the reversible reductive amination of pyruvate to L-alanine. Required for proficient utilization of D- or L-alanine as a nitrogen source. May be required for the adaptation from aerobic growth to anaerobic dormancy. It could be involved in the maintenance of the NAD pool during the shift to an anaerobic dormant state in which oxygen as a terminal electron acceptor becomes limiting.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9493394}.
Interaction partners:
- Alanine racemase
- HTH-type transcriptional regulator AldR
- Alanine aminotransferase
- NAD
- NAD
Sequence:
MLVGIPTEIKNNEYRVAITPAGVAELTRRGHEVIIQAGAGEGSAISDRDFKAAGAEIVNTADQVWSEAELLLKVKEPIEPEYSRMRKGQTLFTYLHLAASKPCTDALLASGTTSIAYETVQTAEGALPLLAPMSEVAGRLSAQVGAYHLMRSYGGRGVLMGGVPGVAPAEVVVIGAGTAGYNAARVAAGMGAHVTVFDLNINTLRRVDGEFGGRIETRYSSSLELEEAVKKADLVIGAVLVPGAKAPKLVTNSTVAHMKPGAVLVDIAIDQGGCFEDSRPTTHDEPTFKVHDTIFYCVANMPGAVPRTSTFALTNSTMPYVLKLADKGWQAACASDSALAKGLSTHDGKLLSEAVAKDLDLPFTDAAQFLA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (E7EPP6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRSAVLKSLQPGSLPDCKAALGGSGNISTSPFWSRRHSEGQDTGTRAVLLYGAGARVCGSVTPSSFGGKSAAFGFLQWWAKDSPPRCSVESWQCPLWKTGTWCKPWEKVPMEKPDIGMPEPDAQRFFHQLMAGVVYLHGIGITHRDIKPENLLLDERDNLKISDFGLATVFRYNNRERLLNKMCGTLPYVAPELLKRREFHAEPVDVWSCGIVLTAMLAGELPWDQPSDSCQEYSDWKEKKTYLNPWKKIDSAPLALLHKILVENPSARITIPDIKKDRWYNKPLKKGAKRPRVTSGGVSESPSGFSKHIQSNLDFSPVNSASSEENVKYSSSQPEPRTGLSLWDTSPSYIDKLVQGISFSQPTCPDHMLLNSQLLGTPGSSQNPWQRLVKRMTRFFTKLDADKSYQCLKETCEKLGYQWKKSCMNQVTISTTDRRNNKLIFKVNLLEMDDKILVDFRLSKGDGLEFKRHFLKIKGKLIDIVSSQKIWLPAT
Protein: PNPLA domain-containing protein (Q8T3F2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MTMINSRPELMNLSFSGCGFLCVYHAGVAAAIKEYAPELLQNKILGASAGSIVACGLITGVCISHATSTILKVVSQARSRTFGPLHPEFNLLGIVRDELEVILPPNAYEMCTGRLVISLTRWSDHENVIIDEYRSNADLIDAIMCSCFIPLYCGITPPKFRGVQYIDGGVSDNQPIYDEHTVTVSPFSGESDICPPDWDSGSMLGVDFNGTSIRFTTRNMFRLMACLWPRSTDDLSRMCLQGFGDALRFLTKCGLAPCIRCLTIQTIDANEPAGRVSSECFSENDDAKKVTHVAVPRMKKRASANALNSFRTRGESECETCGDSDIPLEEVNIQSFFPSIMKKPFEDAVAAERSVFQYMMSFRLVRYATTAMGISKFPFDMALAFVKKLVKCEPADLAILTAFFARVHQYLDMVSPPRWIMLKFRGLADFILGEVEKQKSRYTNFSCLVAVAETDSFGSVLASSTMEKEEHKEIELSEDAKKEMILLRERDRRRKLLKKAGKITPNNSENQFDETSVYDVDSFEHVIDFTKSHEALYEFHYRDENQVMKTFGLFTDSQQRPYSSASQHQHHHTKSLGGTSRLVHVPEEDEDAPLSAVSAPAVIFHGGQEIVELGESDKDSGLSGIDTKRKVPDEPTTSKRDACCSPVREFDDQQHQFTSSQPPQPAESSPRRFEKGRSGQRRYIRDTIDSRKPSKKSSMTAAVSVPTMSSDSEGVDGTEKLFLPSRKAWRASSDFENKDSSNKQSDTTTTA
Protein: Transcription factor MTB3 (Basic helix-loop-helix protein 138) (Protein MYC2-TARGETED BHLH 3) (Transcription factor bHLH138) (bHLH transcription factor bHLH138) (A0A3Q7H216)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Transcription factor that negatively regulates jasmonate (JA) signaling. Negatively regulates JA-dependent response to wounding, JA-induced expression of defense genes, JA-dependent responses against herbivorous insects, and JA-dependent resistance against Botrytis cinerea infection. Plays a positive role in resistance against the bacterial pathogen Pseudomonas syringae pv tomato DC3000.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
Sequence:
MAEKFFLKGEDKVNMEGVLGSEAVEFFSWSASNHMLTEFTSSRGDLGVQQALCKIVEGSDWTYAIYWQVAKSKSGKSALIWGDGHCRETKIGQGEGANDSAHQKMMDGNKKKMVLQKIHTCFGGSEDDNIAAKLESVSDVEVFYLTSMYYIFPFDKPSSPSQSFNSARSIWGSDLKGCLEHFQSRSYLAKLARFETLVFVPLKSGVVELGSVKSIPEDQNLIQMVKTSVVVSNPPQPKANTKIFGRELSLGGAKSGPISINFSPKVEEELSFASDSYEVQAALGSSQVYGNSSNGYRSDEGEGKLYKEELDERKPRKRGRKPANGREEALNHVEAERQRREKLNQRFYALRAVVPNISKMDKASLLGDAIAYITDLQARIRVLDAEKEMVGDKQKQQVILEIDFHQRQDDAVVRVGCPLNAHPVSRVLKTFQEHQVVAQESNVSLTENGELVHMFSIRAPGPAAEDLKEKLTAASRFALKTRWSVSVIRLLCFARLFVYEHQCLAGKFALYFVDYTI
Protein: Beta-citrylglutamate synthase B (EC 6.3.1.17) (N-acetyl-aspartylglutamate synthetase B) (NAAG synthetase B) (NAAGS) (EC 6.3.2.41) (Ribosomal protein S6 modification-like protein B) (Q80WS1)
Organism: Mus musculus (Mouse)
Function: Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20643647}.
Interaction partners:
- N-acetylaspartate synthetase
- Glutamate carboxypeptidase 2
- N-acetylaspartylglutamate synthase A
- Aspartoacylase
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- Isocitrate dehydrogenase subunit gamma 1, mitochondrial
- Isocitrate dehydrogenase subunit
- Probable isocitrate dehydrogenase gamma 2, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
Sequence:
MCSSVTGKLWFLTDRRIREDYPQKEILRALKAKCCEEELDFRAVVMDEMVLTVEQGNLGLRISGELISAYPQVVVVRVPTPWVQSDSDITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEAEVLEFPMVVKNTRGHRGKAVFLARDKHHLADLSHLIRHEAPYLFQKYIKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLAIQVSNILGTDVCGIDLLMKDDGSFCVCEANANVGFIAFDKACNLDVAGIIADYAASLLPAGRLTRRMSLLSVVSTASETSEPELGPPASAAVDNMSASSSSVDSDPESTTEREMLTKLPGGLFNMNQLLANEIKLLVE
Protein: Krueppel-like factor 10 (GDNF-inducible factor) (Transcription factor GIF) (mGIF) (Transforming growth factor-beta-inducible early growth response protein 1) (TGFB-inducible early growth response protein 1) (TIEG-1) (O89091)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor which binds to the consensus sequence 5'-GGTGTG-3'. May play a role in the cell cycle regulation (By similarity). Plays a role in the regulation of the circadian clock; binds to the GC box sequence in the promoter of the core clock component ARTNL/BMAL1 and represses its transcriptional activity. Regulates the circadian expression of genes involved in lipogenesis, gluconeogenesis, and glycolysis in the liver. Represses the expression of PCK2, a rate-limiting step enzyme of gluconeogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:20070857}.
Interaction partners:
- Paired amphipathic helix protein Sin3a
- Forkhead box protein P3
Sequence:
MLNFGASLQQASEGKMELISEKPREGMHPWDKAEQSDFEAVEALMSMSCDWKSHFKKYLENRPVTPVSDTSEDDSLLPGTPDLQTVPAFCLTPPYSPSDFEPSQGSNLTASAPSTGHFKSFSDAAKPPGATPFKEEEKNPLAAPPLPKAQATSVIRHTADAQLCNHQSCPVKAASILNYQDNSFRRRTHGNVEATRKNIPCAAVSPNRSKPEPSTVSDGDEKAGAALYDFAVPSSETVICRSQPAPSSPVQKSVLVSSPTVSTGGVPPLPVICQMVPLPANNSLVSTVVPSTPPSQPPAVCSPVLFMGTQVPEGTVVFVVPQPVVQSPRPPVVSPSGTRLSPIAPAPGFSPSAARVTPQIDSSRVRSHICSHPGCGKTYFKSSHLKAHVRTHTGEKPFSCSWKGCERRFARSDELSRHRRTHTGEKKFACPMCDRRFMRSDHLTKHARRHLSAKKLPNWQMEVSKLNDIALPPTPASAQ
Protein: Transcriptional regulatory protein RstA (P52108)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system RstB/RstA.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Sensor protein RstB
- Sensor protein PhoQ
- Sensor histidine kinase CpxA
- KDP operon transcriptional regulatory protein KdpE
- CsgBAC operon transcriptional regulatory protein
- Sensor histidine kinase EnvZ
- Sensor protein BasS
Sequence:
MNTIVFVEDDAEVGSLIAAYLAKHDMQVTVEPRGDQAEETILRENPDLVLLDIMLPGKDGMTICRDLRAKWSGPIVLLTSLDSDMNHILALEMGACDYILKTTPPAVLLARLRLHLRQNEQATLTKGLQETSLTPYKALHFGTLTIDPINRVVTLANTEISLSTADFELLWELATHAGQIMDRDALLKNLRGVSYDGLDRSVDVAISRLRKKLLDNAAEPYRIKTVRNKGYLFAPHAWE
Protein: Periplasmic pH-dependent serine endoprotease DegQ (EC 3.4.21.107) (Protease Do) (P39099)
Organism: Escherichia coli (strain K12)
Function: DegQ could degrade transiently denatured and unfolded proteins which accumulate in the periplasm following stress conditions. DegQ is efficient with Val-Xaa and Ile-Xaa peptide bonds, suggesting a preference for a beta-branched side chain amino acids. Only unfolded proteins devoid of disulfide bonds appear capable to be cleaved, thereby preventing non-specific proteolysis of folded proteins. DegQ can substitute for the periplasmic protease DegP.
Subcellular location: Periplasm {ECO:0000269|PubMed:8576051}.
Interaction partners:
- Outer membrane protein A
- Lon protease
Sequence:
MKKQTQLLSALALSVGLTLSASFQAVASIPGQVADQAPLPSLAPMLEKVLPAVVSVRVEGTASQGQKIPEEFKKFFGDDLPDQPAQPFEGLGSGVIINASKGYVLTNNHVINQAQKISIQLNDGREFDAKLIGSDDQSDIALLQIQNPSKLTQIAIADSDKLRVGDFAVAVGNPFGLGQTATSGIVSALGRSGLNLEGLENFIQTDASINRGNSGGALLNLNGELIGINTAILAPGGGSVGIGFAIPSNMARTLAQQLIDFGEIKRGLLGIKGTEMSADIAKAFNLDVQRGAFVSEVLPGSGSAKAGVKAGDIITSLNGKPLNSFAELRSRIATTEPGTKVKLGLLRNGKPLEVEVTLDTSTSSSASAEMITPALEGATLSDGQLKDGGKGIKIDEVVKGSPAAQAGLQKDDVIIGVNRDRVNSIAEMRKVLAAKPAIIALQIVRGNESIYLLMR
Protein: Enhancer of split m3 protein (E(spl)m3) (HLH-m3) (Q01068)
Organism: Drosophila melanogaster (Fruit fly)
Function: Transcriptional repressor of genes that require a bHLH protein for their transcription. May serve as a transcriptional regulator of the Achaete-scute complex (AS-C) genes. Belongs to notch signaling pathway and depends on Su(H) for transcriptional activation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Enhancer of split mbeta protein
- Enhancer of split M2 protein
- Enhancer of split malpha protein
- Enhancer of split m7 protein
- Enhancer of split mdelta protein
- Sphingosine-1-phosphate lyase
- Protein groucho
Sequence:
MVMEMSKTYQYRKVMKPLLERKRRARINKCLDDLKDLMVECLQQEGEHVTRLEKADILELTVDHMRKLKQRGGLSLQGVVAGVGSPPTSTSTAHVESFRSGYVHAADQITQVLLQTQQTDEIGRKIMKFLSTRLIELQTQLLQQQQQQQQHQQQQIPQSSGRLAFPLLGGYGPAAAAAAISYSSFLTSKDELIDVTSVDGNALSETASVSSQESGASEPVWRPW
Protein: Putative uncharacterized protein YCL021W-A (Q96VH3)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MVLTDAEELRSPVITSDMSFFDLESNHSSDSVHLLCEKYTHKLPIESESQTTFRLAPTKQRLYRQSTLYVPLSLKQRVFLFTERVKSIWAGLPRCKPNKYFKVAFALAVLTPLAIWIFYIDFRVH
Protein: Protein farnesyltransferase subunit beta (FTase-beta) (EC 2.5.1.58) (CAAX farnesyltransferase subunit beta) (Enhanced response to abscisic acid 1) (Ras proteins prenyltransferase subunit beta) (Q38920)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of a farnesyl moiety from farnesyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X (CaaX). The beta subunit is responsible for peptide-binding. Acts as an abscisic acid (ABA) negative regulator by mediating ASG2 farnesylation and consequently monitoring its subcellular localization. Involved in responses to salt (NaCl) and osmotic (e.g. in response to mannitol and PEG) stresses.
Interaction partners:
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- CAAX prenyl protease 2
- CAAX prenyl protease 1 homolog
- Dehydrodolichyl diphosphate synthase 1
- Dehydrodolichyl diphosphate synthase 6
- Dehydrodolichyl diphosphate synthase 5
- Dehydrodolichyl diphosphate synthase 3
- Dehydrodolichyl diphosphate synthase 4
- Dehydrodolichyl diphosphate synthase 8
- Dehydrodolichyl diphosphate synthase 7
Sequence:
MPVVTRLIRLKCVGLRLDRSGLNRRICHGGHGESTRRRVMEELSSLTVSQREQFLVENDVFGIYNYFDASDVSTQKYMMEIQRDKQLDYLMKGLRQLGPQFSSLDANRPWLCYWILHSIALLGETVDDELESNAIDFLGRCQGSEGGYGGGPGQLPHLATTYAAVNALVTLGGDKALSSINREKMSCFLRRMKDTSGGFRMHDMGEMDVRACYTAISVASILNIMDDELTQGLGDYILSCQTYEGGIGGEPGSEAHGGYTYCGLAAMILINEVDRLNLDSLMNWAVHRQGVEMGFQGRTNKLVDGCYTFWQAAPCVLLQRLYSTNDHDVHGSSHISEGTNEEHHAHDEDDLEDSDDDDDSDEDNDEDSVNGHRIHHTSTYINRRMQLVFDSLGLQRYVLLCSKIPDGGFRDKPRKPRDFYHTCYCLSGLSVAQHAWLKDEDTPPLTRDIMGGYSNLLEPVQLLHNIVMDQYNEAIEFFFKAA
Protein: Protein mono-ADP-ribosyltransferase PARP11 (EC 2.4.2.-) (ADP-ribosyltransferase diphtheria toxin-like 11) (ARTD11) (Poly [ADP-ribose] polymerase 11) (PARP-11) (Q9NR21)
Organism: Homo sapiens (Human)
Function: Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins. Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis (By similarity).
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:25673562}. Note=Colocalizes with NUP153 at nuclear pores. {ECO:0000269|PubMed:25673562}.
Interaction partners:
- Zinc finger CCCH-type antiviral protein 1-like
- E3 ubiquitin-protein ligase RNF114
- Protein mono-ADP-ribosyltransferase PARP8
- E3 ubiquitin-protein ligase RNF166
- Protein mono-ADP-ribosyltransferase PARP16
Sequence:
MWEANPEMFHKAEELFSKTTNNEVDDMDTSDTQWGWFYLAECGKWHMFQPDTNSQCSVSSEDIEKSFKTNPCGSISFTTSKFSYKIDFAEMKQMNLTTGKQRLIKRAPFSISAFSYICENEAIPMPPHWENVNTQVPYQLIPLHNQTHEYNEVANLFGKTMDRNRIKRIQRIQNLDLWEFFCRKKAQLKKKRGVPQINEQMLFHGTSSEFVEAICIHNFDWRINGIHGAVFGKGTYFARDAAYSSRFCKDDIKHGNTFQIHGVSLQQRHLFRTYKSMFLARVLIGDYINGDSKYMRPPSKDGSYVNLYDSCVDDTWNPKIFVVFDANQIYPEYLIDFH
Protein: NHP2-like protein 1 homolog (Protein hoi-polloi) (Q9U3Z7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds to the 5'-stem-loop of U4 snRNA and may play a role in the late stage of spliceosome assembly. The protein undergoes a conformational change upon RNA-binding (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Nucleolar protein 58
- U3 small nucleolar RNA-associated protein 15 homolog
- Nucleolar protein 56
- LD17611p
- Lethal
- rRNA 2'-O-methyltransferase fibrillarin
- U4/U6 small nuclear ribonucleoprotein Prp31
- Precursor RNA processing 3, isoform A
- Small ribosomal subunit protein uS12
- Small ribosomal subunit protein eS6
Sequence:
MTEEVNPKAFPLADAQLTAKIMNLLQQALNYNQLRKGANEATKTLNRGLADIVVLAGDAEPIEILLHLPLLCEDKNVPYVFVRSKQALGRACGVSRPIVACSVTTNEGSQLKSQITSIQQEIERLLV
Protein: Cyclic nucleotide-gated channel alpha-1 (CNG channel alpha-1) (CNG-1) (CNG1) (Cyclic nucleotide-gated cation channel 1) (Cyclic nucleotide-gated channel, photoreceptor) (Rod photoreceptor cGMP-gated cation channel subunit alpha) (cGMP-gated cation channel alpha-1) (Q00194)
Organism: Bos taurus (Bovine)
Function: Subunit of the rod cyclic GMP-gated cation channel, which is involved in the final stage of the phototransduction pathway. When light hits rod photoreceptors, cGMP concentrations decrease causing rapid closure of CNGA1/CNGB1 channels and, therefore, hyperpolarization of the membrane potential.
Subcellular location: Cell membrane {ECO:0000269|PubMed:1370452}; Multi-pass membrane protein {ECO:0000269|PubMed:1370452, ECO:0000269|PubMed:25963832}.
Interaction partners:
- Cyclic nucleotide-gated channel beta-1
- Calmodulin
- EF-hand calcium-binding domain-containing protein 11
- CALML5 protein
- Calmodulin-like protein 4
- Cyclic nucleotide gated channel subunit beta 3
- Nuclear transcription factor, X-box binding like 1
- Guanylyl cyclase-activating protein 1
- Guanine nucleotide-binding protein G
- Guanylyl cyclase-activating protein 2
Sequence:
MKKVIINTWHSFVNIPNVVGPDVEKEITRMENGACSSFSGDDDDSASMFEESETENPHARDSFRSNTHGSGQPSQREQYLPGAIALFNVNNSSNKEQEPKEKKKKKKEKKSKPDDKNENKKDPEKKKKKEKDKDKKKKEEKGKDKKEEEKKEVVVIDPSGNTYYNWLFCITLPVMYNWTMIIARACFDELQSDYLEYWLAFDYLSDVVYLLDMFVRTRTGYLEQGLLVKEERKLIDKYKSTFQFKLDVLSVIPTDLLYIKFGWNYPEIRLNRLLRISRMFEFFQRTETRTNYPNIFRISNLVMYIIIIIHWNACVYFSISKAIGFGNDTWVYPDVNDPDFGRLARKYVYSLYWSTLTLTTIGETPPPVRDSEYFFVVADFLIGVLIFATIVGNIGSMISNMNAARAEFQARIDAIKQYMHFRNVSKDMEKRVIKWFDYLWTNKKTVDEREVLKYLPDKLRAEIAINVHLDTLKKVRIFADCEAGLLVELVLKLQPQVYSPGDYICKKGDIGREMYIIKEGKLAVVADDGITQFVVLSDGSYFGEISILNIKGSKAGNRRTANIKSIGYSDLFCLSKDDLMEALTEYPDAKGMLEEKGKQILMKDGLLDINIANAGSDPKDLEEKVTRMESSVDLLQTRFARILAEYESMQQKLKQRLTKVEKFLKPLIDTEFSAIEGSGTESGPTDSTQD
Protein: Cullin-1 (CUL-1) (Abnormal cell lineage protein 19) (Q17389)
Organism: Caenorhabditis elegans
Function: Probable core component of multiple cullin-RING-based SCF (SKP1-CUL1-F-box) E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. As a scaffold protein may contribute to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme. Required for developmentally programmed transitions from the G1 phase of the cell cycle to the G0 phase or the apoptotic pathway.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Skp1-related protein
- RING-box protein 1
- Skp1-related protein
- Cullin-associated NEDD8-dissociated protein 1
- Skp1-related protein
- Skp1-related protein
- Skp1-related protein
- Skp1-related protein
- Skp1-related protein
- Ubiquitin-like protein NEDD8
Sequence:
MTNSEPRRMTCDSEVVWKKLQDGLDVAYRRENMAPKDYMTLYTSVYDYCTSITLSTSRRDGEDGRAESSTPARTAGADFVGHEMYQRVEEYVKAYVIAVCEKGAELSGEDLLKYYTTEWENFRISSKVMDGIFAYLNRHWIRRELDEGHENIYMVYTLALVVWKRNLFNDLKDKVIDAMLELIRSERTGSMINSRYISGVVECLVELGVDDSETDAKKDAETKKLAVYKEFFEVKFLEATRGFYTQEAANFLSNGGNVTDYMIKVETRLNQEDDRCQLYLNSSTKTPLATCCESVLISNQLDFLQRHFGGLLVDKRDDDLSRMFKLCDRVPNGLDELRKSLENHIAKEGHQALERVAMEAATDAKLYVKTLLEVHERYQSLVNRSFKNEPGFMQSLDKAATSFINNNAVTKRAPPQAQLTKSAELLARYCDQLLRKSSKMPDEAELEELQTKIMVVFKYIDDKDVFSKFYTKMFSKRLISELSASDEAEANFITKLKSMCGYEYTARLSKMVNDTQVSKDLTADFKEKKADMLGQKSVEFNVLVLSSGSWPTFPTTPITLPQQLSKTIEIFGQFYNEKFNGRRLTWVYSQSRGEITSTAFPKKYVFTATTAQMCTMLLFNEQDSYTVEQIAAATKMDEKSAPAIVGSLIKNLVLKADTELQKEDEVPMTATVSLNKAYMNKKVRVDLSKFTMKQDAVRDTENVQKNVEEDRKSVISACIVRIMKTRKRVQHQQLMTEVITQLSGRFKPKVEMIKRCIGSLIEKEYMLRTEGQKDLYEYLA
Protein: Alcohol dehydrogenase patD (EC 1.1.1.-) (Patulin biosynthesis cluster protein D) (A0A075TMP0)
Organism: Penicillium expansum (Blue mold rot fungus)
Function: Alcohol dehydrogenase; part of the gene cluster that mediates the biosynthesis of patulin, an acetate-derived tetraketide mycotoxin produced by several fungal species that shows antimicrobial properties against several bacteria. PatD catalyzes the conversion of neopatulin into E-ascladiol. The pathway begins with the synthesis of 6-methylsalicylic acid by the polyketide synthase (PKS) patK via condensation of acetate and malonate units. The 6-methylsalicylic acid decarboxylase patG then catalyzes the decarboxylation of 6-methylsalicylic acid to yield m-cresol (also known as 3-methylphenol). These first reactions occur in the cytosol. The intermediate m-cresol is then transported into the endoplasmic reticulum where the cytochrome P450 monooxygenase patH converts it to m-hydroxybenzyl alcohol, which is further converted to gentisyl alcohol by the cytochrome P450 monooxygenase patI. The oxidoreductases patJ and patO further convert gentisyl alcohol to isoepoxydon in the vacuole. PatN catalyzes then the transformation of isoepoxydon into phyllostine. The cluster protein patF is responsible for the conversion from phyllostine to neopatulin whereas the alcohol dehydrogenase patD converts neopatulin to E-ascladiol. The steps between isoepoxydon and E-ascladiol occur in the cytosol, and E-ascladiol is probably secreted to the extracellular space by one of the cluster-specific transporters patC or patM. Finally, the secreted patulin synthase patE catalyzes the conversion of E-ascladiol to patulin (Probable).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:30680886}.
Interaction partners:
- Chromatin modification-related protein EAF3
- Glutaredoxin
- Glutathione reductase
- Histone acetyltransferase
- histone acetyltransferase
- Histone acetyltransferase ESA1
- FAD-dependent pyridine nucleotide-disulfide oxidoreductase
- Superoxide dismutase
- Superoxide dismutase
- Uncharacterized protein
Sequence:
MASTTPSTYKQAVFKEQGAGLTLEEVALTLPKRDEILVKVEACGVCHSDHFAQTNLMGGGFPLVPGHEIIGRVAAVGEGETVWKEGDRIGGAWHGGHDGTCGACKKGFFQMCDNEQVNGISRNGGYAEYCIIRREAAVHIPDHVNAAKYAPMLCAGVTVFNAMRHMKIPPGELVAIQGLGGLGHLALQYANKFGYRVVALSRDSTKEEFARKLGAHEYIDTSREDPVAALQKLGGASLIVSTAPVPEIINPLIQGLGVMGKLLILSIVGGIEVHTGLLVGKGKSIWSWPSGHATDSEDAIAFADLHGIDCLIEEFPLDKCNEAFAAMMEGSVRFRAVITM
Protein: Importin subunit alpha (Q583S0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Importin beta-1 subunit, putative
- Importin-alpha re-exporter protein, putative
- Ribosomal RNA processing protein 45
- Ran-binding protein 1, putative
- RanBD1 domain-containing protein
- Ribosomal RNA-processing protein 8
- SUMO1/Ulp2, putative
- Nuclear pore complex protein
- Eukaryotic translation initiation factor 3 subunit A
- GTP-binding nuclear protein
Sequence:
MFSGQNEKPKGAKQTPSVRGGAERRQRQMINIRQKAHGELIKHIREEEVAMEGVDGPTVPDPGNVWSYDQRTRPDDVPVQLLPQFVQMVMNGPTDREVYHGTLMVRKLLSVERSPPHEMVAQSGVIPHLVSFLDRADNPELQFEAAWALTNVAAGTSANTMILVEVGAIPRFINLLSSPSPDCRDQGAWAIGNMAGDGVATRDIALQHNAIPAFVNLISDPDQPLSIVRNATWAISNLCRGKPAPPLHYLLPTLPALANLLFHRDLEIATDASWAISYVSDGPHERVQAVLDTGVVPRVIELLAATSIPLQTSCIRTIGNIASGNDAQTQVIINCGVLEKLAPLVTHRKREIRKETCWTISNIAAGNSEQIDALIKSDLFPLVIKCLQGTELDVKKEAVWSIANVTLCGVSPHLYYLLDCGVIPPLCDVLNTHDPKTLTVALEALMGFLQVGEDRVKTGEVQENPVARAIIECGGVDAIERAQSSTDSSIYSIALCLLETFFNVEEEGAPQQFELGMDHGDPNGQPPQGQFDL
Protein: Toll-like receptor 1 (Q5WA51)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGSLTSIYVFACVFLSILWNNIQPTVENKITANYSGHLLTEVPKNIPVHTHILDLSHNSISEITNFRFTSLSDLQVLNLSHNLITELDFSAFMFNQDLEYLDLSHNNIWTAYCQLLARLRHLDLSFNKFTVLPICQEFGIMFHLEYLGLSAMMIRRSDFRYVAHLQLDTVFLTLEDFSLYEPLSLTALNTRSLHIVFATNQNFNFSLLYDGMSTSEKLKIVNLRYTLSHKDFPSPSLELQKKIKATDLMLDTVDLEWTVILQIFLLVWDSSVEHLTVRNLIFRGPVVELTEYKHVPLLRSLEQLLSLGSSMKALTLERVRNKLYYFNQEILYRQFSEMNIDSLTIHDACMPHMLCPKKPSSFQYINFSRNALTDELFQNCDTLANLKILILHRNKFESLSKVSFMTSRMKSLRYLDMSSNLLRNSRAEGRCQWADSLAELDLSSNQLTEAVFECLPANINKVDLQNNQIANVPKGITELHSLQELNLASNRLADLPGCRAFTGLEILNIERNLILTPSADFFETCPSVKELQAGQNPFKCSCELQDFLRLERQSGGKLSGWPEAYVCKYPEDLSGTQLKDFHLTELACNTTLLLVTALLLTLVLVAVVAFLCIYLDVPWYVRMLWQWTQTKRRAWHDCPEERETALQFHAFISYSERDSLWVKNELIPNLEKGEGCIQLCQHERNFIPGKSIVENIINCIEKSYKSIFVLSPNFVQSEWCHYELYFAHHRLFSENSNSLILILLEPIPSYVIPARYHKLKALMAKRTYLEWPKERSKHALFWANLRAAVNIKLPTSFETDEEQSDVTSTSSITQRLIK
Protein: MYB1 (Myb-like transcription factor 1) (Transcription repressor MYB6-like) (Q43436)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Guanine nucleotide-binding protein alpha subunit
Sequence:
MGRSPCCEKAHTNKGAWTKEEDQRLINYIRVHGEGCWRSLPKAAGLLRCGKSCRLRWINYLRPDLKRGNFTEEEDELIIKLHSLLGNKWSLIAGRLPGRTDNEIKNYWNTHIKRKLISRGIDPQTHRPLNQTANTNTVTAPTELDFRNSPTSVSKSSSIKNPSLDFNYNEFQFKSNTDSLEEPNCTASSGMTTDEEQQEQLHKKQQYGPSNGQDINLELSIGIVSADSSRVSNANSAESKPKVDNNNFQFLEQAMVAKAVCLCWQLGFGTSEICRNCQNSNSNGFYSYCRPLDS
Protein: Sterol carrier protein 2 (AtSCP2) (Q9FMN0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Enhances the transfer of lipids between membranes in vitro. Active on phosphatidylcholine (PC), 1-palmitoyl 2-oleoyl phosphatidylcholine (POPC) and ergosterol, and, to a lower extent, dimyristoyl phosphatidic acid, stigmasterol, desmosterol, beta-sitosterol and steryl glucoside. Inactive or poorly active on palmitic acid, stearoyl-coenzyme A, cholesterol, glucosylceramide and ceramide. Required during seeds and seedlings development.
Subcellular location: Peroxisome {ECO:0000269|PubMed:15456765}.
Interaction partners:
- Peroxisome biogenesis protein 5
- Peroxisomal membrane protein PEX14
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- 2-oxoisovalerate dehydrogenase subunit alpha 1, mitochondrial
- Mannose-P-dolichol utilization defect 1 protein homolog 2
- Peroxisome biogenesis factor 10
- Acetyl-CoA acetyltransferase 1
- Acetyl-CoA acetyltransferase 2
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- Pentatricopeptide repeat-containing protein At3g61360
Sequence:
MANTQLKSDAIMDMMKEHLSTDAGKEVTEKIGLVYQINIAPKKLGFEEVTYIVDLKKGEVTKGKYEGGKVDATFSFKDDDFVKVATGKMNPQMAFIRGAMKIKGSLSAAQKFTPDIFPKPSKL