wanglab/gogpt-training-data huggingface dataset:
Protein: Pumilio homolog 3 (X1WGX5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Inhibits the poly(ADP-ribosyl)ation activity of PARP1 and the degradation of PARP1 by CASP3 following genotoxic stress (By similarity). Binds to double-stranded RNA or DNA without sequence specificity (By similarity). Involved in development of the eye and of primordial germ cells.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q15397}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q15397}. Chromosome {ECO:0000250|UniProtKB:Q15397}.
Interaction partners:
- Ribosome production factor 2 homolog
- Ribosome biogenesis protein BRX1 homolog
- Nucleolar GTP-binding protein 1
- EBNA1-binding protein 2.
- RNA-binding motif protein 28.
- MKI67 FHA domain-interacting nucleolar phosphoprotein
- RNA helicase.
- Ribosomal L1 domain-containing protein 1
- Nucleolar protein 58
- NOC2-like nucleolar-associated transcriptional repressor
Sequence:
MEGKPRKKSFTPRDGKKPSFKSKGKPGGKPQGKRPFKPHNNDKGKGFRKSGGEGGPQKFNRKPTDGKFAKKRKFPGDRIKQEEGDERKKPKWDEFKQKKKELKLNRQQTDRKESYQIVSRAKQVWEMVRRKDCDKQKRTKLMKELQDLVKGKIKTIAFAHDSTRVLQCFIQFGSDKQRKEVFDELKEHIVELSKSKYARNIVKKFLMYGSKEQVGEVMLAFKGKVRQMLRHSEASSVVEYAYNDKAILSQRLMLTEELYGNTFTVLKSSVCPTLEKVLEANPGKLESILDEMKQILTPMAQKEAVIKHSLVHKVFLDFFEHAPDKQRTEMIESIREAVVYMAHTHDGARVTMHCLWHGTTKDRKVIVKTMKSYIAKFAMGEYAHLVLLAAFDCIDDTKLVKQIIISEMVSSLSEIISNKHGKKVLLYLLSPRDPAHLLPEIIQVLEKGDGNAHSKKDVLIRRKELLEAASPSLLNHLCENAQSMVMDKSCCVVVSDILGSAVGDLRPAMEAVAALADGPLIPGGKDGQLHMAEHPAGHLVLKWLIEQDTKMKDTEREERFSRILLEKVGLENLKTWASVNRGAIILCCLLQSADESVAEEVKAMLKSSIPELQRLQNSKGIEVLLEKLA
Protein: glutamate decarboxylase (EC 4.1.1.15) (F4J6E0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable GABA transporter 2
- Aluminum-activated malate transporter 8
- Aluminum-activated malate transporter 7
- Gamma-aminobutyrate transaminase POP2, mitochondrial
- GABA transporter 1
Sequence:
MTGTGQKLNIRRRVGEVNSLSFCCLSPTPTSLDNRCVNMIANLFHAPVGQDEAVISCGIVASSESAGLAFKMKWQHRRKAQGLPIDKPNIVTGVNVQVCWEKFARYFEVELKEVKLSEDYYVMDPAKAVEMVDENSICVAAILGSTFTGEFEYVKLLNDLLAEKNAKTAWETPIHVDAASGGFIASMGEEYQCQ
Protein: Phospholipase A2-gamma (EC 3.1.1.4) (Secretory phospholipase A2-gamma) (AtsPLA2-gamma) (Q9M0D7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. Releases lysophospholipids (LPLs) and free fatty acids (FFAs) from membrane phospholipids in response to hormones and other external stimuli. Plays a role in pollen development and germination and tube growth.
Subcellular location: Secreted. Golgi apparatus, trans-Golgi network. Endoplasmic reticulum.
Interaction partners:
- Myosin-7
- Myb family transcription factor PHL6
- Phospholipase SGR2
- Lecithin-cholesterol acyltransferase-like 4
- Phospholipase A I
- Patatin-like protein 5
- Protein HOMOLOG OF MAMMALIAN LYST-INTERACTING PROTEIN 5
- Probable inactive patatin-like protein 9
- Patatin-like protein 7
Sequence:
MITGLALSRVAFGLTAFLLLAVVSSQEKCSNTCIAQNCNSLGIRYGKYCGIGYFGCPGEPPCDDLDACCMTHDNCVDLKGMTYVNCHKQFKRCVNKLSKSIKHSNGEKIGFSTQCPYSIVIPTVFNGMDYGIFFSGIGNIFNPPVLGSVPVVEVDLARSKVDTKDGLGTKLGLQTKEGSKVSASLNI
Protein: PHO85 cyclin-like protein psl1 (O42979)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Cyclin partner of the cyclin-dependent kinase (CDK) pef1 (PHO85 homolog).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum.
Interaction partners:
- Probable proteasome subunit beta type-1
- Serine/threonine-protein kinase pef1
- ATP-dependent DNA helicase II subunit 2
- Glycerophosphocholine phosphodiesterase gde1
- Uncharacterized protein C19A8.11c
Sequence:
MSLAFTLLTSKDNTDEDEEHLELSSFNQEKLLEMISVFLSRLTRLNDSKQEATESDQIPLSPTSLKNPCLIFSAKNVPSISIQAYLTRILKYCPATNDVFLSVLIYLDRIVHHFHFTVFINSFNIHRFLIAGFTAASKFFSDVFYTNSRYAKVGGIPLHELNHLELSFFVFNDFNLFISLEDLQAYGDLLLSWYRQNGQNYNPTDVSCSIESPISHTPQQNQQDEQPRRPIMDRRLLSSHSIG
Protein: Transcription factor AP-2 beta (O93346)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Potassium channel tetramerization domain containing 1.
- YEATS domain-containing protein 4
- TF_AP-2 domain-containing protein.
Sequence:
MLWKLVENVKYEDIYEDRHDGVPSHSSRLSQLGSVSQGPYSSAPPLSHTPSSDFQPPYFPPPYQPLPYHQSQDPYSHVNDPYSLNPLHQPQQHPWGQRQRQEVGSDTGSLLPQPRAALPQLSGLDPRRDYHSVRRPDVLLHSAHHGLDSGMGDSLSLHGIGHPGMEEVQSVEDANNSGMNLLDQSVIKKVPVPPKSVTSLMMNKDGFLGGISVNTGEVFCSVPGRLSLLSSTSKYKVTVGEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLRERLEKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYICETEFPAKAVSEYLNRQHTDPSDLHSRKNMLLATKQLCKEFTDLLAQDRTPIGNSRPTPILEPGIQSCLTHFSLITHGFGAPAICAALTALQNYLTEALKGMDKMFLNNNTANRHTSGEGPGSKTGDKEEKHRK
Protein: Dishevelled associated activator of morphogenesis, isoform D (M9MSM5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Segment polarity protein dishevelled
- Ras-like GTP-binding protein Rho1
- Profilin
- Frizzled
- Vang-like protein
- Protein prickle
- Diego, isoform A
- Rho-associated protein kinase
- Cdc42 homolog
- Protocadherin-like wing polarity protein stan
Sequence:
MSSMNQMSVLMDKINTTLQSCPIVCINEPDTHSANTEILQTSPESTLEKPKAAPSGGASTSVTSLNGSCIAINGGIGEGATATASAATSTAAGVTKITITSDNGNGNASTSTKAPTTGSSIDGYKNSSLVSITSLNSCSDLSQGSTATLPISSNSCSGNNVSRHPLSNNNSGSDTSSNNFQERFDFEHWKGLLSDYNCFHGLYRYWTQCSGRSSSANDNGGGSDQQQSQSNHENGLGSEAGSFYTHNILGYTFGYPFGLKEDLDGSGNCNSNCNGSSNTNGLGLRKWLSGNTSSNETPLQKHYRHQQKKKMPGFRGRRVWCGCFKDDEPPEICVVEGAFTLQTLTPTQPMPSVDELDTKFAELVEELDLTAPNKEAMLSLPAQKKWQIYCSRKLPLDAADGPDAAAVTQPPTAEHYIERLKELVVHISLSPEDSPSHELGNRLDGHAAFVDALKTALRTSTHSFVLRFVELDGLPALLDLLLQLDIRVANSPLHTSLIGCIKALMNNSMGRAHVLAHPTAIDTIARSLAADNIRTKIAALEILGAVCLVPGGHRKVLQAMLHFQVFATERTRFQSIVNDLDRSTYAYRDNVNLKTALMSFVNAVLNYGPGQENLEFRLHLRYEFLMLGIQPVIDKLRTHENETLDRHLDFFEMVRAEDEKEFARRFKEEHVDTKSAGSMFELLRRKLSHSPAYPHMLSLLQHMLLLPYTGHCTEHWLLIDRVVQQIVLQVEQRPNSDLIVDPDDPEKQLKLAAESPVHDPDVAPLQIDVAKLVRLLVKEEQLTQARKRADELERENFDVQSRLAKKEQELDLRMQEKEDLETGLARMRERLEKESAQHSQAVQRAQTAEMRAEDLQHRLISEQQERARLERLVTEGSIPDDQKVAGLTGCNGAVSPPPAPPMLKAIPPPPPPMAPSMMPPPPPPCPGAPPPPPSMAQTMAPAPPKVDLPKKNVPQPTNPLKSFNWSKLPDAKLQGTVWSELDESKLYNNMELESIDKLFSAYQKNGVSATDGSYEDLRVTGKAAKQKVLSVIDGRRAQNCTILLSKLKMSDMEISKAILSMDSNEQLQLDMVEQLLKFTPSAEERALLDEHSEDIESLARADRFLYEISKIPHYEQRLKSLHYKKRFMLTINDLVPRITSVMEASREVARSRRLRKLLELVLALGNYMNRGARGNASGFRLASLNRLADTKSSAAKGTTLLHYLVQVIERKFKDLLKLEDDIPHVREASKVSLGEMDKDIQMLRTGLADVAREIEFHRSSGPAQQGDRFLPVMREFHAQASVRFAELEDKFQDMKTRFDRAVRLFGEDGSVLQPDEFFGIFDSFLAAFAEARHDNESFRRRQEEEEKRAKQEAELKKRTIERKNKTGLMTSVARNLGLKSGSSNGDPDSPAKGGDNKGEFDDLISALRTGDVFGEDMAKFKRSRKARVLNGGGSSTGHTSPPRHGSLQREESGRERERTVRRQ
Protein: Juvenile hormone acid O-methyltransferase (EC 2.1.1.325) (Juvenile hormone acid methyltransferase) (DmJHAMT) (Q9VJK8)
Organism: Drosophila melanogaster (Fruit fly)
Function: O-methyltransferase that transfers a methyl group from S-adenosyl-L-methionine (SAM) to the carboxyl group of juvenile hormone acids to produce active juvenile hormones in the corpora allata, the last step during juvenile hormone biosynthesis. Also able to methylate farnesoate to methyl farnesoate.
Interaction partners:
- Epoxide hydrolase
- Epoxide hydrolase
- Epoxide hydrolase
- aldehyde dehydrogenase
- Carboxylic ester hydrolase
- Uncharacterized protein, isoform B
- Rab3 interacting molecule, isoform F
- Hydroxymethylglutaryl-CoA synthase
- Krueppel homolog 1
- Farnesyl pyrophosphate synthase
Sequence:
MNQASLYQHANQVQRHDAKLILDEFASTMQWRSDGEDALLDVGSGSGNVLMDFVKPLLPIRGQLVGTDISSQMVHYASKHYQREERTRFQVLDIGCERLPEELSGRFDHVTSFYCLHWVQNLKGALGNIYNLLKPEGGDCLLAFLASNPVYEVYKILKTNDKWSTFMQDVENFISPLHYSLSPGEEFSQLLNDVGFVQHNVEIRNEVFVYEGVRTLKDNVKAICPFLERMPADLHEQFLDDFIDIVISMNLQQGENNEDQKFLSPYKLVVAYARKTPEFVNNVFLEPTHQNLVKGIN
Protein: Basic helix-loop-helix (BHLH) DNA-binding superfamily protein (F4I3E6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Berberine bridge enzyme-like 28
- DEAD-box ATP-dependent RNA helicase 20
- Putative defensin-like protein 15
Sequence:
MRGTTDEEDGVMNFSDVLMMSDDVLSSGEVEEDSFGFRFTGNDAPQMLCFGGGNQNDTDLLFSQPSFSPASPLSSRNNACVVNDQSFRSNKKTGSADGHDRVCDPKPGKRCKRDQKKSSLGNAKVKKEKVGEKITTLQHLVSPYGKTDAASVLHETMGYIKFLQDQVQVLSTPYFKHNPLDDEDTGEVNPTMKVKELRSNGLCLVPLAWTVHVANTNGADLWSSAILSPLTSHTNSEPVEIVEVKSHKDK
Protein: 2-(3-amino-3-carboxypropyl)histidine synthase subunit 1 (EC 2.5.1.108) (Diphthamide biosynthesis protein 1) (Diphtheria toxin resistance protein 1) (Ovarian cancer-associated gene 1 protein homolog) (S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase 1) (Q5NCQ5)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase (By similarity). Acts as a tumor suppressor.
Subcellular location: Nucleus {ECO:0000269|PubMed:11527402}. Cytoplasm {ECO:0000269|PubMed:11527402}. Note=Punctate, primarily perinuclear localization.
Interaction partners:
- 2-
- Diphthamide biosynthesis protein 3
- Elongation factor 2
- Diphthine methyltransferase
- Diphthine methyl ester synthase
- Esterase OVCA2
- DnaJ homolog subfamily C member 24
- Diphthine--ammonia ligase
- Elongation factor G, mitochondrial
Sequence:
MAALVVSETAEPGSRVGPGRGRISRGRLANQIPPEVLNNPQLQAAVQVLPSNYNFEIPKTIWRIQQAQAKKVALQMPEGLLLFACTIVDILERFTEAEVMVMGDVTYGACCVDDFTARALGVDFLVHYGHSCLVPMDTSVQDFRVLYVFVDIRIDTAHLLDSVRLTFTPGSSLALVSTIQFVSTLQAAAQELKADYHISVPQCKPLSPGEILGCTSPRLSKEVEAVVYLGDGRFHLESVMIANPNIPAYRYDPYGKVLSREYYDHQRMQATRQEAIAAARSAKSWGLILGTLGRQGSPKILEHLESQLRNLGLPFVRLLLSEIFPSKLSLLPEVDVWVQVACPRLSIDWGSAFPKPLLTPYEAAVALKDISWQQPYPMDFYSGSSLGPWTVNYGRDRAPRGLCQPASDKVQQGSRGGSPAPACESCNCADQKATSPAP
Protein: Nuclear RNA-binding protein sart-3 (U4/U6 snRNA-associated-splicing factor) (Q17430)
Organism: Caenorhabditis elegans
Function: U6 snRNP-binding protein that functions as a recycling factor of the splicing machinery. Promotes the initial reassembly of U4 and U6 snRNPs following their ejection from the spliceosome during its maturation.
Subcellular location: Nucleus, nucleoplasm {ECO:0000305|PubMed:25753661}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm7
- Probable U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-specific terminal uridylyltransferase
- U6 snRNA-associated Sm-like protein LSm3
- U4/U6 small nuclear ribonucleoprotein Prp31
- Actin maturation protease
Sequence:
MSDVDMESGSDDSGMEDLDEEIQKIKQKMIDDSQSVVLANQLLILLRKNGDFDELDIKRRQFVEWAPLNPLNWKNWIEDFQNRKPEPSVAEVEEMFEKALFDENDVTIWVERAMYAYKVANDKNKKEDFKFCRDVCSKALENLGTRYDSGGHIWLIFLEYEMSYLKNSMNAPDYQRLADQVFALFERALHCPTDQLEDVYVLAEQFCTEFKQHHKLEELKKTYNSTMRQKEQLSKFEELIQQEETKKQGLKQFFDHEKKSGIPSRIKMAHERLVSELDDDEEAWIAYGAWADIELKLPQVAVKVYSRALRHCPYSFVLHQQALLAFERDRRPNEEIDALWERARSNVINSAEEGRSLYRTYAFLLRRRIHLTGSSDYSPMAEVFDEGAALLREWFSMAWDTTADYRQMQAYFYASLMKNMDKCRNIWNDILASGFGRFAGKWIEAVRLERQFGDKENARKYLNKALNSVSDNINEIYMYYVQFEREEGTLAELDLVLEKVNSQVAHRAIRPQKKVSEKPAPAPKSKQDHIQKRTSGGEPIVKKVKGDDGGFKAPLPPSNAKSSSAVSSSNASSTPAPGSFAVQKAAPGTEDARTIFVSNLDFTTTEDEIRQAIEGVASIRFARKANSDLVHRGFAYVVMENDQKAQQALLKDRVPVKGRPMFISANDPEKRVGFKFSTTLEKSKVFVRNVHFQATDDELKALFSKFGTVTSVRRVTHKDGKPKGIAFVDFDTEASAQKCVASGDKLMLRERELEVALSNPPVKKDKSHGKPAAIGASLEEDGPRKGHAAKLQLVPRAITNKTPQITARLDAMDVSEGTSTSQPLSNDQFRKMFMKN
Protein: Metalloendopeptidase (EC 3.4.24.-) (Q49II5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EHEAKLQRLREELSRPVIEAHHHQSHHQKQAQHRQHHQSHHRKKHRRQQQHHRRRGQSTTQYVNHSPPGFNQSQQAQQQSVPEMDLLKAETSKDEEPLRHRVARAVTAKKERIWDYGVIPYEIDGNFSGIHKALFKLAMRHWENSTCIKFVERDPEIHPNYIVFTVRSCGCCSFVGKRGNGPQAISIGRNCDKFGIVVHELGHVVGFWHEHTRPDREKHVVIEHNNIMKGQDYNFNMLSPDEVDSLGMAYDYDSIMHYARNTFSKGTYLDTILPIEMKGRKRPEIGQRLRLSQGDIAQANLLYKCPKCGRTFQESSGIFASPSHYTAGALSNETEHCEWRITATYGERVELKLENMNIFKSNNCETDYLEIRDGYFEKSPLIGRFCGKVDKEVIRTESSRMLLTYVNTHRIEGFRGFKAEFD
Protein: E3 ubiquitin-protein ligase SINAT4 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase SINAT4) (Seven in absentia homolog 4) (Q9STN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates. Modulates directly the ubiquitination and proteasomal-dependent degradation of FREE1, a component of the ESCRT-I complex. Modulates directly the ubiquitination and proteasomal-dependent degradation of ELC/VPS23A, a component of the ESCRT-I complex.
Subcellular location: Endosome, multivesicular body {ECO:0000269|PubMed:32753431, ECO:0000269|PubMed:32786047}. Cytoplasmic vesicle, autophagosome {ECO:0000269|PubMed:32753431}.
Interaction partners:
- Eukaryotic aspartyl protease family protein
- Transport/golgi organization-like protein
- At5g40190
- Myosin heavy chain-like protein
- Thioredoxin-like 4, chloroplastic
- F-box protein SKIP31
- O-fucosyltransferase 7
- Putative RING zinc finger protein
- Ubiquitin-conjugating enzyme E2 28
Sequence:
METDSMECVSSTGNEIHQNGNGHQSYQFSSTKTHGGAAAAAVVTNIVGPTATAPATSVYELLECPVCTYSMYPPIHQCHNGHTLCSTCKVRVHNRCPTCRQELGDIRCLALEKVAESLELPCKFYNLGCPEIFPYYSKLKHESLCNFRPYSCPYAGSECGIVGDIPFLVAHLRDDHKVDMHAGSTFNHRYVKSNPREVENATWMLTVFHCFGQYFCLHFEAFQLGMGPVYMAFLRFMGDEEDARSYSYSLEVGGSGRKLTWEGTPRSIRDSHRKVRDSNDGLIIQRNMALFFSGGDRKELKLRVTGKIWKEQHSPDSGLSIPNLSSS
Protein: Olfactory receptor (Q920P1)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
Sequence:
MILSEKNNSGIIFTLLGFSDYPDLKVPLFLVFLVIYSITVVGNIGMILVIRINPQLHSPMYFFLSHLSFVDFCYSSIIAPKMLVNLVAKDITISFVECIVQYFLFCVFVVTEAFLLVVMAYDRFVAICNPLLYTVAMSQKLCITLVVGSYAWGFTCSLTLTCSTVQLSFHGVNRIDHFFCELSSLLALSSSDTLISQLLLFVFATFNAVSTLLLILLSYLFIVVTVLKMRSASGRRKAFSTCASHLAAITIFHGTILFLFCVPNSKNSRLTVKVGSVFYTVVIPMLNPIIYSLRNKDVQDTIRKIMTLISCVKNDRHN
Protein: AP-4-A phosphorylase (EC 2.7.7.53) (ATP adenylyltransferase) (Diadenosine 5',5'''-P1,P4-tetraphosphate phosphorylase) (AP,A phosphorylase) (P9WMK9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catabolizes diadenosine 5',5'''-P1,P4-tetraphosphate (Ap4A) into ADP and ATP. It does not catalyze the reverse phosphorolysis reaction. The optimum substrates are dinucleoside polyphosphates containing four or five phosphate residues.
Interaction partners:
- Phosphatidylinositol phosphate synthase
- Phosphatidylinositol mannoside acyltransferase
- Threonine--tRNA ligase
- Phosphatidyl-myo-inositol mannosyltransferase
- Probable conserved membrane protein
- Bifunctional enzyme CysN/CysC
- Sulfate adenylyltransferase subunit 2
- Conserved protein
- Conserved protein
- DNA-directed RNA polymerase subunit omega
Sequence:
MSDEDRTDRATEDHTIFDRGVGQRDQLQRLWTPYRMNYLAEAPVKRDPNSSASPAQPFTEIPQLSDEEGLVVARGKLVYAVLNLYPYNPGHLMVVPYRRVSELEDLTDLESAELMAFTQKAIRVIKNVSRPHGFNVGLNLGTSAGGSLAEHLHVHVVPRWGGDANFITIIGGSKVIPQLLRDTRRLLATEWARQP
Protein: GPI ethanolamine phosphate transferase 3 (EC 2.-.-.-) (Glycosylphosphatidylinositol-anchor biosynthesis protein 13) (Q07830)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI third mannose which links the GPI-anchor to the C-terminus of the proteins by an amide bond. Involved in cell wall biosynthesis.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Glycosylphosphatidylinositol anchor biosynthesis protein 11
- GPI mannosyltransferase 3
- GPI-anchor transamidase
- GPI transamidase component GPI16
- GPI transamidase component GAA1
- GPI transamidase component GPI17
- GPI transamidase component GAB1
- GPI mannosyltransferase 2
- Phosphatidylinositol N-acetylglucosaminyltransferase subunit GPI15
- GPI mannosyltransferase 1
Sequence:
MDEKTIKKSILSSSNDEKIIYKSRIKKFQKNHKFYIILLVFIAILQFISIAFFTRGFLLSRHVLDNISSQNETSKLPPRFNKAVILVIDALRFDFAIPVNESHSNYNLNYHNNILSLYDSFASDKDASSLLLKFIADPPTTTLQRLKGLTTGSLPTFIDAGSNFDGTVIEEDNFLKQLHLANKTVKFAGDDTWMALFHPFLSNDSFPLESLNVWDLDTVDNGVMDYFHDHLQQDKEWDVMIGHMLGIDHVGHKYGPDHFTMREKQIQVDQFIDWILKSIDDDTLLVILGDHGMDHTGNHGGDSIDELESTLFLYSKKPDMWRLKETSNYNIDNLGHDYRSVRQIDLVSSLALLMGQPIPFNNLGWPIDEIARNDREWSQFVNSAISQLQLYKDTMQIHHGNDEILEPLAKNISNTPPTSDPEKFVKLGHKYQKVFLQTCEELWAKFDYYSIATGITLLATSLVLLISITKLIPSIVVNQMVPEFVPGIIIMVLVTNLCFHGIFYVYQQPSFVDQFWGTLLATAIGIIIGCYITIFDRYNFIWIAMRLGETLADYWSRIAVMFMIIHALLFTSNSFTIWEDRIVAFLLSTFGMLTLYEFVFLPKRQSTTALLTATISEKEGTTSGVNPSTANSNYLPLTRFARLLGGYHSAVLIIFTRLASMITICREEQGEYCIPTFNNQNNSSWWVLGLCFLMIFILPACITGYYNLTSSYQAAAPIWINVFLKGILGLNFVYWSLTSLENNSAVIAIPFLRDVTIFKFTLARIIAGFSLIASNVGWLMGPLCIKLNIHNTDVKSHEATILGYTNIYGSEFFLLVINVLISILLFNKPLAQLSYFLMCNQLLSILEIIDLLKLKENIIGPIALGLLSYQHFFTTGHQATIPSVQWDIGFMLSEKVTFPFTQIAIILNTFGPHILVSLSVALLTLWSQPPDVLKPQTLLGRIVSNCGILLTYNTILCLSSFIWVTHFRRHLMVWKIFCPRFIFASLSLIVTQLVVTFGTIAFASGRLIKHINDIFWK
Protein: dITP/XTP pyrophosphatase (EC 3.6.1.66) (Deoxyribonucleoside triphosphate pyrophosphohydrolase) (Inosine triphosphate pyrophosphatase) (ITPase) (Non-canonical purine NTP pyrophosphatase) (Non-standard purine NTP pyrophosphatase) (Nucleoside-triphosphate diphosphatase) (Nucleoside-triphosphate pyrophosphatase) (NTPase) (P52061)
Organism: Escherichia coli (strain K12)
Function: Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Can also efficiently hydrolyze 2'-deoxy-N-6-hydroxylaminopurine triphosphate (dHAPTP). Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions. To a much lesser extent, is also able to hydrolyze GTP, dGTP and dUTP, but shows very low activity toward the canonical nucleotides dATP, dCTP and dTTP and toward 8-oxo-dGTP, purine deoxyribose triphosphate, 2-aminopurine deoxyribose triphosphate and 2,6-diaminopurine deoxyribose triphosphate.
Interaction partners:
- GMP synthase
- Inosine-5'-monophosphate dehydrogenase
- Heme chaperone HemW
- Nucleoside diphosphate kinase
- GMP/IMP nucleotidase YrfG
- Xanthine-guanine phosphoribosyltransferase
- 5'/3'-nucleotidase SurE
- Hypoxanthine phosphoribosyltransferase
- Glutamate racemase
- Protein UshA
Sequence:
MQKVVLATGNVGKVRELASLLSDFGLDIVAQTDLGVDSAEETGLTFIENAILKARHAAKVTALPAIADDSGLAVDVLGGAPGIYSARYSGEDATDQKNLQKLLETMKDVPDDQRQARFHCVLVYLRHAEDPTPLVCHGSWPGVITREPAGTGGFGYDPIFFVPSEGKTAAELTREEKSAISHRGQALKLLLDALRNG
Protein: Pectate lyase (EC 4.2.2.2) (Q4JLV6)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MARTMAMAIPSLPLLFLFTFLLLLPLLISSSPVQDPELVVQDVHRAINASKRNLGYLSCGTGNPIDDCWRCDPNWETNRQKLADCAIGFGKNAIGGRDGKIYVVTDSGDDDPVNPKPGTLRHAVIQGEPLWIIFARDMTIQLKEELIMNSFKTIDGRGASVHIAGGPCITVQYVTNIIIHGLNIHDCKQGGNAMVRDSPRHYGWRTISDGDGVSIFGGSHVWVDHNSLSNCKDGLIDAIHGSTAITISNNYMTHHDKVMLLGHSDSYTQDKNMQVTIAFNHFGEGLVQRMPRCRHGYFHVVNNDYTHWEMYAIGGSANPTINSQGNRFTAPDNRFSKEVTKHEDAPESEWKSWNWRSEGDLMVNGAFFISSGAGASSSYAKASSLGVRPSSLVATITTNAGALNCKKGSRC
Protein: Small ribosomal subunit protein uS4m (37S ribosomal protein NAM9, mitochondrial) (Nuclear accommodation of mitochondria protein 9) (P27929)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10529174, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein uS17m
- Small ribosomal subunit protein mS45
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS11m
Sequence:
MPRKANLLKSLARGRVRTSFNKYNLFNLYKKGGVDLKSKSLYQQKWTAKQETRAYHGEHLTEKRWQTVFKPKLDSVAQLDASLRGGEIKETPFLLQTFAVLEKRLDFALFRAMFASSVRQARQFILHGNVRVNGVKIKHPSYTLKPGDMFSVKPDKVLEALGAKKPSFQEALKIDKTQIVLWNKYVKEAKTEPKEVWEKKLENFEKMSDSNPKKLQFQEFLRQYNKNLESQQYNALKGCTQEGILRKLLNVEKEIGKSNNEPLSIDELKQGLPEIQDSQLLESLNNAYQEFFKSGEIRREIISKCQPDELISLATEMMNPNETTKKELSDGAKSALRSGKRIIAESVKLWTKNITDHFKTRMSDISDGSLTFDPKWAKNLKYHDPIKLSELEGDEPKARKLINLPWQKNYVYGRQDPKKPFFTPWKPRPFLSPFAILPHHLEISFKTCHAVYLRDPVARPGQSEVISPFDVPVHERAYMYYLRNGK
Protein: Probable feruloyl esterase B-2 (EC 3.1.1.73) (Ferulic acid esterase B-2) (FAEB-2) (Q2UMX6)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Function: Involved in degradation of plant cell walls. Hydrolyzes the feruloyl-arabinose ester bond in arabinoxylans as well as the feruloyl-galactose and feruloyl-arabinose ester bonds in pectin.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MPSLRRLLPFLAAGSAALASQDTFQGKCTGFADKINLPNVRVNFVNYVPGGTNLSLPDNPTSCGTTSQVVSEDVCRIAMAVATSNSSEITLEAWLPQNYTGRFLSTGNGGLSGCIQYYDLAYTSGLGFATVGANSGHNGTSGEPFYHHPEVLEDFVHRSVHTGVVVGKQLTKLFYEEGFKKSYYLGCSTGGRQGFKSVQKYPNDFDGVVAGAPAFNMINLMSWSAHFYSITGPVGSDTYLSPDLWNITHKEILRQCDGIDGAEDGIIEDPSLCSPVLEAIICKPGQNTTECLTGKQAHTVREIFSPLYGVNGTLLYPRMQPGSEVMASSIMYNGQPFQYSADWYRYVVYENPNWDATKFSVRDAAVALKQNPFNLQTWDADISSFRKAGGKVLTYHGLMDQLISSENSKLYYARVAETMNVPPEELDEFYRFFQISGMAHCSGGDGAYGIGNQLVTYNDANPENNVLMAMVQWVEKGIAPETIRGAKFTNGTGSAVEYTRKHCRYPRRNVYKGPGNYTDENAWQCV
Protein: Heme oxygenase 1, chloroplastic (EC 1.14.14.18) (Protein PHOTOPERIODIC SENSITIVITY 5) (Q69XJ4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the opening of the heme ring to form the open-chain tetrapyrrole biliverdin IX with the release of iron and carbon monoxide (CO). Is a key enzyme in the synthesis of the chromophore of the phytochrome family of plant photoreceptors. Essential for photoperiod response and repression of flowering through cytochromes that inhibit flowering by affecting both HD1 and EHD1 flowering pathways.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Ferrochelatase-2, chloroplastic
- Os01g0949400 protein
- Ferrochelatase-1, chloroplastic
- Heme O synthase
- ferroxidase
- Probable inactive heme oxygenase 2
- Os08g0496000 protein
- Ferritin
- Ferritin
- Os06g0472400 protein.
Sequence:
MAPAAASLTAPNALAATSLPFLHGRKSGGGGVSVHAGAPSPSRAVAVVARRLWGSASSSRRMVVAAATAAEMAPAASGEEGKPFVEEMRAVAMRLHTKDQAKEGEKEPQAPPVARWEPSVDGYLRFLVDSKLVFETLETIVDRAAVPWYAEFRNTGLERSEQLKKDLEWFKEQGHTIPEPSAPGTTYASYLEELAEKDSQAFICHFYNVYFAHTAGGRMIGKKVSENILNKKELEFYKWEGNLSQLLQNVRNKLNEVASSWTREEKDHCLDETEKSFSYSGDLLRHIFT