wanglab/gogpt-training-data huggingface dataset:
Protein: Acetate--CoA ligase CCL3 (HlCCL3) (EC 6.2.1.1) (2-methylbutanoate--CoA ligase CCL4) (EC 6.2.1.-) (2-methylpropanoate--CoA ligase CCL4) (EC 6.2.1.-) (Butanoate--CoA ligase CCL3) (EC 6.2.1.-) (Hexanoate--CoA ligase CCL3) (EC 6.2.1.-) (Isovalerate--CoA ligase CCL3) (EC 6.2.1.-) (Pentanoate--CoA ligase CCL3) (EC 6.2.1.-) (Propionate--CoA ligase CCL3) (EC 6.2.1.17) (M4IS88)
Organism: Humulus lupulus (European hop)
Function: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the ligation of CoA on propanoate to produce propanoyl-CoA. Can also use 2-methylpropanoate (isobutyric acid), acetate, butanoate, isovalerate, pentanoate, hexanoate, 2-methylbutanoate, 2-methylpentanoate, 3-methylpentanoate and 4-methylpentanoate as substrates with a lower efficiency. Triggers the formation of very short chain acyl-CoAs from the corresponding fatty acids, including acetic acid, propanoic acid, butyric acid and its isomer.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:M4IRL4}.
Interaction partners:
Sequence:
MGMVGRDIDDLPKNAANYTALTPLWFLERAATVHPTRTSVIHGSRHYTWLQTYHRCRQFASALNNHSIGLGSTVAVIAPNVPALYEAHFAVPMAGAVVNCVNIRLNASTIAFLLGHSSAAAVMVDQEFFSLAEEALKILAQESKSHYKPPLLVVIGDESCDPKTLEYALKTGAIEYEKFLEGGDPEFDWKPPEDEWQSISLGYTSGTTASPKGVVLSHRGAYLMSLSASVVWGINEGAIYLWTLPMFHCNGWCYTWGMAAFCGTNICLRQVTAKGVYSAIAKYGVTHFCAAPVVLNTIVNAPPEEAIIPLPHLVHVMTAGAAPPPSVLFAMSEKGFKVAHTYGLSETYGPSTICAWKPEWDSLPPIKQARLNARQGVRYIALEGLDVVDTKTMKPVPADGTTMGEIVMRGNAVMKGYLKNPKANEESFADGWFHSGDLAVKHPDGYIEIKDRSKDIIISGGENISSLEVENTLYLHPAVLEVSVVARPDERWGESPCAFVTLKPNIDKSNEQVLAEDIIKFCKSKMPAYWVPKSVVFGPLPKTATGKIQKHVLRAKAKEMGALKKSNL
Protein: Probable methyltransferase PMT15 (EC 2.1.1.-) (Q9ZPH9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Leucine-rich repeat
- Leucine-rich repeat
- Leucine-rich repeat
- Leucine-rich repeat
- Similar to part of disease resistance protein domain-containing protein)
- Leucine-rich repeat
- Similar to part of disease resistance protein domain-containing protein)
- Insulin-like growth factor binding protein
- Lysine-specific demethylase JMJ28
- DNA ligase-like protein
Sequence:
MGNYRWPSKLSKLSLRAKQTNLYRVILIAILCVTFYFVGVWQHSGRGISRSSISNHELTSVPCTFPHQTTPILNFASRHTAPDLPPTITDARVVQIPSCGVEFSEYTPCEFVNRSLNFPRERLIYRERHCPEKHEIVRCRIPAPYGYSLPFRWPESRDVAWFANVPHTELTVEKKNQNWVRYEKDRFLFPGGGTMFPRGADAYIDEIGRLINLKDGSIRTAIDTGCGVASFGAYLMSRNIVTMSFAPRDTHEAQVQFALERGVPAIIGVLASIRLPFPARAFDIAHCSRCLIPWGQYNGTYLIEVDRVLRPGGYWILSGPPINWQRHWKGWERTRDDLNSEQSQIERVARSLCWRKLVQREDLAVWQKPTNHVHCKRNRIALGRPPFCHRTLPNQGWYTKLETCLTPLPEVTGSEIKEVAGGQLARWPERLNALPPRIKSGSLEGITEDEFVSNTEKWQRRVSYYKKYDQQLAETGRYRNFLDMNAHLGGFASALVDDPVWVMNVVPVEASVNTLGVIYERGLIGTYQNWCEAMSTYPRTYDFIHADSVFSLYKDRCDMEDILLEMDRILRPKGSVIIRDDIDVLTKVKKITDAMQWEGRIGDHENGPLEREKILFLVKEYWTAPAPDQSSDP
Protein: Calponin-homology (CH) domain-containing protein (Q57X76)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVSRAKHPCSSSLPPIVFPSGPSATYAAFSQKEDAALDARNKIERHRYAKLLLEYAERYREFSSVSFFVETMLRELAGREGVTNQSRAMAAVWSMKLLSCHSPFKQFMVHITEALLPAIFCNYDAKRLDYAPAAIQALLCDRALHRDNPFFSHSTYMHEYDASLLKLKNISGELKRVSFTGSEWKRIAHMLVVYVQSERKRRAFIAWRDNVKKERVVNKLRRNVVSRHGADSRFLCVALGFLRWKSATAMSRVQFLTERLHDAAFQLESAKNQFHMECFRADKLQLSNEEKDSELKAVMCERDELQLEVERLKEQLKIQERNHEANLRARLLEILTLAQHQNILLKKIVGTQFDAKEVVAGWLHKEDGDYQEREPEHGENEALQGHSFLLRWCNHILRSGEVGVLRRVRNFADDFADGEVFHGIIRYVFPEKKEFATSVDSSVADRLRLVCDFTTNIPLAVSLTVEDFNMKREDRIIVAVAEIFAYYVEKKRADAVSESFRLVVEQDPLQVDSSIATDSEDVSLLTTEEDVKKQLSIWNKELSKQVENFRLGVWCEMDLQKSGMCISREAARLTWERGRGHPRYVVTADASRHFVSLNARKMNDLREKFGSCTPQVWRSVVQSLKRVLWKHVNTITSIFYHYAGENAHEMDEVQFWRFVEDSRLMVEPLSRQTIARIFDTVISPKLMAMLQAKSVEKQAALLEAAEEEMNIRRVKPAQFTEILLHMGAVRFRDSLLDAAGRFLTGLSVPTLCGVTPTTVDFYRPESQRVIRHLQEDLARVFFFYVKQQSENQRKSSKGLKQPSGRFVGRISFDAYLRMFSDCGFVADNKEKENNSRRGSTEPHRYCRKVKFTDVEEITETFNALHERVLLLPEGELCFSLFLESFGIACQYWCPDPKVSFPRKLACFLTDMIERLRTLHSRSALILRELPPPTVEKGDAGCVP
Protein: Uncharacterized protein (Q585X4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKLERSSCFEVQGCISCLTQASNEDACLASTMMNGAHIFHMGDLQHAQCGARQAVTHVETFPHGNFGEGAVISSSFVSYDSCFATGSSSGDIVLVSRHSKNVVQHYSFQNKAAVLSLKEVPNEPSLLLACSPTDAQIIDLETSTARINLHIPKPCVVGGTALTQNTLVVAAYDGKAMLYDVRRGHEPVVILAVPDQIISITSSPDTGAVATGTVSGRVFVLRCLEGNVREEAFSTGKERAPIRSVAMRNGYIAAGDTSAKLTCLDLKEDPKPTRYWDLHSLLTNESGPPSSGAEKLSSVTVPDTESWSLPAVMLQQSDLWAALSSTKYGVSHILAIPI
Protein: Cold shock-like protein CspG (CPS-G) (P0A978)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Cold shock-like protein CspB
- Cold shock-like protein CspH
- Uncharacterized protein YmcE
- 30S ribosome-binding factor
Sequence:
MSNKMTGLVKWFNADKGFGFITPDDGSKDVFVHFTAIQSNEFRTLNENQKVEFSIEQGQRGPAAANVVTL
Protein: Placenta growth factor (PlGF) (Q63434)
Organism: Rattus norvegicus (Rat)
Function: Growth factor active in angiogenesis and endothelial cell growth, stimulating their proliferation and migration. It binds to the receptor FLT1/VEGFR-1. Also promotes cell tumor growth (By similarity).
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Vascular endothelial growth factor receptor 1
- Vascular endothelial growth factor receptor 3
- Vascular endothelial growth factor receptor 2
- Neuropilin-1
- Angiopoietin-1 receptor
- Platelet-derived growth factor receptor beta
- Platelet-derived growth factor receptor alpha
- Macrophage colony-stimulating factor 1 receptor
- Neuropilin-2
- Platelet-derived growth factor C
Sequence:
MLAMKLFTCFLQVLAGLAVHSQGALSAGNNSTEMEVVPFNEVWGRSYCRPMEKLVYIADEHPNEVSHIFSPSCVLLSRCSGCCGDEGLHCVALKTANITMQILKIPPNRDPHSYVEMTFSQDVLCECRPILETTKAERRKTKGKRKQSKTPQTEEPHL
Protein: Pentatricopeptide repeat-containing protein At5g13270, chloroplastic (Q9LYU9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Multiple organellar RNA editing factor 8, chloroplastic/mitochondrial
- Organelle RRM domain-containing protein 1
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic
- Multiple organellar RNA editing factor 9, chloroplastic
- Zinc finger protein VAR3, chloroplastic
- Phosphoglycerate mutase family protein
- Organelle RRM domain-containing protein 2
- Multiple organellar RNA editing factor 2, chloroplastic
- NAD
- Glycine-rich RNA-binding protein 3, mitochondrial
Sequence:
MTILTVQSSFSSSRVPVIKNANFDQIPSWVSLKSSTSSPSVKISHKQGQVENLHLVSLSKHRKLNEAFEFLQEMDKAGVSVSSYSYQCLFEACRELRSLSHGRLLHDRMRMGIENPSVLLQNCVLQMYCECRSLEDADKLFDEMSELNAVSRTTMISAYAEQGILDKAVGLFSGMLASGDKPPSSMYTTLLKSLVNPRALDFGRQIHAHVIRAGLCSNTSIETGIVNMYVKCGWLVGAKRVFDQMAVKKPVACTGLMVGYTQAGRARDALKLFVDLVTEGVEWDSFVFSVVLKACASLEELNLGKQIHACVAKLGLESEVSVGTPLVDFYIKCSSFESACRAFQEIREPNDVSWSAIISGYCQMSQFEEAVKTFKSLRSKNASILNSFTYTSIFQACSVLADCNIGGQVHADAIKRSLIGSQYGESALITMYSKCGCLDDANEVFESMDNPDIVAWTAFISGHAYYGNASEALRLFEKMVSCGMKPNSVTFIAVLTACSHAGLVEQGKHCLDTMLRKYNVAPTIDHYDCMIDIYARSGLLDEALKFMKNMPFEPDAMSWKCFLSGCWTHKNLELGEIAGEELRQLDPEDTAGYVLPFNLYTWAGKWEEAAEMMKLMNERMLKKELSCSWIQEKGKIHRFIVGDKHHPQTQEIYEKLKEFDGFMEGDMFQCNMTERREQLLDHSERLAIAFGLISVHGNAPAPIKVFKNLRACPDCHEFAKHVSLVTGHEIVIRDSRRFHHFKEGKCSCNDYW
Protein: Large ribosomal subunit protein eL36 (60S ribosomal protein L36) (P39032)
Organism: Rattus norvegicus (Rat)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3U8}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y3U8}. Note=Detected on cytosolic polysomes. {ECO:0000250|UniProtKB:Q2YGT9, ECO:0000250|UniProtKB:Q9Y3U8}.
Interaction partners:
- Large ribosomal subunit protein eL18
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS12
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein eL30
Sequence:
MALRYPMAVGLNKGHKVTKNVSKPRHSRRRGRLTKHTKFVRDMIREVCAFAPYERRAMELLKVSKDKRALKFIKKRVGTHIRAKRKREELSNVLAAMRKAAAKKD
Protein: Annexin D7 (AnnAt7) (Q9LX07)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NAD
- BAHD acyltransferase At5g47980
- Alcohol dehydrogenase-like protein
- Alcohol dehydrogenase-like protein
- TORTIFOLIA1-like protein 3
- S-protein homolog
- High-affinity nickel-transport family protein
- Remorin family protein
- Probable fucosyltransferase 4
- F16N3.9 protein
Sequence:
MASLKVPATVPLPEEDAEQLYKAFKGWGTNERMIISILAHRNATQRSFIRAVYAANYNKDLLKELDRELSGDFERAVMLWTFEPAERDAYLAKESTKMFTKNNWVLVEIACTRSALELFNAKQAYQARYKTSLEEDVAYHTSGDIRKLLVPLVSTFRYDGDEVNMTLARSEAKILHEKIKEKAYADDDLIRILTTRSKAQISATLNHYKNNFGTSMSKYLKEDSENEYIQLLKAVIKCLTYPEKYFEKVLRQAINKLGTDEWGLTRVVTTRAEFDMERIKEEYIRRNSVPLDRAIAKDTHGDYEDILLALLGHDHA
Protein: ATP synthase subunit beta, mitochondrial (EC 7.1.2.2) (P22068)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Subunits alpha and beta form the catalytic core in F(1). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane. Note=Peripheral membrane protein.
Interaction partners:
- Putative ATP synthase subunit epsilon, mitochondrial
- ATP synthase subunit 5, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- ATP synthase subunit d
- ATP synthase subunit a
- ATP synthase subunit alpha
- ATP synthase subunit delta, mitochondrial
- ATP synthase subunit 9, mitochondrial
- ATP synthase subunit 4
- ATP synthase subunit g, mitochondrial
Sequence:
MLKKQALSGIRRFSLATKQSFVKTSYKLPRKSWLNTAKFNTIRYASTEAAKHNKGSIKQVIGAVVDCQFEDADSLPSILNALEVKLPDNKRLVLEVAQHVGENTVRTIAMDGTEGLVRGTAVIDTGSPISIPVGPGTLGRIMNVIGEPVDERGPIKAVKYSPIHADAPSFEEQSTTPEILETGIKVVDLLAPYARGGKIGLFGGAGVGKTVFIQELINNIAKAHGGYSVFTGVGERTREGNDLYREMQETGVIKLEGESKAALVFGQMNEPPGARARVALTGLTVAEYFRDIEGQDVLLFIDNIFRFTQAGSEVSALLGRIPSAVGYQPTLATDMGAMQERITTTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRSISELGIYPAVDPLDSKSRMMDPRILGEEHYNLAGSVQQMLQEYKSLQDIIAILGMDELSEADKLTVERARKVQRFLSQPFAVAEVFTGIEGRLVSLKDTIRSFKEILEGKHDSLPESAFYMVGSIDDAVKKAEKIAQELAA
Protein: FI01025p (Lim3, isoform B) (Lim3, isoform C) (Lim3, isoform D) (Lim3, isoform F) (Q9VJ00)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
Sequence:
MMQTLKPPPPLHHHHQHQHQLQHPPQQQPHPHQQLQHPLQQQQHLSAMDNHQQHQPHIHQQQQQQQQLPPTPQASHLVGGQQQQQQHPHHNHLAVDQDDPNPELVLALISRNRALEATIPKCGGCHELILDRFILKVLERTWHAKCLQCSECHGQLNDKCFARNGQLFCKEDFFKRYGTKCSACDMGIPPTQVVRRAQDNVYHLQCFLCAMCSRTLNTGDEFYLMEDRKLICKRDYEEAKAKGLYLDGSLDGDQPNKRPRTTITAKQLETLKTAYNNSPKPARHVREQLSQDTGLDMRVVQVWFQNRRAKEKRLKKDAGRTRWSQYFRSMKGNCSPRTDKFLDKDELKVDYDSFSHHDLSNDSYSTVNLGLDEGASPHSIRGSYMHGSSSPSQYPPSSRSPPPVGQGHTFGSYPDNIVYTNIDQAVGSSLHASKAHHRLHSSNNVSDLSNDSSPDQGYPDFPPSPDSWLGDSGSTNTTSANNNANNNSSSSHNNNNSSGGGSGGVSVSTAPNPSAPGVHY
Protein: Uncharacterized protein C17G6.03 (O13781)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MKPAHTFSLIFSLLFVINPCYSATLPLAIRRELTWGQVNILHTTDIHGWLAGHARDKRYSGDLGDFASFVQHMKHLAKQKDVDLLLVDTGDLHDGTGLSDLTDPPGSWTDSLLANMDYDILVAGNHELYLSTVANDTYHNFIPLWEGRYLAANIDIYDEHVSSFVPFGDRYAIFSTPHNVKILAFGFVNSFSGATDTVRVLPVSQFSLQPWWNDMVSNKDIDLILIPAHVPVHNASELDIVLSELRIHFPTTPIQVLGGHSHIRDYAIYDEKAVGIESGRYCETVGWVSINGIPSFKSLVKLSGISSLMGVESYLAERLRFIGESIRRSSQQIFSSLQSAKSASVSFSRSYIDWNPEGFMFHSKTKKSSFNTSLGEFISNGIYEARKALGLLTPIGCSPKKFAFSEVPFNDSNSIYHLFQSELFPKIVVNESRHHIPHYIIVNSGGIRGGLNSGAFGLDEVFQVCPFKSNIFYVLKDVPWSITKYLPQALQHSGYLIAEDTLQINTPQVSDAKFEDFYEHSIRKTYGYTTHDDLGDDGDDTAHLTTPHYEPLRFICSQVGFDDSFSGDDKQVVDVVAPSFVIPRLDDILNKIADKPLYSPDDWELYFTRPDGKHSMTDLLPLYADLYWDHDCLYK
Protein: D-2-hydroxyglutarate dehydrogenase, mitochondrial (EC 1.1.99.39) (Q7K511)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- L-2-hydroxyglutarate dehydrogenase, mitochondrial
- Electron transfer flavoprotein subunit beta
- Electron transfer flavoprotein subunit alpha
- Electron transfer flavoprotein-ubiquinone oxidoreductase
Sequence:
MRFQQLLHVRRLASAGATTLMRRPITTTTITTTSRTALAATYPAFATTVRTMAGSGAPIPELTEITDNVQRGNYATLTDKDVAHFEQLLGKNFVLTEDLEGYNICFLKRIRGNSKLVLKPGSTAEVAAILKYCNERRLAVVPQGGNTGLVGGSVPICDEIVLSLARLNKVLSVDEVTGIAVVEAGCILENFDQRAREVGLTVPLDLGAKASCHIGGNVSTNAGGVRVVRYGNLHGSVLGVEAVLATGQVLDLMSNFKKDNTGYHMKHLFIGSEGTLGVVTKLSMLCPHSSRAVNVAFIGLNSFDDVLKTFVSAKRNLGEILSSCELIDERALNTALEQFKFLNSPISGFPFYMLIETSGSNGDHDEEKINQFIGDGMERGEIQDGTVTGDPGKVQEIWKIREMVPLGLIEKSFCFKYDISLPLRDFYNIVDVMRERCGPLATVVCGYGHLGDSNLHLNVSCEEFNGEIYKRVEPFVYEYTSKLKGSISAEHGIGFLKKDYLHYSKDPVAIGYMREMKKLLDPNSILNPYKVLN
Protein: Baseplate tail-tube junction protein gp48 (Baseplate-tube cap) (Gene product 48) (gp48) (P13339)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Baseplate protein that forms, together with gp54, the baseplate-tail tube junction. The tail tube first 2 annuli are formed by gp48 and gp54, which are in continuation of the spike complex. Involved in the tail assembly. Morphogenesis of the baseplate is completed by association of gp48 and gp54, which bind the upper part of the baseplate dome to form the platform for polymerization of the tail tube.
Subcellular location: Virion {ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}. Note=Present in 6 copies in the baseplate. {ECO:0000303|PubMed:21129200}.
Interaction partners:
Sequence:
MAIVKEITADLIKKSGEKISAGQSTKSEVGTKTYTAQFPTGRASGNDTTEDFQVTDLYKNGLLFTAYNMSSRDSGSLRSMRSNYSSSSSSILRTARNTISSTVSKLSNGLISNNNSGTISKSPIANILLPRSKSDVDTSSHRFNDVQESLISRGGGTATGVLSNIASTAVFGALESITQGIMADNNEQIYTTARSMYGGAENRTKVFTWDLTPRSTEDLMAIINIYQYFNYFSYGETGKSQYAAEIKGYLDDWYRSTLIEPLSPEDAAKNKTLFEKMTSSLTNVLVVSNPTVWMVKNFGATSKFDGKTEIFGPCQIQSIRFDKTPNGNFNGLAIAPNLPSTFTLEITMREIITLNRASLYAGTF
Protein: Probable WRKY transcription factor 10 (Protein MINISEED 3) (WRKY DNA-binding protein 10) (Q9LG05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Interacts specifically with the W box (5'-(T)TGAC[CT]-3'), a frequently occurring elicitor-responsive cis-acting element (By similarity). Modulates seed size by negatively regulating the cellularization of syncytial endosperm.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00223, ECO:0000269|PubMed:16293693}.
Interaction partners:
- Protein HAIKU1
- Receptor-like protein kinase HAIKU2
- Phosphate transporter PHO1 homolog 4
- VQ motif-containing protein 9
- PHD finger protein At2g01810
- Agamous-like MADS-box protein AGL62
- VQ motif-containing protein 22
- F22C12.10
- Auxin response factor 2
- Polycomb group protein FERTILIZATION-INDEPENDENT SEED 2
Sequence:
MSDFDENFIEMTSYWAPPSSPSPRTILAMLEQTDNGLNPISEIFPQESLPRDHTDQSGQRSGLRERLAARVGFNLPTLNTEENMSPLDAFFRSSNVPNSPVVAISPGFSPSALLHTPNMVSDSSQIIPPSSATNYGPLEMVETSGEDNAAMMMFNNDLPYQPYNVDLPSLEVFDDIATEESFYIPSYEPHVDPIGTPLVTSFESELVDDAHTDIISIEDSESEDGNKDDDDEDFQYEDEDEDQYDQDQDVDEDEEEEKDEDNVALDDPQPPPPKRRRYEVSNMIGATRTSKTQRIILQMESDEDNPNDGYRWRKYGQKVVKGNPNPRSYFKCTNIECRVKKHVERGADNIKLVVTTYDGIHNHPSPPARRSNSSSRNRSAGATIPQNQNDRTSRLGRAPPTPTPPTPPPSSYTPEEMRPFSSLATEIDLTEVYMTGISMLPNIPVYENSGFMYQNDEPTMNAMPDGSDVYDGIMERLYFKFGVDM
Protein: Tripartite motif-containing protein 3 (EC 2.3.2.27) (RING finger protein 22) (RING finger protein HAC1) (Q9R1R2)
Organism: Mus musculus (Mouse)
Function: Probably involved in vesicular trafficking via its association with the CART complex. The CART complex is necessary for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). Positively regulates motility of microtubule-dependent motor protein KIF21B.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O75382}. Early endosome {ECO:0000250|UniProtKB:O75382}. Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:24086586}. Cell projection, dendrite {ECO:0000269|PubMed:24086586}. Note=Mainly located in the Golgi apparatus and transported to the early endosomes upon stimulation with dsRNA. {ECO:0000250|UniProtKB:O75382}.
Interaction partners:
- Alpha-actinin-4
- Tripartite motif-containing protein 44
Sequence:
MAKREDSPGPEVQPMDKQFLVCSICLDRYRCPKVLPCLHTFCERCLQNYIPPQSLTLSCPVCRQTSILPEQGVSALQNNFFISSLMEAMQQAPEGAHDPEDPHPLSAVAGRPLSCPNHEGKTMEFYCEACETAMCGECRAGEHREHGTVLLRDVVEQHKAALQRQLEAVRGRLPQLSAAIALVGGISQQLQERKAEALAQISAAFEDLEQALQQRKQALVSDLESICGAKQKVLQTQLDTLRQGQEHIGSSCSFAEQALRLGSAPEVLLVRKHMRERLAALAAQAFPERPHENAQLELVLEVDGLRRSVLNLGALLTTSATAHETVATGEGLRQALVGQPASLTVTTKDKDGRLVRTGSAELCAEITGPDGVRLAVPVVDHKNGTYELVYTARTEGDLLLSVLLYGQPVRGSPFRVRALRPGDLPPSPDDVKRRVKSPGGPGSHVRQKAVRRPSSMYSTGGKRKDNPIEDELVFRVGSRGREKGEFTNLQGVSAASSGRIVVADSNNQCIQVFSNEGQFKFRFGVRGRSPGQLQRPTGVAVDTNGDIIVADYDNRWVSIFSPEGKFKTKIGAGRLMGPKGVAVDRNGHIIVVDNKSCCVFTFQPNGKLVGRFGGRGATDRHFAGPHFVAVNNKNEIVVTDFHNHSVKVYSADGEFLFKFGSHGEGNGQFNAPTGVAVDSNGNIIVADWGNSRIQVFDSSGSFLSYINTSAEPLYGPQGLALTSDGHVVVADAGNHCFKAYRYLQ
Protein: Small ribosomal subunit protein eS8 (40S ribosomal protein S8) (P62243)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62241}. Membrane {ECO:0000250|UniProtKB:P62241}; Lipid-anchor {ECO:0000250|UniProtKB:P62241}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62241}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P62241}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-like protein FUBI
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS12
Sequence:
MGISRDNWHKRRKTGGKRKPYHKKRKYELGRPAANTKIGPRRIHTVRVRGGNKKYRALRLDVGNFSWGSECCTRKTRIIDVVYNASNNELVRTKTLVKNCIVLIDSTPYRQWYESHYALPLGRKKGAKLTPEEEEILNKKRSKKIQKKYDERKKNAKISSLLEEQFQQGKLLACIASRPGQCGRADGYVLEGKELEFYLRKIKARKGK
Protein: Beta-2 adrenergic receptor (Beta-2 adrenoreceptor) (A0A060YAV5)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Guanine nucleotide-binding protein G
- GNAS complex locus
- Guanine nucleotide-binding protein G
- Endothelin-3
- Neuropeptide Y
- Uncharacterized protein
- Guanine nucleotide-binding protein G
- GNAS complex locus
- GNAS complex locus
- Guanine nucleotide-binding protein G
Sequence:
MEREREREREREEGGGGGXGEPGYSEVEMVLLGMLMSLLVVGIVFGNILVIIAIYRFQRLQNITNCFITSLACADLVMGLIVVPFGACYIIFNTWHFGSFWCEFWTATDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTKCKARVVVLLVWVIAGLISFLPIHMKWWISDDAEAKACIQNSNCCDFNTNTAYAITSSIISFYIPLVVMVFVYSRVFQEAKQQLRKIDRSEGRFHAHNNNMAGGGGGGGGGGGGTKFCLREHKALKTLGIIMGIFTLCWLPFFVLNVVVAIWKVGDIGLAFRILNWIGYANSAFNPLIYCRSPEFRYAFKEILCIKKVRFPNIGPTNGYVYSGHSWQTADGCSGRGEAGGCGAADRTDPNGNCSKGLTTVL
Protein: L-ascorbate oxidase (AAO) (AO) (ASO) (Ascorbase) (EC 1.10.3.3) (M4DUF2)
Organism: Brassica rapa subsp. pekinensis (Chinese cabbage) (Brassica pekinensis)
Function: Ascorbate oxidase involved in a redox system involving ascorbic acid (AsA). The oxidation of AsA represses responses to high salinity and oxidative stress conditions such as vegetative growth and seed production reductions (By similarity). Negative regulator of defense responses toward incompatible Turnip mosaic virus (TuMV strain UK1) by preventing jasmonic acid (JA)- dependent accumulation of ascorbic acid (AsA, AS) and dehydroascobic acid (DHA).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P37064}.
Interaction partners:
- FAD-binding PCMH-type domain-containing protein
- L-gulonolactone oxidase
- Pyruvate dehydrogenase E1 component subunit alpha
- Pyruvate dehydrogenase E1 component subunit alpha
- L-ascorbate peroxidase
- PEROXIDASE_4 domain-containing protein
- L-ascorbate peroxidase
Sequence:
MGMWWIVAVAILAHTASAAVREYAWEVEYKFGWPDCKEGMVMAVNGQFPGPTIHALAGDTIVVHLTNKLATEGLVIHWHGIRQLGSPWADGAAGVTQCAISPGETFTYNFTVDKPGTHFYHGHYGMQRSAGLYGSLIIDVAKGKKEPLRYDGEFNLLLSDWWHEDVLSQEIGLSSRPMRWIGEAQSILINGRGQFNCSLAAQFSSTSLPTCTFKEGDQCAPQRLHVEPNKTYRIRLASSTALASLNFAVQGHKLVVVEADGNYITPFTTDDIDIYSGETYSVLLTTDQDPSQNYYITAGVRGRKPNTPPALTVLNYVTAPSSQLPTSPPPETPRWNDFDRSKNFSKKIFAAMGSPSPPETFDERLILLNTQNLIEGFTKWAINNVSLAVPGTPYLGSVKYNLRTGFNRSSPPKDYPVDYDIMTPPRNRNAKQGNVSCVFPFNVTVDVILQNANGLNANASEIHPWHLHGHDFWVLGYGEGKFKPGVDEKTYNLKNPPLRNTVALYPYGWTALRFVTDNPGVWFFHCHIEPHLHMGMGVVFAEGLNRIGKVPDEALGCGLTKQFLMNRNNP
Protein: Autophagy protein 5 (APG5-like) (Q99J83)
Organism: Mus musculus (Mouse)
Function: Involved in autophagic vesicle formation. Conjugation with ATG12, through a ubiquitin-like conjugating system involving ATG7 as an E1-like activating enzyme and ATG10 as an E2-like conjugating enzyme, is essential for its function. The ATG12-ATG5 conjugate acts as an E3-like enzyme which is required for lipidation of ATG8 family proteins and their association to the vesicle membranes. Involved in mitochondrial quality control after oxidative damage, and in subsequent cellular longevity. Plays a critical role in multiple aspects of lymphocyte development and is essential for both B and T lymphocyte survival and proliferation. Required for optimal processing and presentation of antigens for MHC II. Involved in the maintenance of axon morphology and membrane structures, as well as in normal adipocyte differentiation. Promotes primary ciliogenesis through removal of OFD1 from centriolar satellites and degradation of IFT20 via the autophagic pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24089209}. Preautophagosomal structure membrane {ECO:0000269|PubMed:24089209}; Peripheral membrane protein {ECO:0000269|PubMed:24089209}. Note=The conjugate detaches from the membrane immediately before or after autophagosome formation is completed. Also localizes to discrete punctae along the ciliary axoneme and to the base of the ciliary axoneme.
Interaction partners:
- Autophagy-related protein 16-1
- Ubiquitin-like-conjugating enzyme ATG3
- Ubiquitin-like modifier-activating enzyme ATG7
- Ubiquitin-like protein ATG12
- Tectonin beta-propeller repeat-containing protein 1
- Mitochondrial antiviral-signaling protein
- Microtubule-associated protein 1 light chain 3 beta
- Protein Atg16l2
- Ubiquitin-like-conjugating enzyme ATG10
- FAS-associated death domain protein
Sequence:
MTDDKDVLRDVWFGRIPTCFTLYQDEITEREAEPYYLLLPRVSYLTLVTDKVKKHFQKVMRQEDVSEIWFEYEGTPLKWHYPIGLLFDLLASSSALPWNITVHFKSFPEKDLLHCPSKDAVEAHFMSCMKEADALKHKSQVINEMQKKDHKQLWMGLQNDRFDQFWAINRKLMEYPPEENGFRYIPFRIYQTTTERPFIQKLFRPVAADGQLHTLGDLLREVCPSAVAPEDGEKRSQVMIHGIEPMLETPLQWLSEHLSYPDNFLHISIVPQPTD
Protein: Ribosomal protein S6 kinase (EC 2.7.11.1) (F1MNP4)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MRRRRRRDGFYPAPDFRDREAEDMAGVFDIDLDQPEDAGSEDELEEGGQLNESMDHGGVGPYELGMEHCEKFEISETSVNRGPEKIRPECFELLRVLGKGGYGKVFQVRKVTGANTGKIFAMKVLKKAMIVRNAKDTAHTKAERNILEEVKHPFIVDLIYAFQTGGKLYLILEYLSGGELFMQLEREGIFMEDTACFYLAEISMALGHLHQKGIIYRDLKPENIMLNHQGHVKLTDFGLCKESIHDGTVTHTFCGTIEYMAPEILMRSGHNRAVDWWSLGALMYDMLTGAPPFTGENRKKTIDKILKCKLNLPPYLTQEARDLLKKLLKRNAASRLGAGPGDAGEVQAHPFFRHINWEELLARKVEPPFKPLLQSEEDVSQFDSKFTRQTPVDSPDDSALSESANQVFLGFTYVAPSVLESVKEKFSFEPKIRSPRRFIGSPRTPVSPVKFSPGDFWGRGASASTANPQTPVEYPMETSGIEQMDVTMSGEASAPLPIRQPNSGPYKKQAFPMISKRPEHLRMNL