wanglab/gogpt-training-data huggingface dataset:
Protein: Neurotensin receptor type 1 (NT-R-1) (NTR1) (High-affinity levocabastine-insensitive neurotensin receptor) (NTRH) (P20789)
Organism: Rattus norvegicus (Rat)
Function: G-protein coupled receptor for the tridecapeptide neurotensin (NTS). Signaling is effected via G proteins that activate a phosphatidylinositol-calcium second messenger system. Signaling leads to the activation of downstream MAP kinases and protects cells against apoptosis (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1694443, ECO:0000269|PubMed:24453215, ECO:0000269|PubMed:26205105}; Multi-pass membrane protein {ECO:0000269|PubMed:1694443, ECO:0000269|PubMed:24453215, ECO:0000269|PubMed:26205105}. Membrane raft {ECO:0000250|UniProtKB:P30989}. Note=Palmitoylation is required for localization at CAV1-enriched membrane rafts. {ECO:0000250|UniProtKB:P30989}.
Interaction partners:
- Neurotensin/neuromedin N
- Neurotensin receptor type 2
- Beta-arrestin-1
- Guanine nucleotide-binding protein G
- Beta-arrestin-2
- Sortilin
- Neuromedin-U
Sequence:
MHLNSSVPQGTPGEPDAQPFSGPQSEMEATFLALSLSNGSGNTSESDTAGPNSDLDVNTDIYSKVLVTAIYLALFVVGTVGNSVTAFTLARKKSLQSLQSTVHYHLGSLALSDLLILLLAMPVELYNFIWVHHPWAFGDAGCRGYYFLRDACTYATALNVASLSVERYLAICHPFKAKTLMSRSRTKKFISAIWLASALLAIPMLFTMGLQNRSGDGTHPGGLVCTPIVDTATVKVVIQVNTFMSFLFPMLVISILNTVIANKLTVMVHQAAEQGRVCTVGTHNGLEHSTFNMTIEPGRVQALRHGVLVLRAVVIAFVVCWLPYHVRRLMFCYISDEQWTTFLFDFYHYFYMLTNALFYVSSAINPILYNLVSANFRQVFLSTLACLCPGWRHRRKKRPTFSRKPNSMSSNHAFSTSATRETLY
Protein: UDP-xylose transporter 1 (F4IHS9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nucleotide-sugar transporter that transports UDP-xylose and UMP in a strict counter-exchange mode.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:25804536}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:25804536}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- UDP-galactose/UDP-glucose transporter 2
- Xyloglucan galactosyltransferase XLT2
- GDP-fucose transporter 1
- UDP-glucuronic acid decarboxylase 1
- UDP-glucuronic acid decarboxylase 3
- UDP-galactose/UDP-glucose transporter 1
- Xyloglucan galactosyltransferase MUR3
Sequence:
MGEMKSMQMGVIGALFLSVASSVSIVICNKALMTNLGFPFATTLTSWHLMVTYCTLHVAYKLNFFENKPIDMRTVVLFGLLNGISIGLLNLSLGFNSIGFYQMTKLAIIPFTVLLETLFLNKKFSQKIKFSLFLLLVGVGIASITDLQLNFVGSVLSLLAIATTCVGQILTNTIQKRLNVTSTQLLYQSAPFQAAILFVSGPFVDKYLTSLNVFSFHYSPIVVGFITLSCLIAVSVNFSTFLVIGKTSPVTYQVLGHLKTCLVLAFGYTLLHDPFTPRNIAGILIAVLGMLLYSYFCSVASKSKQASSDSTFLGKDRDTTPLLGQENENHHEAKKLDKHSPV
Protein: ADIPOR-like receptor IZH2 (Phosphate metabolism protein 36) (Q12442)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Probable receptor, which is involved in metabolic pathways that regulate lipid metabolism such as fatty acid oxidation.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Zinc-responsive transcriptional regulator ZAP1
- Acyl-CoA desaturase 1
Sequence:
MSTLLERTKSVQELKKRAAGKTSANPAEVAKAKKVLRRLYSWDEIPEWQRDNDFILHGYVKETSSFIETFKSLFYLHNESVNIYSHLIPALGFFTVLLLDKSTIKVFATTTWLDHMVIDLFYSGAFACLILSSSFHCLKSHSLRIATLGNKLDYLGICILIVTSMVSILYYGYFEKFSLFCLFALITVSFGIACSIVSLKDKFRKREWRPYRAGLFVCFGLSSIIPIFSGLYCYSFSEIWTQIQLFWVLLGGVLYIIGAVLYGMRFPEKICPGKFDIWGHSHQLFHFLVVIAALCHLRGLLNSYELVHIKMENGIVS
Protein: Uncharacterized membrane protein YHL071W (P38745)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Late secretory pathway protein AVL9
- Protein LDB17
Sequence:
MDRTWLLLTWLLLLCGVVQGNQESINQKYHDVCSGMYSKEDFNGKVDPYISFTLEELSLADEDDDGEGVSVAVFDFQDYEHIGVRLPNGEIQYICDDYALDLGLCEDSSEGQFIIQETAIDPFTSKEHKLTSQILTFTQQELGTNDKVYSINKTGYYCVTTSSFISSSSKFKATVNFRNAYGQLDASEAYKMPIYAFLAVAYAVCTLVYSWLCWKHRHELLPLQRYILVFCIFLTADTIFVWMYYIIENQKGNSSVALHVYMVFISIFSAGKMTFTLLLALLISLGYGIVYPKLDRTLLRRCQIFAIFTFAVCVAFLVQKYSQNSESLSNLILITAIPLVLCLFAFYYLTLSSMNKTMTYLREQNQVVKLNMYRKLIILCYISLFILFLGLLVSTFAYVGMDTVDMIEQYWKTEFLITDTWPSFVYFLVFVIFAFFWRPTSTSYLLACSHQLPTDMENVSEFDLDDINSLSDEALPNREPRNDYQEHDHNMDIDLASDFEEVPSVNANTNANNDVLFDVDYDRDAKNDRSTT
Protein: 60S ribosomal protein L5, putative (Q38CY8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- 40S ribosomal protein S4
- 60S ribosomal protein L35A, putative
- Ribosomal protein L37
- 40S ribosomal protein S5, putative
- 60S ribosomal subunit protein L31, putative
- Eukaryotic translation initiation factor 6
- Small ribosomal subunit protein uS4
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S27, putative
- Large ribosomal subunit protein bL21m
Sequence:
MTFVKVVKNKAYYKRFQVKYRRRREGKTDYHARRRMVLQDKTKFGTPKYRLVVRITNRDVIAQIVHAKVVGDEVVMAAYSHELPLFGIEHGLTNYAAAYATGLLVARRMLAKLGLAEKFVGVKEVDGSYAAVRTKDDDQGDDESRFPFKAILDVGLARTTTGARVFGVLKGAVDGGLAVPHRPNRFPGYNKESDALNAKVHRDRIFGRHVADYLKQVREEASSNPDEKTCQFSKFIAAKVSPDDMEGMYKRAHAAIRADPTKRRAKKERPAEAKPKKYNTVKLTGAEKKAAAKAKVAAVIERIRDRAK
Protein: Metalloendopeptidase OMA1, mitochondrial (EC 3.4.24.-) (Metalloprotease-related protein 1) (MPRP-1) (Overlapping with the m-AAA protease 1 homolog) (Q96E52)
Organism: Homo sapiens (Human)
Function: Metalloprotease that is part of the quality control system in the inner membrane of mitochondria. Activated in response to various mitochondrial stress, leading to the proteolytic cleavage of target proteins, such as OPA1, UQCC3 and DELE1. Following stress conditions that induce loss of mitochondrial membrane potential, mediates cleavage of OPA1 at S1 position, leading to OPA1 inactivation and negative regulation of mitochondrial fusion. Also acts as a regulator of apoptosis: upon BAK and BAX aggregation, mediates cleavage of OPA1, leading to the remodeling of mitochondrial cristae and allowing the release of cytochrome c from mitochondrial cristae. In depolarized mitochondria, may also act as a backup protease for PINK1 by mediating PINK1 cleavage and promoting its subsequent degradation by the proteasome. May also cleave UQCC3 in response to mitochondrial depolarization. Also acts as an activator of the integrated stress response (ISR): in response to mitochondrial stress, mediates cleavage of DELE1 to generate the processed form of DELE1 (S-DELE1), which translocates to the cytosol and activates EIF2AK1/HRI to trigger the ISR. Its role in mitochondrial quality control is essential for regulating lipid metabolism as well as to maintain body temperature and energy expenditure under cold-stress conditions (By similarity). Binds cardiolipin, possibly regulating its protein turnover (By similarity). Required for the stability of the respiratory supercomplexes (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:32132707, ECO:0000305|PubMed:20038677}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9D8H7}.
Interaction partners:
- Dynamin-like GTPase OPA1, mitochondrial
- ATP-dependent zinc metalloprotease YME1L1
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- Presenilin-associated rhomboid-like protein, mitochondrial
- Mitochondrial inner membrane m-AAA protease component paraplegin
- Presenilin-associated rhomboid-like protein, mitochondrial
- DAP3-binding cell death enhancer 1
- Mitofusin-1
- Mitofusin-2
- Lon protease homolog, mitochondrial
Sequence:
MSFICGLQSAARNHVFFRFNSLSNWRKCNTLASTSRGCHQVQVNHIVNKYQGLGVNQCDRWSFLPGNFHFYSTFNNKRTGGLSSTKSKEIWRITSKCTVWNDAFSRQLLIKEVTAVPSLSVLHPLSPASIRAIRNFHTSPRFQAAPVPLLLMILKPVQKLFAIIVGRGIRKWWQALPPNKKEVVKENIRKNKWKLFLGLSSFGLLFVVFYFTHLEVSPITGRSKLLLLGKEQFRLLSELEYEAWMEEFKNDMLTEKDARYLAVKEVLCHLIECNKDVPGISQINWVIHVVDSPIINAFVLPNGQMFVFTGFLNSVTDIHQLSFLLGHEIAHAVLGHAAEKAGMVHLLDFLGMIFLTMIWAICPRDSLALLCQWIQSKLQEYMFNRPYSRKLEAEADKIGLLLAAKACADIRASSVFWQQMEFVDSLHGQPKMPEWLSTHPSHGNRVEYLDRLIPQALKIREMCNCPPLSNPDPRLLFKLSTKHFLEESEKEDLNITKKQKMDTLPIQKQEQIPLTYIVEKRTGS
Protein: PARP-type domain-containing protein (Q38AV1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Uncharacterized protein
- 60S acidic ribosomal protein P0
- 60S ribosomal protein L19, putative
- 60S ribosomal protein L17, putative
- 60S ribosomal protein L39, putative
- 60S ribosomal subunit protein L31, putative
- 60S ribosomal protein L5, putative
- 60S ribosomal protein L6, putative
- 60S ribosomal protein L35A, putative
- 60S ribosomal protein L29
Sequence:
MPQLRVEYAKSGRAKCSAASCNKPISKHEVRVGIAVMFQPVGSTSGEPTLSYKWRHVCCFTERQIKNAEAEGGLDAIEGLEELAEVDRDLIAQMMRGELIDRMDVMGRVGDVENSPASRGSLKGEKFSHSDGRAATKRKRGDGSESRETGSPPDLSKRGKSKKGGVVSLTPSRDKDTNEGEISDSTTEEFEVSVEATRPPCPYGKECFRTSVSHMAEYSHGAESDRAVPARLRAVIRHSV
Protein: RNA binding exosome specificity factor Mmi1 (Meiotic mRNA interception protein 1) (YTH domain-containing protein mmi1) (O74958)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: RNA-binding protein that recognizes and binds N6-methyladenosine (m6A)-containing RNAs, a modification present at internal sites of mRNAs and some non-coding RNAs (By similarity). Functions alone and as part of the erh1-mmi1 complex, to recruit the CCR4-NOT complex and the NURS complex to target RNAs. Suppresses the meiotic program during vegetative growth and promotes the meiotic program during mating. Binds to DSR (determinant of selective removal) regions in meiotic mRNA, and recruits the NURS complex to targets. Recruitment of NURS complex to target mRNAs promotes mRNA decay by engagement of the nuclear exosome, and formation of heterochromatin islands at meiotic genes silenced by the exosome. Recruitment of the CCR4-NOT complex to target RNAs promotes heterochromatin formation at RNAi-dependent heterochromatin domains (HOODs), including a subset of meiotic genes, lncRNAs and retrotransposons. Recruitment of the CCR4-NOT complex to rDNA promotes rDNA heterochromatin assembly. Promotes non-canonical transcription termination at meiotic genes and prevents lncRNA transcription from invading and repressing adjacent genes.
Subcellular location: Nucleus {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:16823445}.
Interaction partners:
- NURS complex subunit red1
- Meiosis protein mei2
- Uncharacterized RNA-binding protein C902.04
- Polyadenylate-binding protein 2
- Poly
- Exosome complex exonuclease rrp6
- Enhancer of rudimentary homolog 1
- Uncharacterized RNA-binding protein C644.16
- UPF0400 protein C337.03
- Cell differentiation protein rcd1
Sequence:
MSNTNFSTSRSSKSIPELPNLEALRSLWPPPSLNESGDTRSVWTTHTGEPVASSVLSTSGSNNFSSPLKRPAPESHDAPIGRRLMVDDPRLIKHGKYDFSRHCTDYGHSYEWPYFRSLRRESMLYHTSGSYPESQPPYSSYSTDAPHYYHAGSESSAYYDSRSRLHGIQPPPKRRTLSPPPRRLADPVVVGSSRYVEEEVYRRPPYTLASEVPSSASAYQAGYSSYPVRSSPQLSHEDTRHGIASSGSTRYPFVPANTRASHSPSLLEPYAHSLPSSVAPVGAYPEKSSYLLSNSSNDSASRKEKPKARASTPPPLNFSRASEHRNEKGERISMINPRVVLDENGISHRSRYFIMLCDNETAIAHAKKTSIWAVKKDSSKRISDAYKKASVYFIFVAQQTYNALGYAQVVSDLNSTELPFWSDSSHAGGVRIKWIKTCNLFSAEISEIVSHMDHGSEARDGMEMMYDEGSRLCTLINYAIMKRIGRDR
Protein: Large ribosomal subunit protein eL36A (60S ribosomal protein L36-A) (Q92365)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS5
- Elongation factor 3
- mRNA export factor elf1
- Small ribosomal subunit protein uS7A
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL28
- Small ribosomal subunit protein eS27
- Small ribosomal subunit protein uS14
Sequence:
MAPGLVVGLNKGKVLTKRQLPERPSRRKGQLSKRTSFVRSIVREVAGFAPYERRVMELIRNSQDKRARKLAKKRLGTLKRAKGKIEELTSVIQSSRLAH
Protein: Pyrroline-5-carboxylate reductase (P5C reductase) (P5CR) (EC 1.5.1.2) (PCA reductase) (P0A9L8)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reduction of 1-pyrroline-5-carboxylate (PCA) to L-proline. Does not catalyze the reverse reaction.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01925, ECO:0000269|PubMed:6296787}.
Interaction partners:
- Bifunctional protein PutA
- Glutamate 5-kinase
- Gamma-glutamyl phosphate reductase
- Ribonuclease HI
- Pyridoxal phosphate homeostasis protein
- N5-carboxyaminoimidazole ribonucleotide mutase
Sequence:
MEKKIGFIGCGNMGKAILGGLIASGQVLPGQIWVYTPSPDKVAALHDQFGINAAESAQEVAQIADIIFAAVKPGIMIKVLSEITSSLNKDSLVVSIAAGVTLDQLARALGHDRKIIRAMPNTPALVNAGMTSVTPNALVTPEDTADVLNIFRCFGEAEVIAEPMIHPVVGVSGSSPAYVFMFIEAMADAAVLGGMPRAQAYKFAAQAVMGSAKMVLETGEHPGALKDMVCSPGGTTIEAVRVLEEKGFRAAVIEAMTKCMEKSEKLSKS
Protein: Gamma-aminobutyric acid receptor subunit beta-3 (GABA(A) receptor subunit beta-3) (GABAAR subunit beta-3) (P28472)
Organism: Homo sapiens (Human)
Function: Ligand-gated chloride channel which is a component of the heteropentameric receptor for GABA, the major inhibitory neurotransmitter in the brain. Plays an important role in the formation of functional inhibitory GABAergic synapses in addition to mediating synaptic inhibition as a GABA-gated ion channel. The gamma2 subunit is necessary but not sufficient for a rapid formation of active synaptic contacts and the synaptogenic effect of this subunit is influenced by the type of alpha and beta subunits present in the receptor pentamer (By similarity). The alpha1/beta3/gamma2 receptor exhibits synaptogenic activity. The alpha2/beta3/gamma2 receptor shows very little or no synaptogenic activity (By similarity). Functions also as histamine receptor and mediates cellular responses to histamine. Plays an important role in somatosensation and in the production of antinociception (By similarity).
Subcellular location: Postsynaptic cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:24909990, ECO:0000269|PubMed:35355020, ECO:0007744|PDB:7QN7}. Cell membrane {ECO:0000269|PubMed:18281286, ECO:0000269|PubMed:18514161, ECO:0000269|PubMed:22243422, ECO:0000269|PubMed:22303015, ECO:0000269|PubMed:24909990, ECO:0000269|PubMed:26950270}; Multi-pass membrane protein {ECO:0000269|PubMed:24909990, ECO:0000269|PubMed:35355020, ECO:0007744|PDB:7QN7}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P63079}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit alpha-1
- Gamma-aminobutyric acid receptor subunit gamma-2
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor subunit alpha-4
- Gamma-aminobutyric acid receptor subunit delta
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid type B receptor subunit 2
- Vesicle-fusing ATPase
- Huntingtin-associated protein 1
- Trafficking kinesin-binding protein 2
Sequence:
MWGLAGGRLFGIFSAPVLVAVVCCAQSVNDPGNMSFVKETVDKLLKGYDIRLRPDFGGPPVCVGMNIDIASIDMVSEVNMDYTLTMYFQQYWRDKRLAYSGIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWRGGDKAVTGVERIELPQFSIVEHRLVSRNVVFATGAYPRLSLSFRLKRNIGYFILQTYMPSILITILSWVSFWINYDASAARVALGITTVLTMTTINTHLRETLPKIPYVKAIDMYLMGCFVFVFLALLEYAFVNYIFFGRGPQRQKKLAEKTAKAKNDRSKSESNRVDAHGNILLTSLEVHNEMNEVSGGIGDTRNSAISFDNSGIQYRKQSMPREGHGRFLGDRSLPHKKTHLRRRSSQLKIKIPDLTDVNAIDRWSRIVFPFTFSLFNLVYWLYYVN
Protein: DNA-binding protein inhibitor ID-4 (Inhibitor of DNA binding 4) (Inhibitor of differentiation 4) (Q90X15)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Myoblast determination protein 1 homolog
Sequence:
MKVAAAAPSPLPAGPGGALKAVRPGEAARCGPGPGAVAAEQAAAALLYDMKGCYSRLRALVPTLPRHRRVSKVELLQHVIDYIWDLQLALQPGPPRPPAAAEPPEAPCMAAADRILCR
Protein: Putative proline--tRNA ligase YHR020W (EC 6.1.1.15) (Prolyl-tRNA synthetase) (ProRS) (P38708)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Isoleucine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Glutamate--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
- Aspartate--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
- Asparagine--tRNA ligase, cytoplasmic
Sequence:
MPVSEAFAKLCVNEKPPAESAVAVKSLVFKPKTPKSATPVPIVVVALQSTTTPSALIANATSSKDPRLARDDLVKQAFQSESARAFILGDLANATSNFHLLIDHELGTVDGDTILQLNDSTYMKKSDMMKFLNNFEDSQKVVDFSQEVSKETATEGKKQQKKQQPSKAGTAAAAAAAALEDAKLIGITVDKALDFPGWYQQILTKGEMLDYYDVSGCYILRPPSYAIWENIQKWFDDKIKAIGVQNAYFPMFVSSRVLEKEKDHVEGFAPEVAWVTRAGSSELEEPIAIRPTSETVMYPYYAKWVQSYRDLPLKLNQWNSVVRWEFKHPQPFLRTREFLWQEGHTAHLTAKDAEEEVLQILDFYAGVYEELLAVPVVKGRKTEKEKFAGGDFTTTCEGYIPQTGRGIQGATSHHLGQNFSKMFNLSVENPLGSDHPKIFAYQNSWGLSTRVIGVMVMIHSDNKGLVIPPRVSQFQSVVIPVGITKKTSEEQRKHIHETARSVESRLKKVGIRAFGDYNDNYTPGWKFSQYELKGIPIRIELGPKDIEKNQVVVVRRNDSKKYVVSFDELEARIPEILEEMQGDLFKKAKELFDTHRVIVNEWSGFVPALNKKNVILAPWCGVMECEEDIKESSAKKDDGEEFEEDDKAPSMGAKSLCIPFDQPVLNEGQKCIKCERIAVNYCMFGRSY
Protein: D-psicose 3-epimerase (DPEase) (EC 5.1.3.30) (A9CH28)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Involved in the biosynthesis of D-psicose. Catalyzes the reversible epimerization of D-fructose at the C3 position to yield D-psicose. The enzyme is highly specific for D-psicose and shows very low activity with D-tagatose. The substrate specificity decreases in the following order: D-fructose, D-tagatose, D-ribulose, D-xylulose, and D-sorbose. It shows a higher level of activity for cis ketoses than for trans-ketoses.
Interaction partners:
Sequence:
MKHGIYYSYWEHEWSAKFGPYIEKVAKLGFDIIEVAAHHINEYSDAELATIRKSAKDNGIILTAGIGPSKTKNLSSEDAAVRAAGKAFFERTLSNVAKLDIHTIGGALHSYWPIDYSQPVDKAGDYARGVEGINGIADFANDLGINLCIEVLNRFENHVLNTAAEGVAFVKDVGKNNVKVMLDTFHMNIEEDSFGDAIRTAGPLLGHFHTGESNRRVPGKGRMPWHEIGLALRDINYTGAVIMEPFVKTGGTIGSDIKVWRDLSGGADIAKMDEDARNALAFSRFVLGG
Protein: Serine/threonine-protein kinase atg1 (EC 2.7.11.1) (Autophagy-related protein 1) (Serine/threonine-protein kinase ppk36) (Q9Y7T4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes. Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates. Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (By similarity). Autophagy functions to supply nitrogen and is activated when cells cannot access exogenous nitrogen, thus ensuring that they can adapt and subsequently propagate. Finally, atg13 is also required for glycogen storage during stationary phase and has a role in meiosis and sporulation.
Interaction partners:
- Autophagy-related protein 9
- Autophagy-related protein 2
- Autophagy protein 13
- Vacuolar protein sorting-associated protein atg6
- Autophagy-related protein 8
- Autophagy-related protein 17
- Taz1-interacting factor 1
- Autophagy-related protein 101
- Autophagy protein 5
- Ubiquitin-like protein ATG12
Sequence:
MNLQTSTNQTIGPYVIRSEIGRGSFAIVYKGKHTETNRVISIKSVLTKKLTKKLLENLESEISILKEIRHVHVVELIDCIKAGRFIHLVMEYCSLGDLSYFIRKREKFNSIPSLAWINIDHPPVYKAGLNETLVRHFTQQLASALQFLRSRSLIHRDVKPQNLLLQPPPTAAYLEEHPQFVGSPKLPMLKLADFGFARYLQTSSMAETLCGSPLYMAPEILRYEKYDAKADLWSVGAVLYEMAVGKPPFKAPNHVELLRRIQKAKDVIKFPEEAFIHPDIKTLICALLKQNPADRIDYDGFFSSIVVTTPLDDASTLTGSDIQDAVKEINIPSSSPAYITDFFPKSNPGAPAPPGGLLRQAFQAQGSSIQPSEITGRRVPHRYAQDGNTLPYTPVFPPESAPAASIFPPRLTSKQPIPMASPAKLTSDTSNKSSAYVVVDHHPIISSTQLSNESLTHEQSINGNSPSPNEGVFQGSFSPESAPVNNHAFPHTSRMQIPYMKPNAFPSNPTYIASTPVTQLRRAFEQATAHVPQSGGGARNKSALERALNVANARLNEVVVDGMTDNGNTSLPTKESNLDNNVNIIQPSLPDTGKRLLDVLESIAMKSNSVYHLAEVKLAQIIPSLSDEMKPGDTLLDRPLTPFSLVMLAKESYVLYERDIELLQVAFDGVAAFWANSEERASPDCQQAIEWFRQRYSESLEKSQFLREIIISQSAAHSLPTTKPVSASQLIYHRALDLSRNAATSELSGNDAQACLQNYRLAAHLLESLLESNFSTPDGANDSNNSVTIRNLIALITKRQELLQSKQIQANVANKVTESVAKITLAPNLA
Protein: Killer cell lectin-like receptor subfamily B member 1 (Killer cell lectin-like receptor subfamily B member 1G) (Natural killer cell surface protein NKR-P1G) (Natural killer lectin-like receptor 1E) (Q0ZUP1)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000255}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- C-type lectin domain family 2 member H
- C-type lectin domain family 2 member G
- Granzyme A
- C-type lectin domain family 2 member D
Sequence:
MDAPVLYAELNLAETRGLRCTSAPSLPQDACQGPGWHRVALKLGCAGLIFLLMVLSVLVGFLVQKPLIEKCSVAVQENRTEPTGRSATLECPRDWHPHCDKCLFTSQTSRPWADGLVDCNLKGATLLLIQDEEELRLLQNFSKGKGQQFYIGLKYEEVDKVWKWMNGSILNTNLLQITGKDEENSCALISQTEVFSDSCSSDNHWICQKTLKHV
Protein: Pro-secreted protein ORF2 (Protein ORF2) (pORF2) [Cleaved into: Secreted protein ORF2 (ORF2s)] (Q68985)
Organism: Hepatitis E virus genotype 1 (isolate Human/India/Hyderabad) (HEV-1)
Function: Plays a role in the inhibition of host antibody-mediated neutralization without blocking viral cell entry.
Subcellular location: [Isoform Secreted protein ORF2]: Secreted {ECO:0000250|UniProtKB:Q81871}. Note=Cotranslationally translocated into the ER (PubMed:10196303). Translation from the first AUG produces a full-length protein with a signal peptide that can direct the protein into the secretory pathway (By similarity). {ECO:0000250|UniProtKB:Q9YLQ9, ECO:0000269|PubMed:10196303}.; SUBCELLULAR LOCATION: [Isoform Capsid protein]: Virion {ECO:0000250|UniProtKB:Q81871}. Host cytoplasm {ECO:0000269|PubMed:11934888, ECO:0000269|PubMed:17229684, ECO:0000269|PubMed:8523527}. Host endoplasmic reticulum {ECO:0000250|UniProtKB:Q81871}. Host Golgi apparatus {ECO:0000250|UniProtKB:Q81871}. Host cell surface {ECO:0000269|PubMed:10196303, ECO:0000269|PubMed:17229684, ECO:0000269|PubMed:8523527}. Note=Translation from the internal AUG codon disrupts the signal sequence, producing a cytoplasmic protein that is responsible for virion assembly (By similarity). Shuttles between cytoplasm and nucleus (By similarity). This isoform is found in quasi-enveloped virions (By similarity). {ECO:0000250|UniProtKB:P33426, ECO:0000250|UniProtKB:Q81871, ECO:0000250|UniProtKB:Q9YLQ9}.
Interaction partners:
Sequence:
MGPRPILLLFLMFLPMLLAPPPGQPSGRRRGRRSGGSGGGFWGDRVDSQPFAIPYIHPTNPFAPNVTAAAGAGPRVRQPVRPLGSAWRDQAQRPAAASRRRPTTAGAAPLTAVAPAHDTPPVPDVDSRGAILRRQYNLSTSPLTSSVATGTNLVLYAAPLSPLLPLQDGTNTHIMATEASNYAQYRVARATIRYRPLVPNAVGGYAISISFWPQTTPTPTSVDMNSITSTDVRILVQPGIASELVIPSERLHYRNQGWRSVETSGVAEEEATSGLVMLCIHGSPVNSYTNTPYTGALGLLDFALELEFRNLTPGNTNTRVSRYSSTARHRLRRGADGTAELTTTAATRFMKDLYFTSTNGVGEIGRGIALTLFNLADTLLGGLPTELISSAGGQLFYSRPVVSANGEPTVKLYTSVENAQQDKGIAIPNDIDLGESRVVIQDYDNQHEQDRPTPSPAPSRPFSVLRANDVLWLSLTAAEYDQSTYGSSTGPVYVSDSVTLVNVATGAQAVARSLDWTKVTLDGRPLSTIQQYSKIFFVLPLRGKLSFWEAGTTRPGYPYNYNTTASDQLLVENAAGHRVAISTYTTSLGAGPVSISAVAVLGPHSALALLEDTLDYPARAHTFDDFCPECRPLGLQGCAFQSTVAELQRLKMKVGKTREL