wanglab/gogpt-training-data huggingface dataset:
Protein: Protein ACTIVITY OF BC1 COMPLEX KINASE 7, chloroplastic (ABC1-LIKE KINASE 7) (EC 2.7.11.1) (Salt-induced ABC1 kinase 1, chloroplastic) (AtSIA1) (B9DGY1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in resistance to oxidative stress. Influences responses to reactive oxygen species (ROS) production. Regulates plastoglobules formation in thylakoids. Together with OSA1, regulates iron distribution within the chloroplast and mediates the oxidative stress response. Together with ABC1K8, influences chloroplast lipid synthesis/accumulation and modulates chloroplast membrane composition in response to stress.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000269|PubMed:24117441}; Multi-pass membrane protein {ECO:0000255}. Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:22274653, ECO:0000305|PubMed:22694836}.
Interaction partners:
- Probable plastid-lipid-associated protein 13, chloroplastic
- Tocopherol cyclase, chloroplastic
Sequence:
MAALLASQSCCYGGETARVTKAIGFSSSLENHFTGEATQCYGSKSKRFRIEMRQSELPSKVGINGRSVKMVPASEVVKRKDGVNGSAGKGVNGASLVSSRNINGAASTLVKAPKKTTESYLPPPVEGVRVLPSDEGFSWADENYSSLQRSIDVWSFVISLRIRILFDNSKWAYVGGFTEEKQKSRRRETASWLRESVLQLGPTFIKLGQLSSTRSDLFPREFVDELSKLQDRVPAFSPEKAKRFIEAELGAPISVMYKEFEEQPIAAASLGQVHRAVLHNGEKVVVKVQRPGLKKLFDIDLRNLKLIAEYFQKSESFGTNDWVGIYEECALILYQEIDYINEAKNADRFRRDFRNINWVRVPLVYWDYSAMKVLTLEYVPGVKINNLDALAARGFNRSRIASRAIEAYLIQILKTGFFHADPHPGNLAIDVDESIIYYDFGMMGEIKTFTRKRLLDLFYSVYEKDAKKVMQNLIDLEALQPTGDLSSVRRSVQFFLDNLLSQSPDQQQTLAAIGEDLFAISQDQPFRFPSTFTFVIRAFSTLEGIGYILDPEFSFVKVAAPYAQELLDLKQRQRSGTQLVQEIRKQADDARSSTLSMPYRVQRIEEFVKELDSGDLKLRVRVLESERAARKATILQMATMYTVLGGTLLNIGVTFSNQGSQLVANGSFIGAGIFMLLVLRSMQRVNKLDKFEKMI
Protein: Glutamate receptor (Q90855)
Organism: Gallus gallus (Chicken)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|RuleBase:RU367118}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU367118}.
Interaction partners:
Sequence:
MQHIFAFFCTSFLGVVLGANFPNNIQIGGLFPNQQSQEHAAFRFALSQLTEPPKLLPQIDIVNISDSFEMTYTFCSQFSKGVYAIFGFYERRTVNMLTSFCGALHVCFITPSFPVETSNQFVLQLRPELQDALISVIEHYSWQKFVYIYDADRGLSVLQKVLDTAAEKNWQVTAVNILTTTEEGYRVLFQELQKKKERLVVVDCESERLNIILSKIIKLEKNGNGYHYILANMGFMDIDLTKFRESGANVTGFQLVNYTDTVPARIMQQWRNNDARELPRVDWKRPKYTSALTYDGVRVMAEAFQNLRRQRIDISRRGNAGDCLANPAVPWGQGIDIQRALQQVRFEGLSGNVQFNEKGRRTNYTLHVIEMKHDGIRKIGYWNEDEKLVPVAIDTQTGNESTSLQNRTYIVTTILEDPYVMLKKNANQFEGNERYEGYCVELAAEIAKHVGYHYRLEIVRDGKYGARDPDTKTWNGMVGELVYGRADVAVAPLTITLVREEVIDFSKPFMSLGISIMIKKPQKSKPGVFSFLDPLAYEIWMCIVFAYIGVSVVLFLVSRFSPYEWHTEEFEEGRDQPANDQTNEFGIFNSLWFSLGAFMQQGCDISPRSLSGRIVGGVWWFFTLIIISSYTANLAAFLTVERMVSPIESAEDLAKQTEIAYGTLEAGSTKEFFRRSKIAVFEKMWTYMKSAEPSVFVRTTEEGMIRVRKSKGKYAYLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGIATPKGSALRGPVNLAVLKLSEQGVLDKLKSKWWYDKGECGSKDSGSKDKTSALSLSNVAGVFYILIGGLGLAMLVALIEFCYKSRSESKRMKGFCLIPQQSINEAIRTSTLPRPAAAGGSGENGRVVSHDFPKSMQTIPCMSHSTGMSLGATGL
Protein: Ribonuclease VapC2 (RNase VapC2) (EC 3.1.-.-) (Toxin VapC2) (P9WFB9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Toxic component of a type II toxin-antitoxin (TA) system. Acts as an RNase. Upon expression in M.smegmatis inhibits translation, growth and colony formation. All its toxic effects are neutralized by coexpression with cognate antitoxin VapB2.
Interaction partners:
- Antitoxin VapB2
- Putative antitoxin VapB5
- Ribonuclease VapC5
- Antitoxin VapB30
- Ribonuclease VapC30
- Uncharacterized protein Rv0966c
- Carbamoyl phosphate synthase small chain
- Uncharacterized protein Rv3412
- Dihydroorotase
- Putative antitoxin VapB18
Sequence:
MTDQRWLIDKSALVRLTDSPDMEIWSNRIERGLVHITGVTRLEVGFSAECGEIARREFREPPLSAMPVEYLTPRIEDRALEVQTLLADRGHHRGPSIPDLLIAATAELSGLTVLHVDKDFDAIAALTGQKTERLTHRPPSA
Protein: Probable G-protein coupled receptor 75 (Q6X632)
Organism: Mus musculus (Mouse)
Function: G protein-coupled receptor that is activated by the chemokine CCL5/RANTES. Probably coupled to heterotrimeric Gq proteins, it stimulates inositol trisphosphate production and calcium mobilization upon activation. Together with CCL5/RANTES, may play a role in neuron survival through activation of a downstream signaling pathway involving the PI3, Akt and MAP kinases. CCL5/RANTES may also regulate insulin secretion by pancreatic islet cells through activation of this receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein {ECO:0000305|PubMed:17001303}.
Interaction partners:
- C-C motif chemokine 5
Sequence:
MNTSAPLQNVPNATLLNMPPLHGGNSTSLQEGLRDFIHTATLVTCTFLLAIIFCLGSYGNFIVFLSFFDPSFRKFRTNFDFMILNLSFCDLFICGVTAPMFTFVLFFSSASSIPDSFCFTFHLTSSGFVIMSLKMVAVIALHRLRMVMGKQPNCTASFSCILLLTLLLWATSFTLATLATLRTNKSHLCLPMSSLMDGEGKAILSLYVVDFTFCVAVVSVSYIMIAQTLRKNAQVKKCPPVITVDASRPQPFMGASVKGNGDPIQCTMPALYRNQNYNKLQHSQTHGYTKNINQMPIPSASRLQLVSAINFSTAKDSKAVVTCVVIVLSVLVCCLPLGISLVQMVLSDNGSFILYQFELFGFTLIFFKSGLNPFIYSRNSAGLRRKVLWCLRYTGLGFLCCKQKTRLRAMGKGNLEINRNKSSHHETNSAYMLSPKPQRKFVDQACGPSHSKESAASPKVSAGHQPCGQSSSTPINTRIEPYYSIYNSSPSQQESGPANLPPVNSFGFASSYIAMHYYTTNDLMQEYDSTSAKQIPIPSV
Protein: Meiotic nuclear division protein 1 homolog (AtMND1) (Meiotic nuclear division 1-like protein) (Q8GYD2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for proper homologous chromosome pairing and efficient cross-over and intragenic recombination during meiosis. Stimulates both DMC1/LIM15- and RAD51-mediated homologous strand assimilation, which is required for the resolution of meiotic double-strand breaks.
Subcellular location: Nucleus {ECO:0000269|PubMed:17937504}. Nucleus, nucleolus {ECO:0000269|PubMed:17937504}. Note=Localized to chromatin during meiosis.
Interaction partners:
- Homologous-pairing protein 2 homolog
- DNA repair protein RAD51 homolog 1
- Meiotic recombination protein DMC1 homolog
- DNA mismatch repair protein MSH5
- DNA mismatch repair protein MSH4
- Meiotic recombination protein SPO11-1
- DNA repair protein RAD51 homolog 3
- Meiotic recombination protein SPO11-2
- Meiosis-specific protein ASY1
- DNA mismatch repair protein MSH2
Sequence:
MSKKRGLSLEEKREKMLQIFYESQDFFLLKELEKMGPKKGVISQSVKDVIQSLVDDDLVAKDKIGISIYFWSLPSCAGNQLRSVRQKLESDLQGSNKRLAELVDQCEALKKGREESEERTEALTQLKDIEKKHKDLKNEMVQFADNDPATLEAKRNAIEVAHQSANRWTDNIFTLRQWCSNNFPQAKEQLEHLYTEAGITEDFDYIELSSFPLSSSHEADTAKQLVQDEA
Protein: 3-hydroxyacyl-CoA dehydrogenase type-2 (EC 1.1.1.35) (17-beta-hydroxysteroid dehydrogenase 10) (17-beta-HSD 10) (EC 1.1.1.51, EC 1.1.1.62) (3-hydroxyacyl-CoA dehydrogenase type II) (Hydroxysteroid dehydrogenase) (EC 1.1.1.-, EC 1.1.1.53) (Mitochondrial ribonuclease P protein 2) (Mitochondrial RNase P protein 2) (Scully protein) (Type II HADH) (O18404)
Organism: Drosophila melanogaster (Fruit fly)
Function: Versatile enzyme presenting two types of activity; L-3-hydroxyacyl-CoA dehydrogenase ((3S)-3-hydroxyacyl-CoA dehydrogenase) activity and hydroxysteroid dehydrogenase (HSD) activity with a wide substrate spectrum. As a (3S)-3-hydroxyacyl-CoA dehydrogenase, it functions in the third step of the fatty acid beta-oxidation pathway, a major metabolic process in which fatty acids are oxidized to provide a significant source of energy, while also generating acyl-CoA metabolites used by many metabolic routes (Probable). As a HSD, it functions in the degradation pathways of glucocorticoids and sex steroids and epimerization of bile acids; catalyzes the beta-oxidation at position 17 of androgens and estrogens, has 3-alpha-hydroxysteroid dehydrogenase activity with androsterone, and carries out oxidative conversions of 7-beta-hydroxylated bile acids like ursodeoxycholate or isoursodeoxycholate (also known as 3-beta,7-beta-dihydroxy-5-beta-cholan-24-oate or 7-beta-hydroxyisolithocholate, respectively). Also exhibits 20-beta-OH and 21-OH dehydrogenase activities with C21 steroids. Required for cell survival during embryonic development. May play a role in germline formation.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:27131785, ECO:0000269|PubMed:34199774}. Note=Localizes to the lipid droplet fraction in early embryos (PubMed:16979555). {ECO:0000269|PubMed:16979555}.
Interaction partners:
- Mitochondrial ribonuclease P catalytic subunit
- Mitochondrial ribonuclease P protein 1 homolog
- Probable enoyl-CoA hydratase, mitochondrial
- acetyl-CoA C-acyltransferase
- Trifunctional enzyme subunit alpha, mitochondrial
- HL08109p)
- Transcription initiation factor TFIID subunit 11
- LD23072p
- Protein argonaute-2
- Protein argonaute-1
Sequence:
MIKNAVSLVTGGASGLGRATAERLAKQGASVILADLPSSKGNEVAKELGDKVVFVPVDVTSEKDVSAALQTAKDKFGRLDLTVNCAGTATAVKTFNFNKNVAHRLEDFQRVININTVGTFNVIRLSAGLMGANEPNQDGQRGVIVNTASVAAFDGQIGQAAYSASKAAVVGMTLPIARDLSTQGIRICTIAPGLFNTPMLAALPEKVRTFLAKSIPFPQRLGEPSEYAHLVQAIYENPLLNGEVIRIDGALRMMP
Protein: NADH dehydrogenase [ubiquinone] flavoprotein 2, mitochondrial (EC 7.1.1.2) (NADH-ubiquinone oxidoreductase 24 kDa subunit) (Q9D6J6)
Organism: Mus musculus (Mouse)
Function: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:38575788}; Peripheral membrane protein {ECO:0000269|PubMed:38575788}; Matrix side {ECO:0000269|PubMed:38575788}.
Interaction partners:
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 alpha subcomplex subunit 5
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH-ubiquinone oxidoreductase chain 5
- NADH dehydrogenase iron-sulfur protein 6, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 6
- NADH dehydrogenase 1 beta subcomplex subunit 3
Sequence:
MFSLALRARATGLAAQWGRHARNLHKTAVHNGAGGALFVHRDTPENNPDTPFDFTPENYKRIEAIVKNYPEGHQAAAVLPVLDLAQRQNGWLPISAMNKVAEVLQVPPMRVYEVATFYTMYNRKPVGKYHIQVCTTTPCMLRDSDSILETLQRKLGIKVGETTPDKLFTLIEVECLGACVNAPMVQINDNYYEDLTPKDIEEIIDELKAGKVPKPGPRSGRFCCEPAGGLTSLTEPPKGPGFGVQAGL
Protein: Cytochrome B translational activator CBS2 (P14905)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Translational activator of cytochrome b. The cytochrome b (coB) leader RNA may represent the target sequence for CBS1 and/ or CBS2.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:2270079}.
Interaction partners:
- Cytochrome b translational activator protein CBS1, mitochondrial
- Cytochrome b
- Protein CBP3
- Cytochrome b mRNA maturase bI2
- Cytochrome b mRNA maturase bI3
- Assembly factor CBP4
- Cytochrome B pre-mRNA-processing protein 6
- Cytochrome B pre-mRNA-processing protein 2
- Cytochrome b termination protein 1
- COX3 mRNA-specific translational activator PET494
Sequence:
MSSSIPRVYSLGNSAMTYLLALRIAQLPSQPKVPSVVLLLNDQKKLNRFLNNDSKIIVKSSNNNKETYHRQFMASCVPPILSNGEIAPIENLIVSDPSSKFITAQLSKYNKSLRPETNILFLNPSLNLLEHLHRYRWRFDEARPNLFMGFTTPVDVGTIHQEFQLSLKVKGRIQFHIAKIDGFPRMSSTGKSASLSLRGDRQKNEKENNAFYKLFREISRLRSGIGSDLVSFDLHVHGFQDLFFTELEKLILESCTEPLLAVYDCVYKKELLKIPGAQDIIKKLISEQLSIIDRSYPSLNTNPNYSVIFDKERIFSLVMRDLEVNGHKRAKLAQSLNQLNQTNINELNGFFVSLGKYKKCNCKWNDILLTLIKGKQFITKQKALDYHYL
Protein: Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial (Protein ECSIT) (Q9U6M0)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the innate immune response. Promotes the production of antibacterial peptides.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9BQ95}. Nucleus {ECO:0000250|UniProtKB:Q9BQ95}. Mitochondrion {ECO:0000250|UniProtKB:Q9BQ95}.
Interaction partners:
- Complex I intermediate-associated protein 30, mitochondrial
- GH01161p
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- Complex I assembly factor TIMMDC1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
- Transmembrane protein 70 homolog
- NADH dehydrogenase 1 alpha subcomplex assembly factor 3
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- NADH-ubiquinone oxidoreductase chain 4
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial
Sequence:
MLRRAQCLLRLHGNGGHSLVSRFRNYATDEGNPKQNPNPNPRAQKPGTKNLPALRNPFAAAQDRTKNSYLTMVEIFQERDVHRRNHVEFIYAALKNMADFGVERDLEVYKALINVMPKGKFIPTNMFQAEFMHYPKQQQCIIDLLEQMEDCGVMPDHEMEAMLLNVFGRQGHPLRKYWRMMYWMPKFKNLSPWPLPDPVPDDTLEMAKLALERMCTVDLRSKITVFETSELKDAIDDTWIVSGMSPEQEKLLREHSRQKALYIEGPFHIWLRNRRINYFTLRADADSEFLSELDERQLDEDDVSHIEVPFFGRAPPRRHNQLGKLRSVHQQDDGTIMAICATGTSTKDSLLSWIRLLEANGNPSIGEVPVLFRFTSEVPAKAEEIEGGASVPATSDNSSQDEHISSRQK
Protein: Nonsense-mediated mRNA decay factor EBS1 (EST1-like BCY1 suppressor 1) (Q03466)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a role in nonsense-mediated mRNA decay (NMD). Recruits UPF1 to cytoplasmic mRNA decay bodies (P-bodies). Negative regulator of gene expression. Inhibits translation most likely through effects on eIF-4E (CDC33). Involved in telomere maintenance.
Subcellular location: Nucleus {ECO:0000305}. Chromosome, telomere {ECO:0000305}. Cytoplasm, P-body {ECO:0000269|PubMed:17984081}.
Interaction partners:
- Protein NAM8
- U1 small nuclear ribonucleoprotein A
- Nonsense-mediated mRNA decay protein 3
- ATP-dependent helicase NAM7
- Nuclear cap-binding protein subunit 2
- Cell division control protein 13
- Nonsense-mediated mRNA decay protein 2
- EST/SMG-like protein 1
- Uncharacterized protein YDR274C
- Nonsense-mediated decay protein 4
Sequence:
MEPSNTQKEDLPTAFNGIKSQLNSILKSNQLFQDYALLNGFLAFVHSKLNAAILTSIESQCGKSFAADLDSFDQSSISSILDFSWESVHYPIFKWFQMWRNYILFEKENKKQQTKFIDFRKMNSKMLKFFKTVQNFYVNVINTVYKKYDISVLLPKRIIQDLKLSDIENTTNVGDILAVKTFNSSSPLAHLIPTLFHRCLLFLGTAYRYKTLLEEISNKYSISNFKKSLDFFRLASLVLPSAGETYSQAGAIFLQTGNLGIAVFNFVKGMMTKMPSPVSIKNFGALMVDNKSSLNRSLHTTIMNTYLQESKGPRTPAKEILEFYFLGLFGSVWSPTSWRDDTKPNQLNNGIKLRHLENALYETMSARYLNNIKTIFHNLIITIGGFHLLLKRRSDVSAKTLKDLRSNELDYLNFAFKYIAHILNDIVKESWSENPEVSEILGMVRIINCWIKANPMVLQYSQSNLEFVNALAYLINDIVKKKPSPSFSITEHIPKRTYWFEEDLMVKGLSFVNFQLSDFDDYEKILEMDHSLDRLIGNPPLCDKLSASSEMLLRLQAVVNISSQLLQNNNCGVEWSDNKSRYIFNKKIGFKETVKNSMKTSKQSNEKAKLQRKNKPSTTNGSISMADLERQMRSSSLDSFSPTMGYSGSSVPMAPDTFNVKPSGTITGNKVNVELLKIELSGQNADGAITNISPGYSNAAISSSNSTDESSFDLNNILSSMQQKHAEKSFAKSMQGVNEQIPANDVCHQAQRPMQGGLYSSQQPSSMSSLNSAYQNASMPPSASMVSYPYPFLNQQGQGVFPPYNAQNLQWQSEAYSLKSMNFANPTWLGDQYQTSAPSSAYAQAQRQMFQQPMQQDVGKYMQFPFDAQSNTDSMRGNSRNNMF
Protein: Short-chain dehydrogenase/reductase VdtF (EC 1.-.-.-) (Viriditoxin biosynthesis cluster protein F) (A0A443HJZ3)
Organism: Byssochlamys spectabilis (Paecilomyces variotii)
Function: Short-chain dehydrogenase/reductase; part of the gene cluster that mediates the biosynthesis of viriditoxin, one of the 'classical' secondary metabolites produced by fungi and that has antibacterial activity. The first step is performed by the polyketide synthase VdtA which condenses one acetyl-CoA and 6 malonyl-CoA units to form the heptaketide monomer backbone of viriditoxin. The product of VdtA is then O-methylated on C7 by the O-methyltransferase VdtC. The O-methyl group is important for the stereoselective coupling of the monomers at the final step of viriditoxin biosynthesis. The short-chain dehydrogenase/reductase VdtF then acts as a stereospecific reductase converting the pyrone to dihydropyrone via the reduction of the C3-C4 double bond. The FAD-binding monooxygenase VdtE then converts the ketone group into a methyl-ester group to yield semi-viriditoxin. Finally, the laccase VdtB is involved in dimerization of 2 semi-viriditoxin molecules to yield the final viriditoxin. VdtB is responsible for the regioselective 6,6'-coupling of semi-viriditoxin, which yields (M)-viriditoxin and (P)-viriditoxin at a ratio of 1:2. The non-catalytic carboxylesterase-like protein VdtD affects the stereochemistical outcome of the coupling. The highly reducing polyketide synthase VdtX is not involved in viriditoxin synthesis, but might possibly play a role in the production of additional metabolites not identified yet.
Interaction partners:
Sequence:
MDGKALTASSLFDITGRVAVITGGGTGLGLMMAKALEANGAKVYILGRRLEPLQEAAKQSTHGNIHPVQCSVTSHADLQGVVDHIAAKDGYINLLVNNAGISTPNLGPHATRPTPKWDISKVRDYWFHKSFADYAAVFETNTTASLMVTFAFLELLDKGNKKSEEEAKASQARNGAGKARIEYVRSQVVTLSSVGGFGRDNSAFIYGASKAAATHMMKNLATYLAPWKIRVNVIAPGYFNTDMMGNFYKATGGRLPASLAPEERFGDAQEIGGTIVYLASKAGAYCNGMVLLVDGGYVSNKPSSY
Protein: ArsR family transcriptional regulator (CzrA protein) (HTH-type transcriptional repressor CzrA) (Repressor protein) (Transcriptional repressor, arsR family) (Zn(II)-responsive metalloregulatory transcriptional repressor CzrA) (O85142)
Organism: Staphylococcus aureus
Interaction partners:
Sequence:
MSEQYSEINTDTLERVTEIFKALGDYNRIRIMELLSVSEASVGHISHQLNLSQSNVSHQLKLLKSVHLVKAKRQGQSMIYSLDDIHVATMLKQAIHHANHPKESGL
Protein: E3 ubiquitin-protein ligase CBL (EC 2.3.2.27) (A0A061I5T4)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Interaction partners:
Sequence:
LQLNSLGPEACRDLRDLLLHNQCQITTLRKFKFNPRLGIDNPVLSLAEDQDQSDPWNLRRPRFCLLSKEEEKSFGFHLQQQLGKADHVVCRVDPGSSAQRHGLREGDRILAVNNKNVEHEDYAMVVRCIRASGPRVLLTVLAQHAHDVVRAQQGSDVFCCPALGPEVRPRLCHIVKDEGGFGFSITHGNRGPFWLVLSSGGAAERAGVPPGARLLEVNGVCVEKFTSNQLSRKVVRLCQNPKLALKNSPPYILDLLPDTYQHLRTVLSRYEGKMETLGENEYFRVFMENLMKKTKQTISLFKEGKERMYEENSQPRRNLTKLSLIFSHMLAELKGIFPSGLFQGDTFRITKADAAEFWRKAFGEKNWNSLAVTHPGYMAFLTYDEVKARLQKFIHKPGSYLFPDGRNQNPDLTGLCEPTPQDHIKVTQEQYELYCEMGSTFQLCKICAENDKDVKIEPCGHLMCTSCLTSWQESEGQGCPFCRCEIKGTEPIVVDPFDPRGSGSLLRQGAEGAPSPNYDDDDDERADDSLFMMKELAGAKAASGSLHKDKPLPIPPTLRDLPPPPPPDRPYSVGTETRPQRRPLPCTPGDCPSRDKLPPVPSSRPGDSWLPRPIPKVPIATPSPNDPWNGRELTNRHSLPFSLPSQMEPRVDVPRLGSTFSLDTSMNMNSSPIAGPENEHPKIKPSSSANAIYSLAARPLPVPKLPPGEQGESEEDAEYMTPTSRPVGAQKPEPKRPLEATQSSRACDCDQQIDSCTYEAMYNIQSQALSVTENSTFGEGNLATAPTSTGPEESENEDDGYDVPKPPVPAVLARRTLSDISNASSSFGWLSLDGDPTTNFNEGSQVPERPPKPFPRRINSERKASSCQQGGATANPSATAPSPQLSSEIERLMSQGYSYQDIQKALVIAHNNIEMAKNILREFVSISSPAHVAT
Protein: PPT2 (A0A1U9X8D2)
Organism: Homo sapiens (Human)
Subcellular location: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
Sequence:
MLGLCGQRLPAAWVLLLLPFLPLLLLAAPAPHRASYKPVIVVHGLFDSSYSFRHLLEYINETHPGTVVTVLDLFDGRESLRPLWEQVQGFREAVVPIMAKAPQGVHLICYSQGGLVCRALLSVMDDHNVDSFISLSSPQMGQYGDTDYLKWLFPTSMRSNLYRICYSPWGQEFSICNYWHDPHHDDLYLNASSFLALINGERDHPNATVWRKNFLRVGHLVLIGGPDDGVITPWQSSFFGFYDANETVLEMEEQLVYLRDSFGLKTLLARGAIVRCPMAGISHTAWHSNRTLYETCIEPWLS
Protein: GMP synthase (glutamine-hydrolyzing) (EC 6.3.5.2) (Glutamine amidotransferase) (Q57V01)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Inosine-5'-monophosphate dehydrogenase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- Inosine-5'-monophosphate dehydrogenase
- Guanylate kinase, putative
- Guanylate kinase, putative
- Hypoxanthine phosphoribosyltransferase
- Hypoxanthine phosphoribosyltransferase
- Nucleoside diphosphatase, putative
- Dihydroorotate dehydrogenase
Sequence:
MSVQQEPVTECVVILDAGSQYGKVIDRKVRELRVESRVMPLDTPTDILRSDPSIKGIIISGGPSSISDADAPSYNTDLFSVGKPLLGICYGVQLLTRAFGGKVGCAGVREDGQDEITVDTNSPIFHGLSNKEKVLLTHGDSITEAGPHLKVTARSSAHIIAAVQHESLPLFGVQFHPEVELTENGVQILKNFLTFCGCKFTFTMEDREEKALRLIRERTTQGQKVLCLASGGVDSTVCAVLLLKALGPERVVCIHIDHGFMRLNESQEVVAALRAAGVNVTLIDATKQFSEATTEFPAKRGKGAYQTGKLCEAIDPEEKRVIIGNTFMSVCDAAVKDLNLDVNNLLLAQGTLRPDLIESGSAYASKVADAIKTHHNDTAVVRQLRAEGRIIEPLCDYHKDEVRELGTRLGIPTHLVQRQPFPGPGLAIRVLCSDGSLFKDEHYARTEENVRAVCAGDERFELLKPLCKELRSLQPASCILPIRTVGVQGDGRTYAYAAALSIGRLPNKEEWNSLGRLALVIPKLTSNVNRIVFMFGPKRAEAPLKATKSSLVPEVLDKLRLADDTVNRALIKYGLVRRLSQVPVVLLPIGFEEKGPFSVVIRPFITNDFMTGVPAAPGSADMPLEALKEIVETLQGFDFISRVMYDLTGKPPGTTEWE
Protein: Prostate-associated microseminoprotein (PC3-secreted microprotein) (Q1L6U9)
Organism: Homo sapiens (Human)
Function: Acts as a ligand for C-C chemokine receptor CCR2. Signals through binding and activation of CCR2 and induces a strong chemotactic response and mobilization of intracellular calcium ions. Exhibits a chemotactic activity for monocytes and lymphocytes but not neutrophils.
Subcellular location: Secreted {ECO:0000269|PubMed:17338636, ECO:0000269|PubMed:24442440}.
Interaction partners:
- Non-lysosomal glucosylceramidase
- Beta-microseminoprotein
Sequence:
MALRMLWAGQAKGILGGWGIICLVMSLLLQHPGVYSKCYFQAQAPCHYEGKYFTLGESWLRKDCFHCTCLHPVGVGCCDTSQHPIDFPAGCEVRQEAGTCQFSLVQKSDPRLPCKGGGPDPEWGSANTPVPGAPAPHSS
Protein: NAD(P)H-quinone oxidoreductase subunit I, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit I) (NDH subunit I) (NADH-plastoquinone oxidoreductase subunit I) (P0C386)
Organism: Oryza sativa subsp. japonica (Rice)
Function: NDH shuttles electrons from NAD(P)H:plastoquinone, via FMN and iron-sulfur (Fe-S) centers, to quinones in the photosynthetic chain and possibly in a chloroplast respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be plastoquinone. Couples the redox reaction to proton translocation, and thus conserves the redox energy in a proton gradient.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01351}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01351}.
Interaction partners:
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- NADH dehydrogenase iron-sulfur protein 2
- Os10g0576000 protein
Sequence:
MFPMVTGFMSYGQQTIRAARYIGQSFIITLSHTNRLPITIHYPYEKSITSERFRGRIHFEFDKCIACEVCVRVCPIDLPLVDWRFEKDIKRKQLLNYSIDFGVCIFCGNCVEYCPTNCLSMTEEYELSTYDRHELNYNQIALSRLPISIMGDYTIQTIRNSTQSKIDEEKSWNSRTITDY
Protein: 1-aminocyclopropane-1-carboxylate synthase (EC 4.4.1.14) (A9NIT9)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- aminocyclopropanecarboxylate oxidase
- aminocyclopropanecarboxylate oxidase
- aminocyclopropanecarboxylate oxidase
- aminocyclopropanecarboxylate oxidase
- aminocyclopropanecarboxylate oxidase
- aminocyclopropanecarboxylate oxidase
- aminocyclopropanecarboxylate oxidase
- aminocyclopropanecarboxylate oxidase
- aminocyclopropanecarboxylate oxidase
- aminocyclopropanecarboxylate oxidase
Sequence:
MVAISKIATGNGHGEDSPYFDGWKAYETNPFHPIDRPDGVIQMGLAENQLCFNFIKKWVMEHPEASLCSAEGVNKFKETALFQDYHGMPEFREAVAKFMGKVRGGRVKFDPDRIVMSGGATGAHEMVAFCLADPGEAFLVPTPYYPGFDRDLSWRTGVELVPVVCESSNNFKITRAALEAAYEKAKEANLRVKGLLITNPSNPLGTILDQDTLKGIVKFINEKNIHLIGDEIYAATVFMEPEFVSISEIIEEVECNRDLIHIVYSLSKDMGFPGFRVGIVYSYNDAVVSCARKMSSFGLVSSQTQHLIAKMLSDDDFVDRFIVESKEQLLKRHKYFTLSLSQVGIGSLKSNAGLFIWMDLRKLLKEKTFDAEMDLWRVIINEVKLNVSPGSSFHCDEPGWFRVCFANMDDNTMEVALLRITTFMHKHNEAMVPRKLCRRASLKLSLSRRRDDFMSPNMMSPHSPIPQSPLVRART
Protein: N-acetylmuramoyl-L-alanine amidase AmiC (EC 3.5.1.28) (P63883)
Organism: Escherichia coli (strain K12)
Function: Cell-wall hydrolase involved in septum cleavage during cell division. Can also act as powerful autolysin in the presence of murein synthesis inhibitors.
Subcellular location: Periplasm {ECO:0000269|PubMed:12787347}. Note=Present throughout the periplasm in non-dividing cells, but localizes almost exclusively to a ring at the site of constriction in dividing cells.
Interaction partners:
- Cell division protein FtsN
- Murein hydrolase activator NlpD
- N-acetylmuramoyl-L-alanine amidase AmiB
- N-acetylmuramoyl-L-alanine amidase AmiA
- Peptidoglycan D,D-transpeptidase FtsI
- Cell division protein FtsA
- Penicillin-binding protein 1B
- Cell division protein FtsQ
- Cell division ATP-binding protein FtsE
- Probable peptidoglycan glycosyltransferase FtsW
Sequence:
MSGSNTAISRRRLLQGAGAMWLLSVSQVSLAAVSQVVAVRVWPASSYTRVTVESNRQLKYKQFALSNPERVVVDIEDVNLNSVLKGMAAQIRADDPFIKSARVGQFDPQTVRMVFELKQNVKPQLFALAPVAGFKERLVMDLYPANAQDMQDPLLALLEDYNKGDLEKQVPPAQSGPQPGKAGRDRPIVIMLDPGHGGEDSGAVGKYKTREKDVVLQIARRLRSLIEKEGNMKVYMTRNEDIFIPLQVRVAKAQKQRADLFVSIHADAFTSRQPSGSSVFALSTKGATSTAAKYLAQTQNASDLIGGVSKSGDRYVDHTMFDMVQSLTIADSLKFGKAVLNKLGKINKLHKNQVEQAGFAVLKAPDIPSILVETAFISNVEEERKLKTATFQQEVAESILAGIKAYFADGATLARRG