wanglab/gogpt-training-data huggingface dataset:
Protein: Anthocyanidin 3-O-glucoside 5-O-glucosyltransferase (EC 2.4.1.298) (Anthocyanin 5-O-glucosyltransferase) (Gt5GT7) (B2NID7)
Organism: Gentiana triflora (Clustered gentian)
Function: Catalyzes the glucosylation at the O-5 position of anthocyanidin 3-glucosides to form anthocyanidin 3,5-di-O-glucosides using UDP-glucose as sugar donor. Anthocyanidin 3,5-di-O-glucosides are molecules that are responsible for pigmentation. Involved in biosynsthesis of accumulate gentiodelphin, a unique polyacylated delphinidin-type anthocyanin, in the petals. Also acts on anthocyanidin 3-O-(6-O-malonylglucoside). Much less active with hydroxycinnamoylglucose derivatives. No activity in the absence of the 3-O-glucoside group.
Interaction partners:
Sequence:
MVGRGKGKGREHVLLVVFPAQGHISPALQLAFKIVAHSSIDLTFLTSSSAVASILIGLPPTAPALNFAAFSQGNLHNDDDDDDDAKDYMHTLCKHGSQSVRDIIHSTKKGQGQGQGQGQGQGQGQGHPITRILYTTLLPWAADVAREFRLPSVLLWTQPVTTFLTFHYYFTGYEDAINKVRNQQGTEDDSTIQLPRLPLLSSRDLHSFMLPSNPFKGAINTFKEHLEALDAEETPPTILVNSYDALEEEALQAMIPKYKTMGIGPLIPSSVFDTRETTCEVVSLVPDLAQKSKDDCQWHGWLNSKAEGSVIYVSFGSHVKQSKAQTEEIAKGLLASGHPFLWVITSNEEEEGDEIMEQNLVEEIQEKGMMIVPWCAQFQVLKHPSVGCFMTHCGWNSTLESIACGVPMIGFPKMFDQPTISKLIAHVWKVGVRVNAAVDGIVGQEVIKNCIESVMDPDGIGRELNENVRKFMSLGKKAAEEGGSSHNNFKAFLQDMTGGTTTIN
Protein: Pleckstrin homology domain-containing family A member 2 (PH domain-containing family A member 2) (Tandem PH domain-containing protein 2) (TAPP-2) (Q9HB19)
Organism: Homo sapiens (Human)
Function: Binds specifically to phosphatidylinositol 3,4-diphosphate (PtdIns3,4P2), but not to other phosphoinositides. May recruit other proteins to the plasma membrane (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Nucleus {ECO:0000250}. Note=Locates to the plasma membrane after treatments that stimulate the production of PtdIns3,4P2. {ECO:0000250}.
Interaction partners:
- Tyrosine-protein phosphatase non-receptor type 13
- Utrophin
- Pleckstrin homology domain-containing family A member 1
- Pleckstrin-2
Sequence:
MPYVDRQNRICGFLDIEEHENSGKFLRRYFILDTQANCLLWYMDNPQNLAMGAGAVGALQLTYISKVSIATPKQKPKTPFCFVINALSQRYFLQANDQKDMKDWVEALNQASKITVPKGGGLPMTTEVLKSLAAPPALEKKPQVAYKTEIIGGVVVHTPISQNGGDGQEGSEPGSHTILRRSQSYIPTSGCRASTGPPLIKSGYCVKQGNVRKSWKRRFFALDDFTICYFKCEQDREPLRTIFLKDVLKTHECLVKSGDLLMRDNLFEIITSSRTFYVQADSPEDMHSWIKEIGAAVQALKCHPRETSFSRSISLTRPGSSSLSSGPNSILCRGRPPLEEKKALCKAPSVASSWQPWTPVPQAGEKLLPPGDTSEDSLFTPRPGEGSAPGVLPSSRIRHRSEPQHPKEKPFMFNLDDENIRTSDV
Protein: Wolframin (Q8IMZ9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Participates in the regulation of cellular Ca(2+) homeostasis, at least partly, by modulating the filling state of the endoplasmic reticulum Ca(2+) store (By similarity). In neurons and glial cells, has a role in maintaining neuronal function and integrity during aging.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum {ECO:0000269|PubMed:29357349}. Mitochondrion {ECO:0000269|PubMed:29357349}.
Interaction partners:
- Atf6, isoform C
- Cadherin-99C
Sequence:
MATWTQNEPTGVTKRRRWNLEDRASLNKLKHHIAEEGCPQMQYDLAKELLDNSIVEPNLAKGNQSQKAVNWLVSAAHNGHEDAVKLLRQCYNDGSGITAENTDEVRRCLAMTPGERAARKAARELFACLSNGNEHITPKQLERKMRRIYNLQRKRRRRDDDRSSSSSEGEQEPECEPLEDVPTIDLANVERRRLITEAHLVSAASNYSAGQMPSVNDALTLSVPDPRSLDHVPCFYRMIFHPLIFFTLFYHRLLNLIVSIPNVIPLSVRCSVLVAISWWSSRHMLPLVSYYLSLGIMIWATCKMLKTKQQFVDFRIWSGLFLSYGDQNIEADIAEHRFLRNNMKPYLYFFCAFICNLIVYPLVTDAWLPHSELTIISGALTFITMCVSMYASSHQLPDWLVIVSFAVNVLAKYPYEMDEVVSTRWRFLDLRVPTFSSFVIGNGIEFCLNCRTALYLFIPVLLIMMAKRSRWHGVYTFLIPHCVTLSWLQVCIATSQSSTVFGVMRAALGLAGIVLFLPLFGIVALLVPVFVAIDSLGLASEQLRWGSTALACGLVVVLSCILALNRATQKYITMLQLITAITTACLLVLPYMTSSFKDTPRFNAMPRAGLHSLSETNTLPWDRFHALCAQPVHEQPNKIKAQLRCSLLNGMPVIWEGSVTKVEISRVSNFLEDTIANYLPVWLGRMLRCLHGENISQHFKCDPKLDAQCEEWRSVFKTFNAQSGSCTLQRWNRYEYELLVKVGTKRSGRLLGRSTTTDVILRAHHDFGNFTRLLSEGDVVLFYGILHNSRLLADNVQVKLKTIECVECRSRDLGTASIERVVAASPMDARLQDLMRGIKYLLNALLNPLITFK
Protein: Deoxyhypusine hydroxylase (DOHH) (EC 1.14.99.29) (Deoxyhypusine dioxygenase) (Deoxyhypusine monooxygenase) (Q9V9U4)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the hydroxylation of the N(6)-(4-aminobutyl)-L-lysine intermediate to form hypusine, an essential post-translational modification only found in mature eIF-5A factor (By similarity). Essential for organismal viability and plays a role in a wide number of important processes such as cell growth and proliferation, and regulates induction of autophagy and protein synthesis. Has a role in eIF-5A-mediated translational control.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:19546244}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:19546244}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03101, ECO:0000269|PubMed:19546244}. Note=In larval imaginal disk and Garland cells.
Interaction partners:
- Eukaryotic translation initiation factor 5A
- Probable deoxyhypusine synthase
- Spermidine synthase, isoform A
- Ornithine decarboxylase 1
- Arginase
- Glutamate-rich WD repeat-containing protein 1
- Zinc finger protein 593 homolog
- S-adenosylmethionine decarboxylase proenzyme
- Probable ATP-dependent RNA helicase pitchoune
- Ornithine decarboxylase 2
Sequence:
MVSQQQIEAIGGVLNNKERPLKERFRALFTLKNIGGGAAIEAISKAFDDDSALLKHELAYCLGQMQDAQALDILTKVLKDTTQEPMVRHEAAEAMGAIGHPDVLPILEEYKQDPVVEVAETCAIALDRVRWLQSGQKVDDSNPYASVDPSPPTAGDKSVTELKAIYLDAQQSLFDRYRAMFSLRNLRTEESVLAIAEGLKDSSALFRHEVAFVLGQLQEPCSIPFLQENLEDRLENEMVRHECAEALGAIATEDCIQILNRYAEDDKRVVKESCVIALDMCEYENSPEFQYADGLAKLDATK
Protein: CUGBP Elav-like family member 2 (V9GYD9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNGALDHSDQPDPDAIKMFVGQIPRSWSEKELKELFEPYGAVYQINVLRDRSQNPPQSKGCCFVTFYTRKAALEAQNALHNIKTLPGMHHPIQMKPADSEKSNAVEDRKLFIGMVSKKCNENDIRVMFSPFGQIEECRILRGPDGLSRGCAFVTFSTRAMAQNAIKAMHQSQTMEGCSSPIVVKFADTQKDKEQRRLQQQLAQQMQQLNTATWGNLTGLGGLTPQYLALLQQATSSSNLGAFSGIQQMAGMNALQLQNLATLAAAAAAAQTSATSTNANPLSTTSSALGALTSPVAASTPNSTAGAAMNSLTSLGTLQGLAGATVGLNNINALAGTINSMAALNGGLGATGLTNGTAGTMDALTQAYSGIQQYAAAALPTLYSQSLLQQQSAAGSQKEGFVSYDNPVSAQAAIQAMNGFQIGMKRLKVQLKRSKNDSKPY
Protein: Gamma-secretase subunit Aph-1 (Presenilin-stabilization factor) (Q9VQG2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch. It probably represents a stabilizing cofactor for the presenilin homodimer that promotes the formation of a stable complex.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nicastrin
- Gamma-secretase subunit pen-2
- Presenilin homolog
- Neurogenic locus Notch protein
- Mitochondrial magnesium exporter 1
- LD12265p
Sequence:
MTLPEFFGCTFIAFGPPFALFVFTIANDPVRIIILIAAAFFWLLSLLISSLWYALIPLKEFLAFGVVFSVCFQEAFRYIIYRILRSTEQGLHAVAEDTRVTDNKHILAYVSGLGFGIISGMFALVNVLADMSGPGTMGLKGGTELFFVTSAAQALSIILLHTFWSVIFFNAFDTNNYIHIGYVVFSHLFVSLITLLNANELYTTTLLINYLVTILTGVLAFRVAGGTSRSFRKFITCQ
Protein: ERMES regulator 1 (Q4ZGE1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mediates the formation of endoplasmic reticulum (ER)-mitochondria encounter structure (ERMES) foci, thereby contributing to the formation of ER-mitochondrial contact sites.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:33483504}; Single-pass type III membrane protein {ECO:0000269|PubMed:33483504}.
Interaction partners:
- Uncharacterized AAA domain-containing protein C24B10.10c
- Putative endoplasmic reticulum metallopeptidase 1
- Uncharacterized CDP-alcohol phosphatidyltransferase class-I family protein C22A12.10
- Ubiquitin-conjugating enzyme E2 6
- Translation initiation factor IF-2, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 3
- Mitochondrial Rho GTPase 1
- Phosphatidylserine decarboxylase proenzyme 2, mitochondrial
Sequence:
MLPNLRRIFASFRTEEEERSYSRKAFFHLIGYITCSVLFSWLVRKKVISSPVVSSPIHALS
Protein: Voltage-gated hydrogen channel 1 (Hydrogen voltage-gated channel 1) (HV1) (Voltage sensor domain-only protein) (mVSOP) (Q3U2S8)
Organism: Mus musculus (Mouse)
Function: Mediates the voltage-dependent proton permeability of excitable membranes. Forms a proton-selective channel through which protons may pass in accordance with their electrochemical gradient. Proton efflux, accompanied by membrane depolarization, facilitates acute production of reactive oxygen species in phagocytosis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q96D96}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q96D96}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:24415791}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, flagellum membrane {ECO:0000250|UniProtKB:Q96D96}; Multi-pass membrane protein {ECO:0000255}. Note=Detected within the principal piece of the sperm flagellum. {ECO:0000250|UniProtKB:Q96D96}.
Interaction partners:
- Potassium channel subfamily U member 1 current)
Sequence:
MTSHDPKAVTRRTKVAPTKRMSRFLKHFTVVGDDYHTWNVNYKKWENEEEEEEPAPTSAEGEGNAEGPDAEAGSASTPRQSLDFRSRLRKLFSSHRFQVIIICLVVLDALLVLAELLLDLKIIEPDEQDYAVTAFHYMSFAILVFFMLEIFFKIFVFRLEFFHHKFEILDAFVVVVSFVLDLVLLFKSHHFEALGLLILLRLWRVARIINGIIISVKTRSERQILRLKQINIQLATKIQHLEFSCSEKEQEIERLNKLLKQNGLLGDVN
Protein: RING 1B (F4I2H4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MPSLKSFSAAEEEDDQLGRNSEAERFNPEAVEKEEDPDKMDEKDESGDEEDDVKRDQVEAEDEEALGEEEVSDSKERSQSSSAGELSESEYMVVDLADICKDVQCSICLGIIRKTRTVMECLHRFCRECIDKSMRLGNNECPTCRKHCASRRSLRDDPNFDALIAALFKNIDKFEEEELNFRQDDEARNKQIQASIAQVSQRQSKALVKRKSVGKGTAILSRSRRSGGGSRRRRNCRNIEQDTSEANDDDDQNKRGKDSSSDEPCERQRKKRSATQPSSSNANNNDNCAGNGTEQTHQRDSRVISPVLVWNSELIAWGRGGTRSNTRQGNNNQGAISKRNARLKRLVEYLGSLEGNSVELDIHLKLVSLDTEGLLNLHEPYLCFRPTLLVKQLREVSSLPLYVARHLKLKAEEVELLVSKDGDTVIGNKTSTEKMQSLQDDETVAKLKVDCISSNGYMIVVYRRKQIA
Protein: Leucine-rich repeat, isoform A (RE68846p) (Q8IGL5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGLMRTLCCCFGAGQSNQSSGASPAYKACPDEEPLEELVTDPERADQSPKNEIEQSLAAAISDRATDEVLEALTRYRRGMGIAESPSVLLDEPQTPDIVRSRSSHDADGLIIRPGGRGSILPKLGLESPTATPHLPTKRRSLAKKVRPQSVVENLSLGHFPDLLESPSSHRSNSQLSARAAAGAAALVGAANMTDSIAVDDGGVDECCDSITELPSASFQLQHLVKGRPKRAKTRAPTRPLVTTECAGGSREIGEGLEHFFRPGSVTPTTLTPLVSPTSEECSSLSFVDSPTMSRDGNGHMTSEETTPILEERRPIKLERQSPLLKSASWATRSRSTDNLEKYSPLVGRKSPLVKMRTEGGPGSGSATGAEETSMPSSNLLKATAREDKTRSPSSDSIKSHAAGEGSVIVKTGNGILRTPIVLQKPRPWSVVGSEPKAGGDLITGNGNADSSKTTPDKLEEDDVEIVTFGNTCSGSIVGITPGIALSTSGGGSIVGITPGGALEKKSVRELAAGLNRMELPLKPPVMPRTLLNATSVRTSTSSTGSTSNSVSVSSSTNANTSMTVLNQSQTRSRIVSSTSSTDSTETITERSTTSTSSSSSSSYEKQHAKACANLISNEILSMRNGQLGAKSGSCAESGGVKRIAGKEISTLFEV
Protein: Short tail fiber protein gp12 (Gene product 12) (gp12) (P10930)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Structural component of the short tail fiber. Adhesion protein that binds irreversibly to the lipopolysaccharides component (LPS) on the cell surface of Escherichia coli B strains during virus attachment. After at least three long tail fibers have bound, short tail fibers extend and bind irreversibly to the core region of the host cell LPS.
Subcellular location: Virion {ECO:0000269|PubMed:27193680}.
Interaction partners:
Sequence:
MSNNTYQHVSNESRYVKFDPTDTNFPPEITDVQAAIAAISPAGVNGVPDASSTTKGILFIPTEQEVIDGTNNTKAVTPATLATRLSYPNATETVYGLTRYSTNDEAIAGVNNESSITPAKFTVALNNAFETRVSTESSNGVIKISSLPQALAGADDTTAMTPLKTQQLAIKLIAQIAPSETTATESDQGVVQLATVAQVRQGTLREGYAISPYTFMNSSSTEEYKGVIKLGTQSEVNSNNASVAVTGATLNGRGSTTSMRGVVKLTTTAGSQSGGDASSALAWNADVIQQRGGQIIYGTLRIEDTFTIANGGANITGTVRMTGGYIQGNRIVTQNEIDRTIPVGAIMMWAADSLPSDAWRFCHGGTVSASDCPLYASRIGTRYGGNPSNPGLPDMRGLFVRGSGRGSHLTNPNVNGNDQFGKPRLGVGCTGGYVGEVQIQQMSYHKHAGGFGEHDDLGAFGNTRRSNFVGTRKGLDWDNRSYFTNDGYEIDPESQRNSKYTLNRPELIGNETRPWNISLNYIIKVKE
Protein: Aldo-keto reductase family 1 member D1 (EC 1.3.1.3) (3-oxo-5-beta-steroid 4-dehydrogenase) (Delta(4)-3-ketosteroid 5-beta-reductase) (Delta(4)-3-oxosteroid 5-beta-reductase) (P31210)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the stereospecific NADPH-dependent reduction of the C4-C5 double bond of bile acid intermediates and steroid hormones carrying a delta(4)-3-one structure to yield an A/B cis-ring junction. This cis-configuration is crucial for bile acid biosynthesis and plays important roles in steroid metabolism. Capable of reducing a broad range of delta-(4)-3-ketosteroids from C18 (such as, 17beta-hydroxyestr-4-en-3-one) to C27 (such as, 7alpha-hydroxycholest-4-en-3-one).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P51857}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase type 7
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Cytochrome P450 family 8 subfamily B member 1
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- 11-beta-hydroxysteroid dehydrogenase type 2
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 17-beta-hydroxysteroid dehydrogenase type 3
- UDP-glucuronosyltransferase 2B1
- Aldo-keto reductase family 1, member C1
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
Sequence:
MNLSTANHHIPLNDGNSIPIIGLGTYSDPRPVPGKTFIAVKTAIDEGYRHIDGAYVYRNEHEVGEAIREKVAEGKVKREEIFYCGKLWSTDHDPEMVRPALERTLQTLKLDYIDLYIIEMPMAFKPGEEFYPKDENGRVIYHKSNLCATWEALEACKDAGLVKSLGVSNFNRRQLEVILNKPGLKYKPVTNQVECHPYFTQTKLLEVSASSMTSFIVAYSPLGTCRNPLWVNVSSPPLLKDELLTSLGKKYNKTQAQIVLRFDIQRGLVVIPKSTTPERIKENFQIFDFSLTKEEMKDIEALNKNVRFVEMLMWSDHPEYPFHDEY
Protein: NAD(P)H-quinone oxidoreductase subunit J, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit J) (NADH-plastoquinone oxidoreductase subunit J) (P0C340)
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_01357}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_01357}; Stromal side {ECO:0000255|HAMAP-Rule:MF_01357}.
Interaction partners:
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NADH dehydrogenase iron-sulfur protein 2
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
Sequence:
MQQGWLSNWLVKHEVVHRSLGFDHRGIETLQIKAEDWDSIAVILYVYGYNYLRSQCAYDVAPGGSLASVYHLTRIQYGIDNPEEVCIKVFAQKDNPRIPSVFWIWRSSDFQERESFDMVGISYDNHPRLKRILMPESWIGWPLRKDYITPNFYEIQDAH
Protein: Signal transducer and activator of transcription (F7FAC1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU046415}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU046415}.
Interaction partners:
Sequence:
MSQWNQVQQLEIKFLEQVDQFYDDNFPMEIRHLLAQWIETQDWEVASNNETMATILLQNLLIQLDEQLGRVSKEKNLLLIHNLKRIRKVLQGKFHGNPMHVAVVISNCLREERRILAAANMPIQGPLEKSLQSSSVSERQRNVEHKVAAIKNSVQMTEQDTKYLEDLQDEFDYRYKTIQTMDQGDKNSILVNQEVLTLQEMLNNLDFKRKEALSKMTQIVNETDLLMNSMLLEELQDWKKRQQIACIGGPLHNGLDQLQNCFTLLAESLFQLRQQLEKLQEQSTKMTYEGDPIPAQRVHLLERATFLIYNLFKNSFVVERQPCMPTHPQRPMVLKTLIQFTVKLRLLIKLPELNYQVKVKASIDKNVSTLSNRRFVLCGTHIKAMSSEESSNGSLSVEFRHLQPKEMKCSTGSKGNEGCHMVTEELHSITFETQICLYGLTINLETSSLPVVMISNVSQLPNAWASIIWYNVSTNDSQNLVFFNNPPSVTLGQLLEVMSWQFSSYVGRGLNSDQLNMLAEKLTVQSNYSDGHLTWAKFCKEHLPGKTFTFWTWLEAILDLIKKHILPLWIDGYIMGFVSKEKERLLLKDKMPGTFLLRFSESHLGGITFTWVDQSENGEVRFHSVEPYNKARLSALPFADILRDYKVIMAENIPENPLKYLYPDIPKDKAFGKHYSSQPCEVSRPTERGDKGYVPSVFIPISTIRSDSTEPQSPSDLLPMSPSAYAVLRENLSPTTIETAVCPPPSMVM
Protein: Serine protease 33 (EC 3.4.21.-) (Serine protease EOS) (Q8NF86)
Organism: Homo sapiens (Human)
Function: Serine protease that has amidolytic activity, cleaving its substrates before Arg residues.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Oligodendrocyte transcription factor 2
Sequence:
MRGVSCLQVLLLLVLGAAGTQGRKSAACGQPRMSSRIVGGRDGRDGEWPWQASIQHRGAHVCGGSLIAPQWVLTAAHCFPRRALPAEYRVRLGALRLGSTSPRTLSVPVRRVLLPPDYSEDGARGDLALLQLRRPVPLSARVQPVCLPVPGARPPPGTPCRVTGWGSLRPGVPLPEWRPLQGVRVPLLDSRTCDGLYHVGADVPQAERIVLPGSLCAGYPQGHKDACQGDSGGPLTCLQSGSWVLVGVVSWGKGCALPNRPGVYTSVATYSPWIQARVSF
Protein: Disulfide-bond oxidoreductase YghU (EC 1.8.4.-) (GSH-dependent disulfide-bond oxidoreductase YghU) (GST N2-2) (Organic hydroperoxidase) (EC 1.11.1.-) (Q46845)
Organism: Escherichia coli (strain K12)
Function: Exhibits a robust glutathione (GSH)-dependent disulfide-bond reductase activity toward the model substrate, 2-hydroxyethyl disulfide; the actual physiological substrates are not known. Also displays a modest GSH-dependent peroxidase activity toward several organic hydroperoxides, such as cumene hydroperoxide and linoleic acid 13(S)-hydroperoxide, but does not reduce H(2)O(2) or tert-butyl hydroperoxide at appreciable rates. Exhibits little or no GSH transferase activity with most typical electrophilic substrates, and has no detectable transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) with glutathionylspermidine (GspSH) as the nucleophilic substrate.
Interaction partners:
- Glutathionyl-hydroquinone reductase YqjG
Sequence:
MTDNTYQPAKVWTWDKSAGGAFANINRPVSGPTHEKTLPVGKHPLQLYSLGTPNGQKVTIMLEELLALGVTGAEYDAWLIRIGDGDQFSSGFVEVNPNSKIPALRDHTHNPPIRVFESGSILLYLAEKFGYFLPQDLAKRTETMNWLFWLQGAAPFLGGGFGHFYHYAPVKIEYAINRFTMEAKRLLDVLDKQLAQHKFVAGDEYTIADMAIWPWFGNVVLGGVYDAAEFLDAGSYKHVQRWAKEVGERPAVKRGRIVNRTNGPLNEQLHERHDASDFETNTEDKRQG
Protein: Auxin-responsive protein SAUR29 (Protein SMALL AUXIN UP RNA 29) (Q9SRV9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as positive effectors of cell expansion through modulation of auxin transport (By similarity). Involved in thermo-responsiveness of plant architecture. Enhances plasma membrane H(+)-ATPase.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9FJG1}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9FJG1}.
Interaction partners:
- TORTIFOLIA1-like protein 4
- non-specific serine/threonine protein kinase
- Gibberellin-regulated protein 7
Sequence:
MALVRGFMAAKKILGGSVAGTRKETSAPKGFLAVYVGESQRKKQRHLVPVSYLNQPLFQALLIKAEEEFGFNHPMGGLTIPCPEDTFLTVTSQIQG
Protein: Putative nucleoside permease NupX (P33021)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDVMRSVLGMVVLLTIAFLLSVNKKKISLRTVGAALVLQVVIGGIMLWLPPGRWVAEKVAFGVHKVMAYSDAGSAFIFGSLVGPKMDTLFDGAGFIFGFRVLPAIIFVTALVSILYYIGVMGILIRILGGIFQKALNISKIESFVAVTTIFLGQNEIPAIVKPFIDRLNRNELFTAICSGMASIAGSTMIGYAALGVPVEYLLAASLMAIPGGILFARLLSPATESSQVSFNNLSFTETPPKSIIEAAATGAMTGLKIAAGVATVVMAFVAIIALINGIIGGVGGWFGFEHASLESILGYLLAPLAWVMGVDWSDANLAGSLIGQKLAINEFVAYLNFSPYLQTAGTLDAKTVAIISFALCGFANFGSIGVVVGAFSAVAPHRAPEIAQLGLRALAAATLSNLMSATIAGFFIGLA
Protein: Pleckstrin homology domain-containing family A member 4 (PH domain-containing family A member 4) (Phosphoinositol 3-phosphate-binding protein 1) (PEPP-1) (Q9H4M7)
Organism: Homo sapiens (Human)
Function: Binds specifically to phosphatidylinositol 3-phosphate (PtdIns3P), but not to other phosphoinositides.
Subcellular location: Cytoplasm {ECO:0000305}. Membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}.
Interaction partners:
- Kelch-like protein 12
- Pleckstrin
- Pleckstrin-2
Sequence:
MEGSRPRSSLSLASSASTISSLSSLSPKKPTRAVNKIHAFGKRGNALRRDPNLPVHIRGWLHKQDSSGLRLWKRRWFVLSGHCLFYYKDSREESVLGSVLLPSYNIRPDGPGAPRGRRFTFTAEHPGMRTYVLAADTLEDLRGWLRALGRASRAEGDDYGQPRSPARPQPGEGPGGPGGPPEVSRGEEGRISESPEVTRLSRGRGRPRLLTPSPTTDLHSGLQMRRARSPDLFTPLSRPPSPLSLPRPRSAPARRPPAPSGDTAPPARPHTPLSRIDVRPPLDWGPQRQTLSRPPTPRRGPPSEAGGGKPPRSPQHWSQEPRTQAHSGSPTYLQLPPRPPGTRASMVLLPGPPLESTFHQSLETDTLLTKLCGQDRLLRRLQEEIDQKQEEKEQLEAALELTRQQLGQATREAGAPGRAWGRQRLLQDRLVSVRATLCHLTQERERVWDTYSGLEQELGTLRETLEYLLHLGSPQDRVSAQQQLWMVEDTLAGLGGPQKPPPHTEPDSPSPVLQGEESSERESLPESLELSSPRSPETDWGRPPGGDKDLASPHLGLGSPRVSRASSPEGRHLPSPQLGTKAPVARPRMSAQEQLERMRRNQECGRPFPRPTSPRLLTLGRTLSPARRQPDVEQRPVVGHSGAQKWLRSSGSWSSPRNTTPYLPTSEGHRERVLSLSQALATEASQWHRMMTGGNLDSQGDPLPGVPLPPSDPTRQETPPPRSPPVANSGSTGFSRRGSGRGGGPTPWGPAWDAGIAPPVLPQDEGAWPLRVTLLQSSF
Protein: 26S proteasome non-ATPase regulatory subunit 3 homolog A (26S proteasome regulatory subunit RPN3a) (AtRPN3a) (26S proteasome regulatory subunit S3 homolog A) (Protein EMBRYO DEFECTIVE 2719) (Protein HAPLESS 15) (Q9LNU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Interaction partners:
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 2 homolog A
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 1 homolog A
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome regulatory subunit RPN13
- 26S proteasome non-ATPase regulatory subunit 13 homolog B
- 26S proteasome non-ATPase regulatory subunit 13 homolog A
Sequence:
MTQDVEMKDNNTPSQSIISSSTSTMQNLKEIAALIDTGSYTKEVRRIARAVRLTIGLRQKLTGSVLSSFLDFALVPGSEAHSRLSSFVPKGDEHDMEVDTASSATQAAPSKHLPAELEIYCYFIVLLFLIDQKKYNEAKACSSASIARLKNVNRRTIDVIASRLYFYYSLSYEQTGDLAEIRGTLLALHHSATLRHDELGQETLLNLLLRNYLHYNLYDQAEKLRSKAPRFEAHSNQQFCRYLFYLGKIRTIQLEYTDAKESLLQAARKAPIAALGFRIQCNKWAILVRLLLGEIPERSIFTQKGMEKALRPYFELTNAVRIGDLELFRTVQEKFLDTFAQDRTHNLIVRLRHNVIRTGLRNISISYSRISLPDVAKKLRLNSENPVADAESIVAKAIRDGAIDATIDHKNGCMVSKETGDIYSTNEPQTAFNSRIAFCLNMHNEAVRALRFPPNTHKEKESDEKRRERKQQEEELAKHMAEEDDDDF
Protein: Low affinity immunoglobulin gamma Fc region receptor III-A (IgG Fc receptor III-A) (CD16-2) (FcgammaRIV) (CD antigen CD16a) (Q6XPU4)
Organism: Rattus norvegicus (Rat)
Function: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Binds with intermediate affinity to both IgG2a and IgG2b. Can bind to IgG2a and IgG2b monomers. Does not display binding to IgG1 or IgG3 (By similarity). Recognizes neutralizing virus-specific IgGs displayed on the cell surface of infected cells and triggers antibody-dependent cellular cytotoxicity (ADCC). Confers protection to lethal influenza virus infection (By similarity). On splenic dendritic cells, uptakes antigen immune complexes and efficiently divert them into MHC class I and II antigen presentation pathways to provide for superior priming of CD4-positive and CD8-positive T cell immune responses (By similarity). Mediates neutrophil activation by IgG complexes redundantly with FCGR2A (By similarity). Plays a role in promoting bone resorption by enhancing osteoclast differentiation following binding to IgG2a (By similarity). Also acts as a receptor for the Fc region of immunoglobulin epsilon (IgE). Binds with low affinity to both the a and b allotypes of IgE. Has also been shown to bind to IgE allotype a only but not to allotype b. Binds aggregated IgE but not the monomeric form and bound monomeric IgG is readily displaced by IgE complexes. Binding to IgE promotes macrophage-mediated phagocytosis, antigen presentation to T cells, production of pro-inflammatory cytokines and the late phase of cutaneous allergic reactions (By similarity). Mediates enhanced ADCC in response to afucosylated IgGs.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:A0A0B4J1G0}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MWYLLLPTALLLTVSSGVGAGLQKAVVNLDPEWVRVLEEDCVILRCQGTFSPEDNSTKWFHNKSLISHQDANYVIQSARVKDSGMYRCQTAFSALSDPVQLDVHADWLLLQTTKRLFQEGDPIRLRCHSWRNTPVFKVTYLQNGKGKKYFHRNSELSISKATHADSGSYFCRGIIGRNNISSASLQISIGDPTSPSSFLPWHQITFCLLIGLLFAIDTVLYFSVQRSLQSSVAVYEEPKLHWSKEPQDK