wanglab/gogpt-training-data huggingface dataset:
Protein: 11-beta-hydroxysteroid dehydrogenase type 2 (11-DH2) (11-beta-HSD2) (EC 1.1.1.-) (Corticosteroid 11-beta-dehydrogenase isozyme 2) (NAD-dependent 11-beta-hydroxysteroid dehydrogenase) (P51661)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of biologically active 11beta-hydroxyglucocorticoids (11beta-hydroxysteroid) such as corticosterone, to inactive 11-ketoglucocorticoids (11-oxosteroid) such as 11-dehydrocorticosterone, in the presence of NAD(+) (Probable). Functions as a dehydrogenase (oxidase), thereby decreasing the concentration of active glucocorticoids, thus protecting the nonselective mineralocorticoid receptor from occupation by glucocorticoids. Plays an important role in maintaining glucocorticoids balance during preimplantation and protects the fetus from excessive maternal corticosterone exposure. Catalyzes the oxidation of 11beta-hydroxytestosterone (11beta,17beta-dihydroxyandrost-4-ene-3-one) to 11-ketotestosterone (17beta-hydroxyandrost-4-ene-3,11-dione), a major bioactive androgen. Catalyzes the conversion of 11beta-hydroxyandrostenedione (11beta-hydroxyandrost-4-ene-3,17-dione) to 11-ketoandrostenedione (androst-4-ene-3,11,17-trione), which can be further metabolized to 11-ketotestosterone (By similarity). Converts 7-beta-25-dihydroxycholesterol to 7-oxo-25-hydroxycholesterol in vitro (By similarity). 7-beta-25-dihydroxycholesterol (not 7-oxo-25-hydroxycholesterol) acts as ligand for the G-protein-coupled receptor (GPCR) Epstein-Barr virus-induced gene 2 (EBI2) and may thereby regulate immune cell migration (By similarity).
Subcellular location: Microsome {ECO:0000250|UniProtKB:P80365}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P80365}.
Interaction partners:
- Cytochrome P450 11B2, mitochondrial
- steroid 11beta-monooxygenase
- 11-beta-hydroxysteroid dehydrogenase 1
- Steroid 21-hydroxylase
- Aldo-keto reductase family 1 member D1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 6
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 3
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
Sequence:
MERWPWPSGGAWLLVAARALLQLLRSDLRLGRPLLAALALLAALDWLCQRLLPPPAALVVLAGAGWIALSRLARPPRLPVATRAVLITGCDTGFGKETAKKLDAMGFTVLATVLDLNSPGALELRDLCSPRLKLLQMDLTKAEDISRVLEITKAHTASTGLWGLVNNAGLNIVVADVELSPVATFRKCMEVNFFGALELTKGLLPLLRHSRGRIVTVGSPAGDMPYPCLAAYGTSKAAIALLMDTFGCELLPWGIKVSIIKPGCFKTDAVTNVNLWEKRKQLLLANIPRELLQAYGEDYIEHVHGQFLNSLRMALPDLSPVVDAIIDALLAAQPRSRYYPGRGLGLMYFIHHYLPEGLRRCFLQNFFINHLLPRALRPGQHGPAPA
Protein: Gastrin-releasing peptide receptor (GRP-R) (GRP-preferring bombesin receptor) (P30550)
Organism: Homo sapiens (Human)
Function: Receptor for gastrin-releasing peptide (GRP). Signals via association with G proteins that activate a phosphatidylinositol-calcium second messenger system, resulting in Akt phosphorylation. Contributes to the regulation of food intake. Contributes to the perception of prurient stimuli and transmission of itch signals in the spinal cord that promote scratching behavior, but does not play a role in the perception of pain. Contributes primarily to nonhistaminergic itch sensation. In one study, shown to act in the amygdala as part of an inhibitory network which inhibits memory specifically related to learned fear (By similarity). In another study, shown to contribute to disinhibition of glutamatergic cells in the auditory cortex via signaling on vasoactive intestinal peptide-expressing cells which leads to enhanced auditory fear memories (By similarity). Contributes to the induction of sighing through signaling in the pre-Botzinger complex, a cluster of several thousand neurons in the ventrolateral medulla responsible for inspiration during respiratory activity (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:1655761}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Gastrin-releasing peptide
- Neuromedin-B
- Bombesin receptor subtype-3
- Neuromedin-B receptor
- Guanine nucleotide-binding protein G
- Glutamate carboxypeptidase 2
- Guanine nucleotide-binding protein subunit alpha-11
- Neurotensin/neuromedin N
- Kininogen-1
- Somatostatin
Sequence:
MALNDCFLLNLEVDHFMHCNISSHSADLPVNDDWSHPGILYVIPAVYGVIILIGLIGNITLIKIFCTVKSMRNVPNLFISSLALGDLLLLITCAPVDASRYLADRWLFGRIGCKLIPFIQLTSVGVSVFTLTALSADRYKAIVRPMDIQASHALMKICLKAAFIWIISMLLAIPEAVFSDLHPFHEESTNQTFISCAPYPHSNELHPKIHSMASFLVFYVIPLSIISVYYYFIAKNLIQSAYNLPVEGNIHVKKQIESRKRLAKTVLVFVGLFAFCWLPNHVIYLYRSYHYSEVDTSMLHFVTSICARLLAFTNSCVNPFALYLLSKSFRKQFNTQLLCCQPGLIIRSHSTGRSTTCMTSLKSTNPSVATFSLINGNICHERYV
Protein: Probable inositol 1-monophosphatase ImpA (I-1-Pase) (IMPase) (Inositol-1-phosphatase) (EC 3.1.3.25) (O53907)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the dephosphorylation of inositol 1-phosphate (I-1-P) to yield free myo-inositol, a key metabolite in mycobacteria.
Interaction partners:
- Imidazole glycerol phosphate synthase subunit HisF
- Phosphoribosyl isomerase A
- Inositol-3-phosphate synthase
- Phosphoribosyl-AMP cyclohydrolase
- Imidazole glycerol phosphate synthase subunit HisH
- Imidazoleglycerol-phosphate dehydratase
- Inositol-1-monophosphatase SuhB
- Histidinol dehydrogenase
- Histidinol-phosphate aminotransferase
- Phospholipase C C
Sequence:
MHLDSLVAPLVEQASAILDAATALFLVGHRADSAVRKKGNDFATEVDLAIERQVVAALVAATGIEVHGEEFGGPAVDSRWVWVLDPIDGTINYAAGSPLAAILLGLLHDGVPVAGLTWMPFTDPRYTAVAGGPLIKNGVPQPPLADAELANVLVGVGTFSADSRGQFPGRYRLAVLEKLSRVSSRLRMHGSTGIDLVFVADGILGGAISFGGHVWDHAAGVALVRAAGGVVTDLAGQPWTPASRSALAGPPRVHAQILEILGSIGEPEDY
Protein: Histone H1.2 (CTL-1) (P02253)
Organism: Bos taurus (Bovine)
Function: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).
Subcellular location: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. {ECO:0000250}.
Interaction partners:
- Histone H2A
Sequence:
MSETAPAAPAAAPPAEKTPVKKKAAKKPAGARRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAATGEAKPKAKKAGAAKPKKAAGAAKKTKKATGAATPKKTAKKTPKKAKKPAAAAVTKKVAKSPKKAKAAKPKKAAKSAAKAVKPKAAKPKVAKPKKAAPKKK
Protein: Lysine--tRNA ligase (EC 6.1.1.6) (Lysyl-tRNA synthetase) (LysRS) (O51603)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Subcellular location: Cytoplasm.
Interaction partners:
Sequence:
MKTAHWADFYAEKIKKEKGPKNLYTVASGITPSGTVHIGNFREVISVDLVARALRDSGSKVRFIYSWDNYDVFRKVPKNMPEQELLTTYLRQAITRVPDTRSHKTSYARANEIEFEKYLPVVGINPEFIDQSKQYTSNAYASQIKFALDHKKELSEALNEYRTSKLEENWYPISVFCTKCNRDTTTVNNYDNHYSVEYSCECGNQESLDIRTTWAIKLPWRIDWPMRWKYEKVDFEPAGKDHHSSGGSFDTSKNIVKIFQGSPPVTFQYDFISIKGRGGKISSSSGDVISLKDVLEVYTPEVTRFLFAATKPNTEFSISFDLDVIKIYEDYDKFERIYYGVEDVKEEKKRAFKRIYELSQPYMPSKRIPYQVGFRHLSVISQIFENNINKILNYLKNVQEDQKDKLINKINCAINWIRDFAPEDFKFSLRSKFDNMEILEENSKKAINELLDFLKKNFEVATEQDIQNEIYKISRENNIEPALFFKQIYKILIDKEKGPKLAGFIKIIGIDRFEKITSKYV
Protein: FI16532p1 (Vacuolar H[+] ATPase 36kD subunit 2) (A1Z8V7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- V-type proton ATPase subunit B
- V-type proton ATPase subunit E
- V-type proton ATPase subunit d 1
- Probable V-type proton ATPase subunit d 2
- H
- V-type proton ATPase subunit G
- V-type proton ATPase catalytic subunit A isoform 1
- V-type proton ATPase catalytic subunit A isoform 2
- V-type proton ATPase subunit H
- V-type proton ATPase 16 kDa proteolipid subunit c
Sequence:
MAKRDILPIFPSRANSVIMKQRVLAARRGVGLLKRKRDAIDMKLRELRRIRFDQDMHGDEAMRNAIFSMAKANLLGADFKPQMVSRSHVATVSLRRTEIKIVGVKLNTLELETKGVGAFPLAGLSCGGMQVSRIRDSYTKALKALVEFASLEYQVRMLEAASLQTNMRVNALEHVVIPILQNTYNYICGELEEFEREDFYRLKRSQAKQLEAKMAFTELIKTKNMTDEELETYIKRNINQTRPPAADTPFDQEQFEEREVKRRMREARLSLKQRREQERKEAIKRGEPPPPTSFITTHGASLSFAGRQRDPRASSGDLYSTKRMLLSSGPERKSASNVTERKSDTPPRNSQETQRRSSQMSKDVVNEDPPEES
Protein: Alkylglycerone-phosphate synthase (Alkyl-DHAP synthase) (EC 2.5.1.26) (A0A2R8YEL0)
Organism: Homo sapiens (Human)
Subcellular location: Peroxisome {ECO:0000256|RuleBase:RU363113}.
Interaction partners:
Sequence:
MAEAAAAAGGTGLGAGASYGSAADRDRDPDPDRAGRRLRVLSGHLLGRPREALSTNECKARRAASAATAAPTATPAAQESGTIPKKRQEVMKWNGWGYNDSKFIFNKKGQIELTGKRYPLSGMGLPTFKEWIQNTLGVNVEHKTTSKASLNPSDTPPSVVNEDFLHDLKETNISYSQEADDRVFRAHGHCLHEIFLLREGMFERIPDIVLWPTCHDDVVKIVNLACKYNLCIIPIGGGTSVSYGLMCPADETRTIISLDTSQMNRILWVDENNLTAHVEAGITGQELERQLKESGYCTGHEPDSLEFSTVGGWVSTRASGMKKNIYGNIEDLVVHIKMVTPRGIIEKSCQGPRMSTGPDIHHFIMGSEGTLGVITEATIKIRPVPEYQKYGSVAFPNFEQGVACLREIAKQRCAPASIRLMDNKQFQFGHALKPQVSSIFTSFLDGLKKFYITKFKGFDPNQLSVATLLFEGDREKVLQHEKQVYDIAAKFGGLAAGEDNGQRGYLLTYVIAYIRDLALEYYVLGESFETSAPWDRVVDLCRNVKERITRECKEKGVQFAPFSTCRVTQTYDAGACIYFYFAFNYRGISDPLTVFEQTEAAAREEILANGGSLSHHHGEHEPHSTSTHHGRYRIPQICGRSFPPLDNFQDSSRFLPEPSTQECISPWFHHIHSLPF
Protein: Syntaxin-1B (P35B) (Syntaxin-1B2) (P61265)
Organism: Rattus norvegicus (Rat)
Function: Potentially involved in docking of synaptic vesicles at presynaptic active zones. May mediate Ca(2+)-regulation of exocytosis acrosomal reaction in sperm (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type IV membrane protein {ECO:0000305}.
Interaction partners:
- Syntaxin-binding protein 1
- Vesicle-associated membrane protein 2
- Vesicle-associated membrane protein 3
- Vesicle-associated membrane protein 1
- Multifunctional fusion protein
- Vesicle-associated membrane protein 4
- Synaptosomal-associated protein 23
- Alpha-soluble NSF attachment protein
- Beta-soluble NSF attachment protein
- Synaptotagmin-1
Sequence:
MKDRTQELRSAKDSDDEEEVVHVDRDHFMDEFFEQVEEIRGCIEKLSEDVEQVKKQHSAILAAPNPDEKTKQELEDLTADIKKTANKVRSKLKAIEQSIEQEEGLNRSSADLRIRKTQHSTLSRKFVEVMTEYNATQSKYRDRCKDRIQRQLEITGRTTTNEELEDMLESGKLAIFTDDIKMDSQMTKQALNEIETRHNEIIKLETSIRELHDMFVDMAMLVESQGEMIDRIEYNVEHSVDYVERAVSDTKKAVKYQSKARRKKIMIIICCVVLGVVLASSIGGTLGL
Protein: Heat shock protein beta-1 (HspB1) (Growth-related 25 kDa protein) (Heat shock 25 kDa protein) (HSP 25) (Heat shock 27 kDa protein) (HSP 27) (p25) (P14602)
Organism: Mus musculus (Mouse)
Function: Small heat shock protein which functions as a molecular chaperone probably maintaining denatured proteins in a folding-competent state. Plays a role in stress resistance and actin organization. Through its molecular chaperone activity may regulate numerous biological processes including the phosphorylation and the axonal transport of neurofilament proteins (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P04792}. Nucleus {ECO:0000250|UniProtKB:P04792}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04792}. Note=Cytoplasmic in interphase cells. Colocalizes with mitotic spindles in mitotic cells. Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing speckles. {ECO:0000250|UniProtKB:P04792}.
Interaction partners:
- MAP kinase-activated protein kinase 2
- Heat shock 70 kDa protein 1B
- Cytochrome c, testis-specific
- Cytochrome c, somatic
- MAP kinase-activated protein kinase 5
- Heat shock cognate 71 kDa protein
- MAP kinase-activated protein kinase 3
- RAC-alpha serine/threonine-protein kinase
- Plectin
- Heat shock protein HSP 90-alpha
Sequence:
MTERRVPFSLLRSPSWEPFRDWYPAHSRLFDQAFGVPRLPDEWSQWFSAAGWPGYVRPLPAATAEGPAAVTLAAPAFSRALNRQLSSGVSEIRQTADRWRVSLDVNHFAPEELTVKTKEGVVEITGKHEERQDEHGYISRCFTRKYTLPPGVDPTLVSSSLSPEGTLTVEAPLPKAVTQSAEITIPVTFEARAQIGGPEAGKSEQSGAK
Protein: Olfactory receptor 6P1 (Olfactory receptor OR1-12) (Q8NGX9)
Organism: Homo sapiens (Human)
Function: Odorant receptor.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MRNLSGGHVEEFVLVGFPTTPPLQLLLFVLFFAIYLLTLLENALIVFTIWLAPSLHRPMYFFLGHLSFLELWYINVTIPRLLAAFLTQDGRVSYVGCMTQLYFFIALACTECVLLAVMAYDRYLAICGPLLYPSLMPSSLATRLAAASWGSGFFSSMMKLLFISQLSYCGPNIINHFFCDISPLLNLTCSDKEQAELVDFLLALVMILLPLLAVVSSYTAIIAAILRIPTSRGRHKAFSTCAAHLAVVVIYYSSTLFTYARPRAMYTFNHNKIISVLYTIIVPFFNPAIYCLRNKEVKEAFRKTVMGRCHYPRDVQD
Protein: DNA polymerase III subunit tau (EC 2.7.7.7) (DNA polymerase III subunit gamma) (P06710)
Organism: Escherichia coli (strain K12)
Function: Part of the beta sliding clamp loading complex, which hydrolyzes ATP to load the beta clamp onto primed DNA to form the DNA replication pre-initiation complex. DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3'-5' exonuclease activity. The gamma complex (gamma(3),delta,delta') is thought to load beta dimers onto DNA by binding ATP which alters the complex's conformation so it can bind beta sliding clamp dimers and open them at one interface. Primed DNA is recognized, ATP is hydrolyzed releasing the gamma complex and closing the beta sliding clamp ring around the primed DNA.
Interaction partners:
- DNA polymerase III subunit delta
- DNA polymerase III subunit chi
- Beta sliding clamp
- DNA polymerase III subunit delta'
- DNA polymerase III subunit psi
- DNA polymerase III subunit epsilon
- Single-stranded DNA-binding protein
- DNA polymerase III subunit alpha
- Replicative DNA helicase DnaB
- DNA primase
Sequence:
MSYQVLARKWRPQTFADVVGQEHVLTALANGLSLGRIHHAYLFSGTRGVGKTSIARLLAKGLNCETGITATPCGVCDNCREIEQGRFVDLIEIDAASRTKVEDTRDLLDNVQYAPARGRFKVYLIDEVHMLSRHSFNALLKTLEEPPEHVKFLLATTDPQKLPVTILSRCLQFHLKALDVEQIRHQLEHILNEEHIAHEPRALQLLARAAEGSLRDALSLTDQAIASGDGQVSTQAVSAMLGTLDDDQALSLVEAMVEANGERVMALINEAAARGIEWEALLVEMLGLLHRIAMVQLSPAALGNDMAAIELRMRELARTIPPTDIQLYYQTLLIGRKELPYAPDRRMGVEMTLLRALAFHPRMPLPEPEVPRQSFAPVAPTAVMTPTQVPPQPQSAPQQAPTVPLPETTSQVLAARQQLQRVQGATKAKKSEPAAATRARPVNNAALERLASVTDRVQARPVPSALEKAPAKKEAYRWKATTPVMQQKEVVATPKALKKALEHEKTPELAAKLAAEAIERDPWAAQVSQLSLPKLVEQVALNAWKEESDNAVCLHLRSSQRHLNNRGAQQKLAEALSMLKGSTVELTIVEDDNPAVRTPLEWRQAIYEEKLAQARESIIADNNIQTLRRFFDAELDEESIRPI
Protein: Xaa-Pro dipeptidase (X-Pro dipeptidase) (EC 3.4.13.9) (Imidodipeptidase) (Peptidase D) (Proline dipeptidase) (Prolidase) (P12955)
Organism: Homo sapiens (Human)
Function: Splits dipeptides with a prolyl or hydroxyprolyl residue in the C-terminal position. Plays an important role in collagen metabolism because the high level of iminoacids in collagen.
Interaction partners:
- Apolipoprotein C-II
- Apolipoprotein C-I
- Cytosolic non-specific dipeptidase
Sequence:
MAAATGPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGGEETQRYCTDTGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLPASHATWMGKIHSKEHFKEKYAVDDVQYVDEIASVLTSQKPSVLLTLRGVNTDSGSVCREASFDGISKFEVNNTILHPEIVECRVFKTDMELEVLRYTNKISSEAHREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSSYTCICGSGENSAVLHYGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTADQKAVYEAVLRSSRAVMGAMKPGVWWPDMHRLADRIHLEELAHMGILSGSVDAMVQAHLGAVFMPHGLGHFLGIDVHDVGGYPEGVERIDEPGLRSLRTARHLQPGMVLTVEPGIYFIDHLLDEALADPARASFLNREVLQRFRGFGGVRIEEDVVVTDSGIELLTCVPRTVEEIEACMAGCDKAFTPFSGPK
Protein: Estrogen receptor (ER) (ER-alpha) (Estradiol receptor) (Nuclear receptor subfamily 3 group A member 1) (P16058)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues.
Subcellular location: Nucleus.
Interaction partners:
Sequence:
MLVRQSHTQISKPLGAPLRSRTTLESHVISPPKLSPQQPTTPNSNMYPEETRGGGGAAAFNYLDGGYDYTAPAQGPAPLYYSTTPQDAHGPPSDGSMQSLGSSPTGPLVFVSSSPQLSPQLSPFLHPPSHHGLPSQSYYLETSSTPLYRSSVVTNQLSASEEKLCIASDRQQSYSAAGSGVRVFEMANETRYCAVCSDFASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTMDRNRRKSCQACRLRKCYEVGMVKGGLRKDRGGRVLRKDKRYCGPAGDREKPYGDLEHRTAPPQDGGRNSSSSLNGGGGWRGPRITMPPEQVLFLLQGAEPPALCSRQKVARPYTEVTMMTLLTSMADKELVHMIAWAKKVPGFQELSLHDQVQLLESSWLEVLMIGLIWRSIHCPGKLIFAQDLILDRSEGDCVEGMAEIFDMLLATVSRFRMLKLKPEEFVCLKAIILLNSGAFSFCSNSVESLHNSSAVESMLDNITDALIHHISHSGASVQQQPRRQAQLLLLLSHIRHMSNKGMEHLYSIKCKNKVPLYDLLLEMLDGHRLQSPGKVAQAGEQTEGPSTTTTTSTGSSIGPMRGSQDTHIRSPGSGVLQYGSPSSDQMPIP
Protein: Phosphatidylinositol 4-kinase beta (PI4K-beta) (PI4Kbeta) (PtdIns 4-kinase beta) (EC 2.7.1.67) (Q49GP3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Phosphorylates phosphatidylinositol (PI) in the first committed step in the production of the second messenger inositol-1,4,5,-trisphosphate (PIP).
Subcellular location: Endomembrane system {ECO:0000250}. Mitochondrion outer membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Rough endoplasmic reticulum membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Phosphatidylinositol 4-kinase type 2-alpha
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase.
- ADP-ribosylation factor
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 4-kinase, catalytic, alpha a
- Inositol polyphosphate-5-phosphatase B.
- Phosphatidylinositol 4-kinase type 2-beta
- Inositol polyphosphate 5-phosphatase OCRL
- Neuronal calcium sensor 1
- Synaptojanin-1
Sequence:
MGDTELELSPTHLEELQKSPSTSTTSSLSLPSSPSSGPHPLTSSSPSTSEGLPTSSPPLDVISEGLGELSLVIDTEVAKKACQEVLQKVKFLKGDGEVSSASSEPILANGTAHPEANDGGQPPKISEEEVEPIKSVRRRQKNNSSKQSWLLRLFESKLFDISMAISYLYNSKEPGVQAYIGNRLFSFRNEDVDFYLPQLLNMYIHMDEDVGDAIKPYVVYRCRQSINFSLQCAWLLGAYSSDMHISTQRHSRGTKLRKLILSDELKPSSQRIRREVPQPPPPYPPPLHHGPGMSEHSLSPSKRTHQRSKSDATVSISLSSNLKRTASNPKVETSQDEPVRLTPQREFIKSLMGIGKRLATLPTKEQKTQRLISELSLLNHKLPARVWLPTAAFDHHVVRVPHTQAVVLNSKDKAPYLIYVEVLECENFETSSVPVRIPETQIRSTRSVENLPDCGITPDQRASSFSTVPNYDNDDEAWSVDDIGELQVELPEIHTNSCDNISQFSVDSITSQESKEPIFIAAGDIRRRLSEQLAHTPTTFRKDPEDPSAVALKEPWQEKVRRIREGSPYGHLPNWRLLSVIVKCGDDLRQELLAYQVLKQLQIIWEQERVPLWIKPYKILVISSDSGMIEPVVNAVSIHQVKKQSQLLLLDYFRQEHGNFNTEEFLTAQRNFVQSCAGYCLICYLLQVKDRHNGNILLDSEGHIIHIDFGFILSSSPRNLGFETSAFKLTSEFVDVMGGLDGDMFNYYKMLMLQGLIAARKHMEKVIQIVEIMQQGSQLPCFHGSSTIRNLKERFHMNLTEEQLQVLVEQMVDGSMRSITTKLYDGFQYLTNGIM
Protein: Phosphodiesterase (EC 3.1.4.-) (Q8VBU5)
Organism: Mus musculus (Mouse)
Interaction partners:
- Disrupted in schizophrenia 1 homolog
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Adenosine kinase
- Adenine phosphoribosyltransferase
- GTP:AMP phosphotransferase AK3, mitochondrial
- Deoxycytidine kinase
- Adenylosuccinate lyase
Sequence:
MTAKNSPKEFTASESEVCIKTFKEQMRLELELPKLPGNRPTSPKISPRSSPRNSPCFFRKLLVNKSIRQRRRFTVAHTCFDVENGPSPGRSPLDPQAGSSSGLVLHAAFPGHSQRRESFLYRSDSDYDLSPKAMSRNSSLPSEQHGDDLIVTPFAQVLASLRSVRNNFTLLTNLHGAPNKRSPAASQAPVSRVSLQEESYQKLAMETLEELDWCLDQLETIQTYRSVSEMASNKFKRMLNRELTHLSEMSRSGNQVSEYISNTFLDKQNDVEIPSPTQKDREKKKKQQLMTQISGVKKLMHSSSLNNTSISRFGVNTENEDHLAKELEDLNKWGLNIFNVAGYSHNRPLTCIMYAIFQERDLLKTFKISSDTFVTYMMTLEDHYHSDVAYHNSLHAADVAQSTHVLLSTPALDAVFTDLEILAAIFAAAIHDVDHPGVSNQFLINTNSELALMYNDESVLENHHLAVGFKLLQEEHCDIFQNLTKKQRQTLRKMVIDMVLATDMSKHMSLLADLKTMVETKKVTSSGVLLLDNYTDRIQVLRNMVHCADLSNPTKSLELYRQWTDRIMEEFFQQGDKERERGMEISPMCDKHTASVEKSQVGFIDYIVHPLWETWADLVQPDAQDILDTLEDNRNWYQSMIPQSPSPPLDERSRDCQGLMEKFQFELTLEEEDSEGPEKEGEGHSYFSSTKTLCVIDPENRDSLEETDIDIATEDKSPIDT
Protein: ATP-dependent permease PDR12 (Q02785)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plasma membrane transporter which mediates resistance to water-soluble, monocarboxylic acids with chain lengths of from C1 to C7 by active extrusion of the preservative anions from the cytosol. Also involved in the export of aromatic and branched-chain organic acids produced in amino acid catabolism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9687494}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:9687494}.
Interaction partners:
- Weak acid resistance protein 1
- Oligomycin resistance ATP-dependent permease YOR1
- Polyamine transporter 1
- Polyamine transporter 2
- Transcriptional activator HAA1
- Polyamine transporter 3
- Probable transporter AQR1
- Transcription factor PDR1
Sequence:
MSSTDEHIEKDISSRSNHDDDYANSVQSYAASEGQVDNEDLAATSQLSRHLSNILSNEEGIERLESMARVISHKTKKEMDSFEINDLDFDLRSLLHYLRSRQLEQGIEPGDSGIAFKNLTAVGVDASAAYGPSVEEMFRNIASIPAHLISKFTKKSDVPLRNIIQNCTGVVESGEMLFVVGRPGAGCSTFLKCLSGETSELVDVQGEFSYDGLDQSEMMSKYKGYVIYCPELDFHFPKITVKETIDFALKCKTPRVRIDKMTRKQYVDNIRDMWCTVFGLRHTYATKVGNDFVRGVSGGERKRVSLVEAQAMNASIYSWDNATRGLDASTALEFAQAIRTATNMVNNSAIVAIYQAGENIYELFDKTTVLYNGRQIYFGPADKAVGYFQRMGWVKPNRMTSAEFLTSVTVDFENRTLDIKPGYEDKVPKSSSEFEEYWLNSEDYQELLRTYDDYQSRHPVNETRDRLDVAKKQRLQQGQRENSQYVVNYWTQVYYCMIRGFQRVKGDSTYTKVYLSSFLIKALIIGSMFHKIDDKSQSTTAGAYSRGGMLFYVLLFASVTSLAEIGNSFSSRPVIVKHKSYSMYHLSAESLQEIITEFPTKFVAIVILCLITYWIPFMKYEAGAFFQYILYLLTVQQCTSFIFKFVATMSKSGVDAHAVGGLWVLMLCVYAGFVLPIGEMHHWIRWLHFINPLTYAFESLVSTEFHHREMLCSALVPSGPGYEGISIANQVCDAAGAVKGNLYVSGDSYILHQYHFAYKHAWRNWGVNIVWTFGYIVFNVILSEYLKPVEGGGDLLLYKRGHMPELGTENADARTASREEMMEALNGPNVDLEKVIAEKDVFTWNHLDYTIPYDGATRKLLSDVFGYVKPGKMTALMGESGAGKTTLLNVLAQRINMGVITGDMLVNAKPLPASFNRSCGYVAQADNHMAELSVRESLRFAAELRQQSSVPLEEKYEYVEKIITLLGMQNYAEALVGKTGRGLNVEQRKKLSIGVELVAKPSLLLFLDEPTSGLDSQSAWSIVQFMRALADSGQSILCTIHQPSATLFEQFDRLLLLKKGGKMVYFGDIGPNSETLLKYFERQSGMKCGVSENPAEYILNCIGAGATASVNSDWHDLWLASPECAAARAEVEELHRTLPGRAVNDDPELATRFAASYMTQIKCVLRRTALQFWRSPVYIRAKFFECVACALFVGLSYVGVNHSVGGAIEAFSSIFMLLLIALAMINQLHVFAYDSRELYEVREAASNTFHWSVLLLCHAAVENFWSTLCQFMCFICYYWPAQFSGRASHAGFFFFFYVLIFPLYFVTYGLWILYMSPDVPSASMINSNLFAAMLLFCGILQPREKMPAFWRRLMYNVSPFTYVVQALVTPLVHNKKVVCNPHEYNIMDPPSGKTCGEFLSTYMDNNTGYLVNPTATENCQYCPYTVQDQVVAKYNVKWDHRWRNFGFMWAYICFNIAAMLICYYVVRVKVWSLKSVLNFKKWFNGPRKERHEKDTNIFQTVPGDENKITKK
Protein: Ribonuclease pancreatic (EC 4.6.1.18) (RNase 1) (RNase A) (P61823)
Organism: Bos taurus (Bovine)
Function: Endonuclease that catalyzes the cleavage of RNA on the 3' side of pyrimidine nucleotides. Acts on single-stranded and double-stranded RNA.
Subcellular location: Secreted.
Interaction partners:
- Ribonuclease inhibitor
- Glucagon like peptide 1 receptor
Sequence:
MALKSLVLLSLLVLVLLLVRVQPSLGKETAAAKFERQHMDSSTSAASSSNYCNQMMKSRNLTKDRCKPVNTFVHESLADVQAVCSQKNVACKNGQTNCYQSYSTMSITDCRETGSSKYPNCAYKTTQANKHIIVACEGNPYVPVHFDASV
Protein: SD13983p (Q8IGA1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSFVLQLATRTVQSTIAQVRGVATTMPRQIKEIHEKQENSVKIFEGVNVESPRAHLMLKSACQTKFCPECTLGLDIKHTDVLILSQYVRSDGCMLPRRITGLCHRQQKKMGTLVTMAQKAGLMPNLAPEWSKRDPKKRFGWRKFNKYFLESTIKY
Protein: Uncharacterized protein, isoform A (Uncharacterized protein, isoform B (EC 3.4.21.-)) (Q9VEM8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Trypsin zeta
- Peptidase S1 domain-containing protein
- Peptidase M14 domain-containing protein
- Trypsin theta
- Peptidase S1 domain-containing protein
- Aminopeptidase
- Uncharacterized protein, isoform A
- trypsin
- FI02848p
- Trypsin iota
Sequence:
MVRLGVVQILVILLACTCYKPISAVRLAQLSEDQLEWISKAEGVNFQNRVINGEDVQLGEAKYQISLQGMYGGHICGGCIIDERHVLTAAHCVYGYNPTYLRVITGTVEYEKPDAVYFVEEHWIHCNYNSPDYHNDIALIRLNDTIKFNEYTQPAELPTAPVANGTQLLLTGWGSTELWGDTPDILQKAYLTHVVYSTCQEIMNNDPSNGPCHICTLTTGGQGACHGDSGGPLTHNGVLYGLVNWGYPCALGVPDSHANVYYYLEWIRSMISGPCSNCHCYASNYPSL