wanglab/gogpt-training-data huggingface dataset:
Protein: Lysosomal enzyme receptor protein, isoform D (B7Z0Q8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}.
Interaction partners:
Sequence:
MRCSLQKDCAAPTQENFRQMRFPIVISLLLLLFCSGESVAADAANQLKFSTTECKLKEPIYGSTFDFSGLHSDLAHVVKSMNIGGDQFEFNICGNLSRTCNGESNVAACLKRQGKEYILGRQHELFYNNGNMFLKYKSGAKCDNGTADKPNYQLHVMFSCDYTLDAQPMHVTPYANEVCSFYISYRTPLACLSIPEGLQSNSCRVGDTKSNGTFDLMPLSDSNYHTSNRQGAFFVINVCKPVLYGENSMCPAGSSVCLFDSKATNPKERFINFGNVQTHPVVEKGQLLLRHESPTPCAKNSSANYTSVIYFSCDKFIRNAHPEFAGLGADSCTYQFNFATPLACNDLKPCTAFTSTNELLDLSSLSSKPARTLLKDGKNYTIAVCAHAGAPCQENGGACYEQNSTTISLGNSNSQLRFNQTGSLYLLYEDGAECSTATGMRRWSTKIEFVCANNATKDNGASTAGGSDSLKIIEDSNCQLLIQYQTPLACREPIRCKATTYVDHTNDGLGSSGDELIDLTPLISATDNYEARVELPASMEHLVPKTTKFFLNVCRPLVPKYQLGCAGGSAACMAKVTAAGAPEEERSMGFPLVSLTQRNRTFAELAYLKGDPCPTDNTSELSTHILFNCNMRAGRGQPVLRSVEDCAYRFEWETNVFCPPHECTFSADTCDLVHDELGRRFNFKSAPFTKDGKIEIDYNATKMSVNICGAHRKAMTDYSQALVNIFFTHESPNCGREGTMNVQIRLICSDQTESSSTISSDQQCNLLYVQRTPSICEFLSLGATQQNFESNGSTSSSTSSSSTSTTTSTTTQASPAGKPTKAATSTTTTTVGPDPAATPIGPTASVGTILGAILSVTFCVTCLGLLAFSPARRQRIRRLFRRSNSAVRYSRVQSNEEANLLLEPNGEFTESDDDMLL
Protein: Protein phosphatase 1 regulatory inhibitor subunit PPP1R7 homolog (Q84WJ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Inhibitor of protein-phosphatase 1 (PP1). Binds to and inhibits PP1 activity.
Interaction partners:
- Protein phosphatase 1 regulatory subunit INH3
Sequence:
MNSEKEDEPLEEIGDSNNVLDLTSYQLHSLDTVELPPNLIELDLTANRLSGLDSRIAQLSTLKKLSLRQNLIDDSAVEPLSHWDALSDLEELVLRDNKLAKVPDVSIFTKLLVYDISFNEITSLEGISKASSTLKELYVSKNEVNKIMEIEHLHNLQILELGSNRLRVMENLENFTKLEELWLGRNRIKVVNLCGLKCIKKISLQSNRLTSMKGFEECVALEELYLSHNGISKMEGLSALVNLRVLDVSNNKLTSVDDIQNLTKLEDLWLNDNQIESLEAITEAVTGSKEKLTTIYLENNPCAKSSDYVAAVRQIFPNVEQIDSNLFA
Protein: Probable galacturonosyltransferase-like 7 (EC 2.4.1.-) (Q8VYF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in pectin and/or xylans biosynthesis in cell walls.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Hydroxyproline O-galactosyltransferase GALT4
- Non-classical arabinogalactan protein 30
- Arabinogalactan protein 20
Sequence:
MLWIMRFSGLFSAALVIIVLSPSLQSFPPAEAIRSSHLDAYLRFPSSDPPPHRFSFRKAPVFRNAADCAAADIDSGVCNPSLVHVAITLDFEYLRGSIAAVHSILKHSSCPESVFFHFLVSETDLESLIRSTFPELKLKVYYFDPEIVRTLISTSVRQALEQPLNYARNYLADLLEPCVRRVIYLDSDLIVVDDIAKLWMTKLGSKTIGAPEYCHANFTKYFTPAFWSDERFSGAFSGRKPCYFNTGVMVMDLERWRRVGYTEVIEKWMEIQKSDRIYELGSLPPFLLVFAGEVAPIEHRWNQHGLGGDNVRGSCRDLHPGPVSLLHWSGSGKPWFRLDSRRPCPLDTLWAPYDLYGHYSR
Protein: Variant surface glycoprotein (VSG, atypical), putative (Q580N9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MPPKLGLALPLLIASVTSPRPGEATAGNVIKKANWQAICKVTADAGNLAGLALTNIRAPGLQVAADIKALLRTLIYIEGNSTSAATKVQGKAAAFLAGQTAENLEYYSSTSVATDVTTARDAGRLHGATHEFMSVQADGSTSANGCIGDNESGSNALAGFSAVVEANPNCQLSWETVTTYDGTVTAITKTGLGGKFANAIAHNKFTSGDRKCNINSAASGFKLNNDGTSVDTSGNKPKMAAGIISLDAANGIRTIALANVMGDDEHPYLKAAATAAKRSKQTPKAADLTTADTALASTDFKKAARRHILGKKETADDSDTTLAAKVKKAFGSDESINKLISTNVNNMPIAGILTDNTDAKSLGQITDISELVRLYFYYSDLNKQKLADTAKKPREAEAKTATKSAEEKEKECNTKGKDKQDGCEKLKDQGCVFNKDGDRDKKCTLSKEGKKEAVKAAESKETNKDGKTNTTGRNSFVIKDSPLWLAFLLFN
Protein: Ubiquitin-like protease family profile domain-containing protein (Q54IQ9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MARPKSNLTEEEKRARKREIDRASKRRTKYKNDETTQEYRRVNRERWREKQQKEKDQMELEKHNLFENKLNEKQQEIQKEMEKQYDVQKILLIKEYQEKLEKEKKKIVFEHSQNHIKFNGVYCSSFKTSLLSSEPNLNMHFIHNDKDRTIEPISEKFFKNKGGAMFSENDAVWSNFGKHNIISFFVYTNSGDEIVEWHVSLVVIIKIRRSYYCFIYDPAGSEENYFENEEVKELYSWLLKNNIKILFSKDHTKQKTKNSCALYVHSFIKSFISYLKINENIKSSDVLNLMNHVSKKNPIGELDIEYLNTFNDPSIATYNHSEQ
Protein: Conserved oligomeric Golgi complex subunit 4 (COG complex subunit 4) (Component of oligomeric Golgi complex 4) (Q9H9E3)
Organism: Homo sapiens (Human)
Function: Required for normal Golgi function. Plays a role in SNARE-pin assembly and Golgi-to-ER retrograde transport via its interaction with SCFD1.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:30290151}. Golgi apparatus membrane {ECO:0000305|PubMed:11703943}; Peripheral membrane protein {ECO:0000305|PubMed:11703943}; Cytoplasmic side {ECO:0000305|PubMed:11703943}. Note=Mosty cytosolic, with about 5% membrane-bound. {ECO:0000269|PubMed:30290151}.
Interaction partners:
- Conserved oligomeric Golgi complex subunit 3
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 1
- Conserved oligomeric Golgi complex subunit 7
- Conserved oligomeric Golgi complex subunit 2
- Conserved oligomeric Golgi complex subunit 6
- Conserved oligomeric Golgi complex subunit 5
- Syntaxin-5
- Sec1 family domain-containing protein 1
- Vacuolar protein sorting-associated protein 53 homolog
Sequence:
MADLDSPPKLSGVQQPSEGVGGGRCSEISAELIRSLTELQELEAVYERLCGEEKVVERELDALLEQQNTIESKMVTLHRMGPNLQLIEGDAKQLAGMITFTCNLAENVSSKVRQLDLAKNRLYQAIQRADDILDLKFCMDGVQTALRSEDYEQAAAHTHRYLCLDKSVIELSRQGKEGSMIDANLKLLQEAEQRLKAIVAEKFAIATKEGDLPQVERFFKIFPLLGLHEEGLRKFSEYLCKQVASKAEENLLMVLGTDMSDRRAAVIFADTLTLLFEGIARIVETHQPIVETYYGPGRLYTLIKYLQVECDRQVEKVVDKFIKQRDYHQQFRHVQNNLMRNSTTEKIEPRELDPILTEVTLMNARSELYLRFLKKRISSDFEVGDSMASEEVKQEHQKCLDKLLNNCLLSCTMQELIGLYVTMEEYFMRETVNKAVALDTYEKGQLTSSMVDDVFYIVKKCIGRALSSSSIDCLCAMINLATTELESDFRDVLCNKLRMGFPATTFQDIQRGVTSAVNIMHSSLQQGKFDTKGIESTDEAKMSFLVTLNNVEVCSENISTLKKTLESDCTKLFSQGIGGEQAQAKFDSCLSDLAAVSNKFRDLLQEGLTELNSTAIKPQVQPWINSFFSVSHNIEEEEFNDYEANDPWVQQFILNLEQQMAEFKASLSPVIYDSLTGLMTSLVAVELEKVVLKSTFNRLGGLQFDKELRSLIAYLTTVTTWTIRDKFARLSQMATILNLERVTEILDYWGPNSGPLTWRLTPAEVRQVLALRIDFRSEDIKRLRL
Protein: Probable acyl-CoA dehydrogenase YdiO (EC 1.3.-.-) (P0A9U8)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Putative electron transfer flavoprotein subunit YdiR
- Protein FixB
- Fatty acid oxidation complex subunit alpha
- Fatty acid oxidation complex subunit alpha
- Putative electron transfer flavoprotein subunit YgcQ
- NADH-quinone oxidoreductase subunit C/D
- Protein FixA
- Putative electron transfer flavoprotein subunit YdiQ
- 2,3-dehydroadipyl-CoA hydratase
- Putative electron transfer flavoprotein subunit YgcR
Sequence:
MDFSLTEEQELLLASIRELITTNFPEEYFRTCDQNGTYPREFMRALADNGISMLGVPEEFGGIPADYVTQMLALMEVSKCGAPAFLITNGQCIHSMRRFGSAEQLRKTAESTLETGDPAYALALTEPGAGSDNNSATTTYTRKNGKVYINGQKTFITGAKEYPYMLVLARDPQPKDPKKAFTLWWVDSSKPGIKINPLHKIGWHMLSTCEVYLDNVEVEESDMVGEEGMGFLNVMYNFEMERLINAARSTGFAECAFEDAARYANQRIAFGKPIGHNQMIQEKLALMAIKIDNMRNMVLKVAWQADQHQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEIMIYVAGRQILKDYQNK
Protein: Nuclear nucleic acid-binding protein C1D (hC1D) (Q13901)
Organism: Homo sapiens (Human)
Function: Plays a role in the recruitment of the RNA exosome complex to pre-rRNA to mediate the 3'-5' end processing of the 5.8S rRNA; this function may include MPHOSPH6. Can activate PRKDC not only in the presence of linear DNA but also in the presence of supercoiled DNA. Can induce apoptosis in a p53/TP53 dependent manner. May regulate the TRAX/TSN complex formation. Potentiates transcriptional repression by NR1D1 and THRB (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:11801738}. Cytoplasm {ECO:0000269|PubMed:11801738}. Nucleus, nucleolus {ECO:0000269|PubMed:17412707}. Note=EXOSC10 is required for nucleolar localization (PubMed:17412707). Colocalizes with TSNAX in the nucleus (PubMed:11801738). {ECO:0000269|PubMed:11801738, ECO:0000269|PubMed:17412707}.
Interaction partners:
- Exosome complex component 10
- Exosome complex component RRP45
- Exosome complex component CSL4
- Exosome complex component RRP4
- Exosome complex component RRP40
- Exosome RNA helicase MTR4
- Exosome complex component RRP43
- Exosome complex component RRP46
- Exosome complex component RRP42
- Exosome complex exonuclease RRP44
Sequence:
MAGEEINEDYPVEIHEYLSAFENSIGAVDEMLKTMMSVSRNELLQKLDPLEQAKVDLVSAYTLNSMFWVYLATQGVNPKEHPVKQELERIRVYMNRVKEITDKKKAGKLDRGAASRFVKNALWEPKSKNASKVANKGKSKS
Protein: Exosome component 4 (E9PI41)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFVNLGWQGMGQGWTQGSQLKGARGRHMQDRERKTGGFVLEVTQLPLAEALKVEGEADPQRTVECELEGVGLAHVSVLFQIRGSRARALPDRALVNCQYSSATFSTGERKRRPHGDRKSCEMGLQLRQTFEAAILTQLHPRSQIDIYVQVLQADGGTYAACVNAATLAVLDAGIPMRDFVCACSAGFVDGTALADLSHVEEAAGGPQLALALLPASGQIALLEMDARLHEDHLERVLEAAAQAARDVHTLLDRVVRQHVRE
Protein: Vesicle transport protein USE1 (USE1-like protein) (B0BNG6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004163}.
Interaction partners:
Sequence:
ACHRPLATSRLELNLVRLLCRCESMAAEKREPDEWRLEKYVGALEDMLQALKVQASKPASEVISEYSRKVDFLKGMLQAEKLTSSSEKALANQFLAPGRVPTTAKERVPATKTVHLQSRARYTSEMRSELLGTESSGELEADMRKRVVKGPRPADEKQSASELDLVLQRHQGLQEKLAEEMLGLARSLKTNTLAAQSVIKKDNQTLSHSLKMADQNLEKLKLESERLEQHAQKSVNWLLWAMLIVVCFVFISMILFIRIMPRLK
Protein: Alpha-aminoadipic semialdehyde synthase, mitochondrial (LKR/SDH) [Includes: Lysine ketoglutarate reductase (LKR) (LOR) (EC 1.5.1.8); Saccharopine dehydrogenase (SDH) (EC 1.5.1.9)] (Q99K67)
Organism: Mus musculus (Mouse)
Function: Bifunctional enzyme that catalyzes the first two steps in lysine degradation.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9UDR5}.
Interaction partners:
- Alpha-aminoadipic semialdehyde dehydrogenase
- Spermidine synthase
- 5-phosphohydroxy-L-lysine phospho-lyase
- Biotinidase
- Homogentisate 1,2-dioxygenase
- General transcription factor IIF subunit 1
- Beta-alanine-activating enzyme
Sequence:
MLRAQRPRLARLRACLSRGLHHKPVMALRREDVNAWERRAPLAPKHIKGITKLGYKVLIQPSNRRAIHDKEYVRAGGILQEDITEACLILGVKRPPEEKLMSKKTYAFFSHTIKAQEANMNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHLGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEVFNELPCEYVEPHELREVSKTGDLRKVYGTVLSRHHHLVRKTDGVYDPVEYEKYPERYTSRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLVPVKSSVVPVEGCPELPHKLVAICDISADTGGSIDFMTECTTIERPFCMYDADQQIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGDMLYPYVEEMLLSDASQPLESQNFSPVVRDAVITSNGLLTDKYKYIQKLRESRERIQFLSMSTKKKVLVLGSGYVSGPVLEYLSRDNNIEITLGSDMTNQMQQLSKKYNINPVSLTVGKQEAKLQSLVESQDLVISLLPYVLHPVVAKACIESRVNMVTASYITPAMKELEKSVDDAGITVIGELGLDPGLDHMLAMETIDTAKELGATVESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPASYLLNGKVVNVTGGVSFLNSVTPMDYFPGLNLEGYPNRDSIKYAEIYGISSAHTLLRGTLRYKGYSKALNGFVKLGLINREAYPALRPEANPLTWKQLLCDLVGISRSSPCEKLKEVVFTKLGGDNTQLEAAEWLGLLGDEQVPQAESIVDAFSKHLVSKLSYGPEEKDMIVMRDSFGIRHPSGHLENKTIDLVVYGDFNGFSAMAKTVGLPTAMAAKMLLDGEIEAKGLMGPFTKEIYGPILERIKAEGIVFNTQSTIKL
Protein: 4-hydroxytryptamine kinase (EC 2.7.1.-) (EC 2.7.1.222) (Psilocybin biosynthesis kinase) (P0DPA8)
Organism: Psilocybe cubensis (Psychedelic mushroom) (Stropharia cubensis)
Function: 4-hydroxytryptamine kinase; part of the gene cluster that mediates the biosynthesis of psilocybin, a psychotropic tryptamine-derived natural product. The first step in the pathway is the decarboxylation of L-tryptophan to tryptamine by the decarboxylase psiD. 4-hydroxy-L-tryptophan is accepted as substrate by psiD as well. The cytochrome P450 monooxygenase psiH then converts tryptamine to 4-hydroxytryptamine. The kinase psiK catalyzes the 4-O-phosphorylation step by converting 4-hydroxytryptamine into norbaeocystin. The methyltransferase psiM then catalyzes iterative methyl transfer to the amino group of norbaeocystin to yield psilocybin via a monomethylated intermediate, baeocystin. 4-hydroxy-6-methyl-l-tryptophancan also be converted the decarboxylase PsiD, kinase PsiK, and methyltransferase PsiM into respectively 6-methyl-norbaeocystin, 6-methylbaeocystin, and 6-methylpsilocybin. PsiK kinase can also turn psilocin into psilocybin. This activity may represent a protective mechanism to rephosphorylate the unstable psilocin to the stable psilocybin in case of intracellular ester cleavage. Moreover, psiK is able to O-phosphorylate the quaternary amine 4-hydroxy-N,N,N-trimethyltryptamine (4-OH-TMT) to yield aeruginascin, another bioactive compound found in Psilocybe species.
Interaction partners:
Sequence:
MAFDLKTEDGLITYLTKHLSLDVDTSGVKRLSGGFVNVTWRIKLNAPYQGHTSIILKHAQPHMSTDEDFKIGVERSVYEYQAIKLMMANREVLGGVDGIVSVPEGLNYDLENNALIMQDVGKMKTLLDYVTAKPPLATDIARLVGTEIGGFVARLHNIGRERRDDPEFKFFSGNIVGRTTSDQLYQTIIPNAAKYGVDDPLLPTVVKDLVDDVMHSEETLVMADLWSGNILLQLEEGNPSKLQKIYILDWELCKYGPASLDLGYFLGDCYLISRFQDEQVGTTMRQAYLQSYARTSKHSINYAKVTAGIAAHIVMWTDFMQWGSEEERINFVKKGVAAFHDARGNNDNGEITSTLLKESSTA
Protein: Serine/threonine-protein kinase WNK4 (EC 2.7.11.1) (Protein kinase lysine-deficient 4) (Protein kinase with no lysine 4) (Q7TPK6)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine kinase which plays an important role in the regulation of electrolyte homeostasis, cell signaling, survival and proliferation. Acts as an activator and inhibitor of sodium-coupled chloride cotransporters and potassium-coupled chloride cotransporters respectively. Activates SCNN1A, SCNN1B, SCNN1D, SGK1, TRPV5 and TRPV6. Regulates the activity of the thiazide-sensitive Na-Cl cotransporter, SLC12A3, by phosphorylation which appears to prevent membrane trafficking of SLC12A3. Also inhibits the renal K(+) channel, KCNJ1, via a kinase-independent mechanism by which it induces clearance of the protein from the cell surface by clathrin-dependent endocytosis. WNK4 appears to act as a molecular switch that can vary the balance between NaCl reabsorption and K(+) secretion to maintain integrated homeostasis. Acts as a scaffold to inhibit SLC4A4 as well as CFTR activities and surface expression, recruits STK39 which mediates the inhibition. Phosphorylates NEDD4L (By similarity).
Subcellular location: Cell junction, tight junction {ECO:0000250|UniProtKB:Q80UE6}. Note=Present exclusively in intercellular junctions in the distal convoluted tubule and in both the cytoplasm and intercellular junctions in the cortical collecting duct. WNK4 is part of the tight junction complex. {ECO:0000250|UniProtKB:Q80UE6}.
Interaction partners:
- Kelch-like protein 3
- ATP-sensitive inward rectifier potassium channel 1
- Solute carrier family 12 member 3
- Solute carrier family 12 member 1-chloride cotransporter 1)
- Epithelial sodium channel subunit gamma
- Solute carrier family 12 member 2
- Cullin-3
- Kelch-like protein 2
- STE20/SPS1-related proline-alanine-rich protein kinase
- Transient receptor potential cation channel subfamily V member 5
Sequence:
MLAPRNTETGVHMSQTEADLALRPSPSLTSMGPTRLGPPPRRVRRFSGKAEPRPRSSRPSRRSSVDLGLLSSWSQPASLLPEPPDPPDSAGPMRSPPSNSKEHPEGTWTGAAPVKAADSACPELTVSSGGPGSREPPRVPDAAARERRREQEEKEDTETQAVATSPDGRYLKFDIEIGRGSFKTVYRGLDTDTTVEVAWCELQTRKLSRAERQRFSEEVEMLKGLQHPNIVRFYDSWKSVLRGQVCIVLVTELMTSGTLKTYLRRFREMKPRVLQRWSRQILRGLHFLHSRVPPILHRDLKCDNVFITGPSGSVKIGDLGLATLKRASFAKSVIGTPEFMAPEMYEEKYDEAVDVYAFGMCMLEMATSEYPYSECQNAAQIYRKVTSGTKPNSFYKVKMPEVKEIIEGCIRTDKNERFTIQDLLTHAFFREERGVHVELAEEDDGEKPGLKLWLRMEDARRGGRPRDNQAIEFLFQLGRDAAEEVAQEMVALGLVCEADYQPVARAVRERVAAIQRKREKLRKARELEVLPPDSGPPPATVSMTPGPPSAFPPEPEEPEADQHQSFLFRHASYSSTTSDCETDGYLSSSGFLDASDPALQPPGGMPSSPAEPHLCLPSGFALSIPRSGPGSDFSPGDSYASDAASGLSDMGEGGQMRKNPVKTLRRRPRSRLRVTSVSDQSDRVVECQLQTHNSKMVTFRFDLDGDSPEEIAAAMVYNEFILPSERDGFLSRIREIIQRVETLLKRDAGPSEATEDALSPQEEPAAMPALPGPSDAELQRSISPEQRSWAAFSTSPSSPGTPLSPGTPFSPGTPPVFPCPIFPITSPSCHPYPFSQVSSNPCPQAPSSLLPSSSGASQVPFPSPSLPTSSPLPFSPSYPQVPLHPASLPTCPSPPPLPSTTAAPLLSLASAFSLAVMTVAQSLLSPSPGLLSQSPPAPPGPLPSMPLPLASCDQESLSAQTAETENEASRNPAQPLLGDARLAPISEEGKPQLVGRFQVTSSKEPAEPPLQPASPTLSRSLKLPTPQLTSESSDTEDSAAGGPETREALAESDRAAEGLGVAIDEEKDEGKEPQIGGSSPILSQPSPVWMNYSYSSLCLSSEESESSGEDEEFWAELQNLRQKHLSEVEALQTLQKKEIEDLYSRLGKQPPPGIVAPAAMLSCRQRRLSKGSFPTSRRNSLQRSDLPGPGIMRRNSLSGSSTGSQEQRASKGVTFAGDVGRM
Protein: Microcin C7 (MccC7) (Microcin C51) (McC) (MccC51) (Microcin C) (Q47505)
Organism: Escherichia coli
Function: Antibacterial peptide, active against enterobacteria including species of Klebsiella, Salmonella, Shigella, Yersinia and Proteus, and strains of E.coli. Inhibits protein translation by blocking aspartyl-tRNA synthetase function and inhibiting production of aminoacetylated tRNA-Asp.
Interaction partners:
Sequence:
MRTGNAN
Protein: PAX-interacting protein 1 (PAX transactivation activation domain-interacting protein) (A2VEF9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADVSLFFGGLPAILLKADTIYRIGRQKGLEISIADESMELAHATACILRRGVVRLAALVGKIFVNDQEETVVDIGMENAVAGKVKLRFGNVEARLEFGEDHDEVHDSSGFGECLKNGLNNTTLDSMDVPETQPPSANTSVNTTADSLFIPETQAVLCERPSTGQRVSLGDDFMIPETQDMLADLPPEPPVFKPPVIPVVDKPGPTIDSDEESSQGSIIRMCTQDYNEDAIDDFDTSQVLCDVLLPLPPPTAPIEGLENQDTKRDQLDTTDMEMSALNWSASNSKCCALSSTKADDILPRGDACITPDLTAPSVDRNICTPDLFDLIMGGDRRRDGSSSPDPFVRPADNTNTATPQFGGVKQLVVATIETPTATPDTNSQEKNQDMIATQRFPRHKLLESDEEDNGQNNQDFVATQAFNLGRPQAPQENEANQDLIATQAFNLAPPQKVDSPKPSTANDASNQDFIETQAFNLGIPQANMASPENNEISNQDLIATQAFPAKINSSRCQDFVATQPFHVVNQHSVSLQDKENIPLDDSVKVASATCGEIDAVLNEMISGTVATSPVSPNEESIPFFEPCVIKDKNHYQKICQIEGVFSNVSNRSRGRTDGTGFGRLKRVAKSESPPETPIRKDRRRSEGSERPGSNSRERLNNLVDKKSEALNKSVIREHGIDSIPEEITKEDKSDSEEKGDCFNNVVNQWRSRKRRIQSRPGTPGSSSERNEVNADVVDKPNEEPPTKNIRARKAKKAEKADSSKDIPKPTTRTRRQTSDEDVRTPDLGKGRKAKNTASSKADTSKNIAKGSKRVTRQNSADDAELLEEDSSVQTESGKRVKKVKSSKGETSKDIPKAKPRTRRQTADEDAMTPKAEKERQIQGEETKDMSKPAARTRRKASAEETESAAQAVKPKRGGKGKKNETTKAEATVEKPMVRTRRMTIAEDSSTLTEVKTGGALIKRAVVRISRVSIEQLESSTSAGNNARVTGAAQSRSTTPSIEEPSSSSAAAKEPNVSTATTRRRAKRLTSGEEPTSSSDVPTKKPKMSVDEEVLKNRSGATTTRFSQPDADPLRAINLYVRKAKTTTGKIKVAFTMCNRPALETVLKSLKHVVEITEDPLQCDLLVMDKGERTYKFLTVIASNKPVLSTNWLHSVKKTRSIDIKADHLFSDPTFEETYKFKPSSVLEHPRLLYGLHFMLGKDIVPKANEMKVIIHSAGGKVHAQPPSLAISVDLYVVTTSKDTKSKRRLNNYEKVHFIKTEAVMQALVQHNIEMLQEHTLKL
Protein: G protein-activated inward rectifier potassium channel 1 (GIRK-1) (Inward rectifier K(+) channel Kir3.1) (KGA) (KGB1) (Potassium channel, inwardly rectifying subfamily J member 3) (P63251)
Organism: Rattus norvegicus (Rat)
Function: This potassium channel is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. This receptor plays a crucial role in regulating the heartbeat.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- G protein-activated inward rectifier potassium channel 4
- G protein-activated inward rectifier potassium channel 2
- G protein-activated inward rectifier potassium channel 3
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid type B receptor subunit 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Guanine nucleotide-binding protein G
Sequence:
MSALRRKFGDDYQVVTTSSSGSGLQPQGPGQGPQQQLVPKKKRQRFVDKNGRCNVQHGNLGSETSRYLSDLFTTLVDLKWRWNLFIFILTYTVAWLFMASMWWVIAYTRGDLNKAHVGNYTPCVANVYNFPSAFLFFIETEATIGYGYRYITDKCPEGIILFLFQSILGSIVDAFLIGCMFIKMSQPKKRAETLMFSEHAVISMRDGKLTLMFRVGNLRNSHMVSAQIRCKLLKSRQTPEGEFLPLDQLELDVGFSTGADQLFLVSPLTICHVIDAKSPFYDLSQRSMQTEQFEVVVILEGIVETTGMTCQARTSYTEDEVLWGHRFFPVISLEEGFFKVDYSQFHATFEVPTPPYSVKEQEEMLLMSSPLIAPAITNSKERHNSVECLDGLDDISTKLPSKLQKITGREDFPKKLLRMSSTTSEKAYSLGDLPMKLQRISSVPGNSEEKLVSKTTKMLSDPMSQSVADLPPKLQKMAGGPTRMEGNLPAKLRKMNSDRFT
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (E7FH41)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- UBX domain-containing protein 1
- E2 ubiquitin-conjugating enzyme
- PWWP domain-containing 2B
- E2 ubiquitin-conjugating enzyme
Sequence:
MEGQDNADQGSSDQSEIQRRRQLDRLDREEAFYQFVNNLSEEDYRLMRDNNLLGTPGEITADELLNRLRQVKDGPESPSSNITEERREAPGATEVEGTEENPSGETLLDWLNTVRQTGNTTRSGYRGNQSWRAVSQTNPNSGDFRFSLEINVNRNIAEQQTQTERLEGSQERPDGSVSEPESLMETAEVVEEPVVDELAVIVEPELPVPSTLTLNRDDNVPVDAPNPLTSTPPNLPSVEQPRRGQIRARSRSPEQRRTRARTARGRSPINLERLDGLPPTQHGIPTHNPEILPEPQVEGSSRTRQLFLSRQSTVETETHTLGSATDVPEAPQEREATTGEAGASGRRPPTIMLDLQVRRVRPGEYRQRDSIANRTRSRSQTSNNTLLYETERGGFRRTFSRSERAGVRTYVSTIRIPIRRISDAGLGEATSLALQSMIRQIMTGFGELSYFMEAEVPDSNREDNPPADLSDALGNPDASTGTGASEADPYLPGHGGLNQGGLEARTEEREVEGGLPGAAGPRENRGRQRAPINLDETGSLPFLRLAHFFLLNEEDDDQPRGLTKEQIDNLSMRNFGESDAFKTCSVCITEYAEGNKLRKLPCSHEYHVHCIDRWLSENSTCPICRRAVLISTNRESVV
Protein: Phospholipid transfer protein C2CD2L (C2 domain-containing protein 2-like) (C2CD2-like) (Transmembrane protein 24) (O14523)
Organism: Homo sapiens (Human)
Function: Lipid-binding protein that transports phosphatidylinositol, the precursor of phosphatidylinositol 4,5-bisphosphate (PI(4,5)P2), from its site of synthesis in the endoplasmic reticulum to the cell membrane. It thereby maintains the pool of cell membrane phosphoinositides, which are degraded during phospholipase C (PLC) signaling. Plays a key role in the coordination of Ca(2+) and phosphoinositide signaling: localizes to sites of contact between the endoplasmic reticulum and the cell membrane, where it tethers the two bilayers. In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane, abolishing phosphatidylinositol transport to the cell membrane. Positively regulates insulin secretion in response to glucose: phosphatidylinositol transfer to the cell membrane allows replenishment of PI(4,5)P2 pools and calcium channel opening, priming a new population of insulin granules.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28209843}; Single-pass membrane protein {ECO:0000269|PubMed:28209843}. Cell membrane {ECO:0000269|PubMed:28209843}; Peripheral membrane protein {ECO:0000269|PubMed:28209843}. Note=Localizes to sites of contact between the endoplasmic reticulum and the cell membrane (PubMed:28209843). Embedded into the endoplasmic reticulum membrane via its N-terminal transmembrane domain and associates with cell membrane via its C-terminus (PubMed:28209843). In response to elevation of cytosolic Ca(2+), it is phosphorylated at its C-terminus and dissociates from the cell membrane and localizes to the reticular endoplasmic reticulum (PubMed:28209843). Reassociates with cell membrane upon dephosphorylation (PubMed:28209843). {ECO:0000269|PubMed:28209843}.
Interaction partners:
Sequence:
MDPGWGQRDVGWAALLILFAASLLTVFAWLLQYARGLWLARARGDRGPGPALAGEPAGSLRELGVWRSLLRLRATRAGAAEEPGVRGLLASLFAFKSFRENWQRAWVRALNEQACRNGSSIQIAFEEVPQLPPRASISHVTCVDQSEHTMVLRCQLSAEEVRFPVSVTQQSPAAVSMETYHVTLTLPPTQLEVNLEEIPGEGLLISWAFTDRPDLSLTVLPKLQARERGEEQVELSTIEELIKDAIVSTQPAMMVNLRACSAPGGLVPSEKPPMMPQAQPAIPRPNRLFLRQLRASHLGNELEGTEELCCVAELDNPMQQKWTKPARAGSEVEWTEDLALDLGPQSRELTLKVLRSSSCGDTELLGQATLPVGSPSRPLSRRQLCPLTPGPGKALGPAATMAVELHYEEGSPRNLGTPTSSTPRPSITPTKKIELDRTIMPDGTIVTTVTTVQSRPRIDGKLDSPSRSPSKVEVTEKTTTVLSESSGPSNTSHSSSRDSHLSNGLDPVAETAIRQLTEPSGRVAKKTPTKRSTLIISGVSKVPIAQDELALSLGYAASLEASVQDDAGTSGGPSSPPSDPPAMSPGPLDALSSPTSVQEADETTRSDISERPSVDDIESETGSTGALETRSLKDHKVSFLRSGTKLIFRRRPRQKEAGLSQSHDDLSNATATPSVRKKAGSFSRRLIKRFSFKSKPKANGNPSPQL