wanglab/gogpt-training-data huggingface dataset:
Protein: CTP-dependent diacylglycerol kinase 1 (EC 2.7.1.174) (Diglyceride kinase 1) (DAG kinase 1) (P87170)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: CTP-dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PA phosphatase ned1. May be involved in vesicle trafficking between the endoplasmic reticulum and the Golgi apparatus (By similarity). Involved in pre-tRNA splicing.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372, ECO:0000269|PubMed:26990381}; Multi-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:26990381}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Nuclear elongation and deformation protein 1
- Uncharacterized protein C23C11.01
- Uncharacterized acyltransferase C1851.02
- Putative phosphatidate cytidylyltransferase
- Putative lysophosphatidic acid:oleoyl-CoA acyltransferase
- Probable diacylglycerol pyrophosphate phosphatase 1
- Phospholipase D1
- Probable choline-phosphate cytidylyltransferase
- Lysophospholipid acyltransferase
- Uncharacterized CDP-alcohol phosphatidyltransferase class-I family protein C22A12.10
Sequence:
MSTKLTWSQWSKKHEIPRKALHTSIGFFALLLQGCGYHAAQIIPVIEIGFIPAFTGDVIRFNWPAFSRLYNRVIGPLMRESEKNAWNGVIFYMIGVWIVLKVFPEEIAVMSVLLLSWCDTTASTVGRKWGKYTPKIAKNKSLAGSLGAFVCGVFCCYVYWGLFRTGPDSLAAQSRIPFPWLCLINGFIGAFAEAMDVWGLDDNLVIPVVSACLLYLIM
Protein: Threonine dehydratase biosynthetic, chloroplastic (EC 4.3.1.19) (Threonine deaminase) (P31212)
Organism: Solanum tuberosum (Potato)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
- Acetolactate synthase
Sequence:
PFDAPGVIKGQGTIGTEINRQLKDIHAVFVPVGGGGLISGVAAYFTQVAPHTKIIGVEPYGAASMTLSLYEGHRVKLENVDTFADGVAVALVGEYTFAKCQELIDGMVLVRNDGISAAIKDVYDEGRNILETSGAVAIAGAAAYCEFYNIKNENIVAIASGANMDFSKLHKVTELAELGSDNEALLATFMIEQPGSFKTFAKLVGSMNITEVTYRFTSERKEALVLYRVDVDEKSDLEEMIKKLNSSNMKTFNFSHNELVAEHIKHLVGGSASISDEIFGEFIFPEKAGTLSTFLEAFSPRWNITLCRYRDQGDINGNVLVGFQVPQSEMDEFKSQADGLGYPYELDNSNEAFNIVVAE
Protein: Transcriptional regulator PsrA (M9YCR7)
Organism: Azotobacter vinelandii CA6
Interaction partners:
Sequence:
MPHSETVERILDAAEQLFAERGFAETSLRLITSKADVNLAAVNYHFGSKSALIEAVFSRVLGPFCSGLGRELDRRQAVGVGLEELLEITIAQAQAARPRSGMAIFMRLLGLVLNQGQEHLRRYLEDTYGKLFRRYLLLLEEAVPGIPPLELFWRTHFMLGAATFSLSGIETLRAFAAERFEVQTSSEQALRLLVPFLAAGMRAGSAIEDPQLANARPRPRGKAVQPASAVRPVSPEADE
Protein: Transcription factor PRE3 (Basic helix-loop-helix protein 135) (AtbHLH135) (bHLH 135) (Protein ACTIVATION-TAGGED BRI1 SUPPRESSOR 1) (ATBS1) (Protein PACLOBUTRAZOL RESISTANCE 3) (Protein TARGET OF MOOPTEROS 7) (Transcription factor EN 67) (bHLH transcription factor bHLH135) (Q9CA64)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Atypical and probable non DNA-binding bHLH transcription factor required for MONOPTEROS-dependent root initiation in embryo. Promotes the correct definition of the hypophysis cell division plane. Transcriptionally controlled by MONOPTEROS. Moves from its site of synthesis in pro-embryos cells into the hypophysis. Regulates brassinosteroid (BR) signaling by sequestering negative BR signaling components. May function as positive regulator of gibberellin signaling. May play a role in the regulation of light signaling and possibly auxin signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:20023194, ECO:0000269|PubMed:20220754}. Cytoplasm {ECO:0000269|PubMed:20220754}.
Interaction partners:
- Transcription factor bHLH150
- Transcription factor HFR1
- Transcription factor bHLH148
- Transcription factor IBH1
- Protein SIEL
- Transcription factor bHLH147
- Serine carboxypeptidase 24
- Auxin response factor 5
- Transcription factor AIG1
- Transcription factor bHLH49
Sequence:
MSGRRSRSRQSSGTSRISEDQINDLIIKLQQLLPELRDSRRSDKVSAARVLQDTCNYIRNLHREVDDLSERLSELLANSDTAQAALIRSLLTQ
Protein: ATP-dependent RNA helicase dbp10 (EC 3.6.4.13) (Q09719)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: ATP-binding RNA helicase involved in the biogenesis of 60S ribosomal subunits and is required for the normal formation of 25S and 5.8S rRNAs.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- 25S rRNA
- rRNA biogenesis protein rrp36
- GTPase grn1
- Probable nucleolar complex protein 14
- Pescadillo homolog
- Uncharacterized RNA-binding protein C365.04c
- Uncharacterized RNA-binding protein C1827.05c
- Uncharacterized protein C1604.06c
- Ribosome biogenesis protein erb1
- Brix domain-containing protein C1B9.03c
Sequence:
MSGFQTSDEVDISNSLKAFPVDIATDNQKDKHENVGENVSDEDDGNYIASKLLESNRRTKGKKGNGKASNFQSMGLNQTLLRAIFKKGFKAPTPIQRKTIPLLLEGRDVVGMARTGSGKTAAFVIPMIEHLKSTLANSNTRALILSPNRELALQTVKVVKDFSKGTDLRSVAIVGGVSLEEQFSLLSGKPDIVVATPGRFLHLKVEMKLELSSIEYVVFDEADRLFEMGFAAQLTEILHALPTSRQTLLFSATLPRTLVDFAKAGLQDPVLVRLDVESKVSADLQSAFFSVKTAEREAALLCILQDIIKLPLKDNVRPREIGNVNNPKKRKRALELALKGSESGSPDSTLVFVPTKHHVEYVSELLVQAGYSVSKIYGSLDQEARLNEINNFRLGKTNLLVVTDVASRGIDIPLLANVINYDFPPQPKVFVHRVGRTARAGRTGWAYSLVRAEDAGYLLDLQLFLNRPLVTSSKQVKTDSDCDFTKQIVLGSLPQELVAELLEWVQRIVSRDVELQQLSNVAARGEKLYFRTRATCSAESAKRAKELVDSKGWSSNNPLFGDVSVIEAEEKYAELLSKVSSYRPSETVFEIGQRGHLKTEAAEIMRKRRNKVKPKGIKSEVASDKITDSSPGNMSEASESELEEVFKNPKELSKKKTTDFKDKEYYMSHYAPKESIQETGYAINSGENFTTAARHAILDLTNDEGIEQSRKGGQRWDPKKKKFVNIINDEDGSKGSPKIIRGESGVKLPATYRSGRFDEWKASKAFGANDSPIRENKRYKHNKLQTPKPADKFRDNYHKQNKRNREAKERGIGIKVNSELKSAVEIRKARELKEKRLAKNNRPSKKHR
Protein: Potassium voltage-gated channel subfamily A member 5 (RCK7) (RK4) (Voltage-gated potassium channel subunit Kv1.5) (P19024)
Organism: Rattus norvegicus (Rat)
Function: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane. Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel. Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation. Homotetrameric channels display rapid activation and slow inactivation. May play a role in regulating the secretion of insulin in normal pancreatic islets (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15618540, ECO:0000269|PubMed:2361015}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Voltage-gated potassium channel subunit beta-2
- Voltage-gated potassium channel subunit beta-1
- Voltage-gated potassium channel subunit beta-3
- A-type potassium channel modulatory protein KCNIP2
- Leucine-rich glioma-inactivated protein 1
- Calcium-activated potassium channel subunit alpha-1
- Disks large homolog 4
- Potassium voltage-gated channel subfamily A member 4
- Disks large homolog 1
- Contactin-2
Sequence:
MEISLVPLENGSAMTLRGGGEAGASCVQTPRGECGCPPTSGLNNQSKETLLRGRTTLEDANQGGRPLPPMAQELPQPRRLSAEDEEGEGDPGLGTVEEDQAPQDAGSLHHQRVLINISGLRFETQLGTLAQFPNTLLGDPAKRLHYFDPLRNEYFFDRNRPSFDGILYYYQSGGRLRRPVNVSLDVFADEIRFYQLGDEAMERFREDEGFIKEEEKPLPRNEFQRQVWLIFEYPESSGSARAIAIVSVLVILISIITFCLETLPEFRDERELLRHPPVPPQPPAPAPGINGSVSGALSSGPTVAPLLPRTLADPFFIVETTCVIWFTFELLVRFFACPSKAEFSRNIMNIIDVVAIFPYFITLGTELAEQQPGGGGQNGQQAMSLAILRVIRLVRVFRIFKLSRHSKGLQILGKTLQASMRELGLLIFFLFIGVILFSSAVYFAEADNHGSHFSSIPDAFWWAVVTMTTVGYGDMRPITVGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETDHEEQAALKEEQGNQRRESGLDTGGQRKVSCSKASFCKTGGSLESSDSIRRGSCPLEKCHLKAKSNVDLRRSLYALCLDTSRETDL
Protein: Hepatic sodium/bile acid cotransporter (Cell growth-inhibiting gene 29 protein) (Na(+)/bile acid cotransporter) (Na(+)/taurocholate transport protein) (Sodium/taurocholate cotransporting polypeptide) (NTCP) (Solute carrier family 10 member 1) (SLC10A1) (Q14973)
Organism: Homo sapiens (Human)
Function: As a major transporter of conjugated bile salts from plasma into the hepatocyte, it plays a key role in the enterohepatic circulation of bile salts necessary for the solubilization and absorption of dietary fat and fat-soluble vitamins. It is strictly dependent on the extracellular presence of sodium. It exhibits broad substrate specificity and transports various bile acids, such as taurocholate, cholate, as well as non-bile acid organic compounds, such as estrone sulfate. Works collaboratively with the ileal transporter (NTCP2), the organic solute transporter (OST), and the bile salt export pump (BSEP), to ensure efficacious biological recycling of bile acids during enterohepatic circulation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:14660639, ECO:0000269|PubMed:24867799}; Multi-pass membrane protein {ECO:0000269|PubMed:35545671, ECO:0000269|PubMed:35580629, ECO:0000269|PubMed:35580630, ECO:0000269|PubMed:38233573}.
Interaction partners:
- Solute carrier organic anion transporter family member 1A2
- Bile salt export pump
- Sodium/bile acid cotransporter 7
- Cytochrome P450 7A1
- Probable non-functional immunoglobulin heavy variable 3-16
- Solute carrier organic anion transporter family member 1B1
- Bile acid receptor
- Solute carrier organic anion transporter family member 1B3
- Gastrotropin
- Nuclear receptor subfamily 0 group B member 2
Sequence:
MEAHNASAPFNFTLPPNFGKRPTDLALSVILVFMLFFIMLSLGCTMEFSKIKAHLWKPKGLAIALVAQYGIMPLTAFVLGKVFRLKNIEALAILVCGCSPGGNLSNVFSLAMKGDMNLSIVMTTCSTFCALGMMPLLLYIYSRGIYDGDLKDKVPYKGIVISLVLVLIPCTIGIVLKSKRPQYMRYVIKGGMIIILLCSVAVTVLSAINVGKSIMFAMTPLLIATSSLMPFIGFLLGYVLSALFCLNGRCRRTVSMETGCQNVQLCSTILNVAFPPEVIGPLFFFPLLYMIFQLGEGLLLIAIFWCYEKFKTPKDKTKMIYTAATTEETIPGALGNGTYKGEDCSPCTA
Protein: Actin depolymerizing factor 7 (Actin-depolymerizing factor-like) (A1XJ44)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Profilin
- Profilin
- Profilin
- Profilin
- Profilin
- Profilin
- Profilin
- Profilin
- Profilin
- Profilin
Sequence:
MANSASGMAVNDECKTKFLELKAKRNYRFIVFKIEENLQQIVVEKVGAPKDSYEKLCSSLPSDECRYAVYDFDFTTDENCQKSKIFFIAWSPDTSRVRSKMLYASSKDRFRRELDGVQVELQATDPSEMSFDIVKERAF
Protein: Clock interacting protein circadian, isoform A (Clock interacting protein circadian, isoform B) (HL03650p) (RH68619p) (Q95R29)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- oxaloacetate tautomerase
- 5'-nucleotidase domain-containing protein 1
Sequence:
MAPTICSEKKQLRETRRHHGVATAAISSASATASTASSSSSLSVGSTSAAAATQASSVLNHVAKGSMNSMSRRRPARLQRRMPHILARVSSFSTDTSSGVETEVEMDSEQRMQLDDDRYSDARIQGLQQQPHSSSDNIKTVLQPTTASGYSSKQNRSARAKNCDREVPLQIEDDHDGDSGYEYSQDPIKEQHMYHQNSEGLLSIAIKTIKLVQRNKLLQKRLAQLQLETSEFIASVLANPENRQFRDKMSPKAEAKVSNMLLRH
Protein: Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3Fb (Semaphorin-3F isoform X2) (E7F6C0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MLLDSLWPVQVLLVLSVLTLVLGNEPQNAPRVFLSFKDLRSTGTAHYFSFLLNTSDYRILRMDEDHDRMYVGSKDYILSLDLHDINREPLIIHWPVSPQRKTECVLSGKDTNGECGNFIRLIEPWNRTHLYICGTGAYNPVCTYVNRGRKPMTAMHLQMPQTRGRASRAAEPETVFDETGLQEYVFHLEPGKEDSGKGKCPYDPKLNSVSALINGELYAGVYIDFMGTDSAIFRTLGKNAVMRTDQYNSRWLNDPSFVHVHLIPDSGEKNDDKLYFFFREKSSEMGQSPKSQSRIGRICLNDDGGHCCLVNKWSTFLKARLICSVPGADGIETHFDELRDVYIQPTQDTKNPVIYGVFSVSGSVFKGSAVCVYSMADIRMVFNGPFAHKEGPNYQWVAYTGKIPYPRPGTCPGGTFTPNMKSTKDYPDEVINFMRNHPTMYNSVYPVHKRPLVVRTNVDYEFTTITVDQVTAADGNYEVLFLGTDRGTVQKVIVLPSDDLQTEELVLEEVEVFKVPTSITTMKISSKRQQLYVASAVGVTHMALHRCDVYGEACADCCLARDPYCAWDGKSCSRYSASQKRRSRRQDVKYGNPIRQCRGYNSNINKNTLETVQYGVEGSSTFLECQARSPHAAIKWHLHRDNSDRRREVRSDGRVLKTDQGLLLRSLQSSDSGIYICTATEKNFKHTLVKLQLLVLTNQAVNNILVDTGRPVVSPLQSSAWTPSAGQYKDLLTILSQPEMGLINQYCQDYWQYGDPLTGVIKAKDLKELKEQKKPRNRRHHGDEEET
Protein: Cytochrome P-450 monooxygenase DoxA (EC 1.14.13.181) (13-deoxycarminomycin C-13 hydroxylase) (13-deoxydaunorubicin C-13 hydroxylase) (13-dihydrocarminomycin C-13 hydroxylase) (13-dihydrodaunorubicin C-13 hydroxylase) (Daunorubicin C-14 hydroxylase) (Q93MI2)
Organism: Streptomyces peucetius subsp. caesius
Function: Involved in the biosynthesis of the anthracyclines carminomycin, daunorubicin (daunomycin) and doxorubicin (adriamycin) which are aromatic polyketide antibiotics that exhibit high cytotoxicity and are widely applied in the chemotherapy of a variety of cancers. In vivo, DoxA catalyzes the C-13 hydroxylation of 13-deoxycarminomycin and 13-deoxydaunorubicin to yield 13-dihydrocarminomycin and 13-dihydrodaunorubicin, respectively, as well as the oxidation of these 13-dihydro-anthracyclines to their respective 13-keto forms, carminomycin and daunorubicin. In vivo, it also catalyzes the C-14 hydroxylation of daunorubicin to form doxorubicin. It can only use NADP. DoxA acts jointly with DnrV.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSGEAPRVAVDPFACPMMTMQRKPEVHDAFREAGPVVEVNAPAGGPAWFITDDALSRYVLADPRLVKDPDLAPAAWRGVVDGLDIPVPELRPFTLIAVDGEAHRRLHRIHAPAFNPRRLAERTDRIAAIAGRLLTELADASGRSGEPAELIGGFAYHFPLLVICELLGVPVTVPMAREAVSVLKALASAAQSGGGDGTDPAGGVPDTSALESLLLEAVHSARRNDTPTMTRVLYEHTQAEFGSVSDNQLVYMITGIIFAGHERTGSFLGFLLAEVLAGRLAADADEDAVSRFVEEAVRYHPPVPYTLWRFAATEVTIGGVRLPPGAPVLVDIEGTNTDGRHHDAPHAFHPDRPSWRRLTFGDGPHYCIGEQLAQLESRTMIGVLRSRFPEARLAVPYDELRWCRNGAQTARLTELPVWLR
Protein: Tetraspanin-10 (Tspan-10) (Oculospanin) (Q8VCF5)
Organism: Mus musculus (Mouse)
Function: Regulates maturation of the transmembrane metalloprotease ADAM10.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKEEECSPLLSQDTAGREHPLTRNSPPTANIPCPAPWENQKGSWGCRCCPGAKRQASGEGQASSLPLSTGSNCVKYLIFLSNFLFSLPSLLALAAGLWGLTVKRSQGIGWGGPVPTDPMLMLVLGGLVVSVVSLSGCLGAFCENSCLLHWYCGAVLFCLALEALAGVLMVTLWKPLQDSLKYTLHAAIIHYWDDPDLHFLLDQVQLGLQCCGAVSYQDWQQNLYFNCSSPGVQACSLPASCCINPQEDGAVVNTQCGFGALGLDQNVAGQVVFLQGCWPALQEWLRGNTGAIGDCAVAVVMIQGTELLLAACLLRALAVHEAAEDIEAGPL
Protein: Valine--tRNA ligase (EC 6.1.1.9) (Valyl-tRNA synthetase) (ValRS) (Q72E47)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02004}.
Interaction partners:
- GMP synthase
- Isoleucine--tRNA ligase
- Leucine--tRNA ligase
- Arginine--tRNA ligase
- Alanine--tRNA ligase
- Serine--tRNA ligase
- Aspartate--tRNA
- Phenylalanine--tRNA ligase alpha subunit
- Threonine--tRNA ligase
- Glycine--tRNA ligase beta subunit
Sequence:
MAENALPKGYEPRDVEERWRRHWEDNRTFTPDMDAPGEPYSIVIPPPNVTGALHIGHALNHVLIDVLCRNARQQGKKVLWLPGTDHAGIATQNVVERALAKEGLSRHDLGREAFIERVWQWKEEYGNRILNQIRMLGDSVDWTRERFTMDEGLSKAVRKVFVDLYNGGYIYRGNYIINWCNRCHTALADDEVDHMPEQGHLYHVRYDFEDGSGSVVIATTRPETIMADTGVCVHPEDERYAGLIGKKILVPVIGRAVPLFADTYVDREFGTGALKVTPCHDPNDWTLGERHGLAFIQCIDEDGNMTAEAGPYAGLTKEECRKRIVADLEASGQLVRVEELNHSVGHCYRCKTVVEPHMSEQWFVASTKLAPRARAAVPQMTQIFPESWMKTYFNWLDNIRDWCISRQIWWGHRIPAWTCGKCGKLIVSEQDPTACPDCGCTDLTQDPDVLDTWFSSALWPFSTMGWPDKTKDLATFYPTSVLVTGFDILFFWVARMMMLGMHFMDEVPFKHVYLHALVRDGEGRKMSKSTGNVIDPLAMIDKYGTDSLRFTLAAFAAMGRDIKLSEDRIEGYRHFVNKVWNAARFSLMNLPEEAPAALDLDNVKGMHHKWILHRLEELKASQAAGIDGYRFNEVAQGLYRFWWNEFCDWYLELIKPDMQAGGERQATAQYVLWTVLREALLLLHPFMPFVTAEVWQALPGHAGDDIATKLYPAARPGCRDVKDAEHMELVQATISAVRTIRAELNIAPSYRLTTLVRPASAEDAATLEEGREMLMTLARLDGLTVAVDVEAPKASASSVVAGNEVIVPLTGAVDFEAELARLDKELGKIEKDFVQVNKKLANESFVSKAPADVVAKERARAEELSDAKAKLEALQQRFRDAIGK
Protein: LD02349p (Q8T0H7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSPEPMTLLTAGGAAATKLSNAATLLAAKELHESKKQLEKERSLRRLLEDELQMIKRQLYSVATAPPGTAVAAASGGSSGAYIPREVIEHTDNFVRSEDLEELGGTVSYVEIDEMTGQQQVVVCSSIEELEADAAAEIITEDQVHEEVILSSNSSTESENEVNVNAIAKAYAEGCTSSAAMLQPILQAAIKATPKVEVERIHEKIVKVKTEKHDLPSMQTAPHYQHSHRQNLETIVQAIRHLEGDHLFADGSGGQEKFGQQQNLQQHHHQMSGVHHQQLQHHRLAQDAPLALTTTGKQHAALAELRPFLQLKSGGNKQVIITAKTAKDSGGLVSTSTSSTAVTPTAIFKVQTTGGHGNGSHLPAGSSTGTIITGSNGSGGAQQLTITTSLKQCRPGVIVAKQLPSS
Protein: Eukaryotic translation initiation factor 4E-binding protein 2 (4E-BP2) (eIF4E-binding protein 2) (Phosphorylated heat- and acid-stable protein regulated by insulin 2) (PHAS-II) (P70445)
Organism: Mus musculus (Mouse)
Function: Repressor of translation initiation involved in synaptic plasticity, learning and memory formation. Regulates EIF4E activity by preventing its assembly into the eIF4F complex: hypophosphorylated form of EIF4EBP2 competes with EIF4G1/EIF4G3 and strongly binds to EIF4E, leading to repress translation. In contrast, hyperphosphorylated form dissociates from EIF4E, allowing interaction between EIF4G1/EIF4G3 and EIF4E, leading to initiation of translation. EIF4EBP2 is enriched in brain and acts as a regulator of synapse activity and neuronal stem cell renewal via its ability to repress translation initiation. Mediates the regulation of protein translation by hormones, growth factors and other stimuli that signal through the MAP kinase and mTORC1 pathways.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:18515545}. Nucleus {ECO:0000269|PubMed:18515545}.
Interaction partners:
- Eukaryotic translation initiation factor 4E
- Regulatory-associated protein of mTOR
- Serine/threonine-protein kinase mTOR
- Eukaryotic translation initiation factor 4E-binding protein 3
- Eukaryotic translation initiation factor 4E-binding protein 1
Sequence:
MSASAGGSHQPSQSRAIPTRTVAISDAAQLPQDYCTTPGGTLFSTTPGGTRIIYDRKFLLDRRNSPMAQTPPCHLPNIPGVTSPGALIEDSKVEVNNLNNLNNHDRKHAVGDEAQFEMDI
Protein: PH signal transduction protein PalH (Q2U5X6)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- pH-response transcription factor pacC/RIM101
- Calpain-like protease palB/RIM13
- pH-response regulator protein palC
- Vacuolar-sorting protein SNF7
Sequence:
MGDDVRLAPRQIWAQPTTSSTKTYQPGCTPFVLPSEGYIYLNLSYSIALSENAVFEPVCTSTATASRGPSPMLDTRDPFYASVTPQLYAIGCATVVSYLLVIILLITPRTFYVGGPGGGANFLGRHGMISGSYSGNSSVVGVGGRPWLQKVAALLVAISLTIATADSFKVAEDQYIHGYSDADALASEVIDGMEIRVIRVISSTFLWLAQVQTLIRLFPRHKEKVMIKWAGFALIVLDTIFSILDKFLVQSNTTRPRLYEDAIPALSYLFELALNLLYAAWVIFYSLSKHRFAFFHPKMRNICLVALLSLCAVLIPVVFFVLDIAKPEVAGWGTYIRWVGSAAASVVVWEWVERIEALERDERKDGILGREIFDGDEMLEVTPSEEVDWPRQNNRNDRGGGTGTSSGWGGMMGLTQRPLRTRVGHPGGRNRQTRADAQNPAISNDPRHRGAARPTPPPAAVTPVSRADTTSAASTVYNVHYHPVSSPTPPVAMPHMEEENEADDYGDVAVKELETAVEEHRSNSAHERVSAEQTREESPQIINVDDRWRTILNPFRRRRASLPKEVASAQAEEEQEDPSRDGDELYHGETSEQESSRPVVNRLFALNRKPRPGSGRQGSDTPLPVTVIPARRRGQHTWSPEWFTESSLLEPSPGQRPRPNRTDLPVRVIQPQARTAAPWATPNEGEFGYGDYELRYDPEAAALVGPGESHPYPLSTDNAYYDTNVDPERPSVAERYRPTQELDQSAPERLQSPQHPQPTNSPNDSQATNENSRPR
Protein: Yop proteins translocation protein K (Q01252)
Organism: Yersinia enterocolitica
Function: Belongs to an operon involved in the translocation of Yop proteins across the bacterial membranes or in the specific control of this function.
Interaction partners:
Sequence:
MMENYITSFQLRFCPAAYLHLEQLPSLWRSILPYLPQWRDSAHLNAALLDEFSLDTDYEEPHGLGALPLQPQSQLELLLCRLGLVLHGEAIRRCVLASPLQQLLTLVNQETLRQIIVQHELLIGPWPTNWQRPLPTEIESRTMIQSGLAFWLAAMEPQPQAWCKRLSLRLPLATPSEPWLVAESQRPLAQTLCHKLVKQVMPTCSHLFK
Protein: GlmR transcriptional regulator (Q9HT24)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Glutamine--fructose-6-phosphate aminotransferase
- protein-N
- Phosphofructokinase
- Anti-sigma factor SbrR
Sequence:
MISKRNTPQRRHAILALLSEQGEVSVDALAKRFSTSEVTIRKDLAAMESHGLLLRRYGGAVPMPQELIGEAAQPVSPYKQAIGRAAAARIREHARIIIDSGSTTAAMIPELGHKPGLVVMTNSLNVVNALRELEHEPVLLMTGGTWDPHSESFQGQVAEQVLRSYDFDQLFIGADGIDLERGTTTFNELLGLSRVMAEVAREVIVMAEADKVGRRIPNQELPWSSIHTLITDERLESSAREQITARGVTLICTPVEA
Protein: Equilibrative nucleobase transporter 1 (Protein FOAP-13) (Solute carrier family 43 member 3) (Q8NBI5)
Organism: Homo sapiens (Human)
Function: Sodium-independent purine-selective nucleobase transporter which mediates the equilibrative transport of extracellular purine nucleobases such as adenine, guanine and hypoxanthine. May regulate fatty acid (FA) transport in adipocytes, acting as a positive regulator of FA efflux and as a negative regulator of FA uptake (By similarity).
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:26455426}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MAGQGLPLHVATLLTGLLECLGFAGVLFGWPSLVFVFKNEDYFKDLCGPDAGPIGNATGQADCKAQDERFSLIFTLGSFMNNFMTFPTGYIFDRFKTTVARLIAIFFYTTATLIIAFTSAGSAVLLFLAMPMLTIGGILFLITNLQIGNLFGQHRSTIITLYNGAFDSSSAVFLIIKLLYEKGISLRASFIFISVCSTWHVARTFLLMPRGHIPYPLPPNYSYGLCPGNGTTKEEKETAEHENRELQSKEFLSAKEETPGAGQKQELRSFWSYAFSRRFAWHLVWLSVIQLWHYLFIGTLNSLLTNMAGGDMARVSTYTNAFAFTQFGVLCAPWNGLLMDRLKQKYQKEARKTGSSTLAVALCSTVPSLALTSLLCLGFALCASVPILPLQYLTFILQVISRSFLYGSNAAFLTLAFPSEHFGKLFGLVMALSAVVSLLQFPIFTLIKGSLQNDPFYVNVMFMLAILLTFFHPFLVYRECRTWKESPSAIA
Protein: Uncharacterized protein (Q57WB9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGIIKHVAVILDVSEASLEQHVLERVRQLDEDTVVRRLSEEKAGKLPDFIKLSEDIIEKNDLRKSGEGSVESIQRFVCFVTDNKTRQNGMVAYAMHCLQIPVLSLTKGQKAKGNDDAEHWVSTILYKDLDGSHTDPLAAVNEFFTFPDKVGELLAVEGRDSQLTLQYCRELRSYLQRAWSAEVKLVGPNGCDMSEEGLDGTKCGETDNVEEQVEVESGIHAPLVKELLGNSQLESTHQNDHLLHGAMYALNRHENLPIIRYRLQRGVNIILCRPMSSSLEKLFNKFSRMRGGAEDVRRSFIDAVKSLLQFEGRWLDMPRRRVVLIREGVAHSWSAWLGNEVIHPLVDWIPVDVKAGNIADHCASLEASVKKAVRRLSR
Protein: Trafficking protein particle complex subunit (Q9SYB8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum {ECO:0000256|RuleBase:RU366065}. Golgi apparatus, cis-Golgi network {ECO:0000256|RuleBase:RU366065}.
Interaction partners:
- Tetratricopeptide repeat
- Transport protein particle
- Trafficking protein particle complex subunit
- Trafficking protein particle complex II-specific subunit 130 homolog
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit
- Trafficking protein particle complex subunit 2-like protein
- SNARE-like superfamily protein
- Trafficking protein particle complex II-specific subunit 120 homolog
- Trafficking protein particle complex subunit-like protein
Sequence:
MQFFGGSEISPSPPVPTASGNNAHMMYVFNRNGVCLLYKEWNRPLHTLNPQQDHKLMFGLLFSLKSLTAKMDPVNADKGNLGVPQLPGQGCSFHSFRTNTYKLSFMETPSGIKIILVTHPKTGDLRESLKYIYSLYVEYVVKNPIYSPGSPIKSELFNTALDQYVRSIS