wanglab/gogpt-training-data huggingface dataset:
Protein: 3-isopropylmalate dehydratase small subunit 2 (EC 4.2.1.33) (2-(omega-methylthio)alkylmalate dehydratase small subunit 2) (EC 4.2.1.170) (AtLEUD1) (Isopropylmalate isomerase 2) (Isopropylmalate isomerase small subunit 2) (IPMI SSU2) (Methylthioalkylmalate isomerase small subunit) (MAM-IS) (Q9ZW84)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate (Probable). Functions redundantly with LEUD2 in the methionine chain elongation pathway of aliphatic glucosinolate formation.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:19597944, ECO:0000269|PubMed:20663849}. Plastid {ECO:0000269|PubMed:32612621}.
Interaction partners:
- 3-isopropylmalate dehydrogenase 1, chloroplastic
- 3-isopropylmalate dehydrogenase 3, chloroplastic
- 3-isopropylmalate dehydrogenase 2, chloroplastic
- 3-isopropylmalate dehydratase large subunit, chloroplastic
- 2-isopropylmalate synthase 1, chloroplastic
- 2-isopropylmalate synthase 2, chloroplastic
- Methylthioalkylmalate synthase 1, chloroplastic
- Methylthioalkylmalate synthase 3, chloroplastic
- Methionine aminotransferase BCAT4
- 3-isopropylmalate dehydratase small subunit 3
Sequence:
MAYSLPTFPQALPCSSTKTSSSLATFRSPFLRFNGSTSLIPSSISITSRGTSSPTIIPRAAASESDSNEALANTTFHGLCYVLKDNIDTDQIIPAGAACTFPSNQQERDEIAAHALSGLPDFHKTRFIEPGENRSKYSIIIGGENFGCGSSREHAPVCLGAAGAKAIVAESYARIFFRNSVATGEVFPLESEVRVCEECKTGDTVTIELSDSGGLLTNHTTGKNYKLKSIGDAGPVIDAGGIFAYARMMGMIPSLA
Protein: Phospholipase A and acyltransferase 1 (EC 2.3.1.-) (EC 3.1.1.32) (EC 3.1.1.4) (HRAS-like suppressor 1) (HRSL1) (Phospholipid-metabolizing enzyme A-C1) (Rat LRAT-like protein-2) (RLP-2) (D2KX21)
Organism: Rattus norvegicus (Rat)
Function: Exhibits both phospholipase A1/2 and acyltransferase activities (By similarity). Shows phospholipase A1 (PLA1) and A2 (PLA2) activity, catalyzing the calcium-independent release of fatty acids from the sn-1 or sn-2 position of glycerophospholipids (By similarity). Shows O-acyltransferase activity, catalyzing the transfer of a fatty acyl group from glycerophospholipid to the hydroxyl group of lysophospholipid (By similarity).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q9QZU4}. Nucleus {ECO:0000250|UniProtKB:Q9QZU4}.
Interaction partners:
- Mitochondrial disaggregase
Sequence:
MAVNDCFSLTYPHNPHPGDLIEVFRPCYQHWALYLGDGYVINIAPVDGIPSSFSSAKSVFSTKALVKMQLLKDVVGNDTYRINNKYDTTYPPLPVEEVIQRSEFAIGQEVTYDLLVNNCEHFVTLLRYGEGVSEQANRAIGTIGLVAAGIDIFTFLGLFPKRQGAKS
Protein: Transcription factor PIF4 (Basic helix-loop-helix protein 9) (AtbHLH9) (bHLH 9) (Phytochrome-interacting factor 4) (Short under red-light 2) (Transcription factor EN 102) (bHLH transcription factor bHLH009) (Q8W2F3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor acting negatively in the phytochrome B signaling pathway. May regulate the expression of a subset of genes involved in cell expansion by binding to the G-box motif (By similarity). Activated by CRY1 and CRY2 in response to low blue light (LBL) by direct binding at chromatin on E-box variant 5'-CA[CT]GTG-3' to stimulate specific gene expression to adapt global physiology (e.g. hypocotyl elongation in low blue light).
Subcellular location: Nucleus {ECO:0000269|PubMed:26724867}.
Interaction partners:
- Protein BRASSINAZOLE-RESISTANT 1
- Phytochrome B
- Auxin response factor 6
- DELLA protein RGA
- DELLA protein GAI
- DELLA protein RGL2
- DELLA protein RGL1
- DELLA protein RGL3
- Cryptochrome-1
- Protein EARLY FLOWERING 3
Sequence:
MEHQGWSFEENYSLSTNRRSIRPQDELVELLWRDGQVVLQSQTHREQTQTQKQDHHEEALRSSTFLEDQETVSWIQYPPDEDPFEPDDFSSHFFSTMDPLQRPTSETVKPKSSPEPPQVMVKPKACPDPPPQVMPPPKFRLTNSSSGIRETEMEQYSVTTVGPSHCGSNPSQNDLDVSMSHDRSKNIEEKLNPNASSSSGGSSGCSFGKDIKEMASGRCITTDRKRKRINHTDESVSLSDAIGNKSNQRSGSNRRSRAAEVHNLSERRRRDRINERMKALQELIPHCSKTDKASILDEAIDYLKSLQLQLQVMWMGSGMAAAAASAPMMFPGVQPQQFIRQIQSPVQLPRFPVMDQSAIQNNPGLVCQNPVQNQIISDRFARYIGGFPHMQAATQMQPMEMLRFSSPAGQQSQQPSSVPTKTTDGSRLDH
Protein: FXYD domain-containing ion transport regulator (B0S4R4)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGQFSVLVLLTVLCAFFEETEANPFVYNYERLRIGGLIIAGLLVAGGLFVLLNPKCTRKNKKSEDDTSEL
Protein: Thioredoxin 1 (PfTRX1) (Q7KQL8)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. By modifying the redox status of targeted proteins, induces changes in their structure and activity. Reduces oxidized glutathione (GSSG), thereby acting as a backup for the glutathione redox system. Reduces nitroglutathione (GSNO), a compound involved in the transport of nitric oxide (NO). Also reduces oxidative stress by detoxifying hydrogen peroxide, tert-butyl hydroperoxide and cumene hydroperoxide. Activates ornithine aminotransferase OAT by reducing a disulfide bond in the substrate binding loop, thereby enhancing the affinity of OAT for its substrates. May reduce S-adenosyl-L-homocysteine hydrolase SAHH.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21203490}.
Interaction partners:
- Thioredoxin reductase
- Thioredoxin reductase.
- Thioredoxin peroxidase 1
- Glutathione reductase
- Peroxiredoxin
- Glutathione reductase.
- Glutathione peroxidase
- Plasmoredoxin
Sequence:
MVKIVTSQAEFDSIISQNELVIVDFFAEWCGPCKRIAPFYEECSKTYTKMVFIKVDVDEVSEVTEKENITSMPTFKVYKNGSSVDTLLGANDSALKQLIEKYAA
Protein: Leucine rich repeat containing 7 (A0A494C1A4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MMENLIRGRNPPQYQRSPCKEVRAALRKRPEEELQCLEMTTKRKIIGRLVPCRCFRGEEEIISVLDYSHCSLQQVPKEVFNFERTLEELYLDANQIEELPKQLFNCQALRKLSIPDNDLSNLPTTIASLVNLKELDISKNGVQEFPENIKCCKCLTIIEASVNPISKLPDGFTQLLNLTQLYLNDAFLEFLPANFGRLVKLRILELRENHLKTLPKSMHKLAQLERLDLGNNEFGELPEVLDQIQNLRELWMDNNALQVLPGSIGKLKMLVYLDMSKNRIETVDMDISGCEALEDLLLSSNMLQQLPDSIGLLKKLTTLKVDDNQLTMLPNTIGNLSLLEEFDCSCNELESLPSTIGYLHSLRTLAVDENFLPELPREIGSCKNVTVMSLRSNKLEFLPEEIGQMQKLRVLNLSDNRLKNLPFSFTKLKELAALWLSDNQSKALIPLQTEAHPETKQRVLTNYMFPQQPRGDEDFQSDSDSFNPTLWEEQRQQRMTVAFEFEDKKEDDENAGKVKDLSCQAPWERGQRGITLQPARLSGDCCTPWARCDQQIQDMPVPQNDPQLAWGCISGLQQERSMCTPLPVAAQSTTLPSLSGRQVEINLKRYPTPYPEDLKNMVKSVQNLVGKPSHGVRVENSNPTANTEQTVKEKYEHKWPVAPKEITVEDSFVHPANEMRIGELHPSLAETPLYPPKLVLLGKDKKESTDESEVDKTHCLNNSVSSGTYSDYSPSQASSGSSNTRVKVGSLQTTAKDAVHNSLWGNRIAPSFPQPLDSKPLLSQREAVPPGNIPQRPDRLPMSDTFTDNWTDGSHYDNTGFVAEETTAENANSNPLLSSKSRSTSSHGRRPLIRQDRIVGVPLELEQSTHRHTPETEVPPSNPWQNWTRTPSPFEDRTAFPSKLETTPTTSPLPERKEHIKESTEIPSPFSPGVPWEYHDSNPNRSLSNVFSQIHCRPESSKGVISISKSTERLSPLMKDIKSNKFKKSQSIDEIDIGTYKVYNIPLENYASGSDHLGSHERPDKMLGPEHGMSSMSRSQSVPMLDDEMLTYGSSKGPQQQKASMTKKVYQFDQSFNPQGSVEVKAEKRIPPPFQHNPEYVQQASKNIAKDLISPRAYRGYPPMEQMFSFSQPSVNEDAVVNAQFASQGARAGFLRRADSLVSATEMAMFRRVNEPHELPPTDRYGRPPYRGGLDRQSSVTVTESQFLKRNGRYEDEHPSYQEVKAQAGSFPVKNLTQRRPLSARSYSTESYGASQTRPVSARPTMAALLEKIPSDYNLGNYGDKPSDNSDLKTRPTPVKGEESCGKMPADWRQQLLRHIEARRLDRNAAYKHNTVNLGMLPYGGISAMHAGRSMTLNLQTKSKFDHQELPLQKTPSQQSNILDNGQEDVSPSGQWNPYPLGRRDVPPDTITKKAGSHIQTLMGSQSLQHRSREQQPYEGNINKVTIQQFQSPLPIQIPSSQATRGPQPGRCLIQTKGQRSMDGYPEQFCVRIEKNPGLGFSISGGISGQGNPFKPSDKGIFVTRVQPDGPASNLLQPGDKILQANGHSFVHMEHEKAVLLLKSFQNTVDLVIQRELTV
Protein: Speckle-type POZ protein (HIB homolog 1) (Roadkill homolog 1) (O43791)
Organism: Homo sapiens (Human)
Function: Component of a cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex that mediates the ubiquitination of target proteins, leading most often to their proteasomal degradation. In complex with CUL3, involved in ubiquitination and proteasomal degradation of BRMS1, DAXX, PDX1/IPF1, GLI2 and GLI3. In complex with CUL3, involved in ubiquitination of MACROH2A1 and BMI1; this does not lead to their proteasomal degradation. Inhibits transcriptional activation of PDX1/IPF1 targets, such as insulin, by promoting PDX1/IPF1 degradation. The cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex containing homodimeric SPOP has higher ubiquitin ligase activity than the complex that contains the heterodimer formed by SPOP and SPOPL. Involved in the regulation of bromodomain and extra-terminal motif (BET) proteins BRD2, BRD3, BRD4 stability.
Subcellular location: Nucleus {ECO:0000269|PubMed:22085717, ECO:0000269|PubMed:37622993, ECO:0000269|PubMed:38018242}. Nucleus speckle {ECO:0000269|PubMed:15897469, ECO:0000269|PubMed:9414087}. Cytoplasm {ECO:0000269|PubMed:38018242}.
Interaction partners:
- Cullin-3
- E3 ubiquitin-protein ligase RBX1
- Transcriptional activator GLI3
- Zinc finger protein GLI2
- Zinc finger protein GLI1
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Death domain-associated protein 6
- Pancreas/duodenum homeobox protein 1
- Speckle-type POZ protein-like
- Suppressor of fused homolog
Sequence:
MSRVPSPPPPAEMSSGPVAESWCYTQIKVVKFSYMWTINNFSFCREEMGEVIKSSTFSSGANDKLKWCLRVNPKGLDEESKDYLSLYLLLVSCPKSEVRAKFKFSILNAKGEETKAMESQRAYRFVQGKDWGFKKFIRRDFLLDEANGLLPDDKLTLFCEVSVVQDSVNISGQNTMNMVKVPECRLADELGGLWENSRFTDCCLCVAGQEFQAHKAILAARSPVFSAMFEHEMEESKKNRVEINDVEPEVFKEMMCFIYTGKAPNLDKMADDLLAAADKYALERLKVMCEDALCSNLSVENAAEILILADLHSADQLKTQAVDFINYHASDVLETSGWKSMVVSHPHLVAEAYRSLASAQCPFLGPPRKRLKQS
Protein: Karyopherin subunit alpha 1 (C9JWD9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTTPGKENFRLKSYKNKSLNPDEMRRRREEEGLQLRKQKREEQLFKRRNVATAEEETEEEVMSDGGFHEAQISNMEMAPGGVITSDMIEMIFSKSPEQQLSATQKFRKLLSKEPNPPIDEVISTPGVVARFVEFLKRKENCTLQFESAWVLTNIASGNSLQTRIVIQAGAVPIF
Protein: Telomere repeat-binding protein 1 (AtTRP1) (Q8L7L8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Binds specifically to the plant telomeric double-stranded DNA sequences 5'-GGTTTAG-3'. At least 4 repeats of telomeric sequences are required for binding. Induces DNA bending.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Telomere repeat-binding factor 1
- Ethylene response sensor 1
- Protection of telomeres protein 1b
- ATP-dependent DNA helicase 2 subunit KU70
- Protection of telomeres protein 1a
- Telomerase reverse transcriptase
- Telomere repeat-binding factor 3
- Telomere repeat-binding factor 2
- CST complex subunit STN1
- CST complex subunit TEN1
Sequence:
MVSHKCVEEFGYASYLVPSNARAPRSARKRRSIEKRISKEDDNMCAIDLLATVAGHLSFESGSSLMSIDKLIEDHRVKEEFPEEEKPLMPVALSPYRGSLSPCGFSSVINGKVENEVDGFSYSGGSDACQVGNFSQDVKPDIDGDAVVLDARPNVVVSLGSSSRTEVPSIGNCVSHGVRDDVNLFSRDDDENFSKYIHPRVTKHSPRTVPRIGDRRIRKILASRHWKGGSRHSDTKPWRNYYLHQQRSYPIKKRKNFDHISDSVTDDYRMRTKMHRGSRKGQGASFVASDSHVKLRIKSFRVPELFIEIPETATVGSLKRMVMEAVSTLLSDGHRVGLMVQGKKVRDDNKTLHQTGISQDNSHLDSLDFSLEPSSEMPQLLTSHPLGHACEELLPVCQATKIDNVLESDHHDSALFPSDSLGNNNVTEDSKAMISVALNELSSQSQPPSRKSRRSEQQQQQAAQRRIRRPFSVAEVEALVQAVEKLGTGRWRDVKLCAFEDADHRTYVDLKDKWKTLVHTAKISPQQRRGEPVPQELLNRVLNAHGYWTQQQMQQLQQNVNKLEQETQSQTTEGLLLL
Protein: Protein EFR3 homolog A (Protein EFR3-like) (Q14156)
Organism: Homo sapiens (Human)
Function: Component of a complex required to localize phosphatidylinositol 4-kinase (PI4K) to the plasma membrane. The complex acts as a regulator of phosphatidylinositol 4-phosphate (PtdIns(4)P) synthesis (Probable). In the complex, EFR3A probably acts as the membrane-anchoring component. Also involved in responsiveness to G-protein-coupled receptors; it is however unclear whether this role is direct or indirect.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:25380825}; Lipid-anchor {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:25380825}. Cytoplasm, cytosol {ECO:0000269|PubMed:25380825}. Note=Palmitoylation anchors the protein to the plasma membrane (PubMed:23229899, PubMed:25380825, PubMed:26571211). A small amount is observed in the cytosol (PubMed:25380825). {ECO:0000269|PubMed:23229899, ECO:0000269|PubMed:25380825, ECO:0000269|PubMed:26571211}.
Interaction partners:
- Tetratricopeptide repeat protein 7A
- Phosphatidylinositol 4-kinase alpha
- Tetratricopeptide repeat protein 7B
- Hyccin
Sequence:
MPTRVCCCCSALRPRYKRLVDNIFPEDPKDGLVKTDMEKLTFYAVSAPEKLDRIGSYLAERLSRDVVRHRSGYVLIAMEALDQLLMACHSQSIKPFVESFLHMVAKLLESGEPKLQVLGTNSFVKFANIEEDTPSYHRRYDFFVSRFSAMCHSCHSDPEIRTEIRIAGIRGIQGVVRKTVNDELRATIWEPQHMDKIVPSLLFNMQKIEEVDSRIGPPSSPSATDKEENPAVLAENCFRELLGRATFGNMNNAVRPVFAHLDHHKLWDPNEFAVHCFKIIMYSIQAQYSHHVIQEILGHLDARKKDAPRVRAGIIQVLLEAVAIAAKGSIGPTVLEVFNTLLKHLRLSVEFEANDLQGGSVGSVNLNTSSKDNDEKIVQNAIIQTIGFFGSNLPDYQRSEIMMFIMGKVPVFGTSTHTLDISQLGDLGTRRIQIMLLRSLLMVTSGYKAKTIVTALPGSFLDPLLSPSLMEDYELRQLVLEVMHNLMDRHDNRAKLRGIRIIPDVADLKIKREKICRQDTSFMKKNGQQLYRHIYLGCKEEDNVQKNYELLYTSLALITIELANEEVVIDLIRLAIALQDSAIINEDNLPMFHRCGIMALVAAYLNFVSQMIAVPAFCQHVSKVIEIRTMEAPYFLPEHIFRDKCMLPKSLEKHEKDLYFLTNKIAESLGGSGYSVERLSVPYVPQVTDEDRLSRRKSIVDTVSIQVDILSNNVPSDDVVSNTEEITFEALKKAIDTSGMEEQEKEKRRLVIEKFQKAPFEEIAAQCESKANLLHDRLAQILELTIRPPPSPSGTLTITSGHAQYQSVPVYEMKFPDLCVY
Protein: Sperm protamine P1 (Cysteine-rich protamine) (P04101)
Organism: Sus scrofa (Pig)
Function: Protamines substitute for histones in the chromatin of sperm during the haploid phase of spermatogenesis. They compact sperm DNA into a highly condensed, stable and inactive complex.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Protamine-2
Sequence:
MARYRCCRSHSRSRCRPRRRRCRRRRRRCCPRRRRAVCCRRYTVIRCRRC
Protein: Cell wall alpha-1,3-glucan synthase mok13 (EC 2.4.1.183) (Q9Y719)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MRNKNILVLNLILSIPRLVFTAKYDERESLWNLNQNQSATDPLDYWGKWENHQYHPSPDDWQVPFYTVILDKWKDGDPRNNEANNTIYEYDIYETGFRNGGDIIGLKDSLDYLEIMGIKVIYIAGTPFLNQPWGADQYSPLDYTILDHHSGTIAQWRDTIEEIHRRGFYLVLDLTISTLGDLIGFRKYLNSTTPFSLFEHEAVWKSNVIYPDWNFTNKYDPKCELPRFWGEDGAPVVIDYVGCYDSDFDQYGDTEAFGTHPDWERQLSKFASVQDRLREWRPSVSEKLKHFACMIIAMLDVDGFRIDKATQITVDFLASWAHSVRGCAATFNKKNFFIPGEVTGSSSYGSIYYGRGRQPDQRPPSILTSLNSSSLKENYFLREPKANALDASAFHYSLYRAMTRFLQMDGDLQVGHDLPVDFTDLWNAMAVNEDFYNPNTHKVDPRHMLGITNHDVFRWSAIEFGLERLLLGTMITYFLFPGAPSIYYGDEQGFYVLDNTANNYLYGRQAMPSSIAWKVHGCYALASDQYPELPVIKAYQGCNDDWNIMDHFDFAKPELKMFKIFNFIREQYPALKSGWKSVKLRNWTEYVHFPNSGKTPTEVGVWSIVRGALETLQNFDARNNTAWNGDIWILYTNQNRTTTLDYQCSSSNSVVSPYASGLTLKNLIYPFEEYILQESNKYSSNLKSYYGCIPNIEFPPWGFKILIPKKYYVRYPPQITSFNPQHDSRIYNHNGKQKLVISFTETMDCNEITSKLQFSSKTESGKVMKVDKETVKCSVSNNSADSYYFGLAPARFHWSGDLINIADGIHEIKLQRVHSQDHQSMSDSMYKLLLRFGKLDNPMVFSTANRSSSILSQENEKLYINHKAPGADLFRFSFDYGLHWSEWIDYLSNKTECTEFANNISLKTWKGHHVIVQYWSRLTASANYIQEGGLGSLSSFPHLYMNGPYNQWGFDSGIPNRLIYKNCSWHKTFISDVFPTKFQFNVYNFDESGMPDQKKVYGTIGNSTVLVRLPPSELKESVTWIKEAPPSNFLTWEIIISDLTRTYHLIPRGSSTVSIILFSLFLVSPLICALATMLAFQKFFYQVRLNKGIEKKQEWKEKLLGPFSRISQSNINQGFSHQVALNNSVKSVHPKISRKLILVATLEYDIPDWDIKIKIGGLGVMAELMGKHLTHHDLIWVVPRVGDVNYPDGQELAPLEVVVLDQVYEVRVYSHNLRNITYILLEAPVFRKQTSAEPYPARMDDLSSAIFYSAWNQCIAGIIRRYPIDVYHINDYHGALAPCYLLPNVIPCVLSLHNAEFQGLWPLRTQAEKNEVCAVYNISTKICTKYIQFGNVFNLLHAGVSYIRIHQKGYGVVGVSNKYGKRSKARYPIFWGLKKVGKLPNPDPLDTAQLDDPTNITEEITIDLTAEAEKRAFKRDAQKWTNLELDDSADLLVFVGRWSMQKGIDLIADIAPTLLQDFNAQLITIGPIIDLYGKFAAEKLNALMKKYPKRVYCRPEFTHLPPCIFSGADFVLIPSRDEPFGLVAVEFGRKGALGIGARVGGLGQMPGWWYSVESNATSHVLQQFEEACRKALSSSAEKRALLRAKSAKQRFPVLEWISKLDHLMDNCIRLNVGQRQQGSSSHSMKFRSKNDLSSIKLSTKEGLENEENELKDKAPPNEPNVGSLFLFNKSSMGSVGGPGHYKATDLSQELETNDQDIEYNEFYSQLDTSTSDIFQDTSVDGFPDLQVSSDINVRNDRLSSFVMSSEDLRSSDGHPENSDSVLETISSVHHRSPINQVVRNLNESQLSLDSVISMNLNKEFALTKTENDFTDDNGRALNYFSQKLEELDPKNSVNELCIETFILKMKKEWYDGLRNIRFGIQRPNLLIYDEDKKFINTEHFLGSKVNLNSVTSLGNFNGSSPNSFLFLLKNRTMRIKCFMQMRIGDWPVYSIFLSVGQILAATSYQLVLLSGSSAQFSTQLYIVGSIYTVSSVFWWYLYRMLPSVASLSLPFLLYCASFLLIGISSFINENMYLRLWISHIASWIYAVASASGSLYFSLNFGDEAGAGVVSWIVRACIVQGFQQIWACCLWYWGSYIDRSMQECHSFPHEVYPLGLIAVFSWPLALVMLLFAILLIFGLPDYYWESPGNIPAFYTALLRRKLVLWFFVATILQNYWLSTLYGRSWKYLWGGSLLAPWKMLTIAFFLFLSMWIIMLMFLGRKSLTHSWLLPVFGVGLGSPRWLQMMWGTSNIGVYLPWAGVAGPIVGRILWIWLGVLDSVQGVGVGMILLQTLTRRHIATTLIAGQIIGTLTSMLARATAPNRLGPGLVFLDLTSWRFEDGAKIFRSAPFWICLISQIAVSAGYLLFFRRENLSRP
Protein: aspartate carbamoyltransferase (EC 2.1.3.2) (Q57U84)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Carbamoyl phosphate synthase arginine-specific large chain
- Dihydroorotase, putative
- Adenylosuccinate synthetase
- Orotidine 5'-phosphate decarboxylase
- Asparagine synthetase a, putative
- aspartate transaminase
- Aspartate aminotransferase
- Dihydroorotate dehydrogenase
- Predicted S. cerevisiae Got1 homologue
- Nitrate reductase, putative
Sequence:
MAELQPVTSLKGKSIITAAQFTRPDIDALIRLATALKEKICAGEVLRFLEGRIMTPLFFEDSSRTLNSFCAAMARLGGRVVYFKAETSSVNKGETLGDTVRTLDSYSDVLVLRHPKQEAITEAVAKATHPVLNAGNGAGEHPTQALLDVLTIHSELGRVDGSTIAMIGDLKMGRTVHSLLKLLVRNFKMKTIFFVAPDALQMPQDVVDSLKQEIAASGVTIRSSNSLTEEILGQCDVLYATRLQKERFAAAALDEAKALQAFEAAKADIVINAERMKKAKAKMIVMHPLPRNDELCTSVDEDPRAAYFRQMQYGMYMRMAILYSVLA
Protein: Alpha-lactalbumin (Lactose synthase B protein) (P29752)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
Subcellular location: Secreted.
Interaction partners:
- Beta-1,4-galactosyltransferase 1
- Lactotransferrin
- Albumin
- Beta-1,4-galactosyltransferase 2
- Alpha-S1-casein
- Beta-casein
- UDP-glucose 4-epimerase
- Lactoperoxidase
- Kappa-casein
- Lactase/phlorizin hydrolase
Sequence:
MMHFVPLFLVCILSLPAFQATELTKCKVSHAIKDIDGYQGISLLEWACVLFHTSGYDTQAVVNDNGSTEYGLFQISDRFWCKSSEFPESENICGISCDKLLDDELDDDIACAKKILAIKGIDYWKAYKPMCSEKLEQWRCEKP
Protein: Proteoglycan Cow (Carrier of wingless) (Carrier of wg) (Q9VCR3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Binds to the Wnt signaling protein wg, stabilizes it and promotes its extracellular distribution. This is required for establishment of a wg gradient during development to allow for regulation of target genes at different levels.
Subcellular location: Secreted {ECO:0000269|PubMed:25360738}.
Interaction partners:
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL15
- Large ribosomal subunit protein eL38
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein eL21
- Large ribosomal subunit protein eL19
- Small ribosomal subunit protein eS26
Sequence:
MKHSPLIASACLALVLMSSSLIGSTEARNKKKYVGETGGDFEFIDEINKNTQSNKNLGEHKRWIHDPSSDLCRPLNCKKREICLLEDEFSAVCVSKKELHKNRDEIITKAKYLEEEAKRRVNQQDNQDSQDAEDINNDDEDNSSDGGSSNSSPTGTNNAQASVQGNEETDDEDKSLSLGDDDESKEDDVFYENSIAAGDKQQQQQQLSQPAAGPSVIQQDDDEELDNCKPCPVAKPTFLCGADNRTYSSLCRLDYHNCIHSTSIRIACKGFCPCKEIVDGKRLQRISGYNNKYNKKISLDQQQQQQQQQQQQQQQQQAYKDSNNNNIMMNSGNIMGGNNNDFNTIMNDKEDNNRHNNHINAQYTFTPEEIKYDNKHYKYLKYTAYKKDSKYQEDKHKMRNYNEVVEKQQQKFNKNSNLNAYPSKSAECKPQQLTAIGNRLLDWFSVIMADSKKRRQHSQKSKAHFPPACKTEAKWMFGHLDLNNDGQLSLQEMYDLEHDQNERCIKPFIDTCDLDTDSSINTREWCRCFEKTDRPCAAVRRRIAGDFAGAYAPDCDIQGFYKPTQCHNSVGVCWCVDKHGVEFANTRTRGKPNCESVVNNAASLTSDDEDEGADDEDSAEGSADQMLVF
Protein: Cytochrome c peroxidase, mitochondrial (CCP) (EC 1.11.1.5) (Q5AEN1)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Destroys radicals which are normally produced within the cells and which are toxic to biological systems.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P00431}. Mitochondrion intermembrane space {ECO:0000250|UniProtKB:P00431}.
Interaction partners:
- Cytochrome c
Sequence:
MATFAPHISKITKSSTKFNYGRIAKTFLGVAGSAAIATYFYNNGNPFNNNNNNNNNNGGSKNAAKALFGASAGANVKIAKVPEGKSASDYQKVYNDIATKISENLEFDENAGYYGQLLRLAWHTSGTYDKSDNSGGSYGGTMIFAPEEFDPENAGLQVGREFLMEFLVKYPWISRGDLWTLGGVAAVQESGGPKIEWRPGRVDDNTASKVPPNGRLPDASKDGKYVKDLFARMGFNERETVALLGAHVLGRCHKHNSGYDGPWGPSFNQFTNVFYTTLLGDWHVKKWDGKKQYEDDETGEFMMLPTDMALKEESYFLKYVKMYADDQDLFFKDFAKAFSKLISNGIKYPADSKPILFKTLDEQDEE
Protein: Transcriptional regulator RPN4 (Q59VM4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Transcriptional activator of a number of genes encoding proteasomal subunits. Binds to the DNA sequence 5'-GAAGGCAAAA-3', enriched in regions upstream of proteasome genes.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MTSLAILPQLKRTITDIMDEELYQSPSSPNSMTSFPSGTGNLMSNTNHNTFNQSNNTPFNMNYNHISNRNSINSSPNLSATTFNNANNLGNVLNIPDSFLEQLASQDYIDHLKSQQQQEQAFENPDDIYVQDVHENQVNPFNDYGNPDSFIRAQEQQSQLPQPQQPISQQDKQRPQSQQQQATKAPLPQAFPTRRRRKITLLNDIGGSSTRKKHFDEDYLLYNPDISPGHIVTDCSLDSSLVIPPNSNELFLTESESPEFANDIIPGYENDYLFLDDDDEQIEEDVSDDEGDNYFQVDEDFDDYLMNNNGYDGYPTFNNYESSGNNTDIINNNNNIVDETISDANSNSELEVVFDQPKEVSPSAISPASPDSDDMMIDVEDETEIADATAAKEEINKKHSKSGKKESKSQKENQLTTTTKSKKHSHGISGAEITLNNPNHQCNLINPSTGEPCNKQFSRPYDLIRHQDTIHASMKKIFRCVICEGRLNGGPGNGKEKTFSRGDALSRHIKIKHGLVGQDALDLINEAKENVEYIPV
Protein: E3 ubiquitin-protein ligase Praja-2 (Praja2) (EC 2.3.2.27) (RING finger protein 131) (RING-type E3 ubiquitin transferase Praja-2) (Q80U04)
Organism: Mus musculus (Mouse)
Function: Has E2-dependent E3 ubiquitin-protein ligase activity. Responsible for ubiquitination of cAMP-dependent protein kinase type I and type II-alpha/beta regulatory subunits and for targeting them for proteasomal degradation. Essential for PKA-mediated long-term memory processes. Through the ubiquitination of MFHAS1, positively regulates the TLR2 signaling pathway that leads to the activation of the downstream p38 and JNK MAP kinases and promotes the polarization of macrophages toward the pro-inflammatory M1 phenotype. Plays a role in ciliogenesis by ubiquitinating OFD1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O43164}. Cell membrane {ECO:0000250|UniProtKB:O43164}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43164}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43164}. Golgi apparatus membrane {ECO:0000250|UniProtKB:O43164}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43164}. Synapse {ECO:0000250|UniProtKB:Q63364}. Postsynaptic density {ECO:0000250|UniProtKB:Q63364}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:O43164}. Note=Localizes at the cytoplasmic side of endoplasmic reticulum and Golgi apparatus (By similarity). Expressed in the postsynaptic density region of synapses (By similarity). Colocalizes with PRKAR2A and PRKAR2B in the cytoplasm and the cell membrane (By similarity). {ECO:0000250|UniProtKB:O43164, ECO:0000250|UniProtKB:Q63364}.
Interaction partners:
Sequence:
MSQYTEKEPSVMDQESSKAAWPKPAGGYQTITGRRYGRRHAYVSFKPCMTRHERSLGRAGDDYEVLELDDVPKENTSGSSSLDQVHPALPNEPTVEKSETEISTCGPALNQSTESSPSIATVCHSEEVRETLESNTNLHNRTETEHTPAVCNVSSVQNGIMLVHTDSYDPDSKHDENGSLQLGAEAVEGGRHQKGLGRAVFELENGEAEIYADLSPSVPSLNGEISEAFEELDSAPLEKSSTADAELVHQNGQEFQRSSEDGVVRKRRQDDTDQGRQTENSTEDADCAPGHVEQNTSDRANHHGSSPEQVVRPKVRKVISSSQVDQEIGFNRHEAKQRSVQRWREALEVEECSSDDPIIKCDDYDGDHDCMFLTPTYSRVTQRETERNRVTSENGATASGRQESRDNAFWNACGEYYQLFDKDEDSSECSDGEWSASLPHRFSGTEKDQSSSDDSWETLPGKDENDPELQSDSSGPEEENQELSLQEGEQTSLEEGEIPWLQYNEVNESSSDEGNEPANEFAQPEAFMLDGNNNLEDDSSVSEDLDVDWSLFDGFADGLGVAEAISYVDPQFLTYMALEERLAQAMETALAHLESLAVDVEVANPPASKESIDGLPETLVLEDHTAIGQEQCCPICCSEYIKDDIATELPCHHFFHKPCVSIWLQKSGTCPVCRRHFPPAVIDASAAASSDPDPDASPANDNAEEAP