wanglab/gogpt-training-data huggingface dataset:
Protein: Capsid protein (Core antigen) (Core protein) (HBcAg) (p21.5) (Q2I360)
Organism: Hepatitis B virus (HBV)
Subcellular location: Virion {ECO:0000256|HAMAP-Rule:MF_04076}. Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04076}.
Interaction partners:
Sequence:
MDIDPYKEFGASVELLSFLPSDFYPSVRDLLDTASALFREALESPEHCSPHHTALRQAILCWGDLMTLATWVGANLEDPASRDLVVSYVNTNIALKFRQLLWFHISCLTFGREVVVEYLVSFGVWIRTPPAYRPPNAPILSTLPETTVVRRRGRSPRRRTPSPRRRRAQSPRRRRSKSRESQC
Protein: DnaJ homolog subfamily A member 1 (DnaJ-like protein 1) (Heat shock protein J2) (HSJ-2) (P63036)
Organism: Rattus norvegicus (Rat)
Function: Functions as co-chaperone for HSPA1B and negatively regulates the translocation of BAX from the cytosol to mitochondria in response to cellular stress, thereby protecting cells against apoptosis. Promotes apoptosis in response to cellular stress mediated by exposure to anisomycin or UV. Stimulates ATP hydrolysis, but not the folding of unfolded proteins mediated by HSPA1A (in vitro) (By similarity). Co-chaperone for HSPA8/Hsc70. Plays a role in protein transport into mitochondria via its role as co-chaperone.
Subcellular location: Membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:10816573}. Microsome {ECO:0000269|PubMed:10816573}. Mitochondrion {ECO:0000269|PubMed:10816573}. Nucleus {ECO:0000269|PubMed:10816573}. Cytoplasm, perinuclear region {ECO:0000250}. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Endoplasmic reticulum chaperone BiP
- Heat shock 70 kDa protein 4
- Heat shock 70 kDa protein 1A
- Heat shock cognate 71 kDa protein
- Heat shock 70 kDa protein 1-like
- Heat shock protein 105 kDa
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- DnaJ heat shock protein family
Sequence:
MVKETTYYDVLGVKPNATQEELKKAYRKLALKYHPDKNPNEGEKFKQISQAYEVLADSKKRELYDKGGEQAIKEGGAGGGFGSPMDIFDMFFGGGGRMQRERRGKNVVHQLSVTLEDLYNGATRKLALQKNVICDKCEGRGGKKGAVECCPNCRGTGMQIRIHQIGPGMVQQIQSVCMECQGHGERISPKDRCKSCNGRKIVREKKILEVHIDKGMKDGQKITFHGEGDQEPGLEPGDIIIVLDQKDHAVFTRRGEDLFMCMDIQLVEALCGFQKPISTLDNRTIVITSHPGQIVKHGDIKCVLNEGMPIYRRPYEKGRLIIEFKVNFPENGFLSPDKLSLLEKLLPERKEVEETDEMDQVELVDFDPNQERRRHYNGEAYEDDEHHPRGGVQCQTS
Protein: Somatotropin (Growth hormone) (P34746)
Organism: Oreochromis mossambicus (Mozambique tilapia) (Tilapia mossambica)
Function: Growth hormone plays an important role in growth control and involved in the regulation of several anabolic processes.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MNSVVLQLSVVCLGVSSQQITDSQRLFSIAVNRVTHLYLLAQRLFSDFESSLQTEEQRQLNKIFLQDFCNSDYIISPIDKHETQRSSVLKLLSISYGLVESWEFPSRSLSGGSSLRNQISPRLSELKTGILLLIRANQDEAENYPDTDTLQHAPYGNYYQSLGGNESLRQTYELLACFKKDMHKVETYLTVAKCRLSPEANCTL
Protein: Glyceraldehyde-3-phosphate dehydrogenase 2, cytosolic (EC 1.2.1.12) (Q09054)
Organism: Zea mays (Maize)
Function: Key enzyme in glycolysis that catalyzes the first step of the pathway by converting D-glyceraldehyde 3-phosphate (G3P) into 3-phospho-D-glyceroyl phosphate. Essential for the maintenance of cellular ATP levels and carbohydrate metabolism (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- transketolase
- transketolase
- Phosphoglycerate kinase
- Phosphoglycerate kinase
- phosphoglycerate kinase
- Glucose-6-phosphate isomerase, cytosolic
- Phosphoglycerate kinase
- Triosephosphate isomerase, cytosolic
- transaldolase
- Glucose-6-phosphate isomerase
Sequence:
MGKIKIGINGFGRIGRLVARVALQSEDVELVAVNDPFITTDYMTYMFKYDTVHGQWKHSDIALKDSKTLLFGEKPVTVFGIRNPEEIPWGEAGAEYVVESTGVFTDKDKAAAHLKGGAKKVVISAPSKDAPMFVVGVNEDKYTSDVNIVSNASCTTNCLAPLAKVIHDNFGIIEGLMTTVHAITATQKTVDGPSAKDWRGGRAASFNIIPSSTGAAKAVGKVLPELNGKLTGMSFRVPTVDVSVVDLTVRIEKGASYEEIKKAIKAASEGPLKGIMGYVEEDLVSTDFTGDSRSSIFDAKAGIALNDHFIKLVSWYDNEWGYSNRVVDLIRHMFKTQ
Protein: C-reactive protein [Cleaved into: C-reactive protein(1-205)] (P02741)
Organism: Homo sapiens (Human)
Function: Displays several functions associated with host defense: it promotes agglutination, bacterial capsular swelling, phagocytosis and complement fixation through its calcium-dependent binding to phosphorylcholine. Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells.
Subcellular location: Secreted.
Interaction partners:
- Complement factor H
- Low affinity immunoglobulin gamma Fc region receptor II-a
- Complement factor H-related protein 4
- Complement C3
- Interleukin-6
- Oxidized low-density lipoprotein receptor 1
- Tumor necrosis factor
- Albumin
- Alanine aminotransferase 1
- Leptin
Sequence:
MEKLLCFLVLTSLSHAFGQTDMSRKAFVFPKESDTSYVSLKAPLTKPLKAFTVCLHFYTELSSTRGYSIFSYATKRQDNEILIFWSKDIGYSFTVGGSEILFEVPEVTVAPVHICTSWESASGIVEFWVDGKPRVRKSLKKGYTVGAEASIILGQEQDSFGGNFEGSQSLVGDIGNVNMWDFVLSPDEINTIYLGGPFSPNVLNWRALKYEVQGEVFTKPQLWP
Protein: Mitochondrial 3' processome subunit 1 (A0A120KVR8)
Organism: Trypanosoma brucei brucei
Function: As part of the mitochondrial 3' processome (MPsome), involved in the maturation of guided RNA (gRNA) precursors.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:26833087}.
Interaction partners:
Sequence:
MRRLILSQTLRVAGRHRPPVAMFLQRFYRGHGISTALPLHYSKRHRKREGRMYGKPLRPVSDGENGASGDGGVLTRWEAVVSSRHQCESPVQTLAKSEKPKKAENTVAGKMTGSSRFSHRRDHSAYPSGVQPAPLATSGLPTQSSERQQQKQIGQQQVPLDALHRLFKVHAVMRTNYEALGKCTKVLKSFSTACAEALLQLGVLQKEQPSAMERKGFIDVQLCKSRVTEASKNGTSSPCFVLPPESPLYRTTIKFPTITVEHVLTTTVPAGCGAKDSGGDIMSVDMEGAAPFPMGHCESRPSTSAGNGVTVEYDCEGDVLSHGAAWNSIIEGFGQLALNLKQNASVSDFAQLAETLAYFKWVKDEEQVGWGTEDCVVKKFREAMANAKDTSASGSDPNTSDVSAALAAIAESFLRKIPRVDCIGSAVVHRGGERTAPSVHAIDVMLNLALRMCLSQWHAMSHFERMNIVLFCTYPWFAEDLSIAAGLCLTQSYLQSLLRADADVTYQHTFHYVRRVSRLCWPCIHDTDSAPVKKLLFPRDPQGTAVSSHALEAVSVEEKDNQLNQKEGLQGEEQATTTSESKLMWLPSFKDASCVSYGSSMKQRAAYELLLLWMTCVNPSGLHRSSPHGRYVSATGIAIIDVDLFVTQRFRTGKSKDEWLLLHPVEGDVVASVTIRTMVQHCETPYALTRLFFCNFHSVLPHIWGGIGARRREIIWTAWCRAVAQPLVNTLSGSDEGQREDDGGMQTLQITVDNADRTLDYLKPLISALTSDELFLRLIMRCADKSLEEMACEIGSGNNTLPLSKWCAQLAGFVYSVAFALHCRAKREGCNRDGGPSRPNTATDSANKKVVSGKQTDNLPKGTQEDISDLQLQFKAAVSALLRKLSAGDTQVAEQLLHHFYEPHFSGDQEREVVEDIQRHLQQVCDSQSRDALHAWIECSARASCEATVPLKEELLCKWQRTVLEADAGLPVVLPTIVECCRGLVGLVKKRGRNISGRRQGQQRGTESTTVGEESSCKEVFSKEELPVVITVLSRAMLTRTSTVSTVGLTKISSEISTLLSSCGYETADGNTSGGGRNGRELCDTNTATITSATAGERTVELELILSGEIDQKAGELPWITILEAVQLQLVPYTVVKNLLTSFKGGCDNGKERLRWQELQRDFQRKRHHRLVGNTLVFRWYGCAVPNDEGWEDGSGLMRPMAEDRDNVHSASHQGRTSTELGAFTRRLLKTLARAEVTRLDDRKEITTQTFVVGPSDDSATRHPTPGQEEDANLQRLDLLFRVHTLAAHILMTASTKKPHMIHELYDTLLHLVERVMPTTPNAPGNASDLLLLWLVGSAVAVGLRFRPNFLIKWPSTPEVSSGNLKSCPSAEEKTVHILRDIEPYLQSELLRPTVRLRFVINVLVALRSLELLGARIDVEGLHMDQLLVRASADRRLLSRHVNLFLIGCSALQSTQSSILHTALHLREAKYNLSFAEIERAFVAIALSADTFARQHEALMEQNYQQQQNRTLSVTVAANNTTPALRVSPVQLRHAWSALGRRVLENAGESPTDLFVRGLQCAAAVGCIDSALYQQLLSYVVEFRWEDLHILDWVMILRTVRQSFENRRNLEAYLKEPLQAFMLTMTDSGDNSTEQSVQKVNLKNHEGEQLLEGLCLFAEALPGLFIGDRELWGLLWQALGSQWSACFNAASNIEEQQRITAWLQEINASYAWAARAAGFRGLDEPTAL
Protein: Laminin subunit gamma 2 (F1LRH4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
- Laminin subunit beta-3
- Laminin subunit alpha 3
- Laminin subunit alpha-5
- Laminin subunit beta-1
- CD44 antigen
- Integrin beta-4
- Laminin subunit gamma-1
- Laminin subunit beta-2
- Integrin subunit alpha 5
- Integrin alpha-6
Sequence:
MPALWLSCCLGVALLLPAAQATSRREVCDCNGKSRQCVFDQELHRQTGNGFRCLNCNDNTAGVHCERCREGFYRQRDRDRCLPCNCHSKGSLGAGCDNSGQCRCKPGVVGQRCDRCQPGFHMLTDAGCTRDQRQLDSKCDCDPAGISGPCDSGRCVCKPAVTGERCDRCRAGYYHLDRANPEGCTQCFCYGHSDSCHTSADFSVHKITSTFNQDEDGWKAVQRNWAPAKLHWSPRHQDVFSSARRSDPVYFVAPAKFLGNQQVSYGQSLSFDYRVDRGGRHPSAYDVILEGAGLQIRAPLMPPGKTLPCGITKTYTFRLNEHPSSHWSPQLSYFEYRRLLRNLTALLIRATYGEYSTGYIDNVTLISARPVSGAPAPWVERCVCPAGYKGQFCQECASGYKRDSARLGPFGTCVPCNCQGGGACDPDTGDCYSGDENPDIECADCPIGFYNDPHDPRSCKPCPCHNGFSCSVMPETEEVVCNNCPPGVTGARCELCADGFFGDPFGERGPVRPCQRCQCNNNVDPSASGNCDQLTGRCLKCIYNTAGIYCDQCKAGYFGDPLAPNPADKCRACNCNPVGSEPGECRSDGSCVCKPGFGGLNCAHAAALTSCPACYNQVKTQMDQFAQQLQNLEALVSKAQGGNGAVPSEELEGRMQQAEQALRDILREAQISEGAMRALSLQLAKARSQENNYKNRLDDLKMTVERIRALGSQYQNRVQDTSRLISQMRLSLAESEASLQNTNIHSSEHYVGPNGFKSLAQEAARLADSHVESANTMKQLTRETEDYSKQALSLARKALSGGGGSGVLDSSVVQGLMGKLEKTKSLTQQLSREGTQADIEADRSYQHSLRLLDSASQLQGIRDSSFQAEAKRIRQKADSLSNLVTKQMDAFTSVRNNLGNWEKETRQLLQTGKDRRQTSDQLLSRANLAKSRAQEALSMGNATFYEVENILKNLREFDLQVEDRKAEAEEAMKRLSYISQKVADASDKTQQAETALGSATADTQRAKNAATEALEITSEIEQEIGSLNLEANVTADGALAMEKGLATLKSEMREVEGELARKELEFHTDKDSLQLVITEAQQADARAKSTGVTIQDTLNTLEGILRLIDQPDAVDEEGLMLLEQELFQAKTQINSRLRPLMSELEDRARRQSNHLHLLETSIDGILADVKNLENIRDNLPPGCYNTQALEQQ
Protein: Solute carrier family 2, facilitated glucose transporter member 3 (CEF-GT3) (Glucose transporter type 3) (GLUT-3) (P28568)
Organism: Gallus gallus (Chicken)
Function: Facilitative glucose transporter that can also mediate the uptake of various other monosaccharides across the cell membrane. Mediates the uptake of glucose, 2-deoxyglucose, galactose, mannose, xylose and fucose, and probably also dehydroascorbate. Does not mediate fructose transport.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P11169}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P11169}. Perikaryon {ECO:0000250|UniProtKB:Q07647}. Cell projection {ECO:0000250|UniProtKB:Q07647}. Note=Localized to densely spaced patches along neuronal processes. {ECO:0000250|UniProtKB:Q07647}.
Interaction partners:
- Monocarboxylate transporter 4
- Uncharacterized protein.
- L-lactate dehydrogenase A chain
- Uncharacterized protein.
- Hexokinase domain containing 1.
Sequence:
MADKKKITASLIYAVSVAAIGSLQFGYNTGVINAPEKIIQAFYNRTLSQRSGETISPELLTSLWSLSVAIFSVGGMIGSFSVSLFFNRFGRRNSMLLVNVLAFAGGALMALSKIAKAVEMLIIGRFIIGLFCGLCTGFVPMYISEVSPTSLRGAFGTLNQLGIVVGILVAQIFGLEGIMGTEALWPLLLGFTIVPAVLQCVALLFCPESPRFLLINKMEEEKAQTVLQKLRGTQDVSQDISEMKEESAKMSQEKKATVLELFRSPNYRQPIIISITLQLSQQLSGINAVFYYSTGIFERAGITQPVYATIGAGVVNTVFTVVSLFLVERAGRRTLHLVGLGGMAVCAAVMTIALALKEKWIRYISIVATFGFVALFEIGPGPIPWFIVAELFSQGPRPAAMAVAGCSNWTSNFLVGMLFPYAEKLCGPYVFLIFLVFLLIFFIFTYFKVPETKGRTFEDISRGFEEQVETSSPSSPPIEKNPMVEMNSIEPDKEVA
Protein: Calreticulin (CRP55) (Calregulin) (Endoplasmic reticulum resident protein 60) (ERp60) (HACBP) (P14211)
Organism: Mus musculus (Mouse)
Function: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export (By similarity). Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity). Present in the cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation and might participate in the block to polyspermy (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:8418194}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P27797}. Cytolytic granule {ECO:0000269|PubMed:8418194}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P27797}. Cell surface {ECO:0000250|UniProtKB:P27797}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P28491}. Cytoplasmic vesicle, secretory vesicle, Cortical granule. Note=Also found in cell surface (T cells), cytosol and extracellular matrix. During oocyte maturation and after parthenogenetic activation accumulates in cortical granules. In pronuclear and early cleaved embryos localizes weakly to cytoplasm around nucleus and more strongly in the region near the cortex (By similarity). In cortical granules of non-activated oocytes, is exocytosed during the cortical reaction in response to oocyte activation (By similarity). {ECO:0000250|UniProtKB:P27797, ECO:0000250|UniProtKB:P28491, ECO:0000250|UniProtKB:Q8K3H7}.
Interaction partners:
- Tapasin
- Endoplasmin
- Protein disulfide-isomerase A3
- Beta-2-microglobulin
- Calnexin
- Endoplasmic reticulum chaperone BiP
- Prolow-density lipoprotein receptor-related protein 1
- Thrombospondin-1
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Antigen peptide transporter 2
Sequence:
MLLSVPLLLGLLGLAAADPAIYFKEQFLDGDAWTNRWVESKHKSDFGKFVLSSGKFYGDLEKDKGLQTSQDARFYALSAKFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPSGLDQKDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAAKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDANIYAYDSFAVLGLDLWQVKSGTIFDNFLITNDEAYAEEFGNETWGVTKAAEKQMKDKQDEEQRLKEEEEDKKRKEEEEAEDKEDDDDRDEDEDEEDEKEEDEEESPGQAKDEL
Protein: ERCC excision repair 3, TFIIH core complex helicase subunit (A0A2R8Y762)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XSKTGVPDGIMQFIKLCTVSYGKVKLVLKHNRYFVESCHPDVIQHLLQDPVIRECRLRNSEGEATELITETFTSKSAISKTAESSGGPSTSRVTDPQGKSDIPMDLFDFYEQMDKDEEEEEETQTVSFEVKQEMMLRQGTSFKTGAWHPCWKGIFSITFSFHLFDLPSSVGQIVLRKMHQGLGCAFIGHLGFYKGGGDNIFSNFLGSGVISVYKKC
Protein: RNA-binding protein vts1 (Q9P6R7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: RNA-binding protein involved in post-transcriptional regulation through transcript degradation.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q08831}. Cytoplasm, P-body {ECO:0000250|UniProtKB:J9VVN9}.
Interaction partners:
Sequence:
MEVVEGRRKTCLDVVDSPSSRQKQTIAVSLVDGKNYPTRFLNSRTIDKLKQELNTSNLSTGEMSTNETLKNAQEVAGKLLSEENEDSISEHFDEYLGADKPGISFLTRLKTLESWFQSLSLQDRLTTLRTLLHHLPSQEISTLLSSSLTSSPSNSGLSLDKSLPSSPKGDSPSLSSSLPSLTTKSNLSGNLNMVTPASTQGPAFSSKHGFSNALSTASPIPVRTSSVSSTYLTQDREASSKNCLSKALAFSSIEPPASSASTSPRNTPTPSNNGTSINANVTSSLTSNSTGKTSKTTDLLIAASKKSLPSNSTPSKPNTSFFETPHNNIWDSRDRGAFSAPPAPFFPLGFSPHLNDESSRSRWSNISYSPPPPPPPPELLNHSPKSRPLGDKPYLFYRNNQIGPRTRTEGRSSITEGKPFLSSSLRFEHVPSANDLNSVVNARVEKSTGQPSTPLNRQHYFNELPHSTTPVTLPSLIHGSEIDRRRSGFCLNNFNSTPPFQPYHYEIGSGLPQQMHATNTILTNPIDPNSNISTPVGMHLCTLPYTYQPFSSVEKIETPPNNSKNQTYRRSSRGSNKTRKSISHSKNTDKHVGNELPQDIPSWLRSLRLHKYTNNLKDTDWDALVSLSDLDLQNRGIMALGARRKLLKSFQEVAPLVSSKKMNENLKAAKNQSSESLTSFKGHTDSEDLPSGSMSNEISSNSTKQDVSSSSMD
Protein: At2g27290 (Expressed protein) (FAM210B-like protein, putative (DUF1279)) (Q9XIN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAMMLLQIPPSSSLLNTRNLQIRFFHSSVSASSKKFRCRAVREKAEDIDKNISPPSSSPPPPSAEEVTKKYGLEVGLWKILSSKDDEGSDGDNKKKKSKTDEAKELLAKYGGAYLATSITLSLISFSLCYVLVTSGVDVQALLLKVGISTNETGEKVGAFALAYAAHKAASPIRFPPTVALTPIVANWIGKKVDKEKDDDK
Protein: deoxyribose-phosphate aldolase (EC 4.1.2.4) (2-deoxy-D-ribose 5-phosphate aldolase) (Phosphodeoxyriboaldolase) (E9PPM8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSAHNRGTELDLSWISKIQVNHPAVLRRAEQIQARRTVKKEWQAAWLLKAVTFIDLTTLSGDDTSSNIQRLCYKAKYPIREDLLKALNMHDKGITTAAVCVYPARVCDAVKALKAAGCNIPVASVAAGFPAGQTHLKTRLEEIRLAVEDGATEIDVVINRSLVLTGQWEGSDFIKTSTGKETVNATFPVAIVMLRAIRDFFWKTGNKIGFKPAGGIRSAKDSLAWLSLVKEELGDEWLKPELFRIGASTLLSDIERQIYHHVTGRYAAYHDLPMS
Protein: Prenyl transferase paxC (EC 2.5.1.-) (Paxilline synthesis protein C) (Q9C448)
Organism: Penicillium paxilli
Function: Prenyl transferase; part of the gene cluster that mediates the biosynthesis of paxalline, a mycotoxin that acts as an inhibitor of mammalian maxi-K channels. PaxG, the geranylgeranyl diphosphate (GGPP) synthase is proposed to catalyze the first step in paxilline biosynthesis. Condensation of indole-3-glycerol phosphate with GGPP by paxC then forms 3-geranylgeranylindole (3-GGI), followed by epoxidation and cyclization of this intermediate (by paxM and paxB) to form paspaline. Paspaline is subsequently converted to 13-desoxypaxilline by paxP, the latter being then converted to paxilline by paxQ. Finally paxilline can be mono- and di-prenylated by paxD.
Interaction partners:
Sequence:
MGVAGSGVLYFLFNNVPSPRFWLKKTQLIGTENPEGITGYECPYEYLRKSYGKHHWAAFVDKLSPNLQNEDPAKYRMVLETMDVIHLCLMMVDDISDGSEYRKGKPAAHKIYGAPETANRAYYRVTQILAQTATEFPRLSPWLMTDLRDILEGQDMSLVWRRDGVNGFPGTASERTAAYKRMVLLKTGGLFRLLGHLTLENNSMDEAFSTLGWHSQLQNDCKNVYSSEYAKMKGVVAEDLLNREMTYPIVLALDASGGHWVEAALKSPSRRNVGNALKIIQCDYVRDVCMAELARSGAPVKEWLKLWKREEKLDLKA
Protein: Y-box-binding protein 2-B (Cytoplasmic RNA-binding protein p54) (Frog Y-box protein 2-B) (FRGY2b) (Messenger ribonucleoprotein particle 3) (mRNP3) (P45441)
Organism: Xenopus laevis (African clawed frog)
Function: Putative translation regulator. May be involved in the developmental translational regulation of maternal mRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1729676}. Note=Either free or associated with ribonucleoprotein particles.
Interaction partners:
Sequence:
MSEAEPRETEAVTQPEPAPEIHKPDIVPPRNQINKKLLATQVQGTVKWFNVRNGYGFINRNDSKEDVFVHQTAIKKNNPRKFLRSVGDGETVEFDVVEGEKGAEAANVTGPGGVPVKGSRFAPNRRRFRRQFYRPRADTAGESGGEGVSPEQMSEGEKGEETSPQQRPQRRRPPPFFYRRRFRRGPRPNNQQNQGAEVTDQSENKDPAAPTSEALASGDGQQRPPPRRFQQRFRRPFRPRPPPPQTPEGGDGEAKAEGEPQRQRNRPYVQRRRRQQPPTVQGESKAEPSEHPASEEGTPSDAPTDDGAPVETSEAGVEDTTAPE
Protein: NAD(+) hydrolase ApTIR (EC 3.2.2.6) (TIR domain-containing protein in actinoplanes) (ApTIR) (G8SD34)
Organism: Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110)
Function: NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide.
Subcellular location: Cell membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- WD-40 repeat-containing serine/threonine protein kinase
- Putative WD repeat-containing protein
- Putative WD repeat-containing protein
Sequence:
MRYDAFISYSHAADGALAPAVQRGLQRLARRWHRPRALEVFRDQTGLAVSHALWSSIKVALDQSEFFVLLASPEAAASPWVNQEIEHWLSRHSVDRLLPVVTSGEWVWDADAGDVDLERSTAVPPALRGVFGEEPRHLDLRWARAEHELDLRHGRFRDAIAELAAGMHGMSKEDLDGEDVIRHRQMLRMRRGALAVVCALLLLVAGTAVAWRNARGEVTATNVALQRQRAATAAEQHRTEEAADQARSQQQIVEAEQQRAQKAAEEARGQQAVAEAEQQRALRAAGEARRQEGIAAAEQRRAQKAAAEARRQRGVADAEKAKANRAAAEAERQRKIAADEQRKAHEAAAEAERQREEAVKQQRIAIGRRLLGQAGEARDRDPRTAIQLGIAARHIYPGPQSQAGLVETLVRTHYAGTVTGHTAVVSAVALSGDGRTLVTDGLDGTVMVWDPTDRAAPRRLAQLTSSTAPVYTVALSGDGRTLVTGSEDGTAMVWDLTDRAAPRRLAQLTGHTDVVDAVALSGDGRTLATGSFDGTAMVWDVTDRAAPRRLAQLTDHTAPVTAVALSGDGRTLATGSDDHTAMVWDLTDRAAPRRLAQLTGHTAGVDAVALSGDGRTLATGSYDGTAMLWDLTDRAAPRRLAQLTGHTAQVYTVALSRDGRTLATGSEDHTAMVWDLTDRAAPRRLAQLTGHTDAVDAVALSGDGRTLATAASITRRCCGM
Protein: Sodium-coupled monocarboxylate transporter 1 (Electrogenic sodium monocarboxylate cotransporter) (zSMCTe) (Sodium solute symporter family 5 member 8 protein) (Solute carrier family 5 member 8) (Q3ZMH1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as an electrogenic sodium (Na(+)) and chloride (Cl-)-dependent sodium-coupled solute transporter, including transport of monocarboxylates (short-chain fatty acids including L-lactate, D-lactate, pyruvate, acetate, propionate, valerate and butyrate), lactate, mocarboxylate drugs (nicotinate, benzoate, salicylate and 5-aminosalicylate) and ketone bodies (beta-D-hydroxybutyrate, acetoacetate and alpha-ketoisocaproate), with a Na(+):substrate stoichiometry of between 4:1 and 2:1. Catalyzes passive carrier mediated diffusion of iodide. Mediates iodide transport from the thyrocyte into the colloid lumen through the apical membrane.
Subcellular location: Apical cell membrane {ECO:0000250|UniProtKB:Q8N695}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neutral amino acid uniporter 4
Sequence:
MPGSGGPVATFSVWDYVVFAGLILVAAGIGLFQSFRGRKEASSDEFLLGGRQMTAVPVALSLTASFMSGITVIGTPAEAYLYGTPFWLFFISYAIMSTISAEIFVPLFYRLNITSTYEYLEMRYNKLIRVIGTSMYIIQTALYTGMVIFAPALALNQITGLDLWGVLVATGAVCIIYCTLGGLKAVIWTDVFQMIIMLGGFVAVIARGAVLQGGLGRVWNDSFYGGRLETFSFDPDPLRRHSFWTIVVGGSLMWASMYSINQSQVQRYISCRTMTHAKLSLYVNMVGLWVTVSLAMMSGLTMYSIYKDCDPFTNKDVGATDQLLPYLVMDILADFPGLPGLFVAAAYSGTLSTVSSSINALVAVTVEDFMKPAWPSLTERQLSWINMGMSVFYGAVCIGMAGVASMMGNILQAALSIFGMISGPLLGLYMLGMFFRCANSTGGLAGLASGLAITLWVGIGAQLYPPLPEKTLRLPLSVEGCVALNTSETTTMTPFSTVLQTTTPQPRPALADNWYSLSYLYFSPVGIVVTMIIALIVSAISGGCKQKKVRPELFISKSDLICFRCKKSDSEVSDLIETKPKDNQGLDSPVFYDNEIVLKEKDQQEKITKL
Protein: TATA-box-binding protein (TATA sequence-binding protein) (TATA-binding factor) (TATA-box factor) (Transcription initiation factor TFIID TBP subunit) (P27633)
Organism: Xenopus laevis (African clawed frog)
Function: General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Members of the TBP family are differentially required to regulate transcription and development during early embryogenesis. Binds to the promoters of select genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P20226}.
Interaction partners:
Sequence:
MDQNNSIPPFQGLASPQGSLTPGINIFSPLITYGTGLTPQPVQTTNSLSILEEQQRQQQQTQQSTLQQGNQGSGQTPQLFHPQTLTTAPLPGNTPLYPSPITPMTPISPATPASESSGIVPQLQNIVSTVNLGCKLDLKTIALRARNAEYNPKRFAAVIMRIREPRTTALIFSSGKMVCTGAKSEEQSRLAARKYARVVQKLGFPAKFLDFKIQNMVGSCDVKFPIRLEGLVLTHQQFSSYEPELFPGLIYRMIKPRIVLLIFVSGKVVLTGAKVRAEIYEAFENIYPILKGFRKTT
Protein: Hepatocyte growth factor-regulated tyrosine kinase substrate (SNAP-25-interacting protein Hrs-2) (Q9JJ50)
Organism: Rattus norvegicus (Rat)
Function: Involved in intracellular signal transduction mediated by cytokines and growth factors. When associated with STAM, it suppresses DNA signaling upon stimulation by IL-2 and GM-CSF. Could be a direct effector of PI3-kinase in vesicular pathway via early endosomes and may regulate trafficking to early and late endosomes by recruiting clathrin. May concentrate ubiquitinated receptors within clathrin-coated regions. Involved in down-regulation of receptor tyrosine kinase via multivesicular body (MVBs) when complexed with STAM (ESCRT-0 complex). The ESCRT-0 complex binds ubiquitin and acts as sorting machinery that recognizes ubiquitinated receptors and transfers them to further sequential lysosomal sorting/trafficking processes. Involved in receptor recycling via its association with the CART complex, a multiprotein complex required for efficient transferrin receptor recycling but not for EGFR degradation (By similarity). May contribute to the efficient recruitment of SMADs to the activin receptor complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10825299}. Early endosome membrane {ECO:0000269|PubMed:10825299}; Peripheral membrane protein {ECO:0000269|PubMed:10825299}; Cytoplasmic side {ECO:0000269|PubMed:10825299}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:10825299}; Peripheral membrane protein {ECO:0000269|PubMed:10825299}. Note=Colocalizes with UBQLN1 in ubiquitin-rich cytoplasmic aggregates that are not endocytic compartments. {ECO:0000250|UniProtKB:O14964}.
Interaction partners:
- Signal transducing adapter molecule 2
- Signal transducing adaptor molecule
- Tumor susceptibility gene 101 protein
- Polyubiquitin-C
- Epidermal growth factor receptor pathway substrate 15
- Vacuolar protein sorting-associated protein 28 homolog
- Charged multivesicular body protein 3
- Vacuolar protein-sorting-associated protein 25
- Vacuolar protein-sorting-associated protein 36
- Vacuolar-sorting protein SNF8
Sequence:
MGRGSGTFERLLDKATSQLLLETDWESILQICDLIRQGDTQAKYAVNSIKKKVNDKNPHVALYALEVMESVVKNCGQTVHDEVANKQTMEELKELLKRQVEVNVRNKILYLIQAWAHAFRNEPKYKVVQDTYQIMKVEGHVFPEFKESDAMFAAERAPDWVDAEECHRCRVQFGVVTRKHHCRACGQIFCGKCSSKYSTIPKFGIEKEVRVCEPCYEQLNKKAEGKAASTTELPPEYLTSPLSQQSQLPPKRDETALQEEEELQLALALSQSEAEEKERMRQKSTYTAHPKSEPAPLASSAPPAGSLYSSPVNSSAPLAEDIDPELARYLNRNYWEKKQEEARKSPTPSAPVPLTEPAAQPGEGHTAPNSMVEAPLPETDSQPITSCSGPFSEQYQNGESEESHEQFLKALQNAVSTFVNRMKSNHMRGRSITNDSAVLSLFQSINSTHPQLLELLNRLDERRLYYEGLQDKLAQIRDARGALSALREEHREKLRRAAEEAERQRQIQLAQKLEIMRQKKQEYLEVQRQLAIQRLQEQEKERQMRLEQQKQTVQMRAQMPAFPLPYAQLQAMPTAGGVLYQPSGPTSFPGTFSPAGSVEGSPMHGVYMSQPAPATGPYPSMPGTTADPSMVSAYMYPAGAPGAQAAPQAQAGPTTNPAYSSYQPTPTPGYQNVASQAPQSLPAISQPPQTSNIGYMGSQPMSMGYQPYNMQNLMTTLPGQDASLPAQQPYITGQQPMYQQMAPSTGPPQQQPPVAQPPPTQGPPAQGNETQLISFD