wanglab/gogpt-training-data huggingface dataset:
Protein: Sterol carrier protein 2 (SCP-2) (Acetyl-CoA C-myristoyltransferase) (EC 2.3.1.155) (Non-specific lipid-transfer protein) (NSL-TP) (Propanoyl-CoA C-acyltransferase) (EC 2.3.1.176) (SCP-2/3-oxoacyl-CoA thiolase) (SCP-2/thiolase) (EC 2.3.1.16) (SCP-chi) (Sterol carrier protein X) (SCP-X) (P11915)
Organism: Rattus norvegicus (Rat)
Function: Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA). Also active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro. Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs.
Subcellular location: [Isoform SCP2]: Peroxisome {ECO:0000250|UniProtKB:P32020}. Cytoplasm {ECO:0000250|UniProtKB:P22307}. Mitochondrion {ECO:0000250|UniProtKB:P22307}.; SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome {ECO:0000269|PubMed:8063752, ECO:0000269|PubMed:9325339}.
Interaction partners:
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L2
- Adhesion G protein-coupled receptor L3
Sequence:
MPSVALNSPRLPRVFVVGVGMTKFMKPGGENSRDYPDLAKEAGQKALADRQIPYSAVEQACVGYVYGESTCGQRAIYHSLGLTGIPIINVNNNCSTGSTALFMAQQLVQGGLANCVLALGFEKMEKGSLGTKYSDRSNPLEKHIDVLINKYGMSACPFAPQLFGSAGKEHMETYGTKVEHFAKIGWKNHKHSVNNPYSQFQDEYSLDEIMKSRPVFDFLTVLQCCPTSDGAAAAIVSSEEFVQKHGLQSKAVEIVAQEMVTDMPSTFEEKSVIKMVGYDMSKEAARKCYEKSGLGPSDVDVIELHDCFSTNELLTYEALGLCPEGQGGALVDRGDNTYGGKWVINPSGGLISKGHPLGATGLAQCAELCWQLRGEAGKRQVPGAKVALQHNLGLGGAAVVTLYRMGFPEAASSFRTHQISAAPTSSAGDGFKANLIFKEIEKKLEEEGEEFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPDSDKKADCTITMADSDLLALMTGKMNPQSAFFQGKLKIAGNMGLAMKLQSLQLQPDKAKL
Protein: Rac-like GTP-binding protein ARAC10 (GTPase protein ROP11) (O82481)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in local disassembly of cortical microtubules when associated with ICR5 and KIN13A.
Subcellular location: Membrane; Lipid-anchor. Cytoplasm. Cytoplasm, cytoskeleton. Note=Recruited along cortical microtubules upon interaction with ICR5. {ECO:0000269|PubMed:22984069}.
Interaction partners:
- Interactor of constitutive active ROPs 5
- Rop guanine nucleotide exchange factor 4
- Kinesin-like protein KIN-13A
- Rop guanine nucleotide exchange factor 1
- Rho GTPase-activating protein 3
- Rho GDP-dissociation inhibitor 1
- Protein phosphatase 2C 56
- KOW domain-containing protein
- Guanine nucleotide exchange factor SPIKE 1
- Protein phosphatase 2C 77
Sequence:
MASSASKFIKCVTVGDGAVGKTCMLICYTSNKFPTDYIPTVFDNFSANVVVEGTTVNLGLWDTAGQEDYNRLRPLSYRGADVFVLSFSLVSRASYENVFKKWIPELQHFAPGVPLVLVGTKLDLREDKHYLADHPGLSPVTTAQGEELRKLIGATYYIECSSKTQQNVKAVFDSAIKEVIKPLVKQKEKTKKKKKQKSNHGCLSNVLCGRIVTRH
Protein: Polyamine transport protein PotH (Q9I6I8)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363032}.
Interaction partners:
- Spermidine-binding periplasmic protein SpuE
- Putrescine transport system permease protein PotI
- Spermidine/putrescine import ATP-binding protein PotA
- Putrescine-binding periplasmic protein SpuD
- Probable periplasmic spermidine/putrescine-binding protein
- Putrescine/agmatine-binding protein
- Probable periplasmic spermidine/putrescine-binding protein
- Spermidine/putrescine transport system permease protein PotC
- Polyamine transport protein PotC
- Probable binding protein component of ABC transporter
Sequence:
MPTGRHAVIGVPFLWLFLFFLLPFAIVLKISLAEADVAIPPYTEIFAYADQQLQVLLNLGNYLMLTDDPLYIDAYLGSLKMAFISTLICLLVGYPMAYAIARSSQSSQTVLLLLIMMPTWTAILIRVYAWMGILSNNGLLNSVLMGLGLISEPLTILNTNIAVYIGIVYSYLPFMILPLYANLVKHDPSLLEAASDLGARNFTSFWKITVPLSKNGIIAGCMLVFIPAVGEFVIPELLGGPETLMIGKVLWQEFFNNRDWPVASALAVVMLAILIIPIILFNKNQAKELEGKV
Protein: Proton-coupled amino acid transporter 2 (Proton/amino acid transporter 2) (Solute carrier family 36 member 2) (Transmembrane domain rich protein 1) (Tramdorin-1) (Q495M3)
Organism: Homo sapiens (Human)
Function: Electrogenic proton/amino acid symporter with a high selectivity for the small side chains amino acids glycine, alanine and proline, where both L- and D-enantiomers are transported. Extension of the backbone length, as in beta-alanine and 4-aminobutanoate or methylation of the amino group, as in sarcosine and N,N-dimethylglycine, are also tolerated but decrease transport efficiency. A free carboxyl group is preferred.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19033659}; Multi-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q8BHK3}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q8BHK3}.
Interaction partners:
- Sodium- and chloride-dependent transporter XTRP3
- Inactive sodium-dependent neutral amino acid transporter B
- Sodium-dependent neutral amino acid transporter B
- Neutral amino acid uniporter 4
- Proton-coupled amino acid transporter 1
- Orphan sodium- and chloride-dependent neurotransmitter transporter NTT5
Sequence:
MSVTKSTEGPQGAVAIKLDLMSPPESAKKLENKDSTFLDESPSESAGLKKTKGITVFQALIHLVKGNMGTGILGLPLAVKNAGILMGPLSLLVMGFIACHCMHILVKCAQRFCKRLNKPFMDYGDTVMHGLEANPNAWLQNHAHWGRHIVSFFLIITQLGFCCVYIVFLADNLKQVVEAVNSTTNNCYSNETVILTPTMDSRLYMLSFLPFLVLLVLIRNLRILTIFSMLANISMLVSLVIIIQYITQEIPDPSRLPLVASWKTYPLFFGTAIFSFESIGVVLPLENKMKNARHFPAILSLGMSIVTSLYIGMAALGYLRFGDDIKASISLNLPNCWLYQSVKLLYIAGILCTYALQFYVPAEIIIPFAISRVSTRWALPLDLSIRLVMVCLTCLLAILIPRLDLVISLVGSVSGTALALIIPPLLEVTTFYSEGMSPLTIFKDALISILGFVGFVVGTYQALDELLKSEDSHPFSNSTTFVR
Protein: Jacalin-related lectin 23 (Myrosinase-binding protein-like At2g39330) (O80948)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Polymerizer-type lectin that may facilitate the correct polymerization and activation of BGLU23/PYK10 upon tissue damage.
Interaction partners:
- GDSL esterase/lipase At1g54020
- Protein trichome birefringence-like 26
- Inactive GDSL esterase/lipase-like protein 25
- Inactive GDSL esterase/lipase-like protein 23
- MD-2-related lipid-recognition protein 3
- Uncharacterized protein
- At3g06435
- MATH domain/coiled-coil protein
Sequence:
MAKIYRKLTGYGGEGGREWDDDVYEGVRKVYVGQDINRITYVKFEYVKEDGQVVTTEYGKIIQQPKEFVLQYPDEHIIAVEGNYRGVALCATEVITNLVFKTSKGRKSPLFGPNLLGITTGTKFVIEDGGKKIVGFHGRSGNALDALGVYFVHGSLTTSPPVYKLDAQGGTDGRVWDDGSYDGVKSLRIGQDNSRITYLEFEYEKGGKLETCRHGVKQERSLKFELNPDEYIKSVEATYDKPDIFRNVVITSLTFETSKGRTSFSGYKGGKKFKLEQKGRRLVGFHGKEGSAIDALGAYFAPIPTPTPIIPAKKLPAIGGSGGVAWDDGVYDGVRKILVGQGNDGVAFVKFEYNKGKDLVSGDDHGKMTLLGTEEFVLEDGEYLTAIDGYYDKIFGVETPMIICLQFKTNKRESTPFGMDSGEKFSLGEKGHKIVGFHGQASDVVHSIGVTVVPITNTK
Protein: Charged multivesicular body protein 7 (Q86K93)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Plays a role in the endosomal sorting pathway.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Charged multivesicular body protein 4
- IST1-like protein
- Charged multivesicular body protein 3
- Vacuolar protein-sorting-associated protein 25
- Charged multivesicular body protein 5
- Vacuolar protein sorting-associated protein 28
- Charged multivesicular body protein 1
- Vacuolar protein-sorting-associated protein 36
- ESCRT-I complex subunit tsg101
- Charged multivesicular body protein 2a homolog 2
Sequence:
MNNDKEINSEKSKRAINHFSNKKEIKNSDRRGILFSKLPSQQLNPDRYDNLMTFWNNSLIDISKSCNILIFTPKLLSTYFTVENVSPIYLPLILNEMIKTKFIVKYEEYIKDYGWSKWVWTKMVVQPFQYYTGLSTPNTETEKNVKFILPEMIKDKAEQLYQHQLKNMNSTTDNIISYINLEKSIKDWYITREELDLLLLVLFRDSKVLILTNNKIKNINNNNNGEDRIGIKFAFDGEKVQPIQETDFGILKLQTTYETLKQQESKLLTDIEEISNTIKESIRIKQKNHALLQLKKKKLLESILEKRATASTNIHEILFSIESAKSNQQIIESLCTGVSTLKKVNQEISVDQVDSILDDYQDAITNQREIDDAMKSGFNSVESLSSADIDEDQLEKELDQMLQDHLTLEKEEKQKQKQIEKEKQQQQQPPTSQFNPNLPIPLKNEEDELLKELESLSVTSNPLPKQDENKQKTSELI
Protein: Nidogen-1 (NID-1) (Entactin) (P14543)
Organism: Homo sapiens (Human)
Function: Sulfated glycoprotein widely distributed in basement membranes and tightly associated with laminin. Also binds to collagen IV and perlecan. It probably has a role in cell-extracellular matrix interactions.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane.
Interaction partners:
- Basement membrane-specific heparan sulfate proteoglycan core protein
- Fibronectin
- Laminin subunit gamma-1
- Vitronectin
- CD44 antigen
- Agrin
- Natural cytotoxicity triggering receptor 2
- Nidogen-2
- Laminin subunit alpha-2
- Fibulin-2
Sequence:
MLASSSRIRAAWTRALLLPLLLAGPVGCLSRQELFPFGPGQGDLELEDGDDFVSPALELSGALRFYDRSDIDAVYVTTNGIIATSEPPAKESHPGLFPPTFGAVAPFLADLDTTDGLGKVYYREDLSPSITQRAAECVHRGFPEISFQPSSAVVVTWESVAPYQGPSRDPDQKGKRNTFQAVLASSDSSSYAIFLYPEDGLQFHTTFSKKENNQVPAVVAFSQGSVGFLWKSNGAYNIFANDRESVENLAKSSNSGQQGVWVFEIGSPATTNGVVPADVILGTEDGAEYDDEDEDYDLATTRLGLEDVGTTPFSYKALRRGGADTYSVPSVLSPRRAATERPLGPPTERTRSFQLAVETFHQQHPQVIDVDEVEETGVVFSYNTDSRQTCANNRHQCSVHAECRDYATGFCCSCVAGYTGNGRQCVAEGSPQRVNGKVKGRIFVGSSQVPIVFENTDLHSYVVMNHGRSYTAISTIPETVGYSLLPLAPVGGIIGWMFAVEQDGFKNGFSITGGEFTRQAEVTFVGHPGNLVIKQRFSGIDEHGHLTIDTELEGRVPQIPFGSSVHIEPYTELYHYSTSVITSSSTREYTVTEPERDGASPSRIYTYQWRQTITFQECVHDDSRPALPSTQQLSVDSVFVLYNQEEKILRYALSNSIGPVREGSPDALQNPCYIGTHGCDTNAACRPGPRTQFTCECSIGFRGDGRTCYDIDECSEQPSVCGSHTICNNHPGTFRCECVEGYQFSDEGTCVAVVDQRPINYCETGLHNCDIPQRAQCIYTGGSSYTCSCLPGFSGDGQACQDVDECQPSRCHPDAFCYNTPGSFTCQCKPGYQGDGFRCVPGEVEKTRCQHEREHILGAAGATDPQRPIPPGLFVPECDAHGHYAPTQCHGSTGYCWCVDRDGREVEGTRTRPGMTPPCLSTVAPPIHQGPAVPTAVIPLPPGTHLLFAQTGKIERLPLEGNTMRKTEAKAFLHVPAKVIIGLAFDCVDKMVYWTDITEPSIGRASLHGGEPTTIIRQDLGSPEGIAVDHLGRNIFWTDSNLDRIEVAKLDGTQRRVLFETDLVNPRGIVTDSVRGNLYWTDWNRDNPKIETSYMDGTNRRILVQDDLGLPNGLTFDAFSSQLCWVDAGTNRAECLNPSQPSRRKALEGLQYPFAVTSYGKNLYFTDWKMNSVVALDLAISKETDAFQPHKQTRLYGITTALSQCPQGHNYCSVNNGGCTHLCLATPGSRTCRCPDNTLGVDCIEQK
Protein: Prostaglandin G/H synthase 1 (EC 1.14.99.1) (Cyclooxygenase-1) (Prostaglandin H2 synthase 1) (Prostaglandin-endoperoxide synthase 1) (A0A087X296)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004406}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004406}. Microsome membrane {ECO:0000256|ARBA:ARBA00004174}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004174}.
Interaction partners:
Sequence:
MSRSLLLWFLLFLLLLPPLPVLLADPGAPTPVNPCCYYPCQHQGICVRFGLDRYQCDCTRTGYSGPNCTIPGLWTWLRNSLRPSPSFTHFLLTHGRWFWEFVNATFIREMLMRLVLTGKKQLPDAQLLARRFLLRRKFIPDPQGTNLMFAFFAQHFTHQFFKTSGKMGPGFTKALGHGVDLGHIYGDNLERQYQLRLFKDGKLKYQVLDGEMYPPSVEEAPVLMHYPRGIPPQSQMAVGQEVFGLLPGLMLYATLWLREHNRVCDLLKAEHPTWGDEQLFQTTRLILIGETIKIVIEEYVQQLSGYFLQLKFDPELLFGVQFQYRNRIAMEFNHLYHWHPLMPDSFKVGSQEYSYEQFLFNTSMLVDYGVEALVDAFSRQIAGRIGGGRNMDHHILHVAVDVIRESREMRLQPFNEYRKRFGMKPYTSFQELVGEKEMAAELEELYGDIDALEFYPGLLLEKCHPNSIFGESMIEIGAPFSLKGLLGNPICSPEYWKPSTFGGEVGFNIVKTATLKKLVCLNTKTCPYVSFRVPDASQDDGPAVERPSTEL
Protein: SMARCD2 protein (B9EGA3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGRGAGGFPLPPLSPGGGAAFRPMGPAGPAAQYQRPGMSPGNRMPMAGLQVGPPAGSPFGAAAPLRPGMPPTMMDPFRKRLLVPQAQPPMPAQRRGLKRRKMADKVLPQRIRELVPESQAYMDLLAFERKLDQTIARKRMEIQEAIKKPLTQKRKLRIYISNTFSPSKAEGDSAGTAGTPGGTPAGDKVASWELRVEGKLLDDPSKQKRKFSSFFKSLVIELDKELYGPDNHLVEWHRMPTTQETDGFQVKRPGDLNVKCTLLLMLDHQPPQYKLDPRLARLLGVHTQTRAAIMQALWLYIKHNQLQDGHEREYINCNRYFRQIFSCGRLRFSEIPMKLAGLLQHPDPIVINHVISVDPNDQKKTACYDIDVEVDDPLKAQMSNFLASTTNQQEIASLDVKIHETIESINQLKTQRDFMLSFSTDPQDFIQEWLRSQRRDLKIITDVIGNPEEERRAAFYHQPWAQEAVGRHIFAKVQQRRQELEQVLGIRLT
Protein: Uncharacterized protein (Q389J8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRGRFLSSTFRLGLYRTKQHVRAGSKGQEDQFSSRASHIISRRVRAVDWLYMDPVEKWTILVDLGRRAPMLLEDALSGAPPGGEQGVKAEMNLLGRLLCYCPCVSRNGKRAAAAVSEEHLCGVSSQKHRGLIDGLPYCVRLQLCLSFLMWVRSLRDVQNTLAHLRMPFATTRRFKRGVVADVFPTCLSEMCVDPFTTVSLMMDESLNSTAEQVPAPHAWRPDGYYEDEEERRAWSFASRLGKRRSSCIPSGGGTADSGVASGQSRRRRSCVGLTGRDMVMLREIQGMRPVPSDDDVLAGRSGLHVGRLRLQAPPTNLGQSYTNGLSASSYALSDAQRGALPSPLAVDNEEDEVYHHNIHRGEGCPLDESGQLECTPIHIPVSLAADRVVITRHCAMAHAAILTSLFVEGRTVQFTTNHPLLLDYVSFLFAELVEAGWVSAAICEESLRPYVPLWAVAESVLVLVPPKDTEVCRTHDVRGTADMIVQCAPCSVLTEDVGQISGSRFYRDLREEVQRLQATLISRGNDASWRVSWVPVSKSTSLYATPQKVDCGDAGEFQTSVNEVLRHCHTVTFLYTPRNCRFTPREMEGWWWNGLPRSVLVVGVNSHPLDIVYFFPQAPFLHKKVGNAFRYRAVRRVLLRKNVHGGREGIVRNWLYRSLWCRGLARTGLQGQLAVKDKMRVLPGGDVTKGGEHAVDALKWERTVDYLANPGKMTWMALVAAKLLHI
Protein: Follicle-stimulating hormone receptor (FSH-R) (Follitropin receptor) (P35379)
Organism: Ovis aries (Sheep)
Function: G protein-coupled receptor for follitropin, the follicle-stimulating hormone. The activity of isoform FSH-R1 is mediated by G proteins which activate adenylate cyclase. Isoform FSH-R2 and isoform FSH-R3 also bind FSH, but this does not result in activation of adenylate cyclase. Isoform FSH-R3 may be involved in calcium signaling. Through cAMP production activates the downstream PI3K-AKT and ERK1/ERK2 signaling pathways (By similarity).
Subcellular location: [Isoform FSH-R1]: Cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:9364440}.; SUBCELLULAR LOCATION: [Isoform FSH-R2]: Cell membrane; Multi-pass membrane protein {ECO:0000269|PubMed:9364440}.; SUBCELLULAR LOCATION: [Isoform FSH-R3]: Cell membrane {ECO:0000305|PubMed:10527886}; Single-pass membrane protein {ECO:0000305|PubMed:10527886}.
Interaction partners:
- Follitropin subunit beta
- Anti-Mullerian hormone N-terminal domain-containing protein
- Growth/differentiation factor 9
- Bone morphogenetic protein 15
- Pro-opiomelanocortin
- Glycoprotein hormones alpha chain
- Vasoactive intestinal peptide
- Steroid 17-alpha-hydroxylase/17,20 lyase
- Pro-glucagon
- Gastric inhibitory polypeptide
Sequence:
MALFLVALLAFLSLGSGCHHRLCHCSNGVFLCQDSKVTEMPSDLPRDAVELRFVLTKLRVIPEGAFSGFGDLEKIEISQNDVLEVIEANVFSNLPKLHEIRIEKANNLLYIDPDAFQNLPNLRYLLISNTGIKHLPAVHKIQSLQKVLLDIQDNINIHTVERNSFMGLSFESMIVWLSKNGIQEIHNCAFNGTQLDELNLSDNSNLEELPNDVFQGASGPVILDISRTRIRSLPSYGLENLKKLRAKSTYHLKKLPSLEKFVTLVEASLTYPSHCCAFANWRRQTSDLHPICNKSILRQEVDDMTQARGQRISLAEDDEPSYAKGFDMMYSEFDYDLCSEVVDVTCSPEPDAFNPCEDIMGYDILRVLIWFISILAITGNILVLVILITSQYKLTVPRFLMCNLAFADLCIGIYLLLIASVDVHTKSQYHNYAIDWQTGAGCDAAGFFTVFASELSVYTLTAITLERWHTITHAMQLECKVHVRHAASIMLVGWVFAFAVALFPIFGISSYMKVSICLPMDIDSPLSQLYVMSLLVLNVLAFVVICGCYTHIYLTVRNPNITSSSSDTKIAKRMAMLIFTDFLCMAPISFFAISASLKVPLITVSKSKILLVLFYPINSCANPFLYAIFTRNFRRDFFILLSKFGCYEVQAQTYRSETSFTAHNFHPRNGHCPPAPRVTNGSNYTLIPLRHLAKN
Protein: Protein cwh43 (Q9HDZ2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the maintenance of cell wall integrity. Required for the replacement of the diacylglycerol moiety by ceramides during GPI-anchor maturation (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MTEKTSSLVFSAQYVALVHTICSFAAFFIPLALALYTHYYQVVKNEFYGYPEEWFPSVSATIGDWYPERSVFQWLIALTATPRLLVLLLWFTLSGISRPSVIITTALGVLRTALCGGWVYVTSTDDHDWHDIFMIGYLISNAPWFILVSKCSPVNSMASRIRNIGSALFVLTIFPLIYWYIQHKFKHIPGAYTVYAFFEWSLILWDILFDSALYWDFKPLVFNLHTSKTYSNPSSFATRKKEKGEHLSYAEAAAVGTQAKNIKKDSNVKCSKKQILFSLLYFSSEVYLSFVFWSVLTSLGLLVWYFPLWHMGISGYEACILFELSPFLLGIPLLRKFASKVPVIFLFLNVIGIAAYKLEDPVHRLFVTAFSVCCECLAWTSLFSNISPENLAIERKISTFLFGLLASSIAKYSFFSNNPIWPILNETNGGKQIPALIVGIIACLIFAIFHVQQTTANAVEHFKLRKITALSAALSLGTVLFCLHTFLCDSTVLMTWSWDGYPIKGPQPYPHGAVSIVVSICAVLVAPYLYQSGAFMLIGFVLACFGSYFMYINHGWCSYLGGLIFTSYVLIYSFASIRISSFYSPAKVWGGAFLVYILYSLAHVWVVAYEFVPGGPILRERTSYILIFIGWNLAALVPAYSGESKEPNKADSSVVDIKQSDSSYRRRSFKKSLLTGFCLALMALKFAIQNMPPYDYTPYHPNEKLFTAGIWTIHFGLDNFMYASENRIRDAVRDMELDVFGLLESDTQRLIMGFRDLTQVLAHDLGMYADYGPGPDKHTWGAALLSKFPIVNSTHHLLPSPQGELAPAIHATLDVYGELIDVVVSHNGQYESQLDRRLQSTELARIMRESPRPLVFLGYVVSNVGQEPQTILTRDTGMLDIEPADYDRWCQYIFYRGVKRIGYARLHRSTITDTELQTGKFLVTKDLGRNVRIDKEHVPESHRYPSLFEGTGVNGHYYDNNLVVHEPWYYD
Protein: Bowman-Birk type proteinase inhibitor 2 (Bowman-Birk type proteinase inhibitor II) [Cleaved into: Bowman-Birk type proteinase inhibitor 2 long; Bowman-Birk type proteinase inhibitor 2 short] (P01060)
Organism: Phaseolus vulgaris (Kidney bean) (French bean)
Function: This protein inhibits elastase and trypsin simultaneously and independently.
Interaction partners:
Sequence:
MMVLKVCLLLVFLAGVTTARMDLNHLIGSNHHDSSDEPSESSEPCCDICVCTASIPPICQCTDVRLNSCHSACKSCMCTRSMPGKCRCLDTTDYCYKSCKSSGEDDD
Protein: Citrate synthase (EC 2.3.3.16) (P0ABH7)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Aconitate hydratase A
- Aconitate hydratase B
- Isocitrate dehydrogenase
- Malate dehydrogenase
- Malate synthase A
- Fumarate hydratase class I, aerobic
- Phosphoenolpyruvate carboxylase
- Acetyl-coenzyme A synthetase
- Malate synthase G
- Succinate--CoA ligase subunit beta
Sequence:
MADTKAKLTLNGDTAVELDVLKGTLGQDVIDIRTLGSKGVFTFDPGFTSTASCESKITFIDGDEGILLHRGFPIDQLATDSNYLEVCYILLNGEKPTQEQYDEFKTTVTRHTMIHEQITRLFHAFRRDSHPMAVMCGITGALAAFYHDSLDVNNPRHREIAAFRLLSKMPTMAAMCYKYSIGQPFVYPRNDLSYAGNFLNMMFSTPCEPYEVNPILERAMDRILILHADHEQNASTSTVRTAGSSGANPFACIAAGIASLWGPAHGGANEAALKMLEEISSVKHIPEFVRRAKDKNDSFRLMGFGHRVYKNYDPRATVMRETCHEVLKELGTKDDLLEVAMELENIALNDPYFIEKKLYPNVDFYSGIILKAMGIPSSMFTVIFAMARTVGWIAHWSEMHSDGMKIARPRQLYTGYEKRDFKSDIKR
Protein: Prephenate dehydrogenase (PDH) (EC 1.3.1.12) (O69721)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the NAD(+)-dependent conversion of prephenate to p-hydroxyphenylpyruvate, with the elimination of carbon dioxide. Is a key regulatory enzyme in tyrosine biosynthesis. Displays no chorismate mutase (CM) activity, in contrast to TyrA from E.coli and some other bacteria, that are bifunctional and possess a CM domain.
Interaction partners:
- Prephenate dehydratase
- Aromatic amino acid aminotransferase
- Histidinol-phosphate aminotransferase
- Histidinol-phosphate aminotransferase Rv2231c
- Intracellular chorismate mutase
- Secreted chorismate mutase
- Chorismate synthase
- 3-dehydroquinate synthase
- Homoserine dehydrogenase
- Phosphoribosyltransferase
Sequence:
MTRTVAAPPVCVLGLGLIGGSIMRAAAAAGREVFGYNRSVEGAHGARSDGFDAITDLNQTLTRAAATEALIVLAVPMPALPGMLAHIRKSAPGCPLTDVTSVKCAVLDEVTAAGLQARYVGGHPMTGTAHSGWTAGHGGLFNRAPWVVSVDDHVDPTVWSMVMTLALDCGAMVVPAKSDEHDAAAAAVSHLPHLLAEALAVTAAEVPLAFALAAGSFRDATRVAATAPDLVRAMCEANTGQLAPAADRIIDLLSRARDSLQSHGSIADLADAGHAARTRYDSFPRSDIVTVVIGADKWREQLAAAGRAGGVITSALPSLDSPQ
Protein: Carboxylic ester hydrolase (EC 3.1.1.-) (Q9Y141)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Acetylcholinesterase
- LD22655p
- RE24176p
- Gamma-aminobutyric acid receptor subunit beta
- Vesicular acetylcholine transporter
Sequence:
MLMLFVVELLVLLASSSVLSIEVDTELGRVRGANLTSRLGVNFHAFRGIRYAEPPLGDLRFVNPQPVKPWSPKIFDASEDGPMCPQPWDNMTDVSEDCLRLNVYTKDLKGRRPVIVFLHPGGFYVFSGQSKYLAGPEHFMDRDCVLVSLNYRLGSLGFLATGSKEAPGNAGLKDQVLALRWIQQHIQRFGGDPDSVTLLGYSAGSISVALHMLSPMSRGLFHRGICMSAAPYGPVKYKDNDLQLAKRQAGLLKCPQESIGEMVECMRRKPYLDYVSTYNGMFEFGWNPVLNWRIVVEKDFGQERYLIESPFKTARRGDFHKVALITGITEFEFLSGAFFDLRNESIVNRYNRDWEHYASIALLLEQNSTQSRAASRVFREKYMPESLDKLEYPKSLKGMGELLSDALIGVSFHRFLQLMSPHTPIYTYLFRYKGRYTFLKNPDNQQTIGPVHHDELIYLFHVGLLIPLLKREDPENFMIELLTRMWIEFAQKGDPHNKNDEYLKGLNWPLYNAQDKGYLEIGNNLTAKSGGFFLNRYQIWEDLFPLSSFH
Protein: Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial (MMSDH) (EC 1.2.1.27) (Aldehyde dehydrogenase family 6 member A1) (Malonate-semialdehyde dehydrogenase [acylating]) (Q02252)
Organism: Homo sapiens (Human)
Function: Plays a role in valine and pyrimidine metabolism. Binds fatty acyl-CoA.
Subcellular location: Mitochondrion {ECO:0000305|PubMed:23835272}.
Interaction partners:
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Propionyl-CoA carboxylase beta chain, mitochondrial
- 4-aminobutyrate aminotransferase, mitochondrial
- Aldehyde dehydrogenase, mitochondrial
- Propionyl-CoA carboxylase alpha chain, mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Peroxisomal bifunctional enzyme
- 3-ketoacyl-CoA thiolase, peroxisomal
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MAALLAAAAVRARILQVSSKVKSSPTWYSASSFSSSVPTVKLFIGGKFVESKSDKWIDIHNPATNEVIGRVPQATKAEMDAAIASCKRAFPAWADTSVLSRQQVLLRYQQLIKENLKEIAKLITLEQGKTLADAEGDVFRGLQVVEHACSVTSLMMGETMPSITKDMDLYSYRLPLGVCAGIAPFNFPAMIPLWMFPMAMVCGNTFLMKPSERVPGATMLLAKLLQDSGAPDGTLNIIHGQHEAVNFICDHPDIKAISFVGSNKAGEYIFERGSRHGKRVQANMGAKNHGVVMPDANKENTLNQLVGAAFGAAGQRCMALSTAVLVGEAKKWLPELVEHAKNLRVNAGDQPGADLGPLITPQAKERVCNLIDSGTKEGASILLDGRKIKVKGYENGNFVGPTIISNVKPNMTCYKEEIFGPVLVVLETETLDEAIQIVNNNPYGNGTAIFTTNGATARKYAHLVDVGQVGVNVPIPVPLPMFSFTGSRSSFRGDTNFYGKQGIQFYTQLKTITSQWKEEDATLSSPAVVMPTMGR
Protein: Ubiquitin-like modifier-activating enzyme ATG7 (Autophagy-related protein 7) (F7ESQ7)
Organism: Macaca mulatta (Rhesus macaque)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU366022}. Preautophagosomal structure {ECO:0000256|RuleBase:RU366022}.
Interaction partners:
Sequence:
MAAATGDPGLSKLQFAPFSSALDVGFWHELTQKKLNEYRLDEAPKDIKGYYYNGDSAGLPARLTLEFSAFDMSAPTPARCCPAVGTLYNTNTLESFKTADKKLLLEQAANEIWESIKSGTALENPVLLNKFLLLTFAIEALECAYDNLCQTEGVTALPYFLIKYDENTVLVSLLKHYSDFFQGQRMKITIGVYDPCNLAQYPGWPLRNFLVLAAHRWSSSFQSVEVLCFRDRTMQGARDVAHSIIFEVKLPEMAFSPDCPKAVGWEKNQKGGMGPRMVNLSECMDPKRLAESSVDLNLKLMCWRLVPTLNLDKVVSVKCLLLGAGTLGCNVARTLMGWGVRHITFVDNAKISYSNPVRQPLYEFEDCLAGGKPKALAAADRLQKIFPGVNARGFNMSIPMPGHPVNFSSVTLEQARRDVEQLEQLIESHDVIFLLMDTRESRWLPAVIAASKRKLVINAALGFDTFVVMRHGLKKPKQQGAGDLCPNHPVASADLLGSSLFANIPGYKLGCYFCNDVVAPGDSTRDRTLDQQCTVSRPGLAMIAGALAVELMVSVLQHPEGGYAIASSSDDRMNEPPTSLGLVPHQIRGFLSRFDNVLPVSLAFDKCTACSSKVLDQYEREGFNFLAKVFNSSHSFLEDLTGLTLLHQETQAAEIWDMSDDETI
Protein: tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (G3V3Y5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLVSLKMSYKAAAGEDYKADCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVKGIF
Protein: NR LBD domain-containing protein (E5QCI8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MGQENMRTVPQSSSVIDALMEMEARVNQEMCNRYRRSQIFANGSGGSNGNDTDIQQGSDSGASAFAPPNRPCTTEDLNEISRTTLLLMVEWAKTINPFMDLSMEDKIILLKNYAPQHLILMPAFRSPDTTRVCLFNNTYMTRDNNTDLNGFAAFKTSNITPRVLDEIVWPMRQLQMREQEFVCLKALAFLHPEAKGLSNSSQIMIRDARNRVLKALYAFILDQMPDDAPTRYGNILLLAPALKALTQLLIENMTLTKFFGLAEVDSLLSEFILDDINDHSTAPVSLQQHLSSPTTLPTNGVSPLNPAGSVGSVSSVSGITPTGMLSATLAAPLAIHPLQSQDSILNSEQNNHML
Protein: Nuclear receptor coactivator 4 N-terminal domain-containing protein (Q3UM78)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MNTSLEQSGCYSNRETLLRCSDARRELELAIGGVLRAEQQIKDNLREVKAQIHSCISRHLECLRSREVWLNEQVDLIYQLKEETLQQQAQQLYWLMGQFNCLIHQLEYTQNKDLANQVSVCLERLGSLALKPEDSTVLLFEADTSALRQTITTFGSLKTIQIPEHLMAHASSSSIGPFLEKRGYIQVPEQKSASSGTAVSLSEWLLVSKPAIGLQAPYVPSTNPQDWLIPKQTSENSQTSARACSFFSDAWGNLKGLENWLLNSHQQEIAGKPSSSKCNSHCSTSSFSPEAEKAEDVELLDQDELDLSDWLVTPQEPCELEKPVDGSWETSEKFKLLFQVFREPYNVSDWLVKPDSCTNCQGNQPRGVEIENLGNLKCLNDHLEAKKSVSVPSATISEGWLAQNHQDTWKVEEVCKANEPCTSFAECVCDDNCEKEAVYKWLLKKGGKDKNGMPMEPKSEPEKHRESLTLWLCPSRNELTEQAKAPKALAPARIADSFHVIKNSSLSEWLIGPTCKGGPKDVPNTEERAGKEMLQSSMATSWCPFNTADWVLPGKKVGSLSQFPSGEDKWLLRKKAQEERNFRPDCYGLPAVCDLFACMQLKVDKEKWLYRTPLQM
Protein: Ribonucleotide reductase regulatory TP53 inducible subunit M2B (A0A8I6ACU7)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MGDPERPEAARPEEGEVDLSKDLPHWNKLKSEEKYFISHILAFFAASDGIVNENLVERFSQEVQVPEARCFYGFQILIENVHSEMYSLLIDTYIRDPKKREFLFNAIETMPYVKKKADWALRWIADRKSTFGERVVAFAAVEGIFFSGSFAAIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFQYLVNKPSEERVMEIIVDAVKIEQEFLTEALPVGLIGMNCVLMKQYIEFVADRLLGELGFSKIFQAENPFDFMENISLEGKTNFFEKRVSEYQRFAVMAETTDNVFTLDADF