wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-fucosidase A (EC 3.2.1.51) (Alpha-L-fucoside fucohydrolase A) (Q5AU81)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Alpha-fucosidase involved in degradation of fucosylated xyloglucans. Hydrolyzes alpha-1,2-linked fucose. Active on cotton xyloglucan oligomers but not active on paranitrophenyl-fucoside.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MRKTTLFLAVTFATSNAQGRALRSSSPATYGTTDGSDYILKTGYLIGNGKLGVIPFGPPDTEKLNLNVDSLWSGGPFEVENYTGGNPSSPIYDALPGIRERIFENGTGGMEELLGSGNHYGSSRVLGNITIALDGVEAYSKYKRTLDLSDGVHRTSFTIANRTTAALKSSIFCSYPDQVCVYHLESASDARLPKVTISIENLLVNQSLLQTSCESEAKRAVLRHSGVTQAGPPEGMKYAAVAEVVNPRSSVTTCLGEGALQISSRKKQLTIIIGAATNYDQKAGNAKSGWSFKNAKDPASIVDGIASAAGWKGYQRLLDRHVKDYKKLMGDFSLELPDTTDSASKDTSELIEKYSYASATGNPYLENLLLDYARHLLVSSSRPNSLPANLQGRWTESLTPSWSADYHANINLQMNYWLADQTGLGETQHALWNYMADTWVPRGTETARLLYNASGWVVHNEINIFGFTAMKEDAGWANYPAAAAWMMQHVWDNFDYTHDTAWLVSQGYALLKGIASFWLSSLQEDKFFNDGSLVVNPCNSPETGPTTFGCTHYQQLIHQVFETVLAAQEYIHESDTKFVDSVASALERLDTGLHLSSWGGLKEWKLPDSYGYDNMSTHRHLSHLAGWYPGYSISSFAHGYRNKTIQDAVKETLTARGMGNAADANAGWAKVWRAACWARLNDSSMAYDELRYAIDENFVGNGLSMYWGASPPFQIDANFGFAGAVLSMLVVDLPTPRSDPGQRTVVLGPAIPSAWGGGRAKGLRLRGGAKVDFGWDKRGVVNWVNIVKRGKGTSRVKLVNKEGDILAEM
Protein: CB1 cannabinoid receptor-interacting protein 1 (CRIP-1) (Q5M8N0)
Organism: Mus musculus (Mouse)
Function: Suppresses cannabinoid receptor CNR1-mediated tonic inhibition of voltage-gated calcium channels.
Interaction partners:
Sequence:
MGDLPGLVRLSIALRIQPNDGPVFFKVDGQRFGQNRTIKLLTGSSYKVEVKIKPTTLQVENISIGGVLVPLELKGKEPDGERVVYTGIYDTEGVAPTKSGERQPIQITMPFTDIGTFETVWQVKFYNYHKRDHCQWGSPFSVIEYECKPNETRSLMWVNKESFL
Protein: DnaJ homolog subfamily B member 1 (M0R080)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFAEFFGGRNPFDTFFGQRNGEEGMDIDDPFSGFPMGMGGFTNVNFGRSRSAQEPARKKQDPPVTHDLRVSLEEIYSGCTKKMKISHKRLNPDGKSIRNEDKILTIEVKKGWKEGTKITFPKEGDQTSNNIPADIVFVLKDKPHNIFKRDGSDVIYPARISLREALCGCTVNVPTLDGRTIPV
Protein: ethanolamine-phosphate cytidylyltransferase (EC 2.7.7.14) (CTP:phosphoethanolamine cytidylyltransferase) (Q388W5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVSHYLSDHSFFFTPLERDRVAHADTSVETRPVSFVTLVLHSLWVFLDSTFVPEAVAPNTITLVGLMSSVQSYQILSEYYDQTPQSHTAAATGPILMSSLLCVVAIMCGALDGVHARRCRSATPLGDIFSRVCSSVLRIFFALTLMKAFNIVDISTQWYALMVLQLIEFNTVLGRISAENLRGGKAKTVVYHLTYCFRDSELSFLILCALIARVVFPDMNFYSPVYPNFLRDAFIFLVMVSFTNLLLLKMEKKHKAAIAVCLATRVVPLFNIFSFTNNNVFSLISGSLAVGLLSTEVHVSNVSGRRVHAAVICICVGSVFNDILSIGASILYVIGMMADLSYSARIPLFAPVRNVFCDGVFDLCHAGHKNFLQNALLYGNRLIVGVCGDDECEAYKRRPIMTVDERVNEVKMCKFVSQVIRNSPVTGVTEEMIKRYNIHVVVCGDEYNRPDDTYYAVPRRMGILRTAPRTEGISTSLLIARIRDATEVELSRRDNASSRSTVMEGS
Protein: CesD/SycD/LcrH family type III secretion system chaperone SscA (Type III secretion system chaperone protein) (A0A0H3NG86)
Organism: Salmonella typhimurium (strain SL1344)
Interaction partners:
Sequence:
MKKDPTLQQAHDTMRFFRRGGSLRMLLDDDVTQPLNTLYRYATQLMEVKEFAGAARLFQLLTIYDAWSFDYWFRLGECCQAQKHWGEAIYAYGRAAQIKIDAPQAPWAAAECYLACDNVCYAIKALKAVVRICGEVSEHQILRQRAEKMLQQLSDRS
Protein: Meiotically up-regulated gene 151 protein (Q10069)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Has a role in meiosis.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transcriptional regulatory protein sds3
- Chromatin modification-related protein eaf3
- Putative histone deacetylase complex subunit cti6
- Paired amphipathic helix protein pst2
- Paired amphipathic helix protein pst1
- Paired amphipathic helix protein pst3
- Transcriptional regulatory protein rxt2
- Histone deacetylase clr6
- RbAp48-related WD40 repeat-containing protein prw1
- Uncharacterized protein C2F7.07c
Sequence:
MSLVAYDSEEEEQTSLVNENNDIKGRSEEPHWKIPNSPKAEVDTELEKKIKQFIKLKAKGIHFHTRLSENENFRNPKLLDNLQDFLDIKEPRGTMISKDMWDPTDFHKNVYASALSKSQDEMIARRENYQKHDRTEIKFQTSQHPK
Protein: Transmembrane protein (O06197)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MSIRPTTSPALADQLKDPAYSAYVLLRTLFTVAPILFGLDKFFNLLTHPQHWNMYLAGWINDLVPGTADQCMYLVGAIEIVAGVLVAVAPRIGAWVVAAWLAGIILNLVTGPGFYDIALRDFGLLVGAIALARLAQGVHSGGIGRP
Protein: Spermidine coumaroyl-CoA acyltransferase (SCT) (Spermidine dicoumaroyl transferase) (EC 2.3.1.249) (Q8GYW8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Spermidine coumaroyl-CoA acyltransferase that mediates the conversion of spermidine into dicoumaroyl-spermidine.
Interaction partners:
- Protein DETOXIFICATION 6
- AT5g66780/MUD21_2
- Probable long-chain-alcohol O-fatty-acyltransferase 3
- Anther-specific proline-rich protein APG
- Non-specific lipid-transfer protein 11
- Probable inactive purple acid phosphatase 24
- BAHD acyltransferase BIA1
- Purple acid phosphatase 23
Sequence:
MANQRKPILPLLLEKKPVELVKPSKHTHCETLSLSTLDNDPFNEVMYATIYVFKANGKNLDDPVSLLRKALSELLVHYYPLSGKLMRSESNGKLQLVYLGEGVPFEVATSTLDLSSLNYIENLDDQVALRLVPEIEIDYESNVCYHPLALQVTKFACGGFTIGTALTHAVCDGYGVAQIIHALTELAAGKTEPSVKSVWQRERLVGKIDNKPGKVPGSHIDGFLATSAYLPTTDVVTETINIRAGDIKRLKDSMMKECEYLKESFTTYEVLSSYIWKLRSRALKLNPDGITVLGVAVGIRHVLDPPLPKGYYGNAYIDVYVELTVRELEESSISNIANRVKKAKKTAYEKGYIEEELKNTERLMRDDSMFEGVSDGLFFLTDWRNIGWFGSMDFGWNEPVNLRPLTQRESTVHVGMILKPSKSDPSMEGGVKVIMKLPRDAMVEFKREMATMKKLYFGDTN
Protein: BcDNA.LD28120 (Outsiders, isoform A) (Outsiders, isoform B) (Q9V3F9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEKSSLTEKNHTQVYNDTTKPKKPKRRDKSDLGPDFVAPDGGWGWVVCLAAGLNNFFLFPALQQYGLIYRVRMQSLGFDAKQTTTIVNVVMAISSLVGIVNGAMFRRFTFRQVALTGTSLAFLGVFLSAFCTTFWQYIICLSAIFGIGLGLAMAATSLAVNTYFKLKRRRATGFSWTITGLGPIFFPQVSTVLLGYYGAQGTILIYAGIAMNAILCALTLQPVLWHVKKPEKPVHNTIEGIAETEKLQPELLEANGNLLSPSNDPWKDYECKYCQYQKRSKRGLFSSQYLFNVDDPERPGYEITEPGTPMLARANDGWFGSKLSLTSESAGGARSRTRQALMRQVSSRSRENLDRLEQNRHDQGPDTPSAAALYKPNYFNREREDLDRYASKTSVYSRPGQDELLRCTCAEDKALLQKTAESLQVNLFNNSADNTEAEEEAKRRMTFFQKVSKFFDLDLLRDFTFVNLAVGMSIMMFGEMNFSVLTPFILNSFGYTDTQISLVMSLLACMDISVRFLAPLALEKVKLDNRVLFAFGILCIAVGRVVVAFTDSYEIMIGVFLLIGFGKAFRTIFSPLIIPSYVPLNRLPAASGLQLIFNTIFSFAMGPILGILTEAYGYAATIHTINALTLLALLLWLAESVVRRILGIPSKGLGQ
Protein: Polybia-mastoparan-III (Polybia-MP-III) (Polybia-MPIII) (Mastoparan peptide) (MP) (Venom protein 13b) (VP13b) (P84914)
Organism: Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp)
Function: Antimicrobial peptide. Is active against both Gram-negative and -positive bacteria (Escherichia coli (MIC=38 uM), Pseudomonas aeruginosa (MIC=310 uM), Staphylococcus aureus (MIC=19 uM), and Bacillus cereus (MIC=38 uM)). Also causes moderate mast cell degranulation (ED(50)=100 uM) and low hemolysis (MIC=50 uM). Exhibits chemotactic activity for polymorphonucleated leukocytes (PMNL).
Subcellular location: Secreted {ECO:0000269|PubMed:15150833, ECO:0000269|PubMed:19463874}. Target cell membrane {ECO:0000305|PubMed:19463874}. Note=Forms amphipathic alpha-helical conformations under membrane-mimetic conditions. {ECO:0000305|PubMed:19463874}.
Interaction partners:
Sequence:
IDWLKLGKMVMDVL
Protein: (-)-beta-pinene synthase 2, chloroplastic (EC 4.2.3.120) ((-)-alpha-pinene synthase (-)betapin2, chloroplastic) (EC 4.2.3.119) (Terpene synthase (-)betapin2) (PbTPS-(-)betapin2) (R9QMW5)
Organism: Pinus banksiana (Jack pine) (Pinus divaricata)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-beta-pinene and, to a lower extent, to (-)-alpha-pinene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MDLISVLPSASKSCVCLHKPLSSSTHKLKPFCRKIRILGMPRPRKSVLMVSSMSISVNTLVSDDAVQRRTGGYHSNLWNDDVIQFLSTPYGELAYRERAERLIDEVRNIFSSMSLEDGESSDLIQRLWMVDNVERLGIDRHFKNEIKSALDYVYSYWSQKGIGCGTKSIITDLNSTALGFRILRLHGYPVSAEVFKHFRNQIGQFVSCHSETEEDIRSIVNLYRASLIAFPGEKVMEEAEIFSEKYLKETLQKIPDCSLSREIGDVLEHGWHTNLPRFEARNYMDVFGQDTKNMESNRKAEKLLELAKLEFNIFQSIQKTELESLLRWWNDSGSPQITFTRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITVLDDMYDLFGTVEELKLFTAAIKRWDPSATDCLPQYMKGIYMMVYNTVNEMSAEAQKAQRRDTLNYARQAWEVYLDSYMQEAKWIATGYLPTFEEYLENGKVSSGHRVSALQPMLTMDIPFPPHILKEVDFPSNLNDLACAILRLRGDTRCYQEDRARGEETSCISCYMKDNPGATEEDALNHLNVMISGVIKELNWELLKPDSSVPISSKKINFDITRAFHYGYKYRDGYSVSSVETKSLVMRTLLEPVPL
Protein: Ras GTPase-activating protein nGAP (RAS protein activator-like 2) (Q9UJF2)
Organism: Homo sapiens (Human)
Function: Inhibitory regulator of the Ras-cyclic AMP pathway.
Interaction partners:
- Disabled homolog 2-interacting protein
- GTPase NRas
- GTPase HRas
- GTPase KRas
- Ras-related protein M-Ras
- Ras-related protein R-Ras
- Ras-related protein R-Ras2
Sequence:
MQTPEVPAERSPRRRSISGTSTSEKPNSMDTANTSPFKVPGFFSKRLKGSIKRTKSQSKLDRNTSFRLPSLRSTDDRSRGLPKLKESRSHESLLSPCSTVECLDLGRGEPVSVKPLHSSILGQDFCFEVTYLSGSKCFSCNSASERDKWMENLRRTVQPNKDNCRRAENVLRLWIIEAKDLAPKKKYFCELCLDDTLFARTTSKTKADNIFWGEHFEFFSLPPLHSITVHIYKDVEKKKKKDKNNYVGLVNIPTASVTGRQFVEKWYPVSTPTPNKGKTGGPSIRIKSRFQTITILPMEQYKEFAEFVTSNYTMLCSVLEPVISVRNKEELACALVHILQSTGRAKDFLTDLVMSEVDRCGEHDVLIFRENTIATKSIEEYLKLVGQQYLHDALGEFIKALYESDENCEVDPSKCSSSELIDHQSNLKMCCELAFCKIINSYCVFPRELKEVFASWKQQCLNRGKQDISERLISASLFLRFLCPAIMSPSLFNLMQEYPDDRTSRTLTLIAKVIQNLANFAKFGNKEEYMAFMNDFLEHEWGGMKRFLLEISNPDTISNTPGFDGYIDLGRELSVLHSLLWEVVSQLDKGENSFLQATVAKLGPLPRVLADITKSLTNPTPIQQQLRRFTEHNSSPNVSGSLSSGLQKIFEDPTDSDLHKLKSPSQDNTDSYFRGKTLLLVQQASSQSMTYSEKDERESSLPNGRSVSLMDLQDTHAAQVEHASVMLDVPIRLTGSQLSITQVASIKQLRETQSTPQSAPQVRRPLHPALNQPGGLQPLSFQNPVYHLNNPIPAMPKASIDSSLENLSTASSRSQSNSEDFKLSGPSNSSMEDFTKRSTQSEDFSRRHTVPDRHIPLALPRQNSTGQAQIRKVDQGGLGARAKAPPSLPHSASLRSTGSMSVVSAALVAEPVQNGSRSRQQSSSSRESPVPKVRAIQRQQTQQVQSPVDSATMSPVERTAAWVLNNGQYEEDVEETEQNLDEAKHAEKYEQEITKLKERLRVSSRRLEEYERRLLVQEQQMQKLLLEYKARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKKDHAEMQAVIDAKQKIIDAQEKRIVSLDSANTRLMSALTQVKERYSMQVRNGISPTNPTKLSITENGEFKNSSC
Protein: Inactive beta-amylase 4, chloroplastic (Inactive beta-amylase 6) (Q9FM68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: No alpha-1,4-glucan hydrolase activity, including beta-amylase, alpha-amylase, a-glucosidase or alpha-amyloglucosidase. However, facilitates or regulates starch breakdown, especially at night, by a mechanism involving direct interaction with starch or other alpha-1,4-glucan.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18390594}.
Interaction partners:
- Phosphoglucan phosphatase LSF1, chloroplastic
- Isoamylase 3, chloroplastic
- Phosphoglucan phosphatase DSP4, chloroplastic
- Pullulanase 1, chloroplastic
Sequence:
MTETGVIGCGCRGVTGGNFFHPGGFSLKSCFLEQSTKRNRNFFRSVSMIPPFKRGRFITKLRSVAGNSRIFSMDAREKSRSFVLVSSRHKRVPVFVMMPIDTFGIDASGCPKIKRLKALTVSLKALKLAGVHGIAVEVWWGIVERFSPLEFKWSLYEELFRLISEAGLKLHVALCFHSNMHLFGGKGGISLPLWIREIGDVNKDIYYRDKSGFSNNDYLTLGVDQLPLFGGRTAVQCYEDFMLSFSTKFEPYLGNVIEEISIGLGPSGELRYPAHPSGDGRWKFPGIGEFQCHDKYMMEDLMAVASQEGKPQWGSRDPPNTGCYNSFPSGVPFFEEGNDSFLSDYGRFFLEWYSGKLICHADAILAKAADVLRRRQEEEKSSVMLVAKIGGIYWWYKTSSHPAELTAGYYNTSLRDGYDPVASVLSRHGAALNIPCLDMADSEIPEKYLCSPEGLRRQIHDVSKKWTIHVTGRNTSERFDEMGLRQIRENCVQPNGDTLRSFTFCRMNEKIFRVENWNNFVPFIRQMSADM
Protein: Alcohol dehydrogenase 6 (EC 1.1.1.1) (P28332)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm.
Interaction partners:
- Aldehyde dehydrogenase, mitochondrial
- Cytochrome P450 2E1
- Cytochrome P450 26A1
- Vasopressin-neurophysin 2-copeptin
- Catechol O-methyltransferase
- Aldehyde oxidase
- Amine oxidase [flavin-containing] B
- Amine oxidase [flavin-containing] A
- Aldehyde dehydrogenase 1A1
- Lecithin retinol acyltransferase
Sequence:
MSTTGQVIRCKAAILWKPGAPFSIEEVEVAPPKAKEVRIKVVATGLCGTEMKVLGSKHLDLLYPTILGHEGAGIVESIGEGVSTVKPGDKVITLFLPQCGECTSCLNSEGNFCIQFKQSKTQLMSDGTSRFTCKGKSIYHFGNTSTFCEYTVIKEISVAKIDAVAPLEKVCLISCGFSTGFGAAINTAKVTPGSTCAVFGLGGVGLSVVMGCKAAGAARIIGVDVNKEKFKKAQELGATECLNPQDLKKPIQEVLFDMTDAGIDFCFEAIGNLDVLAAALASCNESYGVCVVVGVLPASVQLKISGQLFFSGRSLKGSVFGGWKSRQHIPKLVADYMAEKLNLDPLITHTLNLDKINEAVELMKTGKW
Protein: Solute carrier family 7 (cationic amino acid transporter, y+ system), member 12 (D3YTZ6)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MNRVFPSIQWISSFLISAFLLGSVSCGIVSASRVFYSASQEGEFPSIYSMLNDHHSPAVADIQIVILSSVAIISSSIIYLVKYVSLGSFCINLLQMIGLLKIRYQNPDIPRPYKVWLPFIFGSIALSLFLIFTPVIQSPSIEHVYQVVFLFCGFLCYWLQANLNGHATCFDTITCYCQLLFNISPSEDPEEQKN
Protein: 3-oxoacyl-[acyl-carrier-protein] synthase 2 (EC 2.3.1.179) (3-oxoacyl-[acyl-carrier-protein] synthase II) (Beta-ketoacyl-ACP synthase II) (KAS II) (P0AAI5)
Organism: Escherichia coli (strain K12)
Function: Involved in the type II fatty acid elongation cycle. Catalyzes the elongation of a wide range of acyl-ACP by the addition of two carbons from malonyl-ACP to an acyl acceptor. Can efficiently catalyze the conversion of palmitoleoyl-ACP (cis-hexadec-9-enoyl-ACP) to cis-vaccenoyl-ACP (cis-octadec-11-enoyl-ACP), an essential step in the thermal regulation of fatty acid composition. Can use acyl chains from C-6 to C-16. Is able to catalyze the condensation reaction when CoA is the carrier for both substrates.
Interaction partners:
- Acyl carrier protein
- 3-oxoacyl-[acyl-carrier-protein] reductase FabG
- Beta-ketoacyl-[acyl-carrier-protein] synthase III
- Enoyl-[acyl-carrier-protein] reductase FabI
- Malonyl CoA-acyl carrier protein transacylase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase FabZ
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta
- Biotin carboxylase
- 3-hydroxydecanoyl-[acyl-carrier-protein] dehydratase
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase
Sequence:
MSKRRVVVTGLGMLSPVGNTVESTWKALLAGQSGISLIDHFDTSAYATKFAGLVKDFNCEDIISRKEQRKMDAFIQYGIVAGVQAMQDSGLEITEENATRIGAAIGSGIGGLGLIEENHTSLMNGGPRKISPFFVPSTIVNMVAGHLTIMYGLRGPSISIATACTSGVHNIGHAARIIAYGDADVMVAGGAEKASTPLGVGGFGAARALSTRNDNPQAASRPWDKERDGFVLGDGAGMLVLEEYEHAKKRGAKIYAELVGFGMSSDAYHMTSPPENGAGAALAMANALRDAGIEASQIGYVNAHGTSTPAGDKAEAQAVKTIFGEAASRVLVSSTKSMTGHLLGAAGAVESIYSILALRDQAVPPTINLDNPDEGCDLDFVPHEARQVSGMEYTLCNSFGFGGTNGSLIFKKI
Protein: FAD-binding domain-containing protein (Q57YQ3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Complex 1 LYR protein domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- Sulfotransferase
- Uncharacterized protein
- Flavoprotein monooxygenase, putative
- SET domain-containing protein
- NADH dehydrogenase 1 beta subcomplex subunit 7
- Uncharacterized protein
Sequence:
MFMCVHVCARAYVLSLSFFLSLRVVMYAVKPWGKVLLVGSGVGAYAMGIGMRWRESNVQLVEKRRDPSHELSNRRRCVITSQTLKLLRDLGCTNAKVERILQKAKGWRFVRPDLETIREGSIFPGCADGESVYHCAEGALQRTLRTEYLRFGGDISWETEAFDAFETGDGSGAWSLQKMYGLETEAEAIITTAKGTSLASLVIADDPDRLAVLFDEETGVSPGGRQTTERIFGAADVVIVVGSGLVIHMWHADNVITWRLIRKARREIQDLHSIALHPAIQEVLGSSTSKSSRVLIVPATTPAIKDSARDVKVSVLGDGLLPVDPFEWRGDRARCGVEEASALCRAFYGKKYHRGNVPRLLREVEQDALAKRAAILARDLRDAEHFLAVLPIIDGEDHAHTESTFSQLPK
Protein: Stevor (Q8IFL0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MLLFPFLFNTFLLSQNVNCQNNLRNKSLINNYTQRKILKSRCLAEIERPLNPHYQNDPELKKIIDQLNEEAMKKYQQSNDTYKQLHELLEKKETKSRSRNSEQEMSKIEKELLKIYEKMSGDENHIMQKSDMYTNENHKSNDKNDKSCECINKNSTDKLSSTNKVHDNYLDNLKTGFVGGLVVCALSSALVGKYGIAAAASAAKGVLQAFINALPSISSSQLTNILNGINFFYETSIKSAFTFGGITSVEYEGAASLASSTFLPYGIAIIAIIVLTIIVIILYVWLRKRRKNSWKHECKKHLCT
Protein: SRY-box-containing protein 5 (Transcription factor SOX-5) (Q3ZM07)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLTEPELPQEFNRMSSKRPASPYGGTDGEVVMATSRQRLEDEEVDGHAVIHLPLSSYCSKVSPRSPRLLDSPPTLHADMDQDGSKGLALSPYAQHNSSTSPSKQQQEDSSMRPGSEPGSASALGTPERRKGSLADVVDTLKQRKMEELIKNEPEEAPSIERLLSKDWKDKLLAMGSGNFGEIKGTPDSLAEKERQLMGMITQLSSLREQLLAAHEEQKKLAASQIEKQRQQMELAKQQQDQIARQQQQLLQQQHKINLLQQQIQQVQGQLPPLMIPVFPPDQRTLAAAAAQRGFLLPPGFNYKPGCSEPYPLQLIPTTMAAAAAATPGLGPLQLQQLYAAQLAAMQVSPGAKHSTVPQANLATGTLSPTSGQSEKNRSAPPPKPKDEGAQPLNLSSKPKASESKSPTSPASPQVPALKLGPGSLKHSAPSSIGGPPSRLSSIDLLSSITSAGYLNDHEAVTKAFQEARKMKEQLKREEQVLDAKVAAVNSLSLNNGRSEKEKAALESLSQQLKQSEESKFTHAMMDFGISGDSDGSPSVSDSRIFREARGRGSSEPHIKRPVNAFMVWAKDERRKILQAFPDMHNSNISKILGSRWKSMTNLEKQPYYEEQARLSKQHLEKYPDYKYKPRPKRTCLVDGKKLRIGEYKAIMRNRRQEMRQYFTVGQQAQLPLSSAGVVYPGALSMAGMPSPQMPSEHSSMSSSPEPVPPTSQASYFKEVEPRVKEELRMDDGNGDAYDDFDYEDDDGDYGSDSENHITQ
Protein: Peptide ABC transporter, permease protein (Q88AW7)
Organism: Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000)
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:
- Peptide ABC transporter, permease protein
- ABC-type dipeptide transporter
- Bacterial extracellular solute-binding protein, family 5
- Inner membrane ABC transporter permease protein YejB
- Inner membrane ABC transporter permease protein YejB
- ABC transporter, periplasmic substrate-binding protein
- Peptide ABC transporter, periplasmic peptide-binding protein
- ABC transporter, periplasmic substrate-binding protein
- Peptide ABC transporter, permease protein
- ABC transporter, permease protein
Sequence:
MLAYVIRRLLLIIPTLLAILIVNFLIVQAAPGGPVEQAIARIQGFSPNGVGGGGGEVAASGTASRSTRGLDPALIEQIKEHYGFDKPMHERLWLMLKNYAQLDFGTSFFRGAPVTELIAQKLPVSLSLGLWATLITYLISIPLGIRKAVRHGSAFDVWSSTLVIIGYATPAFLFAILLIVVFAGGSYLSWFPAQGLLSENFDSLSTWGKVKDYLWHLVLPVSSLVIGGFATLTILTKNSFLNEISRQYVVTARAKGLTEHRVLYGHVFRNAMLLVIAGIPQALIEVFFAGSLLIETIFGLDGLGRMSYEAAVSRDYPIVFGTLFLFTLFGLLIKLIGDLCYTLVDPRIDFSARSA
Protein: PDZ and LIM domain protein 7 (LIM mineralization protein) (LMP) (Protein enigma) (Q9NR12)
Organism: Homo sapiens (Human)
Function: May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. Involved in both of the two fundamental mechanisms of bone formation, direct bone formation (e.g. embryonic flat bones mandible and cranium), and endochondral bone formation (e.g. embryonic long bone development). Plays a role during fracture repair. Involved in BMP6 signaling pathway (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Note=Colocalizes with RET to the cell periphery and in some cytoskeletal components. Colocalizes with TPM2 near the Z line in muscle. Colocalizes with TBX4 and TBX5 to actin filaments (By similarity). {ECO:0000250}.
Interaction partners:
- E3 ubiquitin-protein ligase SMURF1
- Tropomyosin beta chain
- Proteasome subunit beta type-9
- Proto-oncogene tyrosine-protein kinase receptor Ret
- PDZ and LIM domain 5
- NEDD4-like E3 ubiquitin-protein ligase WWP2
- PDZ and LIM domain protein 2
- Alpha-actinin-1
- Drebrin
- T-box transcription factor TBX4
Sequence:
MDSFKVVLEGPAPWGFRLQGGKDFNVPLSISRLTPGGKAAQAGVAVGDWVLSIDGENAGSLTHIEAQNKIRACGERLSLGLSRAQPVQSKPQKASAPAADPPRYTFAPSVSLNKTARPFGAPPPADSAPQQNGQPLRPLVPDASKQRLMENTEDWRPRPGTGQSRSFRILAHLTGTEFMQDPDEEHLKKSSQVPRTEAPAPASSTPQEPWPGPTAPSPTSRPPWAVDPAFAERYAPDKTSTVLTRHSQPATPTPLQSRTSIVQAAAGGVPGGGSNNGKTPVCHQCHKVIRGRYLVALGHAYHPEEFVCSQCGKVLEEGGFFEEKGAIFCPPCYDVRYAPSCAKCKKKITGEIMHALKMTWHVHCFTCAACKTPIRNRAFYMEEGVPYCERDYEKMFGTKCHGCDFKIDAGDRFLEALGFSWHDTCFVCAICQINLEGKTFYSKKDRPLCKSHAFSHV
Protein: Growth hormone (H6ULX7)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613, ECO:0000256|RuleBase:RU003618}.
Interaction partners:
Sequence:
MAPGSWFSPLLIAVVTLGLPHETVATFPTMPLSNMFANAVLRAQHLHLLAAETYKEFERTYIPEDQRYTNKNSQAAFCYSETIPAPTGKDDAQQKSDMELLRFSLVLIQSWLTPVQYLSKVFTNNLVFGTKKRVFEKLKDLEEGLQPLMRELEDRSPRGPQLLRPTYDKFDIHLRHGDALLNNYGLLSCFKKDLHKVETYLKVMKCRRFGESNCTI
Protein: Ammonium transporter Rh type B (Rhesus blood group family type B glycoprotein) (Rh family type B glycoprotein) (Rh type B glycoprotein) (Q68FT6)
Organism: Rattus norvegicus (Rat)
Function: Functions as a specific ammonium transporter.
Subcellular location: Basolateral cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MARIPRHRRLVLPLLCLLFQGATSLLFAIFVRYNHETDAALWHWGNHSNVDNEFYFRYPSFQDVHVMVFVGFGFLMVFLQRYGFSSVGFTFLVATFTLQWATLLQGFLHSFHGGHIHIGVESLINADFCAGAVLISFGAVLGKTGPAQLLLMALLEAVLFSVNEFILLSLLGVRDAGGSMTIHTFGAYFGLFLSRVLYRSQLEKSRHRQTSVYNSDLFAMIGTIFLWVFWPSFNSAPTALGDGQHRTVVNTYYSLTASTLSTFALSALVSGDGRLDMVHIQNAALAGGVVVGTASEMMLTPFGALAAGFLAGTVSTLGYKFFTPILESRFKLQDTCGVHNLHGMPGLLGAILGVLVAALATHEAYGDGLQTVFPLIAKGQRSATSQAMYQLFGMFVTLVFASVGGSLGGLLLKLPFLDSPPDSQCFEDQVYWEVPGEQEAETQRPLRTEEPDTQA
Protein: GATOR complex protein NPRL3 (Nitrogen permease regulator 3-like protein) (Q9VUB4)
Organism: Drosophila melanogaster (Fruit fly)
Function: An essential component of the GATOR subcomplex GATOR1 which functions as an inhibitor of the amino acid-sensing branch of the TORC1 signaling pathway. The two GATOR subcomplexes, GATOR1 and GATOR2, regulate the TORC1 pathway in order to mediate metabolic homeostasis, female gametogenesis and the response to amino acid limitation and complete starvation. The function of GATOR1 in negatively regulating the TORC1 pathway is essential for maintaining baseline levels of TORC1 activity under nutrient rich conditions, and for promoting survival during amino acid or complete starvation by inhibiting TORC1-dependent cell growth and promoting catabolic metabolism and autophagy. In addition, this inhibition of TORC1 is necessary to maintain female fertility under normal conditions and during periods of nutrient stress. GATOR1 and GATOR2 act at different stages of oogenesis to regulate TORC1 in order to control meiotic entry and promote oocyte growth and development. After exactly four mitotic cyst divisions, the GATOR1 complex members (Iml1, Nprl2 and Nprl3) down-regulate TORC1 to slow cellular metabolism and promote the mitotic/meiotic transition. At later stages of oogenesis, the mio and Nup44A components of the GATOR2 complex inhibit GATOR1 and thus activate TORC1 to promote meiotic progression, and drive oocyte growth and development.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24786828}. Lysosome {ECO:0000269|PubMed:24786828, ECO:0000269|PubMed:25512509}. Note=Localizes primarily to the autolysosomes during amino-acid starvation (PubMed:24786828). {ECO:0000269|PubMed:24786828}.
Interaction partners:
- GATOR2 complex protein Wdr24
- GATOR2 complex protein Wdr59
- GH04846p
- GATOR complex protein Iml1
- GATOR complex protein NPRL2
- GATOR2 complex protein Mio
- Protein SEC13 homolog
- Nucleoporin seh1
- GH16429p
- FI04419p
Sequence:
METNVNPLAVILVYFDSKGDRLLYRYPYQTLGQTEVANDEQRKSRKRNPYAVANTDDLLQTPTHLGAAKSQGQLQGFADEVLSALFAVKPQLCNQKFELKLNDVRFVSHPTLIPQKEQRSGPMAKQQMLINIVFALHAQASYSIVKCYHELSKRLGLALKFEEQRSGYLTEQTAQMARTHDEQQQQPLERTLELIAERCSLAQALRSIFHDLCTTGLLSTSLNHNLTLCFCLPAKAHQLHKKGSMVDPETIDRCLRALKPYHGMLLLVDFAELLDCVPPTGARMLWQLVDVYDPLISLQSMSSNADLSIEHVYKLVSHLVYWAKATIIYPLCETNVYVIAPDAPLHTKSHLVEKFSARFAGMSLFEVISDFSLPTSIGHLTTPLQQPARQGILAQMVIWMLQHHLLMQLHTYVQFMPSEDEFGDSASCSNHLRDAISDEEGDQEPDADELHGSMLSMSSHPLPVPAVLVGGHRREASEDHSSLASDNIAVQPSSSHKSNFSITASMSTDNCDSLDSMEDEQKLKELLQVFSDADRAAIRRIPASANVDDLSLLVKLYQMGYFKSEHHLEEIMYFENLRRSQLLQLLDKFRDVLIIYETEDPAIASMYNTK