wanglab/gogpt-training-data huggingface dataset:
Protein: Polyamine oxidase 3 (AtPAO3) (EC 1.5.3.17) (Q9LYT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Flavoenzyme involved in polyamine back-conversion. Catalyzes the oxidation of the secondary amino group of polyamines, such as spermine, spermidine and their acetyl derivatives. Substrate preference is spermidine > spermine > N(1)-acetylspermidine > N(1)-acetylspermine. Plays an important role in the regulation of polyamine intracellular concentration (Probable). Involved in the production of hydrogen peroxide during pollen tube growth. Hydrogen peroxide triggers the opening of the hyperpolarization-activated calcium permeable channels in pollen, and thus regulates pollen tube growth.
Subcellular location: Peroxisome {ECO:0000269|PubMed:18583528, ECO:0000269|PubMed:18703589}.
Interaction partners:
- Spermine synthase
- Spermidine synthase 2
- Spermidine synthase 1
- Aldehyde dehydrogenase family 3 member H1
- N-carbamoylputrescine amidase
- Probable polyamine oxidase 5
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
- Aldehyde dehydrogenase family 3 member F1
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
- Polyamine oxidase 1
Sequence:
MESGGKTNRQLRKAICVSTDEKMKKKRSPSVIVIGGGMAGISAARTLQDASFQVVVLESRDRIGGRVHTDYSFGFPVDLGASWLHGVCKENPLAAVIGRLGLPLYRTSGDNSVLYDHDLESYALFDKAGNQVSQELVTKVGENFEHILEEICKVRDEQDEDMSIAQAFSIVFKRNPELRLEGLAHNVLQWYLCRMEGWFAADAETISAKCWDQEELLPGGHGLMVRGYRPVINTLSKGLDIRLSHRITKISRRYSGVKVTTEKGDTFVADAAVIALPLGVLKSGMITFEPKLPQWKQEAINDLGVGIENKIILNFDNVFWPNVEFLGVVAETSYGCSYFLNLHKATSHPVLVYMPAGQLARDIEKKSDEAAANFAFSQLQKILPDASSPINYLVSRWGSDINSLGSYSYDIVNKPHDLYERLRVPLDNLFFAGEATSSSYPGSVHGAYSTGVLAAEDCRMRVLERYGELEHEMEEEAPASVPLLISRM
Protein: Fibroblast growth factor receptor 1 (FGFR-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (BFGFR) (bFGF-R-1) (Fms-like tyrosine kinase 2) (FLT-2) (N-sam) (Proto-oncogene c-Fgr) (CD antigen CD331) (P11362)
Organism: Homo sapiens (Human)
Function: Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle. Note=After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi apparatus to the cytosol, and from there to the nucleus.
Interaction partners:
- Fibroblast growth factor 18
- Fibroblast growth factor receptor substrate 2
- Fibroblast growth factor 23
- Fibroblast growth factor 3
- Fibroblast growth factor 6
- Fibroblast growth factor 20
- Fibroblast growth factor 1
- Klotho
- Fibroblast growth factor 16
- Fibroblast growth factor 10
Sequence:
MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR
Protein: Asparagine synthetase domain-containing protein (Q21555)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable delta-1-pyrroline-5-carboxylate synthase
- glutamate synthase
- Glutamyl-tRNA
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Probable ornithine aminotransferase, mitochondrial
- Glutamate dehydrogenase
- asparaginase
- Alanine--glyoxylate aminotransferase
- Probable fumarate hydratase, mitochondrial
Sequence:
MGIDYNRWWHLKDETLGEELKGYIKMIEEDYLVYSGTTSQLHVSKLSNGSVNSIVNEILEQQGSWSIIYYNQKLKKLFIGRDVFGRQSLVFNFESMIFGCRTKPETSGKWIEIPFGQVTVFSLDSTDPVIYSYLDEYPENVLDGYFSGSDISRIVVNKKHGLLNVSRSTGGEIDSFNTKDLFQKVIDATKILLKNYHESHVAVCLSGGVDSTFVAHVVHSSVPENMQIDLINVAFGNSEKECEQAPDRKRARKALESFRTAYPTRQFRLILVNVDSQTLEVNRKESISDAAQPASSVLDDSLSCVLWFAVRAEGVDSENQQSVRSPATTCLLGSGADELLAGYARHRTRFEKEQIPENVAEECENELRRLGSRNGGRDARVAAQLGKTILSPLLEDTVVTWLNALPVDSKWDLSLPRGVGEKQLLRETVKMLGSPYDAPKQAMQFGSRMAKMSNAGDNSIKGSDKSPHLLKTDVN
Protein: Ribosomal RNA small subunit methyltransferase NEP1 (EC 2.1.1.-) (18S rRNA (pseudouridine-N1)-methyltransferase) (Ribosome biogenesis protein NEP1) (Q9W4J5)
Organism: Drosophila melanogaster (Fruit fly)
Function: S-adenosyl-L-methionine-dependent pseudouridine N(1)-methyltransferase that methylates a pseudouridine in 18S rRNA. Involved the biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi) conserved in eukaryotic 18S rRNA. Has also an essential role in 40S ribosomal subunit biogenesis independent on its methyltransferase activity, facilitating the incorporation of ribosomal protein S19 during the formation of pre-ribosomes.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q92979}.
Interaction partners:
- Nucleolar protein 14 homolog
- Nucleolar protein 58
- KRR1 small subunit processome component homolog
- RE67794p
- Nucleolar protein 6
- LD10780p
- Bystin
- rRNA-processing protein FCF1 homolog
- Lethal
- HEAT repeat-containing protein 1 homolog
Sequence:
MGGQGKAINRKRKFVGRKADDPEFDLDKKQFKVLHLNATEKRLIIVLEGAQLETVKVHNTFELLNCDDHAGIMRKNQRDPGSCRPDITHQCLLMLFDSPLNRAGLLQVFVRTEHNVLIEINPQTRIPRTFKRFAGLMVQLLHKFQIRANDSSRRLMSVIKNPITDHVPVGCKKYAMSFSGKLLPNCRDLVPHGDETSASYDEPVVIVIGAFAHGVLKTDYTEELFSISNYPLSAAIACSKICSAFEEVWGVV
Protein: Regulator of V-ATPase in vacuolar membrane protein 2 (RAVE complex subunit rav2) (O74387)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the RAVE complex which is required for stable assembly of the vacuolar ATPase complex V-ATPase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Regulator of V-ATPase in vacuolar membrane protein 1
- Suppressor of kinetochore protein 1
- V-type proton ATPase subunit E
- V-type proton ATPase subunit B
- V-type proton ATPase subunit c'
- Oxysterol-binding protein homolog C23H4.01c
Sequence:
MQTEIDASVIVKEKEWLETNVLPEFWESMSEGLKEALNLISSDDPTVLVFTSPKTDAVKGIVSRSSSNVVRVNVTAKVGRTTHVLKLKDSAIIHLDQILNLSNYMHYALYCLPRLRHNTERAIKELQEILHAIVCLLHSIMQEESEKEEIPSNASSISLKSQNSIVSRTSNPFSCLNHSPRQIHKTVRNHLFSPPLPSNLALSFSISNASVCLHLFRLSGPNEVLESFAKNSVDIEMLKPFVSQRIDAFSQDPILLAVTAKLSALQKKVNDVSYRFKTISSSLYGAK
Protein: Epithelial cell-transforming 2 (Protein ECT2 isoform X2) (A0A2R8Q1Z1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MADSSILTLGPGRSILVDSSVYDSRMAETSKEQYFIGLHSDETEGVLPRVETRVVLVGEACKMAELEKALQDLNTPCIKTDNVCDFGDGENCEFETVFVLKDFQAPEYSFLYKNDSRILGPPAVMHCANKGEPLPFSSRPLYSMTMLNLSLCFTGFRKKDEVVALVNLVHHMGGTIRKDFDSAKVTHLIARSTHGEKYRLAVCMGTPILTPDWIRKAWEHRDDINFHAGNELFRTEFKVPPFQDCVLSFLGFSEEEKNNMEERTQKHGGRFQAVGDERCTHLVVEENSIKELPFTPSKRLYVVKQEWFWGSIQMDARAGESMYSYEKPESPAMKKAVSLLSLTTPNSGRKRRRLRETLAQLTKETEISPFPPRKRPSAEHSLSMGSLLDISNTPDTKSSGERRCRRSSGRRRSSRQSRSERLQRTSTPVCRHEDQTENAKIPKSSTPALPKQSARWQVSKELYQTESNYVDILATVLQLFKYPLEKEGQVGGPILAQEEIKTIFGSIPDIYEVHTRIKADLEELVMNWSEERSVGDIILKYSGELVKAYPPFVNFFEMSKETIVRCERQKPRFHAFLKINQSKPECGRQTLVELLIRPVQRLPSVALLLNDIKKHTSDDNPDKLTLEKAIESLKEVMTHINEDKRKTEGQKQIFDVVYEVDGCPANLLSSHRSLVHRVETIALGDKPCDRGEHVTLFLFNDCLEIARKRHKVITNFRSPLGQTRPPAQLKHITLMPLSQIRRVLDIQDTEECQNAFALVVRPPTEQENLLFSFQLTAEDTLKTTWLRTLCRQVANTICRADAEDLIQSTDPDSVQVSTKDMDSTLSRASRAIKKTSKKVTRAFSFTKTPKRVLQRAFMANGTPDERSPCPDADRMSRMSSSSTLAMSRSASTFSLTGSIKSAVVQRSNSLDHAPRPRVPVCVRTPCSPERADEPAAPKSQLRPSILSLPAVQPVAKCRDLLAPPEPGRRLPGSPRRETLL
Protein: Ubiquitin-conjugating enzyme E2 Q2 (EC 2.3.2.23) (E2 ubiquitin-conjugating enzyme Q2) (Ubiquitin carrier protein Q2) (Ubiquitin-protein ligase Q2) (Q8WVN8)
Organism: Homo sapiens (Human)
Function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16300736}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 Q1
- Ubiquitin-conjugating enzyme E2Q-like protein 1
- Ubiquitin-like modifier-activating enzyme 1
Sequence:
MSVSGLKAELKFLASIFDKNHERFRIVSWKLDELHCQFLVPQQGSPHSLPPPLTLHCNITESYPSSSPIWFVDSEDPNLTSVLERLEDTKNNNLLRQQLKWLICELCSLYNLPKHLDVEMLDQPLPTGQNGTTEEVTSEEEEEEEEMAEDIEDLDHYEMKEEEPISGKKSEDEGIEKENLAILEKIRKTQRQDHLNGAVSGSVQASDRLMKELRDIYRSQSYKTGIYSVELINDSLYDWHVKLQKVDPDSPLHSDLQILKEKEGIEYILLNFSFKDNFPFDPPFVRVVLPVLSGGYVLGGGALCMELLTKQGWSSAYSIESVIMQINATLVKGKARVQFGANKNQYNLARAQQSYNSIVQIHEKNGWYTPPKEDG
Protein: Response regulator aspartate phosphatase J (EC 3.1.3.-) (O34327)
Organism: Bacillus subtilis (strain 168)
Function: Involved in the regulation of sporulation (Probable). Acts as a phosphatase that specifically dephosphorylates the sporulation initiation phosphotransferase Spo0F and inhibits its activity.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Competence and sporulation stimulating factor
- Sporulation initiation phosphotransferase F
- RapF inhibitor
- Uncharacterized transporter YetK
Sequence:
MRAKIPSEEVAVKLNEWYKLIRAFEADQAEALKQEIEYDLEDMEENQDLLLYFSLMEFRHRIMLDKLMPVKDSDTKPPFSDMLNEIESNQQKLTGLLEYYFYYFRGMYEFKQKNFILAIDHYKHAEEKLEYVEDEIEKAEFLFKVAEVYYHIKQTYFSMNYASQALDIYTKYELYGRRRVQCEFIIAGNLTDVYHHEKALTHLCSALEHARQLEEAYMIAAAYYNVGHCKYSLGDYKEAEGYFKTAAAIFEEHNFQQAVQAVFSLTHIYCKEGKYDKAVEAYDRGIKSAAEWEDDMYLTKFRLIHELYLGSGDLNVLTECFDLLESRQLLADAEDLLHDTAERFNQLEHYESAAFFYRRLMNIKKKLAEQRFQ
Protein: DCN1-like protein 2 (DCNL2) (DCUN1 domain-containing protein 2) (Defective in cullin neddylation protein 1-like protein 2) (Q6PH85)
Organism: Homo sapiens (Human)
Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes and plays an essential role in the regulation of SCF (SKP1-CUL1-F-box protein)-type complexes activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26906416}. Nucleus {ECO:0000269|PubMed:26906416}.
Interaction partners:
- Cullin-3
- NEDD8-conjugating enzyme Ubc12
- Cullin-2
- Cullin-4B
- Cullin-4A
- NEDD8-conjugating enzyme UBE2F
- Cullin-1
- E3 ubiquitin-protein ligase RBX1
- NEDD8-activating enzyme E1 catalytic subunit
- Cullin-5
Sequence:
MHKLKSSQKDKVRQFMACTQAGERTAIYCLTQNEWRLDEATDSFFQNPDSLHRESMRNAVDKKKLERLYGRYKDPQDENKIGVDGIQQFCDDLSLDPASISVLVIAWKFRAATQCEFSRKEFLDGMTELGCDSMEKLKALLPRLEQELKDTAKFKDFYQFTFTFAKNPGQKGLDLEMAVAYWKLVLSGRFKFLDLWNTFLMEHHKRSIPRDTWNLLLDFGNMIADDMSNYDEEGAWPVLIDDFVEYARPVVTGGKRSLF
Protein: C3H1-type domain-containing protein (Q54MG5)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Transportin
- Uncharacterized protein
- Ribosomal RNA-processing protein 43
- 14-3-3-like protein
- Probable serine/threonine-protein kinase DDB_G0288795
- RAC family serine/threonine-protein kinase homolog
- 5'-3' exoribonuclease
- mRNA-decapping enzyme 2
- phosphatidylinositol-3,4,5-trisphosphate 5-phosphatase
Sequence:
MNNNNSNNNTNNTNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSNTNNNVNPLKSSNGIMKPSNGSNTNTTTSTPTHSKHPPLLHTQSYSQLQVPSSIKNSQFINISNHINSGDNANWLSNSDSLVQPPLKRGLIKAYSDADIQPPLSVQQHHQQQQMLQQAQQDLENEQEDIEDEINGQNRYKTELCRSFQETGVCRYGLKCQFAHGRDELRSVMRHPKYKTETCKTFYSIGSCPYGSRCRFIHTRDPELPIHLMSQLSTSSGSISPPNQTSNNNNNTTNGNNTPASFATEVLLSKTIVPQMIRQHSSPQLQTPLHILQQQKELQQQQKDKESQLNKEKESNNKESSSSSIKSQPSTPQTQSQSSSHPTTVHWSNSWSSDEASSTAPNSSFNQLKSSAPPILKKEDSSKRLAIFKTICSNSTW
Protein: Transcription factor Sox-17-alpha-A (Xsox17alpha) (xSox17alpha1) (Q3KQ35)
Organism: Xenopus laevis (African clawed frog)
Function: Transcriptional activator. Binds to the DNA sequence 5'-AACAAT-3' (By similarity). All of the sox17 proteins are required for embryonic endoderm development and gastrulation movements, and show some redundancy in function. In addition, the sox17 proteins have distinct but overlapping roles in later gut development. Acts downstream of vegt-signaling in endoderm differentiation to induce a range of endodermal genes both directly (including endodermin and dhh/chh) and indirectly. Also represses wnt-responsive genes to inhibit wnt/beta-catenin signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:9363948}.
Interaction partners:
Sequence:
MSSPDGGYASDDQNQGKCSVPIMMTGLGQCQWAEPMTSLGEGKLKSDAGSANSRSKAEARIRRPMNAFMVWAKDERKRLAQQNPDLHNAELSKMLGKSWKSLTLAEKRPFVEEAERLRVQHMQDHPNYKYRPRRRKQVKRMKRAENGFMHMAEAQESAVLGADGRMCLENFSLGYHEQTYPHGQVPQSSHYREPQAVAPHYDGYSLPTPESSPLDLAEADPVFFTSPAQDECQMMPYSYNGSYPHQQNSMLVRQMPQTEQMGQVSPVQGMMACQSSPHMYYGQMYLPGSARHHQLHQAGQPSPPPEAQQMGRADHIQPADMLAEVDRTEFEQYLSYVAKSDLGMHYHAQESVVPTADNGPISSVLSDASTAVYYCNYPSA
Protein: ABC transporter I family member 6, chloroplastic (ABC transporter ABCI.6) (AtABCI6) (ABC transporter ATPase) (Non-intrinsic ABC protein 7) (AtNAP7) (Plastid SufC-like protein) (Q9CAF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Required during embryo development, especially at early stages. Involved in chloroplast differentiation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15184673}.
Interaction partners:
- Iron-sulfur cluster assembly SufBD family protein ABCI8, chloroplastic
- Protein ABCI7, chloroplastic
- Iron-sulfur cluster assembly SufBD family protein ABCI9
- Protein TRIGALACTOSYLDIACYLGLYCEROL 3, chloroplastic
- Cysteine desulfurase 1, chloroplastic
- ABC transporter I family member 17
- Protein TRIGALACTOSYLDIACYLGLYCEROL 1, chloroplastic
- ABC transporter I family member 20
- Cytochrome C assembly protein
- ABC transporter I family member 19
Sequence:
MAGVNLQLRHAYSIAQFVPTVSSPPPLPTQRVRLGTSPSRVLLCNLRANSAAAPILRTTRRSVIVSASSVSSAVDSDSLVEDRDDVGRIPLLEVRDLRAVIAESRQEILKGVNLVVYEGEVHAVMGKNGSGKSTFSKVLVGHPDYEVTGGSIVFKGQNLLDMEPEDRSLAGLFMSFQSPVEIPGVSNMDFLNMAFNARKRKLGQPELDPIQFYSHLVSKLEVVNMKTDFLNRNVNEGFSGGERKRNEILQLAVLGAELAILDEIDSGLDVDALQDVAKAVNGLLTPKNSVLMITHYQRLLDYIKPTLIHIMENGRIIKTGDNSLAKLLEKEGYKAISG
Protein: Probable pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH3 (EC 3.6.4.13) (DEAH RNA helicase homolog PRP43) (O22899)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in pre-mRNA splicing.
Interaction partners:
- U2 small nuclear ribonucleoprotein A'
- Small nuclear ribonucleoprotein Sm D2
- Pre-mRNA-splicing factor SYF2
- DEAD-box ATP-dependent RNA helicase 28
- Protein THALLO
- Something about silencing protein
- DNA-damage-repair/toleration protein 111
- Septin and tuftelin-interacting protein 1 homolog 1
- Transducin/WD40 repeat-like superfamily protein
- G-patch domain-containing protein 1
Sequence:
MGTERKRKVSLFDVMEDPSLSSKNTKSNGLGLAAAAGGGSNLINKWNGKAYSQRYFEILEKRRDLPVWLQKDDFLNTLNSNQTLILVGETGSGKTTQIPQFVLDAVVADNSDKGRKWLVGCTQPRRVAAMSVSRRVADEMDVSIGEEVGYSIRFEDCTSSRTMLKYLTDGMLLREAMADPLLERYKVIILDEAHERTLATDVLFGLLKEVLRNRPDLKLVVMSATLEAEKFQEYFSGAPLMKVPGRLHPVEIFYTQEPERDYLEAAIRTVVQIHMCEPPGDILVFLTGEEEIEDACRKINKEVSNLGDQVGPVKVVPLYSTLPPAMQQKIFDPAPVPLTEGGPAGRKIVVSTNIAETSLTIDGIVYVIDPGFAKQKVYNPRIRVESLLVSPISKASAHQRSGRAGRTRPGKCFRLYTEKSFNNDLQPQTYPEILRSNLANTVLTLKKLGIDDLVHFDFMDPPAPETLMRALEVLNYLGALDDEGNLTKTGEIMSEFPLDPQMSKMLIVSPEFNCSNEILSVSAMLSVPNCFVRPREAQKAADEAKARFGHIDGDHLTLLNVYHAYKQNNEDPNWCFENFVNNRAMKSADNVRQQLVRIMSRFNLKMCSTDFNSRDYYVNIRKAMLAGYFMQVAHLERTGHYLTVKDNQVVHLHPSNCLDHKPEWVIYNEYVLTTRNFIRTVTDIRGEWLVDVAQHYYDLSNFPNCEAKRALEKLYKKREREKNESKNRK
Protein: Flagellar FliJ protein (P52613)
Organism: Escherichia coli (strain K12)
Function: The FliJ protein is a flagellar protein that affects chemotactic events. Mutations in FliJ results in failure to respond to chemotactic stimuli.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Flagellar M-ring protein
- Flagellar protein FliO
- Flagellum-specific ATP synthase
- Flagellar hook-length control protein
- Flagellar assembly protein FliH
- Flagellar protein FliL
- Flagellar motor switch protein FliM
- Flagellar motor switch protein FliG
- Flagellar biosynthetic protein FliP
- Flagellar biosynthetic protein FliQ
Sequence:
MAEHGALATLKDLAEKEVEDAARLLGEMRRGCQQAEEQLKMLIDYQNEYRNNLNSDMSAGITSNRWINYQQFIQTLEKAITQHRQQLNQWTQKVDIALNSWREKKQRLQAWQTLQERQSTAALLAENRLDQKKMDEFAQRAAMRKPE
Protein: Ionotropic receptor 64a (Q9VRL4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Ionotropic receptor 8a
- Ionotropic receptor 25a
- IP13856p
- Ionotropic receptor 93a
- Ionotropic receptor 40a
- Ionotropic receptor 41a
- Ionotropic receptor 21a
- Ionotropic receptor 92a
- Ionotropic receptor 68a, isoform A
- Ionotropic receptor 60a
Sequence:
MHWWLLVFLPLSCQGLPEHELLELELDYGLAEPQRTSLLQSSLILQFSQDYKHIPRITYFTCQKPHLQTPNQIPNAAEHRDAFAAKNFQLIKSLYESELFVRIVLLDVLAQSPTSGRPNRPGNGPTGGFSQTPSQAQSNSEWLEGVLRMEALRQIAVVDLACGAVSRRFLELASAKMLYSEKFHWLLIEDFAWHGRTQTAEGSGKRDDGEMEEEEPPGQQIQATDDEDLPSIESFLGGMNLYMNTELTLAKRMSEAAHYTLFDVWNPGLNYGGHVNLTEIGSFTPTEGIQLHTWFRTTSTVRRRMDMQHARVRCMVVVTNKNMTGTLMYYLTHTMSGHIDTMNRFNFNLLMAVRDMFNWTFVLSRTTSWGYVKNGRFDGMIGALIRNETDIGGAPIFYWLERHKWIDVAGRSWSSRPCFIFRHPRSTQKDRIVFLQPFTNDVWILIVGCGVLTVFILWFLTTIEWKLVPHDGSALIKPKGGAPPRHHYQQQQQQEQVEAPVRPITAVSVVVSKEKVEEKQEEYEDSTPIDAGTLWQRCYQKLNKYIKDRKAKQKKAPERVGLFLESVLFFVGIICQQGLGFSTSFVSGRCIVITSLLFSFCIYQFYSASIVGTLLMEKPKTIKTLSDLVHSSLKVGMEDILYNRDYFLHTKDPVSMELYAKKITSVPTTKENEADEDEPVDPNPVSTDPAKSYRDIVHSHETGAHAKDNAASNWLDPETGLLRHLGFAFHVDVAAAYKIIAETFSEQDICDLTEVSMFPPQKTVSIMQKNSPMRKVISYGLRRVTETGILTYHFNVWHSRKPPCVKKIETSDLHVDMDTVSSALLILLFSYAITLMILGTEILYSKWHNRIQLKWVGAT
Protein: Transmembrane protein 59 (Liver membrane-bound protein) (Q9BXS4)
Organism: Homo sapiens (Human)
Function: Acts as a regulator of autophagy in response to S.aureus infection by promoting activation of LC3 (MAP1LC3A, MAP1LC3B or MAP1LC3C). Acts by interacting with ATG16L1, leading to promote a functional complex between LC3 and ATG16L1 and promoting LC3 lipidation and subsequent activation of autophagy. Modulates the O-glycosylation and complex N-glycosylation steps occurring during the Golgi maturation of several proteins such as APP, BACE1, SEAP or PRNP. Inhibits APP transport to the cell surface and further shedding.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:23376921, ECO:0000269|PubMed:27273576}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:23376921, ECO:0000269|PubMed:27273576}; Single-pass type I membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:23376921}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:20427278}; Single-pass type I membrane protein {ECO:0000255}. Note=Mainly localizes to late endosomes/lysosomes. Probably first exported to the cell surface and then actively endocytosed to transiently localize in early endosomes on its way to the late endosomal/lysosomal compartment where it becomes quickly degraded. {ECO:0000269|PubMed:23376921}.
Interaction partners:
- Autophagy-related protein 16-1
Sequence:
MAAPKGSLWVRTQLGLPPLLLLTMALAGGSGTASAEAFDSVLGDTASCHRACQLTYPLHTYPKEEELYACQRGCRLFSICQFVDDGIDLNRTKLECESACTEAYSQSDEQYACHLGCQNQLPFAELRQEQLMSLMPKMHLLFPLTLVRSFWSDMMDSAQSFITSSWTFYLQADDGKIVIFQSKPEIQYAPHLEQEPTNLRESSLSKMSYLQMRNSQAHRNFLEDGESDGFLRCLSLNSGWILTTTLVLSVMVLLWICCATVATAVEQYVPSEKLSIYGDLEFMNEQKLNRYPASSLVVVRSKTEDHEEAGPLPTKVNLAHSEI
Protein: At3g02900 (F13E7.15 protein) (Low-density receptor-like protein) (Q9M8T2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MASLVAAPISFSGDSHVKAHRNFNAIRKSSTLTVQTKSNRSHKLSVSAGYRGGSKGGGSSDFVTGFLLGSAVFGTLAYIFAPQIRRSVLSENEYGFKKPEQPMYYDEGLEERREILNEKIGQLNSAIDKVSSRLKGGRSGSSKNTSSPSVPVETDAEAEATA
Protein: Glycine cleavage system transcriptional repressor (gcv operon repressor) (P0A9I3)
Organism: Escherichia coli (strain K12)
Function: Negative transcriptional regulator of the glycine cleavage system operon (GCV). Does not autoregulate its own expression. It is not yet known how GcvR acts as a repressor. It does not seem to bind DNA. It could interact with GcvA and suppress its activatory activity.
Subcellular location: Cytoplasm.
Interaction partners:
- Glycine cleavage system transcriptional activator
- Peroxiredoxin Bcp
- 4-hydroxy-tetrahydrodipicolinate synthase
- Aminomethyltransferase
Sequence:
MTLSSQHYLVITALGADRPGIVNTITRHVSSCGCNIEDSRLAMLGEEFTFIMLLSGSWNAITLIESTLPLKGAELDLLIVMKRTTARPRPPMPASVWVQVDVADSPHLIERFTALFDAHHMNIAELVSRTQPAENERAAQLHIQITAHSPASADAANIEQAFKALCTELNAQGSINVVNYSQHDEQDGVK
Protein: tRNA (guanine-N(7)-)-methyltransferase non-catalytic subunit WDR4 (Protein Wuho homolog) (hWH) (WD repeat-containing protein 4) (P57081)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of a methyltransferase complex required for the formation of N(7)-methylguanine in a subset of RNA species, such as tRNAs, mRNAs and microRNAs (miRNAs). In the methyltransferase complex, it is required to stabilize and induce conformational changes of the catalytic subunit. Required for the formation of N(7)-methylguanine at position 46 (m7G46) in tRNA. Also required for the formation of N(7)-methylguanine at internal sites in a subset of mRNAs. Also required for methylation of a specific subset of miRNAs, such as let-7. Independently of METTL1, also plays a role in genome stability: localizes at the DNA replication site and regulates endonucleolytic activities of FEN1.
Subcellular location: Nucleus {ECO:0000269|PubMed:15861136, ECO:0000269|PubMed:26751069}. Chromosome {ECO:0000269|PubMed:26751069}. Note=Localizes at the site of nascent DNA synthesis. {ECO:0000269|PubMed:26751069}.
Interaction partners:
- tRNA
- tRNA
- Pseudouridylate synthase 1 homolog
- tRNA
- tRNA
- tRNA methyltransferase 10 homolog C
- tRNA methyltransferase 10 homolog A
- tRNA
- Pescadillo homolog
- tRNA pseudouridine
Sequence:
MAGSVGLALCGQTLVVRGGSRFLATSIASSDDDSLFIYDCSAAEKKSQENKGEDAPLDQGSGAILASTFSKSGSYFALTDDSKRLILFRTKPWQCLSVRTVARRCTALTFIASEEKVLVADKSGDVYSFSVLEPHGCGRLELGHLSMLLDVAVSPDDRFILTADRDEKIRVSWAAAPHSIESFCLGHTEFVSRISVVPTQPGLLLSSSGDGTLRLWEYRSGRQLHCCHLASLQELVDPQAPQKFAASRIAFWCQENCVALLCDGTPVVYIFQLDARRQQLVYRQQLAFQHQVWDVAFEETQGLWVLQDCQEAPLVLYRPVGDQWQSVPESTVLKKVSGVLRGNWAMLEGSAGADASFSSLYKATFDNVTSYLKKKEERLQQQLEKKQRRRSPPPGPDGHAKKMRPGEATLSC
Protein: BTB domain-containing protein (Q8BSY6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MSTQEERQINTEYAVSLLEQLKLFYEQQLFTDIVLIVEGTEFPCHKMVLATCSSYFRAMFMSGLSESKQTHVHLRNVDAAALQMIIAYAYTGNLAVNDSTVEQLYETACFLQVEDVLQRCREYLIKKINAENCVRLLSFADLFSCEELKQSAKRMVEHKFTAVYRQEAFMQLSHDLLIDILSSDNLNVEKEETVREAAMLWLEYNTESRSQYLSSVLSQIRIDALSEVTQRAWFQGLPPNDKSVVVQGLYKSMPKFFKPRLGMTKEEMMIFIEASSENPCSLYSSVCYSPQAEKVYKLCSPPADLHKVGTVVTPDNDIYIAGGQVPLKNTKTNHSKTSKLQTAFRTVNCFYWFDAQQNTWFPKTPMLFVRVKPSLVCCEGYIYAIGGDSVGGELNRRTVERYDTEKDEWTMVSPLPCAWQWSAAVVVHDCIYVMTLNLMYCYFPRSDSWVEMAMRQTSGSFASAAAFGDKIFYIGGLHIATNSGIRLPSGTVDGSSVTVEIYDVNKNE