wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-binding cassette sub-family C member 8 isoform X2 (A0A1U7R319)
Organism: Mesocricetus auratus (Golden hamster)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 11
- ATP-sensitive inward rectifier potassium channel 8
- Rap guanine nucleotide exchange factor 4
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- Rap guanine nucleotide exchange factor 3
- G protein-activated inward rectifier potassium channel 2
- Syntaxin-1A
- ATP-sensitive inward rectifier potassium channel 1 isoform X1
- ATP-sensitive inward rectifier potassium channel 12 isoform X2
Sequence:
MPLAFCGTENHSAAYRVDQGVLNNGCFVDALNVVPHVFLLFITFPILFIGWGSQSSKVHIHHSTWLHFPGHNLRWILTFILLFVLVCEIAEGILSDGVTESRHLHLYMPAGMAFMAAITSVVYYHNIETSNFPKLLIALLIYWTLAFITKTIKFVKFYDHAIGFSQLRFCLTGLLVILYGMLLLVEVNVIRVRRYIFFKTPREVKPPEDLQDLGVRFLQPFVNLLSKGTYWWMNAFIKTAHKKPIDLRAIGKLPIAMRALTNYQRLCVAFDAQARKDTQSPQGARAIWRALCHAFGRRLILSSTFRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEHSNERLKQTNEMLRGMKLLKLYAWESIFCSRVEVTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDLSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPREPAPQGQAGKYQAVPLKVVNRKRPAREEVRDLLGPLQRLAPSMDGDADNFCVQIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQKVSGAVFWNSNLPDSEGEDPSSPERETAAGSDIRSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQQTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVMERKASEPSQGLPRAMSSRDGLLLDEEEEEEEAAESEEDDNLSSVLHQRAKIPWRACTKYLSSAGILLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALVLSPAARNCSLSQECDLDQSVYAMVFTLLCSLGIVLCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHALLKTEAESYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALISPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPETLLSQKDSVFASFVRADK
Protein: SET domain-containing protein (Q389M6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPPPSVGLLVMFDVRVVANPPGMSWVEDKSRDLESLRKRLKECGHDAESLTIVGRKLHEIAEQAHRKGEWGTLGVESGSGRDEEQAFQLFTHAGELLMRTVISILESFTQHEIHAATRVRIEKEEVDIIETLMRAANTDKTCSALSTLHCRWRRVYAASRAWRWCEAHVTLTSDYKPDLCSGGLYDMLPMTEWWWMPETVSAMTPPKAEATSSMCSDNDDGWLLFEDLFLSTTAPQSSECKRQLHDAETVTAFLNELNSTVDLFSRRIPAGYDELRRLYIGKADIQLQQARLFSHLSFVKGVPGSYQNATDGKTVVSGGVNGCHKLLWISREGLSTSMRCLIDALTAAQIAVAQFNAPCDDLIRRIRLAMFGVGLSSDGEGDTPHSACTPLLHPSVEPSSNRWRIKHGVGLIATNHIMEGAVVVKDRSLLLVGQVSPQKRKQERVTDIVEAPDGENAAVVNGALELFLRGGFVHKDELATSSIVKALRVGKLLGDPVEAPDMHSALHLLAMMPFSGESGMHPTQGAGRENVDYEAAIARDLADLMCCWRRCSVPLEAPQDFRATPKAEVLTPCRALLPLVSLINHSCKPNAIILPLCSEESQGSSSFGEGKGDVCVIALRDIEPGEEITVSYLSSVLIPKTLKDEQNGFCCCCSFCKSSTALLEGVICPECRQLIYDPEDAQKNCDKYQGSAGRQPTRGVHTYPCVLVDLSLPKGQRSYEHASDCSRADSDTYESLSRRILQGYANAVDKACEEFESTSTFGGVGASACEVEVEAGTVGSSEEVQGIEVDGMEEGSDDDDNGAGEDRLAQTALRRLMDLDSFACALPTTHYIRLQTRLECLALSLRSQLTTHDSHMLLLLCEELLEDLRQILPPNHPLLTGVRLQYALARSRHFAESADSSHTTEKHDHGCCGGVRECAATLSLPFLRDGMIRECIVHSFQEFYTTVGWKHEGCTQRELLSSFLEEYAVELLMCGIESIDHMTLLSLVYDASQEASVGL
Protein: BRCA1-associated protein (EC 2.3.2.27) (BRAP2) (Impedes mitogenic signal propagation) (IMP) (RING-type E3 ubiquitin transferase BRAP2) (Q99MP8)
Organism: Mus musculus (Mouse)
Function: Negatively regulates MAP kinase activation by limiting the formation of Raf/MEK complexes probably by inactivation of the KSR1 scaffold protein. Also acts as a Ras responsive E3 ubiquitin ligase that, on activation of Ras, is modified by auto-polyubiquitination resulting in the release of inhibition of Raf/MEK complex formation. May also act as a cytoplasmic retention protein with a role in regulating nuclear transport (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q7Z569}.
Interaction partners:
- Breast cancer type 1 susceptibility protein homolog
- Kinase suppressor of Ras 1
- GTPase HRas
- Polyubiquitin-B
- GTPase KRas
- Kinase suppressor of Ras 2
- GTPase NRas
- Ras-related protein M-Ras
- Ras-related protein R-Ras
- Ras-related protein R-Ras2
Sequence:
MSVSLVVIRLELAGHSPVPTDFGFSAAAGEMSDEEIKKKTLASAVACLEGKSAGEKAAIIHQHLGRREMTDVIIETMKARADEVRDTVEEKKPSAAPVSAQRSREQSESVNTAPESPSKQLPDQISFFSGNPSVEIVHGIMHLYKTNKMTSLKEDVRRSAMLCVLTVPATMTSHDLMKFVAPFNDVIEQMKIIRDSTPNQYMVLIKFSAQADADSFYMACNGRQFNSIEDDVCQLVYVERAEVLKSEDGASLPVMDLTELPKCTVCLERMDESVNGILTTLCNHSFHSQCLQRWDDTTCPVCRYCQTPEPVEENKCFECGVQENLWICLICGHIGCGRYVSRHAYKHFEETQHTYAMQLTNHRVWDYAGDNYVHRLVASKTDGKIVQYECEGDTCQEEKIDALQLEYSYLLTSQLESQRIYWENKIVRIEKDTAEEINNMKTKFKETIEKCDSLELRLSDLLKEKQSVERKCTQLNTRVAKLSTELQEEQELNKCLRANQLVLQNQLKEEEKLLKETCAQKDLQITEIQEQLRDVMFYLETQQQISHLPAETRQEIQEGQINIAMASAPNPPSSGAGGKLQSRKGRSKRGK
Protein: Non-specific lipid-transfer protein 1 (LTP 1) (NS-LTP1) (P83434)
Organism: Vigna radiata var. radiata (Mung bean) (Phaseolus aureus)
Function: Plant non-specific lipid-transfer proteins transfer phospholipids as well as galactolipids across membranes. May play a role in wax or cutin deposition in the cell walls of expanding epidermal cells and certain secretory tissues. Has antifungal activity against F.solani, F.oxysporum, P.aphanidermatum and S.rolfsii. Has antibacterial activity against the Gram-positive bacterium S.aureus but not against the Gram-negative bacterium S.typhimurium.
Interaction partners:
- Non-specific lipid-transfer protein
Sequence:
MTCGQVQGNLAQCIGFLQKGGVVPPSCCTGVKNILNSSRTTADRRAVCSCLKAAAGAVRGINPNNAEALPGKCGVNIPYKISTSTNCNSIN
Protein: UTP--glucose-1-phosphate uridylyltransferase 1 (EC 2.7.7.9) (UDP-glucose pyrophosphorylase 1) (UDPGP 1) (UGPase 1) (P08800)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Plays a central role as a glucosyl donor in cellular metabolic pathways. During development the lack of the enzyme activity leads to cell death and lysis. Strains which lack UDPG pyrophosphorylase accomplish early developmental events but are unable to culminate. The enzyme affects the growth rate of the cells but is not essential for growth.
Interaction partners:
- Phosphoglucomutase-1
- Glycogen phosphorylase 1
- Glycogen phosphorylase 2
- Glycogen [starch] synthase
- UDP-glucose 4-epimerase
- Probable phosphoglucomutase-2
- Glycogen debranching enzyme
- Uncharacterized protein
- Alpha,alpha-trehalose-phosphate synthase B
- Alpha,alpha-trehalose-phosphate synthase A
Sequence:
MTDTATSKATVERPKLQSTGSLHSLFKNVDLFSENDEELYPPLQHGARFAAPIEDSTLLALGMKPDELKAFQKQRHAYINKDQIYTDEIKIPNKTEMVDYHQLHLVSPIDQSNASRLLNKLVVIKLNGGLGNSMGCKTAKSTMEIAPGVTFLDMAVAHIEQINQDYNVDVPLVIMNSYKTHNETNKVIEKYKTHKVSIKTFQQSMFPKMYKDTLNLVPKPNTPMNPKEWYPPGSGDIFRSLQRSGLIDEFLAAGKEYIFISNVENLGSIIDLQVLNHIHLQKIEFGLEVTNRINTDSTGGILMSYKDKLHLLELSQVKPEKLKIFKDFKLWNTNNIWVNLKSVSNLIKEDKLDLDWIVNYPLENHKAMVQLETPAGMGIQNFKNSVAIFVPRDRYRPIKSTSQLLVAQSNIFQFDHGQVKLNSKREGQDVPLVKLGEEFSTVSDYEKRFKSIPDLLELDHLTVSGDVYFGSRITLKGTVIIVANHGERVDIPDGVVLENKVLSGTLRILDH
Protein: ATP-dependent DNA helicase PIF1 (EC 3.6.4.12) (DNA repair and recombination helicase PIF1) (Q384Y1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of mitochondrial (kinetoplast) genome stability. Essential for replication of kinetoplast minicircles. Involved in the segregation of minicircle progeny.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19646907, ECO:0000269|PubMed:20042610}. Note=Localizes to the antipodal sites flanking the kDNA disk.
Interaction partners:
- DNA 3'-5' helicase
- Uncharacterized protein
- TFIIH basal transcription factor complex helicase/translocase XPB subunit
Sequence:
MLRRLLQPAYNVALSGTSASTLPRKSASVGLVRTALMPVDYNAGALFCAMRFTSGTEKERKREPKRGSKRRSKATTTLSTPTDAQTSVTGAREGVALPQENMPDAIQPPATLEVRAAEVKEEPLAATPPQIQPQEETMGPIDGEPQLPLHSTLVYNALTGRMTSETSPSFLCLKSIGFGVNNKRQLYVEKPDVLRDLAQRMRKGTATLPSNWPVTIIRALGVILRNRRVEDPAEAIQQMMQVKINNLTHSRYAAVVNAVGDTDLQNILDGGLADEFVAVDLNEEQEKVINLALKGHLMYIGGSAGTGKTVLLRALCRRMQAEGLRVAMTATTGVAGCHIGGSTFHHAMGVSAQGDFVRKNHLLSYDAIIIDEVSMLPKKMFEEFDRVLREEAGAPDVPFGGVQIILCGDFLQLGVINEPPIIHSTTFREKFVKIRLETQVRQAKSSLFADALQQMRVGLVPESLTASVEQLPPGTMVPAAVNLLPTNKEVNTANEEELKRLPGDAVTLTPETGITALRCDTTATLLMRTTKDFKVEEFTKHLRGLLQATVDIPRASMVSAYRIYEDGHAVRVYLPQSESVAWRDAIRERFLEVAGLINDLDIGATVTEIIPSGDGLHTPEHEECLQRLMAKHPIAQPLTLKKGCRVLLRTNLTSRLVNGSIGTVVDFVECSMENIPVALRCERVNRCVDRYRIYCTMECGMPVPLLPVVKFHSGETIVVPPWEFLVGGNPITQYYSLSSVSLPLSLAYAFTVHKVQGLTLVGRVHLELSRMWPCEHLLYVAMSRVRNPEQLSMSSFDPKMVLANEACVKFDRELNTVDNLPSLAEYPVSSWKRCNDMVYHLRRQGTSLDRYLQNGAAKEGGSVPVQQLGLSGPVKGSLEHSMVVSRRLRKLIKQTERTIRMHERRQKKMAVEGAKQTDTTKASSGESLE
Protein: Uncharacterized protein YML119W (Q03208)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- KH domain-containing protein YLL032C
- Protein ECM9
- Meiotic sister-chromatid recombination protein 3
- Small ribosomal subunit protein uS17m
Sequence:
MSPSPSVSPRRTLNNKSSYINNSGGLVLPPTQFNLNQQPVLSFQQKATFDSNQQFFYYPESPTKNLRPRFNSISQVNKGVNEDHYTGGGSSNNNRPSRYTNTMGAANTNVNSHPHHQSVSHLNSKSLKFNQTKEVSSINEIIFPSRTCTKKRYFTKPIDLYGTRSSTSVAPKLTNSPTKSKTNFNIKKCILPRSVVTTYKLPSPVHETIDDISKKIIILLISLKFEKNYHFLQPIQLSTNSKTRISKSLDELCGVQLTSTLRQQKQLQGNSKPVKNLPNSNAKQRAGASVSTNANESFELSFDGKAMDRSDIFRMVDSFSIAISDEDEEDEEEDSFQQRSANNRILPAEILSNEPLK
Protein: Guanylyl cyclase C (GC-C) (EC 4.6.1.2) (Heat-stable enterotoxin receptor) (STA receptor) (hSTAR) (Intestinal guanylate cyclase) (P25092)
Organism: Homo sapiens (Human)
Function: Guanylyl cyclase that catalyzes synthesis of cyclic GMP (cGMP) from GTP. Receptor for the E.coli heat-stable enterotoxin; E.coli enterotoxin markedly stimulates the accumulation of cGMP in mammalian cells expressing GUCY2C. Also activated by the endogenous peptides guanylin and uroguanylin.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23269669}; Single-pass type I membrane protein {ECO:0000269|PubMed:23269669}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23269669}; Single-pass type I membrane protein {ECO:0000269|PubMed:23269669}. Note=The 145 kDa plasma membrane form of GUCY2C contains sialic acid and galactose residues, while a differencially glycosylated 130 Kda form is a high mannose form that is resident in the endoplasmic reticulum and may serve as the precursor for the cell surface form. {ECO:0000269|PubMed:23269669}.
Interaction partners:
- Guanylin
- Guanylate cyclase activator 2B
- Emerin
- Na
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Bis
- Pyruvate kinase PKLR
- Pyruvate kinase PKM
- Inosine triphosphate pyrophosphatase
Sequence:
MKTLLLDLALWSLLFQPGWLSFSSQVSQNCHNGSYEISVLMMGNSAFAEPLKNLEDAVNEGLEIVRGRLQNAGLNVTVNATFMYSDGLIHNSGDCRSSTCEGLDLLRKISNAQRMGCVLIGPSCTYSTFQMYLDTELSYPMISAGSFGLSCDYKETLTRLMSPARKLMYFLVNFWKTNDLPFKTYSWSTSYVYKNGTETEDCFWYLNALEASVSYFSHELGFKVVLRQDKEFQDILMDHNRKSNVIIMCGGPEFLYKLKGDRAVAEDIVIILVDLFNDQYFEDNVTAPDYMKNVLVLTLSPGNSLLNSSFSRNLSPTKRDFALAYLNGILLFGHMLKIFLENGENITTPKFAHAFRNLTFEGYDGPVTLDDWGDVDSTMVLLYTSVDTKKYKVLLTYDTHVNKTYPVDMSPTFTWKNSKLPNDITGRGPQILMIAVFTLTGAVVLLLLVALLMLRKYRKDYELRQKKWSHIPPENIFPLETNETNHVSLKIDDDKRRDTIQRLRQCKYDKKRVILKDLKHNDGNFTEKQKIELNKLLQIDYYNLTKFYGTVKLDTMIFGVIEYCERGSLREVLNDTISYPDGTFMDWEFKISVLYDIAKGMSYLHSSKTEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPKKDLWTAPEHLRQANISQKGDVYSYGIIAQEIILRKETFYTLSCRDRNEKIFRVENSNGMKPFRPDLFLETAEEKELEVYLLVKNCWEEDPEKRPDFKKIETTLAKIFGLFHDQKNESYMDTLIRRLQLYSRNLEHLVEERTQLYKAERDRADRLNFMLLPRLVVKSLKEKGFVEPELYEEVTIYFSDIVGFTTICKYSTPMEVVDMLNDIYKSFDHIVDHHDVYKVETIGDAYMVASGLPKRNGNRHAIDIAKMALEILSFMGTFELEHLPGLPIWIRIGVHSGPCAAGVVGIKMPRYCLFGDTVNTASRMESTGLPLRIHVSGSTIAILKRTECQFLYEVRGETYLKGRGNETTYWLTGMKDQKFNLPTPPTVENQQRLQAEFSDMIANSLQKRQAAGIRSQKPRRVASYKKGTLEYLQLNTTDKESTYF
Protein: Immunoglobulin kappa chain variable 2-137 (A0A0B4J1H6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRCLAEFLGLLVLWIPGAIGDIVMTQAAPSVPVTPGESVSISCRSSKSLLHSNGNTYLYWFLQRPGQSPQLLIYRMSNLASGVPDRFSGSGSGTAFTLRISRVEAEDVGVYYCMQHLEYP
Protein: KN motif and ankyrin repeat domain-containing protein 2 (X1WE18)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: May be involved in different biological processes including transcription and apoptosis by sequestering specific proteins outside of the nucleus (By similarity). Involved in actin stress fibers formation probably through its interaction with ARHGDIA and the regulation of the Rho signaling pathway (By similarity). May thereby play a role in cell adhesion and migration, regulating for instance podocytes migration during development of the kidney.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q63ZY3}. Mitochondrion {ECO:0000250|UniProtKB:Q63ZY3}.
Interaction partners:
- Inactive rhomboid protein
- Rho GDP dissociation inhibitor
- Inactive rhomboid protein 1
- NPR3-like, GATOR1 complex subunit.
- Kinesin family member 21A
- Rho GTPase-activating protein 24
- Kinesin-like protein KIF21A
- Leucine carboxyl methyltransferase 1
- FAT atypical cadherin 1a
Sequence:
MTIMAQVLHMDSSFPGKINPPVPPSLHAKDQEAPYSVETPYGYRLDLDFLKYVNDIEKGNTIKKVPVQRRPRYGSLPRGYGYTGSWWTSTESLCSNASMDSRHSSYSYCAPGFHTSQRPNFSTARVEKTLMDARRKLEEEKDGRRFSNLGSMHSSMAGSNTSLSSAHSFNRAQGGGSYTPMSSGLSTPVSPTPAHLQHVREQMAVALRKIRELEEQVKTIPVLQVKISVLQEEKRQLSVQLKSQKFLGHTLGFNRSRPRGELYIDIPEEEAGNGAGAANKATGSLSPTTPGSLQDSGCEIEETVIVAGARPGAKREVRTVGVGPEAEERGYRQVGVGVREQDLGLLPETEALKTKVGLLEVQLRKTMQELQSAQQQVEAAQKERQTVCPQVDHAVRATSLGWQDQQGQAGAGLHTVVSFTKQPHQQRTVGIQVYTLEQPTVVGVGTLLRAQGCTHPAQLEASHRRYGESPAAGDSPHEFPIAISSKQVREVLRSEVSKSVPVTNQATPMETKCNQVTAVCQRLKEGEINQQPAEEAIQVDPANPASPQSNLRSIMKRKADGEPGSPYTKKNLQFLGVNGGYESTSSEESSSESSEDESDASEYHEATEKLPESATPQSLVSSCIPQLASETPATQTAQHSTAQIPTNHTPAAQTTSQSHTTDATTQQHVTQSPAAEADVQHCVSQSSVTTTPPPEGDVQCVFQGCNPPSTATSLEQNSVQLSSATQQSKATDSNVQPDLAQTDVSDFAAQQTTTQTQFTSAKPQQEASQSKTADLTAQKGATHSTDGSAKQDIAISSTTKPAADTATPPTNKQTDSLELSGGLMSALHILQKALSEPNAFSHQDARTAYTSVLQEWLRVSCHKAADTAVVKAHMDAFASISPQLLEFVINMADGNGNTALHYTVSHSNFPVVKLLLDTGLCNADKQNKAGYTAIMLTALAAFSSDSDLQTVLQLLRTGDVNAKASQAGQTALMLAVSHGRGDMVKALLACGAQVNLRDDDGSTALMCACEHGHVDIVRQLLSVPGCDATLTDNDGSTALSIALEASQNDIAVLLYAHLNFAKPPSPVSPKSPILGSSPPSSSELK
Protein: Ligand of Numb protein X 2b isoform X1 (Ligand of numb-protein X 2b) (Ligand of numb-protein X-like protein) (Zgc:85925 protein) (A4VCF7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Dharma.
- Transcription factor E4F1
- Homeobox protein Ved
- Ventral homeobox.
Sequence:
MTESKTSSLPTGVTWARVCKECGQCHDGQDSHLFEYQDEVDDELVCHICLQPLLQPMDTPCGHTYCFQCLSNFLHDQDFCPVDRQRIQLQQCRASSLLVRNLLDKLAVLCPFRSECELSMQRCELQPHLHNRCPAFKRLREEAERKKRPSWNELKGSKSDGDLADAKSAQTIGRTAQLSAPSEPGLVNPAFEEGEDDTPLRCSLVAEATVVELFREDPGEDLGLRIVGGKDTPLGNIVIQEIVRDSLVARDGKLAPGDHILEVNDVSLASISHSRAIAVIRQPCSRLRLTVMQEKGFKPRPEHHTQPSASPPTQSPSTNQNHGTVIQVTLVKHERSEALGIKLIRKSEEPGVFILDLLPGGLAAKDGKLRNNDKVLGINGQDLRHGTPESAAQIIQASEMRVNFVVMRLQDVSEEGGEGQSRGARRVPEPQYFRRHSEYMKEPPGGFSSQEKTVTLKKEPRQSLGITIAGGRDCRSRLPVYITSVQPVGCLHRDGTVKTGDVLLSINGIDLTHLTYNEAVTVLKTQTAQSTVTLRVIQTFADDEEQDGESGSREDMDTMEGPKDDDINWVPLWTRWLGLPSCIHWCRDIMLMKTNSESWGFSIVGGYEESRGQQPFFIKTIVPGTPAYFDGRLKCGDEIVAVNGVTTVGMNNSSLIPMLKLQKNKVTLTVVSWPGSLV
Protein: Gluconolactonase (EC 3.1.1.17) (D-glucono-delta-lactone lactonohydrolase) [Cleaved into: Gluconolactonase; Gluconolactonase minor isoform] (Q01578)
Organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)
Function: Hydrolyzes the gluconolactone formed by glucose-fructose oxidoreductase, and that formed in aerobic conditions by the glucose dehydrogenase present.
Subcellular location: Periplasm {ECO:0000305|PubMed:1482681}.
Interaction partners:
- Glucose--fructose oxidoreductase
- Gluconokinase
- SMP-30/Gluconolaconase/LRE domain protein
- Aldose 1-epimerase
Sequence:
MTTGRMSRRECLSAAVMVPIAAMTATATITGSAQAAKNNMNGSTIGKITKFSPRLDAILDVSTPIEVIASDIQWSEGPVWVKNGNFLLFSDPPANIMRKWTPDAGVSIFLKPSGHAEPIPAGQFREPGSNGMKVGPDGKIWVADSGTRAIMKVDPVTRQRSVVVDNYKGKRFNSPNDLFFSKSGAVYFTDPPYGLTNLDESDIKEMNYNGVFRLSPDGRLDLIEAGLSRPNGLALSPDETKLYVSNSDRASPNIWVYSLDSNGLPTSRTLLRNFRKEYFDQGLAGLPDGMNIDKQGNLFASAPGGIYIFAPDGECLGLISGNPGQPLSNCCFGEKGQTLFISASHNVVRVRTKTFG
Protein: Cinnamoyl-CoA reductase 1 (Ph-CCR1) (EC 1.2.1.44) (Coniferylaldehyde synthase) (Coumaroyl-CoA reductase) (Feruloyl-CoA reductase) (Sinapoyl-CoA reductase) (A0A059TC02)
Organism: Petunia hybrida (Petunia)
Function: Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes. Mediates the conversion of feruloyl CoA to coniferylaldehyde. Also active toward p-coumaroyl-CoA and sinapoyl-CoA. Involved in the production of floral volatile phenylpropanoids in flowers of fragrant cultivars (e.g. cv. Mitchell and cv. V26) from cinnamic acid, a common precursor with the anthocyanin biosynthesis pathway involved in flower pigmentation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:24985707}.
Interaction partners:
Sequence:
MRSVSGQVVCVTGAGGFIASWLVKILLEKGYTVRGTVRNPDDPKNGHLRELEGAKERLTLCKADLLDYQSLREAINGCDGVFHTASPVTDDPEQMVEPAVIGTKNVINAAAEANVRRVVFTSSIGAVYMDPNRDPETVVDETCWSDPDFCKNTKNWYCYGKMVAEQAAWEEAKEKGVDLVVINPVLVQGPLLQTTVNASVLHILKYLTGSAKTYANSVQAYVDVKDVALAHILLYETPEASGRYLCAESVLHRGDVVEILSKFFPEYPIPTKCSDVTKPRVKPYKFSNQKLKDLGLEFTPVKQCLYETVKSLQEKGHLPIPTQKDEPIIRIQP
Protein: Alba1 (A0A165TZX1)
Organism: Oryza sativa subsp. indica (Rice)
Interaction partners:
Sequence:
MAVEEITEGVRNLAVEGEPAAAAAAAGGGGEGAQRRAAGSSSNRIQVSNTKKPLFFYVNLAKRYMQQHGDVELSALGMAIATVVTVAEILKNNGFAVEKKIRTSTVEINDESRVRPLQKAKIEIVLEKSEKFDELMAAAAEEREAAEAEEQA
Protein: Protein-export membrane protein SecG (P12) (Preprotein translocase band 1 subunit) (P0AG99)
Organism: Escherichia coli (strain K12)
Function: Subunit of the protein translocation channel SecYEG. Overexpression of some hybrid proteins has been thought to jam the protein secretion apparatus resulting in cell death; while this may be true it also results in FtsH-mediated degradation of SecY. Treatment with antibiotics that block translation elongation such as chloramphenicol also leads to degradation of SecY and SecE but not SecG.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Protein translocase subunit SecF
- Protein translocase subunit SecE
- Protein translocase subunit SecY
- Protein translocase subunit SecA
- Protein translocase subunit SecD
- Membrane protein insertase YidC
- Signal recognition particle receptor FtsY
- Sec translocon accessory complex subunit YajC
- Signal recognition particle protein
- Protein-export protein SecB
Sequence:
MYEALLVVFLIVAIGLVGLIMLQQGKGADMGASFGAGASATLFGSSGSGNFMTRMTALLATLFFIISLVLGNINSNKTNKGSEWENLSAPAKTEQTQPAAPAKPTSDIPN
Protein: Diacylglycerol kinase delta (DAG kinase delta) (EC 2.7.1.107) (E9PUQ8)
Organism: Mus musculus (Mouse)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes. By controlling the levels of diacylglycerol, regulates for instance the PKC and EGF receptor signaling pathways and plays a crucial role during development. May also regulate clathrin-dependent endocytosis (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q16760}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q16760}. Membrane, clathrin-coated pit {ECO:0000250|UniProtKB:Q16760}. Cytoplasm {ECO:0000250|UniProtKB:Q16760}.
Interaction partners:
- Lipoprotein lipase
- Dihydroxyacetone phosphate acyltransferase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Phospholipase D2
- Phospholipase D1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phosphatidate cytidylyltransferase 2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- 5'-3' exonuclease PLD3
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Sequence:
MAAAAGAPPPGPPQPPPPPPPEESSDSEPEAEPGSPQKLIRKVSTSGQIRQKTILKEGMLTKQNNSFQRSKRRYFKLRGRTLYYAKTAKSIIFDEVDLTDASVAESSTKNVNNSFTVITPCRKLILCADNRKEMEDWIAALKTVQNKEHFEPTQYSMDHFSGMHNWYACSHARPTYCNVCREVLSGVTSHGLSCEVCKFKAHKRCAVRATSNCKWTTLASIGKDIIEDEDGIAMPHQWLEGNLPVSAKCIVCDKTCGSVLRLQDWRCLWCKAMVHTSCKESLVMKCPLGLCKVSVIPPTALNSIDSDGFWKATCPPSCTSPLLVFVNSKSGDNQGVKFLRRFKQLLNPAQVFDLMNGGPHLGLRLFQKFDTFRILVCGGDGSVGWVLSEIDSLNLHKQCQLGVLPLGTGNDLARVLGWGSACDDDTQLPQILAKLERASTKMLDRWSVMAYETKLPRQASSSTVTEDFSEDSEVQQILFYEDSVAAHLSKILTSDQHSVVISSAKVLCETVKDFVARVGKAYEKTTESSQESEVMAKKCSVLKEKLDSLLKTLDDESQASSSLSNPPPTIAEEAEDGDGSGNICSSTGDHLVGSACPSRPQIFRPREQLMLRANSLKKAIRQIIEHTEKAVDEQNAQTQEQQGFVLGLSESEKKDLKTDNRVCTSSVHSESCVIAKGRSQRKASRAPCEKLVSKGLSLGSSASLPPGTGSRDSLPALNTKILYPSVRAGMSGSLPGGSVISRLLINADPFNAEPENLEYYTEKCVMNNYFGIGLDAKISLDFNNKRDEHPEKCRSRTKNMMWYGVLGTKELLHRTYRNLEQKVLLECDGRPIPLPSLQGIAVLNIPSYAGGTNFWGGTKEDDTFAAPSFDDKILEVVAVFGSMQMAVSRVIKLQHHRIAQCRTVKISILGDEGVPVQVDGEAWIQPPGYIRIVHKNRAQTLTRDRAFENTLKSWEDKQKCELSRPPSFSLHPEILSEEEATQMDQFGQAAGGLIHSIREIAQSHRAMEQELAHAVNASSKAMERVYGKPRTAEGLNCSFVLEMVNNIRALRSETELLLAGKMALQLDPPQKERLGAALIEMDQQLRKLTDTPWLCQPLEPGEEESLQQNVMLDLTKRSRSGKFRLVTKFKKEKNNKNKEVHSNLGGPVHLWGTEEVAAWLEHLSLCEYKDIFTRHDIRGSELLHLERRDLKDLGVTKVGHMKRILCGIKELSRSSPAAEA
Protein: Integrator complex subunit 11 (EC 3.1.27.-) (Q9VAH9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalytic component of the Integrator complex, a complex involved in the transcription of small nuclear RNAs (snRNA) and their 3'-box-dependent processing (By similarity). Mediates the snRNAs 3' cleavage (By similarity). Involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5. May mediate recruitment of cytoplasmic dynein to the nuclear envelope, probably as component of the INT complex (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:39032490}. Cytoplasm, cytosol {ECO:0000269|PubMed:39032490}.
Interaction partners:
- Integrator complex subunit 1
- Integrator complex subunit 5
- Integrator complex subunit 9
- Integrator complex subunit 4
- Integrator complex subunit 3
- Integrator complex subunit 6
- Integrator complex subunit 7
- Integrator complex subunit 2
- Integrator complex subunit 12
- Integrator complex subunit 10
Sequence:
MPDIKITPLGAGQDVGRSCLLLSMGGKNIMLDCGMHMGYNDERRFPDFSYIVPEGPITSHIDCVIISHFHLDHCGALPYMSEIVGYTGPIYMTHPTKAIAPILLEDMRKVAVERKGESNFFTTQMIKDCMKKVIPVTLHQSMMVDTDLEIKAYYAGHVLGAAMFWIKVGSQSVVYTGDYNMTPDRHLGAAWIDKCRPDLLISESTYATTIRDSKRCRERDFLKKVHECVAKGGKVLIPVFALGRAQELCILLETYWERMNLKYPIYFALGLTEKANTYYKMFITWTNQKIRKTFVHRNMFDFKHIKPFDKAYIDNPGAMVVFATPGMLHAGLSLQIFKKWAPNENNMVIMPGYCVQGTVGNKILGGAKKVEFENRQVVEVKMAVEYMSFSAHADAKGIMQLIQNCEPKNVMLVHGEAGKMKFLRSKIKDEFNLETYMPANGETCVISTPVKIPVDASVSLLKAEARSYNAQPPDPKRRRLIHGVLVMKDNRIMLQNLTDALKEIGINRHVMRFTSKVKMDDSGPVIRTSERLKTLLEEKLAGWTVTMQENGSIAIESVEVKVEEDEKDPKQKNILISWTNQDEDIGAYILNVLQNMC
Protein: Heparin-sulfate lyase (EC 4.2.2.8) (Heparin-sulfate eliminase) (Heparinase III) (HepIII) (Heparitin-sulfate lyase) (Q59289)
Organism: Pedobacter heparinus (strain ATCC 13125 / DSM 2366 / CIP 104194 / JCM 7457 / NBRC 12017 / NCIMB 9290 / NRRL B-14731 / HIM 762-3)
Function: Specifically cleaves heparan sulfate-rich regions of acidic polysaccharides. Does not act on N,O-desulfated glucosamine or N-acetyl-O-sulfated glucosamine linkages. Functions in cleaving metazoan heparan sulfate and providing carbon, nitrogen and sulfate sources for microorganisms.
Subcellular location: Periplasm {ECO:0000269|PubMed:8702264}.
Interaction partners:
- Uncharacterized protein
Sequence:
MTTKIFKRIIVFAVIALSSGNILAQSSSITRKDFDHINLEYSGLEKVNKAVAAGNYDDAAKALLAYYREKSKAREPDFSNAEKPADIRQPIDKVTREMADKALVHQFQPHKGYGYFDYGKDINWQMWPVKDNEVRWQLHRVKWWQAMALVYHATGDEKYAREWVYQYSDWARKNPLGLSQDNDKFVWRPLEVSDRVQSLPPTFSLFVNSPAFTPAFLMEFLNSYHQQADYLSTHYAEQGNHRLFEAQRNLFAGVSFPEFKDSPRWRQTGISVLNTEIKKQVYADGMQFELSPIYHVAAIDIFLKAYGSAKRVNLEKEFPQSYVQTVENMIMALISISLPDYNTPMFGDSWITDKNFRMAQFASWARVFPANQAIKYFATDGKQGKAPNFLSKALSNAGFYTFRSGWDKNATVMVLKASPPGEFHAQPDNGTFELFIKGRNFTPDAGVFVYSGDEAIMKLRNWYRQTRIHSTLTLDNQNMVITKARQNKWETGNNLDVLTYTNPSYPNLDHQRSVLFINKKYFLVIDRAIGEATGNLGVHWQLKEDSNPVFDKTKNRVYTTYRDGNNLMIQSLNADRTSLNEEEGKVSYVYNKELKRPAFVFEKPKKNAGTQNFVSIVYPYDGQKAPEISIRENKGNDFEKGKLNLTLTINGKQQLVLVP