wanglab/gogpt-training-data huggingface dataset:
Protein: Sponge, isoform F (Sponge, isoform G) (A0A0B4KHD2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MWIPSNNKYGVAIHNWHGDVRFGLALDVGDSVDIVEECKHWYRGSCPRKSRAVGLFPKTYIHIKDLSKIDPVVAECTQVLREWSEIWKRLYVDREAYKFQTLRKVMFSILESRRELLSATMTQDQTLELQMVVVSKIDWGNRKLGLDLVPREGPLAVDPHGIGIVKLYNVHVSSADNAKASSSRGTLRRKTQRKILTHHLYFCMRDFGHRIGGDDAEVYFFLYDGSHMRPLSERFLVKISKDGFSNYIERLHSNCTVFTDLGAADLNEELHLVAVVMRVGKIIQSDSIKKIEKSGTLGHGPTFRRPFGVGVLSLGDIAHFDSSLEQSSDEREYNFKLFQCEEKDFHLLPELIIKKSSGKYSPIQASQGTQGIVVSLKLLHGGLGQARQEQPMLFQGSTITRKMGFPDVIMPGDVRNDLFLNLERGEFERGGKNTGKNILVTVVVLDVAGNVLTDCLWGASGMESQPQYRSMILYHQNAPSWNEMLRLSVPIDKFSTAHVRFEFRHCSTRDKTEPKLFAFSFARLMDTGGATLGDGLHELYVYKCEDPAKLQVANYLRLQCRPRDAQAKMDCGGCFSRSSKEVFVLRSLLCSTKLTQNADLLSLLQWRTYPETIQDSLTGVLRLNDEELVKFLQDVLDALFAMFSNEEGNSTQHSGLVFHVLVSIFSLLQSNKFQHFRPVMNEYIENHFAAALVYKGLITSVEHMAVFMTKAEHPDPFQKCFGSLEYIFKLLIQSRKLFARATGGQYEDSFKRDLHSLFTALNGMLAVPSYDVIIPTQEALLNSTGVVLEQLKDTLPAPELGMLARNMLDAIPRGAPIRLIQAKLHAVKDLVSGELFHEDDSRTVVLSVACKHLRMHLSRRDELRLCAEILSEILSQLYDLQKEQREKVTNTLQHDLDSLCKNILGILIRTISIIMEGSNAVLPQLVSCLLGLLQLLDETHYKRYWDELSPNKDPRDLKEFLSKSLLVYEELLTQDWHVFPNDWLVMKLAANDVLRMSLEEFAKPLVYRFLGPQAFDSQLWWSYFSLAVAFLTQPSLQLEQYREPKRLKILHSHGDMRVLMGFQILSMWSQLGEQKLHFIPSMVGPFLEVTLVPEPALRKATLSVFYDMMQCEQAARGSFRLVESELIDKLDLLISENKGDDEYRELFSTMEHLSLVLLEKVQVENPNWKEAGIAFIASVTRLLERLLDYRSVMQGEENRDKRMTCTVNLLNFYKNEINRKEMYLRYIYKLHNLHLQAENYTEAGFTLKLYASMLSWDRETQSFAPFDNSGQPEWQRKERLYHEILKYFDKGKCWEKGIPLCKELAHLYETRRFDYNKLSEILIQEAKFFQNILTQLRPEPEYFRVGFYGMGLPLFVRNKQFVYRGLEYERIGAFTQRLQTEFPSAQILGNNSPPDNAILNAPDQYIQISNVRPVGDAQALKTAMVPVPEKIARFYEVNDVTRFIYDRPMYKGTVDKDNEFKSLWIERTILEIASPLPGILRWYEVKQKTMQELTPVEYACEIISNAGKELSELIVQYKRDPKRNINPFSMRLQGTIDANVMGGISKYQEAFFSEQFLKSPQGAGQQANVQRLKVLILEQIQILEQALELHGQLAPSGVQPLHNRLLERFSQLKQSLSGMGRLKRQHSESIVNTPLPPLPTEQRVAPATASSSLNANAHSNYVYDLDEIYTRPGDTVRPVDPLSSYQTLSKESLSIPLEDTAAPPVPNRPRSQNFIGNGSMDSPEVPPKRQPTLNSPNAPPLPPRGITPDKRASNPLIFNDFGSGDAVGRRHSQQQQQHGQKYSVVDISYDDPEADQQPHSLPPNFQDGSGGHLSVCFAPNDFRDSGISTTSSRELNHMNLNNLSEDSSSISTITVQHREHCRISSNGSLDYNAAASMNITQRESSTSSFDVEDFPVPPPPIPPKSLAVSSNGVNFSLDEAHSPHPSTQANTTQLNHIQNPNQNHSTNSHHHLQQQQNGDGDGYSTLQHPMNGLGLPTLPPPPSAVESPMPASAIASSTSSHQHDGGTF
Protein: Probable ATP-dependent RNA helicase pitchoune (EC 3.6.4.13) (Q9VD51)
Organism: Drosophila melanogaster (Fruit fly)
Function: Probable RNA-dependent helicase. Functions in cell growth and proliferation. May have a role in ribosome biogenesis and, consequently, in protein biosynthesis.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:9716523}.
Interaction partners:
- Ribosomal L1 domain-containing protein CG13096
- RRM domain-containing protein
- Ribosome biogenesis protein BOP1 homolog
- LD11307p
- Ribosome biogenesis protein WDR12 homolog
- Guanine nucleotide-binding protein-like 3 homolog
- Putative rRNA methyltransferase
- Nucleolar protein 58
- Nucleolar GTP-binding protein 1
- Nucleolar complex protein 2
Sequence:
MSIREKLLMKKIVKREKMKKELSQKKGNKNAQKQEPPKQNGNKPSKKPEKLSKKHVAKDEDDDLEEDFQEAPLPKKKQQKQPPKKQQIQVANSDSESDDDEQEDEADEDSDLDEVAEVDEEDVDSGSEDDDQQEDEDEEEPVPAKKTKLLPNKSKAQNGKPAKDDEPFTVESSLAALDYRDSDDRSFASLKGAVSEATLRAIKEMGFTEMTEIQSKSLTPLLKGRDLVGAAQTGSGKTLAFLIPAVELINKLRFMPRNGTGVIIISPTRELSMQTFGVLKELMAHHHHTYGLVMGGSNRQVESEKLGKGINILVATPGRLLDHLQNSPDFLYKNLQCLIIDEVDRILEIGFEEELKQIINLLPKRRQTMLFSATQTARIEALSKLALKSEPIYVGVHDNQDTATVDGLEQGYIVCPSEKRLLVLFTFLKKNRKKKVMVFFSSCMSVKYHHELFNYIDLPVTSIHGKQKQTKRTTTFFQFCNAESGILLCTDVAARGLDIPQVDWIVQYDPPDDPREYIHRVGRTARGSGTSGHALLLMRPEELGFLRYLKAAKVPLNEFEFSWQKIADIQLQLEKLIAKNYFLNQSAKEAFKSYVRAYDSHQLKQIFNVNTLDLQAVAKSFGFLVPPVVDLKVGAAKRERPEKRVGGGGFGFYKKMNEGSASKQRHFKQVNRDQAKKFMR
Protein: RE24343p (Q8SZ11)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSDQIGNTNATFSGSGSGSGTNVASIAESVAESGPDFDALRAACETRLNASGQLAGSGGPGAEAGTHCAGTFDGWLCWPDTAVGTSAYELCPDFITGFDPARYAHKECGLDGEWFKHPLTNKTWSNYTTCVNLEDLNWRHTVNLISEVGYGTSLLAILLSLAILGYFKSLKCARITLHMNLFASFAANNSLWLVWYLLVMPNSELLHQSPMRCVALHITLHYFLLSNYSWMLCEGFYLHTVLVAAFISEKRLVKWLIAFGWGSRPSSYSSIAWLAVWAARPRTIVTAG
Protein: Nuclear factor erythroid 2-related factor 3 (NF-E2-related factor 3) (NFE2-related factor 3) (Nuclear factor, erythroid derived 2, like 3) (Q9WTM4)
Organism: Mus musculus (Mouse)
Function: Activates erythroid-specific, globin gene expression.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Transcription factor MafG
- Transcription factor Maf
- Transcription factor MafK
- Transcription factor Jun
- Transcription factor MafF
Sequence:
MKLPKPWWAGGGLLQLTILLSLVGLRVDLDLFLPPPAAALWEELLPLCPTRPASASNPFSASEGWERTPLLPAKGRLLHEVRALGVPFIPRTRVDAWLVHSVATGNADGAHGLLGTAASSAVGDGGQSASAGGGDPRAAHSSPLAAEEEEEKAAEPTAQVPDAGGCGSQENGMLREKSEAVDHSSQQEENEEGVSAQAKSRQQSKTEEHKMACASAREAEKITEARNESHLHWSDTSFSLEDLFQLLSSQPEHSLEGISVEDIPPFLSSVCESVNSSAQNINLSQAISHDVNLHEAMLLYPNNTFRRDPSARSSQAQEPFLQLNPHTNPEQATPAMSLPPFDNQMRNLTSQDLLYDLDSNIFDGINLMSLATGFSPLEVSQLFEEPDSGLSLNSSYNSTSLTNSYRIYDGTVGYNSDLQSLCHDLGAVGGCYPEPHKHCHMDHRTIAGFHVSLECQQVFHDHTYHLQSGASEPTSESFAWSEKSQKTSGCLDNPDRNLSRDEQRAKALHIPFSVDEIVRMPVDSFNSMLSRYYLTDLQVSLIRDIRRRGKNKVAAQNCRKRKLDIILNLEDDICNLQAKKEALKNEQTQCSKAIDIMRQKLHGLHQDVFNRLRDDQGRPVNPSQYALQYSHDGTVLIVPKELISSGHKKEAPKGKRERRN
Protein: Nucleoporin nup45 (Nuclear pore protein nup45) (Q09793)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope.
Subcellular location: Cytoplasm. Nucleus, nuclear pore complex.
Interaction partners:
- Nucleoporin nup44
- Nucleoporin nsp1
- Nucleoporin nup186
- Nucleoporin nup85
- Meiotically up-regulated gene 87 protein
- Nucleoporin nup107
- Nucleoporin nup184
- Nucleoporin nup189
- Probable nucleoporin C890.06
- Nucleoporin nup120
Sequence:
MFGLNKTPSFGSTGTQNQNTGTSAGTGLFSSNTFGNNTQANTPASTGFGGVTGGAFGQTKPQTGGSLFGNKPNATSTTPGLNLFGQNPQAAPGGSLFGASTTKPQAPGGLFNQNQTQAQPAQAAPTGGLFGLSGQNQTQSQTQPAQANTSLFGQSNIGTTGGLFDQNRPNTSTFGQFSTQPASAGLFGQSTQPSGSTGFGLSNNTQTTPFFSAAQQQPSTTQLPSNPAINATTRYSSLNANTQKFLDDLDKEIFSQIQLAEELQTKLGTVSELVESVPNDVAEVQRRLSSVSTALLIDSDEIETTKRVVDEDTSNARISSRILDVFKTPGATYPFASNDPLMNYFEQFTENAKKRTDLYAATIGELEQHLEQVETTPQNNSPEALLKTIKEEHKLFMALSNRFAQVHDEVKRLQVNTSTSLPFIS
Protein: 5-hydroxyisourate hydrolase (HIU hydrolase) (HIUHase) (EC 3.5.2.17) (Transthyretin-related protein) (Q06S87)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Catalyzes the hydrolysis of 5-hydroxyisourate (HIU) to 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline (OHCU).
Subcellular location: Peroxisome {ECO:0000305}.
Interaction partners:
- Uricase
- 2-oxo-4-hydroxy-4-carboxy-5-ureidoimidazoline decarboxylase
- 5-hydroxyisourate hydrolase
- Methenyltetrahydrofolate synthase domain-containing protein
- Differentially expressed in FDCP 8 homolog
- Guanine deaminase
Sequence:
MNRLQHIRGHIVSADKHINMSATLLSPLSTHVLNIAQGVPGANMTIVLHRLDPVSSAWNILTTGITNDDGRCPGLITKENFIAGVYKMRFETGKYWDALGETCFYPYVEIVFTITNTSQHYHVPLLLSRFSYSTYRGS
Protein: 5-azacytidine resistance protein azr1 (Q09189)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Confers azacytidine resistance in high copy.
Interaction partners:
- Putative cytidine deaminase
- V-type proton ATPase catalytic subunit A
Sequence:
MNVTRLYFRVAGTKQFARYVHKYAAYSSTSFQKKKSHFPSPATLDHPDAGEDAFINLRNENYILNAVFDGVGGWANVGIDPSIFSWGLVREIKKVFNNSDEFQPSPLTLLSKAYAALKKSNTVEAGSSTACLTLFNCGNGKLHSLNLGDSGFLILRNGAIHYASPAQVLQFNMPYQLAIYPRNYRSAENIGPKMGQATVHDLKDNDLVILATDGIFDNIEEKSILDIAGVVDFSSLSNVQKCLDDLAMRICRQAVLNSLDTKWESPFAKTAKSFGFKFQGGKVDDTTITCLLIKSKNYE
Protein: Palmitoyltransferase ZDHHC8 (EC 2.3.1.225) (Zinc finger DHHC domain-containing protein 8) (DHHC-8) (Q5Y5T5)
Organism: Mus musculus (Mouse)
Function: Palmitoyltransferase that catalyzes the addition of palmitate onto various protein substrates and therefore functions in several unrelated biological processes. Through the palmitoylation of ABCA1 regulates the localization of the transporter to the plasma membrane and thereby regulates its function in cholesterol and phospholipid efflux (By similarity). Could also pamitoylate the D(2) dopamine receptor DRD2 and regulate its stability and localization to the plasma membrane (By similarity). Could also play a role in glutamatergic transmission.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9ULC8}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000269|PubMed:18775783}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Integral membrane protein DGCR2/IDD
- Catechol O-methyltransferase
- 39S ribosomal protein L40
- Phospholipid-transporting ATPase ABCA1
- Transport and Golgi organization 2 homolog
- Proline dehydrogenase 1, mitochondrial
Sequence:
MPRSPGTRLKPAKYIPVATAAALLVGSSTLFFVFTCPWLTRAVSPAIPVYNGILFLFVLANFSMATFMDPGVFPRADEDEDKEDDFRAPLYKNVDVRGIQVRMKWCATCHFYRPPRCSHCSVCDNCVEDFDHHCPWVNNCIGRRNYRYFFLFLLSLSAHMVGVVAFGLLYVLNHSEGLGAAHTTITMAVMCVAGLFFIPVIGLTGFHVVLVTRGRTTNEQVTGKFRGGVNPFTRGCYGNVEHVLCSPLAPRYVVEPPRMPLSVSLKPPFLRPELLERAVPLKVKLSDNGLKAGRSKSKGSLDQLDEKPLDLGPPLPPKIEAGTFGRDLKTPRPGSAESALSVQRTSPPTPAMYKFRPAFSTGPKTPFCGPNEQVPGPDSLTLADDSTHSLDFVSEPSLDLPDHGPGGLRPPYPPSPPLNTTDAFSGALRSLSLKAASRRGGDHMTLQPLRSEGGPPTPHRSLFAPHALPNRNGSLSYDSLLNPGSPSGHACPTHPSVGIASYHSPYLHPGPSDPPRPPPRSFSPVLGPRPREPSPVRYDNLSRTIMASIQERKDREERERLLRSQTDSLFGDSGVYDTPSSYSLQQASVLTEGPRGSVLRYGSRDDLVAGPGFGGARNPALQTSLSSLSSSMSRAPRTSSSSLQADQANNNAPGPRPGSGSHRSPARQGLPSPPGTPRSPSYTGSKAVAFIHTDLPDRQPSLAMQRDHPQLKTPPSKLNGQSPGMARLGPAASPMGPNASPARHTLVKKVSGVGGTTYEISV
Protein: CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase (Q8VYY6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein CYSTEINE-RICH TRANSMEMBRANE MODULE 1
- Disease resistance protein RPP1-WsB, putative domain family protein)
- Blue copper protein
- Calcium-binding site protein
- Marker for oxidative stress response protein
- DCD domain-containing protein NRP
- Protein FATTY ACID EXPORT 5
- AT3g16670/MGL6_12
- At3g49350
Sequence:
MNGTSWADQWDNSGDSAKGGRIGSGAVVRSSGSGATSNTTKYKEKMGQGLDKTKAVASSGFKKLKTGSAIGFRWVKDKYHKTTHKQ
Protein: Beta-actin-like protein 2 (Kappa-actin) (Q562R1)
Organism: Homo sapiens (Human)
Function: Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Prefoldin subunit 2
- Actin, cytoplasmic 1
- Prefoldin subunit 1
- Twinfilin-2
- Gelsolin
- RuvB-like 2
- RuvB-like 1
- DNA methyltransferase 1-associated protein 1
- Actin-like protein 6A
Sequence:
MTDNELSALVVDNGSGMCKAGFGGDDAPRAVFPSMIGRPRHQGVMVGMGQKDCYVGDEAQSKRGVLTLKYPIEHGVVTNWDDMEKIWYHTFYNELRVAPDEHPILLTEAPLNPKINREKMTQIMFEAFNTPAMYVAIQAVLSLYASGRTTGIVMDSGDGVTHIVPIYEGYALPHAILRLDLAGRDLTDYLMKILTERGYNFTTTAEREIVRDVKEKLCYVALDFEQEMVRAAASSSPERSYELPDGQVITIGNERFRCPEAIFQPSFLGIESSGIHETTFNSIMKCDVDIRKDLYANTVLSGGSTMYPGIADRMQKEIITLAPSTMKIKIIAPPERKYSVWIGGSILASLSTFQQMWISKQEYDEAGPPIVHRKCF
Protein: Hypoxanthine phosphoribosyltransferase (EC 2.4.2.8) (Q8IJS1)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, ECO:0000256|RuleBase:RU364099}.
Interaction partners:
- Adenylosuccinate synthetase
- Guanylate kinase
- Inosine-5'-monophosphate dehydrogenase
- AMP deaminase
- GMP synthase
- Adenosine deaminase
- Inosine triphosphate pyrophosphatase
- Adenylosuccinate lyase
- cGMP-specific 3',5'-cyclic phosphodiesterase delta
- IMP-specific 5'-nucleotidase 1
Sequence:
MPIPNNPGAGENAFDPVFVKDDDGYDLDSFMIPAHYKKYLTKVLVPNGVIKNRIEKLAYDIKKVYNNEEFHILCLLKGSRGFFTALLKHLSRIHNYSAVETSKPLFGEHYVRVKSYCNDQSTGTLEIVSEDLSCLKGKHVLIVEDIIDTGKTLVKFCEYLKKFEIKTVAIACLFIKRTPLWNGFKADFVGFSIPDHFVVGYSLDYNEIFRDLDHCCLVNDEGKKKYKATSL
Protein: Rrn3 protein (B2GV13)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA1
- DNA-directed RNA polymerase I subunit RPA2
- DNA-directed RNA polymerase subunit
- RNA polymerase I subunit E
- RNA polymerase I and III subunit C.
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
Sequence:
MAAPLLHTRLSSDVAATGSATLSASRTGLSNMLALESDFFSSPPRKTVRFGGTVTDVLLKYKKGETNDLELLKNQLSDPDIKDDQIINWLLEFRSSVMYLTKDFEQLINIILRLPWLNRSQTVVEEYLAFLGNLVSAQTVFLRPCLSMIASHFVPPRVIVKEGGIDVSESEDEDDNLPANFDTCHKALQIITRYVPSTPWFLMPILVEKFPFVRKSERTLECYVHNLLRISLYFPTLRREILELIIEKSLKLDVSVSRQDIDDAEETAAQTYGGTDAAEGLFNMDEDEETDPEKKAEQERPGRMAHPTAERLDILLSLLLSYIDDVCHVQGKIDNNKTKDLYRDLISIFDKLVLPTHASCHVQFFMFFLCSFKLSLLLQGFAEAFLEHLWKKLQDPNNPVIIRQAAANYIGSFLARAKFIPLITVKSCLDLLVNWLHLYLNSQDSGTKAFCDVALHGPFYSACQAVFYTVVFRHKQLLSGNLKEGLRYLQSLNFERIVLSQLNPLKICLPRVVNFFAAITNKYQLVFCYTIMERNNRQMLPVIRSTAGGDSVQTCTNPLDTFFPFDPCMLKRSKKFIDPVYQAWEDMSDEELQELRKPTRKELVEDEDDDFLKGEVPQSDTVAGLTPNSFDTHFRSPSSSVGSPPVLFMPDQSSLLSRICD
Protein: Protein Wnt-8a (Protein Wnt-8d) (Stimulated by retinoic acid gene 11 protein) (Q64527)
Organism: Mus musculus (Mouse)
Function: Ligand for members of the frizzled family of seven transmembrane receptors. Plays a role in embryonic patterning.
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:Q9H1J5}. Secreted {ECO:0000250|UniProtKB:Q9H1J5}.
Interaction partners:
- Frizzled-8
- Protein-serine O-palmitoleoyltransferase porcupine
- Wnt inhibitory factor 1
- Palmitoleoyl-protein carboxylesterase NOTUM
- Cerberus
- Glypican-3
- Protein wntless homolog
- Frizzled-5
- Low-density lipoprotein receptor-related protein 5
- Low-density lipoprotein receptor-related protein 6
Sequence:
MGHLLMLWVAAGMCYPALGASAWSVNNFLITRPKAYLTYTASVALGAQIGIEECKFQFAWERWNCPEHAFQFSTHNRLRAATRETSFIHAIRSAAIMYAVTKNCSMGDLENCGCDESQNGKTGGHGWIWGGCSDNVEFGEKISRLFVDSLEKGKDARALVNLHNNRAGRLAVRASTKRTCKCHGISGSCSIQTCWLQLADFRQMGNYLKAKYDRALKIEMDKRQLRAGNRAEGRWALTEAFLPSTEAELIFLEGSPDYCNRNASLSIQGTEGRECLQNARSASRREQRSCGRLCTECGLQVEERRAEAVSSCDCNFQWCCTVKCGQCRRVVSRYYCTRPVGSARPRGRGKDSAW
Protein: Fructose-1,6-bisphosphatase 1 (FBPase 1) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 1) (Liver FBPase) (P09467)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations, acting as a rate-limiting enzyme in gluconeogenesis. Plays a role in regulating glucose sensing and insulin secretion of pancreatic beta-cells. Appears to modulate glycerol gluconeogenesis in liver. Important regulator of appetite and adiposity; increased expression of the protein in liver after nutrient excess increases circulating satiety hormones and reduces appetite-stimulating neuropeptides and thus seems to provide a feedback mechanism to limit weight gain.
Interaction partners:
- Glucose-6-phosphate isomerase
- Transaldolase
- ATP-dependent 6-phosphofructokinase, muscle type
- Fructose-1,6-bisphosphatase isozyme 2
- Fructose-bisphosphate aldolase B
- Transketolase
- ATP-dependent 6-phosphofructokinase, platelet type
- Transketolase-like protein 2
- Transketolase-like protein 1
- ATP-dependent 6-phosphofructokinase, liver type
Sequence:
MADQAPFDTDVNTLTRFVMEEGRKARGTGELTQLLNSLCTAVKAISSAVRKAGIAHLYGIAGSTNVTGDQVKKLDVLSNDLVMNMLKSSFATCVLVSEEDKHAIIVEPEKRGKYVVCFDPLDGSSNIDCLVSVGTIFGIYRKKSTDEPSEKDALQPGRNLVAAGYALYGSATMLVLAMDCGVNCFMLDPAIGEFILVDKDVKIKKKGKIYSLNEGYARDFDPAVTEYIQRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKSPNGKLRLLYECNPMAYVMEKAGGMATTGKEAVLDVIPTDIHQRAPVILGSPDDVLEFLKVYEKHSAQ
Protein: Long-chain-fatty-acid--CoA ligase (Q7KVJ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Bardet-Biedl syndrome 1
- Bardet-Biedl syndrome 9
- Bardet-Biedl syndrome 8
- long-chain-fatty-acid--CoA ligase
- BBSome complex member BBS4 homolog
Sequence:
MCTAGVVDGGAGATTGGADAADNSGAAPAPSSTALNPPQVSISMNEPENLKPPAKSNFRRYLQWILAPVLTAISGLILYYQGPWYGVATLYAALISILLVRPGWRWFYIAAVTTPRDTVALFAYIRVLLFIKRQERKNLNIGDIFESNVARQPDKLAIVSESQQWTFRQVNEHSNRVANVFHSHGYKKGDVVGLLLENRAEFVATWLGLSKIGVITPLINTNLRGASLQHSITVGQCTALIYGASFRSAVMDIAKDLPAHVGLYQFNDESNQEVVASEGLSQGLAQQLNGLLETAAKDKVAAGASRADHHDKLVYIYTSGTTGLPKAAVITHSRYFFIAAGIHYTLGFKDQDVFYTPLPLYHTAGGVMSMGQALLFGSTVVIRKKFSASGYFSDCARFQCTVGQYIGEMARYILATPSAPHDRNHQVRMVFGNGLRPQIWPQFVERFGIRKVGEFYGATEGNANIMNNDSTVGAIGFISRILPQIYPISIIKADPHTGEPLRNSQGLCERCEADEPGVFVGKIVRGNPCREFLGYVDQKASSKKVVHDVFSKGDMAFISGDLLVADERGYLYFKDRTGDTFRWKGENVSTSEVEAQLSNLAGYKDVIVYGVSIPNTEGRAGMAAIYDPTREVNVSQLGVELAKSLPNYARPQFLRFLRKIDLTGTFKLRKVELQQQGFNPEIIDDELFYAQPDGVYAPLTPSVYERIVRNELRF
Protein: Phosphoribosyl pyrophosphate synthase-associated protein 1 (PRPP synthase-associated protein 1) (39 kDa phosphoribosypyrophosphate synthase-associated protein) (PAP39) (Q14558)
Organism: Homo sapiens (Human)
Function: Seems to play a negative regulatory role in 5-phosphoribose 1-diphosphate synthesis.
Interaction partners:
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 2
- Phosphoribosyl pyrophosphate synthase-associated protein 2
- Influenza virus NS1A-binding protein
- Ribose-phosphate pyrophosphokinase 3
Sequence:
MNAARTGYRVFSANSTAACTELAKRITERLGAELGKSVVYQETNGETRVEIKESVRGQDIFIIQTIPRDVNTAVMELLIMAYALKTACARNIIGVIPYFPYSKQSKMRKRGSIVCKLLASMLAKAGLTHIITMDLHQKEIQGFFSFPVDNLRASPFLLQYIQEEIPNYRNAVIVAKSPDAAKRAQSYAERLRLGLAVIHGEAQCTELDMDDGRHSPPMVKNATVHPGLELPLMMAKEKPPITVVGDVGGRIAIIVDDIIDDVESFVAAAEILKERGAYKIYVMATHGILSAEAPRLIEESSVDEVVVTNTVPHEVQKLQCPKIKTVDISLILSEAIRRIHNGESMAYLFRNITVDD
Protein: Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial (FGAM synthase) (FGAMS) (EC 6.3.5.3) (Formylglycinamide ribonucleotide amidotransferase) (FGAR amidotransferase) (FGAR-AT) (Formylglycinamide ribotide amidotransferase) (Q9M8D3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential to the male gametophyte development. Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18441219}. Mitochondrion {ECO:0000269|PubMed:18441219}.
Interaction partners:
- Phosphoribosylformylglycinamidine cyclo-ligase, chloroplastic
- Phosphoribosylglycinamide formyltransferase, chloroplastic
- Phosphoribosylaminoimidazole-succinocarboxamide synthase, chloroplastic
- Phosphoribosylamine--glycine ligase, chloroplastic
- Adenylosuccinate lyase
- Adenylosuccinate lyase
- AICARFT/IMPCHase bienzyme family protein
- Amidophosphoribosyltransferase 2, chloroplastic
- Urease accessory protein D
- phosphoribosylaminoimidazole carboxylase
Sequence:
MNTSQATRAALFLNGSNRQAMLLQRSSMSQLWGSVRMRTSRLSLNRTKAVSLRCSAQPNKPKAAVSTGSFVTADELPSLVEKPAAEVIHFYRVPLIQESANAELLKAVQTKISNQIVSLTTEQSFNIGLESKLKDEKLSVLKWILQETYEPENLGTDSFLERKKQEGLHAVIVEVGPRLSFTTAWSTNAVSICRACGLDEVTRLERSRRYLLFSKEPLLENQIKEFAAMVHDRMTECVYTQKLVSFETNVVPEEVKYVPVMEKGRKALEEINQEMGLAFDEQDLQYYTRLFREDIKRDPTNVELFDIAQSNSEHSRHWFFAGNMVIDGKPMDKSLMQIVKSTWEANRNNSVIGFKDNSSAIRGFLVNQLRPLLPGSVCLLDVSARDLDILFTAETHNFPCAVAPYPGAETGAGGRIRDTHATGRGSFVVASTSGYCVGNLNMEGSYAPWEDSSFQYPSNLASPLQILIDASNGASDYGNKFGEPMIQGYTRTFGMRLPSGDRREWLKPIMFSAGIGQIDHTHITKGEPEVGMLVVKIGGPAYRIGMGGGAASSMVSGQNDAELDFNAVQRGDAEMSQKLYRVVRACIEMGEKNPIISIHDQGAGGNCNVVKEIIYPQGAEIDIRAVVVGDHTMSVLEIWGAEYQEQDAILVKAESREILQSICKRERLSMAVIGTINGGGRCTLIDSTAAAKCSKEGLPPPPPAVDLELEKVLGDMPKKTFKFNRIAYAREPLDIAPGITLMDALKRVLRLPSVSSKRFLTTKVDRCVTGLVAQQQTVGPLQITLADVAVIAQTFTDLTGGACAIGEQPIKGLLDPKAMARLAVGEALTNLVWAKVTALSDVKASGNWMYAAKLEGEGSAMYDAAIALSEAMIELGIAIDGGKDSLSMAAHADGEVVKAPGNLVISAYVTCPDITKTVTPDLKLGGDDGILLHVDLAKGKRRLGGSALAQVFGQIGNDCPDLDDVPYLKNVFDGVQALIAENLVSAGHDISDGGLVVTALEMAFAGNKGINLDLASNGISLFETLFSEELGLVLEISKTNLDAVMEKLRAFDVTAEIIGNVTDSPLIEVKVDGITHLSEKTSFLRDMWEDTSFQLEKLQRLASCVEMEKEGLKFRHEPNWKLSFIPSSTNNNYMSQDVKPKVAVIREEGSNGDREMSAAFYAAGFEPWDVTVSDLLAGDITLDQFRGIVFVGGFSYADVLDSAKGWAASIRFNEPVLSQFQEFYKRPDTFSLGICNGCQLMALLGWVPGPQVGGSLDTSQPRFVHNESGRFECRFTSVTIKDSPSIMLKGMEGSTLGVWAAHGEGRAYFPDEGVLDHMLHSDLAPLRYCDDDGNVTEAYPFNLNGSPLGIAAICSPDGRHLAMMPHPERCFLMWQFPWYPTSWDVEKAGPSPWLKMFQNARDWLESC
Protein: Myosin phosphatase Rho interacting protein (J3KSW8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KKKRKVEPPTPQEPGPAKVAVTSSSSSSSSSSSIPSAEKVPTTKSTLWQEEMRTKDQPDGSSLSPAQSPSQSQPPAASSLREPGLESKEEESAMSSDRMDCGRKVRVESGYFSLEKTKQDLKAEEQQLPPPLSPPSPSTPNHRRSQVIEKFEALDIEKAEHMETNAVGPSPSSDTRQGRSEKRAFPRKRPDLLNFKKGWLTKQYEDGQWKKHWFVLADQSLRYYRDSVAEEAADLDGEIDLSACYDVTEYPVQRNYGFQIHTKEGEFTLSAMTSGIRRNWIQTIMKHVHPTTAPDVTSSLPEEKNKSSCSFETCPRPTEKQEAELGEPDPEQKRSRARERRREGRSKTFDWAEFRPIQQALAQERVGGVGPADTHEPLRPEAEPGELERERARRREERRKRFGMLDATDGPGTEDAALRMEVDRSPGLPMSDLKTHNVHVEIEQRWHQVETTPLREEKQVPIAPVHLSSEDGGDRLSTHELTSLLEKELEQSQKEASDLLEQNRLLQDQLRVALGREQSAREGYVLQATCERGFAAMEETHQKKIEDLQRQHQRELEKLREEKDRLLAEETAATISAIEAMKNAHREEMERELEKSQRSQISSVNSDVEALRRQYLEELQSVQRELEVLSEQYSQKCLENAHLAQALEAERQALRQCQRENQELNAHNQELNNRLAAEITRLRTLLTGDGGGEATGSPLAQGKDAYELEVLLRVKESEIQYLKQEISSLKDELQTALRDKKYASDKYKDIYTELSIAKAKADCDISRLKEQLKAATEALGEKSPDSATVSGYDIMKSKSNPDFLKKDRSCVTRQLRNIRSKSLKEGLTVQERLKLFESRDLKKD
Protein: Ubiquitin-fold modifier 1 (A8DYH2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to substrate proteins as a monomer or a lysine-linked polymer (By similarity). The so-called ufmylation, requires the UFM1-activating E1 enzyme Uba5, the UFM1-conjugating E2 enzyme Ufc1, and the UFM1-ligase E3 enzyme Ufl1 (By similarity). This post-translational modification on lysine residues of proteins may play a crucial role in a number of cellular processes (By similarity). The Ufm1 cascade might play a role in the development of the neuromuscular junctions.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P61960}. Cytoplasm {ECO:0000250|UniProtKB:P61960}.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme 5
- Ubiquitin-fold modifier-conjugating enzyme 1
- Probable Ufm1-specific protease 2
- Probable Ufm1-specific protease 1
- E3 UFM1-protein ligase 1 homolog
- Ubiquitin-like protein NEDD8
- Adenylyltransferase and sulfurtransferase MOCS3
- DDRGK domain-containing protein 1
- E1 ubiquitin-activating enzyme
- Autophagy protein 12-like
Sequence:
MSKVTFKITLTSDPKLPFKVLSVPEGTPFTAVLKFASEEFKVPAETSAIITDDGIGISPQQTAGNVFLKHGSELRLIPRDRVGHQLS
Protein: Type 2 DNA topoisomerase 6 subunit B (EC 5.6.2.2) (Type II DNA topoisomerase VI subunit B) (TopoVI-B) (O05207)
Organism: Saccharolobus shibatae (strain ATCC 51178 / DSM 5389 / JCM 8931 / NBRC 15437 / B12) (Sulfolobus shibatae)
Function: Relaxes both positive and negative supercoils and exhibits a strong decatenase and unknotting activity; it cannot introduce DNA supercoils. ATP is absolutely required for DNA cleavage; the nonhydrolyzable analog AMP-PNP generates nicked or linear products from a supercoiled dsDNA substrate. Generates staggered two-nucleotide long 5' overhangs. The enzyme is covalently attached transiently to the 5'-ends of the cleaved strands.
Interaction partners:
Sequence:
MSAKEKFTSLSPAEFFKRNPELAGFPNPARALYQTVRELIENSLDATDVHGILPNIKITIDLIDDARQIYKVNVVDNGIGIPPQEVPNAFGRVLYSSKYVNRQTRGMYGLGVKAAVLYSQMHQDKPIEIETSPVNSKRIYTFKLKIDINKNEPIIVERGSVENTRGFHGTSVAISIPGDWPKAKSRIYEYIKRTYIITPYAEFIFKDPEGNVTYYPRLTNKIPKPPQEVKPHPYGVDREEIKILINNLKRDYTIKEFLVNEFQSIGDTTADKILELAGLKPNKKVKNLTEEEITRLVETFKKYEDFRSPSADSLSVIGEDLIELGLKKIFNPDFAASITRKPKAYQGHPFIVEAGVAFGGSIPVGEEPIVLRYANKIPLIYDEKSDVIWKVVEELDWKRYGIESDQYQMVVMVHLCSTKIPYKSAGKESIAEVEDIEKEIKNALMEVARKLKQYLSEKRKEQEAKKKLLAYLKYIPEVSRSLATFLASGNKELVSKYQNEISEGLFKLISKKLDLINIEEYRKVYRVDSE