wanglab/gogpt-training-data huggingface dataset:
Protein: Actin binding protein (Q75JH9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Gelation factor
- Cortexillin-1
- Dynacortin
Sequence:
MSDDKIHLKVRLVDKKVFKKFSFYPKKTVKEARLFIAAELEVDPDQYGLFLPPKDDQNGVWFRDDYPLDFYGLEGENEKEALLFTSKDSAQMEFVEFKKRYRPIKVGKGDNQFRTLMVDDTMNVSDIVKYVSTQVPISSAIDREQYDQMNMYEVEELSNDMTVREQGYVGECTTNLLRGAKGDLGLCVQVPYFEGFIMRKRGGGLIKGLKNWNKRWYSLRKNKLLYFKSKSDSTEMGCILMKTVQTVRPCTEVADIPSKYSKMCFEIVTPARTFVMLANNVSDMKKWVEILESSRRMFAYETHFFGVASKKISEGGGGSFINDDDDDDDDDDENSERKEQKRRLQEQKMEKERQEKERIQAEEKARQDEVERQERIRIEQEQAERQFIEQELARAEEERKERIRQEQEEQDRQEQERRRIEEEEMVKLMIEEEERRRKLEEKRQEDLRKIQEEQELLVKQQQEFIAKQQQLELEKQRQLQDQLEEDRRLEELMLQMEMDQEERIKVKEEQERQEQEKLELAKKMQEEEEKLKEEQERIRLEQERVEKERQEEEKRMELERIEEERLEAIRIEKVRIEKEERERKEEEERKEKERKRQEEEERIKKEQEEKIRQFEEEKKKQEELRLIEQERIRVEQELIRKERLELEEKQRIEQIEKEQQQQLLLLEQSKQSDTDNENVDMMDEFEREEEEREKEQLASKRLRSLQARLESVCAETPELKLLLSEAILSSPENLLLSWANYIVSGISSPSLHSSSRSHIQSELSSSTSGSGLLANNGILLNDGSSVDSNGSNSGVGNSINNANGSSSNSGGRVLKPSTASVTLVPSTASIGSNAGCSISAELSRASLLSSGHLVGSQAVSLVQLKNLKSLDANLEMYANLLFKLEPQEFSLQHYVTLTTNAERAQYIHACLVKLGVTTITEEQLLSSDSDQHLNVLLTIYEEVGGEQWKEEFHTQVVSKRSFATKYIQQLLSNCVSAGLNIATSPEELLPTLMSGRVLCELINKVYPGTIDERVIQKTQQFCKKNLMLAYNGAKALGATSVPDIVFLSDDKDTISSTVLHNLTWSIVETCLLQSADPTKNRHLFHLLRAETRTSFMKLEKEKIMLRWFNYHLRKGSSRSINNFTDDLEDCENYAYLFSIIAPQHSLKSEILKENDWEKRAEMVLSMAAKIGCMSLLSPRDIVETENSQLNQLFVADIMRVAHGLPAYQFRLDVEQLDDQVQKSKDQGNNDVELLQWVNGLAIDGVDAKHLLEDFKSGYLFLKIFEKVTPPGTLDAKRFKTNPTSVFKMVELCNYTMEICHKFKLNVAGTAGTDLANGDIRSNRAILNQIRRVIVGEKTVVDSVIANQSAVLKWANNKIGLDVKVKSIQSFKDQFLQDGLFLLELLSSIEQNSVDRKNIITNCSNEEQQESNCRYFLSCAWSTGIPLNVVWEDVQKVRSKSIKHIVETLQSWDLLKSQHQNLINNNNNNNNNNSNNNNNNINNNNNNNSNNNNSNNNNNNSNNI
Protein: Calumenin-like protein (EF-hand domain-containing protein) (G5EBH7)
Organism: Caenorhabditis elegans
Interaction partners:
- alpha-1,2-Mannosidase
- Ubiquitin-like domain-containing protein
- Membrane-bound transcription factor site-2 protease
- NUCleoBindin homolog
- Calreticulin
- Large ribosomal subunit protein uL10
- Endoplasmic reticulum transmembrane protein
- CDK5RAP3 protein homolog
- Nuclear migration protein nudC
Sequence:
MKVLLFVGLLAATALASHHSSDPSKDGEHFKGKEHDKKYDHEQFLGKDTAAEFDELTPEKSKEKLAKLVPKMDADSDGFIEENELKDHINFMQKRYVNNDVDRTWKNYKAEKIVDGKIKWEDYREMVYGSADGAGQELSPEYAKMIARDEKRWAVADYDSNGALDRTEYGCFMHPEDCDHMRDVVVAETVDDIDKNKDGSVDLDEYIGDMYRPDDYPELNGKEPDWVQSEREMFKEHRDKDGDGKLNQEEMRDWIMPVGFDHAEAEARHLVGIADDNKDGKLNLDEIVAHYDTFVGSQATDYGEQLQKHDPAEL
Protein: Dynein light chain (RE37471p) (Uncharacterized protein, isoform A) (Uncharacterized protein, isoform B) (Uncharacterized protein, isoform C) (Q9VH45)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dynein light chain Tctex-type
- Dynein light chain roadblock
- Dynein light chain roadblock
- IP01982p
- Dynein light chain roadblock
- Dynein light chain 1, cytoplasmic
- Cytoplasmic dynein 2 light intermediate chain 1
- Sperm-specific dynein intermediate chain 1, isoform A
- Dynein light chain roadblock
- Ig-like domain-containing protein
Sequence:
MADKQSTEETTKSVQTLTVPNPADRKSEKSASGSLHSGSADGLENQEKSEKPGDQPTAYSMRPAFGEMFPLPTIKSIMNNVMAEKLKDKTYDKDVAKKWTSEIADEVNQQIASSSLVKRYKHVVQVMLGQELGAGATYNSRCCWDCDCDTSVSEVFSNTSLFCVCTVFGTYQY
Protein: Zinc finger protein 90 (Zfp-90) (Q4V8A8)
Organism: Rattus norvegicus (Rat)
Function: Inhibits the transcriptional repressor activity of REST by inhibiting its binding to DNA, thereby derepressing transcription of REST target genes.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q61967}. Note=Colocalizes with REST in the nucleus. {ECO:0000250|UniProtKB:Q61967}.
Interaction partners:
Sequence:
MAPRPPTATPQESVTFKDVAVNFTQEEWRHVGPAQRSLYRDVMLENYSHLVSLGYQVSKPEVIFKLEQGEEPWISERELQRPFCPDWKTRPDIKSWSSQQGVSEVSHSANVWSHATFGDIWGVNTQRHQESWRRHLGPEASSQKKITALEKIAEQNKFGEDSGLSTDLVPQLDVSSSIRPSECKTFGNNLEYNSELVTQSGIPAKKKPYKCDKCRKSFIHRSSLNKHEKIHKDDAYSNGTDQGVPSGRKHHECTDCGKTFLWRTQLTEHQRIHTGEKPFECNVCGKAFRHSSSLGQHENAHTGEKPYQCSLCGKAFQRSSSLVQHQRIHTGEKPYRCNLCGRSFRHSTSLTQHEVTHSGEKPFQCKECGKAFSRCSSLVQHERTHTGEKPFECSICGRAFGQSPSLYKHMRIHKRSKPYQSNNFSIAFEPNIPLTQGESVLTDVKSYHCIDCGKDFSHITDFTEHQRIHAGENSYDSEQALRQQSLSHPREKPYQCNVCGKAFKRSTSFIEHHRIHTGEKPYECNECGEAFSRLSSLTQHERTHTGEKPYECIDCGKAFSQSSSLIQHERTHTGEKPYECNECGRAFRKKTNLHDHQRIHTGEKPYACKECGKNFSRSSALTKHHRIHSRNKL
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Q8MNY0)
Organism: Caenorhabditis elegans
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Polyubiquitin-A
- Ubiquitin-like domain-containing protein
Sequence:
MASATGGWQALESNPETINPFLSKIGVSGVECVDVFSFDDEMLQFIPTPQLALILCFPSSGVREFRAKQYEEVEKNGKKPDGIFFMNQKKEIGHACGTFSLFHSLANLENRVNLGNGKFSKWFEKAKLVGEGERSDLLLADTDLAEAHKETAEEGETEHPEHVAYHFITYVNKNGQLFEIDSCSPFPRPLGATTDSTMIRDAFSTSIKDLMDNVQKLSFSAMALVGI
Protein: Nuclear receptor coactivator 5 (NCoA-5) (Coactivator independent of AF-2) (CIA) (Q91W39)
Organism: Mus musculus (Mouse)
Function: Nuclear receptor coregulator that can have both coactivator and corepressor functions. Interacts with nuclear receptors for steroids (ESR1 and ESR2) independently of the steroid binding domain (AF-2) of the ESR receptors, and with the orphan nuclear receptor NR1D2. Involved in the coactivation of nuclear steroid receptors (ER) as well as the corepression of MYC in response to 17-beta-estradiol (E2) (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:24268775}.
Interaction partners:
- Estrogen receptor beta
- E3 SUMO-protein ligase RanBP2
- Nuclear pore complex protein Nup93
- Nucleoporin 205
- Nuclear pore complex protein Nup155
- Nuclear pore complex protein Nup54
- Nuclear pore complex protein Nup107
- Nuclear pore complex protein Nup133
- Protein SEC13 homolog
- Nuclear pore complex protein Nup85
Sequence:
MNTAPSRPSPTRRDPYSFGDSRDTRRDRSPIRGSPRREPRDGRNGRDARDSRDIRDPRDLRDRRDSRDIRDHRDSRSVREARDLRDFRDFRDLRDSRDFRDHRDPVYDRYRDIRDSRDPLYRREGSYDRYLRVDDYCRRKDDSYFDRYRDSFDGRGPPGPESQSRAKERLKREERRREELYRRYFEEIQRRFDAERPVDCSVIVVNKQTKDYAESVGRKVRDLGMVVDLIFLNTEVSLSQALEDVSRGGSPFAIVITQQHQIHRSCTVNIMFGTPQEHRNMPQADAMVLVARNYERYKNDCREKEREEIARQAAKMANDAILQERDRGGPEEGGRGGHPPAIQSLINLLADNRYLTAEETDKIINYLRERKERLLRSSADSLPGPISRQPLGAASGSSLKSQPSSQPLQSGQVLPSATPTPAAPPTSQQELQAKILSLFNSGAVAANSSSASPSVATGSSQNQNFSTAANSQPQQRPQASGNQPPNIVGQAGSARNMGPRPGAPSQGLFGQPSSRLAPASTMASQRPVSSTGINFDNPSVQKALDTLIQSGPALSHLVSQTAAQVGRPQAPMGSYQRHY
Protein: Acyl-CoA dehydrogenase family member 9 (Acyl-Coenzyme A dehydrogenase family, member 9, isoform CRA_b) (cDNA FLJ12506 fis, clone NT2RM2001700, weakly similar to ACYL-COA DEHYDROGENASE, VERY-LONG-CHAIN SPECIFIC) (Q9H9W4)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004637}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004637}.
Interaction partners:
Sequence:
MYSRLGEIISMDGSITVTLAAHQAIGLKGIILAGTEEQKAKYLPKLASGEHIAAFCLTEPASGSDAASIRSRATLSEDKKHYILNGSKVWITNGGLANIFTVFAKTEVVDSDGSVKDKITAFIVERDFGGVTNGKPEDKLGIRGSNTCEVHFENTKIPVENILGEVGDGFKVAMNILNSGRFSMGSVVAGLLKRLIEMTAEYACTRKQFNKRLSEFGLIQEKFALMAQKAYVMESMTYLTAGMLDQPGFPDCSIEAAMVKVFSSEAAWQCVSEALQILGGLGYTRDYPYERILRDTRILLIFEGTNEILRMYIALTGLQHAGRILTTRIHELKQAKVSTVMDTVGRRLRDSLGRTVDLGLTGNHGVVHPSLADSANKFEENTYCFGRTVETLLLRFGKTIMEEQLVLKRVANILINLYGMTAVLSRASRSIRIGLRNHDHEVLLANTFCVEAYLQNLFSLSQLDKYAPENLDEQIKKVSQQILEKRAYICAHPLDRTC
Protein: Golgin IMH1 (Integrins and myosins homology protein 1) (Q06704)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in vesicular transport between an endosomal compartment and the Golgi apparatus.
Subcellular location: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Note=IMH1 is recruited to the Golgi apparatus by ARL1.
Interaction partners:
- ADP-ribosylation factor-like protein 1
- GTP-binding protein YPT6
- ADP-ribosylation factor-like protein 3
- Protein SGM1
- GRIP domain-containing protein RUD3
- Protein SYS1
- Vacuolar protein sorting-associated protein 53
- Vacuolar protein sorting-associated protein 52
Sequence:
MFKQLSQIGKNLTDELAKGLADDMSPTPSEQQIEDDKSGLPKEIQAKLRKFEKYEQKYPLLLSAYKNEKLKSEKLEAVEKILAENTPISNIDDAVDTLPAFFQDLNNKNNLLNDEIKRLTKQNSEIPESASSETLKDKEEEFLKKEQNYKNDIDDLKKKMEALNIELDTVQKEKNDTVSGLREKIVALENILKEEREAKKQKEEVSISELKEELAIKNHSLEDSRMKITELEQNLSSKSTIMEEKSSELAELNITLKEKERKLSELEKKMKELPKAISHQNVGNNNRRKKNRNKGKKNKGGITTGDISEEETVDNSINTEEYDKLKENLQELQEKYKDCEDWKQKYEDIEAELKDAKELENSQLEKSAKELETLNTELIDTKKSLKEKNSELEEVRDMLRTVGNELVDAKDEIKESSSKQNEEVKTVKLELDDLRHKNATMIEAYEAKNTELRSKIELLSKKVEHLKNLCTEKEKEQTTSQNKVAKLNEEISQLTYEKSNITKELTSLRTSYKQKEKTVSYLEEQVKQFSEQKDVAEKSTEQLRKDHAKISNRLDLLKKENETLHNDIAKNSNSYEEYLKENGKLSERLNILQEKYNTLQNVKSNSNEHIDSIKRQCEELNVKLKESTKKILSLEDELNEYANIVQDKTREANTLRRLVSDSQTDDSSKQKELENKLAYLTDEKNKLEAELDLQTSRKATELQEWKHTVTELKSEIHALKLREEGLKSEVDALKHVNNDIKRKTQATSDDSDQLEQITSNLKLSLSKADEKNFELQSANEKLLNLNNELNKKFDRLLKNYRSLSSQLNALKERQYSDKSGRVSRSGSIGTLANANIDSSPANNSNPTKLEKIRSSSSLELDSEKNEKIAYIKNVLLGFLEHKEQRNQLLPVISMLLQLDSTDEKRLVMSLK
Protein: Hyaluronan synthase 1 (EC 2.4.1.212) (Hyaluronate synthase 1) (Hyaluronic acid synthase 1) (HA synthase 1) (Q61647)
Organism: Mus musculus (Mouse)
Function: Catalyzes the addition of GlcNAc or GlcUA monosaccharides to the nascent hyaluronan polymer. Therefore, it is essential to hyaluronan synthesis a major component of most extracellular matrices that has a structural role in tissues architectures and regulates cell adhesion, migration and differentiation. This is one of the isozymes catalyzing that reaction. Also able to catalyze the synthesis of chito-oligosaccharide depending on the substrate.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Hyaluronidase-1
- Hyaluronidase-2
- UDP-glucose 6-dehydrogenase
Sequence:
MRQDMPKPSEAARCCSGLARRALTIIFALLILGLMTWAYAAGVPLASDRYGLLAFGLYGAFLSAHLVAQSLFAYLEHRRVAAAARRSLAKGPLDAATARSVALTISAYQEDPAYLRQCLTSARALLYPHTRLRVLMVVDGNRAEDLYMVDMFREVFADEDPATYVWDGNYHQPWEPAEATGAVGEGAYREVEAEDPGRLAVEALVRTRRCVCVAQRWGGKREVMYTAFKALGDSVDYVQVCDSDTRLDPMALLELVRVLDEDPRVGAVGGDVRILNPLDSWVSFLSSLRYWVAFNVERACQSYFHCVSCISGPLGLYRNNLLQQFLEAWYNQKFLGTHCTFGDDRHLTNRMLSMGYATKYTSRSRCYSETPSSFLRWLSQQTRWSKSYFREWLYNALWWHRHHAWMTYEAVVSGLFPFFVAATVLRLFYAGRPWALLWVLLCVQGVALAKAAFAAWLRGCVRMVLLSLYAPLYMCGLLPAKFLALVTMNQSGWGTSGRKKLAANYVPVLPLALWALLLLGGLARSVAQEARADWSGPSRAAEAYHLAAGAGAYVAYWVVMLTIYWVGVRRLCRRRSGGYRVQV
Protein: Protein SSX1 (Cancer/testis antigen 5.1) (CT5.1) (Synovial sarcoma, X breakpoint 1) (Q16384)
Organism: Homo sapiens (Human)
Function: Could act as a modulator of transcription.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:36796361}.
Interaction partners:
- Protein SSXT
- Calcium-responsive transactivator
- Transducin-like enhancer protein 1
- Afadin- and alpha-actinin-binding protein
- Zinc finger protein 83
- Zinc finger protein 117
- Protein SSX3
- Melanoma-associated antigen C2
- Melanoma-associated antigen 1
Sequence:
MNGDDTFAKRPRDDAKASEKRSKAFDDIATYFSKKEWKKMKYSEKISYVYMKRNYKAMTKLGFKVTLPPFMCNKQATDFQGNDFDNDHNRRIQVEHPQMTFGRLHRIIPKIMPKKPAEDENDSKGVSEASGPQNDGKQLHPPGKANISEKINKRSGPKRGKHAWTHRLRERKQLVIYEEISDPEEDDE
Protein: Cytokine receptor-like factor 2 (Thymic stromal lymphopoietin protein receptor) (TSLP receptor) (Q8R4S8)
Organism: Rattus norvegicus (Rat)
Function: Receptor for thymic stromal lymphopoietin (TSLP). Forms a functional complex with TSLP and IL7R which is capable of stimulating cell proliferation through activation of STAT3 and STAT5 (By similarity). Also activates JAK2 (By similarity). Implicated in the development of the hematopoietic system.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Interleukin-7 receptor subunit alpha
- Thymic stromal lymphopoietin
- Tyrosine-protein kinase JAK2
- Interleukin-33
- Interleukin-7
- Tyrosine-protein kinase
- Interleukin-4
- Interleukin-13
- Interleukin-5
- Tyrosine-protein kinase JAK3
Sequence:
MRAVTWAIVAMLLPRVLGAIPTRTPRTGGVGDTLSVAIVCHDLESVEVTWGPGSAHHGLSANLSLEFRYGNQVPQPCPHYFLLDSVRAGCVLPMGKGLLEVVLREGGGAKLFSRKKKASAWLRPRPPWNVTLSWVGDTVAVSCPSHSYPGLEYEVQHRDDFDPEWQSTSAPFCNLTVGGLDPGRCYDFRVRATPQDFYYGPEARPSKWTGVASLQGVGPTGSCTGPTLPRTPGTPTPPLALACGLAVALLTLVLLLALLRMRRVKEALLPGVPDPRGSFPGLFEKHHGNFQAWIADSQAAVPTVPEQDKDDDVIRPQTKGVETQEDDDVIAPGSPCLGGGALMSVGGASFLMGDSGYTTL
Protein: Probable small nuclear ribonucleoprotein E (snRNP-E) (Sm protein E) (Sm-E) (SmE) (Q9XTU6)
Organism: Caenorhabditis elegans
Function: Plays a role in pre-mRNA splicing as a core component of the spliceosomal U1, U2, U4 and U5 small nuclear ribonucleoproteins (snRNPs), the building blocks of the spliceosome.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P62304}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62304}.
Interaction partners:
- Probable small nuclear ribonucleoprotein-associated protein B
- Probable small nuclear ribonucleoprotein F
- Probable small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D3
- Probable small nuclear ribonucleoprotein G
- Probable small nuclear ribonucleoprotein Sm D2
- U6 snRNA-associated Sm-like protein LSm5
- U6 snRNA-associated Sm-like protein LSm6
- U6 snRNA-associated Sm-like protein LSm8
- U6 snRNA-associated Sm-like protein LSm2
Sequence:
MSTRKLNKVMVQPVNLIFRYLQNRTRVQIWLYEDVTHRLEGYIIGFDEFMNVVFDEAEEVNMKTKGRNKIGRILLKGDNITLIHAAQQEA
Protein: DNA polymerase processivity factor BMRF1 (Early Antigen Diffused) (EA-D) (Polymerase accessory subunit) (P03191)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Acts as a DNA polymerase processivity factor; a transcriptional activator for several EBV promoters and inhibits the host DNA damage response (DDR) to double-stranded DNA breaks. Plays an essential role in the viral lytic DNA replication by acting as a polymerase accessory subunit. Stimulates the viral DNA polymerase activity and appears to function with it as a holoenzyme. Increases the processivity of the viral polymerase, probably by acting as a sliding clamp that prevents dissociation of the polymerase from the active template. In addition, BMRF1 transcriptionally activates the oriLyt early BHLF1 promoter. Promotes G1/S cell cycle arrest through p53 induction.
Subcellular location: Virion tegument. Host nucleus. Note=BMRF1 shows homogeneous, not dot-like, distribution in the replication compartments, which coincides with the newly synthesized viral DNA.
Interaction partners:
Sequence:
METTQTLRFKTKALAVLSKCYDHAQTHLKGGVLQVNLLSVNYGGPRLAAVANAGTAGLISFEVSPDAVAEWQNHQSPEEAPAAVSFRNLAYGRTCVLGKELFGSAVEQASLQFYKRPQGGSRPEFVKLTMEYDDKVSKSHHTCALMPYMPPASDRLRNEQMIGQVLLMPKTASSLQKWARQQGSGGVKVTLNPDLYVTTYTSGEACLTLDYKPLSVGPYEAFTGPVAKAQDVGAVEAHVVCSVAADSLAAALSLCRIPAVSVPILRFYRSGIIAVVAGLLTSAGDLPLDLSVILFNHASEEAAASTASEPEDKSPRVQPLGTGLQQRPRHTVSPSPSPPPPPRTPTWESPARPETPSPAIPSHSSNTALERPLAVQLARKRTSSEARQKQKHPKKVKQAFNPLI
Protein: Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein (P-Rex1) (PtdIns(3,4,5)-dependent Rac exchanger 1) (Q69ZK0)
Organism: Mus musculus (Mouse)
Function: Functions as a RAC guanine nucleotide exchange factor (GEF), which activates the Rac proteins by exchanging bound GDP for free GTP. Its activity is synergistically activated by phosphatidylinositol 3,4,5-trisphosphate and the beta gamma subunits of heterotrimeric G protein. May function downstream of heterotrimeric G proteins in neutrophils (By similarity).
Subcellular location: Cytoplasm, cytosol. Cell membrane. Note=Mainly cytosolic. Some amount is apparently associated to the plasma membrane (By similarity). {ECO:0000250}.
Interaction partners:
- Ras-related C3 botulinum toxin substrate 2
- Ras-related C3 botulinum toxin substrate 3
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
Sequence:
MEAPGSGGGDGGGDPGGDGAHPDARGPVSGPCAAARDSERQLRLRLCVLNEILGTERDYVGTLRFLQSAFLQRIRQNVADSVEKGLTEENVKVLFSNIEDILEVHKDFLAALEYCLHPEPQSQHELGNVFLKFKDKFCVYEEYCSNHEKALRLLVELNKVPAVRAFLLSCMLLGGRKTTDIPLEGYLLSPIQRICKYPLLLKELAKRTPGKHPDHTAVQSALQAMKTVCSNINETKRQMEKLEALEQLQSHIEGWEGSNLTDICTELLLQGNLLKISAGNIQERAFFLFDNLLVYCKRKSRVTGSKKSTKRTKSINGSLYIFRGRINTEVMEVENVEDGTADYHSNGYTVTNGWKIHNTAKNKWFVCMAKTAEEKQKWLDALIREREQRESLKLGMERDAYVMIAEKGEKLYHMMMSKKVNLIKDRRRKLSTVPKCFLGNEFVAWLLEIGEISKTEEGVNLGQALLENGIIHHVSDKHQFKNEQVMYRFRYDDGTYKARSELEDIMSKGVRLYCRLHSLYAPVIKDRDYHLKTYKSVVPGSKLVDWLLAQGDCQTREEAVALGVGLCNNGFMHHVLEKSEFKDESQYFRFHADEEMEGTSSKNKQLRNDFKLVENILAKRLLIPPQEDDYGFDLEEKNKAVVVKSVQRGSLAEMAGLQAGRKIYSINEDLVFLRPFSEVETILNQFFCSRRPLRLLVATKAKETIKVPDHPEALSFQIRGTAPPCVFAVGRGSEAVAAGLCAGQCILKVNGTSVANDGALEVLEHFQAFRNHREEALGLYQWVYHSHEDAQLARASQGAPDEDPQEDDQPDSALPLLSLGPQLSLHEDSAVVSLTLDNVHLEHGVVYEYMSTAGAKCHVLEKIVEPRGCFRLAAKILEAFAVDDSIFVQNCGRLMAMSSAIVTMSHYEFHNICDTKLESIGQRIACYQEFAAQLKSRVSPPFKQASLEPHPLCGLDFCPTNCHVNLMEVSYPKTTPSVGRSFSIRFGRKPSLIGLDPEQGLNPMAYTQHCITTMAAPSWKCSPAVDEDSQGQGLNDSSYGSASGAPSQQDRGLSFLLKQEDREIQDAYLQLFTKLDVALKEMKQYVTQINRLLSTITEPTSAAPAPCDPSLVEETSSSPPVSEESEVDRTDHSGIKKVCFKVSEDEQEDSGHDTMSYRDSYSECNSNRDSVLSYTSVRSNSSYLGSDEMGSGDELPCDMRIPSDKQDKLHGCLEHLFNQVDSIHALLKGPVMSRAFEETRHFPMKHSWQEFKQKEECTVRGRNLIQISIQEDPWNLPSSIRTLVDNIQQYVEDGKNQLLLALLKCTDTELQLRRDAVFCQALVAAVCTFSEQLLAALDYRYNNNGEYEESSRDASRKWLEQVAATGVLLHWQSLLAPASVKEERTMLEDIWVTLSELDNVTFSFKQLDENSVANTNVFYHIEGSRQALKVVFYLDGFHFSRLPSRLEGGASLRLHTVLFTKALESVEGPPPPGNQAAEELQQEINAQSLEKVQQYYRKLRAFYLERSNLPTDAGATAVKIDQLIRPINALDELYRLMKTFVHPKAGAAGSLGAGLIPVSSELCYRLGACQITMCGTGMQRSTLSVSLEQAAILARSHGLLPKCVMQATDIMRKQGPRVEILAKNLRIKDPMPQGAPRLYQLCQPPVDGDL
Protein: Free fatty acid receptor 1 (G-protein coupled receptor 40) (O14842)
Organism: Homo sapiens (Human)
Function: G-protein coupled receptor for medium and long chain saturated and unsaturated fatty acids that plays an important role in glucose homeostasis. Fatty acid binding increases glucose-stimulated insulin secretion, and may also enhance the secretion of glucagon-like peptide 1 (GLP-1). May also play a role in bone homeostasis; receptor signaling activates pathways that inhibit osteoclast differentiation (By similarity). Ligand binding leads to a conformation change that triggers signaling via G-proteins that activate phospholipase C, leading to an increase of the intracellular calcium concentration. Seems to act through a G(q) and G(i)-mediated pathway. Mediates the anti-inflammatory effects of omega-3 polyunsaturated fatty acids (PUFAs) via inhibition of NLRP3 inflammasome activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17699519, ECO:0000269|PubMed:25043059}; Multi-pass membrane protein {ECO:0000269|PubMed:25043059}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Free fatty acid receptor 4
- Pro-glucagon
- Gastric inhibitory polypeptide
- Guanine nucleotide-binding protein subunit alpha-11
- Galanin receptor type 2
- G-protein coupled receptor 84
- Galanin receptor type 1
- Glucose-dependent insulinotropic receptor
- Galanin peptides
Sequence:
MDLPPQLSFGLYVAAFALGFPLNVLAIRGATAHARLRLTPSLVYALNLGCSDLLLTVSLPLKAVEALASGAWPLPASLCPVFAVAHFFPLYAGGGFLAALSAGRYLGAAFPLGYQAFRRPCYSWGVCAAIWALVLCHLGLVFGLEAPGGWLDHSNTSLGINTPVNGSPVCLEAWDPASAGPARFSLSLLLFFLPLAITAFCYVGCLRALARSGLTHRRKLRAAWVAGGALLTLLLCVGPYNASNVASFLYPNLGGSWRKLGLITGAWSVVLNPLVTGYLGRGPGLKTVCAARTQGGKSQK
Protein: Transport and Golgi organization protein 11 (Tango-11) (Q961C9)
Organism: Drosophila melanogaster (Fruit fly)
Function: May play a role in mitochondrial and peroxisomal fission.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16452979}; Single-pass type IV membrane protein {ECO:0000269|PubMed:16452979}. Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Peroxisome {ECO:0000250}.
Interaction partners:
- Mitochondrial fission 1 protein
- dynamin GTPase
- Transmembrane GTPase Marf
- Dynamin
- Gdap1, isoform A
- Dynamin-like GTPase OPA1, mitochondrial
- Transmembrane GTPase fzo
Sequence:
MVTPQSPTPMFNGLDDDLYSDAKYAHEINDKMRVPKRIKATGEYSNEDLLLSNQNGMISSWNYHDKIDMNVPDRIVVLGHNQHLETRSAPREIQLENSILPKNPSVGLVRVQTPPRIITLTDQHFPSASEESSPIRANGHHLYGNDLDEDADDEEVHATQYVRANGVARMGFQGNDTNSVESDSQLTTGSASKRSQLNQQQHNNLDASMLAHREGTPMGELTPHEEILYLRRQLAKLNRRVLNIEINNEQRTQREKIVYCLGLAYFVLKTIFWLNRN
Protein: Protein SAWADEE HOMEODOMAIN HOMOLOG 1 (DNA-binding transcription factor 1) (Q9XI47)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in RNA-directed DNA methylation (RdDM). Required for the silencing of some endogenous RdDM targets and accumulation of 24-nt siRNAs, but not for the production of Pol V-dependent transcripts. Functions in transcriptional silencing through both DNA methylation-dependent and -independent pathways. Required for both maintenance and de-novo DNA methylation. Plays a role in the recruitment of Pol IV to genomic regions associated with K9 methylated histone H3 that are targets for RdDM.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone H3.1
- Histone H3.3
- SNF2 domain-containing protein CLASSY 1
- DNA-directed RNA polymerase IV subunit 1
- Protein DEFECTIVE IN MERISTEM SILENCING 3
- RNA-dependent RNA polymerase 2
- Histone H3-like centromeric protein CENH3
- Histone H3-like 2
- Histone H3-like 3
- Histone H3-like 4
Sequence:
MAASDDSSHYFTEFTLSEIVDMENLYKELGDQSLHKDFCQTVASTFSCSVNRNGKSSITWKQVQIWFQEKLKHQSQPKSKTLPSPPLQIHDLSNPSSYASNASNATFVGNSTFVQTRKGKASDLADLAFEAKSARDYAWYDVSSFLTYRVLRTGELEVRVRFSGFDNRHDEWVNVKTSVRERSIPVEPSECGRVNVGDLLLCFQEREDQALYCDGHVLNIKRGIHDHARCNCVFLVRYELDNTEESLGLERICRRPEE
Protein: Fatty acid oxidation complex subunit alpha [Includes: Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] (P28793)
Organism: Pseudomonas fragi
Function: Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate.
Interaction partners:
- 3-ketoacyl-CoA thiolase
- isovaleryl-CoA dehydrogenase
- acyl-CoA dehydrogenase
- acetyl-CoA acetyltransferase
- acetyl-CoA acetyltransferase
- acetyl-CoA acetyltransferase
- acyl-CoA dehydrogenase
- methylcrotonoyl-CoA carboxylase
- enoyl-CoA hydratase
- acetyl-CoA acetyltransferase
Sequence:
MIYEGKAITVTALESGIVELKFDLKGESVNKFNRLTLNELRQAVDAIKADASVKGVIVSSGKDVFIVGADITEFVENFKLPDAELIAGNLEANKIFSDFEDLNVPTVAAINGIALGGGLEMCLAADFRVMADSAKIGLPEVKLGIYPGFGGTVRLPRLIGVDNAVEWIASGKENRAEDALKVSAVDAVVTADKLGAAALDLIKRAISGELDYKAKRQPKLEKLKLNAIEQMMAFETAKGFVAGQAGPNYPAPVEAIKTIQKAANFGRDKALEVEAAGFAKLAKTSASNCLIGLFLNDQELKKKAKVYDKIAKDVKQAAVLGAGIMGGGIAYQSASKGTPILMKDINEHGIEQGLAEAAKLLVGRVDKGRMTPAKMAEVLNGIRPTLSYGDFGNVDLVVEAVVENPKVKQAVLAEVENHVREDAILASNTSTISISLLAKALKRPENFVGMHFFNPVHMMPLVEVIRGEKSSDLAVATTVAYAKKMGKNPIVVNDCPGFLVNRVLFPYFGGFAKLVSAGVDFVRIDKVMEKFGWPMGPAYLMDVVGIDTGHHGRDVMAEGFPDRMKDDRRSAIDALYEAKRLGQKNGKGFYAYEADKKGKQKKLVDSSVLEVLKPIVYEQRDVTDEDIINWMMIPLCLETVRCLEDGIVETAAEADMGLVYGIGFPLFRGGALRYIDSIGVAEFVALADQYAELGALYHPTAKLREMAKNGQSFFG