wanglab/gogpt-training-data huggingface dataset:
Protein: Protein lin-54 homolog (Myb complex protein of 120 kDa) (A1Z9E2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication at the chorion loci. During development, the complex represses transcription of developmentally controlled E2F target genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Lin-52, isoform A
- LD07342p
- LD06557p
- Transcription factor E2F2
- RE32990p
- Myb protein
- Retinoblastoma family protein
- Chromatin assembly factor 1 p55 subunit
- Transcription factor Dp
- Histone deacetylase HDAC1
Sequence:
MDTSGGNLDSLDDTEPLPELSFEDFLEPTSEKSSQHMEIEALDSEEDNIGGEDLADPANDSLNTPQFKKNVVHILEDKRLNSSGLTVLKSHAIKMVTAGGTPPAKAQVTDVKILNKLKPIPSSTLKIGSTTIATKSTPGSITKTLGNLTQIRTKDGQVIFVQKSVPGTQSSTAVTGSPSGGIRRLVAPSGIQKAVLSKGVTMASTGLVKAAVPAKASTSVPGSAITLKGIQPLAGGTAKASTSSTTATTSPSLAQPNKIQVVRTADGKIIKINQAGPSLLVNAKQGTGTTVTPGGSAATSVKLSPSTGNVVLNKPVGQVVVRTETPVKTATGSVASASATPGKMLVQSGGKQILVSNKNIIKLSPNASATSSTTHTTGGQTPSTSSGLHAIQLPGKGGIQYVRVLNNNKSAAGTSATASIPKTVQTQKITVVRPPAATGVPATSTTTSAAAASPAAASKANLAMGNTNKIVMRSMGGSIVPLPSVQTLVSKRALGAISNASKPASAASSSATPSASQELPRKHRLTDLNVQLKQSASVSSEASDSSDAGPEAKKPRYVITMQQGSQKAASQPVQKLINRTANVQRVVSSSTSPSSNSTKKIYNYVQPTGSNGAKYMICNSGVPQSSTSAMRRGYTGYVENKTRRPPPISPQQHRFKQMGPQQQSKHQQLQAQAKQRIRQQQLPTEQSTPIKVEPKLPTLPPGVKANVPAKPLFEVLKPPATAAAAGAVDPLGGMTSRRKHCNCSKSQCLKLYCDCFANGEFCQDCTCKDCFNNLDYEVERERAIRSCLDRNPSAFKPKITAPNSGDMRLHNKGCNCKRSGCLKNYCECYEAKIPCSSICKCVGCRNMEDRPDVDMDSLDGLMGVEGQKKDKAKNKQLNENRANIYFTDDVIEATIMCMISRIVMHEKQNVAVEDMEREVMEEMGESLTQIIAFAKEKQETSQIDESKPSS
Protein: Odorant receptor 7a (Q9W3I5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability. Highly sensitive to the sex pheromone of the silkworm moth, bombykol. Intriguingly, the fruit fly detectors are more sensitive than the receptors of the silkworm moth, although its ecological significance is unknown. Responds also to pyrazines.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 82a
- Odorant receptor 85b
- Odorant receptor 13a
- Odorant receptor 30a
- Odorant receptor 56a
- Odorant receptor 47a
- Odorant receptor 88a
- Odorant receptor 65a
- Odorant receptor 67b
- Odorant receptor 22c
Sequence:
MAVSTRVATKQEVPESRRAFRNLFNCFYALGMQAPDGSRPTTSSTWQRIYACFSVVMYVWQLLLVPTFFVISYRYMGGMEITQVLTSAQVAIDAVILPAKIVALAWNLPLLRRAEHHLAALDARCREQEEFQLILDAVRFCNYLVWFYQICYAIYSSSTFVCAFLLGQPPYALYLPGLDWQRSQMQFCIQAWIEFLIMNWTCLHQASDDVYAVIYLYVVRIQVQLLARRVEKLGTDDSGQVEIYPDERRQEEHCAELQRCIVDHQTMLQLLDCISPVISRTIFVQFLITAAIMGTTMINIFIFANTNTKIASIIYLLAVTLQTAPCCYQATSLMLDNERLALAIFQCQWLGQSARFRKMLLYYLHRAQQPITLTAMKLFPINLATYFSIAKFSFSLYTLIKGMNLGERFNRTN
Protein: HIG1 domain-containing protein (B7WN91)
Organism: Caenorhabditis elegans
Subcellular location: Mitochondrion membrane {ECO:0000256|ARBA:ARBA00004325}.
Interaction partners:
Sequence:
MNVAGVHEEPKKGSYEWKKEHMTPQQLARTMDNAEKYNGIPAIPVDIGYHSGKNTGGAQKTGVVSNAASNPGVILGMGLTTAALLGMFKSSFLGDKVGAQKMMQYRIMAQFFTVTALVAGVTIFGATYEDEEHQK
Protein: Endonuclease domain-containing 1 protein (EC 3.1.30.-) (O94919)
Organism: Homo sapiens (Human)
Function: May act as a DNase and a RNase. Plays a role in the modulation of innate immune signaling through the cGAS-STING pathway by interacting with RNF26.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- E3 ubiquitin-protein ligase RNF26
- Transmembrane protein 43
- Transmembrane protein 33
Sequence:
MGTARWLALGSLFALAGLLEGRLVGEEEAGFGECDKFFYAGTPPAGLAADSHVKICQRAEGAERFATLYSTRDRIPVYSAFRAPRPAPGGAEQRWLVEPQIDDPNSNLEEAINEAEAITSVNSLGSKQALNTDYLDSDYQRGQLYPFSLSSDVQVATFTLTNSAPMTQSFQERWYVNLHSLMDRALTPQCGSGEDLYILTGTVPSDYRVKDKVAVPEFVWLAACCAVPGGGWAMGFVKHTRDSDIIEDVMVKDLQKLLPFNPQLFQNNCGETEQDTEKMKKILEVVNQIQDEERMVQSQKSSSPLSSTRSKRSTLLPPEASEGSSSFLGKLMGFIATPFIKLFQLIYYLVVAILKNIVYFLWCVTKQVINGIESCLYRLGSATISYFMAIGEELVSIPWKVLKVVAKVIRALLRILCCLLKAICRVLSIPVRVLVDVATFPVYTMGAIPIVCKDIALGLGGTVSLLFDTAFGTLGGLFQVVFSVCKRIGYKVTFDNSGEL
Protein: Thioredoxin reductase 2, mitochondrial (EC 1.8.1.9) (Selenoprotein Z) (SelZ) (TR-beta) (Thioredoxin reductase TR3) (Q9NNW7)
Organism: Homo sapiens (Human)
Function: Involved in the control of reactive oxygen species levels and the regulation of mitochondrial redox homeostasis. Maintains thioredoxin in a reduced state. May play a role in redox-regulated cell signaling.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10215850}.
Interaction partners:
- Thioredoxin, mitochondrial
- Selenide, water dikinase 2
- Thyroid hormone receptor beta
- Selenocysteine lyase
- Thioredoxin reductase 1, cytoplasmic
- Selenide, water dikinase 1
- Cystathionine gamma-lyase
- Kynurenine--oxoglutarate transaminase 3
- Kynurenine--oxoglutarate transaminase 1
- Thioredoxin reductase 3
Sequence:
MAAMAVALRGLGGRFRWRTQAVAGGVRGAARGAAAGQRDYDLLVVGGGSGGLACAKEAAQLGRKVAVVDYVEPSPQGTRWGLGGTCVNVGCIPKKLMHQAALLGGLIQDAPNYGWEVAQPVPHDWRKMAEAVQNHVKSLNWGHRVQLQDRKVKYFNIKASFVDEHTVCGVAKGGKEILLSADHIIIATGGRPRYPTHIEGALEYGITSDDIFWLKESPGKTLVVGASYVALECAGFLTGIGLDTTIMMRSIPLRGFDQQMSSMVIEHMASHGTRFLRGCAPSRVRRLPDGQLQVTWEDSTTGKEDTGTFDTVLWAIGRVPDTRSLNLEKAGVDTSPDTQKILVDSREATSVPHIYAIGDVVEGRPELTPIAIMAGRLLVQRLFGGSSDLMDYDNVPTTVFTPLEYGCVGLSEEEAVARHGQEHVEVYHAHYKPLEFTVAGRDASQCYVKMVCLREPPQLVLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKLRISKRSGLDPTVTGCUG
Protein: PrfA (Positive regulatory factor A) (Listeriolysin regulatory protein) (Transcriptional regulator) (Q4TVQ0)
Organism: Listeria monocytogenes
Interaction partners:
Sequence:
MNAQAEEFKKYLETNGIKPKQFHKKELIFNQWDPQEYCIFLYDGITKLTSISENGTIMNLQYYKGAFVIMSGFIDTETSVGYYNLEVISEQATAYVIKINELKELLSKNLTHFFYVFQTLQKQVSYSLAKFNDFSINGKLGSICGQLLILTYVYGKETPDGIKITLDNLTMQELGYSSGIAHSSAVSRIISKLKQEKVIVYKNSCFYVQNLDYLKRYAPKLDEWFYLACPATWGKLN
Protein: Enoyl-[acyl-carrier-protein] reductase, mitochondrial (EC 1.3.1.104) (2-enoyl thioester reductase) (Mitochondrial respiratory function protein 1) (P38071)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (fatty acid synthesis type II). Fatty acid chain elongation in mitochondria uses acyl carrier protein (ACP) as an acyl group carrier, but the enzyme accepts both ACP and CoA thioesters as substrates in vitro. Required for respiration and the maintenance of the mitochondrial compartment.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:11509667, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Hydroxyacyl-thioester dehydratase type 2, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase homolog
- Uncharacterized peptide chain release factor-like protein YLR281C
- Acyl-coenzyme A oxidase
- Fatty acid synthase subunit beta dehydratase; Enoyl-[acyl-carrier-protein] reductase; [Acyl-carrier-protein] acetyltransferase; [Acyl-carrier-protein] malonyltransferase; S-acyl fatty acid synthase thioesterase]
- Fatty acid synthase subunit alpha reductase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Octanoyltransferase, mitochondrial
- Acetyl-CoA carboxylase, mitochondrial
Sequence:
MLPTFKRYMSSSAHQIPKHFKSLIYSTHEVEDCTKVLSVKNYTPKQDLSQSIVLKTLAFPINPSDINQLQGVYPSRPEKTYDYSTDEPAAIAGNEGVFEVVSLPSGSSKGDLKLGDRVIPLQANQGTWSNYRVFSSSSDLIKVNDLDLFSAATVSVNGCTGFQLVSDYIDWNSNGNEWIIQNAGTSSVSKIVTQVAKAKGIKTLSVIRDRDNFDEVAKVLEDKYGATKVISESQNNDKTFAKEVLSKILGENARVRLALNSVGGKSSASIARKLENNALMLTYGGMSKQPVTLPTSLHIFKGLTSKGYWVTEKNKKNPQSKIDTISDFIKMYNYGHIISPRDEIETLTWNTNTTTDEQLLELVKKGITGKGKKKMVVLEW
Protein: Ethylene-responsive transcription factor ERF109 (Q9SZ06)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Probable WRKY transcription factor 40
- Transcription factor MYC2
- Putative cyclin-D6-1
Sequence:
MHYPNNRTEFVGAPAPTRYQKEQLSPEQELSVIVSALQHVISGENETAPCQGFSSDSTVISAGMPRLDSDTCQVCRIEGCLGCNYFFAPNQRIEKNHQQEEEITSSSNRRRESSPVAKKAEGGGKIRKRKNKKNGYRGVRQRPWGKFAAEIRDPKRATRVWLGTFETAEDAARAYDRAAIGFRGPRAKLNFPFVDYTSSVSSPVAADDIGAKASASASVSATDSVEAEQWNGGGGDCNMEEWMNMMMMMDFGNGDSSDSGNTIADMFQ
Protein: Acyl carrier protein (Q7KWJ1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Nodulation protein E
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- Malonyl CoA-acyl carrier protein transacylase
- Cytochrome b-c1 complex subunit Rieske, putative
- Uncharacterized protein
- Acyl-CoA synthetase
- Cytochrome c1, putative
- Cytochrome b-c1 complex subunit 7, putative
- Large ribosomal subunit protein bL21m
- Ribosomal protein L21, apicoplast, putative
Sequence:
MKILLLCIIFLYYVNAFKNTQKDGVSLQILKKKRSNQVNFLNRKNDYNLIKNKNPSSSLKSTFDDIKKIISKQLSVEEDKIQMNSNFTKDLGADSLDLVELIMALEEKFNVTISDQDALKINTVQDAIDYIEKNNKQ
Protein: 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI12 (HMP-P synthase) (Hydroxymethylpyrimidine phosphate synthase) (EC 2.-.-.-) (Thiamine biosynthesis protein 12) (Thiamine pyrimidine synthase) (P42883)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
Interaction partners:
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20
- Thiamine thiazole synthase
- Putative pyridoxal kinase BUD16
- Pyridoxamine 5'-phosphate oxidase
- Thiamine biosynthetic bifunctional enzyme
- Probable pyridoxal 5'-phosphate synthase subunit SNZ2
- Probable pyridoxal 5'-phosphate synthase subunit SNO3
- Uncharacterized protein YGR017W
- Putative pyridoxal kinase BUD17
Sequence:
MSTDKITFLLNWQPTPYHIPIFLAQTKGYFKEQGLDMAILEPTNPSDVTELIGSGKVDMGLKAMIHTLAAKARGFPVTSVASLLDEPFTGVLYLKGSGITEDFQSLKGKKIGYVGEFGKIQIDELTKHYGMKPEDYTAVRCGMNVAKYIIEGKIDAGIGIECMQQVELEEYLAKQGRPASDAKMLRIDKLACLGCCCFCTVLYICNDEFLKKNPEKVRKFLKAIKKATDYVLADPVKAWKEYIDFKPRLNNDLSYKQYQRCYAYFSSSLYNVHRDWKKVTGYGKRLAILPPDYVSNYTNEYLSWPEPEEVSDPLEAQRLMAIHQEKCRQEGTFKRLALPA
Protein: At4g01700 (Chitinase family protein) (Putative chitinase) (T15B16.5 protein) (Q9ZSI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- RING-type E3 ubiquitin transferase
- Regulator of Vps4 activity in the MVB pathway protein
- At1g25420/F2J7_16
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- Regulator of Vps4 activity in the MVB pathway protein
- At2g05540/T20G20.11
Sequence:
MEKQISLLLCLLLFIFSISSSLHETEARKHNKYKPAPIMSLVPRTLYDQIFIHKDNNACPAKGFYPYEAFVEATRSFPKFGSVGNFWTRRREVAAFLAQISHETTGGWATAPDGPYAWGLCFKEEVSPQSNYCDASNKDWPCVSGKSYKGRGPIQLSWNYNYGQAGRALGFDGLQNPELVANNSVLAFKTALWFWMTEQTPKPSCHNVMVNRYRPTKADRAANRTVGYGLVTNIINGGLECGIPGDGRVTDRVGYFQRYAQLFKVTTGPNLDCENQRPFS
Protein: Monoacylglycerol lipase (MAG lipase) (EC 3.1.1.23) (Q03649)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Converts monoacylglycerides (MAG) to free fatty acids and glycerol. Has a preference for palmitoyl-MAG. Does not play a significant role in ethyl ester biosynthesis. Also possesses ester hydrolase and low but persistent TAG lipase activity.
Interaction partners:
- Monoglyceride lipase
- Alcohol O-acetyltransferase 1
Sequence:
MRLKELLPNFLIVHQEVPEDPIAFKSTDKRENENKEITIPELIDTKVPELADGATDTLYGLLVNGHLQTAYGSFRHFDNIYKVQYKRMIIKYPHGGEGTVDFAVNGRSTKRRKVEKEYVPTSQPVFNGNLKRRYSYYSPDDPKLNSDDAKPMLIILHGLTGGSRESYVRAIVHEITTKYDFEACVFNARGCCYSAITTPLLYNGGWTNDIRYCVNDLRKRFPNRKFYMMGFSLGASIMTNYLGEESDRTKIECAISVSNPFDLYNSAYFINSTPMGSRFYSPALGHNLLRMVRNHLSTLEENPDFKDVIEKHLKKIRTVRQFDNLLTGPMFGYKNAEEYYKNASSYKRIPGIRTPFIALHAQDDPIVGGDLPIDQIKSNPYTLLLETSTGGHVGWFKDRSGRRWYAEPLCRFLKIFHDEITVKGLKPDLENVQLPDPNCEPIATTFRAN
Protein: Casein kinase II subunit alpha' (CK II) (EC 2.7.11.1) (P19454)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity). Phosphorylates YTA7 during S-phase to promote transcription of histones.
Interaction partners:
- Casein kinase II subunit alpha
- Nucleolar protein 19
- Casein kinase II subunit beta'
- Casein kinase II subunit beta
- U3 small nucleolar RNA-associated protein 11
- Probable ATP-dependent RNA helicase DHR2
- Ribosomal RNA-processing protein 7
- U3 small nucleolar RNA-associated protein 22
- FACT complex subunit SPT16
- FACT complex subunit POB3
Sequence:
MPLPPSTLNQKSNRVYSVARVYKNACEERPQEYWDYEQGVTIDWGKISNYEIINKIGRGKYSEVFSGRCIVNNQKCVIKVLKPVKMKKIYRELKILTNLTGGPNVVGLYDIVQDADSKIPALIFEEIKNVDFRTLYPTFKLPDIQYYFTQLLIALDYCHSMGIMHRDVKPQNVMIDPTERKLRLIDWGLAEFYHPGVDYNVRVASRYHKGPELLVNLNQYDYSLDLWSVGCMLAAIVFKKEPFFKGSSNPDQLVKIATVLGTKELLGYLGKYGLHLPSEYDNIMRDFTKKSWTHFITSETKLAVPEVVDLIDNLLRYDHQERLTAKEAMDHKFFKTKFE
Protein: SD01848p (Q8MQY1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EFLLWTLKRRLSSLNNKSYSIWKAIEWIAMFRTRVHRNLSWISTNSSRTTTTHGQHYQYLQCSKLPTLYFQRSLPRLPIPLLENSCRRFLEATKPLLSPAEQAETQQTVEQFRQGIGMELHAKLKSHDAQNKHTSYISQPWFDMYLADRAPLPLNYNPLLVMKSDTRPEYQQQVVRATNLIISSLRFWRSLQADLLEPEVYHMNAKKSDTSSYRRWMKVAPKAFATYASYAFKAFPLDMSQYNRLFGTSRIPRIGKDELVQSPDAKHILVMRRGHMYAVNVLDSSGYIESPSVILGRLRAVLKLDADREAASVPLGVLTSGQRDEWAKTRQHFVSNNKNADLLEREVDAALFCVCLDGEEDGVFNENQQEPLLKHLLAGKAQNRWFDKSISLLISADGTTAINFEHSWGDGVAVLRYFNELYKDTLKQPFVSTETVHTPAEGDFSNVRPINFEIDDATKSAVSEAYNKNASIVDNLDMNVLKYPHINKPTCKQYGLSPDSIIQLSFQLAYRQAYSGYVGSYESCSTSAFRHGRTETMRPCTNATRDFCEAILQPERSKPSAGELRAMIDNCSKVHGQLTKEAAMGQGFDRHLFALRHTAQKEGIPIPDLYETEAYKRINNNIISTSTLGSDALLAGSFGPVVKNGFGIGYSIQNDFAGAIVTTYKNQADGKVFIDSLESAFDKICAVIQQSSSSKK
Protein: 4-hydroxymandelate synthase (HMS) (HmaS) (EC 1.13.11.46) (4-hydroxyphenylpyruvate dioxygenase II) (O52791)
Organism: Amycolatopsis orientalis (Nocardia orientalis)
Function: Required to synthesize hydroxyphenylglycine, a recurring skeletal component of nonproteinogenic macrocyclic peptide antibiotics such as vancomycin. Catalyzes the conversion of p-hydroxyphenylpyruvate to p-hydroxymandelate. The decarboxylation and hydroxylation activities of HmaS show novel and distinct regioselectivity, compared to all other known p-hydroxyphenylpyruvate dioxygenases, by hydroxylating the benzylic position of the substrate instead of the phenyl ring.
Interaction partners:
- 4-hydroxymandelate oxidase
- (S)-3,5-dihydroxyphenylglycine transaminase (p-hydroxyphenylglycine transaminase)
- Homogentisate 1,2-dioxygenase
- 4-hydroxyphenylpyruvate dioxygenase
- Aminotransferase
- fumarylacetoacetase
Sequence:
MQNFEIDYVEMYVENLEVAAFSWVDKYAFAVAGTSRSADHRSIALRQGQVTLVLTEPTSDRHPAAAYLQTHGDGVADIAMATSDVAAAYEAAVRAGAEAVRAPGQHSEAAVTTATIGGFGDVVHTLIQRDGTSAELPPGFTGSMDVTNHGKGDVDLLGIDHFAICLNAGDLGPTVEYYERALGFRQIFDEHIVVGAQAMNSTVVQSASGAVTLTLIEPDRNADPGQIDEFLKDHQGAGVQHIAFNSNDAVRAVKALSERGVEFLKTPGAYYDLLGERITLQTHSLDDLRATNVLADEDHGGQLFQIFTASTHPRHTIFFEVIERQGAGTFGSSNIKALYEAVELERTGQSEFGAARR
Protein: Protein Daple (Coiled-coil domain-containing protein 88C) (Dvl-associating protein with a high frequency of leucine residues) (Q6VGS5)
Organism: Mus musculus (Mouse)
Function: Required for activation of guanine nucleotide-binding proteins (G-proteins) during non-canonical Wnt signaling. Binds to ligand-activated Wnt receptor FZD7, displacing DVL1 from the FZD7 receptor and leading to inhibition of canonical Wnt signaling. Acts as a non-receptor guanine nucleotide exchange factor by also binding to guanine nucleotide-binding protein G(i) alpha (Gi-alpha) subunits, leading to their activation. Binding to Gi-alpha subunits displaces the beta and gamma subunits from the heterotrimeric G-protein complex, triggering non-canonical Wnt responses such as activation of RAC1 and PI3K-AKT signaling. Promotes apical constriction of cells via ARHGEF18.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9P219}. Cell junction {ECO:0000269|PubMed:30948426}. Note=Enriched at apical cell junctions. {ECO:0000269|PubMed:30948426}.
Interaction partners:
- Segment polarity protein dishevelled homolog DVL-1
Sequence:
MDVTVSQLVELFLQSPLVTWVKTFGSFGSGHQDNLTLYMDLVDGIFLNQIMLQIDPRPSNQRINKHVNNDVNLRIQNLSILVRNIKTYYQEVLQQLIVMNLPNVLMIGKDPLSGKSMEEIKKVLLLVLGCAVQCERKEEFIERIKQLDIETQAGIVAHIQEVTHNQENVFDLQWLDLPDVAPEELEALSRNMVFHLRRLIDERDECTELIVDLTQERDYLQTQQPPSPGKFSSPDSTPSPTSSLSSEDKQHLAVELADTKARLRRVRQELEEKTEQLADTRHEVDQLVLELQKAKQDNIQLAADARSARAYRDELDSLREKANRVERLEMDLVRCKEKLHDVDFYKARMEELREDNIILIETKAMLEEQLTASRARSDKVHELEKENLQLKSKLHDLELDRDADKKQIEKLLEEYMVLEMAQKQSMKESAHLGWELEQLSKNADLSDASRKSFVFELNECASSRILKLEKENQSLQSTIQGLRDTSLALEESSLKYGELEKENQQLSKKIEKLQTQLEREKQSNQDLETLSEELIREKEQLQSGMEALKADRARQIKDLEQEKGHLHQAVWSLRERPQVNSTKDVEKENRALHQAVTEAGSKLSQLELEKQQLHRDLEEAKEKGEQAEALEKELHRLEKENEQLTKEVTSLKAATEKVEALEHQSQGLELENRSLRKSLDTLQNVSVQLEGLERDKQQLGQENLELRKMVEAMRFTSAKMAQIETENRQLEREKEELRRDVELLKTLSKKSERLELSYQSVSAENLQLQHSLESSTHKSQALQRELSQLEAERQALRRDLETLQLTHKQLEGAEEDRKALEQEVAQLEKDKKLLEKEARRLWQQVELKDAILDDSAAKLSAAEKESRALDKELARCRDVGSKLKELEKDNRDLTKQVTMHTRTLTTLREDLVLEKLKSQQLSSELDKLSQELEKVGLSKDLLLQEDDGHGDGKGKTESALKTTLAMKEEKIVFLEAQVEEKESLSRQLQIELQMIKKEHEQLRQTQEGGDKAQNALKRPPGKVTSHQEKEAWEPSHKEATMELLRVKDRAIELERSNAALQAERQLLKEQLQHLETQNVSFSSQILTLQKQSAFLQEHTTTLQTQTAKLQVENSTLSSQNAALSAQYTVLQSQQAAKEAEHEGLQQQQEQLAAVYEALLQDHKHLGTLYECQSSEYEALIRQHSCLKTLHRNLELEHKELGERHGDLQQRKAELEELEKVLSTEREALEREQKTNAIATSENQRLRGELDRISFLHQQLKGEYEELHAHTKELKTSLNNSQLELSRWQVRFDELKEQHQSMDISLTKMDNHCELLSRLKGNLEEENHHLLSQIQLLSQQNQMLLEQNMESKEQYHEEQKQYIDKLNALRRHKEKLEEKIMDQYKFYDPAPKKKNHWIGAKALVKLIKPKKEGSRERLKSTTDSPPWQLEPSDPASPSPSQALRSQTENPDNPPSGPNCVEERDTHNGPVGKGPGDLKPKRGSPRGGSVDRTDTSTDPAVKSWPSEPGSRTFSTSATTAALSSSTPIPKHLGRTKGCNSDDNLCEPSSEPDGPYHRQQASRPNSLESSRNASSNSSPLSLKGSSDHLHSRCESFSSADLIPSRDPATLSRDGNTSGRGLLGRHEYPPPRNGPVSQETIQKKGAASTHTGVRPHSASPSSEMVTLEEFLEESNRGGSPTHDTPSCRDDLLSDYFRKAHDPPALGGQPGPPARKDGAKMPTSFVAPTIKMSINTSEGQQLKPGHYVKPNLRPSEAEALAGMPSRQVQPPQSLSLGRPRQTTMTQNCHMPVSRSASLSRAFSLASADLLRASGPEACRPESPQKPGGHEAAGARETSTHSLQGSHILARERTPIVGKADSPSPGQGTRGRPLDTRRFSLAPPKEERLAPLQQSATAPALATGCSSGSNPQIQHFSPTVAPAVRTKSKVPQHSGEVATVAPVRPGLGTSEGDGGPGHGYSEGLLTKSPGRSSDLPPHVKRGPDDFSQGSSSKSTPASPEPGGDPQTVWYEYGCV
Protein: GDP-fucose protein O-fucosyltransferase 2 (EC 2.4.1.221) (Patterning defective protein 2) (Peptide-O-fucosyltransferase 2) (O-FucT-2) (Q8WR51)
Organism: Caenorhabditis elegans
Function: Catalyzes the reaction that attaches fucose through an O-glycosidic linkage to a conserved serine or threonine residue in the consensus sequence C1-X-X-S/T-C2 of thrombospondin type I repeats (TSRs) where C1 and C2 are the first and second cysteines of the repeat, respectively. O-fucosylates members of several protein families including the ADAMTS superfamily and the thrombospondin (TSP) and spondin families (By similarity).
Subcellular location: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9Y2G5}. Golgi apparatus {ECO:0000269|PubMed:15233996}. Note=Mainly located in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q9Y2G5}.
Interaction partners:
- GDP-fucose protein O-fucosyltransferase 1
- N-acetylgalactosaminide beta-1,3-galactosyltransferase
- N-acetylgalactosaminide beta-1,3-galactosyltransferase
- N-acetylgalactosaminide beta-1,3-galactosyltransferase
- N-acetylgalactosaminide beta-1,3-galactosyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1.
- N-acetylgalactosaminide beta-1,3-galactosyltransferase
- N-acetylgalactosaminide beta-1,3-galactosyltransferase
- Putative alpha-L-fucosidase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
Sequence:
MHFFPIQLLVLFFAEKIAFAENSDQTVSRVDSNRYSVAAEKKFLLYDVNFGEGFNLRRDVYMRVANTVRSLRDSGENYILVLPPWGRLHHWKRMEVALSWRLFFDLESLNRFIPVIEFEDFLDENRPIDQVIYLQHYAEGWGTEYVRKFEKRSCLPPAESHYKQVEEFKWKGWFYSYEDVYSRNFQCVSIQGDSGTLKDLLKHSNFSESTSIMVDRAETILHEHYGEVDYWKARRSMRYSNDLVDVADAFRKKYLDSDDKRDKTKLVDDWTKEKPRRTAIGGPYLGIHWRRRDFLYARRAQLPTIPGTAKILQDLCKKLDLQKIYLATDAPDQEVDELKALLNGELEVYRFTDTQKLNDGQIAIIDQYLCAHAAYFIGSYESTFTFRIQEDREIIGFPISTTFNRLCPDTEPTCEQPAKWKIVY
Protein: RhoGAP1A (Q6W456)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EEENTIFFKIDELYDLHTGFLSDLKTIVSHEGGDVLIGEPFRRLAEMFDLYSAFLHNYKNAIETVKKCSANNPQFKKIVSTIVLNLQTEQSLTLEDLLHKPVARVQINALVFNDLLRETPNAHPDHQPLRQAQKIIQMFLNQFNVVNQRLPIESNRNLRRMVRNSFIVELVDGHRKLRHLFLFNDVIACAKYKALGRDRIDYELKWFIPLKDVSIYEEADPAVELKESSPANISQVKRNLRSVRDQLAMEVANSGSGGFRSGDKYRRKLADLESQLVLATPNLVLRLGNKANNKTITFFLSSDFERTQWIDSILSLK
Protein: diguanylate cyclase (EC 2.7.7.65) (Q9HUW7)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Cyclic di-GMP phosphodiesterase PA2567
- Sel1 repeat family protein
- Probable transcriptional regulator
- Probable two-component response regulator
- EAL domain-containing protein
- histidine kinase
- Uncharacterized protein
- Pilus assembly protein PilZ
- EAL domain-containing protein
- cyclic-guanylate-specific phosphodiesterase
Sequence:
MMTEHDDPTLDRLKHHFAQRVINQARQVLEVWQRLTRAEWNSDGMEELADATLRLQRYAERFEQAEHAQLAGAIDRTLDVVEANRGRLSSESISELNQLMQRLSRTGLRHGDQLEHTVLPPLRKPVYLALKDRERAERLAQQLEFFGLQALSCETADAFRASMRERYPAAIVMEVDFAGPDMGLRLASEAQAGLEHKLPVLFFSDSETDTPTRLAAARAGGQEFFTGTLDASSVLEKIETLSRLSFYEPYRVLIVDDSRAQALHTEMVLNSAGIITRALTEPLSVMAELSDFQPDLIILDMYMPECLGTELAKVIRQHERHVSVPIIYLSAEDDLDKQLDAMSEGGDDFLTKPIRPRHLIATVRTRASRARSLKARMVRDSLTGLYNHTHTLQLLEDARLRARRDGRPLSFAMLDIDHFKQVNDRFGHPMGDRVIKGLALFLKQRLRKTDHIGRYGGEEFAVVLPDTDLDAARLVLDEIRQRFAEIHYPAQPTDLRCTFSCGIAELTPDLDIKSMAKQADEALYRAKHGGRNRIEVYRPDAR
Protein: TFIIH basal transcription factor subunit (Q381H9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- TFIIH basal transcription factor subunit
- TFIIH basal transcription factor subunit
- TFIIH basal transcription factor subunit
- TFIIH basal transcription factor subunit
Sequence:
MPSYIFILHSSGVSCDSALLSQAAHCASALFSSVRGCSSDFVPTVAVIRANPVEGVRYAYTSTVSDNRYDSFVEDAVMQYSGNVNEADGSDRASPRFSGRSVVNLQRAILQCGDIRVSDKQDAEPVGVWRCLAGAILAACCFLRSYSTCPSESFDECGAEVCDAFVPAGVAMIIFSGVCDTRPLSFSEECPFSAAVTAATRLRTAVHVFGPAVVSSALGLRLQALANTTGGIWAPQFALSHVGYLMELAVRRNGQREMDSATNSRRQRELLVERYVVPPACLPQDPAQTGVASGENVSYLAWLCSACLATLVRHPHEEVGAIRMCPYCAASK
Protein: Elastin-like, isoform B (Q8IMV1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLSRRVIAFAALALIQIASGQASQFSRDESQEDQKTEFNLASTLTGGITSSRHRQRANLNSQLYPGLGQLGSGYAGATGSIDDAHGHEQGGSGVRVARGHQIPAYPPPGFPGQQAPVPYPAAGGSSGGSSSSGGYQSAGAVSPPGYPVAGAVPAQYPVGVPPQQPVGAGAPGYFPGTGAYPGYPYPGVYLPQYPAYPQPAQFPAYGVLPGAVAQPGVPGVAGVPGAPGVAGVPGAAGQAPATSGMNYHRYPAHNPADPSHWDHHFSMNTEYKEDGVHKGPFGVLNNHNAFGYGSGYGGGYNGAFNSPAY