wanglab/gogpt-training-data huggingface dataset:
Protein: Nervy, isoform D (A0A0B4KEZ2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MMALDGKAIIKEEITDKDAYDAAAAAAAAVAAGAALAVASAAAVQVPPASSSSAGSASSAAAAATNNTTSAAATAAAISRRLKASSSGGDKSSTSSSSSKDSSHTSSSRSERDRERERERERERDRLCRTPPDSPPDSSRSLAPRSPHSPLQLHQHPQRNASVSPVVNGSSSGGGGVGSSGTSPTPTPGSQHAASLAAAAAAAAAAHVEQARLVSKMRKFLGALVQFSQELGQPEVCERVRALVLSLCSGSISVEEFRLALQEAINLPLRPYVVPLLKNSIALVQREILALARATNQSALQYVTNNEQAVMEFAPHGVASAEFGDIFIQLEAPTSNGSSAVFKRRSSDSMMEHGGHNGLQEWNEYMASGGAGYPPPPSKRLTLHPAHSVVAYGEYGVSSAEGLPSAAAFMQRDERDLRMSEAQARHAAPPQRAGNPQPNPNAAAPGAPGAGGEEEWKNIHTMLNCISAMVDKTKRAITILQQRGIEPQHPNSGQEVTPAAMAELRRQTEEKVAEFKRNAEDAVTQVKRQAVIEIQRAVVAAETRAAEIMTQERLRMEKFFMEMSRHSSGERDLDNKSPSMASAQNGSNLQQQCWNCGRKATETCSGCNMARYCSASCQYRDWDSHHQVCGNTRASELSAKHLHSASNLSLRNAMATRSPPTPNSAAHLQAAAAAAAAAAGAREAVSAPVGGPGAGIAVGTGAGSGGQSGGGGGGGGGGGGGAAAAAVAAATPGALVANGLGSKXRIRMMKPKKKYLC
Protein: PRA1 family protein (H2KZJ7)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363107}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU363107}.
Interaction partners:
Sequence:
MTTSSENMQIMNGVEVPPFRNFHEFLLETDRYERPPFNDFKKWNNRIISNLLYFQTNYFVTIITLFLLHTFISSQDIFVGLIAVVAVIATLIFAVSADANIKKMRTDHPLVTLGGIILVAYFFISVFQSVLVVAFALLFPVFLVLVHASLRLRGIANRAANVKEQLGIRTSVMGQILDRTGLNVKV
Protein: No mechanoreceptor potential B, isoform D (Q7KRS6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Outer segment 5
- Intraflagellar transport 52
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 57 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport 20
- Clusterin associated protein 1
- Tetratricopeptide repeat protein 30 homolog
- Intraflagellar transport protein 122 homolog
- Intraflagellar transport protein 172 homolog
Sequence:
MTSQITANGTQRLPEPVSEHEAVPPPPPTAAGRPRPPTSQLFSRGNLASSRATGGDKSGLARPSTAVRAVGYAANCESAHQRFEQFFLEKAKQQTLSSRAAVDAIKDVNPQMKYKNLEEKIVKLLESSIVLAWQGSPNKLLNLDTKLAEALSKAKEAFSLDRTLHQFRDQHGENVYHNFDLTYAQYERSEMHIEALNTYSIMAKNKMFPHVNQLKLNMGNIYYSMGIYQKAVKMYRMALDSVPKSLSQLRLKIRENIGILFIRMGSYSDAASSFEFIMTERANIRSSIHLLLCYFALGDVEKVKLAFRRLCDVQTEAIESDMESETNIIKLQQQAEPIQQIGETDGYQSLNNEPVTGSVIKAEGGGKLNETVKFAATVKHRYVVQALKKDELAVYRNERRNAVKRSITMIVDLISPFIEDNYNDGYNWCIEIIKTSNLAWLANELELNKALVYLRQNDVHQAIETLQMYDRKSEGSMTASALTNLSFIYIKMASHCVNQLHEIGSLKNNAPGLINAGIVELGSHNLILASERFEGALQLQPMNFEARYNLGLVALAQNDYELAEERFELLKEQLMLPSSVQHSHVFYQLAKLQERRLESGLISNFTPGAALQAYLQVVGISASDIDSRLFEKVGSLYEQIQDHQEANQYYNEAYRINMSDIGIASSIGSYYIKLQATERALFYYERAVLADPNDPNLMLRIASCFRNSYLPTKQYLGLFQKIHARFPDNLTCIRALMQVTKSLELGDLYERYASEYTRLQSQQQERQSEQRYQQQRFPSAAKFSNRLRSIRQSNEEHLKEVGENFNSVVHTQSPYTSILQFDPLGPPAERPKTGRPLQSRDDVDDDAEMNPESLLPI
Protein: Glycine dehydrogenase (decarboxylating), mitochondrial (EC 1.4.4.2) (Glycine cleavage system P protein) (Glycine decarboxylase) (Glycine decarboxylase complex subunit P) (Glycine dehydrogenase (aminomethyl-transferring)) (P49095)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The glycine cleavage system (glycine decarboxylase complex) catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein.
Subcellular location: Mitochondrion {ECO:0000250}.
Interaction partners:
- Glycine cleavage system H protein, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Aminomethyltransferase, mitochondrial
- Dihydrolipoyl dehydrogenase, mitochondrial
- Serine hydroxymethyltransferase, mitochondrial
- Low specificity L-threonine aldolase
- Alanine--glyoxylate aminotransferase 1
- Methylenetetrahydrofolate dehydrogenase [NAD
- DASH complex subunit DAD4
- Glutamate synthase
Sequence:
MLRTRVTALLCRATVRSSTNYVSLARTRSFHSQSILLKTAATDITSTQYSRIFNPDLKNIDRPLDTFARRHLGPSPSDVKKMLKTMGYSDLNAFIEELVPPNILKRRPLKLEAPSKGFCEQEMLQHLEKIANKNHYKVKNFIGKGYYGTILPPVIQRNLLESPEWYTSYTPYQPEISQGRLEALLNFQTVVSDLTGLPVANASLLDEGTAAGEAMLLSFNISRKKKLKYVIDKKLHQQTKSVLHTRAKPFNIEIIEVDCSDIKKAVDVLKNPDVSGCLVQYPATDGSILPPDSMKQLSDALHSHKSLLSVASDLMALTLLKPPAHYGADIVLGSSQRFGVPMGYGGPHAAFFAVIDKLNRKIPGRIVGISKDRLGKTALRLALQTREQHIKRDKATSNICTAQALLANVASSYCVYHGPKGLQNISRRIFSLTSILANAIENDSCPHELINKTWFDTLTIKLGNGISSEQLLDKALKEFNINLFAVDTTTISLALDETTTKADVENLLKVFDIENSSQFLSEDYSNSFPREFQRTDEILRNEVFHMHHSETAMLRYLHRLQSRDLSLANSMIPLGSCTMKLNSTVEMMPITWPQFSNIHPFQPSNQVQGYKELITSLEKDLCSITGFDGISLQPNSGAQGEYTGLRVIRSYLESKGENHRNVCLIPVSAHGTNPASAAMAGLKVVPVNCLQDGSLDLVDLKNKAEQHSKELAAVMITYPSTYGLFEPGIQHAIDIVHSFGGQVYLDGANMNAQVGLTSPGDLGADVCHLNLHKTFSIPHGGGGPAGAPICVKSHLIPHLPKHDVVDMITGIGGSKSIDSVSSAPYGNALVLPISYAYIKMMGNEGLPFSSVIAMLNSNYMMTRLKDHYKILFVNEMSTLKHCAHEFIVDLREYKAKGVEAIDVAKRLQDYGFHAPTLAFPVPGTLMIEPTESENLEELDRFCDAMISIKEEINALVAGQPKGQILKNAPHSLEDLITSSNWDTRGYTREEAAYPLPFLRYNKFWPTVARLDDTYGDMNLICTCPSVEEIANETE
Protein: Actin related protein 2/3 complex, subunit 3 (A0A8I6AL89)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MPAYHSSLMDPDTKLIGNMALLPIRSQFKGPAPRETKDTDIVDEAIYYFKANVFFKNYEIKNEADRTLIYITLYISECLKKLQKCNSRSQGEKEMYTLGITNFPIPGEPGFPLNAIYAKPASKQEDGENRTVSVQECVCARACTCVAILSLCLTLGIGVCFFWSFLRHDISLSLSLSSPDWS
Protein: Cytochrome P450 2B9 (EC 1.14.14.1) (CYPIIB9) (Cytochrome P450 clone PF26) (Cytochrome P450-16-alpha) (Testosterone 16-alpha hydroxylase) (P12790)
Organism: Mus musculus (Mouse)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450 7A1
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
- Cytochrome P450
- UDP-glucuronosyltransferase
- Cytochrome P450 3A
- Cytochrome P450 4A14
- Cytochrome P450 2C38
- Cytochrome P450 4A10
Sequence:
MDPSVLLLLAVLLSLFLLLVRGHAKIHGHLPPGPHPLPLLGNLLQMDRGGLLKCFIQLQEKHGDVFTVHLGPRPVVVLCGTQTIREALVDHAEAFSGRGTIAAAQLVMQDYGIFFASGQRWKTLRRFSLATMKEFGMGKRSVEERIKEEAQCLVEELKKYQGVPLDPTFLFQCITANIICSIVFGERFDYTDDQFLHLLNLMYKIFSLLSSFSGQMFELFSGFLKYFPGVHRQIVKKQQELLDYIAHSVEKHKATLDPSAPRDYIDTYLLRMEKEKSNHNTEFHHQNLMMSVLSLFFAGTETTSATLHYGVLLMLKYPHVTEKVQKEIDQVIGSHRLPTLDDRTKMPYTDAVIHEIQRFSDLVPIGLPHKVIKDTLFRGYLLPKNTEVYPVLSSALHDPQYFEQPDKFNPEHFLDANGALKKCEAFLPFSTGKRICLGESIARNELFIFFTTILQNFSVASPVAPKDIDLTPKESGIGKIPPAHQIYFLAR
Protein: FNIP repeat-containing protein DDB_G0290617 (Q54FS2)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- F-box/WD repeat-containing protein A
Sequence:
MIENKIELNCALHTNKNLEFLCLDCKLIPCCTLCISRGGEHHRHGIDSLESIQTSSILSMMNNFKDVYPKVIERIENDQQILKDSDEIFNEIQSQYNKNKITINEEFKKIHNILSIIQLDIERQLTTDFQENTLINTTITSSINNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNSITDILNISIKYIQQQYNNDDHFKIDSNSIELIKQYQQSLLLLNNNNNDNLNKLKEYNNQTIKFDNQLINDIKNNLKTIYSFENNNNNNNNNNNNNNNNNNYNDNDNNNNYNDNNNNYNSNKAEKLNIEIDENNYKFIKKRNKNYYIYSENNEFPKNKEGIAFGEDCGSLLEFNWNKNLKNVMLLDGFKESLEPGVLPNGIVHLEIGDIKTPLVVGSIPSTVISLTFNDGFNQSLEPGVLLNSILNLRIGDIKTPLVVGSIPSSVFSLALHDGFNQSLEPGIIPQNNKYKDFSSMQGVKYLTLHNIKSELNIGSIPKSVYQLTLRDGFSKTLKPGVIPRSVEIVTLQEITKPLIIGSIPYTVLTVQFLTGFNQLLTPGIIPEGVKVLEFYQVKDLLTPGSIPKSIYSLSFKDGFDQILSPGIITDGVCELYLRGIKQPLVLNSIPNSVTKLDIYNEFNQELTPGIIPNSIKELTLGSLNTQLVEGSIPKTIQKIILYGNIEPSSLDVCKLDKSVLIYKK
Protein: Vasodilator-stimulated phosphoprotein (VASP) (P50552)
Organism: Homo sapiens (Human)
Function: Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.
Subcellular location: Cytoplasm. Cytoplasm, cytoskeleton. Cell junction, focal adhesion. Cell junction, tight junction {ECO:0000250}. Cell projection, lamellipodium membrane. Cell projection, filopodium membrane. Note=Targeted to stress fibers and focal adhesions through interaction with a number of proteins including MRL family members. Localizes to the plasma membrane in protruding lamellipodia and filopodial tips. Stimulation by thrombin or PMA, also translocates VASP to focal adhesions. Localized along the sides of actin filaments throughout the peripheral cytoplasm under basal conditions. In pre-apoptotic cells, colocalizes with MEFV in large specks (pyroptosomes).
Interaction partners:
- Protein enabled homolog
- Zyxin
- Ena/VASP-like protein
- Vinculin
- Profilin-1
- Amyloid beta A4 precursor protein-binding family B member 1-interacting protein
- Ras-associated and pleckstrin homology domains-containing protein 1
- Actin, alpha skeletal muscle
- Profilin-3
- Profilin-4
Sequence:
MSETVICSSRATVMLYDDGNKRWLPAGTGPQAFSRVQIYHNPTANSFRVVGRKMQPDQQVVINCAIVRGVKYNQATPNFHQWRDARQVWGLNFGSKEDAAQFAAGMASALEALEGGGPPPPPALPTWSVPNGPSPEEVEQQKRQQPGPSEHIERRVSNAGGPPAPPAGGPPPPPGPPPPPGPPPPPGLPPSGVPAAAHGAGGGPPPAPPLPAAQGPGGGGAGAPGLAAAIAGAKLRKVSKQEEASGGPTAPKAESGRSGGGGLMEEMNAMLARRRKATQVGEKTPKDESANQEEPEARVPAQSESVRRPWEKNSTTLPRMKSSSSVTTSETQPCTPSSSDYSDLQRVKQELLEEVKKELQKVKEEIIEAFVQELRKRGSP
Protein: (3R)-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.n12) (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (HSD17B8) (3-ketoacyl-[acyl-carrier-protein] reductase alpha subunit) (KAR alpha subunit) (3-oxoacyl-[acyl-carrier-protein] reductase) (Estradiol 17-beta-dehydrogenase 8) (EC 1.1.1.62) (Protein Ke6) (Ke6) (Short chain dehydrogenase/reductase family 30C member 1) (Testosterone 17-beta-dehydrogenase 8) (EC 1.1.1.239) (Q92506)
Organism: Homo sapiens (Human)
Function: Required for the solubility and assembly of the heterotetramer 3-ketoacyl-[acyl carrier protein] (ACP) reductase functional complex (KAR or KAR1) that forms part of the mitochondrial fatty acid synthase (mtFAS). Alpha-subunit of the KAR complex that acts as a scaffold protein required for the stability of carbonyl reductase type-4 (CBR4, beta-subunit of the KAR complex) and for its 3-ketoacyl-ACP reductase activity, thereby participating in mitochondrial fatty acid biosynthesis. Catalyzes the NAD-dependent conversion of (3R)-3-hydroxyacyl-CoA into 3-ketoacyl-CoA (3-oxoacyl-CoA) with no chain length preference; this enzymatic activity is not needed for the KAR function. Prefers (3R)-3-hydroxyacyl-CoA over (3S)-3-hydroxyacyl-CoA and displays enzymatic activity only in the presence of NAD(+). Cooperates with enoyl-CoA hydratase 1 in mitochondria, together they constitute an alternative route to the auxiliary enzyme pathways for the breakdown of Z-PUFA (cis polyunsaturated fatty acid) enoyl-esters (Probable). NAD-dependent 17-beta-hydroxysteroid dehydrogenase with highest activity towards estradiol (17beta-estradiol or E2). Has very low activity towards testosterone and dihydrotestosterone (17beta-hydroxy-5alpha-androstan-3-one). Primarily an oxidative enzyme, it can switch to a reductive mode determined in the appropriate physiologic milieu and catalyze the reduction of estrone (E1) to form biologically active 17beta-estradiol.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:19571038}.
Interaction partners:
- 3-oxoacyl-[acyl-carrier-protein] reductase
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- Very-long-chain 3-oxoacyl-CoA reductase
- 17-beta-hydroxysteroid dehydrogenase type 3
- 17-beta-hydroxysteroid dehydrogenase type 1
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- Fatty acid synthase
- Hydroxyacyl-thioester dehydratase type 2, mitochondrial
- Aldo-keto reductase family 1 member C3
- Zinc transporter SLC39A7
Sequence:
MASQLQNRLRSALALVTGAGSGIGRAVSVRLAGEGATVAACDLDRAAAQETVRLLGGPGSKEGPPRGNHAAFQADVSEARAARCLLEQVQACFSRPPSVVVSCAGITQDEFLLHMSEDDWDKVIAVNLKGTFLVTQAAAQALVSNGCRGSIINISSIVGKVGNVGQTNYAASKAGVIGLTQTAARELGRHGIRCNSVLPGFIATPMTQKVPQKVVDKITEMIPMGHLGDPEDVADVVAFLASEDSGYITGTSVEVTGGLFM
Protein: Transcription elongation factor B polypeptide 3 (Elongin-A) (RNA polymerase II transcription factor SIII subunit A) (dEloA) (Q9VCP0)
Organism: Drosophila melanogaster (Fruit fly)
Function: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex). May play an important role in metamorphosis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00649}.
Interaction partners:
- Elongin-C
- Elongin-B
- Cyclin-dependent kinase 9
- Hyrax
- FACT complex subunit Ssrp1
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- Cyclin-T
- Ell-associated factor Eaf
- RNA polymerase II elongation factor Ell
Sequence:
MASTSNLLDVVRHYQRSIEKHGEDEQRLLHCITKLFNLPIKFEHLQETGIGKTVNALRKISGEVGVAAKTLVTKWKAMVAKEDPSIASTPTAIHNEEDSGKTKSSDEDPDQENKGGNSSSGEDLNTSKHKSKHAKSTKHERSSSSRSHSKSRSDSDKKHKSSRHDKSKDRDKDREGQKEAKEHKEKKSNGEHKSKDSSKSSSSHKSSKSESHKSEHTKSKHEKDKTSHSELKEVKDKSSKHKSSSSKSSKRSHSPPRHEEESQKAKIPKVKSKSEEDSADGFDSSMGANFDDVLGLLNIPISSKKSSSNSKSKFVAKPTAAPSSSALSAPTTAGSSKEALSTSSRPTSKKPELLASTAKLEPLDPNIALELPTISNNYKPMPLNQTVMDVVFNQGGSHKAQASRYFNESEALAQGISSKTMRTKIYSGVRTGQILQVPSLFDLCTRVLQKNIDALEYTGGVPFEVLRPVLERATPQQLLNFEEYNPYLMDDSDVLWQQHVQRHCRSQRREEMETWREMFLRCQEEKDRKLSILAESIKASQKISEAPVRKTQLAFVDSMVKPPRSVQRKQEQYGTKGKLIATPAARVAALSSVTPNAAKVGDARLRVLAAARDTAQVGAGPARSKKAPLMAKTLQFMRGRLKR
Protein: Acyclic carotenoid 1,2-hydratase (EC 4.2.1.131) (1-hydroxyneurosporene hydratase) (Hydroxylycopene hydratase) (Hydroxyneurosporene synthase) (Lycopene hydratase) (Neurosporene hydratase) (P95619)
Organism: Rubrivivax gelatinosus (Rhodocyclus gelatinosus) (Rhodopseudomonas gelatinosa)
Function: Involved in the biosynthesis of carotenoids spheroidene and spirilloxanthin. Catalyzes the hydration of neurosporene to the corresponding hydroxylated carotenoids 1-HO-neurosporene and 1,1'-(HO)2-neurosporene and that of lycopene to 1-HO-lycopene and 1,1'-(HO)2-lycopene. Can also act on demethylspheroidene, spheroidene, 1-HO-3,4-didehydrolycopene and geranylgeraniol.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12745254}.
Interaction partners:
Sequence:
MRAAESGADARVRPVDRVEPADAPAGDAGGLRAAVPGDGGSAVRPGDARLDVLVPPGLVDEPAAGALPGGGQRAPGAGRADGGDVRPVGGRDADGAPRFDQPVPPGGYLWWYVDAVSDDGRHGLTFIAFVGSVFSPYYAWAGGPKADRADPENHCALNIALYGDAGKRWTMTERGRRWMRRSRDEFVIGPSRLHWDGESLLVEFDEVGVPIPRRVKGRVRVWPKALCRFVTSLDSGGRHRWGPIAPCSRIEVELDSPRVRWSGHAYLDSNEGDEPIDRPFREWDWSRATMADSSTAVIYDVRQKRDGDRVIAERFLLDGSTESFEAPPRQPLPTTLWRIGRTMRTEPGVPALVEQTLEDTPFYARSMVRSGLLGEVVTSVHETMLLPRVITLPVRLMLPWRMPRRA
Protein: GPI-anchored protein (Q9LFA8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSSQQYPVRRTAGENLLYSDGEKSDYEWLVTPPGSPSRNVTNHLNAPDDNLMTLISRLENYSKEESEHQTTSLHSSSSVSGIRRPSSSSSSRSTSRPPTPTRKSKTPAKRPSTPTSRATSTTTRATLTSSSTTSSTRSWSRPSSSSGTGTSRVTLTAARATRPTTSTDQQTTGSATSTRSNNRPMSAPNSKPGSRSSTPTRRPSTPNGSSTVLRSKPTKPLSKPALSLEASPIVRSRPWEPYEMPGFSVEAPSNLRTTLPDRPQTASSSRTRAFDASSSSRSASTERDVAKRQSCSPSRSRAPNGNVNGAVPSLRGQRAKTNNDDGRLISHAAKGNQKVEKVVNMRKLATPRLTESGSRRLGGGGGDSSAGKSSSGSGGFGFGRNLSKSSIDMALRHMDVRKGSMAGNFRHSVTKAPATSVYSVRSCRNRPVSSSRSSESSVNILCLDGSDDNLSDMSCS
Protein: ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) (Q7KTC3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Vacuole membrane {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
Interaction partners:
Sequence:
MADDTSSPMDRFCGSTFWNATETWYTNDPDFTPCFEQTALVWTPCAFYWAFVIFDFYYLKASLDRNIPWNKLNVSKALVNLGLLVITALDLIMALVKKGGDSELPLYDLDVWGPIIKFATFLLLFIFIPLNRKYGVQTTGCQFIFWFLLTVLSIPRCRTEVRLDAERQKILNSQQPSEQDFSWEEYQFVSFFIFFTFTSIMLILNCFADGMPRQTKYQRGENEIPELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNKARVEPKAQFSNGNVTFENPHGEKNGRKKGMASIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLIDENNVLDATKTFVSLSLFNILRFPLTMLPMLITNLVQTQVSVNRINKFLNSEELDPNSVLHDSSKPHPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEGNEEEEELNQIKRQISSTADVPELLGTVEKAIKLARTESLSDSISVTSADSLMGGGGSLRRRTKRQDSHDSVASAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYLGVYGAFGFGQVATNFFSSLAISLGCLKCSQLLHQTLLYYNLRWPMELFDTTPLGRIVNRFSKDIDTIDNVLPFNIRVVIGQAYMVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQKTIRTEFKECTVLTIAHRLNTILDSDKVIVLDKGQIIEFASPTELLDNPKSAFYSMAKDANLV
Protein: EG:8D8.1 protein (Female sterile (1) nasrat) (RE10379p) (O76904)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Protein trunk
- Female sterile
- pH-sensitive chloride channel 2
- Protein swallow
- Torso-like protein
- Vitellogenin receptor Yl
Sequence:
MLIWHLLLWPALIASAPPRPLTDQKAEVAKLRSELEKALEHDDGGAPPGVVVAPTWTQQAGQMPLGKTSKVVVDHSSLSSASAIRQEIQQAVAHQGQNQEVLQLEALLKARGSSKESTAQVSTSRQEVLGATVQEANVVESHSTSQTVDLEQLQRLELSKRRTRDMLVLGRIEELLNYSMPTDVDRWLTLQANGSVFLVGQQQEGLLVLSEEFTPLQSYVHPFPITAMLGTDRWNRRVHMQEGLLVMASQDQLIWLRLEPSLGLKPIWHWTIGSHVTKIRAFNMEGQDYLALVANHTLNIYVYDLEAEEFWIAQRVQMAETISNLAILDTGRELLLAVGQWDEVLIYACTSKGQPLHLRQQVAAPEVAGVTAFQMGGRSYLALGGIMPQILVYVQGQLVPRTILGQNFGFVDHYLPIPVRSYRDDLLLLVQHRVVFDTHSLLVLEVLVWNGEAFEAGLPPPCGTAYGAGCMLDQDREAGISGAVLLRRSTNQPPLVVVPRKEAPTGIFVLETQLLARNSETQDLLEIRQFMQDWVHEQEELIQLAEELLAEKSESQYIEELSTPLVVSEGGTVEELFVNEARWTGADAVVDVSSLLQQILLLDGEMSSRRSKRQPETLFNFHYEQLEVEAVDSVELNLEKLNHETFYIRNGSLDLHLGTLNVQQLELLEAPKLELVPVHGAESYKILKMATDLDSIFINEMEWDKLLQDLVWRHQPLKLSQLHVEGPVIFEDVLSLHSLNDLSFPGDYLWSQGNETSVVQAPKEFTQTLSANAVDTTGTINAVYPHDVITLSDSQEWPGLVTFSHLEVSEELELNGSAQGRQFEEAPLNPTLLESRVISADCHFEQLLVRGPLRLLGKVDNDSFGSLLGDLVQRSPNSAQELQISGQKRVDQLLLPVDAHIADNQLSGIFLNDFVTKHTPQTLSNLSQLGGYVYFHQLELGKESSYDGVRLEELLSKSLRLDSPFPLSSPHTRLRFVGHAPNFTRLQVENTLNKVPLSSGYQLLHEPLHLGRANFSRLMAGQAQVNYDVSGNGLLNGRSLIRILQEQPRTWSGEVHVQELILPQGVQANQLQGIKADLLLDFLQQLDELPLLILQGRIQVERIAVNGSVQAAETLNMQPFHELQRQVVWLDRQNELGTRWVLKESPQFQQNLQVLGSFNERLLPELLDDIVLRSDAHEVLIEGTKSFLAPVNTKELHLAALNGIPFNHMANKLSPLHLTGNVRIQGRIFVEDLQLNGQVNGDPDIPADLQKLLRWDPNAGGFVHRGVVELPKKELERLVVLGHLKNRSREPVQELFDQLVFKQQRGIHLHGHKTFTGRLRIEDGAHIKFFNGRNLEQFLENLIYVDSQGEIRLETPVRFAADVKMDHLEADRLVLSGELLNGCNVSQWLRDTIRVDRDFQQPEIAFAKGSLDGNFLEVEELNEVNLSLVVTRFTEQQLSDPLEADDLLLDGQLVVRGTVNGYNLPEEYANTLMINPLREQQVDTPLLLSNIFVTGPLEVTAPVHGLNISDVAILGEDPVLLQSPLYFDTLHAPFLRAQQNINGFDFRAWYGGSLWARGREQQEISGNWRVKKLQVKQGDELRPRRQTAEESYREFCEGLVRILLPYKVQKLRRRFDLNQERDQENIRRVFALEAPGGISYLLINERGCWTRIHRWNGSLFDRSGAFKSGPVDEAVALRVGNTSSNQDFAFMTSYELQDDQNEPSLNCSAVKPILLSWNLNKTKSTTEHMELSADTLRNLKDQYEQLKNQPLPNPSYQQAFKYLQRPSIKSQLGSQWQENKHELSPSEMARMRRRLLDTLEFRLQAEVNITQLSIPESDLFDEHLVEDFLELMRQLRTLRRRLDTETLPLPNTPARVLAARSAQLIWPTLQELREVSSGNDSSFQEQVLEQTLLDVLMLANEENGSGDDEKLHAVIQRLRNLKGELQGQEEDDEGPAASYSDRNEQRLPLPEVDWRPIQTLRLAVGPANRPRLLYARLTVVTPTDGPPPTTPSTAPAAHIQLHHANGSLFQTLAGEHGARHLTSLRVRDETLLAFMEGCCRIRVLIYRGVQGFVDFVRFPAPAQEAKSGDGEVLQLLSLRLPLNRPPGAMYLLAVVQARRVTFYEVVVAGLLEPWLQCP
Protein: RNA helicase (EC 3.6.4.13) (A0A2R8YCW1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLVATPGRLVDMMERGKIGLDFCKYLVLDEADRMLDMGFEPQIRRIVEQDTMPPKGVRHTMMFSATFPKEIQMLARDFLDEYIFLAVGRVGSTSENITQKVVWVEESDKRSFLLDLLNATGKDSLTLVFVETKKGADSLEDFLYHEGYACTSIHGDRSQRDREEALHQFRSGKSPILVATAVAARGLDISNVKHVINFDLPSDIEEYVHRIGRTGRVGNLGLATSFFNERNINITKDLLDLLVEAKQEVPSWLENMAYEHHYKGSSRGRSKSRFSGGFGARDYRQSSGASSSSFSSSRASSSRSGGGGHGSSRGFGGGGYGGFYNSDGYGGNYNSQGVDWWGN
Protein: Keratin, type I cytoskeletal 10 (Cytokeratin-10) (CK-10) (Keratin-10) (K10) (P13645)
Organism: Homo sapiens (Human)
Function: Plays a role in the establishment of the epidermal barrier on plantar skin (By similarity). Involved in the maintenance of cell layer development and keratin filament bundles in suprabasal cells of the epithelium (By similarity).
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:12427098}. Cell surface {ECO:0000269|PubMed:19627498}. Cytoplasm {ECO:0000269|PubMed:32179842}.
Interaction partners:
- Keratin, type II cytoskeletal 1
- Loricrin
- Involucrin
- Filaggrin-2
- Filaggrin
- Keratin, type II cytoskeletal 2 epidermal
- Keratin, type II cytoskeletal 1b
- Keratin, type II cytoskeletal 5
- Keratin, type I cytoskeletal 16
- Serine protease 1
Sequence:
MSVRYSSSKHYSSSRSGGGGGGGGCGGGGGVSSLRISSSKGSLGGGFSSGGFSGGSFSRGSSGGGCFGGSSGGYGGLGGFGGGSFRGSYGSSSFGGSYGGIFGGGSFGGGSFGGGSFGGGGFGGGGFGGGFGGGFGGDGGLLSGNEKVTMQNLNDRLASYLDKVRALEESNYELEGKIKEWYEKHGNSHQGEPRDYSKYYKTIDDLKNQILNLTTDNANILLQIDNARLAADDFRLKYENEVALRQSVEADINGLRRVLDELTLTKADLEMQIESLTEELAYLKKNHEEEMKDLRNVSTGDVNVEMNAAPGVDLTQLLNNMRSQYEQLAEQNRKDAEAWFNEKSKELTTEIDNNIEQISSYKSEITELRRNVQALEIELQSQLALKQSLEASLAETEGRYCVQLSQIQAQISALEEQLQQIRAETECQNTEYQQLLDIKIRLENEIQTYRSLLEGEGSSGGGGRGGGSFGGGYGGGSSGGGSSGGGHGGGHGGSSGGGYGGGSSGGGSSGGGYGGGSSSGGHGGSSSGGYGGGSSGGGGGGYGGGSSGGGSSSGGGYGGGSSSGGHKSSSSGSVGESSSKGPRY
Protein: C-C chemokine receptor type 10 (C-C CKR-10) (CC-CKR-10) (CCR-10) (Chemokine C-C receptor 9) (G-protein coupled receptor 2) (Q9JL21)
Organism: Mus musculus (Mouse)
Function: Receptor for chemokines SCYA27 and SCYA28. Subsequently transduces a signal by increasing the intracellular calcium ions level.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- C-C motif chemokine 27
- C-C motif chemokine ligand 27A
- C-C motif chemokine 28
- C-C motif chemokine
- C-C motif chemokine 22
- C-C motif chemokine 1
- Guanine nucleotide-binding protein G
- Predicted gene, 20878
- C-C motif chemokine 2
- Stromal cell-derived factor 1
Sequence:
MGTKPTEQVSWGLYSGYDEEAYSVGPLPELCYKADVQAFSRAFQPSVSLMVAVLGLAGNGLVLATHLAARRTTRSPTSVHLLQLALADLLLALTLPFAAAGALQGWNLGSTTCRAISGLYSASFHAGFLFLACISADRYVAIARALPAGQRPSTPSRAHLVSVFVWLLSLFLALPALLFSRDGPREGQRRCRLIFPESLTQTVKGASAVAQVVLGFALPLGVMAACYALLGRTLLAARGPERRRALRVVVALVVAFVVLQLPYSLALLLDTADLLAARERSCSSSKRKDLALLVTGGLTLVRCSLNPVLYAFLGLRFRRDLRRLLQGGGCSPKPNPRGRCPRRLRLSSCSAPTETHSLSWDN