wanglab/gogpt-training-data huggingface dataset:
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8I220)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MVRTGGSGGGGVDKDGIDHQSAKHLLDSIGKKVHDQVKNGADGTGASGDAKNYIDDLKGDLQKAPNINPKLIGTDDPCKLVEDYYNNHVNGDGKGERYPCTELSGKKFQNPFSDTLGGQCTNSKMRSGCEGACAPYRRLHLCHHNLESIETTSKTASDTLLLEVCMAAKYEGQSINTHYTKHEHSNKDSPSQLCTVLARSFADIGDIVRGKDLFYGNTYESARREKLENKLKEVFGKIHGGLSEEAKKKYQDGDGNYYQLREDWWTANRETVWKAITCEVKSGNNYFRATCGDEKNPSLTSKQCRCDKDKAGKPIKGSGNVNIVPTYFDYVPQYLRWFEEWAEDFCRLRKHKLKDAIKKCRGKNGEEKYCDLNRYDCKNTASGKHVFFEDFDCKDCQYSCAPFVDWIDNQKLEFLKQRKKYTKEITSGGSCGGSGRKKRDATTTNYEEYEKKFYKELKGTKYKVVNNFLEKLNDEDVCTKNNDIKDGGNIDFKNVHSGSAKKGDGNNKTFYRTKYCEACPWCGAEKVEGGWKAKEENCSQTKDYDPDKTTTIEILTGDTRKSDMVQKYKKFCNGNGGNGEKSATPNATSREKGKKGDQMEKWICYYDENKEKKYGSDAINFCVLQDGKQHRKEQKVTSYNAFFWKWVHDMLHDSVEWRERLNSCINNAKSQNCKNNEKCNKECGCFEKWVKQKKEKEWEAIKDHFGKQKDIIEQTGCDAGVTLAAVLKLEFLNEDTEEKSEKGLDAEEAKEIKHLRQMLEQAGVRDLAAVGGPCTEGGVAEQNTIMDKFLDEELKEAEQCKNCPKPKAQQEGPGGARSADSPPAGTEDHPDAEDDDDEDDDDDDDEDEEEEEEEEDPQCKTVNDILSTDDRTKQVGDCHEKNYGKNGPDWKCGDLTLVDDTKVCMPPRRQKLCLYYIAHESETKNIETQDDLRDAFIRTAAAETFLSWQYYKIKNGADAKQLDNGTIPEEFLRSMYFTYGDYRDICLNTDISKTVNDVAKAKDKIGKFFSKDGSKSPSGTTTPQDWWQTYGKDIWKGMICALTHGVTNTEKKTKIKNDYSYDKVNQSQNGNPSLEDFAKKPQFLRWMIEWGEEFCAERGKLEQNIGKSCNGINPIQYCSDNRHPCNKACDEYKNYVETKQKEFRGQTTKFVRDANLENADQEYKDYKTTQGPSKQGNDYLKDKCDNKKCSCMEGNVLTDVSSKKPFGIYAHKYSEKCNCLGAKFVPTNVPPAPPPQPPPPPAIPAPATTPGVNPCEIVNTLFSDTNKFKDACTLKYGPKAPTSWKCIPTGNTSNEGAATDSEGSDAKSRHKRDLAPSSGSNQGSICVPPRRRKLYVTPLTKWAEETTKGSKSQESGKAEGTSESSGSEASSPGGTSSQGEKSPQGLSTPASTSSPSNSRDDDLLKAFVESAAVETFFLWHKYKMDKQKELDEKKKQQRESGLVGALDGNSGNVDDEDKDPQKKLEKGDIPEEFKRQMFYTLGDYRDILVRGGNTSDSGNTNGSNNNNIVIEASGDKQDEMKKIQKAIDEHINSLKQAASVPNPQRPGQQQQNSSLTRETLWKEHAPSIWEGMICALTYKENDEKKIVKDNEVYEKFFGTTPGTTSGKYKEKYEYNTVKLDENSDTEAKDTKATAPSDNTPTFLSHFVLRPPYFRYLEEWGETFCKERKKKLAQIKVDCKVDSADYKCSGYGEECKIEDISNIGVFADLKCPGCGRECRKYKKWIERKKIEFGEQKSAYVKQKTKCKEESGGGGNGVCGTVKTCDTAAQFLERLGPCKNNDNGEGKIEFNEQSETFKHTKHCDPCSSFKIDCRNGKCKSGDTKGKCDGITTIDAKEIAKMISSTPDVVMRVSDNDTNTFEGDDLKVCEGKGIFKGIRKEEWKCRNECGLDVCGLKKGDNNGKLDDKQIILIRALIKRWLEYFLEDYNKIKHKISDCINNGEGNICKRDCQNKCNCVGEWIKLKKEEWEKIKKHYLEKNKEGDNDMKSSVRNFLEKFEHRPEFNKAIKPCKGLTQFESFCGLNGDKPSQNGHQDAIDCMIKKLEDKITSCLSSTSGEQTETECQEHTPLPDDEDLLLEETENPVGKQQPSFCPKVEEKKETVDEGKCGEDTSEPKKTEDEESKKKKDESTPDSPEPPPPATPEAPKEEKKVEPQPQPQPTTPQIVDKTPALVTSTLAWSVGIGFAAFTYFFLKKKTKSTIDLLRVINIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEEMDINDIYAPRAPKYKTLIEVVLEPSGNNTTASGNNTTASGNNTTASGNNTTASGKNTPSDTQNDIQSDGIPSSKITDNEWNTLKDEFISQYIQSEQPKDVPNDYSSGDIPFNTQHNTLYFDKPDEKPFITSIHDRNLYTGEEYNYDMSTNSGNNDLYNGKNNLYSGQNNVYSGIDPTSDNRGLTSGKHDSYSGIDLINDTLSGNQHIDIYDEVLKRKENELFGTNHVKHTTINRFAKPARDDPLHNQLELFHTWLDRHRNMCEKWNNKEELLDKLKEEWENETHSGNTHPSDSNKTLNTDVSIQIDMDNPKPINQFTNMDINVDTPTMDNMEDDIYYDVNDHDTSTVDSNTMDVPSKVQIEMDVNTKLVKEKYPIADVWDI
Protein: Adenylosuccinate synthetase isozyme 1 (AMPSase 1) (AdSS 1) (EC 6.3.4.4) (Adenylosuccinate synthetase, basic isozyme) (Adenylosuccinate synthetase, muscle isozyme) (M-type adenylosuccinate synthetase) (IMP--aspartate ligase 1) (M0R629)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03126}.
Interaction partners:
- Adenylosuccinate lyase
- Bifunctional purine biosynthesis protein ATIC
- Inosine-5'-monophosphate dehydrogenase 2
- Trifunctional purine biosynthetic protein adenosine-3
- Inosine-5'-monophosphate dehydrogenase 1
- AMP deaminase 1
- GMP reductase 1
- GMP reductase
- AMP deaminase 2
- Inosine triphosphate pyrophosphatase
Sequence:
MSGTRASNDRPPGTGGVKRGRLQQEAAATGSRVTVVLGAQWGDEGKGKVVDLLATDADIVSRCQGGNNAGHTVVVDGKEYDFHLLPSGIINTKAVSFIGNGVVIHLPGLFEEAEKNEKKGLKDWEKRLIISDRAHLVFDFHQAVDGLQEVQRQAQEGKNIGTTKKGIGPTYSSKAARTGLRICDLLSDFDEFSARFKNLAHQHQSMFPTLEIDVEGQLKRLKGFAERIRPMVRDGVYFMYEALHGPPKKILVEGANAALLDIDFGTYPFVTSSNCTVGGVCTGLGIPPQNIGDVYGVVKAYTTRVGIGAFPTEQINEIGDLLQNRGHEWGVTTGRKRRCGWLDLMILRYAHMVNGFTALALTKLDILDVLSEIKVGISYKLNGKRIPYFPANQEILQKVEVEYETLPGWKADTTGARKWEDLPPQAQSYVRFVENHLGVAVKWVGVGKSRESMIQLF
Protein: Sorting nexin-9 (SH3 and PX domain-containing protein 1) (Protein SDP1) (SH3 and PX domain-containing protein 3A) (Q9Y5X1)
Organism: Homo sapiens (Human)
Function: Involved in endocytosis and intracellular vesicle trafficking, both during interphase and at the end of mitosis. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Plays a role in endocytosis via clathrin-coated pits, but also clathrin-independent, actin-dependent fluid-phase endocytosis. Plays a role in macropinocytosis. Promotes internalization of TNFR. Promotes degradation of EGFR after EGF signaling. Stimulates the GTPase activity of DNM1. Promotes DNM1 oligomerization. Promotes activation of the Arp2/3 complex by WASL, and thereby plays a role in the reorganization of the F-actin cytoskeleton. Binds to membranes enriched in phosphatidylinositol 4,5-bisphosphate and promotes membrane tubulation. Has lower affinity for membranes enriched in phosphatidylinositol 3-phosphate.
Subcellular location: Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network. Cell projection, ruffle. Cytoplasm. Note=Localized at sites of endocytosis at the cell membrane. Detected on newly formed macropinosomes. Transiently recruited to clathrin-coated pits at a late stage of clathrin-coated vesicle formation. Colocalizes with the actin cytoskeleton at the cell membrane.
Interaction partners:
- Disintegrin and metalloproteinase domain-containing protein 15
- Disintegrin and metalloproteinase domain-containing protein 9
- Actin nucleation-promoting factor WASL
- Sorting nexin-33
- Sorting nexin-18
- Synaptojanin-1
- Dynamin-1
- Actin nucleation-promoting factor WAS
- Dynamin-2
- Endophilin-A1
Sequence:
MATKARVMYDFAAEPGNNELTVNEGEIITITNPDVGGGWLEGRNIKGERGLVPTDYVEILPSDGKDQFSCGNSVADQAFLDSLSASTAQASSSAASNNHQVGSGNDPWSAWSASKSGNWESSEGWGAQPEGAGAQRNTNTPNNWDTAFGHPQAYQGPATGDDDDWDEDWDGPKSSSYFKDSESADAGGAQRGNSRASSSSMKIPLNKFPGFAKPGTEQYLLAKQLAKPKEKIPIIVGDYGPMWVYPTSTFDCVVADPRKGSKMYGLKSYIEYQLTPTNTNRSVNHRYKHFDWLYERLLVKFGSAIPIPSLPDKQVTGRFEEEFIKMRMERLQAWMTRMCRHPVISESEVFQQFLNFRDEKEWKTGKRKAERDELAGVMIFSTMEPEAPDLDLVEIEQKCEAVGKFTKAMDDGVKELLTVGQEHWKRCTGPLPKEYQKIGKALQSLATVFSSSGYQGETDLNDAITEAGKTYEEIASLVAEQPKKDLHFLMECNHEYKGFLGCFPDIIGTHKGAIEKVKESDKLVATSKITLQDKQNMVKRVSIMSYALQAEMNHFHSNRIYDYNSVIRLYLEQQVQFYETIAEKLRQALSRFPVM
Protein: Probable cation-transporting ATPase 13A4 (EC 7.2.2.-) (P5-ATPase isoform 4) (Q4VNC1)
Organism: Homo sapiens (Human)
Subcellular location: Early endosome membrane {ECO:0000250|UniProtKB:Q5XF90}; Multi-pass membrane protein {ECO:0000255}. Late endosome membrane {ECO:0000250|UniProtKB:Q5XF90}; Multi-pass membrane protein {ECO:0000255}. Recycling endosome membrane {ECO:0000250|UniProtKB:Q5XF90}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGHFEKGQHALLNEGEENEMEIFGYRTQGCRKSLCLAGSIFSFGILPLVFYWRPAWHVWAHCVPCSLQEADTVLLRTTDEFQIYSWKKVIWIYLSALNSAFGLTPDHPLMTDEEYIINRAIRKPDLKVRCIKVQKIRYVWNYLEGQFQKIGSLEDWLSSAKIHQKFGSGLTREEQEIRRLICGPNTIDVEVTPIWKLLIKEVLNPFYIFQLFSVCLWFSEDYKEYAFAIIIMSIISISLTVYDLREQSVKLHHLVESHNSITVSVCGRKAGVQELESRVLVPGDLLILTGNKVLMPCDAVLIEGSCVVDEGMLTGESIPVTKTPLPKMDSSVPWKTQSEADYKRHVLFCGTEVIQAKAACSGTVRAVVLQTGFNTAKGDLVRSILYPKPVNFQLYRDAIRFLLCLVGTATIGMIYTLCVYVLSGEPPEEVVRKALDVITIAVPPALPAALTTGIIYAQRRLKKRGIFCISPQRINVCGQLNLVCFDKTGTLTRDGLDLWGVVSCDRNGFQEVHSFASGQALPWGPLCAAMASCHSLILLDGTIQGDPLDLKMFEATTWEMAFSGDDFHIKGVPAHAMVVKPCRTASQVPVEGIAILHQFPFSSALQRMTVIVQEMGGDRLAFMKGAPERVASFCQPETVPTSFVSELQIYTTQGFRVIALAYKKLENDHHATTLTRETVESDLIFLGLLILENRLKEETKPVLEELISARIRTVMITGDNLQTAITVARKSGMVSESQKVILIEANETTGSSSASISWTLVEEKKHIMYGNQDNYINIRDEVSDKGREGSYHFALTGKSFHVISQHFSSLLPKILINGTIFARMSPGQKSSLVEEFQKLDYFVGMCGDGANDCGALKMAHVGISLSEQEASVASPFTSKTPNIECVPHLIKEGRAALVTSFCMFKYMALYSMIQYVGVLLLYWETNSLSNYQFLFQDLAITTLIGVTMNLNGAYPKLVPFRPAGRLISPPLLLSVIFNILLSLAMHIAGFILVQRQPWYSVEIHSACTVQNESISELTMSPTAPEKMESNSTFTSFENTTVWFLGTINCITVALVFSKGKPFRQPTYTNYIFVLVLIIQLGVCLFILFADIPELYRRLDLLCTPVLWRASIVIMLSLNFIVSLVAEEAVIENRALWMMIKRCFGYQSKSQYRIWQRDLANDPSWPPLNQTSHSDMPECGRGVSYSNPVFESNEEQL
Protein: Zinc finger ZPR1-type domain-containing protein (A0A178UA90)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDNKNDQDIDVRSVVEAVSADLSFGAPLYVVESMCMRCQENGTTRFLLTLIPHFRKVLISAFECPHCGERNNEVQFAGEIQPRGCCYNLEVLAGDVKIFDRQVVKSESATIKIPELDFEIPPEAQRGSLSTVEGILARAADELSALQEERKKVDPKTAEAIDQFLSKLRACAKAETSFTFILDDPAGNSFIENPHAPSPDPSLTIKFYERTPEQQATLGYVANPSQAGQSEGSLGAPSTKTAYVPNGTIGATAGHRAIAQSNSTDISDNLFRYSAPEEVMTFPSTCGACTEPCETRMFVTKIPYFQEVIVMASTCDSCGYRNSELKPGGAIPEKGKKITLSVRNITDLSRDVIKSDTAGVIIPELDLELAGGTLGGMVTTVEGLVTQIRESLARVHGFTFGDSMEESKLNKWREFGARLTKLLSFEQPWTLILDDELANSFIAPVTDDIKDDHQLTFEEYERSWDQNEELGLNDIDTSSADAAYESTETTKLP
Protein: Ferritin (C1BEL9)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MPLVRQNFHQDCEAAINRQINLELYASYVYLSMAYYFDRDDQALHNFAKFFKNQSHEEREHAEKLMKVQNQRGGRIFLQDVKKPEKDEWGCGVEALESALQLEKSVNQSLLDLHKVCADNNDPHMCDFIETHYLDEQVKSIKELGDWVTNLRRMGAPQNGMAEYLFDKHTLGKEST
Protein: Forkhead box protein O1-B (A3RK75)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor that regulates metabolic homeostasis in response to oxidative stress (By similarity). Binds to the consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3' (By similarity). Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9R1E0}. Nucleus {ECO:0000250|UniProtKB:Q9R1E0}. Note=Shuttles between the cytoplasm and nucleus. {ECO:0000250|UniProtKB:Q9R1E0}.
Interaction partners:
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- V-akt murine thymoma viral oncogene homolog 2,-like.
- non-specific serine/threonine protein kinase
- Non-specific serine/threonine protein kinase.
- Ubiquitin carboxyl-terminal hydrolase 7
- Signal transducer and activator of transcription
- Inhibitor of nuclear factor kappa B kinase subunit beta.
- Serine/threonine kinase 11
- cyclin-dependent kinase
Sequence:
MAEPQQQLVDIDPDFEPLSRPRSCTWPLHRPEFSEQPGNSNTSSPAPSVKPEQGIVDFINSLSLLEETEDYPDEKPVLLNDFHCQDNCAHPQQQHPQQPNPQLTHPQQVPPLPAPASGSSPAAAQRKSSSSRRNAWGNMSYADLITKAIESSPEKRLTLSQIYEWMVKSVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFVRVQNEGTGKSSWWMLNPEGGKSGKSPRRRATSMDNNSKFTKSRGRAAKKKMSLQGGLDGGSNSPGSQYPKWLGSPNSHSNDDFEPWGNFRTRASSDASTLSGRRSPFLPEEDEAAEVHIGYPGTKLGGPLPSLSEVAGHHGSENMMDNLLENLNLISPKNNTQGSQEAQTALSSPLMQGSPGYPSYTSPNMGPQPQVQQDYRKCLYGQGGVGGLNPISIPTLSDSKPGGYGPFVGQYNCAPGLLKELLTADADPRGELMQSGEGQPVLPSYASQGQMAQGGKMITHPHLHAHPRSLHQLPSPAMGLNGCAMLPHGHPVRLSSMKPQPHLPHHTHLGRGGGEAGMPSYTNGNGFHRHGAIAHHHHSHPERLPSDLDDMLIDQLDVECDVERVLHDTLMDGDALDFNFDPMSSQQSFTHSVKTSTHNWVSG
Protein: Uric acid transporter UacT (Q46821)
Organism: Escherichia coli (strain K12)
Function: Proton-dependent high-capacity transporter for uric acid. Shows also a low capacity for transport of xanthine at 37 degrees Celsius but not at 25 degrees Celsius.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:22437829}; Multi-pass membrane protein {ECO:0000269|PubMed:22437829}.
Interaction partners:
- Putative purine permease YbbY
- Guanine/hypoxanthine permease GhxQ
- Adenine permease AdeQ
- Adenine permease AdeP
- Guanine/hypoxanthine permease GhxP
- Xanthine permease XanQ
- Inner membrane protein YqcE
- Uncharacterized protein YqfG
- D-phenylhydantoinase
- Inner membrane protein YijD
Sequence:
MSAIDSQLPSSSGQDRPTDEVDRILSPGKLIILGLQHVLVMYAGAVAVPLMIGDRLGLSKEAIAMLISSDLFCCGIVTLLQCIGIGRFMGIRLPVIMSVTFAAVTPMIAIGMNPDIGLLGIFGATIAAGFITTLLAPLIGRLMPLFPPLVTGVVITSIGLSIIQVGIDWAAGGKGNPQYGNPVYLGISFAVLIFILLITRYAKGFMSNVAVLLGIVFGFLLSWMMNEVNLSGLHDASWFAIVTPMSFGMPIFDPVSILTMTAVLIIVFIESMGMFLALGEIVGRKLSSHDIIRGLRVDGVGTMIGGTFNSFPHTSFSQNVGLVSVTRVHSRWVCISSGIILILFGMVPKMAVLVASIPQFVLGGAGLVMFGMVLATGIRILSRCNYTTNRYNLYIVAISLGVGMTPTLSHDFFSKLPAVLQPLLHSGIMLATLSAVVLNVFFNGYQHHADLVKESVSDKDLKVRTVRMWLLMRKLKKNEHGE
Protein: Lipase E, hormone sensitive type (M0QXM5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MDLRTMTQSLVTLAEDNIAFFSSQGPGETAQRLSGVFAGVREQALGLEPALGRLLGVAHLFDLDPETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALVYYAQRLLVTNRPGVLFFEGDEGLTADFLREYVTLHKGCFYGRCLGFQFTPA
Protein: N-acetylgalactosamine-6-phosphate deacetylase (GalNAc-6-P deacetylase) (EC 3.5.1.-) (N-acetylglucosamine-6-phosphate deacetylase) (GlcNAc-6-P deacetylase) (EC 3.5.1.25) (A0KYQ5)
Organism: Shewanella sp. (strain ANA-3)
Function: Involved in the pathway of N-acetyl-D-galactosamine degradation. Catalyzes the conversion of N-acetyl-D-galactosamine 6-phosphate to D-galactosamine 6-phosphate and acetate. It can also catalyze the conversion of N-acetyl-D-glucosamine 6-phosphate.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:22711537}.
Interaction partners:
- N-acetylgalactosamine kinase AgaK
- ATPase, BadF/BadG/BcrA/BcrD type
- Sugar isomerase
- D-galactosamine-6-phosphate deaminase AgaS
- Glutamine--fructose-6-phosphate aminotransferase
- Phosphoglucosamine mutase
- N-acetylgalactosamine-6-phosphate deacetylase
- Transcriptional regulator, DeoR family
- 6-phosphogluconolactonase
- Tagatose-bisphosphate aldolase noncatalytic subunit
Sequence:
MKPNTDFMLIADGAKVLTQGNLTEHCAIEVSDGIICGLKSTISAEWTADKPHYRLTSGTLVAGFIDTQVNGGGGLMFNHVPTLETLRLMMQAHRQFGTTAMLPTVITDDIEVMQAAADAVAEAIDCQVPGIIGIHFEGPHLSVAKRGCHPPAHLRGITEREWLLYLRQDLGVRLITLAPESVTPEQIKRLVASGAIISLGHSNADGETVLKAIEAGASGFTHLYNGMSALTSREPGMVGAAFASENTYCGIILDGQHVHPISALAAWRAKGTEHLMLVTDAMSPLGSDQTEFQFFDGKVVREGMTLRDQHGSLAGSVLDMASAVRYAATELNLGLSNAVQMATRTPAEFIQRPQLGDIAEGKQADWVWLDDDQRVLAVWIAGELLYQAEQARFA
Protein: Farnesoic acid O-methyl transferase domain-containing protein (Q9W2M4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
Sequence:
MPIEVNTPDKLEYQFFPASGGVFTFKVRSPKDAHLALTPAPEENGPIFEIFLGGWENTKSVIRKDRQKPEVAEVPTPGILDAGEFRGFWVRWYDNVITVGREGDAAAFLSYDAGSLFPVNFVGICTGWGASGTWLIDEPAPSAPVMGFAAPTGSGPGCWVPAANGEVPPNALEGGFDSSEQLYIARARHEGDLIPGKLHPSHGVTYVAWGGGEHGHAEYEVLCAGGGQWLPVDAGNIPPNALPAGETAEGEPLFIGRATHDGTITVGKVQPSHGCCYIPYGGEELAYKEFEIYVTN
Protein: 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 3 (At3BETAHSD/D3) (EC 1.1.1.170) (4alpha-carboxysterol-C3-dehydrogenase/C4-decarboxylase isoform 1-3) (Reticulon-like protein B20) (AtRTNLB20) (Sterol-4-alpha-carboxylate 3-dehydrogenase 3, decarboxylating) (A9X4U2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Methylsterol monooxygenase 1-3
- Methylsterol monooxygenase 1-2
- Methylsterol monooxygenase 1-1
- Methylsterol monooxygenase 2-1
- Methylsterol monooxygenase 2-2
- Reticulon-like protein B21
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 2
- 3beta-hydroxysteroid-dehydrogenase/decarboxylase isoform 1
- Ergosterol biosynthetic protein 28
- Reticulon-like protein B17
Sequence:
MDEDSVHGDSHLKTCVVLGGRGFIGRSLVSRLLRLGNWTVRVADSGHTLHLDESDSLLEDALSSGRASYHCVDVRDKPQIVKVTEGSYVVFYMGATDLRSHDYFDCYKVIVQGTRNVISACRESGVRKLIYNSTADVVFDGSQPIRDGDESLRRPLKFQSMLTDFKAQAEALIKLANNRDGLLTCALRSSIVFGPGDTEFVPFLVNLAKSGYAKFILGSGENISDFTYSENVSHAHICAVKALDSQMEFVAGKEFFITNLKPVRFWDFVSHIVEGLGYPRPSIKLPVRLVLYVFSLLKWTHEKEGLGSNYDTAHQYALLASSTRTFNCNAAKKHLGYTPVVTLEDGIASTLQWFSRDLEKSDDTIIQSTADQLLGCGKVADILLWRNEKKTFVSFLVLNLFYYWFFFSGNTFTSSAAQLLFIFAVALYGVSFVPSKIFGFQVNKIPPWRFEISESAVRDLSSDIVVVWNQGVRSFKSLSSGGDWIKFFKIAGSLYLLKLIVSRSLAAFLFTVMSFSFTGFFIYEQYELELYHLARIFVECLTFIKRMVIPVSDASSKPMFM
Protein: Heterogeneous nuclear ribonucleoprotein D like (Heterogeneous nuclear ribonucleoprotein D-like, isoform CRA_b) (A0A087WUK2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MEVPPRLSHVPPPLFPSAPATLASRSLSHWRPRPPRQLAPLLPSLAPSSARQGARRAQRHVTAQQPSRLAGGAAIKGGRRRRPDLFRRHFKSSSIQRSAAAAAATRTARQHPPADSSVTMEDMNEYSNIEEFAEGSKINASKNQQDDGKMFIGGLSWDTSKKDLTEYLSRFGEVVDCTIKTDPVTGRSRGFGFVLFKDAASVDKVLELKEHKLDGKLIDPKRAKALKGKEPPKKVFVGGLSPDTSEEQIKEYFGAFGEIENIELPMDTKTNERRGFCFITYTDEEPVKKLLESRYHQIGSGKCEIKVAQPKEVYRQQQQQQKGGRGAAAGGRGGTRGRGRGQQSTYGKASRGGGNHQNNYQPY
Protein: Glutathione S-transferase F12 (AtGSTF12) (EC 2.5.1.18) (GST class-phi member 12) (Glutathione S-transferase 26) (Protein TRANSPARENT TESTA 19) (Q9FE46)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the transport and/or accumulation of both anthocyanins and proanthocyanidins (PA)s in the vacuole. Functions in the cytosol to maintain the regular accumulation in the vacuole of PA precursors, such as epicatechin and glycosylated epicatechin.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20180920}.
Interaction partners:
- Dihydroflavonol 4-reductase
- Leucoanthocyanidin dioxygenase
- Protein DETOXIFICATION 41
- Transcription factor TT8
- Transcription factor MYB75
- ATPase 10, plasma membrane-type
- Anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase
- Flavonoid 3'-monooxygenase
- UDP-glycosyltransferase 75C1
- Malonyl-CoA:anthocyanidin 5-O-glucoside-6''-O-malonyltransferase
Sequence:
MVVKLYGQVTAACPQRVLLCFLEKGIEFEIIHIDLDTFEQKKPEHLLRQPFGQVPAIEDGDFKLFESRAIARYYATKFADQGTNLLGKSLEHRAIVDQWADVETYYFNVLAQPLVINLIIKPRLGEKCDVVLVEDLKVKLGVVLDIYNNRLSSNRFLAGEEFTMADLTHMPAMGYLMSITDINQMVKARGSFNRWWEEISDRPSWKKLMVLAGH
Protein: Protein Diedel (Q9VAK8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Cytokine which promotes survival following infection by Sindbis virus by suppressing the immune deficiency pathway. Following infection by the enteropathogenic bacteria E.carotovora limits intestinal stem cells proliferation. When secreted from muscle or adipose tissue, can attenuate age-related intestinal tissue degeneration by inhibiting apoptosis.
Subcellular location: Secreted {ECO:0000269|PubMed:22442689, ECO:0000269|PubMed:26739560, ECO:0000269|PubMed:30036358}. Note=Secreted into the hemolymph. {ECO:0000269|PubMed:26739560}.
Interaction partners:
- HDC05827
- Phenoloxidase-activating factor 2
- Protein Turandot M
- Dysfusion, isoform D
Sequence:
MASPVVSLLLVGICALAFVHVARSECCTSRELVEFKMDRGDCEAVRAIENYPNGCEVTICADGVAQLGAYCGQGSCNIFGCNCDGGCLSGDWSQEFVRRNQQYGIQIIKVTRLPF
Protein: DNA-directed RNA polymerase I subunit RPA14 (A14) (DNA-directed RNA polymerase I 14 kDa polypeptide) (P50106)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: DNA-dependent RNA polymerases catalyze the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase I (Pol I) which synthesizes ribosomal RNA precursors. RPA14 seems to play a role in the stability of subunits RPO26 and RPA43. In vitro, the RPA14-RPA43 subcomplex binds single-stranded RNA.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA-directed RNA polymerase I subunit RPA190
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- DNA-directed RNA polymerase I subunit RPA43
- DNA-directed RNA polymerase I subunit RPA12
- DNA-directed RNA polymerase I subunit RPA34
- DNA-directed RNA polymerase I subunit RPA135
- DNA-directed RNA polymerase I subunit RPA49
- DNA-directed RNA polymerases I and III subunit RPAC1
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
Sequence:
MMKGSRRTGNNTATTLNTPVVIHATQLPQHVSTDEVLQFLESFIDEKENIIDSTTMNTISGNAADADAAAVANTSLNIDTNLSSSISQLKRIQRDFKGLPPAQDFSAAPIQVSTTEKKETSIGVSATGGKKTTFADE
Protein: Integrin beta (D3ZP06)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU000633}. Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MLKIRPLKKYPVDLYYLVDVSASMHNNIEKLNSVGNDLSKKMALFSHDFRLGFGSYVDKTVSPYISIHPERIHNQCSDYNLDCMPPHGYIHVLSLTENITEFEKAVHRQKISGNIDTPEGGFDAMLQAAVCESHIGWRKEAKRLLLVMTDQTSHLALDSKLAGIVVPNDGNCHLKNNVYVKSTTMEHPSLGQLSEKLIDNNINVIFAVQGKQFHWYKDLLPLLPGAIAGEIESKAANLNNLVVEAYKVLFNVTVVMKTCDIIGGKNYAIIKPIGFNETTKVHIHRSCSCQCEDHRGLKGQCAEAAPDPKCPQCDDGKCHFDEDQFPSEACKPQEDQPVCSGRGVCICGKCLCHKTKLGRVYGQYCEKDDFSCPYLHGDVCSGHGECEGGRCQCFNGWEGDRCQCPSASAQHCVNSKGQVCSGRGTCVCGRNCLQCLHPHNLSQAVLDQCKASCAVMEQHPVAQTSECLSGPSYLRIFFIIFIVTFLIGLLKVLIIRQVILQWNSNKIKSSSDYRVSASKKDKLILQSVCTRAVTYRREKPEEIKMDISKLNAQEAFRCNF
Protein: PSME3-interacting protein (NEFA-interacting nuclear protein NIP30) (PA28G-interacting protein) (Q9GZU8)
Organism: Homo sapiens (Human)
Function: Promotes the association of the proteasome activator complex subunit PSME3 with the 20S proteasome and regulates its activity. Inhibits PSME3-mediated degradation of some proteasome substrates, probably by affecting their diffusion rate into the catalytic chamber of the proteasome. Also inhibits the interaction of PSME3 with COIL, inhibits accumulation of PSME3 in Cajal bodies and positively regulates the number of Cajal bodies in the nucleus.
Subcellular location: Nucleus {ECO:0000269|PubMed:29934401}.
Interaction partners:
- Homeobox protein goosecoid
- Proteasome activator complex subunit 3
- Splicing factor Cactin
- Pre-mRNA-splicing factor SYF1
- Cell division cycle 5-like protein
- Pre-mRNA-processing-splicing factor 8
- Protein FAM32A
- PRKR-interacting protein 1
- ATP-dependent RNA helicase DHX8
- Pre-mRNA-splicing factor SLU7
Sequence:
MDGGDDGNLIIKKRFVSEAELDERRKRRQEEWEKVRKPEDPEECPEEVYDPRSLYERLQEQKDRKQQEYEEQFKFKNMVRGLDEDETNFLDEVSRQQELIEKQRREEELKELKEYRNNLKKVGISQENKKEVEKKLTVKPIETKNKFSQAKLLAGAVKHKSSESGNSVKRLKPDPEPDDKNQEPSSCKSLGNTSLSGPSIHCPSAAVCIGILPGLGAYSGSSDSESSSDSEGTINATGKIVSSIFRTNTFLEAP
Protein: Malonyl-CoA decarboxylase, mitochondrial, putative (EC 4.1.1.9) (Q57VP8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Acetyl-CoA carboxylase, putative
- Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex
- Dihydrolipoamide acetyltransferase, putative
- Acetyl-coenzyme A synthetase
Sequence:
MLTLVRRPYCSRRMRFPFHLDNISRVSHRYNATDVTLQLSEDRLANWCRRLWALAQGGGDGDDDGSAVPASNGTTKSGSVFSGRGPHTEFTLVEEMKSVLVGEKGQLPPSVVSAVWDVYESIIPPSTLFDLSETISPNQEDAFFSFVALLMELDVDIVEVQAAVAQLNNTIQNIEDLNAQSGQFIAGGCSATVSAESCFREENRSGVGAAVLSSKLVKAKNNLLRQCVAALHAGSPVYYMWFKQSASVERGVRRLMDLRRCVMYFQKRCHCQVAQLQAELKRQHERQSSRQVIDSPPNSGPLTTNRELELWLLRQHHVSSIDVSLEYLFGDFFSKQWLVMEELTWRTTPPLLLEKVMAAESVHPFVGGLVDMKQRLQPAKNRHLFAFFHPAVVEEPLIAVQVALTRGIARSVDIILGRPHPPSVQERQNDQLGAANGEVADACSGARKHDPVEDVDTSMFYSINSVQSALRGVNLGNMLIKRVVREIEARLNGERHCAGLSPITTFSTISPVPGYLRWLVGEVAKLQQQVEMRSGSISLCSSSKKFAQPRIFGECSKPKAAELFSILRGAVLGLSHHRGRGCGHFISRLHYHLREGNEDAANLVTMQYLLALFGSPEEDGTGESGAPGKADEDVISPWWNDSEFTRTVEKPLLRSVAHYLYKEKHRNRILDPVGNFHISNGATMFRLNFLANCTADGSRQSATVMVNYLYEPACVDERVKAYGMQRSVPIGDDVLRLLNIS
Protein: At3g04640 (F7O18.12 protein) (Glycine-rich protein) (Q9SR10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Nuclease
- At3g04210/T6K12_17)
- At1g49000
- Berberine bridge enzyme-like 8
- Putative metallothionein-like protein 1B
- Kinase family with leucine-rich repeat domain-containing protein
- Cytochrome P450 89A9
- Protein SULFUR DEFICIENCY-INDUCED 2
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase
- Glutathione S-transferase L1
Sequence:
MDLKKASLFLFLLLCLHLQLQHHFAHAVSRSSTSLAFVDPNHDDLPFQEVELKPDGDVIEANLPKLTVVVKKGGGGGGRGGGGFGGGGRSFGGGGSSSRGGGGSSSRGGGGSSSRGGGLRPIPIYGGGTHRSGHHSSGGRETASGWLGLSILAGLGLVF