wanglab/gogpt-training-data huggingface dataset:
Protein: GEO07594p1 (Mitochondrial ribosomal protein S17) (RE28524p) (Q9W199)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- 28S ribosomal protein S14
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS3m
- Small ribosomal subunit protein mS40
- GEO10172p1
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein mS25
Sequence:
MSRRGLLLMGQCMPCIKQNASKIRIRRMELDKNLNMYFKKDEFYFAHDPQKVCKTGDVVLIRELPERLTRLITHNVEKVVYPLGDITDPLTGKKVVVGNYREDIEMANQLFGKSEKAFDYEKAPPRGRLEGTKDFTHGETYIKYHEDGKDQPFAV
Protein: Bifunctional purine biosynthesis protein ATIC (EC 2.1.2.3) (EC 3.5.4.10) (AICAR transformylase/inosine monophosphate cyclohydrolase) (V9HWH7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
Sequence:
MAPGQLALFSVSDKTGLVEFARNLTALGLNLVASGGTAKALRDAGLAVRDVSELTGFPEMLGGRVKTLHPAVHAGILARNIPEDNADMARLDFNLIRVVACNLYPFVKTVASPGVTVEEAVEQIDIGGVTLLRAAAKNHARVTVVCEPEDYVVVSTEMQSSESKDTSLETRRQLALKAFTHTAQYDEAISDYFRKQYSKGVSQMPLRYGMNPHQTPAQLYTLQPKLPITVLNGAPGFINLCDALNAWQLVKELKEALGIPAAASFKHVSPAGAAVGIPLSEDEAKVCMVYDLYKTLTPISAAYARARGADRMSSFGDFVALSDVCDVPTAKIISREVSDGIIAPGYEEEALTILSKKKNGNYCVLQMDQSYKPDENEVRTLFGLHLSQKRNNGVVDKSLFSNVVTKNKDLPESALRDLIVATIAVKYTQSNSVCYAKNGQVIGIGAGQQSRIHCTRLAGDKANYWWLRHHPQVLSMKFKTGVKRAEISNAIDQYVTGTIGEDEDLIKWKALFEEVPELLTEAEKKEWVEKLTEVSISSDAFFPFRDNVDRAKRSGVAYIAAPSGSAADKVVIEACDELGIILAHTNLRLFHH
Protein: Laminin subunit beta-2 (Laminin B1s chain) (Laminin-11 subunit beta) (Laminin-14 subunit beta) (Laminin-15 subunit beta) (Laminin-3 subunit beta) (Laminin-4 subunit beta) (Laminin-7 subunit beta) (Laminin-9 subunit beta) (S-laminin subunit beta) (S-LAM beta) (P55268)
Organism: Homo sapiens (Human)
Function: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components.
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane. Note=S-laminin is concentrated in the synaptic cleft of the neuromuscular junction.
Interaction partners:
- Laminin subunit alpha-2
- Laminin subunit gamma-1
- Laminin subunit gamma-2
- Laminin subunit gamma-3
- Laminin subunit alpha-4
- Laminin subunit alpha-5
- Laminin subunit alpha-3
- CD44 antigen
- Laminin subunit alpha-1
- Integrin alpha-5
Sequence:
MELTSRERGRGQPLPWELRLGLLLSVLAATLAQAPAPDVPGCSRGSCYPATGDLLVGRADRLTASSTCGLNGPQPYCIVSHLQDEKKCFLCDSRRPFSARDNPHSHRIQNVVTSFAPQRRAAWWQSENGIPAVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWHVYRYFSYDCGADFPGVPLAPPRHWDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPDPYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYALYELVVRGNCFCYGHASECAPAPGAPAHAEGMVHGACICKHNTRGLNCEQCQDFYRDLPWRPAEDGHSHACRKCECHGHTHSCHFDMAVYLASGNVSGGVCDGCQHNTAGRHCELCRPFFYRDPTKDLRDPAVCRSCDCDPMGSQDGGRCDSHDDPALGLVSGQCRCKEHVVGTRCQQCRDGFFGLSISDRLGCRRCQCNARGTVPGSTPCDPNSGSCYCKRLVTGRGCDRCLPGHWGLSHDLLGCRPCDCDVGGALDPQCDEGTGQCHCRQHMVGRRCEQVQPGYFRPFLDHLIWEAEDTRGQVLDVVERLVTPGETPSWTGSGFVRLQEGQTLEFLVASVPKAMDYDLLLRLEPQVPEQWAELELIVQRPGPVPAHSLCGHLVPKDDRIQGTLQPHARYLIFPNPVCLEPGISYKLHLKLVRTGGSAQPETPYSGPGLLIDSLVLLPRVLVLEMFSGGDAAALERQATFERYQCHEEGLVPSKTSPSEACAPLLISLSTLIYNGALPCQCNPQGSLSSECNPHGGQCLCKPGVVGRRCDLCAPGYYGFGPTGCQACQCSHEGALSSLCEKTSGQCLCRTGAFGLRCDRCQRGQWGFPSCRPCVCNGHADECNTHTGACLGCRDHTGGEHCERCIAGFHGDPRLPYGGQCRPCPCPEGPGSQRHFATSCHQDEYSQQIVCHCRAGYTGLRCEACAPGHFGDPSRPGGRCQLCECSGNIDPMDPDACDPHTGQCLRCLHHTEGPHCAHCKPGFHGQAARQSCHRCTCNLLGTNPQQCPSPDQCHCDPSSGQCPCLPNVQGPSCDRCAPNFWNLTSGHGCQPCACHPSRARGPTCNEFTGQCHCRAGFGGRTCSECQELHWGDPGLQCHACDCDSRGIDTPQCHRFTGHCSCRPGVSGVRCDQCARGFSGIFPACHPCHACFGDWDRVVQDLAARTQRLEQRAQELQQTGVLGAFESSFWHMQEKLGIVQGIVGARNTSAASTAQLVEATEELRREIGEATEHLTQLEADLTDVQDENFNANHALSGLERDRLALNLTLRQLDQHLDLLKHSNFLGAYDSIRHAHSQSAEAERRANTSALAVPSPVSNSASARHRTEALMDAQKEDFNSKHMANQRALGKLSAHTHTLSLTDINELVCGAPGDAPCATSPCGGAGCRDEDGQPRCGGLSCNGAAATADLALGRARHTQAELQRALAEGGSILSRVAETRRQASEAQQRAQAALDKANASRGQVEQANQELQELIQSVKDFLNQEGADPDSIEMVATRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTCQ
Protein: Putative 2-hydroxyacid dehydrogenase UNK4.10 (EC 1.-.-.-) (O14075)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Mitochondrial 2-methylisocitrate lyase
- Uncharacterized kinase mug58
- D-amino-acid oxidase
- Ureidoglycolate lyase
- Large ribosomal subunit protein uL22A
- Large ribosomal subunit protein uL22B
- Putative endonuclease C1F12.06c
- Protein mmf1, mitochondrial
- Branched-chain-amino-acid aminotransferase, mitochondrial
Sequence:
MTLSGKPAALLVGTLKHAHKEWEALGKYAELKTYSDGTREDFLAKCKTEFQNVKAICRTYNSKFYMGIFDKEIIDNLPPSVKFICHLGAGYETVDVAACTARGIQVSHVPKAVDDATADVGIFLMLGALRGFNQGIFELHKNNWNANCKPSHDPEGKTLGILGLGGIGKTMAKRARAFDMKIVYHNRTPLPEEEAEGAEFVSFDDLLAKSDVLSLNLPLNAHTRHIIGKPEFQKMKRGIVIVNTARGAVMDEAALVEALDEGIVYSAGLDVFEEEPKIHPGLLENEKVILLPHLGTNSLETQYKMECAVLMNVKNGIVNDSLPNLVPEQRGDIE
Protein: Always early (Q2PNQ1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRHQLKKPRKMVAAWQNDELFIKRPNFAPRIRISEKPEIQGRVKPGVASKRTENFTKKPSKISVDVSEDEKAKEKEKEQDPYSNDFILGKRLYNFLKYLSSHRWIWCEFVDSFLDKPTLTMGYDMKRFIAEYCPLLHSCFMPRRGWQLVRRNMGKARRFSAAFIELEREELECQRRIVRQLQQHKFNPKENVGYLDQIPKRVPLPLAKDATVSSFLHGKSFEGIVNGTVMGYDPQDYTYLVRFNRNDNAVVLSLPDSQLYSDEETAAVPLSIIMRGNKSSSVISESAKTEKFGNKRYTKELLESVLRVGKLQDVKHKILMDLARMNEDFETFKEIGSSSSRRDAKVTPQRENLQRRYSASMITLHRVNADILEPLRILHDYLVEYQKQDEEEESKRGRPASEVYQKCRMQAEQDLKTAADEKFLKIESDRTQEFVRNLHTILYLNGKLGRENSSNLETIIADLVTHMVDNIQPSLGRKLKDGVDSLEPLRQQVVQIFKDVKKPERFQITQQAPMQTEDGIYNFVVEAQPDTPS
Protein: Uncharacterized protein Rv1109c (P9WM59)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Exodeoxyribonuclease 7 large subunit
- Exodeoxyribonuclease 7 small subunit
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase 2
- Uncharacterized protein Rv2091c
- Conserved protein
- Conserved protein
- Conserved alanine valine rich protein
- Probable conserved transmembrane protein
- Probable conserved transmembrane protein
Sequence:
MATAPYGVRLLVGAATVAVEETMKLPRTILMYPMTLASQAAHVVMRFQQGLAELVIKGDNTLETLFPPKDEKPEWATFDEDLPDALEGTSIPLLGLSDASEAKNDDRRSDGRFALYSVSDTPETTTASRSADRSTNPKTAKHPKSAAKPTVPTPAVAAELDYPALTLAQLRARLHTLDVPELEALLAYEQATKARAPFQTLLANRITRATAK
Protein: Patatin-like phospholipase domain-containing protein 2 (EC 3.1.1.3) (Adipose triglyceride lipase) (Calcium-independent phospholipase A2-zeta) (iPLA2-zeta) (EC 3.1.1.4) (Desnutrin) (Pigment epithelium-derived factor receptor) (PEDF-R) (TTS2.2) (Transport-secretion protein 2) (TTS2) (Q96AD5)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial step in triglyceride hydrolysis in adipocyte and non-adipocyte lipid droplets. Exhibits a strong preference for the hydrolysis of long-chain fatty acid esters at the sn-2 position of the glycerol backbone and acts coordinately with LIPE/HLS and DGAT2 within the lipolytic cascade (By similarity). Also possesses acylglycerol transacylase and phospholipase A2 activities. Transfers fatty acid from triglyceride to retinol, hydrolyzes retinylesters, and generates 1,3-diacylglycerol from triglycerides. Regulates adiposome size and may be involved in the degradation of adiposomes. May play an important role in energy homeostasis (By similarity). May play a role in the response of the organism to starvation, enhancing hydrolysis of triglycerides and providing free fatty acids to other tissues to be oxidized in situations of energy depletion (By similarity).
Subcellular location: Lipid droplet {ECO:0000269|PubMed:16239926, ECO:0000269|PubMed:28578400, ECO:0000269|PubMed:34903883}. Cell membrane {ECO:0000269|PubMed:17032652}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:Q8BJ56}.
Interaction partners:
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Perilipin-5
- Monoglyceride lipase
- Hormone-sensitive lipase
- Lipoprotein lipase
- Pancreatic triacylglycerol lipase
- Hepatic triacylglycerol lipase
- Perilipin-1
- Phospholipid phosphatase 4
- Phospholipid phosphatase 5
Sequence:
MFPREKTWNISFAGCGFLGVYYVGVASCLREHAPFLVANATHIYGASAGALTATALVTGVCLGEAGAKFIEVSKEARKRFLGPLHPSFNLVKIIRSFLLKVLPADSHEHASGRLGISLTRVSDGENVIISHFNSKDELIQANVCSGFIPVYCGLIPPSLQGVRYVDGGISDNLPLYELKNTITVSPFSGESDICPQDSSTNIHELRVTNTSIQFNLRNLYRLSKALFPPEPLVLREMCKQGYRDGLRFLQRNGLLNRPNPLLALPPARPHGPEDKDQAVESAQAEDYSQLPGEDHILEHLPARLNEALLEACVEPTDLLTTLSNMLPVRLATAMMVPYTLPLESALSFTIRLLEWLPDVPEDIRWMKEQTGSICQYLVMRAKRKLGRHLPSRLPEQVELRRVQSLPSVPLSCAAYREALPGWMRNNLSLGDALAKWEECQRQLLLGLFCTNVAFPPEALRMRAPADPAPAPADPASPQHQLAGPAPLLSTPAPEARPVIGALGL
Protein: Transmembrane protein (Q586R6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTGKDGKVLVADLPMMYPKDLLRFEKEGGVWGQQYRVRRQQLTLAVGAAAFSTLLGIGYVRRRRNTGFVVFSTFTGFTVLGFCLGATLSPIIYPNVASNRETSMMRRVWWAKECAKHWDYSQMDGNSWHAAHPHDRLPQQLKGNNEECATA
Protein: RNA-binding protein Hfq (Q9HUM0)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: RNA chaperone that binds small regulatory RNA (sRNAs) and mRNAs to facilitate mRNA translational regulation in response to envelope stress, environmental stress and changes in metabolite concentrations. Also binds with high specificity to tRNAs.
Interaction partners:
- Catabolite repression control protein
- Translational regulator CsrA
- GTPase HflX
- RNA polymerase sigma factor RpoS
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease E
- Transcription termination factor Rho
- Poly
- tRNA dimethylallyltransferase
- Integration host factor subunit alpha
Sequence:
MSKGHSLQDPYLNTLRKERVPVSIYLVNGIKLQGQIESFDQFVILLKNTVSQMVYKHAISTVVPSRPVRLPSGDQPAEPGNA
Protein: YscU (Q56844)
Organism: Yersinia enterocolitica W22703
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MSGEKTEQPTPKKIRDARKKGQVAKSKEVVSTTLIVALSAMLMGLSDYYFEHLSRLMLIPAEQSYLPFSQALSYVVDNVLLEFFYLCFPLLTVAALMAIASHVVQYGFLISGEAIKPDIKKINPIEGAKRIFSIKSLVEFLKSILKVVLLSILIWIIIKGNLVTLLQLPTCGIECITPLLGQILRQLMVICTVGFVVISIADYAFEYYQYIKELKMSKDEIKREYKEMEGSPEIKSKRRQFHQEIQSGNMRENVKRSSVVVANPTHIAIGILYKRGETPLPLVTFKYTDAQVQTVRKIAEEEGVPILQRIPLARALYWDALVDHYIPAEQIEATAEVLRWLERQNIEKQHSEML
Protein: Small aggregate formation protein (P54661)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Knockout of the gene for this protein causes small aggregate formation. May regulate the secretion or processing of a secreted factor that regulates aggregate size.
Subcellular location: Cytoplasm.
Interaction partners:
- Counting factor 45-1
- Suppressor of smlA
Sequence:
MEEIKETVEKKNKEKKYLNDYKIISEGNNIKVLQKKDFKPKFSLVSYKNYEQNFDFENAKIVSTNFAIDRHIKMKNPPDPFVFIKMPSSKLVQSQLKLYYENEGYKDIPVWITPCSAFMRYIKSYPIVGTVTETMEKKKGFTNRFLSTSETKASVSVGFFGCESSMEVTSGYEYEDTVTSEETRSWSQTLNEGSYIVYQNVLVYAYIIYGGSYKPYIDQMNKFNPGLNIKFFREDKCIFFVPINRDDAFTLRYQDNTWDPVEYDVLIDYLGQNQDKWFSGGLP
Protein: Peptidyl-prolyl cis-trans isomerase E (PPIase E) (EC 5.2.1.8) (Cyclophilin 33) (Cyclophilin E) (Rotamase E) (Q9V3G3)
Organism: Drosophila melanogaster (Fruit fly)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Combines RNA-binding and PPIase activities (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor syf1 homolog
- Pre-mRNA-processing factor 19
- RNA helicase aquarius
- Puff-specific protein Bx42
- Pleiotropic regulator 1
- Pre-mRNA-splicing factor SPF27
- Cell division cycle 5, isoform A
- RE31520p
- Protein crooked neck
- Protein BUD31 homolog
Sequence:
MSNDKRTIYVGGLADEVTERLLNNAFIPFGDIADIQMPADYESQRHRGFAFIEYEQSEDAAAAIDNMNDSELCGRTIRVNLAKPVRVKEDSFKPIWADDDWLQKHAGATLQPEGEPEAEKVETPSTGPAVIEKAEKRNPQVFFDIRIGGNDAGRIVMLLRADVVPKTAENFRQLCTHEQGYGYKGCSFHRVIPEFMCQGGDFTNNNGTGGKSIYGKKFNDENFNLKHNSFGTLSMANSGANTNGSQFFICTTKTDWLDNKHVVFGHVISGAEVVRKMERCGSKSGTPSQKIVIYSCGELK
Protein: DNA replication licensing factor MCM6 (EC 3.6.4.12) (Minichromosome maintenance protein 6) (P53091)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Once loaded onto DNA, double hexamers can slide on dsDNA in the absence of ATPase activity. Required for the entry in S phase and for cell division.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA replication complex GINS protein PSF3
- Minichromosome maintenance protein 10
- DNA replication complex GINS protein PSF1
- DNA replication licensing factor MCM2
- Nucleolar complex-associated protein 3
- DNA replication complex GINS protein SLD5
- DDK kinase regulatory subunit DBF4
- Minichromosome maintenance protein 5
- DNA replication licensing factor MCM3
- Topoisomerase 1-associated factor 1
Sequence:
MSSPFPADTPSSNRPSNSSPPPSSIGAGFGSSSGLDSQIGSRLHFPSSSQPHVSNSQTGPFVNDSTQFSSQRLQTDGSATNDMEGNEPARSFKSRALNHVKKVDDVTGEKVREAFEQFLEDFSVQSTDTGEVEKVYRAQIEFMKIYDLNTIYIDYQHLSMRENGALAMAISEQYYRFLPFLQKGLRRVVRKYAPELLNTSDSLKRSEGDEGQADEDEQQDDDMNGSSLPRDSGSSAAPGNGTSAMATRSITTSTSPEQTERVFQISFFNLPTVHRIRDIRSEKIGSLLSISGTVTRTSEVRPELYKASFTCDMCRAIVDNVEQSFKYTEPTFCPNPSCENRAFWTLNVTRSRFLDWQKVRIQENANEIPTGSMPRTLDVILRGDSVERAKPGDRCKFTGVEIVVPDVTQLGLPGVKPSSTLDTRGISKTTEGLNSGVTGLRSLGVRDLTYKISFLACHVISIGSNIGASSPDANSNNRETELQMAANLQANNVYQDNERDQEVFLNSLSSDEINELKEMVKDEHIYDKLVRSIAPAVFGHEAVKKGILLQMLGGVHKSTVEGIKLRGDINICVVGDPSTSKSQFLKYVVGFAPRSVYTSGKASSAAGLTAAVVRDEEGGDYTIEAGALMLADNGICCIDEFDKMDISDQVAIHEAMEQQTISIAKAGIHATLNARTSILAAANPVGGRYNRKLSLRGNLNMTAPIMSRFDLFFVILDDCNEKIDTELASHIVDLHMKRDEAIEPPFSAEQLRRYIKYARTFKPILTKEARSYLVEKYKELRKDDAQGFSRSSYRITVRQLESMIRLSEAIARANCVDEITPSFIAEAYDLLRQSIIRVDVDDVEMDEEFDNIESQSHAASGNNDDNDDGTGSGVITSEPPADIEEGQSEATARPGTSEKKKTTVTYDKYVSMMNMIVRKIAEVDREGAEELTAVDIVDWYLLQKENDLGSLAEYWEERRLAFKVIKRLVKDRILMEIHGTRHNLRDLENEENENNKTVYVIHPNCEVLDQLEPQDSS
Protein: Transcription factor TGA9 (Protein TGACG (TGA) motif-binding protein 9) (bZIP transcription factor 21) (AtbZIP21) (Q93XM6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with TGA10, basic leucine-zipper transcription factor required for anther development, probably via the activation of SPL expression in anthers and via the regulation of genes with functions in early and middle tapetal development. Required for signaling responses to pathogen-associated molecular patterns (PAMPs) such as flg22 that involves chloroplastic reactive oxygen species (ROS) production and subsequent expression of H(2)O(2)-responsive genes.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:20805327}.
Interaction partners:
- Glutaredoxin-C7
- Glutaredoxin-C8
- Regulatory protein NPR1
- Regulatory protein NPR3
- Regulatory protein NPR5
- Basic leucine zipper 8
Sequence:
MANHRMSEATNHNHNHHLPYSLIHGLNNNHPSSGFINQDGSSSFDFGELEEAIVLQGVKYRNEEAKPPLLGGGGGATTLEMFPSWPIRTHQTLPTESSKSGGESSDSGSANFSGKAESQQPESPMSSKHHLMLQPHHNNMANSSSTSGLPSTSRTLAPPKPSEDKRKATTSGKQLDAKTLRRLAQNREAARKSRLRKKAYVQQLESSRIKLSQLEQELQRARSQGLFMGGCGPPGPNITSGAAIFDMEYGRWLEDDNRHMSEIRTGLQAHLSDNDLRLIVDGYIAHFDEIFRLKAVAAKADVFHLIIGTWMSPAERCFIWMAGFRPSDLIKILVSQMDLLTEQQLMGIYSLQHSSQQAEEALSQGLEQLQQSLIDTLAASPVIDGMQQMAVALGKISNLEGFIRQADNLRQQTVHQLRRILTVRQAARCFLVIGEYYGRLRALSSLWLSRPRETLMSDETSCQTTTDLQIVQSSRNHFSNF
Protein: aspartate transaminase (EC 2.6.1.1) (Q8IHB4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VASKFQAKLAKMFIILKRLNYPGLLQNFQLSTMSIYADVPKGPAIEVFALTQAFKDDSNPNKVNLSVGAYRTDAGVPWVLPVVRKTEISIASDEQVNHEYLPVTGLETFTNAATELVLGADSPAIKENRAFGVQTISGTGALRVAADFLHTQLNRNVVYYSNPTWENHHKIFCDAGFTTVKSYRYWDQNKRELDFKNMLADLNDAPPGAVIILHACAHNPTGIDPTQEQWTELADLMEKKKLFPLFDSAYQGFASGDPDRDAWAARYFVQRGFELFICQSFAKNFGLYCERTGNLTVVQKNGATKAAVHSQLTLLIRGQYSNPPAYGARIVSKVLNTPELRKEWMASIQAMSSRIREMRTALRDKLVALGTPGTWDHIVNQIGMFSYTGLNESHVRVLIDQYHIYLLKTGRISMSGLNKGNVEYVAKAIHAAVTGSGESAACPCENKL
Protein: Rhesus-like glycoprotein A (Rh50-like protein rhgA) (Q9NIV0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May be a carbon dioxide/bicarbonate transporter.
Subcellular location: Contractile vacuole {ECO:0000269|PubMed:11220631, ECO:0000269|PubMed:16478785}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MTHNDDDHKWVTTKRKEPIFFTVILFIFQIFMIICFAALTGYDTNKNYTGSENPDEFKGGEVQERVNNFYGYFRDINIMIFFGFGFLMTFLRRYGYSALGYTFIISALVSQWSVLLNGFFEAWSHSNKHGEFPSTWEFSMDSLLQGFFCSGSVMISYGAILGRVTPLHMLIMGIIEPIFFFLNVFIGEMNLEAIDVGGGMYIHLFGSVFGLTVAWFLTDRKSKECTDNAPSYSGDNFAMAGTLFLWMMWPSFNAAIAPLGEPQFRAIANTFLSLTGSTVATFIVSRLFSHLGNKLDMVHVQNSSLAGGVVQGCIAHMNINPGGAIAMGFIAGTISVCGYLFITPKVQRKLHIQDTCGILNLHCIPGFLGSIAAIFAAIKGLNNPNMYSKVEFEQIFRAGDSQASANLIATMVSIGLGIVGGLLVGVILLQLKKIKGLKSKEYYQDSAFWILPIDYPKDVATVVALNNAATSEDTAGGDDEEEGVGKEHGAVEMGKHNRIVQPKQDNKYHKQLPSDDEEEDEFKQEPI
Protein: Rab family GTPase (A0A1D8PTI2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Rab guanine nucleotide exchange factor SEC2
- Phosphatidylinositol 4-kinase PIK1a
- Myosin 2
- Rab GDP dissociation inhibitor
- Exocyst complex component SEC15
- Ras-related protein SEC4
- Rab family GTPase
- Rga2p
- Rcy1p
- Rab proteins geranylgeranyltransferase
Sequence:
MADNSDDYSYDYEYLYKIVLIGDSGVGKSNLLSRFTRDEFNLESRSTIGVEFATRTLEIDGKRVKAQIWDTAGQERYRAITSAYYRGAVGALIVYDIAKTESYESVSRWLKELKEHADANIIIELVGNKSDLDHLRAVPTEEAKNFAMENNLLFTEASALSSDNVDLSFHQLLKNIYEMISKHQLENNDSKQTNTAGGPTISLTPAPQEKKNKNNGXLLLRH
Protein: Transmembrane 9 superfamily member (Q9VIK1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Peptidoglycan-recognition protein LC
Sequence:
MILLSGLLPLLGVVLLHLATPTQAFYLPGLAPVNFCKKTDVSSTCKSEILLYVNRLNTEESVIPYEYHHFDFCLGEEQNSPVENLGQVVFGERIRPGPYKIQFLENQQCATTCVKTYKGDDPASNRRMMVLKKGISLNYQHHWIVDNMPVTWCYPLENGKQYCGIGFPMGCLVRSDGEGCPINSIYNQPMHYYPFNHVDLEITYHSGQSEDWGIQFGNSGRIISVKVTPKSIKHTDKENPNCLSTEPLAISENSLKAGEQLEIVYTYSVKFVKNDSIKWSSRWDYILESMPHTNIQWFSILNSLVIVLFLSGMVAMIMLRTLHKDIARYNQMDSGEDAQEEFGWKLVHGDVFRPPRKGMLLSVFLGSGVQVLVMAMITLAFACLGFLSPANRGALMTCSMVLFVSLGTPAGYVSARIYKSFGGLKWKSNVILTSIVCPGVVFSLFFVMNLVLWGENSSGAVPFSTLIALLALWFGVSVPLTFVGAYFGFRKRALEHPVRTNQIPRQIPDQSIYTQPIPGIVMGGVLPFGCIFIQLFFILSSLWSSQIYYMFGFLFLVFVILVITCSETTILLCYFHLCAEDYHWWWRSFLTSGFTAVYLFIYCCHYFVTKLSIKDSASTFLYFGYTAIMVFLFFLLTGTIGFFACFWFIRKIYSVVKVD
Protein: Ubiquitin-activating enzyme E1 2 (AtUBA2) (EC 6.2.1.45) (P92974)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activates ubiquitin by first adenylating its C-terminal glycine residue with ATP, and thereafter linking this residue to the side chain of a cysteine residue in E1, yielding a ubiquitin-E1 thioester and free AMP.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 7
- Ubiquitin-conjugating enzyme E2 14
- Ubiquitin-conjugating enzyme E2 3
- Ubiquitin-conjugating enzyme E2 27
- E3 ubiquitin-protein ligase UPL3
- SUMO-conjugating enzyme UBC9
- E3 ubiquitin-protein ligase UPL4
- At1g65900/F12P19_7
- Ubiquitin-ribosomal protein eL40y fusion protein
- Ubiquitin-ribosomal protein eL40z fusion protein
Sequence:
MEPFVVKENIIASASSPMKKRRIDHTESADGSAINASNSSSIGLNNSIGGNDTVMSMAEFGNDNSNNQEIDEDLHSRQLAVYGRETMRKLFASNVLISGMQGLGVEIAKNIILAGVKSVTLHDENVVELWDLSSNFVFTEEDIGKNRALASVHKLQELNNAVAVSTLTGKLTKEQLSDFQVVVFVDISFEKATEIDDYCHSHQPPIAFIKADVRGLFGSLFCDFGPHFTVLDVDGEEPHSGIIASVSNENPGFVSCVDDERLEFEDGNLVVFSEVEGMTELNDGKPRKIKNVKPFSFTLEEDTSSYGQYMKGGIVTQVKQPKVLNFKPLREALKDPGDFLLSDFSKFDRPPLLHLAFQALDRFSSQAGRFPFAGSEEDAQKLVEIAVDINEGLGDARLEDVNSKLLRHLAFGSRAVLNPMAAMFGGIVGQEVVKACSGKFHPIFQFFYFDSVESLPKEPLDASEFRPQNSRYDAQISVFGSTLQKKLEDARVFVVGAGALGCEFLKNLALMGVSCGTQGKLTVTDDDVIEKSNLSRQFLFRDWNIGQAKSTVAATAAAGINSRLNIDALQNRVGPETENVFDDSFWENLTVVVNALDNVTARLYVDSRCVYFQKPLLESGTLGAKCNTQMVIPHLTENYGASRDPPEKQAPMCTVHSFPHNIDHCLTWARSEFEGLLEKTPAEVNAYLSDPVEYMKAMRTAGDAQARDTLGRVVECLEKEKCNSFQDCITWARLRFEDYFANRVKQLCYTFPEDAATSTGAPFWSAPKRFPRPLQFSSTDLSHINFVMAASILRAETFGIPTPEWAKTRAGLAEAVERVIVPDFEPKKDATIVTDEKATTLSTASVDDAAVIDELNAKLVRCRMSLQPEFRMKAIQFEKDDDTNYHMDMIAGLANMRARNYSVPEVDKLKAKFIAGRIIPAIATSTAMATGFVCLEMYKVLDGSHKVEDYRNTFANLALPLFSMAEPVPPKVVKHQDQSWTVWDRWVMRGNPTLRELLDWLKEKGLNAYSISCGSSLLYNSMFSRHKERMNRRVVDLARDVAGVELPAYRRHVDVVVACEDDNDADVDIPLVSVYFA
Protein: Nuclear speckle splicing regulatory protein 1 homolog (Coiled-coil domain-containing protein 55 homolog) (Q09252)
Organism: Caenorhabditis elegans
Function: Required for the cessation of distal tip cell migration at the end of larval morphogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22285439}. Nucleus {ECO:0000269|PubMed:22285439}. Note=Predominantly nuclear localization in the distal tip cell. {ECO:0000269|PubMed:22285439}.
Interaction partners:
- E3 ubiquitin ligase rnf-121
- Cell division cycle 5-like protein
- PWI domain-containing protein
- Splicing factor YJU2
- Peptidyl-prolyl cis-trans isomerase sig-7
- Splicing factor Cactin
- UPF3 domain-containing protein
- Peptidyl-prolyl cis-trans isomerase 4
- Pre-mRNA-processing factor 17
- Peptidyl-prolyl cis-trans isomerase 10
Sequence:
MASKRHVGLNIRKKDEPKAAPIRVSSVFGDDDDDDNVPATATNMASASVIRVQKAAEREHQKAEAEDPTIFDYDGNYDEIQAIKNEKKEEARKADKNRESKYAENIIKAHARRQLEQFSREERQQLREREKEGDEFDDKEVFVTGAYRKQQEEVKKHREQEAEEAAFNDMTSVQKQKLWEIGMGRTLLNDLARDPTAIKQRKKEQKNVRKREDSDEEIDPKPEKSDKKPAEKLKKSIYSDDSDEEKAPKPPQKNFEGDLKPGLNTVSKKKATTHAERIRQRNYTPTPPSSDDEGARAPRARRRTSSPSPTSRKSIESRESGSRRSPEGKSEKSEKAPKISLKDKLKPKKIDKEARLDGLKEILKQRNTEEDIEAARQRYFERKEQGIVVPPL
Protein: Dipeptide and tripeptide permease B (P36837)
Organism: Escherichia coli (strain K12)
Function: Proton-dependent permease that transports di- and tripeptides. Has a clear preference for dipeptides and tripeptides composed of L-amino acids, and discriminates dipeptides on the basis of the position of charges within the substrate.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YahM
Sequence:
MNTTTPMGMLQQPRPFFMIFFVELWERFGYYGVQGVLAVFFVKQLGFSQEQAFVTFGAFAALVYGLISIGGYVGDHLLGTKRTIVLGALVLAIGYFMTGMSLLKPDLIFIALGTIAVGNGLFKANPASLLSKCYPPKDPRLDGAFTLFYMSINIGSLIALSLAPVIADRFGYSVTYNLCGAGLIIALLVYIACRGMVKDIGSEPDFRPMSFSKLLYVLLGSVVMIFVCAWLMHNVEVANLVLIVLSIVVTIIFFRQAFKLDKTGRNKMFVAFVLMLEAVVFYILYAQMPTSLNFFAINNVHHEILGFSINPVSFQALNPFWVVLASPILAGIYTHLGNKGKDLSMPMKFTLGMFMCSLGFLTAAAAGMWFADAQGLTSPWFIVLVYLFQSLGELFISALGLAMIAALVPQHLMGFILGMWFLTQAAAFLLGGYVATFTAVPDNITDPLETLPVYTNVFGKIGLVTLGVAVVMLLMVPWLKRMIATPESH
Protein: D(3) dopamine receptor (Dopamine D3 receptor) (P19020)
Organism: Rattus norvegicus (Rat)
Function: Dopamine receptor whose activity is mediated by G proteins which inhibit adenylyl cyclase. Promotes cell proliferation (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- D
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Neurotrophic factor BDNF precursor form
Sequence:
MAPLSQISTHLNSTCGAENSTGVNRARPHAYYALSYCALILAIIFGNGLVCAAVLRERALQTTTNYLVVSLAVADLLVATLVMPWVVYLEVTGGVWNFSRICCDVFVTLDVMMCTASILNLCAISIDRYTAVVMPVHYQHGTGQSSCRRVALMITAVWVLAFAVSCPLLFGFNTTGDPSICSISNPDFVIYSSVVSFYVPFGVTVLVYARIYIVLRQRQRKRILTRQNSQCISIRPGFPQQSSCLRLHPIRQFSIRARFLSDATGQMEHIEDKQYPQKCQDPLLSHLQPPSPGQTHGGLKRYYSICQDTALRHPSLEGGAGMSPVERTRNSLSPTMAPKLSLEVRKLSNGRLSTSLRLGPLQPRGVPLREKKATQMVVIVLGAFIVCWLPFFLTHVLNTHCQACHVSPELYRATTWLGYVNSALNPVIYTTFNVEFRKAFLKILSC