wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphoglycerate kinase (EC 2.7.2.3) (P46273)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9043109}. Secreted, cell wall {ECO:0000269|PubMed:9043109}. Mitochondrion {ECO:0000250|UniProtKB:P00560}.
Interaction partners:
- Phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Fructose-bisphosphate aldolase
- Glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Enolase 1
- Phosphoglycerate mutase
- Pyruvate kinase
- Pyruvate decarboxylase
- mRNA 3'-end-processing protein RNA14
Sequence:
MSLSNKLSVKDLDVAGKRVFIRVDFNVPLDGKTITNNQRIVAALPTIKYVEEHKPKYIVLASHLGRPNGERNDKYSLAPVATELEKLLGQKVTFLNDCVGPEVTKAVENAKDGEIFLLENLRYHIEEEGSSKDKDGKKVKADPEAVKKFRQELTSLADVYINDAFGTAHRAHSSMVGLEVPQRAAGFLMSKELEYFAKALENPERPFLAILGGAKVSDKIQLIDNLLDKVDMLIVGGGMAFTFKKILNKMPIGDSLFDEAGAKNVEHLVEKAKKNNVELILPVDFVTADKFDKDAKTSSATDAEGIPDNWMGLDCGPKSVELFQQAVAKAKTIVWNGPPGVFEFEKFANGTKSLLDAAVKSAENGNIVIIGGGDTATVAKKYGVVEKLSHVSTGGGASLELLEGKDLPGVVALSNKN
Protein: Kainate-type ionotropic glutamate receptor subunit 1D (Q9VDH5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Postsynaptic cell membrane {ECO:0000256|ARBA:ARBA00034100}.
Interaction partners:
- Fife, isoform D
Sequence:
MRSSGVLVLPLLLLQLILNCRKAQSLPDIIKIGGLFHPADDHQELAFRQAVDRINADRSILPRSKLVAQIERISPFDSFHAGKRVCGLLNIGVAAIFGPQSSHTASHVQSICDNMEIPHLENRWDYRLRRESCLVNLYPHPNTLSKAYVDIVRHWGWKTFTIIYENNDGIVRLQELLKAHGMTPFPITVRQLSDSGDYRPLLKQIKNSAEAHIVLDCSTERIHEVLKQAQQIGMMSDYHSYLVTSLDLHTVNLDEFRYGGTNITGFRLINEKIVSDVVRQWSIDEKGLLRSANLTTVRSETALMYDAVHLFAKALHDLDTSQQIDIHPISCDGQSTWQHGFSLINYMKIVEMKGLTNVIKFDHQGFRTDFMLDIVELTPAGIRKIGTWNSTLPDGINFTRTFSQKQQEIEANLKNKTLVVTTILSNPYCMRKESAIPLSGNDQFEGYAVDLIHEISKSLGFNYKIQLVPDGSYGSLNKLTGEWNGMIRELLEQRADLAIADLTITFEREQAVDFTTPFMNLGVSILYRKPIKQPPNLFSFLSPLSLDVWIYMATAYLGVSVLLFILAKFTPYEWPAYTDAHGEKVESQFTLLNCMWFAIGSLMQQGCDFLPKALSTRMVAGIWWFFTLIMISSYTANLAAFLTVERMDSPIESAEDLAKQTRIKYGALKGGSTAAFFRDSKISTYQRMWSFMESARPSVFTASNGEGVERVAKGKGSYAFLMESTSIEYVTERNCELTQVGGMLDTKSYGIATPPNSPYRTAINSVILKLQEEGKLHILKTKWWKEKRGGGKCRVETSKSSSAANELGLANVGGVFVVLMGGMGVACVIAVCEFVWKSRKVAVEERLSAILNE
Protein: Indole-3-acetaldehyde oxidase (IAA oxidase) (EC 1.2.3.7) (Aldehyde oxidase 2) (AO-2) (AtAO-2) (AtAO3) (Q7G192)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In higher plant aldehyde oxidases (AO) appear to be homo- and heterodimeric assemblies of AO subunits with probably different physiological functions. In vitro, AO-gamma uses heptaldehyde, benzaldehyde, naphthaldehyde and cinnamaldehyde as substrates; AO-beta uses indole-3-acetaldehyde (IAAld), indole-3-aldehyde (IAld) and naphtaldehyde; the AAO2-AAO3 dimer uses abscisic aldehyde.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Nitrilase 2
- Nitrilase 3
- Nitrilase 1
- Aldehyde dehydrogenase family 2 member B7, mitochondrial
- Aldehyde dehydrogenase family 3 member H1
- Aldehyde dehydrogenase family 3 member F1
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- Aldehyde dehydrogenase family 7 member B4
- Aldehyde oxidase 4
Sequence:
MSLVFAINGQRFELELSSVDPSTTLLEFLRYQTSFKSVKLSCGEGGCGACVVLLSKFDPVLQKVEDFTVSSCLTLLCSVNHCNITTSEGLGNSRDGFHPIHKRLSGFHASQCGFCTPGMSVSLFSALLDADKSQYSDLTVVEAEKAVSGNLCRCTGYRPIVDACKSFASDVDIEDLGLNSFCRKGDKDSSSLTRFDSEKRICTFPEFLKDEIKSVDSGMYRWCSPASVEELSSLLEACKANSNTVSMKLVAGNTSMGYYKDEREQNYDKYIDITRIPHLKEIRENQNGVEIGSVVTISKVIAALKEIRVSPGVEKIFGKLATHMEMIAARFIRNFGSIGGNLVMAQRKQFPSDMATILLAAGAFVNIMSSSRGLEKLTLEEFLERSPLEAHDLVLSIEIPFWHSETNSELFFETYRAAPRPHGSALAYLNAAFLAEVKDTMVVNCRLAFGAYGTKHAIRCKEIEEFLSGKVITDKVLYEAITLLGNVVVPEDGTSNPAYRSSLAPGFLFKFLHTLMTHPTTDKPSNGYHLDPPKPLPMLSSSQNVPINNEYNPVGQPVTKVGASLQASGEAVYVDDIPSPTNCLYGAFIYSKKPFARIKGIHFKDDLVPTGVVAVISRKDVPKGGKNIGMKIGLGSDQLFAEDFTTSVGECIAFVVADTQRHADAAVNLAVVEYETEDLEPPILSVEDAVKKSSLFDIIPFLYPQQVGDTSKGMAEADHQILSSEIRLGSQYVFYMETQTALAVGDEDNCIVVYSSTQTPQYVQSSVAACLGIPENNIRVITRRVGGGFGGKSVKSMPVATACALAAKKLQRPVRTYVNRKTDMIMTGGRHPMKITYSVGFKSTGKITALELEILIDAGASYGFSMFIPSNLIGSLKKYNWGALSFDIKLCKTNLLSRAIMRSPGDVQGTYIAEAIIENIASSLSLEVDTIRKINLHTHESLALFYKDGAGEPHEYTLSSMWDKVGVSSKFEERVSVVREFNESNMWRKRGISRVPIIYEVLLFATPGRVSVLSDGTIVVEIGGIELGQGLWTKVKQMTSYALGMLQCDGTEELLEKIRVIQSDSLSMVQGNFTGGSTTSEGSCAAVRLCCETLVERLKPLMERSDGPITWNELISQAYAQSVNLSASDLYTPKDTPMQYLNYGTAVSEVEVDLVTGQTTVLQTDILYDCGKSLNPAVDLGQIEGSFVQGLGFFMLEEYIEDPEGLLLTDSTWTYKIPTVDTIPKQFNVEILNGGCHEKRVLSSKASGEPPLLLAASVHCATRQAVKEARKQLCMWKGENGSSGSAFQLPVPATMPVVKELCGLDIIESYLEWKLHDNSNL
Protein: alcohol dehydrogenase (EC 1.1.1.1) (Q4WTV5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
- Pyruvate decarboxylase
- Pyruvate decarboxylase
- Pyruvate decarboxylase
- Amine oxidase
- catechol O-methyltransferase
- catechol O-methyltransferase
- O-methyltransferase, putative
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- aldehyde dehydrogenase
Sequence:
MTIPDKQWAQVVLEKGSPPVYKEIPVPKPGPDDILVKLRYSGVCHTDLHAMKGDWPLALKLPLVGGHEGVGVVVAKGELVTGFEIGDHAGIKWLNGSCMECEFCKQSEEPLCPRATMSGYTVDGTFQQYCVAKATHASKIPNGVPLDAAAPILCAGLTVYKGLKESGARPGQTVAIVGAGGGLGSLAQQYAKAMGLRVVAIDGGDEKREMCEKLGAEAYIDFTKSTNVVEDVKAATPGGLGAHAVLLLAVSEKPFQQATDYVRSRGTIVAIGMPAGAYLKAPVFNTVVKMITIKGSYVGNRQDGVEAIDFFARGLINAPFKKAPLKDLPRIFELMEQGKVAGRYVLEIPE
Protein: cAMP responsive element binding protein 1 (C9JBT4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYTASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARK
Protein: Hemopexin (Q91X72)
Organism: Mus musculus (Mouse)
Function: Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation.
Subcellular location: Secreted.
Interaction partners:
- Prolow-density lipoprotein receptor-related protein 1
- Albumin
- Haptoglobin
- Protein AMBP
- Alpha-2-HS-glycoprotein
- Metalloproteinase inhibitor 2
- Scavenger receptor cysteine-rich type 1 protein M130
- Choline/ethanolamine transporter FLVCR1
- Fibrinogen gamma chain
- Plasminogen
Sequence:
MARTAVALNILVLLGLCWSLAVASPLPTANGRVAEVENGTKPDSDVPEHCLDTWSFDAATMDHNGTMLFFKGEFVWRGHSGTRELISARWKNPITSVDAAFRGPDSVFLIKEDKVWVYPPEKKENGYPKLFQEEFPGIPYPPDAAVECHRGECQSEGVLFFQGNRKWFWDFATRTQKERSWSTVGNCTAALRWLERYYCFQGNKFLRFNPVTGEVPPRYPLDARDYFVSCPGRGHGRPRNGTAHGNSTHPMHSRCSPDPGLTALLSDHRGATYAFTGSHYWRLDSSRDGWHSWPIAHHWPQGPSTVDAAFSWDDKVYLIQGTQVYVFLTKGGNNLVSGYPKRLEKELGSPPGISLETIDAAFSCPGSSRLYVSSGRRLWWLDLKSGAQATWTEVSWPHEKVDGALCLDKSLGPNTCSSNGSSLYFIHGPNLYCYSSIDKLNAAKSLPQPQKVNSILGCSQ
Protein: receptor protein serine/threonine kinase (EC 2.7.11.30) (Q7JQ36)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MESNIYLVFLLTFLLYNNARAEISDHLREDIPDLDMELSSASSAHLNGKELPAVPQNSVQTHPRYKCYSCEPPCRDPYEFTHTCQNAIQCWKSRTRDADGQVQESRGCSTSPDQLPMICSQNSLKINGPSKRNTGKFVNVVCCAGDYCNEGDFPELLPFDSNDVTVITADTSSISKMLVAVLGPFLVIALLGAVTIFFIRRSHRKRLAASRTKQDPEAYLVNDELLRATSAGDSTLREYLQHSVTSGSGSGLPLLVQRTLAKQVTLIECIGRGKYGEVWRGHWHGESIAVKIFFSRDEESWKRETEIYSTILLRHENILGFIGSDMTSRNSCTQLWLMTHYYPLGSLFDHLNRNALSHNDMVWICLSIANGLVHLHTEIFGKQGKPAMAHRDLKSKNILVTSNGSCVIADFGLAVTHSHVTGQLDLGNNPKVGTKRYMAPEVLDESIDLECFEALRRTDIYAFGLVLWEVCRRTISCGIAEEYKVPFYDVVPMDPSFEDMRKVVCIDNYRPSIPNRWSSDSLMTGMSKLMKECWHQNPDVRLPALRIKKTIHKLASADEKIRLDFDEVCV
Protein: Large ribosomal subunit protein mL102 (rPPR5) (Pentatricopeptide repeat-containing protein At2g37230) (Q9ZUU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000303|PubMed:36423343}.
Interaction partners:
- Ankyrin repeat family protein
- Valine--tRNA ligase, mitochondrial 1
Sequence:
MAFISRSKRYQSKARVYLSLPRSSNSSLFSLPRLFSTIEETQTPANANPETQSPDAKSETKKNLTSTETRPLRERFQRGKRQNHEKLEDTICRMMDNRAWTTRLQNSIRDLVPEWDHSLVYNVLHGAKKLEHALQFFRWTERSGLIRHDRDTHMKMIKMLGEVSKLNHARCILLDMPEKGVPWDEDMFVVLIESYGKAGIVQESVKIFQKMKDLGVERTIKSYNSLFKVILRRGRYMMAKRYFNKMVSEGVEPTRHTYNLMLWGFFLSLRLETALRFFEDMKTRGISPDDATFNTMINGFCRFKKMDEAEKLFVEMKGNKIGPSVVSYTTMIKGYLAVDRVDDGLRIFEEMRSSGIEPNATTYSTLLPGLCDAGKMVEAKNILKNMMAKHIAPKDNSIFLKLLVSQSKAGDMAAATEVLKAMATLNVPAEAGHYGVLIENQCKASAYNRAIKLLDTLIEKEIILRHQDTLEMEPSAYNPIIEYLCNNGQTAKAEVLFRQLMKRGVQDQDALNNLIRGHAKEGNPDSSYEILKIMSRRGVPRESNAYELLIKSYMSKGEPGDAKTALDSMVEDGHVPDSSLFRSVIESLFEDGRVQTASRVMMIMIDKNVGIEDNMDLIAKILEALLMRGHVEEALGRIDLLNQNGHTADLDSLLSVLSEKGKTIAALKLLDFGLERDLSLEFSSYDKVLDALLGAGKTLNAYSVLCKIMEKGSSTDWKSSDELIKSLNQEGNTKQADVLSRMIKKGQGIKKQNNVSL
Protein: BEL1-like homeodomain protein 3 (BEL1-like protein 3) (Q9FWS9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that is responsive of the nuclear import of SHOOT MERISTEMLESS (STM).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription repressor OFP1
- At2g01260
- Transcription repressor OFP5
- Transcription repressor OFP4
- Transcription repressor OFP2
- Protein KNATM
Sequence:
MAVYYPNSVGMQSLYQESIYLNEQQQQQQQASSSSAASFSEIVSGDVRNNEMVFIPPTSDVAVNGNVTVSSNDLSFHGGGLSLSLGNQIQSAVSVSPFQYHYQNLSNQLSYNNLNPSTMSDENGKSLSVHQHHSDQILPSSVYNNNGNNGVGFYNNYRYETSGFVSSVLRSRYLKPTQQLLDEVVSVRKDLKLGNKKMKNDKGQDFHNGSSDNITEDDKSQSQELSPSERQELQSKKSKLLTMVDEVDKRYNQYHHQMEALASSFEMVTGLGAAKPYTSVALNRISRHFRCLRDAIKEQIQVIRGKLGERETSDEQGERIPRLRYLDQRLRQQRALHQQLGMVRPAWRPQRGLPENSVSILRAWLFEHFLHPYPKESEKIMLSKQTGLSKNQVANWFINARVRLWKPMIEEMYKEEFGESAELLSNSNQDTKKMQETSQLKHEDSSSSQQQNQGNNNNNIPYTSDAEQNLVFADPKPDRATTGDYDSLMNYHGFGIDDYNRYVGLGNQQDGRYSNPHQLHDFVV
Protein: Poly(A) polymerase (PAP) (EC 2.7.7.19) (Polynucleotide adenylyltransferase) (P29468)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Polymerase component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB.
Subcellular location: Nucleus {ECO:0000269|PubMed:12819204, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Pre-mRNA polyadenylation factor FIP1
- Cleavage factor two protein 2
- Endoribonuclease YSH1
- RNA end formation protein 2
- Protein CFT1
- mRNA 3'-end-processing protein RNA14
- Serine/threonine-protein phosphatase PP1-2
- mRNA 3'-end-processing protein YTH1
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Polyadenylation factor subunit 2
Sequence:
MSSQKVFGITGPVSTVGATAAENKLNDSLIQELKKEGSFETEQETANRVQVLKILQELAQRFVYEVSKKKNMSDGMARDAGGKIFTYGSYRLGVHGPGSDIDTLVVVPKHVTREDFFTVFDSLLRERKELDEIAPVPDAFVPIIKIKFSGISIDLICARLDQPQVPLSLTLSDKNLLRNLDEKDLRALNGTRVTDEILELVPKPNVFRIALRAIKLWAQRRAVYANIFGFPGGVAWAMLVARICQLYPNACSAVILNRFFIILSEWNWPQPVILKPIEDGPLQVRVWNPKIYAQDRSHRMPVITPAYPSMCATHNITESTKKVILQEFVRGVQITNDIFSNKKSWANLFEKNDFFFRYKFYLEITAYTRGSDEQHLKWSGLVESKVRLLVMKLEVLAGIKIAHPFTKPFESSYCCPTEDDYEMIQDKYGSHKTETALNALKLVTDENKEEESIKDAPKAYLSTMYIGLDFNIENKKEKVDIHIPCTEFVNLCRSFNEDYGDHKVFNLALRFVKGYDLPDEVFDENEKRPSKKSKRKNLDARHETVKRSKSDAASGDNINGTTAAVDVN
Protein: M95 protein (H2A1V9)
Organism: Murid herpesvirus 1 (MuHV-1) (Mouse cytomegalovirus)
Interaction partners:
Sequence:
MATAAGGVYAGGEDQQQQQRPRATDVSTALCDVEALAAVEEGRVSEADVNRYREAVDAALIACEASSPRDRFRLIETAGGNFLLVTNALPKDRTEQQPPCVLEGSGRASSSNNNYEGIGTPSAGSGNAFDGLLALERGTSGGGLTATVPSAPGYVAKSVNTLSYDGRLLSNSYVLYTKEQLRKSLSPDKRAIVERILRFVDTPGILDHNNVQDVEAVLWLLFCGPQSVCQNPTCFGRDRECEVSYPVLLPPVFYDPITDYSAYINLAELYVYVWYRNYDFDSEPTRCYELGTVAMDRVKKTLQSVRQRFSDRSVPVWPVSSRTCVFCALYNQNRVCLDLAKSDVDVTSYSPIIIKDCRDAATNVTLSHVLPGQRVASLFPVYDIGTLLRALCDSNDGEERRKRMRETIDSALSTTDDAV
Protein: Putative FBD-associated F-box protein At3g60710 (Q9LZZ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MEDLISQLPNELLQEILLNLPTSESVRTSVLPTRWRNLWQSVPGLYLISRQILKFVNLRTPSDVVLEMLISCSPVLQVLSICDVGVDFLKVRSQTLRSLSLWTFIFKGENDDVSLGDDGESGLVIDTPSLEFLRIRDFPLEDFRVESVISSIKMCIDGTYAYTKLQQLPEFKNLTRLYAFLHTDYSEMLPIYLSSSPNLKSIDLELHGYPKMEEIASSPVPKCLQTSIENVKIKMTPKADQEKSRKAETEVANYILENATLLKLTLWLDDEEEDESSSVLEKILTFQNYSFVEVKIGREASKFRLGYTFDEAKHFSRRFL
Protein: Scinderin (Adseverin) (Q9Y6U3)
Organism: Homo sapiens (Human)
Function: Ca(2+)-dependent actin filament-severing protein that has a regulatory function in exocytosis by affecting the organization of the microfilament network underneath the plasma membrane. Severing activity is inhibited by phosphatidylinositol 4,5-bis-phosphate (PIP2) (By similarity). In vitro, also has barbed end capping and nucleating activities in the presence of Ca(2+). Required for megakaryocyte differentiation, maturation, polyploidization and apoptosis with the release of platelet-like particles. Plays a role in osteoclastogenesis (OCG) and actin cytoskeletal organization in osteoclasts (By similarity). Regulates chondrocyte proliferation and differentiation (By similarity). Inhibits cell proliferation and tumorigenesis. Signaling is mediated by MAPK, p38 and JNK pathways.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, podosome {ECO:0000250|UniProtKB:Q60604}.
Interaction partners:
- Hematopoietic lineage cell-specific protein
- Src substrate cortactin
- Talin-1
- Actin nucleation-promoting factor WASL
- Talin-2
- Phosphatidylinositol 4-phosphate 5-kinase type-1 gamma
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
Sequence:
MARELYHEEFARAGKQAGLQVWRIEKLELVPVPQSAHGDFYVGDAYLVLHTAKTSRGFTYHLHFWLGKECSQDESTAAAIFTVQMDDYLGGKPVQNRELQGYESNDFVSYFKGGLKYKAGGVASGLNHVLTNDLTAKRLLHVKGRRVVRATEVPLSWDSFNKGDCFIIDLGTEIYQWCGSSCNKYERLKANQVATGIRYNERKGRSELIVVEEGSEPSELIKVLGEKPELPDGGDDDDIIADISNRKMAKLYMVSDASGSMRVTVVAEENPFSMAMLLSEECFILDHGAAKQIFVWKGKDANPQERKAAMKTAEEFLQQMNYSKNTQIQVLPEGGETPIFKQFFKDWRDKDQSDGFGKVYVTEKVAQIKQIPFDASKLHSSPQMAAQHNMVDDGSGKVEIWRVENNGRIQVDQNSYGEFYGGDCYIILYTYPRGQIIYTWQGANATRDELTTSAFLTVQLDRSLGGQAVQIRVSQGKEPVHLLSLFKDKPLIIYKNGTSKKGGQAPAPPTRLFQVRRNLASITRIVEVDVDANSLNSNDVFVLKLPQNSGYIWVGKGASQEEEKGAEYVASVLKCKTLRIQEGEEPEEFWNSLGGKKDYQTSPLLETQAEDHPPRLYGCSNKTGRFVIEEIPGEFTQDDLAEDDVMLLDAWEQIFIWIGKDANEVEKKESLKSAKMYLETDPSGRDKRTPIVIIKQGHEPPTFTGWFLGWDSSKW
Protein: Sorting nexin-3 (Golgi retention deficient protein 19) (Q08826)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for retention of late Golgi membrane proteins. Component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment. Binds phosphatidylinositol 3-phosphate (PtdIns(P3)).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9456318}. Golgi apparatus membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Prevacuolar compartment membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Mainly cytoplasmic. A minor amount associates with membranes.
Interaction partners:
- Vacuolar protein sorting-associated protein 35
- Carboxypeptidase Y-deficient protein 8
- Vacuolar protein sorting-associated protein 5
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 27
- Vacuolar protein sorting-associated protein 17
- Sorting nexin-4
- Vacuolar protein sorting/targeting protein VPS10
- Sorting nexin MVP1
- Plasma membrane iron permease
Sequence:
MPREFKSFGSTEKSLLSKGHGEPSYSEIYAEPENFLEIEVHNPKTHIPNGMDSKGMFTDYEIICRTNLPSFHKRVSKVRRRYSDFEFFRKCLIKEISMLNHPKVMVPHLPGKILLSNRFSNEVIEERRQGLNTWMQSVAGHPLLQSGSKVLVRFIEAEKFVG
Protein: Capsid polyprotein VP90 [Cleaved into: Capsid polyprotein VP70; Core protein VP34; Spike protein VP27; Spike protein VP25] (O12792)
Organism: Human astrovirus-1 (HAstV-1)
Function: The capsid polyprotein VP90 self-assembles and undergoes a proteolytic cleavage by host caspases to yield the VP70 virions. This immature virion is composed of 180 VP70 subunits with 90 dimeric spikes and displays a T=3 icosahedral symmetry. The mature virion is obtained by further cleavages resulting in three structural proteins VP25, VP27 and VP34. This forms contains only 30 spikes located on the icosahedral 2-fold axes. Plays a role in the attachment to target host cell. This attachment induces virion internalization through clathrin-dependent endocytosis (By similarity).
Subcellular location: [Capsid polyprotein VP90]: Virion {ECO:0000250|UniProtKB:Q9IFX1}. Note=Immature capsid. {ECO:0000250|UniProtKB:Q9IFX1}.; SUBCELLULAR LOCATION: [Capsid polyprotein VP70]: Virion {ECO:0000250|UniProtKB:Q9IFX1}. Note=Immature capsid after cleavage by host caspases. {ECO:0000250|UniProtKB:Q9IFX1}.; SUBCELLULAR LOCATION: [Core protein VP34]: Virion {ECO:0000269|PubMed:26656707}. Note=Capsid. {ECO:0000269|PubMed:26656707}.; SUBCELLULAR LOCATION: [Spike protein VP27]: Virion {ECO:0000269|PubMed:26656707}. Note=Capsid. {ECO:0000269|PubMed:26656707}.; SUBCELLULAR LOCATION: [Spike protein VP25]: Host extracellular space {ECO:0000305|PubMed:26656707}. Virion. Note=Capsid (PubMed:26656707). Spike protein VP25 that lacks the core attachment region may need to dimerize with spike protein VP27 to remain stably bound to the viral particle (Probable). {ECO:0000269|PubMed:26656707, ECO:0000305}.
Interaction partners:
Sequence:
MASKSNKQVTVEVSNNGRSRSKSRARSQSRGRDKSVKITVNSRNRARRQPGRDKRQSSQRVRNIVNKQLRKQGVTGPKPAICQRATATLGTVGSNTSGTTEIEACILLNPVLVKDATGSTQFGPVQALGAQYSMWKLKYLNVKLTSMVGASAVNGTVSGVSLNPTTTPTSTSWSGLGARKHLDVTVGKNATFKLKPSDLGGPRDGWWLTNTNDNASDTLGPSIEIHTLGRTMSSYKNEQFTGGLFLVELASEWCFTGYAANPNLVNLVKSTDNQVSVTFEGSAGSPLIMNVPEGSHFARTVLARSTTPTTLARAGERTTSDTVWQVLNTAVSAAELVTPPPFNWLVKGGWWFVKLIAGRTRTGSRSFYVYPSYQDALSNKPALCTGSTPGGMRTRNPVTTTLQFTQMNQPSLGHGEAPAAFGRSIPAPGEEFKVVLTFGAPMSPNANNKQTWVNKPLDAPSGHYNVKIAKDVDHYLTMQGFTSIASVDWYTIDFQPSEAPAPIQGLQVLVNSSKKADVYAIKQFVTAQTNNKHQVTSLFLVKVTTGFQVNNYLSYFYRASATGDATTNLLVRGDTYTAGISFTQGGWYLLTNTSIVDGAMPPGWVWNNVELKTNTAYHMDKGLVHLIMPLPESTQMCYEMLTSIPRSRASGHGYESDNTEYLDAPDSADQFKEDIETDTDIESTEDEDEADRFDIIDTSDEEDENETDRVTLLSTLVNQGMTMTRATRIARRAFPTLSDRIKRGVYMDLLVSGASPGNAWSHACEEARKAAGEINPCTSGSRGHAE
Protein: Unconventional myosin class XV (Q8T6M1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDWAEGDLVWFDPGMGHPIPGEIQEVHRAAQVIVVQALIKGKPQTFALQPGEGSLRARQDLGSSGVEDMTLLDDLHEASLLWNLRLRYDKGLIYTFAGSILIAVNPYKM
Protein: GTX/Nkx6B-like homeodomain protein (HGTX, isoform A) (IP01125p) (RE53769p) (Q9NHP8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108, ECO:0000256|RuleBase:RU000682}.
Interaction partners:
- Lim3, isoform G
- GH17679p
Sequence:
MDLINPYMRHHSFAAAAQGSPPSAAQRHHLAAAMSNGFADVHAHAMAAADYQQQLADYHSAAAAAAVYANNNNNNNNNSSNNNNSSPLMLLKAAHGGGLKDSDSPSTTPPPASSRLHSDSSPSPRYEHNSSPGVDSAKSYALSQRSSGAEDPCQTSESASPPPQGQNDYSPENLSSQRAKFQHHHGVNPLALHNANHAGNPGCHNNNNHMDHKLPLSFLGPPLAALHSMTTEMKGQGVGGSSASANGLSYSHSPNSHLISDRGSGGSSSSSSTTTTNTNSQGAPNPHGIDTILSKPPPVTSAGLSALTGAGIPRFSIAAAAAGMAQYLSQSQGAPLKTHAGHIVDRTHLYWPGLQGLVANPIAWRERLSNTMSANLSQSHQHHPSNDKDGKKKHTRPTFSGQQIFALEKTFEQTKYLAGPERAKLAYALGMSESQVKVWFQNRRTKWRKRHAAEMATAKRKQDDMGGDNDGDCSETMDSDNESLDMGESPAQNKRCRSNSSGSSQQQQDNYRH
Protein: Dopamine receptor 4 (Q18775)
Organism: Caenorhabditis elegans
Function: Receptor for dopamine. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. In terms of antagonist responses, would be classed with the D1-like dopamine receptor group.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Dopamine receptor 3
- Dopamine receptor 2
- Aromatic-L-amino-acid decarboxylase
Sequence:
MLAYGSDPNAEDLYITMTPSVSTENDTTVWATEEPAAIVWRHPLLAIALFSICLLTVAGNCLVVIAVCTKKYLRNPTGYLIISLAIADLIVGVIVMPMNSLFEIANHTWLFGLMMCDVFHAMDILASTASIWNLCVISLDRYMAGQDPIGYRDKVSKRRILMAILSVWVLSAILSFPGIIWWRTSSPHLYEDQSQCLFTDSKMYVSFSSLVSFYIPLFLILFAYGKVYIIATRHSKGMRMGIKTVSIKKRNGKKSNTETESILSSENEPTLRIHFGRGKQSSSSLRNSRFHARESTRLLLKQVSCKSLNDRGEHNNNNTVRQPLLRGTEGCHSDSISRSSQRNFRGRNVTIGSNCSSTLLQVDQPDRMSLSSNSQMVMTSPLSTRRKLNVREKSRQMMRYVHEQRAARTLSIVVGAFILCWTPFFVFTPLTAFCESCFSNKETIFTFVTWAGHLNSMLNPLIYSRFSRDFRRAFKQILTCQRQQKVKTAFKTPLSLVFTQLISVTQMWEQPPNTSIE
Protein: Protein VASCULATURE COMPLEXITY AND CONNECTIVITY (Protein DESIGUAL 1) (Q9ZV57)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required, together with OPS, for embryo provasculature development and cotyledon vascular complexity and connectivity. Necessary, partially redundantly with DEAL2 and DEAL3, to ensure bilateral symmetry development and early leaf margin patterning, probably via the regulation of auxin and CUC2 distribution. Regulates cell proliferation but not cell expansion.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:29139551}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein CUP-SHAPED COTYLEDON 2
Sequence:
MTKIGGILVCLVIVGLDVAAAILGIQAEVAQNQVKHMRLWLFECREPSQDAFRLGLGAAAILVMAHVLLNLVGGCLCICSQDEFQRSSSTRQISMACLVLTWIVFAVGFGSIVIGTMSNSKSRSSCGFTHHHFLSIGGILCFLHALFCVAYYVSATAAKDEAK
Protein: Glutathione S-transferase U6 (AtGSTU6) (EC 2.5.1.18) (GST class-tau member 6) (Glutathione S-transferase 24) (Q9ZW26)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase DHAR3, chloroplastic
- Glutathione S-transferase DHAR2
- Glutathione synthetase, chloroplastic
Sequence:
MGKNEEVKLLGIWASPFSRRIEMALKLKGVPYEYLEEDLENKSSLLLALSPIHKKIPVLVHNGKTIIESHVILEYIDETWKHNPILPQDPFQRSKARVLAKLVDEKIVNVGFASLAKTEKGREVLIEQTRELIMCLEKELAGKDYFGGKTVGFLDFVAGSMIPFCLERAWEGMGVEMITEKKFPEYNKWVKKLKEVEIVVDCIPLREKHIEHMNNMAEKIRSA
Protein: Variant surface glycoprotein (VSG)-related, putative (Q586J1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MKATGCWVPLVVTVIGQLSCVVGAREPLVNEQEFGALCAMINFSQDLETQQLEESVKDSARHIGAIGLAVGLQSLSEAEDVENVQVGRQGEGGGGGGYWSFWEEAGTKLKGDKTRYIQWVEANFDILRKEKIKEAVENAHTCMKTNNNLWLELKMSPINKSLSDALSGSNKADVMIKQHLEAVEVCGGKGGQPSVWAGKSLIVDLLCICGGSPMPNDRQQACCEGCSTGANEDPWKPVEQSNTRWKHLAQRCKSIGTNEKLSSSSLSRATKVFLEVLKRSTAQKEGTKTFLGAASGEPQHGCTGHTQPGNGKCVQYPTEMVGNENPAVPWLLVLQQAATRIDKLREIEKKLKDILRNVESIKTSKLSQMPRSGISQLKDGTTCNKGRGQKGPSSGVECSECESQAECTHTGCNKREGNCIDIKRPPLASQADKISVPLWLFFLP