wanglab/gogpt-training-data huggingface dataset:
Protein: Rab effector MyRIP (Exophilin-8) (Myosin-VIIa- and Rab-interacting protein) (Synaptotagmin-like protein lacking C2 domains C) (SlaC2-c) (Slp homolog lacking C2 domains c) (Q8NFW9)
Organism: Homo sapiens (Human)
Function: Rab effector protein involved in melanosome transport. Serves as link between melanosome-bound RAB27A and the motor proteins MYO5A and MYO7A. May link RAB27A-containing vesicles to actin filaments. Functions as a protein kinase A-anchoring protein (AKAP). May act as a scaffolding protein that links PKA to components of the exocytosis machinery, thus facilitating exocytosis, including insulin release (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8K3I4}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q7TNY7}. Cytoplasmic vesicle, secretory vesicle {ECO:0000250|UniProtKB:Q7TNY7}. Note=In presynaptic and postsynaptic areas in photoreceptor cells and in the basal microvilli of retinal pigment epithelium cells. Associated with melanosomes. Colocalizes with actin filaments. {ECO:0000250|UniProtKB:Q7TNY7}.
Interaction partners:
- Ras-related protein Rab-27A
- Unconventional myosin-Va
- Unconventional myosin-VIIa
- Ras-related protein Rab-27B
- Exocyst complex component 3
- Exocyst complex component 4
- Synaptotagmin-like protein 1
Sequence:
MGRKLDLSGLTDDETEHVLQVVQRDFNLRKKEEERLSELKQKLDEEGSKCSILSKHQQFVEHCCMRCCSPFTFLVNTKRQCGDCKFNVCKSCCSYQKHEKAWVCCVCQQARLLRAQSLEWFYNNVKSRFKRFGSAKVLKNLYRKHRLESGACFDILGGSLFESNLENEGSISGSDSTFYRQSEGHSVMDTLAVALRVAEEAIEEAISKAEAYGDSLDKQNEASYLRDHKEELTEELATTILQKIIRKQKSKSEQQVEEEPGWPHPQSCSTKVADEGTSASPGGYRAPAALWRSQSAFSITGEEALKTPPVEAPSRQPRDQGQHPRAESALPSWKSVDRLDETNLAPVLQSPDGNWVALKDGAPPPTRLLAKPKSGTFQALEVASSVASAYDEMGSDSEEDFDWSEALSKLCPRSRALPRNPQPQPTQAQSSDQGPIAASPSSALSPNPEAMCSDSETSSAGSSREVGHQARLSWLQRKAPRNPAAEKMRLHGELDVNFNPQLASRETSDSSEPEEAPHTTDRRARRWRRARLGSEEPSKEPSSPSAQLRDLDTHQVSDDLSETDISNEARDPQTLTDTTEEKRRNRLYELAMKMSEKETSSGEDQESEPKTESENQKESLSSEDNSQSVQEELKKKFSAVSLCNISTEVLKVINATEELIAGSTGPWESPQVPPDRQKGMFPRGTDQVRLDEQLTSLEENVYLAAGTVYGLETQLTELEDAARCIHSGTDETHLADLEDQVATAAAQVHHAELQISDIESRISALTIAGLNIAPCVRFTRRRDQKQRTQVQTIDTSRQQRRKLPAPPVKAEKIETSSVTTIKTFNHNFILQGSSTNRTKERKGTTKDLMEPALESAVMY
Protein: Trypsin theta (EC 3.4.21.4) (P42278)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted, extracellular space.
Interaction partners:
- Uncharacterized protein, isoform A
- Zinc carboxypeptidase A 1
- Retinoid-inducible serine carboxypeptidase
- Bazooka, isoform B
- GH20109p
- RE65433p
- FI02848p
- Serine protease 3
- Jonah 99Fii
- Jonah 25Biii
Sequence:
MHRLVVLLVCLAVGSACAGTVGVSNGDPFEREGRIVGGEDTTIGAHPYQVSLQTKSGSHFCGGSLINEDTVVTAAHCLVGRKVSKVFVRLGSTLYNEGGIVVAVRELAYNEDYNSKTMEYDVGILKLDEKVKETENIRYIELATETPPTGTTAVVTGWGSKCYFWCMTLPKTLQEVYVNIVDWKTCASDEYKYGEIIYDSMVCAYEKKKDACQGDSGGPLAVGNTLVGIVSWGYACASNLLPGVYSDVPALRKWILNASETL
Protein: C9orf72-SMCR8 complex subunit (A0A2R8Y5K2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTLCPPPSPAVAKTEIALSGKSPLLAATFAYWDNILGPRVRHIWAPKTEQVLLSDGEITFLANHTLNGEILRNAESGAIDVKFFVLSEKGVIIVSLIFDGNWNGDRSTYGLSIILPQTELSFYLPLHRVCVDRLTHIIRKGRIWMHKERQENVQKIILEGTERMEDQGQSIIPMLTGEVIPVMELLSSMKSHSVPEEIDIADTVLNDDDIGDSCHEGFLLNAISSHLQTCGCSVVVGSSAEKVNKIVRTLCLFLTPAERKCSRLCEAESSFKYESGLFVQGLLKDSTGSFVLPFRQVMYAPYPTTHIDVDVNTVKQMPPCHEHIYNQRRYMRSELTAFWRATSEEDMAQDTIIYTDESFTPDLFMCTCAGVLYRNIFQDVLHRDTLVKAFLDQVFQLKPGLSLRSTFLAQFLLVLHRKALTLIKYIEDDTQKGKKPFKSLRNLKIDLDLTAEGDLNIIMALAEKIKPGLHSFIFGRPFYTSVQERDVLMTF
Protein: SH3 domain-containing protein (Q6AHQ8)
Organism: Caenorhabditis elegans
Interaction partners:
- Dynamin-type G domain-containing protein
- Osteoclast-stimulating factor 1
- ADP-ribosylation factor 6
- Transducer of Cdc42-dependent actin assembly protein 1 homolog
- Amphiphysin
- Transducer of Cdc42-dependent actin assembly protein 2 homolog
- Ras-related protein Rab-10
- Dynamin
Sequence:
MSCLPCMAADVLAPGFWEVGSYKHNVKRFKDGVEQLDDYCKMSRERAEIEAKYSKMLSQHAEKWRAHVDRTVSAGSVKTVWNELIGEATALSRVHNSLKDCLIDDIVNETTTYRKNSLHTSVFKGPKEIREIEDHFEKAQKPWKKLVDKMEDKRGKYYNVCRQEKSALVNLQNCQTDTSVSPDAATKFRERHEKLKEEVQRTKVDYQKTLTNLNEYKNVYMEAMAHVFKMCQEKEMDRSQFLIGIVQKTQRHYANIIRNSQMSGLHQQLEQSIRSADSEAVKRDLAQWSSVNGVDAFSEWPSFVEYSPEIRNIAARGGSTKDAGGVILTRQINRSEDIPSTHSNTLPSVAVNTASSHEDVGKSSPKSSSESDTSTFDSRKHNSTANKYKNQPQNTTQIQPPPVGWHPSDGPDSPPLSTETPDSAKYGDFEEFTTSKPAVVLYDYAPAEGDEIALRKGEMIEVLTEPDSLGWCTGRVSGNVGLFPASYVQCQGEKS
Protein: NDR1/HIN1-like protein 26 (Q9FI03)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of sugar, amino acid and some primary metabolite export from companion cells (CCs) to sieve elements (SEs) in phloem. Required for apoplastic phloem sugar loading in source leaves in order to transport it to sink tissues. Required for correct sugar partitioning between source leaves and sink organs.
Subcellular location: Cell junction, plasmodesma {ECO:0000269|PubMed:23715470}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:23715470}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Late embryogenesis abundant
- Calmodulin-binding protein-like protein
- Non-race specific disease resistance protein
- ABA-inducible protein-like
- Late embryogenesis abundant
- Late embryogenesis abundant domain-containing protein / LEA domain-containing protein
- Agamous-like MADS-box protein AGL81
- F6D8.10
- At5g54370 protein-like protein)
- Late embryogenesis abundant protein 32
Sequence:
MSQISITSPKHCAKKGGININNRHKKLFFTFSTFFSGLLLIIFLVWLILHPERPEFSLTEADIYSLNLTTSSTHLLNSSVQLTLFSKNPNKKVGIYYDKLLVYAAYRGQQITSEASLPPFYQSHEEINLLTAFLQGTELPVAQSFGYQISRERSTGKIIIGMKMDGKLRWKIGTWVSGAYRFNVNCLAIVAFGMNMTTPPLASLQGTRCSTTI
Protein: Tubulin beta chain (Q4GYY6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Tubulin alpha chain
- Cytoplasmic dynein 2 heavy chain 1
- Dynein heavy chain, cytosolic, putative
- Cytoplasmic dynein 2 heavy chain 1
- Ras-related protein Rab-7b
- Nucleoside diphosphate kinase-like domain-containing protein
- Histone H3, putative
- Histone H3 variant
- Trypanin
- Tubulin-specific chaperone A
Sequence:
MREIVCVQAGQCGNQIGSKFWEVISDEHGVDPTGTYQGDSDLQLERINVYFDEATGGRYVPRSVLIDLEPGTMDSVRAGPYGQIFRPDNFIFGQSGAGNNWAKGHYTEGAELIDSVLDVCCKEAESCDCLQGFQICHSLGGGTGSGMGTLLISKLREQYPDRIMMTFSIIPSPKVSDTVVEPYNTTLSVHQLVENSDESMCIDNEALYDICFRTLKLTTPTFGDLNHLVSAVVSGVTCCLRFPGQLNSDLRKLAVNLVPFPRLHFFMMGFAPLTSRGSQQYRGLSVPELTQQMFDAKNMMQAADPRHGRYLTASALFRGRMSTKEVDEQMLNVQNKNSSYFIEWIPNNIKSSVCDIPPKGLKMAVTFIGNNTCIQEMFRRVGEQFTLMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATIEEEGEFDEEEQY
Protein: Calcium-dependent protein kinase 18 (OsCDPK18) (OsCPK18) (EC 2.7.11.1) (OsCDPK5) (Q0D715)
Organism: Oryza sativa subsp. japonica (Rice)
Function: May play a role in signal transduction pathways that involve calcium as a second messenger (By similarity). Functions upstream of MPK5 in a signaling pathway that represses defense gene expression and negatively regulates resistance to rice blast fungus. Phosphorylates MPK5 at Thr-14 and Thr-32 and activates MPK5 independently of MAP kinase kinase (MKK) phosphorylation. May be involved in arbuscular mycorrhizal presymbiotic phase signaling. Phosphorylates the elicitor-responsive protein ERG1 in vitro. Phosphorylation is calcium-dependent.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21595879}; Lipid-anchor {ECO:0000269|PubMed:21595879}.
Interaction partners:
- Respiratory burst oxidase homolog protein B
- Os12g0541300 protein
- Os11g0537400 protein
- Os09g0438000 protein.
- Os08g0453700 protein
- Serine/threonine-protein phosphatase BSL1 homolog
- Os05g0465800 protein
- Os04g0375500 protein
- Os01g0835500 protein.
Sequence:
MGLCSSSSARRDAGTPGGGNGAGNKDNAGRKGIVACGKRTDFGYDKDFEARYALGKLLGHGQFGYTFAAVDRRSSERVAVKRIDKNKMVLPVAVEDVKREVKILKALQGHENVVHFYNAFEDDNYVYIVMELCEGGELLDRILAKKDSRYSEKDAAVVVRQMLKVAAECHLHGLVHRDMKPENFLFKSTKEDSSLKATDFGLSDFIRPGKHFRDIVGSAYYVAPEVLKRKSGPESDVWSIGVITYILLCGRRPFWDKTEDGIFKEVLKNKPDFRRKPWPNITPCAKDFVQKLLVKDPRARLTAAQALSHEWVREGGQASDIPLDISVLHNMRQFVKYSRFKQFALRALASTLNAEELSDLRDQFNAIDVDKNGTISLEELKQALAKDVPWRLKGPRVLEIVEAIDSNTDGLVDFEEFVAATLHVHQLVEHDTEKWKSLSQAAFDKFDVDGDGYITSDELRMQTGLKGSIDPLLEEADIDRDGKISLDEFRRLLKTASMSSRNVQTPRSVHRS
Protein: ATP-binding cassette sub-family C member 11 (EC 7.6.2.2) (EC 7.6.2.3) (Multidrug resistance-associated protein 8) (Q96J66)
Organism: Homo sapiens (Human)
Function: ATP-dependent transporter of the ATP-binding cassette (ABC) family that actively extrudes physiological compounds, and xenobiotics from cells. Participates in physiological processes involving bile acids, conjugated steroids and cyclic nucleotides. Stimulates the ATP-dependent uptake of a range of physiological lipophilic anions, including the glutathione S-conjugates leukotriene C4 and dinitrophenyl S-glutathione, steroid sulfates such as dehydroepiandrosterone 3-sulfate (DHEAS) and estrone 3-sulfate, glucuronides such as estradiol 17-beta-D-glucuronide (E(2)17betaG), the monoanionic bile acids glycocholate and taurocholate, and methotrexate. Enhances also the cellular extrusion of cAMP and cGMP. Confers resistance to anticancer drugs, such as 5-fluorouracil (5-FU) and methotrexate. Probably functions to secrete earwax. Required for the secretion of components contributing to axillary odor formation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19383836, ECO:0000269|PubMed:25896536}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000269|PubMed:19383836}. Cytoplasmic vesicle membrane {ECO:0000269|PubMed:25896536}. Apical cell membrane {ECO:0000269|PubMed:16359813}; Multi-pass membrane protein.
Interaction partners:
Sequence:
MTRKRTYWVPNSSGGLVNRGIDIGDDMVSGLIYKTYTLQDGPWSQQERNPEAPGRAAVPPWGKYDAALRTMIPFRPKPRFPAPQPLDNAGLFSYLTVSWLTPLMIQSLRSRLDENTIPPLSVHDASDKNVQRLHRLWEEEVSRRGIEKASVLLVMLRFQRTRLIFDALLGICFCIASVLGPILIIPKILEYSEEQLGNVVHGVGLCFALFLSECVKSLSFSSSWIINQRTAIRFRAAVSSFAFEKLIQFKSVIHITSGEAISFFTGDVNYLFEGVCYGPLVLITCASLVICSISSYFIIGYTAFIAILCYLLVFPLAVFMTRMAVKAQHHTSEVSDQRIRVTSEVLTCIKLIKMYTWEKPFAKIIEDLRRKERKLLEKCGLVQSLTSITLFIIPTVATAVWVLIHTSLKLKLTASMAFSMLASLNLLRLSVFFVPIAVKGLTNSKSAVMRFKKFFLQESPVFYVQTLQDPSKALVFEEATLSWQQTCPGIVNGALELERNGHASEGMTRPRDALGPEEEGNSLGPELHKINLVVSKGMMLGVCGNTGSGKSSLLSAILEEMHLLEGSVGVQGSLAYVPQQAWIVSGNIRENILMGGAYDKARYLQVLHCCSLNRDLELLPFGDMTEIGERGLNLSGGQKQRISLARAVYSDRQIYLLDDPLSAVDAHVGKHIFEECIKKTLRGKTVVLVTHQLQYLEFCGQIILLENGKICENGTHSELMQKKGKYAQLIQKMHKEATSDMLQDTAKIAEKPKVESQALATSLEESLNGNAVPEHQLTQEEEMEEGSLSWRVYHHYIQAAGGYMVSCIIFFFVVLIVFLTIFSFWWLSYWLEQGSGTNSSRESNGTMADLGNIADNPQLSFYQLVYGLNALLLICVGVCSSGIFTKVTRKASTALHNKLFNKVFRCPMSFFDTIPIGRLLNCFAGDLEQLDQLLPIFSEQFLVLSLMVIAVLLIVSVLSPYILLMGAIIMVICFIYYMMFKKAIGVFKRLENYSRSPLFSHILNSLQGLSSIHVYGKTEDFISQFKRLTDAQNNYLLLFLSSTRWMALRLEIMTNLVTLAVALFVAFGISSTPYSFKVMAVNIVLQLASSFQATARIGLETEAQFTAVERILQYMKMCVSEAPLHMEGTSCPQGWPQHGEIIFQDYHMKYRDNTPTVLHGINLTIRGHEVVGIVGRTGSGKSSLGMALFRLVEPMAGRILIDGVDICSIGLEDLRSKLSVIPQDPVLLSGTIRFNLDPFDRHTDQQIWDALERTFLTKAISKFPKKLHTDVVENGGNFSVGERQLLCIARAVLRNSKIILIDEATASIDMETDTLIQRTIREAFQGCTVLVIAHRVTTVLNCDHILVMGNGKVVEFDRPEVLRKKPGSLFAALMATATSSLR
Protein: Pleiotropic ABC efflux transporter of multiple drugs PDH1 (P leiomorphic drug resistance homolog 1) (Pleiotropic drug resistance protein 2) (O74208)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Pleiotropic ABC efflux transporter that confers resistance to structurally and functionally unrelated compounds including caspofungin or azoles such as fluconazole, itraconazole, posaconazole, voriconazole, and isavuconazole. Does not play a role in the azole resistance in mature biofilms.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12244114}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pleiotropic ABC efflux transporter of multiple drugs CDR1
- Transcription factor PDR1
- Lanosterol 14-alpha demethylase
- Candida glabrata strain CBS138 chromosome G complete sequence
Sequence:
MNTPDDSSVSSVDSHQPYMGFDDNVEKRIRELARSLTQQSLTSSNRSVNKEAPADGSAPLDRVSTRASSIFSADFKGVNPVFSDEEEDDYDARLDPNSDEFSSKAWVQNMAKITTGDPEFYKPYSIGCCWKDLSASGESADVSYQSTFLNLPVKLLNAVWRKARPARESDTFRILKPMDGLLKPGELLVVLGRPGSGCTTLLKSISSTTHGFQISKDSVISYNGLTPNEIKKHYRGEVVYNAEADIHLPHLTVYQTLVTVARLKTPQNRVKGVTREDFANHVTDVAMATYGLSHTRDTKVGNDLVRGVSGGERKRVSIAEVWICGSKFQCWDNATRGLDSATALEFVRALKTQAHIAKNVATVAIYQCSQDAYNLFNKVSVLYEGYQIYFGDAQHAKVYFQKMGYFCPKRQTIPDFLTSITSPAERRINKEYLDKGIKVPQTPLDMVEYWHNSEEYKQLREEIDETLAHQSEDDKEEIKEAHIAKQSKRARPSSPYVVSYMMQVKYILIRNFWRIKNSASVTLFQVFGNSAMAFILGSMFYKIQKGSSADTFYFRGAAMFFAILFNAFSSLLEIFSLYEARPITEKHRTYSLYHPSADAFASVISEIPPKIVTAILFNIIFYFLVNFRRDAGRFFFYFLINVIAVFAMSHLFRCVGSLTKTLQEAMVPASMLLLALSMYTGFAIPRTKMLGWSKWIWYINPLAYLFESLMVNEFHDRRFPCNTYIPRGGAYNDVTGTERVCASVGARPGNDYVLGDDFLKESYDYENKHKWRGFGVGMAYVIFFFFVYLILCEFNEGAKQKGEMLVFPHSVVKRMKKEGKIRDKTKMHTDKNDIENNSESITSNATNEKNMLQDTYDENADSESITSGSRGGSPQVGLSKSEAIFHWQNLCYDVPIKTEVRRILNNVDGWVKPGTLTALMGASGAGKTTLLDCLAERTTMGVITGDVMVNGRPRDTSFSRSIGYCQQQDLHLKTATVRESLRFSAYLRQPSSVSIEEKNEYVEAVIKILEMETYADAVVGVPGEGLNVEQRKRLTIGVELAAKPKLLVFLDEPTSGLDSQTAWATCQLMKKLANHGQAILCTIHQPSAMLMQEFDRLLFLQKGGQTVYFGDLGKGCKTMIKYFEDHGAHKCPPDANPAEWMLEVVGAAPGSHANQDYHEVWRNSEQFKQVKQELEQMEKELSQKELDNDEDANKEFATSLWYQFQLVCVRLFQQYWRTPDYLWSKYILTIFNQLFIGFTFFKADHTLQGLQNQMLSIFMYTVIFNPLLQQYLPTFVQQRDLYEARERPSRTFSWKAFILAQIVVEVPWNIVAGTLAYCIYYYSVGFYANASQAHQLHERGALFWLFSIAFYVYVGSLGLFVISFNEVAETAAHIGSLMFTMALSFCGVMATPDAMPRFWIFMYRVSPLTYLIDALLSTGVANVDIRCSNTELVTFTPPQGLTCGQYMTPYLNVAGTGYLTDPSATDECHFCQFSYTNDFLATVSSKYYRRWRNYGIFICFIVFDYVAGIFLYWLARVPKTNGKIAKNGKTAKVNFIRRLIPF
Protein: FAM3 metabolism regulating signaling molecule C (C9JMN4)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRVAGAAKLVVAVAVFLLTFYVISQVFEIKMDASLGNLFARSALDTAARSTKPPRYKCGISKACPEKHFAFKMASGAANVVGPKICLEDNVLMSGVKNNVGRGINVALANGKTGEVLDTKYFDMWGGDVAPFIEFLKAIQDGTIVLMGTYD
Protein: Synembryn (Protein Ric-8) (X1WG58)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cell cortex {ECO:0000256|ARBA:ARBA00004544}.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate synthase
Sequence:
MTVDVEKIIQFIKQGDQDNVQSHLDDYNTENSQCFFFDVEERERKKQRELEEFRRNKVREYVPDSDSDCDSDNSEDPDLVLRRRLAAALIWFIRMRLQPGVLRVCLRTLRIISRDRKALAPLITDYAIITLARLGGISALPTWPEEEDDQWGSSHNDVAPENETDTLPDNDTNTQCPACCSETDDSCCGSTVCAASSVREGGLHFSPMNNTSNPRETQNDHCEESVRKDGVCGLLTRGKRETRGERDEEGEEGHDDGEIWRKEAMKTLCNVIYNSPKAQERASTLRLLHGLSVRIKDGIHSSSPPSGQFYELRLLFLLTALRPELRIELCQERGVSMLTAALEQCLDVIWGETHEVLTDLTAPPLCKELSQRALEILKTLFNITYSVHRQDLDEEAAALYRRLAAVLRHCLLVPCEGEDRKEELQGHTVNVLSALPLQCLDVLLSVRLSEGSEESGGVNMDCVHTLLLFMEKRLDRGHKLKEKLTPVLNLLTESSKAHRETRHYLRQQILPPLRDVELRPEQGNTLRSRLVRLMTHVDTDIKHCAAELLFVLCKENVSRFVKYTGYGNAAGLLAARGLLNGRGSSPQPQYSSDSDSDTEEYRQARDRINPVTGRVEEEQPDPMEGMTEEEKEAEALRLINMFNRLSRGKIIQPMGVTTDGKLAPLCGQTRHSAVQEEEEEDEEDDDCSETEQ
Protein: Protein ABA DEFICIENT 4, chloroplastic (Q8LFP9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for neoxanthin biosynthesis, an intermediary step in abscisic acid (ABA) biosynthesis. Probably not involved directly in the enzymatic conversion of violaxanthin to neoxanthin. Cannot convert violaxanthin to neoxanthin in vitro. Required for ABA biosynthesis in response to drought stress. Required for neoxanthin biosynthesis which is involved in photoprotection of photosystem II (PSII). Neoxanthin acts as an antioxidant within the photosystem PSII supercomplex.
Subcellular location: Plastid, chloroplast membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Zeaxanthin epoxidase, chloroplastic
- Xanthoxin dehydrogenase
- Molybdenum cofactor sulfurase
- Abscisic-aldehyde oxidase
- 9-cis-epoxycarotenoid dioxygenase NCED2, chloroplastic
- 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic
- Violaxanthin de-epoxidase, chloroplastic
- Probable 9-cis-epoxycarotenoid dioxygenase NCED5, chloroplastic
- Prolycopene isomerase, chloroplastic
- 
Sequence:
MGFSSFISQPLSSSLSVMKRNVSAKRSELCLDSSKIRLDHRWSFIGGSRISVQSNSYTVVHKKFSGVRASWLTTTQIASSVFAVGTTAVLPFYTLMVVAPKAEITKKCMESSVPYIILGVLYVYLLYISWTPETLKYMFSSKYMLPELSGIAKMFSSEMTLASAWIHLLVVDLFAARQVYNDGLENQIETRHSVSLCLLFCPVGIVSHFVTKAIINNQYK
Protein: Proline-rich AKT1 substrate 1 (40 kDa proline-rich AKT substrate) (Q96B36)
Organism: Homo sapiens (Human)
Function: Subunit of mTORC1, which regulates cell growth and survival in response to nutrient and hormonal signals. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Within mTORC1, AKT1S1 negatively regulates mTOR activity in a manner that is dependent on its phosphorylation state and binding to 14-3-3 proteins. Inhibits RHEB-GTP-dependent mTORC1 activation. Substrate for AKT1 phosphorylation, but can also be activated by AKT1-independent mechanisms. May also play a role in nerve growth factor-mediated neuroprotection.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9D1F4}. Note=Found in the cytosolic fraction of the brain. {ECO:0000250|UniProtKB:Q9D1F4}.
Interaction partners:
- DEP domain-containing mTOR-interacting protein
- Target of rapamycin complex subunit LST8
- Regulatory-associated protein of mTOR
- Serine/threonine-protein kinase mTOR
- Target of rapamycin complex 2 subunit MAPKAP1
- GTP-binding protein Rheb
- RAC-alpha serine/threonine-protein kinase
- Ras-related GTP-binding protein A
- TELO2-interacting protein 1 homolog
- Rapamycin-insensitive companion of mTOR
Sequence:
MASGRPEELWEAVVGAAERFRARTGTELVLLTAAPPPPPRPGPCAYAAHGRGALAEAARRCLHDIALAHRAATAARPPAPPPAPQPPSPTPSPPRPTLAREDNEEDEDEPTETETSGEQLGISDNGGLFVMDEDATLQDLPPFCESDPESTDDGSLSEETPAGPPTCSVPPASALPTQQYAKSLPVSVPVWGFKEKRTEARSSDEENGPPSSPDLDRIAASMRALVLREAEDTQVFGDLPRPRLNTSDFQKLKRKY
Protein: Transmembrane protein 94 (Endoplasmic reticulum magnesium ATPase) (Q7TSH8)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:38513662}; Multi-pass membrane protein {ECO:0000305|PubMed:38513662}.
Interaction partners:
Sequence:
MDLREKHLGEPPLALGLSTRKALSVLKEQLEAVLEKHLKERKKSLTWKEAWRSSFLHLSNRCSCFHWPGASLMLLAVLLLLCCCGGQPAGSQGVELVNASALFLLLLLNLVLIGRQDRLKRREVERRLRGIIDQIQDALRDGKEIKWPNSMYPDLHMPFAPSWSLHWAYRDGHLVNLPVSLLVEGDIIALRPGQESFASLRGIKDDEHIVLEPGDLFPPFSPPPSPRGEVKRGPQNPQQHRLFRVLETPVIDNIRWCLDTALSRPVTALDNERFTVQSVMLHYAVPVVLAGFLITNALRFMFKAPGVTSWQYTLLQLQVNGMLPILPLLFPVLWVLATACGEARVLAQMSKASPSSLLAKFSEDTLSSYTEAVSSQEMLRCIWGHFLRVIQGTSPTLSHSASLLHSLGSVTVLCCVDKQGILSWPNPSPETVLFFSGKVEPPHSSHEDLTDDLSTRSFCHPEVEEEPHEHDALLAGSLNNTLHLSNEQERSDWLADGPKPSEPYPHHKGHGRSKHPSGSNVSFSRDTEGGEEEPSKAQPGTEGDPYEAEDFVCDYHLEMLSLSQDQQNPSCIQFDDSNWQSHLTSLKPLGLNVLLNLCNASVTERLCRFSDHLCNIALQESHSAVLPVHVPWGLCELARLIGFTPGAKELFKQENHLALYRLPSAETLKETSLGRPSCVTKRRPPLSHMISLFIKDTATSTEQMLSHGSADVVVEACTDFWDGADIYPLSGSDRKKVLDFYQRACLSGYCSAFAYKPMNCTLSSQLNGKCIELVQVPGQNSIFTMCELPSTIPIKPNNRRSSWSSDEGIGEVLEKEDCMQALSGQIFMGMVSSQYQARLDIVRLIDGLVNACIRFVYFSLEDELRSKVFAEKMGLETGWNCHISLTPNGDMPGSEIPPSSPSHAGSLHDDLNQVSRDDAEGLLLLEEEGHSDLISFQPTDSDIPSFLEDCNRAKLPRGIHQVRPHLQNIDNVPLLVPLFTDCTPDTMCEMIKIMQEYGEVTCCLGSSANLRNSCLFLQSDVSIALDPLYPSRCSWETFGYATSTTMAQASDGLSPLQLSGQLNSLPCSLTFRQEESISIIRLIEQARHATYGIRKCFLFLLQCQLTLVVIQFLSCLVQLPPLLSTTDILWLSCFCYPLLSISLLGKPPHSSIMSMATGKNLQSIPKKTQHYFLLCFLLKFSLTISSCLVCFGFTLQSFCDSARARNLTNCSSVMLCSNDDRAPAWFEDFANGLLSAQKLTAALIVLHTVFISITHVHRTKPLWRKSPLTNLWWAVTVPVVLLGQVVQTVVDLQLWTHRDSRVHFGLEDVPLLTWLLGCLSLVLVVVTNEIVKLHEIRVRVRYQKRQKLQFETKLGMNSPF
Protein: AarF domain-containing kinase 1 (EC 2.7.-.-) (Q9W133)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential for maintaining mitochondrial cristae formation and mitochondrial function by acting via YME1L to regulate the mitochondrial structural proteins Opa1 and Mitofilin. This function is likely to be kinase-independent (By similarity). Functions in tracheal development and larval molting probably by acting in sterol modification and/or intracellular lipid trafficking. The action of this enzyme is not yet clear (Probable). It is not known if it has protein kinase activity and what type of substrate it would phosphorylate (Ser, Thr or Tyr) (Probable).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q86TW2}.
Interaction partners:
- 2-methoxy-6-polyprenyl-1,4-benzoquinol methylase, mitochondrial
- Ubiquinone biosynthesis monooxygenase COQ6, mitochondrial
- Ubiquinone biosynthesis O-methyltransferase, mitochondrial
- Ubiquinone biosynthesis protein COQ4 homolog, mitochondrial
Sequence:
MLLRRVLGYGVVGAGLASAGWSLHTNDYDPNSLGIVRLSRSAAAVVDVALTYKRELYYKEWDKETPEYKAEKSRVHKIAAEKLLQLICINKGVYIKVGQHIGALEYLLPKEFVQTMKVLHSDAPQNPIEDLYKVIRQDLHCNPEEIFDSFEREPLGTASLAQVHKARLKTGELVAVKVQHPYVKGNSRVDMKTMELAVNVLARIFPDFKIHWLVEESKKNLPIELDFLNEGRNAEKVAKQFKKYSWLRVPKIYWKYSSSRVLVMEYLEGGHVTDLDYIRRNKIDSFAVANRIGQLYSEMIFRTGFVHSDPHPGNILVRRTPENSLEIVLLDHGLYANLTDKFRYDYSNLWLSILKVDRKAMRQHSEQLGIKGDLYGLFACMVTGRPWETVMQGLTKVKYSKEEKNTLQNNTSLVLPHISDVLEQVDRQMLLILKTNDLIRGIESTLRTQNRMTAFWVMSKCCVQSSYAEQRAKQSDSGSSRILWLRVRERWELFKLNCYYLYLGLINFGFLEALKQVI
Protein: Large ribosomal subunit protein eL19A (60S ribosomal protein L19-A) (L23) (RP15L) (RP33) (YL14) (P0CX82)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. eL19 may play a role in the last stages of translation initiation, in particular subunit joining and shedding/releasing factors.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL10
- Ubiquitin-ribosomal protein eS31 fusion protein
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL34A
- Large ribosomal subunit protein eL24A
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL31A
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
Sequence:
MANLRTQKRLAASVVGVGKRKVWLDPNETSEIAQANSRNAIRKLVKNGTIVKKAVTVHSKSRTRAHAQSKREGRHSGYGKRKGTREARLPSQVVWIRRLRVLRRLLAKYRDAGKIDKHLYHVLYKESKGNAFKHKRALVEHIIQAKADAQREKALNEEAEARRLKNRAARDRRAQRVAEKRDALLKEDA
Protein: Bone morphogenetic protein 16 (D2TEB7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MFPASLLVLMILLLPQASSGHQEGPSQTHGKLDSLLEPSLAHTIQNLLLTRLGLQSHPNPSTKAQVPQYLLDLYRFHTQQYHLIEDPEFSYPSKHVQGANTVRCFHHTDSPTPSLPEEQKTTVDGIHIGFNLSSIPSEESVVSAELRLLHEGSSGGSHVASLYLSNHDPSSKPILLHSRQLTRDRKSAQLWETFPLDREVFQNLSKTSGSLSFILDVIPDSNSSSTLPKDRHLRVRRSTLQDGPTWERQRPLLVTYSHDGRSEPFVNLNKRKSSRSRSRWTRFKGDRGQGSDWNERRVKRNNRRAAKLKRLSRARCRRHPLYVDFKDVGWNKWIIAPSGYDAFFCLGECRFPLADHMNSSSHAMVQTLVSSVNGAVPRPCCVPTALSPIALLFLDQEERVVLKNYQDMVVEGCGCR