wanglab/gogpt-training-data huggingface dataset:
Protein: Fatty acid desaturase domain-containing protein (G8B5R3)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Interaction partners:
- Acyl-CoA desaturase
- Cytochrome b5 heme-binding domain-containing protein
- Very-long-chain
- Very-long-chain 3-oxoacyl-CoA reductase
- Elongation of fatty acids protein
- Elongation of fatty acids protein
Sequence:
MSSATTSSYSSSFNDASTTKVEKKGNVASFKTTPNGYKTNLTAIDTYGNTFKVPDYSIKDILSAIPSHCYERRLLESFYYVFRDIFMMVTLGYIANNYIELLPNQFVRFAAWAGYVWCQGLIATGIWVLAHECGHQAFSDYGWVNDLTGWVLHSYLLVPYFSWKFSHSKHHKATGHLTRDMVFIPKTKEQFLQSRGVEDLDDLLGDSPMFSLLQMVFQQTFGWIAYLFANVSGPKFPGASWMQVNHFNPSSLLFDKKDYYYILLSDVGILIQCTILYTWYKNFGGFNFLVNYFLPYLFVNHWLVFITYLQHSDPQMPHYEAHQWTFARGAAATIDREFGFVGKHIFHDIIETHVLHHYVSRIPFYNAREASEAIKKVMGIHYQHSNENMWKSLWKSARWCQYVDGKDGVMMYRNINGLGVDPKKEK
Protein: Pentatricopeptide repeat-containing protein At1g59720, chloroplastic/mitochondrial (Protein CHLORORESPIRATORY REDUCTION 28) (Q0WQW5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in multiple sites RNA editing events in chloroplasts. Involved in the editing of the site 2 of ndhB (ndhB-2) and site 3 of ndhD (ndhD-3) transcripts, which are two plastid-encoded subunits of the chloroplast NAD(P)H dehydrogenase (NDH) complex. Required for the activity of the NDH complex of the photosynthetic electron transport chain.
Subcellular location: Plastid, chloroplast {ECO:0000255}. Mitochondrion {ECO:0000269|PubMed:15269332}.
Interaction partners:
- Phosphoglycerate mutase family protein
- Organelle RRM domain-containing protein 1
- NAD
- Zinc finger protein VAR3, chloroplastic
- NAD
- Multiple organellar RNA editing factor 9, chloroplastic
- Organelle RRM domain-containing protein 2
- Protoporphyrinogen oxidase 1, chloroplastic
- Multiple organellar RNA editing factor 2, chloroplastic
Sequence:
MVVRSIIVSPPTTITYYHPMSIGLLVHPLSPHIPPASSPSASTAGNHHQRIFSLAETCSDMSQLKQLHAFTLRTTYPEEPATLFLYGKILQLSSSFSDVNYAFRVFDSIENHSSFMWNTLIRACAHDVSRKEEAFMLYRKMLERGESSPDKHTFPFVLKACAYIFGFSEGKQVHCQIVKHGFGGDVYVNNGLIHLYGSCGCLDLARKVFDEMPERSLVSWNSMIDALVRFGEYDSALQLFREMQRSFEPDGYTMQSVLSACAGLGSLSLGTWAHAFLLRKCDVDVAMDVLVKNSLIEMYCKCGSLRMAEQVFQGMQKRDLASWNAMILGFATHGRAEEAMNFFDRMVDKRENVRPNSVTFVGLLIACNHRGFVNKGRQYFDMMVRDYCIEPALEHYGCIVDLIARAGYITEAIDMVMSMPMKPDAVIWRSLLDACCKKGASVELSEEIARNIIGTKEDNESSNGNCSGAYVLLSRVYASASRWNDVGIVRKLMSEHGIRKEPGCSSIEINGISHEFFAGDTSHPQTKQIYQQLKVIDDRLRSIGYLPDRSQAPLVDATNDGSKEYSLRLHSERLAIAFGLINLPPQTPIRIFKNLRVCNDCHEVTKLISKVFNTEIIVRDRVRFHHFKDGSCSCLDYW
Protein: Mitochondrial import inner membrane translocase subunit TIM23-2 (Q38820)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of the TIM17:23 complex, a complex that mediates the translocation of transit peptide-containing proteins across the mitochondrial inner membrane. Links the inner and outer membranes (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit TIM50
- Mitochondrial import inner membrane translocase subunit TIM17-2
- Probable mitochondrial import inner membrane translocase subunit TIM21
- Mitochondrial import inner membrane translocase subunit TIM44-1
- Mitochondrial import inner membrane translocase subunit TIM44-2
- Mitochondrial import inner membrane translocase subunit TIM17-3
- Mitochondrial import inner membrane translocase subunit TIM17-1
- Mitochondrial import inner membrane translocase subunit PAM16 like 1
- Mitochondrial import inner membrane translocase subunit TIM22-1
- Mitochondrial import inner membrane translocase subunit TIM22-4
Sequence:
MAANNRSDHGSDENTRLYNPYQNYEVPINKSQYLYKLPTSPEFLFTEEALRQRRSWGENLTFYTGTAYLGGSVAGASVGVITGVKSFESGDTTKLKINRILNSSGQTGRTWGNRIGIIGLVYAGIESGIVAATDRDDVWTSVVAGLGTGAVCRAARGVRSAAVAGALGGLAAGAVVAGKQIVKRYVPI
Protein: Patatin family protein (Q54XY1)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Guanylyl cyclase, membrane
- Guanylyl cyclase
Sequence:
MGDNKKENIRIILSLDGGGTKGLYTIEVIEHFVKLSGSDFTKHVDLFGGTSTGGILSIAKSKEISNSELLNMYEGKESKKIFGSLWDEVKGVFTRGEMFNSDELINIANSWFPSSPDGADTQITELNEKKFFVVSLKKTGEKNDILTPVIISNYKFDETTTIAGNNNNNNNHFIKGEEIERLYTIGEEALSLADAIRATSSIPAAFQKHKQGDEEYLDGGFKYNNPMEIAYHEARIIYPNDYLVIISIGCTDKDVQGLTENNKEINDRLEKLLDNMEDGVETKGIFSVPHYLKSNWITDFLDTIKLNKNSKSSQQLYIEAMQNIKDSNAFLLRFDSVETHSLLSFSDTSKEFFEKLRKCSSALSKDSEFIRTADLLKRIIDLKKDE
Protein: phospholipase A2 (EC 3.1.1.4) (A0A590UJC7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQFFGRLVNTFSGVTNLFSNPFRVKEVAVADYTSSDRVREEGQLILFQNTPNRTWDCVLVNPRNSQSGFRLFQLELEADALVNFHQYSSQLLPFYESSPQVLHTEVLQHLTDLIRNHPSWSVAHLAVELGIRECFHHSRIISCANCAENEEGCTPLHLACRKGDGEILVELVQYCHTQMDVTDYKGETVFHYAVQGDNSQVLQLLGRNAVAGLNQVNNQGLTPLHLACQLGKQEMVRVLLLCNARCNIMGPNGYPIHSAMKFSQKGCAEMIISMDSSQIHSKDPRYGASPLHWAKNAEMARMLLKRGCNVNSTSSAGNTALHVAVMRNRFDCAIVLLTHGANADARGEHGNTPLHLAMSKDNVEMIKALIVFGAEVDTPNDFGETPTFLASKIGRPCPALCLTELQDLMHISRARKPAFILGSMRDEKRTHDHLLCLDGGGVKGLIIIQLLIAIEKASGVATKDLFDWVAGTSTGGILALAILHSKSMAYMRGMYFRMKDEVFRGSRPYESGPLEEFLKREFGEHTKMTDVRKPKVMLTGTLSDRQPAELHLFRNYDAPETVREPRFNQNVNLRPPAQPSDQLVWRAARSSGAAPTYFRPNGRFLDGGLLANNPTLDAMTEIHEYNQDLIRKGQANKVKKLSIVVSLGTGRSPQVPVTCVDVFRPSNPWELAKTVFGAKELGKMVVDCCTDPDGRAVDRARAWCEMVGIQYFRLNPQLGTDIMLDEVSDTVLVNALWETEVYIYEHREEFQKLIQLLLSP
Protein: 1,3-beta-glucanosyltransferase gel2 (EC 2.4.1.-) (Glucan elongating glucanosyltransferase 2) (P0C954)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Splits internally a 1,3-beta-glucan molecule and transfers the newly generated reducing end (the donor) to the non-reducing end of another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta linkage, resulting in the elongation of 1,3-beta-glucan chains in the cell wall. Involved in cell wall morphogenesis (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Protein ecm33
Sequence:
MLPTYVRLFTAVCALATTASAVVPIEVKGKDFVNSKTGDRFQILGVDYQPGGSSGFTKDKDPLSDPDACLRDAALMQRLGVNTIRIYNLSPSLNHDECASIFNAAGIYMILDVNSPLYGGYLDRTDPESTYNDVYFKQVFGVIEAFKNFPNTLAFFAGNEVINEQSVKNVPTYVRAIQRDMKDYIAKNLDRSIPVGYSAADIRPILMDTLNYFMCADDANSQSDFFGLNSYSWCGNSSYTKSGYDVLTKDFADASIPVFFSEYGCNEVQPRYFSEVQALYGQEMTQSFSGGLVYEYTQEENDYGLVQINDNGTVTLLVDYDNLMAQYSKLDMSRIQASNTTQTSAKPPKCESSLITNSTFTDSFDLPKRPSKVQTMIDKGLSDANTGKLVEVKNTDIKQKIYNANGEEITGIKLSILASGESNTPGAHSSGSTSGSSSSGGSSSSSSDKESAAGTISVPFVGLLSAASFMAFFML
Protein: Protein jagged-1 (Jagged1) (CD antigen CD339) (Q9QXX0)
Organism: Mus musculus (Mouse)
Function: Ligand for multiple Notch receptors and involved in the mediation of Notch signaling. May be involved in cell-fate decisions during hematopoiesis. Seems to be involved in early and late stages of mammalian cardiovascular development. Inhibits myoblast differentiation (By similarity). May regulate fibroblast growth factor-induced angiogenesis.
Subcellular location: Membrane; Single-pass type I membrane protein. Cell membrane {ECO:0000250|UniProtKB:P78504}.
Interaction partners:
- Neurogenic locus notch homolog protein 1
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 3
- Neurogenic locus notch homolog protein 4
- Protein jagged-2
- Recombining binding protein suppressor of hairless
- Hairy/enhancer-of-split related with YRPW motif protein 1
- Delta-like protein 1
- Beta-1,3-N-acetylglucosaminyltransferase lunatic fringe
- Hairy/enhancer-of-split related with YRPW motif protein 2
Sequence:
MRSPRTRGRPGRPLSLLLALLCALRAKVCGASGQFELEILSMQNVNGELQNGNCCGGVRNPGDRKCTRDECDTYFKVCLKEYQSRVTAGGPCSFGSGSTPVIGGNTFNLKASRGNDRNRIVLPFSFAWPRSYTLLVEAWDSSNDTIQPDSIIEKASHSGMINPSRQWQTLKQNTGIAHFEYQIRVTCDDHYYGFGCNKFCRPRDDFFGHYACDQNGNKTCMEGWMGPDCNKAICRQGCSPKHGSCKLPGDCRCQYGWQGLYCDKCIPHPGCVHGTCNEPWQCLCETNWGGQLCDKDLNYCGTHQPCLNRGTCSNTGPDKYQCSCPEGYSGPNCEIAEHACLSDPCHNRGSCKETSSGFECECSPGWTGPTCSTNIDDCSPNNCSHGGTCQDLVNGFKCVCPPQWTGKTCQLDANECEAKPCVNARSCKNLIASYYCDCLPGWMGQNCDININDCLGQCQNDASCRDLVNGYRCICPPGYAGDHCERDIDECASNPCLNGGHCQNEINRFQCLCPTGFSGNLCQLDIDYCEPNPCQNGAQCYNRASDYFCKCPEDYEGKNCSHLKDHCRTTTCEVIDSCTVAMASNDTPEGVRYISSNVCGPHGKCKSQSGGKFTCDCNKGFTGTYCHENINDCESNPCKNGGTCIDGVNSYKCICSDGWEGAHCENNINDCSQNPCHYGGTCRDLVNDFYCDCKNGWKGKTCHSRDSQCDEATCNNGGTCYDEVDTFKCMCPGGWEGTTCNIARNSSCLPNPCHNGGTCVVNGDSFTCVCKEGWEGPICTQNTNDCSPHPCYNSGTCVDGDNWYRCECAPGFAGPDCRININECQSSPCAFGATCVDEINGYQCICPPGHSGAKCHEVSGRSCITMGRVILDGAKWDDDCNTCQCLNGRVACSKVWCGPRPCRLHKSHNECPSGQSCIPVLDDQCFVRPCTGVGECRSSSLQPVKTKCTSDSYYQDNCANITFTFNKEMMSPGLTTEHICSELRNLNILKNVSAEYSIYIACEPSLSANNEIHVAISAEDIRDDGNPVKEITDKIIDLVSKRDGNSSLIAAVAEVRVQRRPLKNRTDFLVPLLSSVLTVAWVCCLVTAFYWCVRKRRKPSSHTHSAPEDNTTNNVREQLNQIKNPIEKHGANTVPIKDYENKNSKMSKIRTHNSEVEEDDMDKHQQKVRFAKQPVYTLVDREEKAPSGTPTKHPNWTNKQDNRDLESAQSLNRMEYIV
Protein: 2,4-dienoyl-coa reductase-like protein (Q582G9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Electron transfer flavoprotein subunit beta
- Electron transfer flavoprotein subunit alpha
- DNA
- Bifunctional NAD
- Peptidase T, putative
- Aminoacylase, putative
Sequence:
MPLGIVAAPAARKATSLFSPIAIGANNRVVLPNRFVMLPMYLNIEQELDMWSDAHMDAMGTFFAERARNGAKLIVCGGLGVSRLGKWRVDSMSLDTRDAAKALSRVTEAVHKEGGLILAQALHPGRAARRRWFVSSTSTPSPVQPFPQAHPWRVPGMLLEYIVSEHERFARLAEAAGFDGIEIPVSEGALLHNFLSPAVNDRNDRFGRSLDGRIEPTLRTLDAVRRSLSDPEKFLLSVRLCVHDLKVGGTSMAETVAVAEALARFGGVDMLSTSVGMHDSPVQTMASYVPQATFARCVQHVREQLHLRGVILPVVATHRVHSIAVAERLLKDGVCDLVGVGRPLLADPQMIRKAEEGHTEDIIPCIACNHCVNRLYKHQRMTCALNPFSGYERERRCTPALFKKSIAVVGAGAAGVTCALTLWRRGHDVTLFEKSNYVGGQLNLAKVVPGKESYQEILEYWTRQLRESAINVRLGAEFTREEMARNHQFFHAVVLCCGSVPRPATSHQLPGTSESRLVVPFEKILNGSVRAGRRVVIIGNGAISHDVASYLLHDPRVSRSIHEYCDEWGVNLDDGSLDPQAAFRVPRNNRDVVLFNKADKDADLSRGRGWTQKLWIRNHGGTIIKHGLVENIDGNGVHISMVPPDSRKFFVECDTIVWAYGMLPNISVGTWIYEWMKDGAKKRGEMIRDFSIYNAGSCRDSYSGEGHGEQDLLQAVHEGYEIGYKI
Protein: A kinase anchor protein 10 isoform 1 (A0A0S2Z4Z7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRGAGPSPRQSPRTLRPDPGPAMSFFRRKVKGKEQEKTSDVKSIKASISVHSPQKSTKNHALLEAAGPSHVAINAISANMDSFSSSRTATLKKQPSHMEAAHFGDLGRSCLDYQTQETKSSLSKTLEQVLHDTIVLPYFIQFMELRRMEHLVKFWLEAESFHSTTWSRIRAHSLNTVKQSSLAEPVSPSKKHETTASFLTDSLDKRLEDSGSAQLFMTHSEGIDLNNRTNSTQNHLLLSQECDSAHSLRLEMARAGTHQVSMETQESSSTLTVASRNSPASPLKELSGKLMKSIEQDAVNTFTKYISPDAAKPIPITEAMRNDIIARICGEDGQVDPNCFVLAQSIVFSAMEQEHFSEFLRSHHFCKYQIEVLTSGTVYLADILFCESALFYFSEYMEKEDAVNILQFWLAADNFQSQLAAKKGQYDGQEAQNDAMILYDKYFSLQATHPLGFDDVVRLEIESNICREGGPLPNCFTTPLRQAWTTMEKVFLPGFLSSNLYYKYLNDLIHSVRGDEFLGGNVSLTAPGSVGPPDESHPGSSDSSASQSSVKKASIKILKNFDEAIIVDAASLDPESLYQRTYAGKMTFGRVSDLGQFIRESEPEPDVRKSKGSMFSQAMKKWVQGNTDEAQEELAWKIAKMIVSDIMQQAQYDQPLEKSTKL
Protein: Intraflagellar transport protein 22 homolog (Rab-like protein 5) (Q9H7X7)
Organism: Homo sapiens (Human)
Function: Small GTPase-like component of the intraflagellar transport (IFT) complex B.
Subcellular location: Cell projection, cilium {ECO:0000250}.
Interaction partners:
- Intraflagellar transport protein 46 homolog
- Intraflagellar transport protein 74 homolog
- Intraflagellar transport protein 52 homolog
- Intraflagellar transport protein 27 homolog
- Intraflagellar transport protein 81 homolog
- Intraflagellar transport protein 25 homolog
- Intraflagellar transport protein 57 homolog
- TRAF3-interacting protein 1
- Intraflagellar transport protein 70B
- Intraflagellar transport protein 88 homolog
Sequence:
MLKAKILFVGPCESGKTVLANFLTESSDITEYSPTQGVRILEFENPHVTSNNKGTGCEFELWDCGGDAKFESCWPALMKDAHGVVIVFNADIPSHRKEMEMWYSCFVQQPSLQDTQCMLIAHHKPGSGDDKGSLSLSPPLNKLKLVHSNLEDDPEEIRMEFIKYLKSIINSMSESRDREEMSIMT
Protein: Ribosome-recycling factor (RRF) (Ribosome-releasing factor) (O82853)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00040}.
Interaction partners:
- Elongation factor Ts
- Large ribosomal subunit protein uL13
- Uridylate kinase
- Large ribosomal subunit protein bL20
- Large ribosomal subunit protein uL16
- Small ribosomal subunit protein uS2
- Large ribosomal subunit protein uL1
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL27
- Large ribosomal subunit protein uL3
Sequence:
MINEIKKEAQERMGKTLEALGHAFAKIRTGRAHPSILDSVMVSYYGADTPLRQVANVTVEDSRTLALAVFDKSMIQAVEKAIMTSDLGLNPATAGTTIRVPMPALTEETRKGYTKQARAEAEQARVSVRNIRRDALAQLKDLQKEKEISEDEERRAGDDVQKLTDKFIGEIEKALEAKEADLMAV
Protein: Sucrose synthase 1 (EC 2.4.1.13) (Shrunken-1) (Sucrose-UDP glucosyltransferase 1) (P04712)
Organism: Zea mays (Maize)
Function: Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways. Most active in the sink tissues where it is responsible for the breakdown of the arriving sucrose.
Interaction partners:
- Sugary1.
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic/amyloplastic
- Starch synthase, chloroplastic/amyloplastic
- Starch synthase, chloroplastic/amyloplastic
- Alcohol dehydrogenase 1
- Alcohol dehydrogenase 1
- p-loop containing nucleoside triphosphate hydrolase superfamily protein
- Uncharacterized protein.
Sequence:
MAAKLTRLHSLRERLGATFSSHPNELIALFSRYVHQGKGMLQRHQLLAEFDALFDSDKEKYAPFEDILRAAQEAIVLPPWVALAIRPRPGVWDYIRVNVSELAVEELSVSEYLAFKEQLVDGQSNSNFVLELDFEPFNASFPRPSMSKSIGNGVQFLNRHLSSKLFQDKESLYPLLNFLKAHNYKGTTMMLNDRIQSLRGLQSSLRKAEEYLLSVPQDTPYSEFNHRFQELGLEKGWGDTAKRVLDTLHLLLDLLEAPDPANLEKFLGTIPMMFNVVILSPHGYFAQSNVLGYPDTGGQVVYILDQVRALENEMLLRIKQQGLDITPKILIVTRLLPDAAGTTCGQRLEKVIGTEHTDIIRVPFRNENGILRKWISRFDVWPYLETYTEDVSSEIMKEMQAKPDLIIGNYSDGNLVATLLAHKLGVTQCTIAHALEKTKYPNSDIYLDKFDSQYHFSCQFTADLIAMNHTDFIITSTFQEIAGSKDTVGQYESHIAFTLPGLYRVVHGIDVFDPKFNIVSPGADMSVYYPYTETDKRLTAFHPEIEELIYSDVENSEHKFVLKDKKKPIIFSMARLDRVKNMTGLVEMYGKNARLRELANLVIVAGDHGKESKDREEQAEFKKMYSLIDEYKLKGHIRWISAQMNRVRNGELYRYICDTKGAFVQPAFYEAFGLTVIESMTCGLPTIATCHGGPAEIIVDGVSGLHIDPYHSDKAADILVNFFDKCKADPSYWDEISQGGLQRIYEKYTWKLYSERLMTLTGVYGFWKYVSNLERRETRRYIEMFYALKYRSLASQVPLSFD
Protein: Heterodimeric geranylgeranyl pyrophosphate synthase large subunit 1, chloroplastic (GGPP synthase 1) (GGPS1) (EC 2.5.1.-) ((2E,6E)-farnesyl diphosphate synthase 1) (Dimethylallyltranstransferase 1) (EC 2.5.1.1) (Farnesyl diphosphate synthase 1) (Farnesyltranstransferase 1) (EC 2.5.1.29) (Geranyltranstransferase 1) (EC 2.5.1.10) (P34802)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heterodimeric geranyl(geranyl)-diphosphate (GPP) synthase large subunit. In vitro, the large subunit catalyzes mainly the trans-addition of the three molecules of IPP onto DMAPP to form geranylgeranyl pyrophosphate while the small subunit alone is inactive. Upon association of the two subunits, the product profile changes and the production of gerany-diphosphate is strongly increased.
Subcellular location: [Isoform 1]: Plastid, chloroplast {ECO:0000269|PubMed:10759500, ECO:0000269|PubMed:27707890}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm {ECO:0000269|PubMed:27707890}.
Interaction partners:
- Geranylgeranyl diphosphate reductase, chloroplastic
- Phytoene synthase 1, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Dehydrodolichyl diphosphate synthase 3
- Isopentenyl phosphate kinase
- Ent-copalyl diphosphate synthase, chloroplastic
- Diphosphomevalonate decarboxylase MVD1, peroxisomal
- Alpha-humulene/
- Diphosphomevalonate decarboxylase MVD2, peroxisomal
- Squalene synthase 1
Sequence:
MASVTLGSWIVVHHHNHHHPSSILTKSRSRSCPITLTKPISFRSKRTVSSSSSIVSSSVVTKEDNLRQSEPSSFDFMSYIITKAELVNKALDSAVPLREPLKIHEAMRYSLLAGGKRVRPVLCIAACELVGGEESTAMPAACAVEMIHTMSLIHDDLPCMDNDDLRRGKPTNHKVFGEDVAVLAGDALLSFAFEHLASATSSDVVSPVRVVRAVGELAKAIGTEGLVAGQVVDISSEGLDLNDVGLEHLEFIHLHKTAALLEASAVLGAIVGGGSDDEIERLRKFARCIGLLFQVVDDILDVTKSSKELGKTAGKDLIADKLTYPKIMGLEKSREFAEKLNREARDQLLGFDSDKVAPLLALANYIAYRQN
Protein: Cytochrome b-c1 complex subunit 9 (Complex III subunit 9) (Complex III subunit X) (Cytochrome c1 non-heme 7 kDa protein) (Ubiquinol-cytochrome c reductase complex 7.2 kDa protein) (Q9UDW1)
Organism: Homo sapiens (Human)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22289}; Single-pass membrane protein {ECO:0000250|UniProtKB:P22289}.
Interaction partners:
- Cytochrome b-c1 complex subunit 6, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 8
- Cytochrome c oxidase subunit 6B1
- NADH dehydrogenase 1 alpha subcomplex subunit 2
- Cytochrome b-c1 complex subunit 10
- Cytochrome c oxidase subunit 7C, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 11
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
Sequence:
MAAATLTSKLYSLLFRRTSTFALTIIVGVMFFERAFDQGADAIYDHINEGKLWKHIKHKYENK
Protein: Lipoxygenase homology domain-containing protein 1 (Q8IVV2)
Organism: Homo sapiens (Human)
Function: Involved in hearing. Required for normal function of hair cells in the inner ear (By similarity).
Subcellular location: Cell projection, stereocilium {ECO:0000250}.
Interaction partners:
- Cytosolic carboxypeptidase 4
- Solute carrier family 4 member 11
- Tissue-type plasminogen activator
- Transmembrane channel-like protein 1
- Myosin-IIIa
- Unconventional myosin-XV
- Collagen alpha-2
- Transmembrane protease serine 3
- Otoferlin
- Protocadherin-15
Sequence:
MMPQKKRRRKKDIDFLALYEAELLNYASEDDEGELEHEYYKARVYEVVTATGDVRGAGTDANVFITLFGENGLSPKLQLTSKSKSAFEKGNVDVFRVRTNNVGLIYKVRIEHDNTGLNASWYLDHVIVTDMKRPHLRYYFNCNNWLSKVEGDRQWCRDLLASFNPMDMPRGNKYEVKVYTGDVIGAGTDADVFINIFGEYGDTGERRLENEKDNFEKGAEDRFILDAPDLGQLMKINVGHNNKGGSAGWFLSQIVIEDIGNKRKYDFPLNRWLALDEDDGKIQRDILVGGAETTAITYIVTVFTGDVRGAGTKSKIYLVMYGARGNKNSGKIFLEGGVFDRGRTDIFHIELAVLLSPLSRVSVGHGNVGVNRGWFCEKVVILCPFTGIQQTFPCSNWLDEKKADGLIERQLYEMVSLRKKRLKKFPWSLWVWTTDLKKAGTNSPIFIQIYGQKGRTDEILLNPNNKWFKPGIIEKFRIELPDLGRFYKIRVWHDKRSSGSGWHLERMTLMNTLNKDKYNFNCNRWLDANEDDNEIVREMTAEGPTVRRIMGMARYHVTVCTGELEGAGTDANVYLCLFGDVGDTGERLLYNCRNNTDLFEKGNADEFTIESVTMRNVRRVRIRHDGKGSGSGWYLDRVLVREEGQPESDNVEFPCLRWLDKDKDDGQLVRELLPSDSSATLKNFRYHISLKTGDVSGASTDSRVYIKLYGDKSDTIKQVLLVSDNNLKDYFERGRVDEFTLETLNIGNINRLVIGHDSTGMHASWFLGSVQIRVPRQGKQYTFPANRWLDKNQADGRLEVELYPSEVVEIQKLVHYEVEIWTGDVGGAGTSARVYMQIYGEKGKTEVLFLSSRSKVFERASKDTFQTDTFTIYAIDLGALTKIRIRHDNTGNRAGWFLDRIDITDMNNEITYYFPCQRWLAVEEDDGQLSRELLPVDESYVLPQSEEGRGGGDNNPLDNLALEQKDKSTTFSVTIKTGVKKNAGTDANVFITLFGTQDDTGMTLLKSSKTNSDKFERDSIEIFTVETLDLGDLWKVRLGHDNTGKAPGWFVDWVEVDAPSLGKCMTFPCGRWLAKNEDDGSIIRDLFHAELQTRLYTPFVPYEITLYTSDVFAAGTDANIFIIIYGCDAVCTQQKYLCTNKREQKQFFERKSASRFIVELEDVGEIIEKIRIGHNNTGMNPGWHCSHVDIRRLLPDKDGAETLTFPCDRWLATSEDDKKTIRELVPYDIFTEKYMKDGSLRQVYKEVEEPLDIVLYSVQIFTGNIPGAGTDAKVYITIYGDLGDTGERYLGKSENRTNKFERGTADTFIIEAADLGVIYKIKLRHDNSKWCADWYVEKVEIWNDTNEDEFLFLCGRWLSLKKEDGRLERLFYEKEYTGDRSSNCSSPADFWEIALSSKMADVDISTVTGPMADYVQEGPIIPYYVSVTTGKHKDAATDSRAFIFLIGEDDERSKRIWLDYPRGKRGFSRGSVEEFYVAGLDVGIIKKIELGHDGASPESCWLVEELCLAVPTQGTKYMLNCNCWLAKDRGDGITSRVFDLLDAMVVNIGVKVLYEMTVWTGDVVGGGTDSNIFMTLYGINGSTEEMQLDKKKARFEREQNDTFIMEILDIAPFTKMRIRIDGLGSRPEWFLERILLKNMNTGDLTMFYYGDWLSQRKGKKTLVCEMCAVIDEEEMMEWTSYTVAVKTSDILGAGTDANVFIIIFGENGDSGTLALKQSANWNKFERNNTDTFNFPDMLSLGHLCKLRVWHDNKGIFPGWHLSYVDVKDNSRDETFHFQCDCWLSKSEGDGQTVRDFACANNKICDELEETTYEIVIETGNGGETRENVWLILEGRKNRSKEFLMENSSRQRAFRKGTTDTFEFDSIYLGDIASLCVGHLAREDRFIPKRELAWHVKTITITEMEYGNVYFFNCDCLIPLKRKRKYFKVFEVTKTTESFASKVQSLVPVKYEVIVTTGYEPGAGTDANVFVTIFGANGDTGKRELKQKMRNLFERGSTDRFFLETLELGELRKVRLEHDSSGYCSGWLVEKVEVTNTSTGVATIFNCGRWLDKKRGDGLTWRDLFPSV
Protein: Zinc finger protein ZOP1 (Zinc-finger and OCRE domain-containing protein 1) (Q7XA66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Nucleic acid-binding protein that promotes Pol IV-dependent small interfering RNA (siRNA) accumulation, DNA methylation and transcriptional silencing. May possess both RNA-directed DNA methylation (RdDM)-dependent and -independent roles in transcriptional silencing. Acts as a pre-mRNA splicing factor that associates with several typical components of the splicing machinery as well as with Pol II.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00130, ECO:0000269|PubMed:23524848, ECO:0000269|PubMed:25684655}. Nucleus, Cajal body {ECO:0000269|PubMed:23524848, ECO:0000269|PubMed:25684655}.
Interaction partners:
- U4/U6 small nuclear ribonucleoprotein Prp31 homolog
- Nuclear protein-like
- Pre-mRNA-splicing factor 38
- Protein STABILIZED1
- Suppressor of mec-8 and unc-52 protein homolog 1
- Protein RDM16
- Suppressor of mec-8 and unc-52 protein homolog 2
- Sm-like protein LSM6A
- Peptidyl-prolyl cis-trans isomerase CYP22
- Sm-like protein LSM4
Sequence:
MTEYWVSQGNKWCEFCKIWIQNNPTSIRNHDLGKRHRECVDKKLTDMRERSAAKDKELKKNEKLLQQIEAKATRSYQKDIATAQQVAKANGAPEDGTSDWMLDSASGYYYNQTNGLHYDSQSGFYYSDSIGHWVTQDEAYAAVKTSSGTKVPLVKKPVSSSGAGPSVGKPPGRLVTASLNPKRAVKGAASSVDLGNNKRKRQDEKPKKVSAEEKAALKAREAARKRVEDREKPLLGLYNRPF
Protein: Lysozyme g (EC 3.2.1.17) (C1BHK0)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MGVGVGVGIGGFITFLTLASCFGDITKVDTSGASEITARQDKLTVQGVDASHKLAEHDLVRMNKYKKLITRVGQKHGLDPAIIAGIISRESRAGAVLDHGWGDHGNGFGLMQVDKRYHKIVGTWDSEEHISQGSEILKEFIRRIQAKFPAWPKEHQLKGGISAYNAGDKNVRTYERMDVGTTGGDYSNDVVARSQWFKRQGY
Protein: 3-beta-hydroxysteroid-Delta(8),Delta(7)-isomerase (EC 5.3.3.5) (Cholestenol Delta-isomerase) (Cholesterol-5,6-epoxide hydrolase subunit EBP) (EC 3.3.2.11) (Delta(8)-Delta(7) sterol isomerase) (D8-D7 sterol isomerase) (Emopamil-binding protein) (P70245)
Organism: Mus musculus (Mouse)
Function: Catalyzes the conversion of Delta(8)-sterols to their corresponding Delta(7)-isomers.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q15125}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q15125}. Nucleus envelope {ECO:0000250|UniProtKB:Q15125}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:Q15125}. Note=During interphase, detected on the endoplasmic reticulum and the nuclear envelope. During mitosis, detected on cytoplasmic vesicles. {ECO:0000250|UniProtKB:Q15125}.
Interaction partners:
- Lathosterol oxidase
- Delta
- Delta
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 7-dehydrocholesterol reductase
- Sterol-4-alpha-carboxylate 3-dehydrogenase, decarboxylating
- Lanosterol synthase
Sequence:
MTTNTVPLHPYWPRHLKLDNFVPNDLPTSHILVGLFSISGGLIVITWLLSSRASVVPLGAGRRLALCWFAVCTFIHLVIEGWFSLYNGILLEDQAFLSQLWKEYSKGDSRYILSDSFVVCMETVTACLWGPLSLWVVIAFLRQQPFRFVLQLVVSMGQIYGDVLYFLTELHEGLQHGEIGHPVYFWFYFVFLNAVWLVIPSILVLDAIKHLTSAQSVLDSKVMKIKSKHN