wanglab/gogpt-training-data huggingface dataset:
Protein: Probable NADPH-dependent quinone reductase tdiC (EC 1.1.1.-) (Terrequinone biosynthesis protein C) (A7XRY6)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Probable NADPH-dependent quinone reductase; part of the gene cluster that mediates the biosynthesis of terrequinone A, an antitumor agent. The first step in the biosynthetic pathway for terrequinone A is formation of indole pyruvic acid (IPA) from L-tryptophan by the aminotransferase tdiD. The nonribosomal peptide synthase tdiA then immediately converts unstable IPA to didemethylasterriquinone D (DDAQ D), via condensation of 2 IPA molecules. The symmetric connectivity of the 2 IPA molecules is thought to arise by head-to-tail dual Claisen condensations facilitated by the TE domain. TdiB then catalyzes reverse prenylation by transferring dimethylallyl diphosphate to carbon atom 2' of DDAQ D, to yield asterriquinone C-1. Finally, tdiC and tdiE enzymes robustly convert asterriquinone C-1 to terrequinone A via a transformation involving regular prenylation at carbon atom 5, which requires elimination of the hydroxy group on C-5.
Interaction partners:
- Aminotransferase tdiD
- Probable methyltransferase tdiE
- Indole prenyltransferase tdiB
Sequence:
MHAALVPTWSSPCPIYTEIPDPGPPPPEQLQLKVLAVGIPRVVRLRARGIHPTAKSASLPYDPSIDGVGIDEQTGIMYYILPLSASCLAEKVNVDRDNLVPLQPGAPKPQPRNGPENGYGIALGDAADHRAETLDPIAIAGLVNPVSSSWMALRTRVDGEITGKTVLVLGATSKSGRAAVLVARFLGANKVIGVARREEGLRSVEGLDGWVTSGDMLPGETGVRFALPDWVGPVHIVLDYVGGSVAAGVLGSAEIEEGRELQYVQVGNLALELGTGEKHMFETLPGHLISRKPICIRGSGMGSFSRRDLVREMPGLVAFLARMKAPFGIASAPMCEVASVWQDEDTKGSRVVIVP
Protein: Replication protein A 70 kDa DNA-binding subunit (RP-A p70) (Replication factor A protein 1) (RF-A protein 1) (Q6NY74)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism. Thereby, it plays an essential role both in DNA replication and the cellular response to DNA damage.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P27694}. Nucleus, PML body {ECO:0000250|UniProtKB:P27694}.
Interaction partners:
- Replication protein A3.
- WRN RecQ-like helicase.
- DNA repair protein RAD52 homolog
- Helicase ATP-binding domain-containing protein.
- FA complementation group M.
- BLM RecQ-like helicase.
- DNA topoisomerase
- Replication factor A protein 2
- RecQ-mediated genome instability protein 1
- DNA-directed primase/polymerase protein
Sequence:
MTVRLSEGAIESLSKGTEVNNPILQCVNIRKIDGGNGVSRFRVMMSDGLHTMSSFMLSTQLNPMAEQNQLATNCVCVLKRSVTNVLKDGRRVVVILDIEVLKSADQMPGKIGDPTPYVEGQSKAPSTAPAPTARPLQPQNGSDGSTYRPSAQSFGKKPMAAPNTPGGSSKVVPIASLNPYQSKWTIRARVTNKSAIRTWSNSRGDGKLFSMELVDESGEIRATGFNNEVDKFFSLIEQGKVFYISKGTLKIANKQFSSLKNDYEMTLNGETSIIPCEDSNDVPMLQCDFVSIADLESREKDTILDVIGVCKNAEDVARIMTKNSREVSKRNIQLIDMSGRVIQLTMWGSDAETFDGSGQPILAIKGARLSDFGGRSLSTLYSSTVMINPDIPEAYKLRGWYDKEGHALDGQSMTELRGPGGGGNTNWKTLAEVKNEHLGHGDKADYFSCIATIVYIRKENCLYQACPSKDCNKKVVDQQNGMFRCEKCDKEFPDFKYRLMLSANIADFGDNQWVTCFQDTAETLLGQNSSYLGQLKDTNEAAFDEVFQHANFNTFVFRNRVKLETYNDESRIKVTVVDAKPVDHREYSKRLIINIRKLAAQ
Protein: Gamma-aminobutyric acid receptor subunit beta (GABA(A) receptor subunit beta) (Protein cyclodiene resistance) (P25123)
Organism: Drosophila melanogaster (Fruit fly)
Function: Gamma-aminobutyric acid (GABA) receptor voltage channel subunit. GABA, an inhibitory neurotransmitter, mediates neuronal inhibition by binding to the GABA receptor and opening an integral chloride channel. Together with glutamate receptor GluClalpha, plays an important role in the visual response by regulating the activity of ON/OFF-selective neurons. Plays a role in promoting sleep and sleep latency by regulating the activity of peptidergic PDF neurons. In large ventral lateral clock neurons, clustering is mediated by Nlg4 and protein levels undergo daily degradation in response to the circadian clock. In neurons in the mushroom bodies, has a role in odor memory acquisition where it inhibits appetitive and aversive olfactory learning, probably upstream of adenylyl cyclase rut and GTPase activating protein Nf1. In male-specific GABAergic neurons, plays a role in inhibiting male aggressive behavior during courtship.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24068821, ECO:0000269|PubMed:29174887}; Multi-pass membrane protein {ECO:0000255}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P15431}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P15431}. Cell projection, dendrite {ECO:0000269|PubMed:18093529}. Cell projection, axon {ECO:0000269|PubMed:18093529, ECO:0000269|PubMed:24068821}. Note=Localizes to large ventral lateral clock neurons axonal varicosities which are synaptic inputs to ventral lateral neuron dendrites. {ECO:0000269|PubMed:24068821}.
Interaction partners:
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor alpha-like
- IP03705p
- Wide awake
- Carboxylic ester hydrolase
- Glutamate-gated chloride channel
- Acetylcholinesterase
- IP12579p
Sequence:
MSDSKMDKLARMAPLPRTPLLTIWLAINMALIAQETGHKRIHTVQAATGGGSMLGDVNISAILDSFSVSYDKRVRPNYGGPPVEVGVTMYVLSISSLSEVKMDFTLDFYFRQFWTDPRLAYRKRPGVETLSVGSEFIKNIWVPDTFFVNEKQSYFHIATTSNEFIRVHHSGSITRSIRLTITASCPMNLQYFPMDRQLCHIEIESFGYTMRDIRYKWNEGPNSVGVSSEVSLPQFKVLGHRQRAMEISLTTGNYSRLACEIQFVRSMGYYLIQIYIPSGLIVIISWVSFWLNRNATPARVALGVTTVLTMTTLMSSTNAALPKISYVKSIDVYLGTCFVMVFASLLEYATVGYMAKRIQMRKQRFMAIQKIAEQKKQQLDGANQQQANPNPNANVGGPGGVGVGPGGPGGPGGGVNVGVGMGMGPEHGHGHGHHAHSHGHPHAPKQTVSNRPIGFSNIQQNVGTRGCSIVGPLFQEVRFKVHDPKAHSKGGTLENTVNGGRGGPQSHGPGPGQGGGPPGGGGGGGGGGGPPEGGGDPEAAVPAHLLHPGKVKKDINKLLGITPSDIDKYSRIVFPVCFVCFNLMYWIIYLHVSDVVADDLVLLGEE
Protein: Brain-specific protein p25 alpha, isoform CRA_b (Fibroblast growth factor-2 repression protein-1) (Tubulin polymerization promoting protein) (cDNA FLJ30358 fis, clone BRACE2007749, highly similar to Tubulin polymerization-promoting protein) (Q4L233)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADKAKPAKAANRTPPKSPGDPSKDRAAKRLSLESEGAGEGAAASPELSALEEAFRRFAVHGDARATGREMHGKNWSKLCKDCQVIDGRNVTVTDVDIVFSKIKGKSCRTITFEQFQEALEELAKKRFKDKSSEEAVREVHRLIEGKAPIISGVTKAISSPTVSRLTDTTKFTGSHKERFDPSGKGKGKAGRVDLVDESGYVSGYKHAGTYDQKVQGGK
Protein: Plasma membrane ascorbate-dependent reductase CYBRD1 (EC 7.2.1.3) (Cytochrome b reductase 1) (Duodenal cytochrome b) (Ferric-chelate reductase 3) (Q53TN4)
Organism: Homo sapiens (Human)
Function: Plasma membrane reductase that uses cytoplasmic ascorbate as an electron donor to reduce extracellular Fe(3+) into Fe(2+). Probably functions in dietary iron absorption at the brush border of duodenal enterocytes by producing Fe(2+), the divalent form of iron that can be transported into enterocytes. It is also able to reduce extracellular monodehydro-L-ascorbate and may be involved in extracellular ascorbate regeneration by erythrocytes in blood. May also act as a ferrireductase in airway epithelial cells (Probable). May also function as a cupric transmembrane reductase (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:17068337}; Multi-pass membrane protein {ECO:0000269|PubMed:30272000}. Apical cell membrane {ECO:0000305|PubMed:12949720}; Multi-pass membrane protein {ECO:0000269|PubMed:30272000}. Note=Localized at the brush border of duodenal cells. {ECO:0000269|PubMed:12949720}.
Interaction partners:
- Natural resistance-associated macrophage protein 2
- Ferroportin
- Hepcidin
- Hereditary hemochromatosis protein
- Transferrin receptor protein 1
- Hephaestin
- Transferrin receptor protein 2
- Zinc transporter ZIP1
- Hemojuvelin
- Metalloreductase STEAP3
Sequence:
MAMEGYWRFLALLGSALLVGFLSVIFALVWVLHYREGLGWDGSALEFNWHPVLMVTGFVFIQGIAIIVYRLPWTWKCSKLLMKSIHAGLNAVAAILAIISVVAVFENHNVNNIANMYSLHSWVGLIAVICYLLQLLSGFSVFLLPWAPLSLRAFLMPIHVYSGIVIFGTVIATALMGLTEKLIFSLRDPAYSTFPPEGVFVNTLGLLILVFGALIFWIVTRPQWKRPKEPNSTILHPNGGTEQGARGSMPAYSGNNMDKSDSELNSEVAARKRNLALDEAGQRSTM
Protein: V-type proton ATPase subunit (A0A1D8PKX3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- V-type proton ATPase subunit a
- V-type proton ATPase subunit a
- H
- V-type proton ATPase subunit B
- V-type proton ATPase subunit D
- V-type proton ATPase subunit H
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit F
- H
- V-type proton ATPase subunit C
Sequence:
MEGLFFNIDYGYLEGVVRGYKSGLLTSNQYVNLTQCDNLEDLKLQLSSTDYGNFLANYSGPLSTTVIQENLTKKLFQQYQYIQSQSSGKLTKFMDFINYGYMIDNVILMITGTLHERDKSEILRKTNALGWFDTLPTLSIATDIESLYSTVLIDTPLAPFFKNCVSADDLDDLNIEIIRNRLYKNYLEGFVDWCDKNLDGPDKEIMERLLTLEADKRVINIALNSLNNPDLSPEDKLSLFPSHGKLYPTYHLELSQVDDVEQLKSIVELVGDYKDIFSETNENLKSLGDWFYYLEMQLCRNAFTQQFTLASVYAWLKSKEQEIRNITWIAECIAQNQKNRIESYIAVY
Protein: Natural resistance-associated macrophage protein 1 (NRAMP 1) (Solute carrier family 11 member 1) (O77741)
Organism: Sus scrofa (Pig)
Function: Divalent transition metal (iron and manganese) transporter involved in iron metabolism and host resistance to certain pathogens. Macrophage-specific membrane transport function. Controls natural resistance to infection with intracellular parasites. Pathogen resistance involves sequestration of Fe(2+) and Mn(2+), cofactors of both prokaryotic and eukaryotic catalases and superoxide dismutases, not only to protect the macrophage against its own generation of reactive oxygen species, but to deny the cations to the pathogen for synthesis of its protective enzymes (By similarity).
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:P49279}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000250|UniProtKB:P49279}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Solute carrier family 11 member 2
- Protein S100-A12
Sequence:
MTGDTDPPKQSRTQYGSISSSPSPGPPQVPPGGTYLSEKIPIPNAEPGTFSLRKLWAFTGPGFLMSIAYLDPGNIQSDLQAGAVAGFKLLWVLLWATVLGLLCQRLAARLGVVTGKDLGEICHLYYPKVPRTLLWLNMELAIVGSDMQEVIGTAIAFNLLSAGRIPLWGGVLITVVDTFFFLYLNNYGLRKLEAFFAFLIAIMAFTFGYEYVVARPAQGALLRGLFLPSCSGCGQPELLQAVGIVGAIIMPHNIYLHSALVKSREVDRTRREDIREANMYFLIESTIALFVSFFINLFVMAVFGQAFYQQTNQAAFNICANSSLHDYAKIFPRNNLTVAVDFYQGGVILGCLFGPAALYIWAVGLLAAGQSSTMTGTYAGQFVMEGFLKLRWSRFARLLLTRSCAILPALLVAVFKELQDLSSLNDLLNVLQSLLLPFAVLPILTFTSMPALMQEFASGRVNKVITSSIMLLVCAINFYFLVSYLPSLPHPAYFGLVALLAVIYLGLTTYLVWTCLIAHGATLLVHSSHQHFLYGLLE
Protein: Inter-alpha-trypsin inhibitor heavy chain H5 (ITI heavy chain H5) (ITI-HC5) (Inter-alpha-inhibitor heavy chain 5) (Q86UX2)
Organism: Homo sapiens (Human)
Function: May act as a tumor suppressor.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Prolargin
Sequence:
MLLLLGLCLGLSLCVGSQEEAQSWGHSSEQDGLRVPRQVRLLQRLKTKPLMTEFSVKSTIISRYAFTTVSCRMLNRASEDQDIEFQMQIPAAAFITNFTMLIGDKVYQGEITEREKKSGDRVKEKRNKTTEENGEKGTEIFRASAVIPSKDKAAFFLSYEELLQRRLGKYEHSISVRPQQLSGRLSVDVNILESAGIASLEVLPLHNSRQRGSGRGEDDSGPPPSTVINQNETFANIIFKPTVVQQARIAQNGILGDFIIRYDVNREQSIGDIQVLNGYFVHYFAPKDLPPLPKNVVFVLDSSASMVGTKLRQTKDALFTILHDLRPQDRFSIIGFSNRIKVWKDHLISVTPDSIRDGKVYIHHMSPTGGTDINGALQRAIRLLNKYVAHSGIGDRSVSLIVFLTDGKPTVGETHTLKILNNTREAARGQVCIFTIGIGNDVDFRLLEKLSLENCGLTRRVHEEEDAGSQLIGFYDEIRTPLLSDIRIDYPPSSVVQATKTLFPNYFNGSEIIIAGKLVDRKLDHLHVEVTASNSKKFIILKTDVPVRPQKAGKDVTGSPRPGGDGEGDTNHIERLWSYLTTKELLSSWLQSDDEPEKERLRQRAQALAVSYRFLTPFTSMKLRGPVPRMDGLEEAHGMSAAMGPEPVVQSVRGAGTQPGPLLKKPYQPRIKISKTSVDGDPHFVVDFPLSRLTVCFNIDGQPGDILRLVSDHRDSGVTVNGELIGAPAPPNGHKKQRTYLRTITILINKPERSYLEITPSRVILDGGDRLVLPCNQSVVVGSWGLEVSVSANANVTVTIQGSIAFVILIHLYKKPAPFQRHHLGFYIANSEGLSSNCHGLLGQFLNQDARLTEDPAGPSQNLTHPLLLQVGEGPEAVLTVKGHQVPVVWKQRKIYNGEEQIDCWFARNNAAKLIDGEYKDYLAFHPFDTGMTLGQGMSREL
Protein: Eukaryotic peptide chain release factor GTP-binding subunit (ERF-3) (ERF2) (Polypeptide release factor 3) (Translation release factor 3) (Q59YE8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Translation termination factor eRF1
- Chaperone ATPase
- Polyadenylate-binding protein, cytoplasmic and nuclear
- ATP-dependent RNA helicase
- Adenylyl-sulfate kinase
- Swi1p
- Small ribosomal subunit protein uS3
- Translation initiation factor RLI1
- Ssz1p
- Elf1p
Sequence:
MSDQQNTQDQLSGAMANASLNGDQSKQQQQQQQQQQQNYYNPNAAQSFVPQGGYQQFQQFQPQQQQQQYGGYNQYNQYQGGYQQNYNNRGGYQQGYNNRGGYQQNYNNRGGYQGYNQNQQYGGYQQYNSQPQQQQQQQSQGMSLADFQKQKTEQQASLNKPAVKKTLKLAGSSGIKLANATKKVDTTSKPQSKESSPAPAPAPAAFASQEEKKEEKEAAAATPETKKETSAPAETKKEATPTPAAKKESTPTPATATKKESTPVSNSASVATADALVKEQEDEIDEEVVKDMFGGKDHVSIIFMGHVDAGKSTMGGNILYLTGSVDKRTVEKYEREAKDAGRQGWYLSWVMDTNKEERNDGKTIEVGKAYFETDKRRYTILDAPGHKMYVSEMIGGASQADVGILVISARKGEYETGFEKGGQTREHALLAKTQGVNKIIVVVNKMDDSTVGWSKERYQECTTKLGAFLKGIGYAKDDIIYMPVSGYTGAGLKDRVDPKDCPWYDGPSLLEYLDNMDTMNRKINGPFMMPVSGKMKDLGTIVEGKIESGHVKKGTNLIMMPNKTPIEVLTIFNETEQECDTAFSGEQVRLKIKGIEEEDLQPGYVLTSPKNPVKTVTRFEAQIAIVELKSILSNGFSCVMHLHTAIEEVKFIELKHKLEKGTNRKSKKPPAFAKKGMKIIAILEVGELVCAETYKDYPQLGRFTLRDQGTTIAIGKITKLL
Protein: Deca-heme c-type cytochrome (O87540)
Organism: Shewanella putrefaciens (Pseudomonas putrefaciens)
Interaction partners:
Sequence:
MMNAQKSKIALLLAASAVTMALTGCGGSSGNNGNDGSDGGEPAGSIQTLNLDITKVSYENGAPMVTVFATNEADMPVIGLANLEIKKALQLIPEGATGPGNSANWQGLGSSKSYVDNKNGSYTFKFDAFDSNKVFNAQLTQRFNVVSAAGKLADGTTVPVAEMVEDFDGQGNAPQYTKNIVSHEVCASCHVEGEKIYHQATEVETCISCHTQEFADGRGKPHVAFSHLIHNVHNANKAWGKDNKIPTVAQNIVQDNCQVCHVESDMLTEAKNWSRIPTMEVCSSCHVDIDFAAGKGHSQQLDNSNCIACHNSDWTAELHTAKTTATKNLINQYGIETTSTINTETKAATISVQVVDANGTAVDLKTILPKVQRLEIITNVGPNNATLGYSGKDSIFAIKNGALDPKATINDAGKLVYTTTKDLKLGQNGADSDTAFSFVGWSMCSSEGKFVDCADPAFDGVDVTKYTGMKADLAFATLSGKAPSTRHVDSVNMTACANCHTAEFEIHKGKQHAGFVMTEQLSHTQDANGKAIVGLDACVTCHTPDGTYSFANRGALELKLHKKHVEDAYGLIGGNCASCHSDFNLESFKKKGALNTAAAADKTGLYSTPITATCTTCHTVGSQYMVHTKETLESFGAVVDGTKDDATSAAQSETCFYCHTPTVADHTKVKM
Protein: Hydroxymethylglutaryl-CoA synthase, mitochondrial (HMG-CoA synthase) (EC 2.3.3.10) (3-hydroxy-3-methylglutaryl coenzyme A synthase) (P54869)
Organism: Mus musculus (Mouse)
Function: Catalyzes the first irreversible step in ketogenesis, condensing acetyl-CoA to acetoacetyl-CoA to form HMG-CoA, which is converted by HMG-CoA reductase (HMGCR) into mevalonate.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P22791}.
Interaction partners:
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Acetyl-CoA acetyltransferase, mitochondrial
- 3-ketoacyl-CoA thiolase B, peroxisomal
- 3-ketoacyl-CoA thiolase A, peroxisomal
- Acetyl-CoA acetyltransferase, cytosolic
- Acetyl-Coenzyme A acetyltransferase 3
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
- Succinyl-CoA:3-ketoacid coenzyme A transferase 1, mitochondrial
Sequence:
MQRLLAPARRVLQVKRAMQETSLTPAHLLSAAQQRFSTIPPAPLAKTDTWPKDVGILALEVYFPAQYVDQTDLEKFNNVEAGKYTVGLGQTRMGFCSVQEDINSLCLTVVQRLMERTKLPWDAVGRLEVGTETIIDKSKAVKTVLMELFQDSGNTDIEGIDTTNACYGGTASLFNAANWMESSYWDGRYALVVCGDIAVYPSGNARPTGGAGAVAMLIGPKAPLVLEQGLRGTHMENAYDFYKPNLASEYPLVDGKLSIQCYLRALDRCYAAYRKKIQNQWKQAGNNQPFTLDDVQYMIFHTPFCKMVQKSLARLMFNDFLSSSSDKQNNLYKGLEAFRGLKLEETYTNKDVDKALLKASLDMFNQKTKASLYLSTNNGNMYTSSLYGCLASLLSHHSAQELAGSRIGAFSYGSGLAASFFSFRVSKDASPGSPLEKLVSSVSDLPKRLDSRRRMSPEEFTEIMNQREQFYHKVNFSPPGDTSNLFPGTWYLERVDEMHRRKYARCPV
Protein: Uncharacterized protein (Q72ER8)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Interaction partners:
- Large ribosomal subunit protein uL4
Sequence:
MLKHFEGLGDKWRALVENPDETVKGLVQTIANEGGTREAWQSHTPDGHTVLMAWPATEPCRAGLIIRGDQNGENYQPVSALPLLEGLENELEVTEVHPWGNDAEGEIAACRAGDDSIWFYDPLLYRDRWSCIVGQKQVFTLSALAYALRPATRDSIQVKGGPQFDSYAKAYVDKNPGVDPASIPPLTLPLKGARIMQQYVNASEYQIRVPVEEVATCQFNGEKVFMLTVSLAGKDDKALRAMLYVAERTLGGFEPKAGDDIEAIVWLQGRLVD
Protein: Cytochrome P450 705A22 (EC 1.14.-.-) (Protein GRAVITY PERSISTENCE SIGNAL 1) (Q9LJY5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in the gravitropic response of the inflorescence stems and roots. May affect the synthesis of flavonols that have a role in regulating auxin transport.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEAVISFDFQNCFIFILIFLLTFLCFFFFFKKPKDSRVNFDLPPSPPSLPIIGHVHLLLSTLTHKSLQKLSSRYGPLLYLRIFNVPIILVSSASVAYEIFRTQDVNISSRGVTAVDESLVFGSSSFVTAPYGDYWKFMKKLTVMKLLGPQAQEQSRDIRADDIKRFCRNLLDKARKKESVEIGKEAMNLMNNILCKMSMGRSFSEENGETEKLRGLVTESIGLMKKMFLAVLLRRQLQKLGISLFKKDIMGVSNKFDVLLEKVLVEHREKPEKDQGTVMLDVLLAAYGDENAEYKITKNHIKAFFVDLFIGATDTSVQTIQWTMAEIMNNTHILERMREEIDSVVGKSRLIQETDLPNLPYLHAVIKEALRLHPPGPLLPREFQQGCKIGGFYIPEKTTLLINAYVVMRDPNVWEDPEEFKPERFLASSRSGQEDERREQALKFLPFGSGRRGCPGSNLAYMIVGSAIGMMVQCFDWRIEGEKVNMKEAVKGTILTMAHPLKLTPVTRQPPLTWI
Protein: N-alpha-acetyltransferase 16, NatA auxiliary subunit (NMDA receptor-regulated 1-like protein) (NARG1-like protein) (Q6N069)
Organism: Homo sapiens (Human)
Function: Auxillary subunit of the N-terminal acetyltransferase A (NatA) complex which displays alpha (N-terminal) acetyltransferase activity.
Interaction partners:
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 11
- N-alpha-acetyltransferase 50
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- Huntingtin-interacting protein K
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 25, NatB auxiliary subunit
Sequence:
MPNVLLPPKESNLFKRILKCYEQKQYKNGLKFCKMILSNPKFAEHGETLAMKGLTLNCLGKKEEAYEFVRKGLRNDVKSHVCWHVYGLLQRSDKKYDEAIKCYRNALKLDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPTQRASWIGYAIAYHLLKDYDMALKLLEEFRQTQQVPPNKIDYEYSELILYQNQVMREADLLQESLEHIEMYEKQICDKLLVEEIKGEILLKLGRLKEASEVFKNLIDRNAENWCYYEGLEKALQISTLEERLQIYEEISKQHPKAITPRRLPLTLVPGERFRELMDKFLRVNFSKGCPPLFTTLKSLYYNTEKVSIIQELVTNYEASLKTCDFFSPYENGEKEPPTTLLWVQYFLAQHFDKLGQYSLALDYINAAIASTPTLIELFYMKAKIYKHIGNLKEAAKWMDEAQSLDTADRFINSKCAKYMLRANMIKEAEEMCSKFTREGTSAMENLNEMQCMWFQTECISAYQRLGRYGDALKKCHEVERHFFEITDDQFDFHTYCMRKMTLRAYVDLLRLEDILRRHAFYFKAARSAIEIYLKLYDNPLTNESKQQEINSENLSAKELKKMLSKQRRAQKKAKLEEERKHAERERQQKNQKKKRDEEEEEASGLKEELIPEKLERVENPLEEAVKFLIPLKNLVADNIDTHLLAFEIYFRKGKFLLMLQSVKRAFAINSNNPWLHECLIRFSKSVSNHSNLPDIVSKVLSQEMQKIFVKKDLESFNEDFLKRNATSLQHLLSGAKMMYFLDKSRQEKAIAIATRLDETIKDKDVKTLIKVSEALLDGSFGNCSSQYEEYRMACHNLLPFTSAFLPAVNEVDNPNVALNHTANYDVLANEI
Protein: Creatine kinase U-type, mitochondrial (EC 2.7.3.2) (Acidic-type mitochondrial creatine kinase) (Mia-CK) (Ubiquitous mitochondrial creatine kinase) (U-MtCK) (P30275)
Organism: Mus musculus (Mouse)
Function: Reversibly catalyzes the transfer of phosphate between ATP and various phosphogens (e.g. creatine phosphate). Creatine kinase isoenzymes play a central role in energy transduction in tissues with large, fluctuating energy demands, such as skeletal muscle, heart, brain and spermatozoa.
Subcellular location: Mitochondrion inner membrane; Peripheral membrane protein; Intermembrane side.
Interaction partners:
- Non-selective voltage-gated ion channel VDAC1
- Non-selective voltage-gated ion channel VDAC2
- ADP/ATP translocase 1
- Creatine kinase S-type, mitochondrial
- Non-selective voltage-gated ion channel VDAC3
- Ankyrin repeat and SOCS box protein 9
- Glycine amidinotransferase, mitochondrial
- Mitochondrial disaggregase
- ADP/ATP translocase 2
Sequence:
MAGPFSRLLSARPGLRLLALAGAGSLTAGILLRPESVGAAAAERRRLYPPSAEYPDLRKHNNCMASHLTPAVYARLCDKTTPTGWTLDQCIQTGVDNPGHPFIKTVGMVAGDEETYEVFAELFDPVIQERHNGYDPRTMKHTTDLDASKIRSGYFDERYVLSSRVRTGRSIRGLSLPPACTRAERREVERVVVDALSGLKGDLAGRYYRLSEMTEAEQQQLIDDHFLFDKPVSPLLTAAGMARDWPDARGIWHNNEKSFLIWVNEEDHTRVISMEKGGNMKRVFERFCRGLKEVEKLIQERGWEFMWNERLGYILTCPSNLGTGLRAGVHIKLPLLSKDNRFPKILENLRLQKRGTGGVDTAATGSVFDISNLDRLGKSEVELVQLVIDGVNYLIDCERRLERGQDIRIPPPLVHSKH
Protein: Hit locus orf4 (Q6MRH6)
Organism: Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIMB 9529 / HD100)
Interaction partners:
- Flp pilus assembly protein TadA
- TadB protein
- Flp2 protein
- Similar to cell wall-associated protein wapA
- Putative pilus assembly transmembrane protein
Sequence:
MKRLLVLSILLTLGFSFAGTASADENANRPVNPGEDPNEAFRSTPFEATTSALGDCRECIAYRTGATTGKGSRRHDDTVSREIKGSSATPGGSEKAGTGRQ
Protein: TonB-dependent receptor (E0SIE9)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell outer membrane {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004571, ECO:0000256|PROSITE-ProRule:PRU01360}.
Interaction partners:
- Achromobactin-binding periplasmic protein
- Putative AcsD
Sequence:
MKVRALYALTPLFLFAQANAADSTNKNDNEMVVTASRTDTEKKDSPQVVTIITKEQIEQQRQITSDSSQILSNLLPSMAPSRQKMSGSGETFRGRAPLILVDGIPQSNPLRPTGREMHTIDFAMVDRIEVIHGASASNGIGATGGVINIITRRPEPGSFNQHFSVETTSPTKVSSDSMSYKTTYGFSGREEYLDYLFSVSYEDQGLFLDGKDRPIGVDNTQGDLMDSRAYDIMAKVGYWLDNDQRIQFSLNRYQIKGKMNYLGVTGDRNNGIAATSVSGRPIGDAPMNSVWSTSATYDNYNLAGMKLNSLVYYQNYESLFGADNSGSFQDISIAPRNQLYDQSRVTSSRYGSKVALTKDDIWDDYLKATVGFDTLFDTGKQDLWLTKRVYAPQMKYTDLSPFMQFDIQPIESLKITTGVRYEYARLDIDSFRTVAASTVSAPNNSVDVQGGRLSFNKTLYNVGAVWTTPYQPLSLFANYSQGFGIPDVGRTLRSIRTAGQSVSMLQLEPIVTDNVETGFRIQKDPVEFELSYYRSTSKLGERVVDVNGTFQSERQKTRIDGIETSLGYKVNDDHRLKFGYSHIQGWFDNDGNGSLDSKLDGLNIPPDRLTASWSANWTPQWSSFIQANYAFDRIMDNRQMDFNGYVLFDAAVGYKLPKGKINLAVSNLFDKEYITYYSQSGNVSPLRYFSGRGRTVTLGYSVDF
Protein: Glucoside xylosyltransferase 1 (EC 2.4.2.42) (Glycosyltransferase 8 domain-containing protein 3) (Q4G148)
Organism: Homo sapiens (Human)
Function: Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose.
Subcellular location: Membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- UDP-glucose:glycoprotein glucosyltransferase 1
- Glucoside xylosyltransferase 2
- Coagulation factor VII
- Protein O-glucosyltransferase 1
Sequence:
MRRYLRVVVLCVACGFCSLLYAFSQLAVSLEEGTGGGGGKPQAAVASWLAGGGRGAVRGAGVAGPAAHPGVSDRCKDFSLCYWNPYWMLPSDVCGMNCFWEAAFRYSLKIQPVEKMHLAVVACGERLEETMTMLKSAIIFSIKPLQFHIFAEDQLHHSFKGRLDNWSFLQTFNYTLYPITFPSENAAEWKKLFKPCASQRLFLPLILKEVDSLLYVDTDILFLRPVDDIWSLLKKFNSTQIAAMAPEHEEPRIGWYNRFARHPYYGKTGVNSGVMLMNMTRMRRKYFKNDMTTVRLQWGDILMPLLKKYKLNITWGDQDLLNIVFFHNPESLFVFPCQWNYRPDHCIYGSNCQEAEEGGIFILHGNRGVYHDDKQPAFRAVYEALRNCSFEDDNIRSLLKPLELELQKTVHTYCGKIYKIFIKQLAKSVRDRYARSPKEK
Protein: Innexin-14 (Protein opu-14) (O62136)
Organism: Caenorhabditis elegans
Function: Structural component of the gap junctions.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00351}. Cell junction, gap junction {ECO:0000250}.
Interaction partners:
- EF-hand domain-containing protein
- PUM-HD domain-containing protein
- C-type lectin domain-containing protein 88
- Innexin
- Innexin
- F-box domain-containing protein
- Innexin-8
Sequence:
MIWEIPIIGDFITKPFKAAKLYEFYDRLHLFTVYLLGFFVLLTGAKQHFGNPIDCMLPKQHDDLKSWRDYIHNFCLFYGTFRYDVSNGTSEFGSYTEDASVNYYQWVPFFFAFQVCCFLLPFWCWAYMQKLIYIDMAFIVDYSGKINSEKTFEKTKEKVDRIVNYMHDHFKFRRAHKMGYLSWITFNSAFPSVLYSLTKLFFITNVIIQVNLVCKFLDVDSWTWGFDLLGKFIHPTPRAPEFSSFSDKQRFAAILTDGSYNRFQYFPILVGCEYQLQESVSNFVNHKAQCIIPMNVINEKIFIGLYFWLLVLTALSVIGTVKWILRIKSKKLNEVMIYKLIKKSLEREPFDSNIHDHRYNFVHKYLCADGILLIYFMMDTNGFLKTEEVIGALFKKYCSDAGLEPLQTAPTLTSSPRDLAYSETNYGFAAPQKI