wanglab/gogpt-training-data huggingface dataset:
Protein: 3-ketoacyl-CoA synthase 19 (KCS-19) (EC 2.3.1.199) (Very long-chain fatty acid condensing enzyme 19) (VLCFA condensing enzyme 19) (Q9LZ72)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Very-long-chain 3-oxoacyl-CoA reductase 1
- Protein MAINTENANCE OF MERISTEMS
- Very-long-chain 3-oxoacyl-CoA reductase-like protein At1g24470
- Oleosin family protein
- Oleosin family protein
Sequence:
MELFSLSSLLLLSTLFVFYIFKFVFKRRNQRNCYMLHYECYKGMEERKLDTETCAKVVQRNKNLGLEEYRFLLRTMASSGIGEETYGPRNVLEGREDSPTLLDAHSEMDEIMFDTLDKLFHKTKGSISPSDIDILVVNVSLFAPSPSLTSRVINRYKMREDIKSYNLSGLGCSASVISIDIVQRMFETRENALALVVSTETMGPHWYCGKDRSMMLSNCLFRAGGSSVLLTNAARFKNQALMKLVTVVRAHVGSDDEAYSCCIQMEDRDGHPGFLLTKYLKKAAARALTKNLQVLLPRVLPVKELIRYAIVRALKRRTSAKREPASSGIGLNLKTGLQHFCIHPGGRAIIEGVGKSLGLTEFDIEPARMALHRFGNTSSGGLWYVLGYMEAKNRLKKGEKILMMSMGAGFESNNCVWEVLKDLDDKNVWEDSVDRYPELSRIPNPFVEKYDWINDDTMSFVRVD
Protein: Microtubule-associated tumor suppressor candidate 2 (Cardiac zipper protein) (Microtubule plus-end tracking protein TIP150) (Tracking protein of 150 kDa) (Q5JR59)
Organism: Homo sapiens (Human)
Function: Binds microtubules. Together with MAPRE1 may target the microtubule depolymerase KIF2C to the plus-end of microtubules. May regulate the dynamics of microtubules at their growing distal tip.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:19543227}. Note=Associated with the microtubule network at the growing distal tip (the plus-end) of microtubules.
Interaction partners:
- Cytotoxic T-lymphocyte protein 4
- Programmed cell death 1 ligand 1
- Microtubule-associated protein RP/EB family member 1
- Programmed cell death protein 1
- Hepatitis A virus cellular receptor 2
- T-cell surface glycoprotein CD4
- Kinesin-like protein KIF2C
- T-cell immunoreceptor with Ig and ITIM domains
- T-cell surface glycoprotein CD8 alpha chain
- Lymphocyte activation gene 3 protein
Sequence:
MSVPVAPKKSCYTQLRDNRNAARNNNESILSLGDTNANQIMLEVSSSHDESKTCDLGDEIGNTNSSEPENRTHFHKEFHQLQGFGKGSQAGSASLKDFRLSSTIQRELNEEHTVERGTDSLQTTRSIQGPSLSSWRNVMSEASLDVLAKRDAEIPRHVPKDKLAKTLDNEELRRHSLERASSSVAAVGSLTPQHPQPLSLDSREARGQIPGGGEGPQKTLPDHAVPAAFPATDSTSEGKSVRHPKPSTSESKQSTPSETQTVGAHVLQVCSEHTSHSAHPEPALNLTLASKEIPSKLEAQLGQGKGEAKLDLKYVPPRRVEQEGKAAQEGYLGCHKEENLSALEGRDPCGEAHPEATDALGHLLNSDLHHLGVGRGNCEEKRGVNPGEQDSLHTTPKQGSASLGGADNQPTGKISPCAGEKLGERTSSSFSPGDSHVAFIPNNLTDSKPLDVIEEERRLGSGNKDSVMVLVFNPSVGENKTEVPEPLDPQSGRSEARESKEVTTSVAENRNLLENADKIESTSARADSVLNIPAPLHPETTVNMTYQPTTPSSSFQDVSVFGMDAGSPLVVPPPTDSARLLNTSPKVPDKNTCPSGIPKPVFTHSKDTPSSQEGMENYQVEKTEERTETKPIIMPKPKHVRPKIITYIRRNPQALGQVDASLVPVGLPYAPPTCTMPLPHEEKAAGGDLKPSANLYEKFKPDLQKPRVFSSGLMVSGIKPPGHPFSQMSEKFLQEVTDHPGKEEFCSPPYAHYEVPPTFYRSAMLLKPQLGLGAMSRLPSAKSRILIASQRSSASAIHPPGPITTATSLYSSDPSADLKKASSSNAAKSNLPKSGLRPPGYSRLPAAKLAAFGFVRSSSVSSVSSTQSGDSAQPEQGRPATRSTFGNEEQPVLKASLPSKDTPKGAGRVAPPASSSVTAPRRSLLPAPKSTSTPAGTKKDAQKDQDTNKPAVSSPKRVAASTTKLHSPGYPKQRTAAARNGFPPKPDPQAREAERQLVLRLKERCEQQTRQLGVAQGELKRAICGFDALAVATQHFFRKNESALVKEKELSIELANIRDEVAFHTAKCEKLQKEKEELERRFEDEVKRLGWQQQAELQELEERLQLQFEAEMARLQEEHGDQLLSIRCQHQEQVEDLTASHDAALLEMENNHTVAITILQDDHDHKVQELMSTHELEKKELEENFEKLRLSLQDQVDTLTFQSQSLRDRARRFEEALRKNTEEQLEIALAPYQHLEEDMKSLKQVLEMKNQQIHEQEKKILELEKLAEKNIILEEKIQVLQQQNEDLKARIDQNTVVTRQLSEENANLQEYVEKETQEKKRLSRTNEELLWKLQTGDPTSPIKLSPTSPVYRGSSSGPSSPARVSTTPR
Protein: Odorant-binding protein 59a (Q86BF9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant-binding protein required for hygrotaxis behavior in humidity-detecting sensilla.
Subcellular location: Secreted {ECO:0000269|PubMed:30230472}.
Interaction partners:
- General odorant-binding protein 84a
- General odorant-binding protein 83a
- General odorant-binding protein 28a
- Odorant-binding protein 73a, isoform B
- General odorant-binding protein lush
- General odorant-binding protein 19a
Sequence:
MKQLIFLLICLSCGTCSIYALKCRSQEGLSEAELKRTVRNCMHRQDEDEDRGRGGQGRQGNGYEYGYGMDHDQEEQDRNPGNRGGYGNRRQRGLRQSDGRNHTSNDGGQCVAQCFFEEMNMVDGNGMPDRRKVSYLLTKDLRDRELRNFFTDTVQQCFRYLESNGRGRHHKCSAARELVKCMSEYAKAQCEDWEEHGNMLFN
Protein: Solute carrier family 2, facilitated glucose transporter member 12 (Glucose transporter type 12) (GLUT-12) (Q6NWF1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Insulin-regulated facilitative glucose transporter.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8BFW9}; Multi-pass membrane protein {ECO:0000255}. Endomembrane system {ECO:0000250|UniProtKB:Q5J316}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q8TD20}. Note=Localizes primarily perinuclear region in the absence of insulin. {ECO:0000250|UniProtKB:Q8TD20}.
Interaction partners:
- Protein FAM110B
- Na
- Rh family, C glycoprotein,-like 1
Sequence:
MDAPEESIRMTSDPQSKIYVQNPDTHIHLEQGPSAKSGNGRALVLCSVSVACLSGLLMGYEMSLISGALLQLRDVLTLSCPEQEQVVGSLLLGAFLLSLGGGTILDHYGRRFTIILTALLCVLGTLLSVCVVSFWALVVGRMLVGMSVALSGTASCLYAAEVAPAAWRGRCVCVYELMVVLGMLLGFGLSWAFAGVPDGWRFTFGGALLPALLQAGVMPLLPDSPRFLLAQQREKEAHATLLRLRAGIKEVEPVEDELRAIRLAMGAERLHGFLDLFQSRDNMLQRLLVGAALVFLQQATGQPNILAYASTVLSSVGFHGNEAATLASTGFGVVKVGGTIPAIFLVDKVGPKALLCVGVVVMMLSTATLGAITMQSRTHVSSLCRGPGNTANFTLFETGDETDIQTNTPLGLYQPQNKLKTNTFLTSINDTREHWILNHTYNHRTALMETAELSKKDSAKIALQSLHEVSPSLKWISLVSLLVYVAGFSISLGPMVHVVLSAIFPTGIRGKAVSVISAFNWATNLLISMTFLTLTERIGLPTVIFSYSAMSFLLVVFVIVFVPETKGRSLEQISKELAMKNHLRGTLLCHRRKHKATAQPSQEEKALATV
Protein: Adenylate isopentenyltransferase 7, mitochondrial (AtIPT7) (EC 2.5.1.112) (Adenylate dimethylallyltransferase 7) (Cytokinin synthase 7) (Q94ID1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in cytokinin biosynthesis. Catalyzes the transfer of an isopentenyl group from dimethylallyl diphosphate (DMAPP) to ATP and ADP.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14726522}.
Interaction partners:
- Cytokinin hydroxylase
- Cytokinin hydroxylase
- Isopentenyl-diphosphate Delta-isomerase II, chloroplastic
- Isopentenyl-diphosphate Delta-isomerase I, chloroplastic
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, chloroplastic
- Cytokinin dehydrogenase 1
- Cytokinin dehydrogenase 5
- Cytokinin dehydrogenase 3
- Cytokinin dehydrogenase 7
- Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG4
Sequence:
MKFSISSLKQVQPILCFKNKLSKVNVNSFLHPKEKVIFVMGATGSGKSRLAIDLATRFQGEIINSDKIQLYKGLDVLTNKVTPKECRGVPHHLLGVFDSEAGNLTATQYSRLASQAISKLSANNKLPIVAGGSNSYIEALVNHSSGFLLNNYDCCFIWVDVSLPVLNSFVSKRVDRMMEAGLLEEVREVFNPKANYSVGIRRAIGVPELHEYLRNESLVDRATKSKMLDVAVKNIKKNTEILACRQLKKIQRLHKKWKMSMHRVDATEVFLKRNVEEQDEAWENLVARPSERIVDKFYNNNNQLKNDDVEHCLAASYGGGSGSRAHNMI
Protein: Neuronal acetylcholine receptor subunit alpha-10 (Nicotinic acetylcholine receptor subunit alpha-10) (NACHR alpha-10) (Q9JLB5)
Organism: Rattus norvegicus (Rat)
Function: Ionotropic receptor with a probable role in the modulation of auditory stimuli. Agonist binding may induce an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is permeable to a range of divalent cations including calcium, the influx of which may activate a potassium current which hyperpolarizes the cell membrane. In the ear, this leads to a reduction in basilar membrane motion, altering the activity of auditory nerve fibers and reducing the range of dynamic hearing. This may protect against acoustic trauma.
Subcellular location: Synaptic cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:11248107, ECO:0000269|PubMed:12117536}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neuronal acetylcholine receptor subunit alpha-9
- Acetylcholine receptor subunit alpha
- Glutaredoxin and cysteine rich domain containing 2
- Neuronal acetylcholine receptor subunit alpha-5
- Stereocilin
Sequence:
MGTRSHYLDLGFLLLLFLPAECLGAEGRLAHKLFRDLFANYTSALRPVADTDQTLNVTLEVTLSQIIDMDERNQVLTLYLWIRQEWTDAYLHWDPKAYGDLDAIRIPSRLVWRPDIVLYNKADTQPPASASTNVVVRHDGAVRWDAPAITRSSCRVDVSAFPFDAQRCGLTFGSWTHGGHQLDVRPRGTSASLADFVENVEWRVLGMPARRRVLTYGCCSEPYPDVTFTLLLRRRAAAYVCNLLLPCVFISLLAPLAFHLPADSGEKVSLGVTVLLALTVFQLILAESMPPAESVPLIGKYYMATMTMVTFSTALTILIMNLHYCGPNAHPVPAWARVLLLGHLAKGLCVRERGEPCGQSKPLESAPSLQPPPASPAGPCHEPRCLCHQEALLHHIASIASTFRSHRAAQRRHEDWKRLARVMDRFFLGIFFCMALVMSLIVLVQAL
Protein: Malonamoyl-CoA synthetase vrtB (EC 6.2.1.-) (Viridicatumtoxin synthesis protein B) (D7PHZ3)
Organism: Penicillium aethiopicum
Function: Malonamoyl-CoA synthetase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system. The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyketide synthase vrtA. The aldolase vrtJ may be involved in the synthesis of the malonamate substrate for malonamoyl-CoA synthetase vrtB. The polyketide synthase vrtA then may utilize the malonamoyl-CoA starter unit, followed by sequential condensation of eight malonyl-CoA units to form the polyketide backbone. The cyclization of the last ring could be mediated by the lactamase-like protein vrtG. The proposed post-PKS tailoring steps are an hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase vrtE, a hydroxylation at C12a catalyzed by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase vrtF. VrtC is then proposed to catalyze the transfer of a geranyl group synthesized by vrtD to the aromatic C ring of the tetracyclic polyketide intermediate of viridicatumtoxin to yield previridicatumtoxin. Finally, the cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to afford viridicatumtoxin.
Interaction partners:
Sequence:
MAPYLQHFIAWFGKDSILSKLIQIFNPPSHSDSAKIIISDDDGRSPEPPGGEEILWRHSAPKSTQMWAFLQKVNKKYGYSLRTYQDLHHWSITHRGQFWGEAWDYCGIRHSRQYDEVVDEAAAMWPRPAWFRGARLNFAENLLFPKVPQAVSDEAIAVISVDEGGKRDFITWQDLRERVRRCQSGMRALKIQPSDRVAGYVANHSNALVAMLATASLGAIWTAVSPDTGVIGAVDRLVQIEPRLLFTDNAVIYNGRIHPVLTKTQEIITALPSLEAVVVMRTVAGVQEDLPSSPRSPAKRLTYNSFLAQGPETQKLEFVHMPAEHPLYILYSSGTTGPPKCIVHGAIGTLMQHKKEHMLQSDIQPGDRLCFVTTCMWMMWHWLVSGLASGATVVLYNGSPFYYAPSSHGTSAKDDLAMPKLVDELGITQFGASATYFSMLERRKHLPRSLTQGRLSLETLKAVYSTGSPLAPSTFRYIYQAFGSQVNLGSISGGTDIIADFGVPSPLQAVVAGEIQVIALGMAVQAWGPTGMDLSVTGEPGELVQFWGPSGASKYESSYFAKYPGVWAHGDHIQINPRTGGLIMLGRSDGTLNPKGVRFGSAEIYHVLQYHFAAQVEDALCVGRRRRQDTDEMVVLFVKMRQDQLWSLALAEAIRRTVREELSPRHVPELIIECPEIPVTANGKKVEVLVKRIVSGVEVPAAGGSGTVNADCLQWFQEWATQN
Protein: Gag polyprotein (Pr65gag) (Core polyprotein) [Cleaved into: Matrix protein p15 (MA); RNA-binding phosphoprotein p12 (pp12); Capsid protein p30 (CA); Nucleocapsid protein p10-Gag (NC-gag)] (P03332)
Organism: Moloney murine leukemia virus (isolate Shinnick) (MoMLV)
Function: Plays a role in budding and is processed by the viral protease during virion maturation outside the cell. During budding, it recruits, in a PPXY-dependent or independent manner, Nedd4-like ubiquitin ligases that conjugate ubiquitin molecules to Gag, or to Gag binding host factors. Interaction with HECT ubiquitin ligases probably links the viral protein to the host ESCRT pathway and facilitates release.
Subcellular location: [Gag polyprotein]: Virion {ECO:0000305}. Host cell membrane {ECO:0000269|PubMed:8991095}; Lipid-anchor {ECO:0000305}. Host late endosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P26807}. Note=These locations are probably linked to virus assembly sites. {ECO:0000305}.; SUBCELLULAR LOCATION: [Matrix protein p15]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein p30]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [Nucleocapsid protein p10-Gag]: Virion {ECO:0000305}.; SUBCELLULAR LOCATION: [RNA-binding phosphoprotein p12]: Host cytoplasm {ECO:0000269|PubMed:21085616, ECO:0000269|PubMed:23300449}. Note=Localizes to the host cytoplasm early in infection and binds to the mitotic chromosomes later on. {ECO:0000269|PubMed:23300449}.
Interaction partners:
Sequence:
MGQTVTTPLSLTLGHWKDVERIAHNQSVDVKKRRWVTFCSAEWPTFNVGWPRDGTFNRDLITQVKIKVFSPGPHGHPDQVPYIVTWEALAFDPPPWVKPFVHPKPPPPLPPSAPSLPLEPPRSTPPRSSLYPALTPSLGAKPKPQVLSDSGGPLIDLLTEDPPPYRDPRPPPSDRDGNGGEATPAGEAPDPSPMASRLRGRREPPVADSTTSQAFPLRAGGNGQLQYWPFSSSDLYNWKNNNPSFSEDPGKLTALIESVLITHQPTWDDCQQLLGTLLTGEEKQRVLLEARKAVRGDDGRPTQLPNEVDAAFPLERPDWDYTTQAGRNHLVHYRQLLLAGLQNAGRSPTNLAKVKGITQGPNESPSAFLERLKEAYRRYTPYDPEDPGQETNVSMSFIWQSAPDIGRKLERLEDLKNKTLGDLVREAEKIFNKRETPEEREERIRRETEEKEERRRTEDEQKEKERDRRRHREMSKLLATVVSGQKQDRQGGERRRSQLDRDQCAYCKEKGHWAKDCPKKPRGPRGPRPQTSLLTLDD
Protein: Protocadherin 1 isoform 2b (Q2TJI7)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
YCRQREAKSGYQAGKKETKDLYAPKPSGKAAKGSKSKGKKSKSPRPVKPVEDEDDTGLQKSLKFNLMSDAPGDSPRIHLPLNYPPGSPDLGRHYRSNSPLPSIQLQPQSPSASKKHQVVQDLPPANTFVGTGDTTSTGSEQYSDYSYRTNPPKYPSKQLPHRRVTFSATSQAQELQDPSQHSYYDSGLEESETPSSKSSSGPRLGPLALPEDHYERTTPDGSIGEMEHPENDLRPLPDVAMTGTCTRECSEFGHSDTCWMPGQSSPSRRTKSSALKLSTFVPSYSAFSHSSHDSCKDSATLEEIPLTQTSDFPPTATPASAQTAAKREIYL
Protein: Protein UL76 (Q6SW66)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Function: May participate in nuclear egress of viral particles. Plays a role in the dispersal of several host nucleolar proteins including NCL/nucleolin and NPM1. Since deletion of host NCL/nucleolin negatively impact on nuclear egress, UL76 supposedly acts on this process through its effect on host nucleoli (By similarity). Induces cell cycle arrest in host cells at the G2/M phase following by apoptosis. The mechanism involves the inhibition of host mitotic complex cyclinB/CDK1.
Subcellular location: Virion. Host cytoplasm {ECO:0000250}. Host nucleus, host nucleolus {ECO:0000250}. Host Golgi apparatus {ECO:0000250}.
Interaction partners:
Sequence:
MPSGCGDDADSTGNALRRLPHVRKRIGKRKHLDIYRRLLRVFPSFVALNRLLGGLFPPELQKYRRRLFIEVRLSRRIPDCVLVFLPPDSGSRGIVYCYVIEFKTTYSDADDQSVRWHATHSLQYAEGLRQLKGALVDFDFLRLPRGGGQVWSVVPSLVFFQQKADRPSFYRAFRSGRFDLCTDSVLDYLGRRQDESVAHLLAATRRRLLRAARGKRAALPRARASAVAGGRGGGNARRGLARGRAHGPGAQTVSASGAEGSGSQGTDLLRGSRRARVRGGGAVEPAVRARRRTVAADAATTTVSSAFVVPRDRRGRSFRRPTRSL
Protein: Isoflavone 7-O-glucosyltransferase 1 (EC 2.4.1.170) (UDP-glucose:isoflavone 7-O-glucosyltransferase) (A6BM07)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: Involved in the biosynthesis of isoflavonoids. Specific for UDP-glucose. Can use genistein > daidzein > formononetin > quercetin > kaempferol > 4,2',4',6'-tetrahydroxychalcone > apigenin > aureusidin > esculetin > naringenin as substrates, but not cyanidin, trans-p-coumaric acid, caffeic acid, benzoic acid, m- and p-hydroxybenzoic acids, salicylic acid, salicyl alcohol, and hydroquinone.
Interaction partners:
- Malonyl-CoA:isoflavone 7-O-glucoside-6''-O-malonyltransferase
- 2-hydroxyisoflavanone dehydratase
- isoflavone 7-O-methyltransferase
- isoflavone 7-O-methyltransferase
- isoflavone 7-O-methyltransferase
- isoflavone 7-O-methyltransferase
- Uncharacterized protein
- isoflavone 7-O-methyltransferase
- isoflavone 7-O-methyltransferase
- isoflavone 7-O-methyltransferase
Sequence:
MKDTIVLYPNLGRGHLVSMVELGKLILTHHPSLSITILILTPPTTPSTTTTTLACDSNAQYIATVTATTPSITFHRVPLAALPFNTPFLPPHLLSLELTRHSTQNIAVALQTLAKASNLKAIVIDFMNFNDPKALTENLNNNVPTYFYYTSGASTLALLLYYPTIHPTLIEKKDTDQPLQIQIPGLSTITADDFPNECKDPLSYACQVFLQIAETMMGGAGIIVNTFEAIEEEAIRALSEDATVPPPLFCVGPVISAPYGEEDKGCLSWLNLQPSQSVVLLCFGSMGRFSRAQLKEIAIGLEKSEQRFLWVVRTELGGADDSAEELSLDELLPEGFLERTKEKGMVVRDWAPQAAILSHDSVGGFVTHCGWNSVLEAVCEGVPMVAWPLYAEQKMNRMVMVKEMKVALAVNENKDGFVSSTELGDRVRELMESDKGKEIRQRIFKMKMSAAEAMAEGGTSRASLDKLAKLWKQS
Protein: Photosystem II reaction center protein K (PSII-K) (P0C409)
Organism: Oryza sativa subsp. indica (Rice)
Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation.
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00441}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00441}.
Interaction partners:
- Photosystem II CP47 reaction center protein
- Cytochrome b559 subunit alpha
- Photosystem II reaction center protein H
- Cytochrome b559 subunit beta
- Photosystem II CP43 reaction center protein
- Photosystem II D2 protein
- Photosystem II reaction center protein L
- Photosystem II protein D1
- Photosystem II reaction center protein I
- Photosystem II reaction center protein J
Sequence:
MPNILSLTCICFNSVIYPTSFFFAKLPEAYAIFNPIVDFMPVIPVLFFLLAFVWQAAVSFR
Protein: Sodium channel protein (A0A0A0MT39)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
Interaction partners:
Sequence:
MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIIMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRKRMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRKETRFEEGEQPGQGTPGDPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQTPEDSCSEGSTADMTNTAELLEQIPDLGQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYHIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINILAKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRGDCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRSLKHASFLFRQQAGSGLSEEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSVTRATSDNLQVRGSDYSHSEDLADFPPSPDRDRESIV
Protein: Elongin-B (EloB) (Elongin 18 kDa subunit) (RNA polymerase II transcription factor SIII subunit B) (SIII p18) (Transcription elongation factor B polypeptide 2) (P62870)
Organism: Rattus norvegicus (Rat)
Function: SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (By similarity). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q15370}.
Interaction partners:
- von Hippel-Lindau disease tumor suppressor
- Elongin-C
- Cullin-5
- Cullin 2
- E3 ubiquitin-protein ligase RBX1
- RING-box protein 2
- Hypoxia-inducible factor 1-alpha
- Endothelial PAS domain-containing protein 1
- Elongin-A
- single-stranded DNA cytosine deaminase
Sequence:
MDVFLMIRRHKTTIFTDAKESSTVFELKRIVEGILKRPPEEQRLYKDDQLLDDGKTLGECGFTSQTARPQAPATVGLAFRADDTFEALRIEPFSSPPELPDVMKPQDSGGSANEQAVQ
Protein: B3 domain-containing protein REM3 (Protein REPRODUCTIVE MERISTEM 3) (Q8VZQ9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00326}.
Interaction partners:
- B3 domain-containing protein At1g16640
- Protein BASIC PENTACYSTEINE3
- B3 domain-containing protein At1g20600
- Putative B3 domain-containing protein At4g03170
Sequence:
MANHPLSSSRSNRPFFVRSLAGHTSNLIIPDEFFTAHLEGKTGLTKLKLTSDASDRIWDVRLNGRRFAGGWDDFSAAHCLRDDDVLVFRLDVKMVFHVTPSGRSFSQIRTSSSSGDYDSDDDDDEAGDDDSDSKNISLKKKSRFEAESSSSEKYCLLGLTASNLRLNRVSFTKHFSRANGLTKRCCMIDLMNLSGESWTLGLRHNKRTGQAFIRGRWRSFCHANELKPGSFYRFKLVRNGTRPLLQLCFKVIPQGNCSNSKANGKANVSEKYSREDGSASTKQNKFLTVTLKHYMIQSGQLRLRRSFVRENGIKEAEEIILVDKNGVEWPSYVSSSKQRREFYMAHGWIRFCEANKLKTGETFTLEFVRGEGTTPMLKFCSEAKIEQEEAPEERGTPLPKRARVSAEVGHSRRTQAPNKSSDDPKILQRKQPLQPCSFSDQAKKVKQSIVNILTGIKRFRSELELKERNLEAALLEIDALGDKVSEINKILK
Protein: Methyl-accepting chemotaxis protein CtpL (Q9HUW6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. Chemoreceptor for inorganic phosphate, which is required for taxis at low concentrations of phosphate. Is also responsible for the positive chemotaxis toward 4-chloroaniline (4CA) and catechol. Does not recognize inorganic phosphate directly, but via a complex between the periplasmic protein PstS and inorganic phosphate.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:27353565}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Chemotaxis protein CheA
- Chemotaxis protein CheA
- Chemotaxis protein CheA
- Chemotaxis protein CheA
- Probable purine-binding chemotaxis protein
- Chemotaxis protein methyltransferase 1
- Chemotaxis protein CheW
- Probable biofilm formation methyltransferase WspC
- Protein-glutamate methylesterase/protein-glutamine glutaminase 1
- Chemotaxis protein methyltransferase 2
Sequence:
MRLKQLTNLNTLLLLTVCLALGITLWWSQRAMERPFQLLDQYLELSQRFDEQVARNIRQYLGSGDAVRQQAALQALESLAEALPELPPDLARTLAPSLAELREFSAGDLLAAGKLAGDPQGLLLQAERDLTGNLEQWSAYLDAAAGQPQAGAYRTPLLLASLHLTRLSLARAKLVESANPALAGDVERELANLREQAGRIEALPLLGVLDEQRSASDDFAAMMGLAGDAEAGAGNAEDRGVALRRELASLLQRYPDELRRTRDLIERRQQLSADTGARLDAVRQALATLEPQVRGERQRLQGQVRLIQGGMIALILLIALAIDSLQRRLARVLGQLVPALSAWADGDFSRPISLRTRTEDLRNLEDSLNRLRSFLAELVGAIHRRAEQVAGSSQTLAEVSSGLHAGVERQAGDTGQIRDALGDMEAAIQQVAGDASQTADASRSAGQAVEHGQRVIGESLGGLRELVDEVQGNAQSIERLAEESATIGSVLTVIRSIAEQTNLLALNAAIEAARAGDQGRGFAVVAEEVRSLAQRTAGATEEIQQLIGRLQQAARQSVEAMRSQVEHAERTAEQAGAAEGALDEVVAAIHTIGVMAERIAEGSTQQSQAVGEIRSHSERIHALGGENLRLIGHSREQGEQLRQLGGDLRTTVQAFRL
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.27) (Q9VW25)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|RuleBase:RU367115}.
Interaction partners:
Sequence:
MSQQRSTEQIAASNNNTSDVIALDDDEDTDVQFVAALRPTAPVIDLCVSPSTSAAAAAAAAAAAHSGGGSGEDPAVGSASGAAASDTDSLASSPDEGALATGVDAAAAVSGEDSPSAAAAALECPICLQTCIHPARLPCGHIFCFLCVKGVAYKNRRCAMCRREIPAEFLDHPQLVNGIEDICTTRATEDGFQWYYEGRNGWWQYDDRTSQDIEDAFKKGDKSCTILVAGYVYIVDLEQLVQQRQNEPTRCRRVKRDLATIPKKGVAGLRIEGNQVTSDTVFSRPTNTANPTTVAAAASSFISTIAATDAAIRIASDIIGSTLAHADELTRGLTASNLNDDLSSSDSFSICTPPLLLTAKCVFVASLISTVYLKLY