wanglab/gogpt-training-data huggingface dataset:
Protein: T. brucei spp.-specific protein (Q387S5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRSSSAASSTRALTPGKLKQPGSTRGLKSTHSGSEEAVLSDKLLLFLQQSRERTSHNHAARISLLESQYTQSLHGLSGARGSSTLFTEASLNARKGGRHGRDPAGIVDKEIVIEVDMSESEDEVSSQPIETNHRAQQREHAATQFSSVRLTASSCRVTATAAATDLSPQSLSESYGVSPEVRTPISPFIEKMHYREVLCAPELPQGPEKRNKTTTHYTATELSLGRAQAGVRANVGRGMVSSLPPCAAARNEVSVSLERAINEARDKHNWSESTTANVMSRGTTTAPPMLPRTNAVTSKVDDEVQHSPLFPHEPEIEEFLAWEAAKPAELLKCLRAGFSNHCPIATAYAAVRPEVHWLSLLCNSESDVKSEAKGSPLRPDSAPSRFIEWIASDVDCYEGLLLQRGAVAPIVARSAKS
Protein: Alpha-ketoglutarate-dependent dioxygenase alkB homolog 4 (Alkylated DNA repair protein alkB homolog 4) (DNA N6-methyl adenine demethylase ALKBH4) (EC 1.14.11.51) (Lysine-specific demethylase ALKBH4) (EC 1.14.11.-) (Q9D8F1)
Organism: Mus musculus (Mouse)
Function: Dioxygenase that mediates demethylation of actin monomethylated at 'Lys-84' (K84me1), thereby acting as a regulator of actomyosin-processes (By similarity). Demethylation of actin K84me1 is required for maintaining actomyosin dynamics supporting normal cleavage furrow ingression during cytokinesis and cell migration (By similarity). In addition to proteins, also demethylates DNA: specifically demethylates DNA methylated on the 6th position of adenine (N(6)-methyladenosine) DNA, thereby regulating Polycomb silencing.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9NXW9}. Nucleus {ECO:0000269|PubMed:25153837}. Nucleus, nucleolus {ECO:0000269|PubMed:25153837}. Midbody {ECO:0000250|UniProtKB:Q9NXW9}. Note=Associates with the contractile ring and midbody. {ECO:0000250|UniProtKB:Q9NXW9}.
Interaction partners:
- Alpha-ketoglutarate-dependent dioxygenase alkB homolog 7, mitochondrial
- Probable RNA/DNA demethylase ALKBH6
- Nucleic acid dioxygenase ALKBH1
- N
- DNA oxidative demethylase ALKBH2
- Methyltransferase HEMK2
Sequence:
MAAAAEVSLLQECGCKGIRTCLICERQRHRDPPWQICLQKKCCFLYCPDTGWAAGAEGSDLEGWAFPFPGVTLIQDFVTPEEEAEMVRLMDCDPWKLSQSGRKKQDYGPKVNFRKQKLKMAGFQGLPGFSQKVVQRMGLYPGLEDFQPVEQCNLDYSPERGSAIDPHLDDAWLWGERLVSLNLLSATVVSMSPEAPGSLLLCSAPSVRPDAFEDSLVAPSRSVPCQEVEVAITVPRRSLLVLTGAARHQWTHAIHRRHIKARRVCATFRELSSEFLPGGKQQELGQELLQAALSFQGRPV
Protein: Phenylacetate-coenzyme A ligase (EC 6.2.1.30) (Phenylacetyl-CoA ligase) (PA-CoA ligase) (O33469)
Organism: Pseudomonas putida (Arthrobacter siderocapsulatus)
Function: Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA). Involved in the phenylalanine metabolism. Can also use CTP and UTP as substrate.
Interaction partners:
Sequence:
MNMYHDADRALLDPMETASVDALRQHQLERLRWSLKHAYDNVPLYRQRFAECGAHPDDLTCLEDLAKFPFTGKNDLRDNYPYGMFAVPQEEVVRLHASSGTTGKPTVVGYTQNDINTWANVVARSIRAAGGRKGDKVHVSYGYGLFTGGLGAHYGAERLGCTVIPMSGGQTEKQVQLIRDFQPDIIMVTPSYMLNLADEIERQGIDPHDLKLRLGIFGAEPWTDELRRSIEQRLGINALDIYGLSEIMGPGVAMECIETKDGPTIWEDHFYPEIIDPVTGEVLPDGQLGELVFTSLSKEALPMVRYRTRDLTRLLPGTARPMRRIGKITGRSDDMLIIRGVNVFPTQIEEQVLKIKQLSEMYEIHLYRNGNLDSVEVHVELRAECQHLDEGQRKLVIGELSKQIKTYIGISTQVHLQACGTLKRSEGKACHVYDKRLAS
Protein: Pentatricopeptide repeat-containing protein ELI1, chloroplastic (Protein EDITING LACKING INSERTIONAL MUTANT 1) (Q9SZT8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a major role in single RNA editing events in chloroplasts. Acts as a site-recognition transacting factor involved in the edition of the site 5 of ndhB1 and ndhB2 (ndhB1-5 and ndhB2-5 sites corresponding to cytidine-830), which are plastid-encoded subunits of the NADH-plastoquinone oxidoreductase. May provide the catalytic activity for editing site conversion.
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MASSPLLATSLPQNQLSTTATARFRLPPPEKLAVLIDKSQSVDEVLQIHAAILRHNLLLHPRYPVLNLKLHRAYASHGKIRHSLALFHQTIDPDLFLFTAAINTASINGLKDQAFLLYVQLLSSEINPNEFTFSSLLKSCSTKSGKLIHTHVLKFGLGIDPYVATGLVDVYAKGGDVVSAQKVFDRMPERSLVSSTAMITCYAKQGNVEAARALFDSMCERDIVSWNVMIDGYAQHGFPNDALMLFQKLLAEGKPKPDEITVVAALSACSQIGALETGRWIHVFVKSSRIRLNVKVCTGLIDMYSKCGSLEEAVLVFNDTPRKDIVAWNAMIAGYAMHGYSQDALRLFNEMQGITGLQPTDITFIGTLQACAHAGLVNEGIRIFESMGQEYGIKPKIEHYGCLVSLLGRAGQLKRAYETIKNMNMDADSVLWSSVLGSCKLHGDFVLGKEIAEYLIGLNIKNSGIYVLLSNIYASVGDYEGVAKVRNLMKEKGIVKEPGISTIEIENKVHEFRAGDREHSKSKEIYTMLRKISERIKSHGYVPNTNTVLQDLEETEKEQSLQVHSERLAIAYGLISTKPGSPLKIFKNLRVCSDCHTVTKLISKITGRKIVMRDRNRFHHFTDGSCSCGDFW
Protein: NEP-interacting protein 2 (F4INM3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MASSSSSSYRFQSGSYPLSSSPSLGNFVERIKDACHFLVSAVLGTIISAILTFFFALVGTLLGALTGALIGQETESGFIRGAAIGAISGAVFSIEVFESSLDLWKSDESGFGCFLYLIDVIVSLLSGRLVRERIGPAMLSAVQSQMGAVDTAFDDHTSLFDTGGSKGLTGDLVEKIPKMTITGNNNTDASENTDSCSVCLQDFQLGETVRSLPHCHHMFHLPCIDNWLLRHDISTARTSRVCSALLPSSLSFM
Protein: LIM domain kinase 2 (LIMK-2) (EC 2.7.11.1) (P53671)
Organism: Homo sapiens (Human)
Function: Serine/threonine-protein kinase that plays an essential role in the regulation of actin filament dynamics. Acts downstream of several Rho family GTPase signal transduction pathways. Involved in astral microtubule organization and mitotic spindle orientation during early stages of mitosis by mediating phosphorylation of TPPP. Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro. Suppresses ciliogenesis via multiple pathways; phosphorylation of CFL1, suppression of directional trafficking of ciliary vesicles to the ciliary base, and by facilitating YAP1 nuclear localization where it acts as a transcriptional corepressor of the TEAD4 target genes AURKA and PLK1.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:22328514}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:25849865}.; SUBCELLULAR LOCATION: [Isoform LIMK2a]: Cytoplasm {ECO:0000269|PubMed:8954941}. Nucleus {ECO:0000269|PubMed:8954941}.; SUBCELLULAR LOCATION: [Isoform LIMK2b]: Cytoplasm {ECO:0000269|PubMed:8954941}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:8954941}. Nucleus {ECO:0000269|PubMed:8954941}. Note=Mainly present in the cytoplasm and is scarcely translocated to the nucleus. {ECO:0000269|PubMed:8954941}.
Interaction partners:
- Cofilin-1
- Cofilin-2
- Rho-associated protein kinase 1
- LIM domain kinase 1
- Serine/threonine-protein kinase PAK 4
- Rho-associated protein kinase 2
- Collectin-12
- Serine/threonine-protein kinase PAK 1
- Serine/threonine-protein kinase PAK 5
- Serine/threonine-protein kinase PAK 6
Sequence:
MSALAGEDVWRCPGCGDHIAPSQIWYRTVNETWHGSCFRCSECQDSLTNWYYEKDGKLYCPKDYWGKFGEFCHGCSLLMTGPFMVAGEFKYHPECFACMSCKVIIEDGDAYALVQHATLYCGKCHNEVVLAPMFERLSTESVQEQLPYSVTLISMPATTEGRRGFSVSVESACSNYATTVQVKEVNRMHISPNNRNAIHPGDRILEINGTPVRTLRVEEVEDAISQTSQTLQLLIEHDPVSQRLDQLRLEARLAPHMQNAGHPHALSTLDTKENLEGTLRRRSLRRSNSISKSPGPSSPKEPLLFSRDISRSESLRCSSSYSQQIFRPCDLIHGEVLGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKKLNLLTEYIEGGTLKDFLRSMDPFPWQQKVRFAKGIASGMAYLHSMCIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEERKRAPMEKATTKKRTLRKNDRKKRYTVVGNPYWMAPEMLNGKSYDETVDIFSFGIVLCEIIGQVYADPDCLPRTLDFGLNVKLFWEKFVPTDCPPAFFPLAAICCRLEPESRPAFSKLEDSFEALSLYLGELGIPLPAELEELDHTVSMQYGLTRDSPP
Protein: AT3g18240 (Ribosomal protein S24/S35) (Q9LJQ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- At1g64880
- Small ribosomal subunit protein mS29
- Translation elongation factor EF1B/ribosomal protein S6 family protein
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein bS18c
- Large ribosomal subunit protein mL46
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein uL23m
Sequence:
MRGALLRNASLCARRIILSPRITHQISPNVPFLAPIAAPAAPKFRFFSSESGENSTTAPESSPTDSPEKKDLVVEDVSNKELKSRIEKYFNEGNEDALPGVIEALLQRRLVDKHAETDDELLEKIESLPFKDDVKDEDFESDFEEAHSTDEELEDLYNSPEYVAEKMRKNEFFNMDDKKWDHMIREGIQHGCLTDTKECEEILEDMLKWDQLLPDDLKKKVEAKFNELGDMCERGEIEAEAAYELFKEFEDEMVIQYGDQMEAEGPPQFGETDASDRNTDLDDPPGKGPILRWQSRIVFAPGGDAWHPKNRKVKMSVTVKELGLSKHQAKRLRELVGKRYHSGKDELTITSERFEHREENRKDCLRTLYGLIEEAGKANKIAEDIRTSYVKQRLRANPAFMQKLQAKIIRSKESDAINA
Protein: Homeobox protein HMX2 (Homeobox protein Nkx-5.2) (P43687)
Organism: Mus musculus (Mouse)
Function: Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MGSKEDVGKGCPAAGGVSSFTIQSILGGGPSEAPREPAGWPARKRSLSVSSEEEEPEEGWKAPACFCPDPHGPKEPSPKHHTPIPFPCLGTPKGSGGAGPAASERTPFLSPSHPDFKEEKERLLPAGSPSPGPERPRDGGAERQTGAAKKKTRTVFSRSQVYQLESTFDMKRYLSSSERACLASSLQLTETQVKTWFQNRRNKWKRQLSAELEAANMAHASAQTLVGMPLVFRDSSLLRVPVPRSLAFPAPLYYPSSNLSALPLYNLYNKLDY
Protein: Glucosidase II subunit alpha (Q7KMM4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
- Glucosidase 2 subunit beta
- Mannosyl-oligosaccharide glucosidase
- alpha-1,2-Mannosidase
- RE55916p
- NFU1 iron-sulfur cluster scaffold homolog
- Glycogen debranching enzyme
- LD08455p
- UDP-glucose:glycoprotein glucosyltransferase
- Calnexin 99A, isoform A
- GH11935p
Sequence:
MRFALATVAIIWALFVLADGVDPGNFKTCEQSSFCRRSRKIQGSGSKYALIPGTLNTYADSLTADLVNKENHHQFAFKLEALVGSTFRLQIDEKQPLRPRYRVEHALKGPTQAGRIRVQRETDGEIVITSEKNKAVIHGDPFRIDFFENDVLVVSVNAKNWLYFEHLRQKAQEPTSHPAENENQQEQDAAVETPKAADTIDDPGAWEENFKSHHDSKPYGPEAVALDFSFPAAKVLFGIPEHADSFILKSTSGTDPYRLYNLDVFEYVVDSKMALYGSVPVIYGHGAQRTAGVYWQNAAETWVDIQTSETNVVSSLVNFVSGSQKTPPPAAHFMSESGIVDAFIMLGPKPMDTFKQYAALTGTHELPQLFALAYHQSRWNYNDERDVTSVSAKFDEYNIPMDTMWLDIEHTDGKRYFTWDKFKFPHPLAMIKNLTELGRHLVVIVDPHIKRDNNYFFHRDCTDRGYYVKTREGNDYEGWCWPGAASYPDFFNPVVREYYASQYALDKFQTVTADVMLWNDMNEPSVFNGPEITAPKDLIHYGNWEHRDVHNLYGHMHLMGSFAGLQQRDPNQRPFILTRAHFAGSQRYAAIWTGDNFADWSHLQHSVKMCLTEAVAGFSFCGADVGAFFGNPDTELLERWYQTGAFLPFFRAHAHIDTKRREPWLFPERTRQVIQNAVIKRYSYLPLWYTAFYELELTGEPVIRPLLAQYPLDKEAFGVDNQLLVQDRLLVRPVMQQGVSKVDVYFPAIDDKKNGDWWYDVDTYQRQERSGYVSVPVDDFKIPVWQRGGSIVPKKERQRRASTLMLHDPYTLIICLDRQGKASGSLYLDDEKSYAYRQGQRIHVNYEFAHDQLVNSFVGKPKYKTLAWIERIVIAGLEKVPSSASITVNGVSQQLEVLHHDNTVVVRKPGVKMDVDFAIKLNFA
Protein: Thin, isoform C (B7YZK8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Tropomyosin-2
- Ubiquitin-conjugating enzyme E2-17 kDa
- Paramyosin, long form
Sequence:
MEQFEQLLTCCVCLDRYRIPKLLPCQHSFCMEPCMEGLVDYVRRQVKCPECRAEHRIPYNGVQAFPTNVTLQRFLELHIEITGELPDPTSGQIMERCGVCSEKAYLSHCAHCEKKICEDCKSAHMDILRREITRFNSQIRRSLHRLQDSLAIIEKNTMSLQTNAISVTEEIDEIYQRITKAIKDRSDQLKGEIDRYLAVELRNLTTLKENLDLEITNITSNCDTVDKYMNETVEWDDCELMDTKEIFLKTVEFLRHFEYENNDYSRRVRFLVSIDPNQLVMNLATFGDLNIAPHSTPSGGSVSSSHLAPPSALQPGLMRSKSDHRLATQFRQQEERSGYNDEPVLGGRKFGERPQRSATQANNDRYGRSGGDYDYENDYDNEGSSGRAGKSSRFRSRFVRSHQNDDSDSEQQQQQRQQELKERKDRVLDSEDVSRGQLSGIIRLSDCSRVVQRLADIGKEKKEKKSDAAAAAQAAVQAAIQAQKAAMQRQQQKNQQNAADEEELARQKRKNAGSSSTGGAATSTSSGGGDTASDQRVAALKNRGGEESDGSSNQAASPVRNSAASTTRAEVSVNEANTEEEGVASESSDSEEDEEVEDEDEEEEVDEEEEQVEESVEEEEAPRELLNLPEEALQPTSSEVTEEEESSSEYEEVTATESEEEQEEVEGRVIEIESQDLPVINVLPPENDIAHKVEESPVDHISNQELMEETDKSTDESPEEEEEEEYTEEEIESKPPVSAQVAAVKKTQRSGSSDSSASTESSASSAAAAAVAATSTSATAAAPATSSSNSTSQNAKAPSSSRYSTARDTTAVPEKKPFVSRFLPQHSTASTTNGSADKKKAESSSSSEEETSSESESESEPETKAKSSATSSTTNTKSTPNSAASSTTAASSSTTSGSYRDRLEARRASRDDSSSTAAGRSSYATPSSSGYGSGSGTTGGRTRAVPAPHHTSESEDRYGSGTGSSYTSRFLNKSKSSAIVTQPSLSTPTASFDEDATGTGDDSDSRYGTGRSRYLAMKERRTRLARSRSSHQFGNDDEDLDEPVSPTTVSPSAYLASRCAYSGYGSSDLSRSRSSHALKSRDNSPITDRGAGSSRSSGLGGSSTTDSKDGEALSSWARYLKNKYGNKSSKDSAGSSGSARDTHAGSSTSSSAAASSSHAHGYGSGTSGSSGRSTASDVSRRLSLGLPLRQANELASSDDDGSKNGLGSPTSPTVAAAVAAAGITGAAGTIPKQVYLRKRQQLFQLGGRGSEPGSFTWPRGLAVGPDNSIVVADSSNHRVQVFDSNGIFVKEFGEYGNGEGEFDCLAGVAVNRIGQYIIADRYNHRIQVLDPQGRFLRAFGSQGTADGKFNYPWGVTTDALGFIYVCDKENHRVQVFQSDGSFVGKFGSCGRGEGQLEHPHYIAVSNTNRVIVSDSNNHRIQIFDVNGKVLSTVGGEGSDDGQFKFPRGVAVDDQGYIFVADSGNNRIQIFNPDGSFLKTFGSWGSGDSEFKGLEGVAIMSNGNILVCDRENHRVQVF
Protein: Luqin-like RYamide peptides lury-1 [Cleaved into: LURY-1-1; LURY-1-2] (Q9XW71)
Organism: Caenorhabditis elegans
Function: Acts as a ligand for the npr-22 receptor and controls food-related processes including feeding, lifespan, egg-laying and roaming behavior. Secreted in the presence of food, leading to reduced feeding and roaming behavior and increased egg laying and lifespan. Activity may be latent under normal conditions but induced under conditions that cause hyperactivation of the pharynx such as abrupt refeeding after starvation.
Subcellular location: [LURY-1-1]: Secreted {ECO:0000269|PubMed:28847365}. Note=Secreted from the M1 and M2 pharyngeal neurons in a food-dependent manner with secretion positively controlled by the presence of food. {ECO:0000269|PubMed:28847365}.; SUBCELLULAR LOCATION: [LURY-1-2]: Secreted {ECO:0000269|PubMed:28847365}. Note=Secreted from the M1 and M2 pharyngeal neurons in a food-dependent manner with secretion positively controlled by the presence of food. {ECO:0000269|PubMed:28847365}.
Interaction partners:
- Neuropeptide receptor 22
- Probable G-protein coupled receptor tkr-1
- FMRFamide-like neuropeptides 7
Sequence:
MLTRVPVLILAVIVMLALCQEPEKPEKRPALLSRYGRAVLPRYGKRSGNLMESSQNSLTEESSDVVCQLIDGKYICLPVDAVRFRPFFL
Protein: Putative RNA polymerase II subunit B1 CTD phosphatase RPAP2 homolog (EC 3.1.3.16) (RNA polymerase II-associated protein 2 homolog) (F4K1B1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Putative RNA polymerase II subunit B1 C-terminal domain (CTD) phosphatase involved in RNA polymerase II transcription regulation.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA-directed RNA polymerase II subunit 4
- DNA-directed RNA polymerases II, IV and V subunit 11
- DNA-directed RNA polymerases IV and V subunit 4
- DNA-directed RNA polymerases IV and V subunit 3B
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerases II, IV and V subunit 9B
- DNA-directed RNA polymerases II and V subunit 8A
- DNA-directed RNA polymerases II, IV and V subunit 9A
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerases II and V subunit 6B
Sequence:
MAKDNEAIAINDAVHKLQLYMLENTTDQNQLFAARKLMSRSDYEDVVTERAIAKLCGYTLCQRFLPSDVSRRGKYRISLKDHKVYDLQETSKFCSAGCLIDSKTFSGSLQEARTLEFDSVKLNEILDLFGDSLEVKGSLDVNKDLDLSKLMIKENFGVRGEELSLEKWMGPSNAVEGYVPFDRSKSSNDSKATTQSNQEKHEMDFTSTVIMPDVNSVSKLPPQTKQASTVVESVDGKGKTVLKEQTVVPPTKKVSRFRREKEKEKKTFGVDGMGCAQEKTTVLPRKILSFCNEIEKDFKNFGFDEMGLASSAMMSDGYGVEYSVSKQPQCSMEDSLSCKLKGDLQTLDGKNTLSGSSSGSNTKGSKTKPEKSRKKIISVEYHANSYEDGEEILAAESYERHKAQDVCSSSEIVTKSCLKISGSKKLSRSVTWADQNDGRGDLCEVRNNDNAAGPSLSSNDIEDVNSLSRLALAEALATALSQAAEAVSSGNSDASDATAKAGIILLPSTHQLDEEVTEEHSEEEMTEEEPTLLKWPNKPGIPDSDLFDRDQSWFDGPPEGFNLTLSNFAVMWDSLFGWVSSSSLAYIYGKEESAHEEFLLVNGKEYPRRIIMVDGLSSEIKQTIAGCLARALPRVVTHLRLPIAISELEKGLGSLLETMSLTGAVPSFRVKEWLVIVLLFLDALSVSRIPRIAPYISNRDKILEGSGIGNEEYETMKDILLPLGRVPQFATRSGA
Protein: Aminomethyltransferase (EC 2.1.2.10) (Glycine cleavage system T protein) (A0A1B0GVP5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000256|ARBA:ARBA00004173, ECO:0000256|RuleBase:RU003981}.
Interaction partners:
Sequence:
MVAFAGWSLPVQYRDSHTDSHLHTRQHCSLFDVSHMLQTKILGSDRVKLMESLVVGDIAELRPNQGTLSLFTNEAGGILDDLIVTNTSEGHLYVVSNAGCWEKDLALMQDKVRELQNQGRDVGLEVLDNALLALQAQVLQAGVADDLRKLPFMTSAVMEVFGVSGCRVTRCGYTGEDGVEISVPVAGAVHLATAILKNPEVKLAGLAARDSLRLEAGLCLYGNDIDEHTTPVEGSLSWTLGKRRRAAMDFPGAKVIVPQLKGRVQRRRVGLMCEGAPMRAHSPILNMEGTKIGTVTSGCPSPSLKKNVAMGYVPCEYSRPGTMLLVEVRRKQQMAVVSKMPFVPTNYYTLK
Protein: Low affinity K(+) transporter 1 (P47114)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Low affinity potassium transporter that, with PRM6/KCH2, participates in high-affinity Ca(2+) influx system (HACS) activation during the response to mating pheromone. Directly promotes K(+) influx and HACS may electrochemically respond to this K(+) influx. KCH1 and KCH2 act at the apex of the calcium signaling pathway that is used for survival during prolonged exposures to mating pheromones.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}. Cell membrane {ECO:0000269|PubMed:23204190}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Low-affinity potassium transport protein
- High-affinity potassium transport protein
Sequence:
MFNHDWKYSINSKTFADLNIELFRNHKFKTVLNYIIGVVGWNGLKLALFVSDIYTCIKLLAFNSWSNNIIKPYLPFKISKWLFSGCILASIVLLIWEAIAGMRIYKTGNISLTYVNNFSRNLNSVLNYSKFCVYNMIERKGFRQKMTFFTFFQLKDCIRLIFTDTPRQVINGLTLWSVLVTVNKNEDLGDLESFTGLINKIKNIGQTNHEEAVILSLMLFSFIIWALFVFKFLLAVICSIFVYYKIINDQEYSGLREYICVTVSENVDELVERQRKKENDDTIYKTGLLESQTFDDFKEVENKIETSFNDTSYASNNDSMIELIERRPEYKSQDVCGPIPTMKKTETMESFVDNGNPQYTTRFSAILDSPYINSYESNDIKKAKIQSRSVNTPKYEDLSSSDIFNKIHSAGQLKSTTSMEFHGPLDSMPNTTNNIRNFNSNSSRPRPPPLQTKSSINSKADSNDNGRIYTPMKAYFREPDLPRKGLLEDEDRTYNYT
Protein: Hgt19p (Q5A7L9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Fmp45p
Sequence:
MSTNPEKPTRNEDLFENSSSSSSVPHNKEASELESVNSTAEREGGEHGNILAQYTEEQVMQMGRNYAHKYDLDPDLFGRAAALARAPSAFNSMPFLTDEEKQGLYLEATKKWHIPRKLIEVIAVGAIAAATQGMDESTISGATLFYPKAFGVTEMKNADLIEGLVNSAPYLCCSVIACWTSDYWNRHLGRKWTIFWTCLISAVTCIWQGFVNNWWHLFIARFFLGFGIGVKSATVPAYAAECTPKHVRGALVMLWQFFTAVGIMFGFVSALAFYYVPHKSFGTGLNWRLMLGSACIPPIIVLFQIPFVPESPRWLMGKERHKEAFESLKALRFEEIAAARDCFYQYVLLKEEGTYDIPTWKRLIQMFTIRRNRNGAIGSWIVMFMQQFCGINVIAYYASSIFIKARYSEISALLASWGFGMINFVFAIPAFLTIDKFGRRNLLLFSFPLMGVFLLIAGFGFLIHDRQGQLAMVTTGIYIFSAIYSSSEGPVPFTYSAEAFPLYIRDLGMSWATATCWFFNFILAFTWPRLQNAFTPTGAFGWYAAWNVIGFFLVLWFLPETKGLTLEELDDVFAVPMYEHAVYRTKELLNGFQRVILRRNIPPMPPLYHHQRMAVTNPEWNDKTEVDHIE
Protein: Multifunctional dye peroxidase DyP2 (EC 1.11.1.16) (EC 1.11.1.19) (EC 1.11.1.7) (Dye decolorizing peroxidase 2) (DyP2) (Manganese peroxidase) (K7N5M8)
Organism: Amycolatopsis sp. (strain ATCC 39116 / 75iv2)
Function: Displays both high peroxidase and manganese peroxidase activity. Is likely involved in lignin degradation. Also has a Mn-dependent oxidase mode of action that expands its substrate scope in vitro; is thus able to catalyze the O(2)- and Mn-dependent oxidative decarboxylation of 4-methoxymandelate to anisaldehyde.
Subcellular location: Secreted {ECO:0000305|PubMed:23054399}. Note=Although no signal sequence is found, the secretory machinery for actinomycetes is not fully characterized, and the low pH optimum for DyP2 along with the observation that many DyPs have been isolated from the secreted protein fraction imply that DyP2 could be secreted and still possibly play a role in extracellular oxidation chemistry (PubMed:23054399).
Interaction partners:
Sequence:
MPVDLSTTLSWKSATGEAATMLDELQPNILKAHVRDRLTVLFLGFGDAAEARTFLNGLSGLMKSARTHLQEVEAHKLTKAVGTPYLGVGLTAHGYATLGVTAPADPSFTAGAKAAVEKLADPAVTEWEGHYQQTIDAVLLLGDATAGPVRTLRRQVEALRPASVTVVGEESGLGLANANGDGIEHFGYVDGRSQPLFLTEDVDAERDTTDGVNDWDPSAPLEQVLVPDPAAPDPTVHFGSYFVFRKLEQNVRLFKEAERDLAHDLGLRGEDRERAGAMLVGRFEDGTPLTAQSAPGSHHPVGNDFSYDSDKLGQKCPFHAHIRKTNPRGSGGAEAPEEERKHLMARRGQTYGRRHDDPNADLPPRLRPAKDVGLLFMAFNSNLGNQFEFTQQIWANNPAFPFPPDGSQPGLDPVIGQGARAPQKYAPEWGHNNVAEATDPIPQAVTMKGGEYFFMPSLAFLRSL
Protein: Protein grindelwald (Q9VJ83)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts as a receptor for egr. Plays a role in activation of JNK signaling and is required for egr-induced apoptosis. May also play an egr-independent role in cell proliferation.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:25874673}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Tumor necrosis factor family member eiger
- Tumor necrosis factor receptor superfamily member wgn
Sequence:
MSVRKLSALSLSIGGVPLIPSVSLVAAANGESRDCHGTICHPVNEFCYVATERCHPCIEVCNNQTHNYDAFLCAKECSAYKTFEPLKAEMLDIQNTQQLILLLLTILLVLIALRCAFQFLRWLIGNRCFQKLMRRLQSKAYPHPATANGKDLNATTIQNLNAINHPGSDLERAQSQIYSVAGAAEGSVVTMTTPVSTRYPAENSTTPTTVMTEIGYGYDNQAMVVTPVSEKPSAATIPVAF
Protein: Casein kinase II subunit alpha-2 (CK II) (EC 2.7.11.1) (Casein kinase alpha 2) (AtCKA2) (Q08466)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates (By similarity). The alpha chain contains the catalytic site. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis. CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation. Acts as circadian clock component that maintains the correct period length through phosphorylation of CCA1. May act as an ectokinase that phosphorylates several extracellular proteins.
Subcellular location: Nucleus {ECO:0000269|PubMed:16926165}. Nucleus, nucleolus {ECO:0000269|PubMed:16926165}. Note=Enriched in the nucleolus. {ECO:0000269|PubMed:16926165}.
Interaction partners:
- Casein kinase II subunit beta-1
- Casein kinase II subunit beta-2
- Casein kinase II subunit beta-3
- Putative casein kinase II subunit beta-4
- UPF0235 protein At5g63440
- FACT complex subunit SSRP1
- Protein CCA1
- At1g09850
- Probable cysteine protease RD21B
- Cysteine proteinase RD21A
Sequence:
MHLIFFFSYFLRRYLLLLCAILILRAPLAHSLIPPLTCVNTGTVESDVTGIRFDRCLDTDSLAKISLSTVMSKARVYTDVNVIRPKDYWDYESLNVQWGEQDDYEVVRKVGRGKYSEVFEGINMNNNEKCIIKILKPVKKKKIRREIKILQNLCGGPNIVKLLDVVRDQHSKTPSLIFEYVNSTDFKVLYPTLTDYDIRYYIYELLKALDFCHSQGIMHRDVKPHNVMIDHELRKLRLIDWGLAEFYHPGKEYNVRVASRYFKGPELLVDLQDYDYSLDMWSLGCMFAGMIFRKEPFFYGHDNQDQLVKIAKVLGTDELNAYLNKYQLELDTQLEALVGRHSRKPWSKFINADNRHLVSPEAIDYLDKLLRYDHQDRLTAKEAMAHPYFAQVRAAESSRMRTQ
Protein: Uncharacterized protein (Q4QEJ8)
Organism: Leishmania major
Interaction partners:
- Eukaryotic translation initiation factor 3 subunit 7-like protein
- Putative eukaryotic translation initiation factor 5
- Small ribosomal subunit protein eS1
- Putative translation initiation factor
- CSN8/PSMD8/EIF3K domain-containing protein
- Eukaryotic translation initiation factor 3 subunit I
- Small ribosomal subunit protein uS10
- Eukaryotic translation initiation factor 3 subunit E
- Putative elongation initiation factor 2 alpha subunit
- Translation initiation factor-like protein
Sequence:
MDRAATSDARARSSLSKAQEHLKNNDVKEAIDALSSHLRFNQVTPIGFECLELLADLCLTQEKLEPVKLIEVLRRCRSGLRGSQHMEESVQRIVDSVMIRIRQMCAKAKERAEAMQVNATEGDRMLAALNGISLAALAEKRHIIPCHAALRRLIRHFCGNNTIGFAKKLTFIYNKTVRQFLYMCKEFNAPACVLDISSAVSRAVSHMALDHLHDHDDAASRNAVQELLKERAAFLTSTSAVTETVETLCCLLNDICSLRQYGGAFDVLSCLKRVCDKVQRNEEFVDVVSGAYETMSDIFWTCSVYNYHAYCLSVAASMKRQEKRGPLAARAVLASLCVADGDMELDPFGRYREKNARIDELFESPITTKTSLIANLKTKGVHTLASPDIVKIAANLEDPNFSDFTGLHKSVTALTAANSDLARYGNELHKMILRYQLEVLSGTCNYVEVLSLAAYNGNLTAAEYVNNIEPVILGDDSVSVDIDTRTNTLSFRDSSKAKMLSYFNKIVANVDTVPASSLATTSGRYSDFTHVAASSSKREVMPLAADLDAARARSTSIYALQKACMNSKAERIEEAKKSEDKKRERAVAERREQEEAKKEETQKAYIRKLYAEYNERQRQERGKEVLRKLRIKYPGFKVDESIVYRSAAGFEDELTRLLAAFKRRGVDNDRKEILQANLYERALRALEIPKRKDYEAQNAERTRAERAAARENYLAEHRREYDRRQNEKAVLSKFLHDADEFERTWRKRANIDKPSKRDEQQRLLEEEMRRLGGE
Protein: Dynein regulatory complex protein 10 (IQ domain-containing protein D) (Q96DY2)
Organism: Homo sapiens (Human)
Function: Component of the nexin-dynein regulatory complex (N-DRC), a key regulator of ciliary/flagellar motility which maintains the alignment and integrity of the distal axoneme and regulates microtubule sliding in motile axonemes.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000250|UniProtKB:A8J0N6}.
Interaction partners:
Sequence:
MALDILAMAPLYQAPAINRIGPKTDPSKRPADPLKPLVLSRTKLTTIEAKRIMSILDEAIYKVELVTLLSYVASNREDMEGMLGEDVMRAVREHEDLCQVLLENVRCLKEKERQLQEQKEAEEEGWLRDRLLSIELQKSSLSPLMQQIKDSTKNVLRLLLSNPQAARLLQMQTQGRSAEAQNFIDSLIELRGFLFEKLLTSPMEARDKAQFLQDISRQNSNNQQIIDTLEKELAERMKNRNAEVEKENFVIQELKNHLHQVLKFSENSLVRTKQEAEKQQKADFRASQARVAKIQQEILQLQSQFYNLVMENREAEQALRKKKYKVETEIENWIQKYDTEMGEKQEELEDLDAVHREEKISLEELRRRHKVLVGEFAQIREEREINSKKRMEAEQEMVRMVRAATLIQALWKGYLVRSLLRSKKKRGKGKAKDKEKGKQKGKEKGKGKK
Protein: Hydroxyacylglutathione hydrolase, putative (EC 3.1.2.6) (Q585D9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- hydroxyacylglutathione hydrolase
- Aldo-keto reductase, putative
Sequence:
MEVVVKSIGTAFTVAVIPVLKDNYSYVIHDKATNTLAAVDVSVDIDPVIDYVRRLGGVDRTTDLRTILSTHKHHDHSGGNISLQKKLNAMGAFRIIGGANEPIPGVTEKVREGDHFSIGELKVDVLDAPCHTSGHVLYKVYHPQKAENGIALFTGDTMFVGGIGAFFEGDAVLMCSALRKVYNLNGACESSACDATDVQKRDNHTYIFPGHEYTVNFLRFSRDALPASHPDVSFVEAQLRRYTESVAGNVPTVPSTLAEEKRQNLFLRTCDEAFVRVMNKGETAVKLMDFLYNTCP