wanglab/gogpt-training-data huggingface dataset:
Protein: Multidrug transporter TPO1_2 (Clotrimazole exporter TPO1_2) (Drug:H(+) antiporter TPO1_2) (DHA TPO1_2) (Q6FV98)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Multidrug resistance transporter involved in resistance to azole antifungal drugs such as the imidazoles miconazole, ketoconazole, and tioconazole; as well as the triazoles itraconazole and fluconazole. Also plays a role in the resistance to other antifungal drug families such as the polyene amphotericin B, the pyrimide analog flucytosine, the fungicide mancozeb, and the polyamine spermine. Decreases the intracellular accumulation of clotrimazole by mediating its extrusion from cells. Plays a role in biofilm formation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26512119}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSSTSSDRPYDPLAPENEGVASSDVESTDSGEIRSYGPEEVLKNGSQIKDKGPALSKNSTQTSAVESAVAANRRLSKILTNTVDEPDVLEVDYSKCPPMGGGRPFPPTLPEKTQFEVTFDGPNDPLHPFNWPLRKKVMLCIILCLNCISITMGSSIFATGIRQICEIYHVIPVVAILGITLYVLGFAASPVIYAPLSEIYGRRGVLVISSFGFALFNFAVATAKDLQTIMICRFFAGFIGAAPLAVVPAAFADMFDTNIRGKAICLFSLGVFVGPILAPVIGSYITQHTTWRWLEYVIACFASAIFVAILFFFEESHHPSILVGKAKELRKLTGNWGIHAAHEDVELSVKEIAEKTITRPIIMLFTEPLLLIVTIYNSFVYGILYLLLEAYPIVFEQGYGFHTNGELPYISLIIGMAICGAFIWWMDEDYLRRYRKKGGLVPEARLLPMVVAGIVFPIGILWFCWTGNYPHKIHWIVPTIAGAFTGFGLIGIFLPCLNYIIESYLLIAASAVAANTFMRSGFGAAFPLFAGYMFNGMGVNYAGLLLGLLAVAMIPVPLLFLKYGPGIRKRSKYAYSL
Protein: At5g19340 (Q6NM33)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- RING-type E3 ubiquitin transferase
- AT1G11360 protein
- Protein IQ-DOMAIN 32
- Probable inactive receptor kinase At1g27190
- SAP domain-containing protein
- DEK domain-containing chromatin-associated protein 3
- Serine/arginine-rich splicing factor RS2Z32
- Protein LIFEGUARD 2
- At3g48120
- Protein BTR1
Sequence:
MVSAETATMAEAEPSTTGPRISFSADLSSSDSDGDFICINPVMNLIVGREEKDKSSVKAGDFEFLSENATMLSADELFSEGKLLPFWQVKHSEKLKNVTLKPKVEVQQEEEDHKVVNEEGFVHNKEQENNNNNNNNNNNRGSWFLDDDPSPRPPKCTVLWKELLRLKKQRTTTTTTASTRVSSLSPSSSSSSTSSSSSSIGDAVKKEEREKEGKRGKKGLERTRSVTMRIRPMIHVPVCTPSKSSSRLPPLFPLRLQKNRVER
Protein: Inositol polyphosphate-1-phosphatase isoform 2 (A0A0S2Z3X1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSDILRELLCVSEKAANIARACRQQEALFQLLIEEKKEGEKNKKFAVDFKTLADVLVQEVIKQNMENKFPGLEKNIFGEESNEFTNDWGNLPLWTSVCHHFNWCL
Protein: Tomoregulin-1 (TR-1) (H7365) (Transmembrane protein with EGF-like and one follistatin-like domain) (Q8IYR6)
Organism: Homo sapiens (Human)
Function: May inhibit NODAL and BMP signaling during neural patterning (By similarity). May be a tumor suppressor in brain cancers.
Subcellular location: Cell membrane {ECO:0000269|PubMed:12743596, ECO:0000269|PubMed:39048830}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Palmitoyltransferase ZDHHC5
Sequence:
MGAAAAEAPLRLPAAPPLAFCCYTSVLLLFAFSLPGSRASNQPPGGGGGSGGDCPGGKGKSINCSELNVRESDVRVCDESSCKYGGVCKEDGDGLKCACQFQCHTNYIPVCGSNGDTYQNECFLRRAACKHQKEITVIARGPCYSDNGSGSGEGEEEGSGAEVHRKHSKCGPCKYKAECDEDAENVGCVCNIDCSGYSFNPVCASDGSSYNNPCFVREASCIKQEQIDIRHLGHCTDTDDTSLLGKKDDGLQYRPDVKDASDQREDVYIGNHMPCPENLNGYCIHGKCEFIYSTQKASCRCESGYTGQHCEKTDFSILYVVPSRQKLTHVLIAAIIGAVQIAIIVAIVMCITRKCPKNNRGRRQKQNLGHFTSDTSSRMV
Protein: Multicopy suppressor of sporulation protein msa1 (Q10277)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Negative regulator of sexual differentiation. Acts by repressing the transcription of meiosis-inducing, ste11-regulated genes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Probable proteasome subunit beta type-7
- Negative regulator of differentiation 1
- DNA replication licensing factor mcm5
- Meiotically up-regulated gene 110 protein
- Meiosis protein mei2
Sequence:
MVVSSPSVSLLHSPVEKLSAQLEKTTLLQDIPPGSLSENDNSTTFIKPPLETASSSTPIPSSSSSGVLNPSSVRGKPVACLFVASLNSSRSEEELTATVKDYFQQWGPLLHVKVLKDWLQRPYSFVQFQNTDDASKALSEAQNTILDGRHIRIERAKVNRTIRISSAPHQPYITKKDIDNLLEPYGEVEDVTEIPDQSAFLVRFVYRDEAIAAYTALKHSAWPVLWAENVTYQNGHYKKKGSSPFSPPNAHSRRRKSQGKDQSNTPVIKAPAPIPFSVSSDPPSTMGRSNSAVQSPSYFAHSLVNSTEFSTPNESLSSLPSILPSIPSLESGKAELPTDGSFEQPGYPMNPSMMFAAMPPPIDPYSIFVGQLDPVNCTHYLLVDLFSKYGKVIDCKIIHQSKKPAFAFLRFDSQQAAYAAVCGKTRSPHQKKPLRVEFRQLRPMQQFSPQYQYPSYPYPMFPAPFSPPRNAMMPIPAPMDQFSTFHQSMATLPPGAVPTSIPQSYYPIYSPEMAMPQSYSPMYYTHNPPMDGN
Protein: SP295 (Q9U3W8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MNWTRVLLIGLTALALTFVDVASLSLDPVASAELEQFIRKGDVVISTRHIRPRRKLHISIEALFMIDFPMLKHKMSFFLDRKQQRVTLDISANGATESRNFEIPNINETSTIRSLALQFSKNRITLHVDCKASTHHDIDMNLAKLYTQMDDPVIKLFRERKYPLHFDGDMEHSLQRANCQKGNHRRGNRRMLHNKITEREKNKKRDVRGWYEPTIAREGVVDHRHQEVPTDVERGDIPVLNGDCEDALARSLSDLLALVKLLREDVAHQRQEIAYLRMLLENCAGCKNPLTTDNQLRIEPDCRSANPCYPGVECLDSAAGPRCGHCPLGFIGDGKSCKPGVTCAHHMCYPGVQCHDTVNGAQCDSCPAGYEGDGRTCSLRNPCLDTPCPSGNILVPSHNVQHYQRQSQYTARKYSVVTN
Protein: Polybine-2 (Polybine-II) (P84389)
Organism: Polybia paulista (Neotropical social wasp) (Swarm-founding polistine wasp)
Function: Venom component which lacks hemolytic or antibiotic properties, but produces an inflammatory response via mast cell degranulation and produces a chemotactic effect on leukocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:15572194}.
Interaction partners:
Sequence:
SVDMVMKGIKLWPL
Protein: ATP-dependent 6-phosphofructokinase, muscle type (ATP-PFK) (PFK-M) (EC 2.7.1.11) (6-phosphofructokinase type A) (Phosphofructo-1-kinase isozyme A) (PFK-A) (Phosphohexokinase) (P08237)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03184}.
Interaction partners:
- Glucose-6-phosphate isomerase
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
- ATP-dependent 6-phosphofructokinase, liver type
- ATP-dependent 6-phosphofructokinase, platelet type
- Hexokinase-1
- Fructose-bisphosphate aldolase A
- Transaldolase
- Fructose-1,6-bisphosphatase 1
- Fructose-1,6-bisphosphatase isozyme 2
- Fructose-bisphosphate aldolase B
Sequence:
MTHEEHHAAKTLGIGKAIAVLTSGGDAQGMNAAVRAVVRVGIFTGARVFFVHEGYQGLVDGGDHIKEATWESVSMMLQLGGTVIGSARCKDFREREGRLRAAYNLVKRGITNLCVIGGDGSLTGADTFRSEWSDLLSDLQKAGKITDEEATKSSYLNIVGLVGSIDNDFCGTDMTIGTDSALHRIMEIVDAITTTAQSHQRTFVLEVMGRHCGYLALVTSLSCGADWVFIPECPPDDDWEEHLCRRLSETRTRGSRLNIIIVAEGAIDKNGKPITSEDIKNLVVKRLGYDTRVTVLGHVQRGGTPSAFDRILGSRMGVEAVMALLEGTPDTPACVVSLSGNQAVRLPLMECVQVTKDVTKAMDEKKFDEALKLRGRSFMNNWEVYKLLAHVRPPVSKSGSHTVAVMNVGAPAAGMNAAVRSTVRIGLIQGNRVLVVHDGFEGLAKGQIEEAGWSYVGGWTGQGGSKLGTKRTLPKKSFEQISANITKFNIQGLVIIGGFEAYTGGLELMEGRKQFDELCIPFVVIPATVSNNVPGSDFSVGADTALNTICTTCDRIKQSAAGTKRRVFIIETMGGYCGYLATMAGLAAGADAAYIFEEPFTIRDLQANVEHLVQKMKTTVKRGLVLRNEKCNENYTTDFIFNLYSEEGKGIFDSRKNVLGHMQQGGSPTPFDRNFATKMGAKAMNWMSGKIKESYRNGRIFANTPDSGCVLGMRKRALVFQPVAELKDQTDFEHRIPKEQWWLKLRPILKILAKYEIDLDTSDHAHLEHITRKRSGEAAV
Protein: Acid-sensing ion channel 1 (ASIC1) (Amiloride-sensitive cation channel 2, neuronal) (Q1XA76)
Organism: Gallus gallus (Chicken)
Function: Proton-gated sodium channel; it is activated by a drop of the extracellular pH and then becomes rapidly desensitized. Generates a biphasic current with a fast inactivating and a slow sustained phase. Has high selectivity for sodium ions and can also transport lithium ions with high efficiency. Can also transport potassium ions, but with lower efficiency. It is nearly impermeable to the larger rubidium and cesium ions.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17882215, ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:24507937}; Multi-pass membrane protein {ECO:0000269|PubMed:17882215, ECO:0000269|PubMed:19641589, ECO:0000269|PubMed:24507937}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q6NXK8}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q6NXK8}.
Interaction partners:
- Stomatin
- HTH La-type RNA-binding domain-containing protein.
- Transient receptor potential cation channel subfamily V member 1
Sequence:
MMDLKVDEEEVDSGQPVSIQAFASSSTLHGISHIFSYERLSLKRVVWALCFMGSLALLALVCTNRIQYYFLYPHVTKLDEVAATRLTFPAVTFCNLNEFRFSRVTKNDLYHAGELLALLNNRYEIPDTQTADEKQLEILQDKANFRNFKPKPFNMLEFYDRAGHDIREMLLSCFFRGEQCSPEDFKVVFTRYGKCYTFNAGQDGKPRLITMKGGTGNGLEIMLDIQQDEYLPVWGETDETSFEAGIKVQIHSQDEPPLIDQLGFGVAPGFQTFVSCQEQRLIYLPPPWGDCKATTGDSEFYDTYSITACRIDCETRYLVENCNCRMVHMPGDAPYCTPEQYKECADPALDFLVEKDNEYCVCEMPCNVTRYGKELSMVKIPSKASAKYLAKKYNKSEQYIGENILVLDIFFEALNYETIEQKKAYEVAGLLGDIGGQMGLFIGASILTVLELFDYAYEVIKHRLCRRGKCRKNHKRNNTDKGVALSMDDVKRHNPCESLRGHPAGMTYAANILPHHPARGTFEDFTC
Protein: Amphoterin-induced protein 1 (AMIGO-1) (Alivin-2) (Q80ZD8)
Organism: Mus musculus (Mouse)
Function: Promotes growth and fasciculation of neurites from cultured hippocampal neurons. May be involved in fasciculation as well as myelination of developing neural axons. May have a role in regeneration as well as neural plasticity in the adult nervous system. May mediate homophilic as well as heterophilic cell-cell interaction and contribute to signal transduction through its intracellular domain (By similarity). Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent potassium channel KCNB1.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21983541, ECO:0000269|PubMed:22056818}; Single-pass type I membrane protein {ECO:0000269|PubMed:21983541}. Perikaryon {ECO:0000269|PubMed:22056818}. Cell projection, dendrite {ECO:0000269|PubMed:22056818}. Note=Colocalizes with KCNB1 at high-density somatodendritic clusters on the surface of hippocampal and cortical neurons (PubMed:22056818). Associated with axons of neuronal cells (By similarity). {ECO:0000250|UniProtKB:Q80ZD7, ECO:0000269|PubMed:22056818}.
Interaction partners:
- Potassium voltage-gated channel subfamily B member 1
Sequence:
MQPQRDLRGLWLLLLSVFLLLFEVARAGRSVVSCPANCLCASNILSCSKQQLPNVPQSLPSYTALLDLSHNNLSRLRAEWTPTRLTNLHSLLLSHNHLNFISSEAFVPVPNLRYLDLSSNHLHTLDEFLFSDLQALEVLLLYNNHIVVVDRNAFEDMAQLQKLYLSQNQISRFPVELIKDGNKLPKLMLLDLSSNKLKKLPLTDLQKLPAWVKNGLYLHNNPLECDCKLYQLFSHWQYRQLSSVMDFQEDLYCMHSKKLHNIFSLDFFNCSEYKESAWEAHLGDTLTIRCDTKQQGMTKVWVSPSNEQVLSQGSNGSVSVRNGDLFFKKVQVEDGGVYTCYAMGETFNETLSVELKVYNFTLHGHHDTLNTAYTTLVGCILSVVLVLIYLYLTPCRCWCRGVEKPSSHQGDSLSSSMLSTTPNHDPMAGGDKDDGFDRRVAFLEPAGPGQGQNGKLKPGNTLPVPEATGKGQRRMSDPESVSSVFSDTPIVV
Protein: Integrin beta (A0A8I6AQL1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251, ECO:0000256|RuleBase:RU000633}.
Interaction partners:
Sequence:
MPRVPATLYACLLGLCALVPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEYFGNPRSIISRCDLKANLIRNGCGGEIESPASSTHVLRNLPLSSKGSSAMGSDVIQMTPQEIAVSLRPGDQATFQLQVRQVEDYPVDLYYLMDLSLSMKDDLDNIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASDQMDYPSLALLGEKLAENNINLIFAVTKNHYMLYKNFTALIPGTTVEILHGDSKNIIQLIINAYSSIRAKVELSVWDQPEDLNLFFTATCQDGLSYPGQRKCEGLKIGDTASFEVSVEARSCPGRHTTQSFTLRPVGFRDSLQVEVAYNCTCGCSAGLEPNSARCSGNGTYVCGLCECDPSYLGTRCECQEGENQSGYQNLCREAEGKPLCSGRGECSCNQCSCFESEFGRIYGPFCECDSFSCARNKGVLCSGHGECHCGECKCHVGYIGDNCNCSTDISTCRAKDGQICSDRGRCVCGQCQCTEPGAFGETCEKCPTCPDACSSKRDCVECSLLHQGKPDNQTCHHQCKDEVITWVDSIVKDDQEAVLCFYKTAKDCVMMFSYTELPNGKSNLTVLREPECGSAPNAMTILLAVVGSILLVGMALLAIWKLLVTIHDRREFAKFQSLKPPVQKAHLHTYCRFCLQQVQQILQWLSGLLLDGWRGTEDKGVSRTPWTICSR
Protein: Guanylyl cyclase domain containing 1 (M0R6B5)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
VPEWVLACGKPQDFVQLPVPTIQQLYHWDCGLACSRMVLRYLGQLDDREFENALQELQLTRSIWTIDLAYLMRHFGVRHRFCTQTLGVDKGYKNQSFYRKHFDTEETRVNQLFAQAKACKVQVEKCTVSVQDIQAHLAQGHVAIVLVNSGVLHCELCSSPVKYCCFTPRGHRCFCRAPDYQGHFIVLRGYNRATGCIFYNNPAYADRMCSTSISNFEEARTSYGTDEDILFVYLDS
Protein: DNA replication licensing factor mcm2 (EC 3.6.4.12) (BM28-homolog) (Minichromosome maintenance protein 2) (xMCM2) (p112) (P55861)
Organism: Xenopus laevis (African clawed frog)
Function: Acts as component of the MCM2-7 complex (MCM complex) which is the replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. Core component of CDC45-MCM-GINS (CMG) helicase, the molecular machine that unwinds template DNA during replication, and around which the replisome is built. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for the entry in S phase and for cell division.
Subcellular location: Nucleus {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}. Chromosome {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}. Note=Associated with chromatin before the formation of nuclei and detaches from it as DNA replication progresses. {ECO:0000269|PubMed:9214646, ECO:0000269|PubMed:9214647}.
Interaction partners:
Sequence:
MADSSESFNIATSPRAGSRRDALTSSPGRDLPPFEDESEGMFGDGVVPEEEEDGEELIGDAMERDYRPISELDRYEVEGLDDEEDVEDLTASQREAAEQSMRMRDREMGRELGRMRRGLLYDSDEEEEDRPARKRRMAERAAEGAPEEDEEMIESIENLEDMKGHTVREWVSMAATRLEIYHRFKNFLRTHVDEHGHNVFKEKISDMCKENKESLPVNYEDLAAREHVLAYFLPEAPAEMLKIFDEAAKEVVLVMYPKYDRIAREIHVRISHLPLVEELRSLRQLHLNQLIRTSGVVTCCTGVLPQLSMVKYNCNKCNFILGPFFQSQNQEVRPGSCPECQSFGPFEINMEETVYQNYQRITIQESPGKVAAGRLPRSKDAILLADLVDSCKPGDEIELTGIYHNNYDGSLNTANGFPVFATVILANHITKKDDKVAVGELTDEDVKAIVALSKDERIGERIFASIAPSIYGHEDIKRGLALALFGGEAKNPGGKHKVRGDINVLLCGDPGTAKSQFLKYVEKVASRAVFTTGQGASAVGLTAYVQRHPVTKEWTLEAGALVLADRGVCLIDEFDKMNDQDRTSIHEAMEQQSISISKAGIVTSLQARCTVIAASNPIGGRYDPSLTFSENVDLTEPIVSRFDILCVVRDTVDPVQDEMLARFVVSSHIKHHPSSKDIANGDAAEFALPNTFGVEALPQEVLKKYIMYAKEKIRPKLNQMDQDKVAKMYSDLRKESMATGSIPITVRHIESMIRMAEAHARMHLRDYVVEDDVNMAIRVMLESFIDTQKFSVMRSMRKTFARYLAFRRDNNELLLFVLKQLIAEQVTYQRNRYGAQQDTIEVPEKDLVDKARQINIHNLSAFYDSDLFKMNKFTHDVKKKLIIQQF
Protein: Adenine DNA glycosylase (EC 3.2.2.31) (Q9HU37)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- DNA mismatch repair protein MutL
- Formamidopyrimidine-DNA glycosylase
- Sugar fermentation stimulation protein homolog
- DNA helicase II
- DNA polymerase IV
- Exodeoxyribonuclease III
- AsmA domain-containing protein
- UvrABC system protein B
- UvrABC system protein C
- UvrABC system protein A
Sequence:
MTPEGFNGAVLDWYDRHGRKDLPWQQGITPYRVWVSEIMLQQTQVSTVLGYFDRFMAALPDVEALAAAAEDEVLHLWTGLGYYSRARNLHKTAQIVVERHAGEFPRDVEQLAELPGIGRSTAGAIASLSMGLRAPILDGNVKRVLARYLAQDGYPGEPKVARALWEAAERFTPHARVNHYTQAMMDLGATLCTRSKPSCLLCPLVSGCRAHLLGREADYPQPKPRKALPQKRTLMPILANRDGAILLYRRPSSGLWGGLWSLPELDDLDGLEPLAARHSLALGERRELSGLTHTFSHFQLAIEPWLVAVEGAPRAVAEGDWLWYNLATPPRLGLAAPVKKLLKRAEQELGRGTAA
Protein: Matrix metalloproteinase-9 (EC 3.4.24.35) (92 kDa gelatinase) (92 kDa type IV collagenase) (Gelatinase B) (Q7T317)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498}.
Interaction partners:
Sequence:
MRLGVLAFLVLGTCSLRAWCLPLKSVFVTFPGDVIKNMTNTQLADEYLKRYGYVDVLQRSGLQAVISNAKALKKLQRQLGLEETGLLDQPTVDAMKQPRCGVPDIRNYKTFDGDLKWDHTDVTYRILNYSPDMEASLIDDAFARAFKVWSDVTPLTFTRLFDGIADIMISFGKLDHGDPYPFDGKDGLLAHAYPPGEGTQGDAHFDDDEYWTLGSGPAIQTRYGNAEGAMCHFPFLFEGTSYSTCTTEGRTDGLPWCSTTADYDKDKKFGFCPSELLFTFDGNSNEAPCVFPFVFDGKKYDSCTTEGRNDGYRWCSTTANFDTDKKYGFCPNRDTAVIGGNSEGEPCHFPFTFLGNTYSSCTSEGRNDGKLWCGTTSNYDTDKKWGFCPDRGYSLFLVAAHEFGHALGLDHSNIKDALMYPMYKYVEGFPLHRDDIDGIQYLYGPRTGPEPTAPQPRTTTSSPVVPTKPSPSDKTTTASTTTQVVPSDDACQIKEFDAITEIQKELHFFKDGRYWKISGNGERKGPFMISAKWPALPAVINSAFEDHLTKKIYFFSERQFWVYSGNDVLGPRKIEKLGLPSDLDKVEGSMQRGKGKVLLFNGENFWRLDVKAQLIDRGYPRFTDAAFGGVPIDSHDVFLYKGFFYFCRESFYWRMNAKRQVDRVGYVKYDLLKCSDIHSL
Protein: L-fuconate dehydratase (EC 4.2.1.68) (A2R805)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MVKITSFTTRDVRFPTSLDKTGSDAMNAAGDYSSAYCIIYTDSDYTGHGMTFTIGRGNEIVCSAISLLAPLVVGKDLDELTADWGKTWRYLVSDSQLRWIGPEKGVIHLALGAVVNALWDLWAKTLNKPVWRIVADMTPEEFVRCIDFRYITDAITPEEAIALLKEVEAGKQDRIKEAEQSQAVPAYTTSAGWLGYSEEKLKVLLKESVEQGYKHFKLKVGGNVEEDRRRLAIAREAIGYDKGNILMVDANQVWSVPEAITWMQQLAEFKPWFIEEPTSPDDILGHAAIKKALQDTPYGPIGVATGEMCQNRVVFKQLLQAGALTVLQADACRVGGVNEVLAILLLARKFGVPIVPHSGGVGLPEYTQHLSTIDYVVVSGKKSVLEYVDHLHEHFVHPSSVKDGYYVTPMEPGYSVEMKAESMDAFSFPGEEGKSWWRSEEAKTILEGPRIV
Protein: Vacuolar protein sorting-associated protein 55 (P47111)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in protein transport from endosomes to the vacuole.
Subcellular location: Endosome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 68
Sequence:
MMEFKVSPLTKIISLSGFLALGFLLVILSCALFHNYYPLFDILIFLLAPIPNTIFNAGNKYHTSDFMSDSSNTGQDLAHFLTGMLVTSGIALPVVFYHCQLIGHLSCIMCMIGGLIIYSSIVIFKWFFKKDFNEDDSLFG
Protein: Protein VAPYRIN (PhVpy) (Protein PENETRATION AND ARBUSCULE MORPHOGENESIS 1) (C7B178)
Organism: Petunia hybrida (Petunia)
Function: Required for arbuscular mycorrhizal (AM) symbiosis with AM fungi (e.g. Glomus intraradices, G. mosseae and Gigaspora margarita) both during fungal passage across root epidermis and for arbuscule formation in cortical cells; this symbiosis promotes phosphorus (P) and copper (Cu) uptake. Essential for infection by symbiotic nitrogen-fixing rhizobial bacteria leading to the formation of root nodules (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:20804456}. Nucleus {ECO:0000269|PubMed:20804456}. Cell membrane {ECO:0000250|UniProtKB:D3J162}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Associated with mobile spherical structures that are associated with the tonoplast referred to as 'tonospheres'. In mycorrhizal roots, tonospheres are observed in the vicinity of intracellular hyphae (arbuscules) (PubMed:20804456). Observed associated with EX70I in zones adjacent to the periarbuscular membrane (PAM) around the arbuscule hyphal tips (By similarity). {ECO:0000250|UniProtKB:D3J162, ECO:0000269|PubMed:20804456}.
Interaction partners:
Sequence:
MDRLLSLEPSNVVTIRLEPGQKCSGVLTLRNVMYTMPVAFRLQPLNKIRYSIRPQSGIISPLTTITLEIIYHLPPNTTLPDSFPHCDDSFLLHSVVAPGATAKDTSSTLDMVPSDWFTTKRKQVFIDSAIKIMFVGSPVLCYLVRKGYMDEIREVLEKSDTTWKSVDSVNFEGQTLLHLAISQGRPDLVQLLLEFGPNIEAHSRSCSSPLEAASATGEALIVELLLAKKASTERTEFSASGPIHLAAGNGHLEVLKLLLLKGANVNSLTKDGNTALHLAVEERRRDCARLLLANGARADICSTGNGDTPLHIAAGLGDEHMVRVLLQKGAEKYIRNKYGKTAYDVAAEHGHNKLFDALRLGDSLCVAARKGEVRTVQRLLENGASINGRDQHGWTALHRACFKGRIEVVKALIDNGIDVNARDEDGYTALHCAVESGHVDVAELLVKKGADIELRTSKGITALQIAQSLHYSGLTRVLMQGGATKEVGTMETNIVKSSGKIAVRDLDIGTIKKRSVNKSRTRRSSFDRNAPLAVL
Protein: Aurora kinase (EC 2.7.11.1) (Q384J7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ATP synthase subunit beta
- Ubiquitin-conjugating enzyme E2, putative
- Kinesin motor domain-containing protein
- Kinesin-like protein
- Rev7, putative
- Serine/threonine-protein kinase, putative
- Chromosomal passenger protein
- Chromosomal passenger protein
- Serine/threonine-protein kinase PLK
- Uncharacterized protein
Sequence:
MRSTEVGRVVEDFIVLPPTPKSKWKLSDFELLHKLGGGNYGDVHLASVKDCNFVCALKRLSIKKLADFDIATQLRREIEIAFNTRHKYLLRTYAYFFDETDIYLIMEPCSNGMLYTELNRVKCFAPPTAARYVAQLAEALLYLHQHHILHRDIKPENILLDHNNNIKLADFGWSVHDPDNRRKTSCGTPEYFPPEIVGRQAYDTSADLWCLGIFCYELLVGKTPFVGKDTDQICKNIHSMHFKIPENIPSEAKDLIANLLLRDGSRRLALHRVVNHQFLLKYYYLPNNLQPPTGKRPRLDAEPTAGKEN
Protein: Scarecrow-like protein 21 (AtSCL21) (GRAS family protein 11) (AtGRAS-11) (Q9S7H5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in plant development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Protein PAT1 homolog
- Holliday junction resolvase MOC1, chloroplastic
- Phytochrome A
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Thiohydroximate-O-sulfate sulfur/sulfate-lyase
- Protein S-acyltransferase 11
- Phytochrome B
Sequence:
MDNVRGSIMLQPLPEIAESIDDAICHELSMWPDDAKDLLLIVEAISRGDLKLVLVACAKAVSENNLLMARWCMGELRGMVSISGEPIQRLGAYMLEGLVARLAASGSSIYKSLQSREPESYEFLSYVYVLHEVCPYFKFGYMSANGAIAEAMKDEERIHIIDFQIGQGSQWIALIQAFAARPGGAPNIRITGVGDGSVLVTVKKRLEKLAKKFDVPFRFNAVSRPSCEVEVENLDVRDGEALGVNFAYMLHHLPDESVSMENHRDRLLRMVKSLSPKVVTLVEQECNTNTSPFLPRFLETLSYYTAMFESIDVMLPRNHKERINIEQHCMARDVVNIIACEGAERIERHELLGKWKSRFSMAGFEPYPLSSIISATIRALLRDYSNGYAIEERDGALYLGWMDRILVSSCAWK
Protein: Uncharacterized protein (A0A1D8PG37)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 13
- NADH-ubiquinone oxidoreductase chain 1
- NADH dehydrogenase 1 alpha subcomplex subunit
- NADH-ubiquinone oxidoreductase chain 5
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NAD-dependent epimerase/dehydratase domain-containing protein
- NADH-ubiquinone oxidoreductase 78 kDa subunit, mitochondrial
- Fesur1p
- NADH-ubiquinone oxidoreductase chain 2
- NADH dehydrogenase iron-sulfur protein 3, mitochondrial
Sequence:
MLVRFIGKSTTTPVGVYASTVSKRYSSIISVHRDTKEDNPNIAFEFNSENKKRAEEIIAKYPPQYKKGACMPLLDLGQRQLGFTSISVMNYVAKLLDMPPMRVYEVATFYTMYNRHPMGKYNLQVCTTTPCQLCGSDSIMKAITDYLKIKPGQTTPDKLFTLQEVECLGACVNAPMIAINDDYHEDLSPEATINLLKQLQEGKELTEIGPVDGKRQSCEPFSGPKVLLNKEPNDIRKFTRADL
Protein: SLIT and NTRK-like family, member 3 (D4A062)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Receptor-type tyrosine-protein phosphatase delta
- Receptor-type tyrosine-protein phosphatase S
- Neuroligin-2
- Interleukin-1 receptor accessory protein-like 1
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L3
- Adhesion G protein-coupled receptor L2
- Neuroligin-1
- Neurexin-2
Sequence:
MKPTITEMLHRGRMLWIILLSTIALGWTTPIPLIEDSEEIDEPCFDPCYCEVKESLFHIHCDSKGFTNISQITEFWSRPFKLYLQRNSMRKLYTNSFLHLNNAVSINLGNNALQDIQTGAFNGLKILKRLYLHENKLDVFRNDTFLGLESLEYLQADYNVIKRIESGAFRNLSKLRVLILNDNLIPVLPTNLFKAVSLTHLDLRGNRLKVLFYRGMLDHIGRSLMELQLEENPWNCTCEIVQLKSWLERIPYTALVGDITCETPFHFHGKDLREIKKTELCPLLSDSEVEASLGIPHLSSSKENAWPTKPSSMLSSVHFTASSVEYKSSNKQPKPTKQPRTPRPPSTSQALYPGPNQPPIAPYQTRPPIPIICPTGCTCNLHINDLGLTVNCKERGFNNISELLPRPLNAKKLYLSSNLIQKIYRSDFWNFSSLDLLHLGNNRISYVQDGAFINLPNLKSLFLNGNDIEKLTPGMFRGLQSLHYLYFEFNVIREIQPAAFSLMPNLKLLFLNNNLLRTLPTDAFAGTSLARLNLRKNYFLYLPVAGVLEHLNAIVQIDLNENPWDCTCDLVPFKQWIETISSVSVVGDVLCRTPENLTHRDVRTIELEVLCPEMLHIAQPGPSPPQSGDYHPNGGPTSASPYDFSPPGGPVPLSVLILSLLVLFFSAVFVAAGLFAYVLRRRRKKLPFRSKRQEGVDLTGIQMQCHRLFEDSGGSGGGSGSGGRPTLSSPEKAPPVGHVYEYIPHPVTQMCNNPIYKPREEEEVAASAAQDTGATDRGGPGTQPPGMGEVLLGSEQFAETPKENHSNYRTLLEKEKEWALAVSNSQLNTIVTVNHHHPHPHHSAVGGVSGVGGGTGGDLAGFRHHEKNGGVVLFPPGGGCGGGSLLLERERPQPAPCTVGFVDCLYGTVPKLKELHVHPPGMQYPDLQQDARLKETLLFSAGKGFTDHQTPKSDYLDLRAKLQTKPDYLEVLEKTAYRF