wanglab/gogpt-training-data huggingface dataset:
Protein: ADP-ribosylation factor 1 (EC 3.6.5.2) (P84077)
Organism: Homo sapiens (Human)
Function: Small GTPase involved in protein trafficking between different compartments. Modulates vesicle budding and uncoating within the Golgi complex. In its GTP-bound form, triggers the recruitment of coatomer proteins to the Golgi membrane. The hydrolysis of ARF1-bound GTP, which is mediated by ARFGAPs proteins, is required for dissociation of coat proteins from Golgi membranes and vesicles. The GTP-bound form interacts with PICK1 to limit PICK1-mediated inhibition of Arp2/3 complex activity; the function is linked to AMPA receptor (AMPAR) trafficking, regulation of synaptic plasticity of excitatory synapses and spine shrinkage during long-term depression (LTD) (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:17555535}; Lipid-anchor {ECO:0000269|PubMed:17555535}; Cytoplasmic side {ECO:0000305}. Synapse, synaptosome {ECO:0000250|UniProtKB:P84079}. Postsynaptic density {ECO:0000250|UniProtKB:P84079}. Note=In the GDP-bound form, associates transiently with the membranes via its myristoylated N-terminus where guanine nucleotide-exchange factor (GEF)-mediated nucleotide exchange occurs (By similarity). Following nucleotide exchange, the GTP-bound form undergoes a conformational change, leading to the exposure of a myristoylated N-terminal amphipathic helix that provides stable membrane anchorage (By similarity). {ECO:0000250|UniProtKB:P84080}.
Interaction partners:
- Cytohesin-2
- Cytohesin-1
- Pleckstrin homology domain-containing family A member 3
- ADP-ribosylation factor-binding protein GGA1
- AP-1 complex subunit beta-1
- Coatomer subunit beta
- Phospholipase D2
- IQ motif and SEC7 domain-containing protein 1
- ADP-ribosylation factor GTPase-activating protein 1
- Cytohesin-3
Sequence:
MGNIFANLFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAVLLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQK
Protein: tryptophan--tRNA ligase (EC 6.1.1.2) (Tryptophanyl-tRNA synthetase) (G3V3H8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MLVSLKMSYKAAAGEDYKADCPPGNPAPTSNHGPDATEAEEDFVDPWTVQTSSAKGIDYDKLIVRFGSSKIDKELINRIERATGQRPHHFLRRGIFFSHRDMNQVLDAYENKKPFYLYTGRGPSSEAMHVGHLIPFIFTKWLQDVFNVPLVIQMTDDEKYLWKDLTLDQAYSYAVENAKDIIACGFDINKTFIFSDLDYMGMSSGFYKNVVKIQKHVTFNQVK
Protein: Deoxynucleoside-5'-monophosphate kinase (EC 2.7.4.13) (Q6QGP4)
Organism: Escherichia phage T5 (Enterobacteria phage T5)
Function: Allows the synthesis of deoxyribonucleoside triphosphates necessary for the rapid viral DNA replication. Phosphorylates all four dNMPs.
Interaction partners:
Sequence:
MSVLVGLHGEAGSGKDTVAKLIIDWCNDTYPTCLSRRYSFAKPVYELASVILGVTPEFLGERRGKEIDQWFTVTQSQLERARDVWFKYGIDKFEDFSYVWPIFEEKYLNPQQLISENKEDGLYSLFISPRKMLQLVGTELGRQLVHERIWLIILEQSIAKDDPDVAVITDVRFPNEGELLRETNHLDMDSLLVNVVPAEQKFTIKSDHPSESGIPAKYITHELVNKFDGINNLKLEVYNFCDLELEPLVG
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (Q95XP6)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
Sequence:
MPEYGASLEELRALMEYRSAEAKEKIETDYGGTTGLCERLKTDPNNGLPNNEEELERRRNVFGANEIPPHPPKCFLQLVWEALQDVTLVILLVSAIVSLALSFYRPPGEDTAGSDDSEHDAGWIEGVAILISVIVVVLVTALNDYTKERQFRGLQAKIETEHRFFVLRGGQSVQVVVNELVVGDIAQIKYGDLIPSDGIIIQSNDLKMDESSLTGESDQIRKSPEHDPIILSGTHVMEGSGKMLVTAVGVNSQTGIIMTLLGAAKTVAEEERKTAKREGGDGASGAEEGTAQALLDSKGDEAMANGKAVAAAESDGKKERSVLQAKLTRLAIQIGYAGSFVAGCTVLILIIRFCISRYAIDGKSFSLADFQHFINFLIIGVTVLVVAVPEGLPLAVTLSLAYSVKKMMLDNNLVRHLDACETMGNATAICSDKTGTLTTNRMTVVQSFVNDVHYKDTPKIESLDQNTAKLMMDCISINSSYSSQVIPPKQLGEQATQLGNKTECGMLGFVLALGKSYQEIRDRHPEETIPKVYTFNSVRKSMSTVINLPDGGYRVFSKGASEIVTKRCKYFLGKNGTLTKFSSKDAENLVRDVIEPMASDGLRTICVAYKDYVPSSKKTADNQIAYSSEPDWENEEMIVGDMTAIAVLGIQDPVRPEVPAAITRCQEAGITVRMVTGDNINTARSIATACGILKPGEDFIALEGKEFNARIRDENGEVSQEKLDLIWPKLRVLARAQPSDKYVLVKGIIDSRVTDSREVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSIAKFLQFQLTVNVVAVVVAFVGACAIQDTPLKAVQMLWVNLIMDTLASLALATEMPTEELLKRKPYGRTSPLISRTMCKNILGHAVYQLVILFTLIFYGEVCFNIPSGRWAPLHSPPSKHFTIVFNTFVMMTLFNEINARKIHGERNIFKGLFSNPIYYVIWIATMISQVVIIQFGGRWFSTSALNTTEWLWCLAFGVGTLLWGQIVTSIPTGSLPANMTIGSGEAPTNDPLMPDYEDSDTHEKRSGQILWVRGLTRLQTQVIGGERSDHLIPVPLSSAPTDQAIRVVKAFQAGLDRREPSLTGQSAARLREISRQLRLQVDSENRSRSTSRGNIKETNNL
Protein: Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 1 (Q9JKB0)
Organism: Rattus norvegicus (Rat)
Function: Hyperpolarization-activated ion channel exhibiting weak selectivity for potassium over sodium ions. Contributes to the native pacemaker currents in heart (If) and in neurons (Ih). May mediate responses to sour stimuli.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11675786}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O60741}.
Interaction partners:
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 2
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 3
- Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel 4
Sequence:
MEGGGKPNSASNSRDDGNSVYPSKAPATGPAAADKRLGTPPGGGAAGKEHGNSVCFKVDGGGGEEPAGSFEDAEGPRRQYGFMQRQFTSMLQPGVNKFSLRMFGSQKAVEKEQERVKTAGFWIIHPYSDFRFYWDLIMLIMMVGNLVIIPVGITFFTEQTTTPWIIFNVASDTVFLLDLIMNFRTGTVNEDSSEIILDPKVIKMNYLKSWFVVDFISSIPVDYIFLIVEKGMDSEVYKTARALRIVRFTKILSLLRLLRLSRLIRYIHQWEEIFHMTYDLASAVVRIFNLIGMMLLLCHWDGCLQFLVPLLQDFPPDCWVSLNEMVNDSWGKQYSYALFKAMSHMLCIGYGAQAPVSMSDLWITMLSMIVGATCYAMFVGHATALIQSLDSSRRQYQEKYKQVEQYMSFHKLPADMRQKIHDYYEHRYQGKIFDEENILSELNDPLREEIVNFNCRKLVATMPLFANADPNFVTAMLSKLRFEVFQPGDYIIREGAVGKKMYFIQHGVAGVITKSSKEMKLTDGSYFGEICLLTKGRRTASVRADTYCRLYSLSVDNFNEVLEEYPMMRRAFETVAIDRLDRIGKKNSILLQKFQKDLNTGVFNNQENEILKQIVKHDREMVQAIPPINYPQMTALNCTSSTTTPTSRMRTQSPPVYTATSLSHSNLHSPSPSTQTPQPSAILSPCSYTTAVCSPPIQSPLATRTFHYASPTASQLSLMQQPQPQLQQSQVQQTQPQPQPQPQQPQQQQQQQQQQQQQQQQQQQQQQPQTPGSSTPKNEVHKSTQALHNTNLTREVRPLSASQPSLPHEVSTMISRPHPTVGESLASIPQPMATVHSTGLQAGSRSTVPQRVTLFRQMSSGAIPPNRGVPPAPPPPAAVQRESPSVLNKDPDAEKPRFASNL
Protein: Peroxisomal fatty acid beta-oxidation multifunctional protein (MFP) [Includes: Enoyl-CoA hydratase/3-2-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase (EC 4.2.1.17) (EC 5.1.2.3) (EC 5.3.3.8); 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35)] (Q8W1L6)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Multifunctional enzyme involved in fatty acid beta-oxidation. Also binds to RNA and microtubules. Possible role in subcellular mRNA localization and RNA-cytoskeleton interactions.
Subcellular location: Peroxisome {ECO:0000305}. Cytoplasm, cytoskeleton {ECO:0000305}.
Interaction partners:
- acetyl-CoA C-acyltransferase
- acetyl-CoA C-acyltransferase
- Os01g0110400 protein
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Acyl-coenzyme A oxidase
- Enoyl-CoA hydratase/isomerase family protein, expressed
- Os09g0252100 protein
- Os07g0675000 protein
- Os05g0163700 protein
Sequence:
MAGAIRVTMEVGADGVAVVTICNPPVNALHPIIIQGLKEKYAEAMDRDDVKAIVLTGAGGKFCGGFDINVFTEVHKTGNVSLMPDVSVELVSNLMEAGKKPSVAAIQGLALGGGLELTMGCHARISTPEAQLGLPELTLGIIPGFGGTQRLPRLVGLPKAIEMMLQSKFITAKEGKEGGLVDALCSPDELIKMSRLWALEIANYRKPWIRSLARTDRLGSLSEARSVLNSARQQAKKVAANLPQHQACLDVMEEGVLCGGHAGVLKEAKVFKELVLSPTSKALVHAFFAQRLTTKVPGVTDVQLKPRKIRKVAVIGGGLMGSGIATALLVSNTSVVLKEVNPQFLQRGQKMIAANLEGLVKRGSLTKDKMNKAMSLLKGALDYSDFKDVDMVIEAVIEKIPLKQSIFSDLEKVCPPHCILATNTSTIDLNVVGEKTNSQDRIIGAHFFSPAHIMPLLEIVRTEKTSPQAILDLITVGKMIKKVPVVVGNCTGFAVNRTFFPYTQGSHLLVSIGIDVFRIDRVISSFGMPMGPFQLQDLAGYGVALAVKDIYAAAFGTRNLDSNLVDLMVQNGRQGKSNGKGYYLYEKGGKPKPDPSVQVVIDEYRRCAKTMPGGKPVTLSDQDILEMIFFPVVNEACRVMDENVVIRASDLDIASILGMGFPKFRGGLVFWADTIGAPYIHSKLSKWTEIYGDFFKPSSYLEDRAKRSLPLSAPNATQQASSRSRM
Protein: Aspartate kinase (EC 2.7.2.4) (Aspartokinase) (Q88EI9)
Organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)
Function: Involved in the biosynthesis of L-aspartate-beta-semialdehyde which is a central intermediate in the biosynthesis of different amino acids (L-lysine, L-methionine, L-threonine). Catalyzes the phosphorylation of the beta-carboxyl group of L-aspartate to yield 4-phospho-L-aspartate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Aspartate-semialdehyde dehydrogenase
- homoserine dehydrogenase
- Homoserine dehydrogenase
- Diaminopimelate decarboxylase
- Aspartate-semialdehyde dehydrogenase
- Diaminopimelate decarboxylase
- Homoserine O-succinyltransferase
- Argininosuccinate synthase
- 4-hydroxy-tetrahydrodipicolinate reductase
- asparagine synthase
Sequence:
MALIVQKFGGTSVGSIERIEQVAEKVKKHREAGDDLVVVLSAMSGETNRLIDLAKQITDQPVPRELDVIVSTGEQVTIALLTMALIKRGVPAVSYTGNQVRILTDSSHNKARILQIDDQKIRADLKEGRVVVVAGFQGVDEHGSITTLGRGGSDTTGVALAAALKADECQIYTDVDGVYTTDPRVVPQARRLEKITFEEMLEMASLGSKVLQIRSVEFAGKYNVPLRVLHSFKEGPGTLITIDEEESMEQPIISGIAFNRDEAKLTIRGVPDTPGVAFKILGPISASNIEVDMIVQNVAHDNTTDFTFTVHRNEYEKAQSVLENTAREIGAREVIGDTKIAKVSIVGVGMRSHAGVASCMFEALAKESINIQMISTSEIKVSVVLEEKYLELAVRALHTAFDLDAPARQGE
Protein: Helicase swr1 (EC 3.6.4.12) (O13682)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549}.
Interaction partners:
- Histone H2A.Z
- RuvB-like helicase 2
- Actin-like protein arp6
- SWR1 complex subunit vps71
- SWR complex protein 2
- RuvB-like helicase 1
- SWR1-complex protein 4
- Actin-related protein 4
- Actin
- Protein AF-9 homolog
Sequence:
MTYEESEKNKNGLSSYIKKEGSSDLKVRVRFREPKLLVTHSGHITEQPKYEHLEQYLDSYVSLEDGDHDPKEAKELVFREVQLRHRINEFRKKGYFTAEAPVELKKAPSSNNIPISYRDNLLSHVNGYARSMHNDRKVRASRSRRISGMILAHFKRLSGADEKKAKEEDKRIRLLAKRTAWEIRKKWKVIEREVRRRRAERAAEAQRVAGKEQLANILKHSTDLLEARIERANINISAQTSESAVDWNYLLKTSDDLLSVDELKLKYSNPDLIKNIEREEEAEETSDDEPLSSEDEENEDEDITEESNLRKRKVSDKTRVVNKHPPSLRRSRRFFAKKSYNHVSDLDGEVIVMKKEDITDGVSTKKDLNDGDQNEVPLHDTGSSSSLSLLYNEDVASKKKRRVNDDGLARKKSIAGISEQRKFDEPNGSPVLHANKIQVPFLFRGTLREYQQYGLEWLTALHDSNTNGILADEMGLGKTIQTIALLAHLACEKENWGPHLIIVPTSVMLNWEMEFKKFLPGFKILTYYGNPQERKEKRSGWYKPDTWHVCITSYQLVLQDHQPFRRKKWQYMILDEAHNIKNFRSQRWQSLLNFNAEHRLLLTGTPLQNNLVELWSLLYFLMPAGVTQNNSAFANLKDFQDWFSKPMDRLIEEGQDMNPEAMNTVAKLHRVLRPYLLRRLKTEVEKQMPAKYEHVVYCQLSKRQRFLYDDFINRARTREILASGNFMSIINCLMQLRKVCNHPNLHEERPIVTSFALRRSAIADLEIKDLLVRKRLLHEEPMTKLDLSTLRLIRTDSEAFDTFVSDELNSLCATNAYNRISTFLRMQIDEECKPCQFKKSNFKEHFQNKIYQEQLDKLNFQKYLNESKCSHSPIYGSNLIRLAEKLPKHSTSIDYTLYAKDDPLYLLNTTKALRSCILSTEERASNMKEIIQRFACITPKAVVVDLPELFCKTIPRDLLYEVSRKINPLHQASTRLAIAFPDKRLLQYDCGKLQVLDRLLKDLVSNGHRVLIFTQMTKVLDILEQFLNIHGHRYLRLDGATKIEQRQILTERFNNDDKIPVFILSTRSGGLGINLTGADTVIFYDSDWNPQLDAQAQDRSHRIGQTRDVHIYRLISEYTVESNMLRRANQKRMLDKIVIQGGEFTTEWFRKADVLDLFDLDDESLKKVKADSDSGSTKNEENWEVALAAAEDEEDVQAAQVARKESALEQTEFSETSTPQAMLTKDSTPLSSDSATPGFERDSTEEQSNTNDMDEDRSELEEDLDETVGHIDEYMISFLEQEGTSDEW
Protein: Ankyrin repeat family protein (At2g03430) (Putative ankyrin) (Q8GZ22)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome non-ATPase regulatory subunit 4 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 7 homolog B
- 26S proteasome non-ATPase regulatory subunit 7 homolog A
- 26S proteasome regulatory subunit 4 homolog A
- 26S proteasome regulatory subunit RPN13
- 26S proteasome non-ATPase regulatory subunit 12 homolog A
- 26S proteasome regulatory subunit 6A homolog B
Sequence:
MEIATDTAKQMRDEELFKAAEWGDSSLFMSLSEEQLSKSLNFRNEDGRSLLHVAASFGHSQIVKLLSSSDEAKTVINSKDDEGWAPLHSAASIGNAELVEVLLTRGADVNAKNNGGRTALHYAASKGRLEIAQLLLTHGAKINITDKVGCTPLHRAASVGKLEVCEFLIEEGAEIDATDKMGQTALMHSVICDDKQVAFLLIRHGADVDVEDKEGYTVLGRATNEFRPALIDAAKAMLEG
Protein: Small ribosomal subunit protein uS8 (C3SR12)
Organism: Escherichia coli
Interaction partners:
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein uS7
- 50S ribosomal protein L11
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS17
- GTP pyrophosphokinase
- Alternative ribosome-rescue factor A
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein uL6
- DNA-directed RNA polymerase subunit alpha
Sequence:
MSMQDPIADMLTRIRNGQAANKAAVTMPSSKLKVAIANVLKEEGFIEDFKVEGDTKPELELTLKYFQGKAVVESIQRVSRPGLRIYKRKDELPKVMAGLGIAVVSTSKGVMTDRAARQAGLGGEIICYVA
Protein: Proteasome subunit alpha type-7 (Proteasome subunit alpha 4) (Q95005)
Organism: Caenorhabditis elegans
Function: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Proteasome subunit beta type-2
- Proteasome subunit alpha type-1
- Proteasome subunit alpha type-3
- Proteasome subunit alpha type-2
- Proteasome subunit pbs-5
- Proteasome subunit alpha type-5
- Proteasome subunit beta type-1
- Proteasome subunit beta
- Proteasome subunit beta type-3
- Proteasome subunit beta
Sequence:
MNRYDRAITIFSPDGHLFQVEYAQEAVKKGSTAVGVRGKDCIVIGVEKKSIPALQDDRTIRKIHMIDDHVMLAFAGLSADARVLVDRARIECQSYKLTLEDPVTVAYISRYIANTKQRFTQSPGRRPFGISMLIGGFDHDGTPRLFKTEPSGAYYEYVANATGRGEKPVREYLEEQYSEENTVDEATTLKLVVKSLAQVVPPGSQNIEIAVMKKVNDELQQRVLSTEEIEALLKVVETERVAAEAEEAASKKK
Protein: SMC5-SMC6 complex localization factor 2 (B1AL16)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTRRCMPARPGFPSSPAPGSSPPRCHLRPGSTAHAAAGKRTESPGDRKQSIIDFFKPASKQDRHMLDSPQKSNIKYGGSRLSITGTEQFERKLSSPKESKPKRVPPEKSPIIEAFMKGVKEHHEDHGIHESRRPCLSLASKYLAKGTNIYVPSSYHLPKEMKSLKKKHRSPERRKSLFIHENNEKNDRDRGKTNADSKKQTTVAEADIFNNSSRSLSSRSSLSRHHPEESPLGAKFQLSLASYCRERELKRLRKEQMEQRINSENSFSEASSLSLKSSIERKYKPRQEQRKQNDIIPGKNNLSNVENGHLSRKRSSSDSWEPTSAGSKQNKFPEKRKRNSVDSDLKSTRESMIPKARESFLEKRPDGPHQKEKFIKHIALKTPGDVLRLEDISKEPSDETDGSSAGLAPSNSGNSGHHSTRNSDQIQVAGTKETKMQKPHLPLSQEKSAIKKASNLQKNKTASSTTKEKETKLPLLSRVPSAGSSLVPLNAKNCALPVSKKDKERSSSKECSGHSTESTKHKEHKAKTNKADSNVSSGKISGGPLRSEYGTPTKSPPAALEVVPCIPSPAAPSDKAPSEGESSGNSNAGSSALKRKLRGDFDSDEESLGYNLDSDEEEETLKSLEEIMALNFNQTPAATGKPPALSKGLRSQSSDYTGHVHPGTYTNTLERLVKEMEDTQRFVSIKINLLNLTFCLFVWLTFNLPFLKNHEKLACILDSVVNCVRIRYVGRTQWLMPVITTLWETQARLLEPRSSRLR
Protein: EGF-like repeat and discoidin I-like domain-containing protein 3 (Developmentally-regulated endothelial cell locus 1 protein) (Integrin-binding protein DEL1) (O43854)
Organism: Homo sapiens (Human)
Function: Promotes adhesion of endothelial cells through interaction with the alpha-v/beta-3 integrin receptor. Inhibits formation of vascular-like structures. May be involved in regulation of vascular morphogenesis of remodeling in embryonic development.
Subcellular location: Secreted.
Interaction partners:
- Ubiquitin-like protein FUBI
- Hyaluronan and proteoglycan link protein 1
Sequence:
MKRSVAVWLLVGLSLGVPQFGKGDICDPNPCENGGICLPGLADGSFSCECPDGFTDPNCSSVVEVASDEEEPTSAGPCTPNPCHNGGTCEISEAYRGDTFIGYVCKCPRGFNGIHCQHNINECEVEPCKNGGICTDLVANYSCECPGEFMGRNCQYKCSGPLGIEGGIISNQQITASSTHRALFGLQKWYPYYARLNKKGLINAWTAAENDRWPWIQINLQRKMRVTGVITQGAKRIGSPEYIKSYKIAYSNDGKTWAMYKVKGTNEDMVFRGNIDNNTPYANSFTPPIKAQYVRLYPQVCRRHCTLRMELLGCELSGCSEPLGMKSGHIQDYQITASSIFRTLNMDMFTWEPRKARLDKQGKVNAWTSGHNDQSQWLQVDLLVPTKVTGIITQGAKDFGHVQFVGSYKLAYSNDGEHWTVYQDEKQRKDKVFQGNFDNDTHRKNVIDPPIYARHIRILPWSWYGRITLRSELLGCTEEE
Protein: Capsid protein (Coat protein) (p38) (P06663)
Organism: Turnip crinkle virus (TCV)
Function: Capsid protein self-assembles to form an icosahedral capsid with a T=3 symmetry, about 32-35 nm in diameter, and consisting of 180 capsid proteins. Also acts as a suppressor of RNA-mediated gene silencing known as post-transcriptional gene silencing (PTGS), a mechanism of plant viral defense that limits the accumulation of viral RNAs. May suppress other innate immunity by binding to host TIP protein, thereby preventing it to migrate in the nucleus where it could trigger an antiviral response.
Subcellular location: Virion.
Interaction partners:
Sequence:
MENDPRVRKFASDGAQWAIKWQKKGWSTLTSRQKQTARAAMGIKLSPVAQPVQKVTRLSAPVALAYREVSTQPRVSTARDGITRSGSELITTLKKNTDTEPKYTTAVLNPSEPGTFNQLIKEAAQYEKYRFTSLRFRYSPMSPSTTGGKVALAFDRDAAKPPPNDLASLYNIEGCVSSVPWTGFILTVPTDSTDRFVADGISDPKLVDFGKLIMATYGQGANDAAQLGEVRVEYTVQLKNRTGSTSDAQIGDFAGVKDGPRLVSWSKTKGTAGWEHDCHFLGTGNFSLTLFYEKAPVSGLENADASDFSVLGEAAAGSVQWAGVKVAERGQGVKMVTTEEQPKGKWQALRI
Protein: M93 protein (H2A1V7)
Organism: Murid herpesvirus 1 (MuHV-1) (Mouse cytomegalovirus)
Interaction partners:
Sequence:
METHLRFEQAASEDDRDRLVPVHVVFAEDALSYREFEGLHTLCFKIISRPDARWEHIPYFERLDREFVLKSLFHDKCRHLSASPGDGPWTLHGGGDENCRYGLAFSVVLHLRDVEWWKDVIKFRLFIGDDETVDIDCTFVRLLREGLRFFGEVRRTRQPRSGPRSASSRLLHHHHPHHHRAGAAGDDDGDVDDDEGLPEGLLGAAADGPGFFDLGDNRKMSEEMEDRLARFALKRVSAADFGPLEPPSKVRGREIKARRGEFFRDGDAPAAPDPVRSRSDRWFGCDNAIRISYAQEVTGSRRFAVIWYSESIGSTVDVDVGRADDGEAAVTSFEHTRRWETAVTRVYGATSRQLAAAVTRVGGLAQRFYVNLYAGLRAGDLVELLLLSRDAWLVNGTGGGCIIKALSSDLHRRRRSGDLVDGCRVGWADVIWYAQARVASGIPIKLMRVGGDGLWRSFLDSGKLTDWELNTDVCVLYAFEDRSLFWVLPGGFCAAFQLQVDHGDVQTIREKFEKHQ
Protein: Beta-citrylglutamate synthase B (EC 6.3.1.17) (N-acetyl-aspartylglutamate synthetase B) (NAAG synthetase B) (NAAGS) (EC 6.3.2.41) (Ribosomal protein S6 modification-like protein B) (Q9ULI2)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of beta-citryl-L-glutamate and N-acetyl-L-aspartyl-L-glutamate. Beta-citryl-L-glutamate is synthesized more efficiently than N-acetyl-L-aspartyl-L-glutamate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- N-acetylaspartate synthetase
- Glutamate carboxypeptidase 2
- Aspartoacylase
- N-acetylaspartylglutamate synthase A
- Isocitrate dehydrogenase subunit gamma, mitochondrial
- Isocitrate dehydrogenase subunit alpha, mitochondrial
- Isocitrate dehydrogenase subunit beta, mitochondrial
- Citrate synthase, mitochondrial
- 2-oxoglutarate dehydrogenase-like, mitochondrial
- 2-oxoglutarate dehydrogenase complex component E1
Sequence:
MCSSVAAKLWFLTDRRIREDYPQKEILRALKAKCCEEELDFRAVVMDEVVLTIEQGNLGLRINGELITAYPQVVVVRVPTPWVQSDSDITVLRHLEKMGCRLMNRPQAILNCVNKFWTFQELAGHGVPLPDTFSYGGHENFAKMIDEAEVLEFPMVVKNTRGHRGKAVFLARDKHHLADLSHLIRHEAPYLFQKYVKESHGRDVRVIVVGGRVVGTMLRCSTDGRMQSNCSLGGVGMMCSLSEQGKQLAIQVSNILGMDVCGIDLLMKDDGSFCVCEANANVGFIAFDKACNLDVAGIIADYAASLLPSGRLTRRMSLLSVVSTASETSEPELGPPASTAVDNMSASSSSVDSDPESTERELLTKLPGGLFNMNQLLANEIKLLVD
Protein: UTP--glucose-1-phosphate uridylyltransferase (EC 2.7.7.9) (Q9VSW1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Phosphoglucomutase 1
- Probable galactose-1-phosphate uridylyltransferase
- Glycogen phosphorylase
- BcDNA.GH08860
- Glycogen [starch] synthase
- Glycogen debranching enzyme
- UDP-glucose 4-epimerase
- UDP-glucose 6-dehydrogenase
- Phosphoglucomutase 2b
- Phosphoglucomutase 2a
Sequence:
MPSGIRPIDVLLERAGVRGHQRAPSDSKEFHEVTKRDALRLLEHDVDRLLETTEKARQPALKAEMGRFADLFGRFIQEEGPALDWNKIQKLPENAVMNYSNLKSPKNEQNEIRNMLDKLVVIKLNGGLGTSMGCHGPKSVIPVRSDLTFLDLTVQQIEHLNKTYDANVPLVLMNSFNTDEDTEKIVRKYKGFRVQIHTFNQSCFPRISREHYLPVAKDFDVEKDMEAWYPPGHGDFYDTFRNSGLLKKFIEEGREYCFLSNIDNLGATVDLNILNKLVGEERATTPVEFVMEVTDKTRADVKGGTLIQMENKLRLLEIAQVPPEHVDDFKSVKTFKFFNTNNIWANLAAIDRVLRERTLNMEIIVNNKTLENGTRVIQLETAVGAAMKCFDGAIGINVPRSRFLPVKKSSDLLLVMSNLYTLKNGSLVMSPQRMFPTTPLVKLGENHFSKVKEFLGRFANIPDIIELDHLTVSGDVTFGRGVSLRGTVIIIANHGDRIDIPAGAILENKIVSGNMRILDH
Protein: Protein E6 (Q77E16)
Organism: Human papillomavirus type 16
Subcellular location: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123}.
Interaction partners:
Sequence:
MFQDPQERPIKLPDLCTELQTTIHDIILECVYCKQQLLRREVYDFAFRDLCIVYRDGNPYAVCDKCLKFYSKISEYRYYCYSLYGTTLEQQYNKPLCDLLIRCINCQKPLCPEEKQRHLDKKQRFHNIRGRWTGRCMSCCRSSRTRRETQL
Protein: E3 ubiquitin-protein ligase RGLG5 (EC 2.3.2.27) (RING domain ligase 5) (Q8LB88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with RGLG1, mediates the ubiquitination and subsequent proteasomal degradation of the target protein PP2CA. Functions as positive regulator of abscisic acid (ABA) signaling through ABA-dependent degradation of PP2CA, a major inhibitor of ABA signaling.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}.
Interaction partners:
- Protein phosphatase 2C 37
- U-box domain-containing protein 12
- U-box domain-containing protein 13
- E3 ubiquitin-protein ligase RHA2A
- E3 ubiquitin-protein ligase RHA2B
- Abscisic acid receptor PYL8
- E3 ubiquitin-protein ligase SDIR1
- DET1- and DDB1-associated protein 1
Sequence:
MGGSSSKESPRGGGSGRRYERSVSGSSSYSSAWDQSSYYQTPNHPSASPVSSYNSGRQTPKNLERKYSRIADNYRSIDEVTAALSHAGLESSNLIVGIDVTKSNEWTGARSFGRKSLHFIGTTPNPYQQAISIIGKTLSVFDEDNLIPCYGFGDATTHDQDVFSFNPNDTYCNGFEEVLMCYREIVPQLRLSGPTSFAPIIERAMTIVEESGGQYHVLLIIADGQVTRSVDTDNGGFSPQEQQTIDAIVRASEYPLSIVLVGVGDGPWDTMRQFDDNIPARAFDNFQFVNFTDIMSKNIDPARKEAEFALSALMEIPSQYKATLELGLLGQRTGHCPDRIALPPPTYATQSMRNSPRTSRSTSFQNKPYDNGVSSTPPSTTHNESQQQFCPVCLVSAKNMAFNCGHQTCAGCGEDLHVCPICRSSISVRIKLY
Protein: R2R3 MYB protein (R2R3 MYB transcription factor) (M1FPW6)
Organism: Thinopyrum intermedium
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDMDKEYYKACMGMEALPMSPAGLSAVTTEVAMAAATASEDEGDLRGGPWTAEEDMLLVDYISKHGEGRWNSLARCAGLRRTGKSCRLRWLNYLRPDVRRGNITPEEQLLILDLHSRWGNRWSKIAQRLPGRTDNEVKNYWRTRVQKHAKQLHCDVNSDRFRDVVRQVWMPRLLERIQAESSSSAGAAAAGVGVPALTRAMGSPAGASQYHCFDHASSGEPSRKVAVTMSPDTSSTLRSSLSPAETYGAHFPAWGAATATANVDGSMMQCGGRECGAIGGDQYVIHGDSLSGSWSELLAATDIPDFEFGNFDDNLWNLEDIYC
Protein: Cation-chloride cotransporter 1 (OsCCC1) (Potassium-chloride cotransporter 1) (Q6Z0E2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Probable cation/chloride cotransporter that may mediate potassium-chloride cotransport. Involved in plant development and K(+) and Cl(-) homeostasis. May not be involved in sodium-chloride cotransport.
Subcellular location: Membrane {ECO:0000269|PubMed:21369877}; Multi-pass membrane protein {ECO:0000269|PubMed:21369877}.
Interaction partners:
Sequence:
MENGEIEGAADDGVPVPAPPNGRRYRPVGSSDRAVIQMTSMEPGSSSSTAVAAVSGITPQPPRNLTVDPSMQEDHTVSQGDSKLELFGFDSLVNILGLKSMTGEQIQAPSSPRDGEDVAITIGRPKETGPKFGTMMGVFVPCLQNILGIIYYIRFTWIVGMAGVWQSLVLVSFCGACTFLTGISLSAIATNGAMKGGGPYYLIGRALGPEVGVSIGLCFFLGNAVAGSMYVLGAVETFLDAVPSAGFFKESVTVVNNTLVNGTATASTATISTPSLHDLQVYGVIVTILLCFIVFGGVKIINKVAPAFLIPVLFSLLCIYLGVFIAPRHNAPKGITGLSITTFKDNWGSEYQRTNNAGVPDPNGSIYWDFNALVGLFFPAVTGIMAGSNRSASLKDTQRSIPIGTLSATLTTTAMYLFSVLLFGALATREELLTDRLLTATVAWPAPAVIYIGIILSTLGAALQSLTGAPRLLAAIANDDILPVLNYFKVSEGAEPHSATLFTAFICICCVVIGNLDLITPTITMFFLLCYAGVNLSCFLLDLLDAPSWRPRWKFHHWSLSLVGALLCVVIMFLISWSFTVVSLALASLIYYYVSLKGKAGDWGDGFKSAYFQLALRSLRSLGANQVHPKNWYPIPLIFCRPWGKLPENVPCHPKLADFANCMKKKGRGMSIFVSIIDGDYHELAEDAKTACRQLDTYIEYKRCEGVAEIIVAPSMSEGFRSIVQTMGLGNLKPNIIVMRYPEIWRRENLIQIPSTFVSIINDCIIANKAVVIVKGLDEWPNEYQRQYGTIDLYWIVRDGGLMLLLSQLLLTKETFESCKIQVFCIAEEDTDAEELKADVKKFLYDLRMHAEVIVVTMKSWEPHMESSSSGAPQDDSQEAYTSAQRRISTYLSEMKETAQREGHPLMEDGKQVVVNEQKIEKFLYTMFKLNSTILRYSRMAAVVLVSLPPPPLNHPAYFYMEYMDLLVENVPRMLIVRGYRRDVVTFFT