wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-ionylideneethane synthase aba3 (EC 4.2.3.-) (Abscisic acid biosynthesis cluster protein 3) (Sesquiterpene synthase aba3) (Q14RS2)
Organism: Botryotinia fuckeliana (Noble rot fungus) (Botrytis cinerea)
Function: Alpha-ionylideneethane synthase; part of the gene cluster that mediates the biosynthesis of abscisic acid (ABA), a phytohormone that acts antagonistically toward salicylic acid (SA), jasmonic acid (JA) and ethylene (ETH) signaling, to impede plant defense responses. The first step of the pathway catalyzes the reaction from farnesyl diphosphate to alpha-ionylideneethane performed by the alpha-ionylideneethane synthase aba3 via a three-step reaction mechanism involving 2 neutral intermediates, beta-farnesene and allofarnesene. The cytochrome P450 monooxygenase aba1 might then be involved in the conversion of alpha-ionylideneethane to alpha-ionylideneacetic acid (Probable). Alpha-ionylideneacetic acid is further converted to abscisic acid in 2 steps involving the cytochrome P450 monooxygenase aba2 and the short-chain dehydrogenase/reductase aba4, via the intermediates 1'-deoxy-ABA or 1',4'-trans-diol-ABA, depending on the order of action of these 2 enzymes (Probable). Aba2 is responsible for the hydroxylation of carbon atom C-1' and aba4 might be involved in the oxidation of the C-4' carbon atom.
Interaction partners:
Sequence:
MQQVITQTLVDDRFIQISDSKKSEGLATDSTKRQSQEQPIHDKDPIKAATAAMATTPLVKEHQDTWYYPPDIANDLQSINLPAELKGEIFACAWEYTRCVIPNYTNWNRYVAFMRIIIMGIIAEFRGEMVDVTASNNLLGYDLDATLAALFEGTPGHKEMAREYKTFLLITADKASERRDGELFRRYVNALAQSPRHWFRMRDCDALARFTIASALACNDLDDIWFTEDQFEILTEIGDTLYDAVAFYKHRAEGETNSTFAYMPEDLRIKAYSECREILWALDAAWARNPKLANVINFVRFFGGPIHMMMRRYRFVEENLTIGKSETDKVVDQTRKNFKLWNRVDANKRSVLNTQRYKALIARSEELMFPGLAEFLEMGGDGICDKCKYRESTVQNCHTSLVVLNYAANADYRGEST
Protein: Sodium- and chloride-dependent betaine transporter (BGT-1) (Na(+)/Cl(-) betaine/GABA transporter) (Sodium- and chloride-dependent GABA transporter 2) (GAT-2) (Solute carrier family 6 member 12) (P31651)
Organism: Mus musculus (Mouse)
Function: Transports betaine and GABA. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation (By similarity).
Subcellular location: Basolateral cell membrane {ECO:0000269|PubMed:22071246}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:22071246}; Multi-pass membrane protein {ECO:0000255}. Note=In kidney, locates in basolateral membranes of renal medulla. In liver, locates in hepatocytes cell membrane. {ECO:0000269|PubMed:22071246}.
Interaction partners:
- Cytosolic arginine sensor for mTORC1 subunit 2
- Glutamate decarboxylase 1
- Glutamate decarboxylase 2
- Sodium/myo-inositol cotransporter
Sequence:
MDRKVAVHEDGYPVVSWVPEEGEMMDQKGKDQVKDRGQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYFIFFFSCGIPVFFLEVALGQYSSQGSVTAWRKICPLLQGIGMASVVIESYLNIYYIIILAWALFYLFSSFTWELPWTTCTNSWNTEHCVDFLNHSSARGVSSSENFTSPVMEFWERRVLGITSGIHDLGSLRWELALCLLLAWIICYFCIWKGVKSTGKVVYFTATFPYLMLIILLIRGVTLPGAYQGIVFYLKPDLLRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYRDSIALCFLNSATSFVAGFVVFSILGFMSQEQGIPISEVAESGPGLAFIAFPKAVTMMPLSQLWSCLFFIMLLFLGLDSQFVCMECLVTASMDMFPQQLRKSGRRDVLILAISVLCYLMGLLLVTEGGMYIFQLFDYYASSGICLLFLSLFEVICIGWVYGADRFYDNVEDMIGYRPWPLVKISWLFLTPGLCLATFFFSLSKYTPLKYNNVYMYPSWGYSIGWLLAFSSMACVPLFIIITFLKTQGSFKKRLRRLITPDPSLPQPGRRPPQDGSSAQNCSSSPAKQELIAWEKETHL
Protein: Beta-amyrin 28-monooxygenase (EC 1.14.14.126) (Beta-amyrin 28-oxidase) (Cytochrome P450 716A17) (VvCYP716A17) (A5BFI4)
Organism: Vitis vinifera (Grape)
Function: Catalyzes the carboxylation of beta-amyrin at the C-28 position to form oleanolic acid. May be involved in saponin biosynthesis in fruit skin.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MEVFFLSLLLICVLSVSIRLYLLLYKHRSHFTGPNLPPGKIGWPMVGESLEFLSTGWKGHPEKFIFDRISKYSSEVFKTSLLGEPAAVFAGAAGNKFLFSNENKLVHAWWPSSVDKVFPSSTQTSSKEEAKKMRKLLPQFLKPEALQRYTGIMDHIAQRHFADSWDNRDEVIVFPLAKRFTFWLACRLFMSIEDPAHVAKFEKPFHVLASGLITIPIDLPGTPFHRAIKASNFIRKELRAIIKQRKIDLAESKASKTQDILSHMLLATDEDGCHMNEMSIADKILGLLIGGHDTASSAITFLVKYMAELPHIYEKVYKEQMEIANSKAPGELLNWDDVQKMRYSWNVACEVMRLAPPLQGAFREAITDFVFNGFSIPKGWKLYWSANSTHKSLECFPQPEKFDPTRFEGAGPAPYTFVPFGGGPRMCPGKEYARLEILIFMHNLVKRFKWDKLLPDEKIIVDPMPMPAKGLPVRLHPHKP
Protein: Ras suppressor protein 1 (RSP-1) (Rsu-1) (Q15404)
Organism: Homo sapiens (Human)
Function: Potentially plays a role in the Ras signal transduction pathway. Capable of suppressing v-Ras transformation in vitro.
Interaction partners:
- LIM and senescent cell antigen-like-containing domain protein 1
- Scaffold protein ILK
- Alpha-parvin
- Beta-parvin
- Gamma-parvin
- LIM and senescent cell antigen-like-containing domain protein 2
- Radial spoke head protein 6 homolog A
- Radial spoke head protein 3 homolog
Sequence:
MSKSLKKLVEESREKNQPEVDMSDRGISNMLDVNGLFTLSHITQLVLSHNKLTMVPPNIAELKNLEVLNFFNNQIEELPTQISSLQKLKHLNLGMNRLNTLPRGFGSLPALEVLDLTYNNLSENSLPGNFFYLTTLRALYLSDNDFEILPPDIGKLTKLQILSLRDNDLISLPKEIGELTQLKELHIQGNRLTVLPPELGNLDLTGQKQVFKAENNPWVTPIADQFQLGVSHVFEYIRSETYKYLYGRHMQANPEPPKKNNDKSKKISRKPLAAKNR
Protein: 60 kDa U4/U6 snRNP-specific spliceosomal protein (PRP4 pre-mRNA processing factor 4 homolog (Yeast), isoform CRA_b) (Q5T1M7)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MASSRASSTATKTKAPDDLVAPVVKKPHIYYGSLEEKERERLAKGESGILGKDGLKAGIEAGNINITSGEVFEIEEHISERQAEVLAEFERRKRARQINVSTDDSEVKACLRALGEPITLFGEGPAERRERLRNILSVVGTDALKKTKKDDEKSKKSKEEYQQTWYHEGPNSLKVARLWIANYSLPRAMKRLEEARLHKEIPETTRTSQMQELHKSLRSLNNFCSQIGDDRPISYCHFSPNSKMLATACWSGLCKLWSVPDCNLLHTLRGHNTNVGAIVFHPKSTVSLDPKDVNLASCAADGSVKLWSLDSDEPVADIEGHTVRVARVMWHPSGRFLGTTCYDRSWRLWDLEAQEEILHQEGHSMGVYDIAFHQDGSLAGTGGLDAFGRVWDLRTGRCIMFLEGHLKEIYGINFSPNGYHIATGSGDNTCKVWDLRQRRCVYTIPAHQNLVTGVKFEPIHGNFLLTGAYDNTAKIWTHPGWSPLKTLAGHEGKVMGLDISSDGQLIATCSYDRTFKLWMAE
Protein: WD and tetratricopeptide repeats protein 1 (Q80ZK9)
Organism: Mus musculus (Mouse)
Function: May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex.
Interaction partners:
- DNA damage-binding protein 1
- Cullin-4A
- Cullin-4B
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 4
- DDB1- and CUL4-associated factor 10
- COP9 signalosome complex subunit 8
- DDB1- and CUL4-associated factor 4
- COP9 signalosome complex subunit 5
- DET1- and DDB1-associated protein 1
Sequence:
MAKVNITRDLIRRQVKERGALSFERRYHVTDPFIRRLGLEAELQGHSGCVNCLEWNEKGDLLASGSDDQHTIVWDPLHHKKLLSMHTGHTANIFSVKFLPHAGDRILITGAADSKVHVHDLTVKETIHMFGDHTNRVKRIATAPMWPNTFWSAAEDGLIRQYDLRENSKHSEVLIDLTEYCGPMVEAKCLTVNPQDNNCLAVGASGPFVRLYDIRMIHNHRKSMRQSPSAGVHTFCDRQKPLPDGAAQYYVAGHLPVKLPDYNSRLRVLVATYVTFSPNGTELLVNMGGEQVYLFDLTYKQRPYTFLLPRKCHSVEVQNGKMSTNGVSNGVSNGLHLHSNGFRLPESKGCISPQVELPPYLERVKQQANEAFACQQWTQAIQLYSQAVQKAPHNAMLYGNRAAAYMKRKWDGDHYDALRDCLKAISLNPCHLKAHFRLARCLFELKYVAEALECLDDFKGKFPEQAHSSACDALGRDITAALFSKSDGEEKKAAGGGGGPVRLRSTSRKDSISEDEMVLRERSYDYQFRYCGHCNTTTDIKEANFFGSNAQYIVSGSDDGSFFIWEKETTNLVRVLQGDESIVNCLQPHPSYCFLATSGIDPVVRLWNPRPESEDLTGRVVEDMEGASQANQRRMNANPLEAMLLDMGYRITGLSSGGAGASDDEDSAEGQVQCRPS
Protein: Thrombospondin type-1 domain-containing protein 4 (A disintegrin and metalloproteinase with thrombospondin motifs-like protein 6) (ADAMTS-like protein 6) (ADAMTSL-6) (ADAMTS-like protein 4) (ADAMTSL-4) (Q3UTY6)
Organism: Mus musculus (Mouse)
Function: Promotes FBN1 matrix assembly. Attenuates TGFB signaling, possibly by accelerating the sequestration of large latent complexes of TGFB or active TGFB by FBN1 microfibril assembly, thereby negatively regulating the expression of TGFB regulatory targets, such as POSTN.
Subcellular location: [Isoform 1]: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743, ECO:0000269|PubMed:19940141}. Note=Mostly deposited into pericellular fibrillar matrices (PubMed:19940141). Colocalizes with FBN1 (PubMed:19940141). {ECO:0000269|PubMed:19940141}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:19940141}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18757743, ECO:0000269|PubMed:19940141}. Note=Mostly secreted in the extracellular milieu (PubMed:19940141). In the pericellular fibrillar matrix, colocalizes with FBN1 (PubMed:19940141, PubMed:21880733). {ECO:0000269|PubMed:19940141, ECO:0000269|PubMed:21880733}.
Interaction partners:
- Fibrillin-1
Sequence:
MVSYLTSCLSALSTLLLLLGSQLVCPQPSTEHRKVPQRMAVTEGTPEDSGSGSPGVWGSWGPWSACSRSCSGGVMEQTRPCLPSSYRARGGSRPNGRALSITGHVVSAVRTSVPLHRSQEDQRALAGSNASRQGPAVVRGSRHPQARGREPSERRSRTRGPIGPGKYGYGKAPYILPLQTDTTHTPQRLRRQRPSSRHSRSQEASASKQGYRPPTHQFSHSQPLYQSDSGPRSGLPPSEASIYQLPLTHDQSYPAASSLFHRPELSSHHGARPHGAAQAFPQHLRSTAISCIGAYRQYKLCNTNACPESGRSIREVQCASYNNKPFMGRFYEWEPFAEVKGNRKCELNCQATGYRFYVRQAEKVIDGTPCDQNGTAICVSGQCKSIGCDDFLGSDKVLDKCGVCGGDNTGCQVVSGVFKHALTSLGYHRVVEIPQGATKINITEMHKSNNYLALRSRSGRSIINGNWAIDRPGKYEGGGTMFTYKRPNEVSSTAGESFLAEGPTNEILDVYMIHQQPNPGVHYEYVIMRNNAISPQVPPHRRPGEPFNGQLEEEDRGQEDREEREKNQEKEDSQVEAPEVFTSESTQTFPVRHPERFPSHRPDNLVPPAPQPPRRSRDHNWKQLGTTECSTTCGKGSQYPIFRCVHRNTHEEVPESYCDSSMKPTPEEEPCNLFPCPAFWDIGEWSECSKTCGLGMQHRQVLCRQVYANRSLTVQPYRCQHLEKPETTSTCQLKICSEWQIRTDWTSCSVPCGVGQRTRDVKCVSNIGDMVHDEECNMKLRPNDIENCDMGPCAKSWFLTEWSERCSAECGAGVRTRSVVCMTNHVSSLPLEGCGNNRPVEATPCDNGPCTGKVEWFTGSWSQCSIECGSGTQQREVICVRKNADTFEVLDPYECSFLEKPPSQQACHLKPCGAKWFSTEWSMCSKSCQGGFRVREVRCLSDDMTPSSLCDPQLKPEERESCNTQDCVPEVDENCKDKYYNCNVVVQARLCVYNYYKTACCASCTRVANRHVGFLGSR
Protein: Lipoate--protein ligase 1 (EC 6.3.1.20) (LplA1) (A0A0H3JR16)
Organism: Staphylococcus aureus (strain Mu50 / ATCC 700699)
Function: Catalyzes the lipoylation of proteins, such as GcvH (SAV0833) and GcvH-L (SAV0324), likely via the ATP-dependent activation of lipoate to lipoyl-AMP and the transfer of the activated lipoyl onto the lipoyl domain of the target protein.
Interaction partners:
Sequence:
MKFISNNNITDPTLNLAMEEYVLKNLPAEESYFLFYINRPSIIVGKNQNTIEEVNQTYIDAHNIDVVRRISGGGAVYHDTGNLNFSFITDDDGNSFHNFQKFTEPIVQALQSLGVNAELTGRNDIQVGQAKISGNAMVKVKNRMFSHGTLMLNSDLDEVQNALKVNPAKIKSKGIKSVRKRVANIQEFLNDPLEIEEFKKIILKTIFGETEVEEYKLTDEDWENIEKLSNDKYRTWAWNYGRNPKYNFEREEKFEKGFVQIKFDVKRGKIEHAKIFGDFFGVGDVTDLENALVGCLHDFEHIEEALSEYDLYHYFGDIDRHELIRLMS
Protein: Polyphosphatase (PolyPase) (EC 3.6.1.11) (Exopolyphosphatase) (Metaphosphatase) (P38698)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Polyphosphatase (polyPase) involved in the degradation of inorganic polyphosphates (polyP) that is able to degrade a range of chains from three to several hundreds of residues in a highly processive manner. Exclusively shows exopolyphosphatase activity, cleaving inside the polyP chain.
Interaction partners:
- Endopolyphosphatase
- Zinc-dependent endopolyphosphatase
- Diphosphoinositol polyphosphate phosphohydrolase DDP1
- Vacuolar transporter chaperone complex subunit 4
Sequence:
MSPLRKTVPEFLAHLKSLPISKIASNDVLTICVGNESADMDSIASAITYSYCQYIYNEGTYSEEKKKGSFIVPIIDIPREDLSLRRDVMYVLEKLKIKEEELFFIEDLKSLKQNVSQGTELNSYLVDNNDTPKNLKNYIDNVVGIIDHHFDLQKHLDAEPRIVKVSGSCSSLVFNYWYEKLQGDREVVMNIAPLLMGAILIDTSNMRRKVEESDKLAIERCQAVLSGAVNEVSAQGLEDSSEFYKEIKSRKNDIKGFSVSDILKKDYKQFNFQGKGHKGLEIGLSSIVKRMSWLFNEHGGEADFVNQCRRFQAERGLDVLVLLTSWRKAGDSHRELVILGDSNVVRELIERVSDKLQLQLFGGNLDGGVAMFKQLNVEATRKQVVPYLEEAYSNLEE
Protein: Multifunctional fusion protein [Includes: Delta-1-pyrroline-5-carboxylate dehydrogenase (P5C dehydrogenase) (L-glutamate gamma-semialdehyde dehydrogenase); L-glutamate gamma-semialdehyde dehydrogenase (EC 1.2.1.88)] (Q38BS5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proline dehydrogenase
- Pyrroline-5-carboxylate reductase
- Aspartate aminotransferase
- NAD-specific glutamate dehydrogenase
- aspartate transaminase
- glutamine synthetase
- Aminomethyltransferase
- Glycine cleavage system H protein
- Glycine cleavage system P protein
- Dihydrolipoamide dehydrogenase, putative
Sequence:
MLRRTLPFAFAFVKSPPAVNERMDSFQPGSDSARGTLEACKRLRCGATDCPIVIGGKEYRTDNAINRMIPSSHQQQVAKGYNATPELAQKAIDTALGAAKEWSQMPFKDRAAIFLHAAHLISTKYRHELRAATMLGQSKNPFQAEIDVIAESCDFLRFSVKYAEELYNQQPISPASGPVWNALDYRPLEGFVSVIAPFNFSAIAANLVACPALMGNVILWKPSPNAVLSNYLLYKVFEEAGLPAGVVNFMPCEPKVMTEVVNSHPELAGVAFTGSTNVFLSINKQIYSRLEEYRNIPRISGETGGKDFHLIHPTADMKMTAALTVRGAFEYQGQKCSATSRIYVPQSRWEELKGYLLELHGKLKMGQPDDFQSFMCAVIDETAFDRNKKYIDIAKADSSAYTIIAGGGCDKSEGWFIQPTIIVAKDPNAQLLREEIFGPILTVHVYDDSKPDFWSEACNLVNNATKYALTGSIFAQDRKAIRDATEKHLRYAAGNYYINDKCTGAVVGQQPFGGARASGSNDKPGSALFLTRWVSARTIKENFDHSAQVSYPHQLPDYVTL
Protein: Major capsid protein (Gene product 5) (gp5) (Major head protein) [Cleaved into: Scaffolding domain delta] (P49861)
Organism: Enterobacteria phage HK97 (Bacteriophage HK97)
Function: Assembles to form an icosahedral capsid of 66 nm, with a T=7 laevo symmetry. Responsible for its self-assembly into a procapsid. The phage does not need to encode a separate scaffolfing protein because its capsid protein contains the delta domain that carries that function.
Subcellular location: [Major capsid protein]: Virion. Note=Forms the icosahedral capsid shell which contains 420 major capsid proteins. {ECO:0000269|PubMed:11000116}.
Interaction partners:
Sequence:
MSELALIQKAIEESQQKMTQLFDAQKAEIESTGQVSKQLQSDLMKVQEELTKSGTRLFDLEQKLASGAENPGEKKSFSERAAEELIKSWDGKQGTFGAKTFNKSLGSDADSAGSLIQPMQIPGIIMPGLRRLTIRDLLAQGRTSSNALEYVREEVFTNNADVVAEKALKPESDITFSKQTANVKTIAHWVQASRQVMDDAPMLQSYINNRLMYGLALKEEGQLLNGDGTGDNLEGLNKVATAYDTSLNATGDTRADIIAHAIYQVTESEFSASGIVLNPRDWHNIALLKDNEGRYIFGGPQAFTSNIMWGLPVVPTKAQAAGTFTVGGFDMASQVWDRMDATVEVSREDRDNFVKNMLTILCEERLALAHYRPTAIIKGTFSSGS
Protein: Sodium/calcium exchanger 1 (Na(+)/Ca(2+)-exchange protein 1) (Solute carrier family 8 member 1) (Q01728)
Organism: Rattus norvegicus (Rat)
Function: Mediates the exchange of one Ca(2+) ion against three to four Na(+) ions across the cell membrane, and thereby contributes to the regulation of cytoplasmic Ca(2+) levels and Ca(2+)-dependent cellular processes. Contributes to Ca(2+) transport during excitation-contraction coupling in muscle. In a first phase, voltage-gated channels mediate the rapid increase of cytoplasmic Ca(2+) levels due to release of Ca(2+) stores from the endoplasmic reticulum. SLC8A1 mediates the export of Ca(2+) from the cell during the next phase, so that cytoplasmic Ca(2+) levels rapidly return to baseline. Required for normal embryonic heart development and the onset of heart contractions (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:10894800, ECO:0000269|PubMed:12502557, ECO:0000269|PubMed:16914199, ECO:0000269|PubMed:8422940}; Multi-pass membrane protein {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:16914199}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit beta
- Sodium/calcium exchanger 2
- cAMP-dependent protein kinase catalytic subunit alpha
- cGMP-dependent protein kinase 2
- Sodium/calcium exchanger 3
- Ryanodine receptor 2
- Sarcoplasmic/endoplasmic reticulum calcium ATPase 2
- Plasma membrane calcium-transporting ATPase 1
- Voltage-dependent L-type calcium channel subunit alpha-1C
Sequence:
MLRLSLPPNVSMGFRLVTLVALLFTHVDHITADTEAETGGNETTECTGSYYCKKGVILPIWEPQDPSFGDKIARATVYFVAMVYMFLGVSIIADRFMSSIEVITSQEKEITIKKPNGETTKTTVRIWNETVSNLTLMALGSSAPEILLSVIEVCGHNFTAGDLGPSTIVGSAAFNMFIIIALCVYVVPDGETRKIKHLRVFFVTAAWSIFAYTWLYIILSVSSPGVVEVWEGLLTFFFFPICVVFAWVADRRLLFYKYVYKRYRAGKQRGMIIEHEGDRPASKTEIEMDGKVVNSHVDNFLDGALVLEVDERDQDDEEARREMARILKELKQKHPDKEIEQLIELANYQVLSQQQKSRAFYRIQATRLMTGAGNILKRHAADQARKAVSMHEVNMDVVENDPVSKVFFEQGTYQCLENCGTVALTIIRRGGDLTNTVFVDFRTEDGTANAGSDYEFTEGTVIFKPGETQKEIRVGIIDDDIFEEDENFLVHLSNVRVSSEVSEDGILDSNHVSAIACLGSPNTATITIFDDDHAGIFTFEEPVTHVSESIGIMEVKVLRTSGARGNVIIPYKTIEGTARGGGEDFEDTCGELEFQNDEIVKTISVKVIDDEEYEKNKTFFIEIGEPRLVEMSEKKALLLNELGGFTLTEGKKMYGQPVFRKVHARDHPIPSTVISISEEYDDKQPLTSKEEEERRIAEMGRPILGEHTKLEVIIEESYEFKSTVDKLIKKTNLALVVGTNSWREQFIEAITVSAGEDDDDDECGEEKLPSCFDYVMHFLTVFWKVLFAFVPPTEYWNGWACFIVSILMIGLLTAFIGDLASHFGCTIGLKDSVTAVVFVALGTSVPDTFASKVAATQDQYADASIGNVTGSNAVNVFLGIGVAWSIAAIYHAANGEQFKVSPGTLAFSVTLFTIFAFINVGVLLYRRRPEIGGELGGPRTAKLLTSSLFVLLWLLYIFFSSLEAYCHIKGF
Protein: Zinc finger protein 432 (M0R0E2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MINAQELLTLEDVTVEFTWEEWQLLGPFQKDLYRDVMLEIYSNLLSMGYQVSKPDALSKLERGEEPWTMEDERHSRICPENNEVDDHLQDHLENQRMLKSVEQYHEHNAFGNTASQTKSLCLFRENHDTFELYIKTLKSNLSLVNQNKSCEINNSTKFSGDGKSFLHGNYEELYSAAKF
Protein: N5-carboxyaminoimidazole ribonucleotide mutase (N5-CAIR mutase) (EC 5.4.99.18) (5-(carboxyamino)imidazole ribonucleotide mutase) (P0AG18)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR).
Interaction partners:
- N5-carboxyaminoimidazole ribonucleotide synthase
- Phosphoribosylaminoimidazole-succinocarboxamide synthase
- Phosphoribosylformylglycinamidine synthase
- Phosphoribosylformylglycinamidine cyclo-ligase
- Phosphoribosylamine--glycine ligase
- Amidophosphoribosyltransferase
- Phosphoribosylglycinamide formyltransferase
- Bifunctional purine biosynthesis protein PurH
- Formate-dependent phosphoribosylglycinamide formyltransferase
- Adenylosuccinate lyase
Sequence:
MSSRNNPARVAIVMGSKSDWATMQFAAEIFEILNVPHHVEVVSAHRTPDKLFSFAESAEENGYQVIIAGAGGAAHLPGMIAAKTLVPVLGVPVQSAALSGVDSLYSIVQMPRGIPVGTLAIGKAGAANAALLAAQILATHDKELHQRLNDWRKAQTDEVLENPDPRGAA
Protein: Beta-1,3-galactosyltransferase 1 (Beta-1,3-GalTase 1) (Beta3Gal-T1) (Beta3GalT1) (EC 2.4.1.86) (UDP-galactose:beta-N-acetyl-glucosamine-beta-1,3-galactosyltransferase 1) (Q9Y5Z6)
Organism: Homo sapiens (Human)
Function: Beta-1,3-galactosyltransferase that transfers galactose from UDP-alpha-D-galactose to substrates with a terminal beta-N-acetylglucosamine (beta-GlcNAc) residue. Involved in the biosynthesis of the carbohydrate moieties of glycolipids and glycoproteins. Inactive towards substrates with terminal alpha-N-acetylglucosamine (alpha-GlcNAc) or alpha-N-acetylgalactosamine (alpha-GalNAc) residues.
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Beta-1,4-galactosyltransferase 1
- Beta-1,4-galactosyltransferase 2
- Beta-1,4-galactosyltransferase 4
- Galactoside alpha-
- Galactoside alpha-
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 4
- 3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase FUT3
- Beta-1,4-galactosyltransferase 3
- Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase
- Beta-1,3-galactosyltransferase 5
Sequence:
MASKVSCLYVLTVVCWASALWYLSITRPTSSYTGSKPFSHLTVARKNFTFGNIRTRPINPHSFEFLINEPNKCEKNIPFLVILISTTHKEFDARQAIRETWGDENNFKGIKIATLFLLGKNADPVLNQMVEQESQIFHDIIVEDFIDSYHNLTLKTLMGMRWVATFCSKAKYVMKTDSDIFVNMDNLIYKLLKPSTKPRRRYFTGYVINGGPIRDVRSKWYMPRDLYPDSNYPPFCSGTGYIFSADVAELIYKTSLHTRLLHLEDVYVGLCLRKLGIHPFQNSGFNHWKMAYSLCRYRRVITVHQISPEEMHRIWNDMSSKKHLRC
Protein: ATP-citrate synthase alpha chain protein 2 (ATP-citrate synthase A-2) (EC 2.3.3.8) (ATP-citrate lyase A-2) (Citrate cleavage enzyme A-2) (O22718)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: ATP citrate-lyase is the primary enzyme responsible for the synthesis of cytosolic acetyl-CoA, used for the elongation of fatty acids and biosynthesis of isoprenoids, flavonoids and malonated derivatives. May supply substrate to the cytosolic acetyl-CoA carboxylase, which generates the malonyl-CoA used for the synthesis of a multitude of compounds, including very long chain fatty acids and flavonoids. Required for normal growth and development and elongation of C18 fatty acids to C20 to C24 fatty acids in seeds. In contrast to all known animal ACL enzymes having a homomeric structure, plant ACLs are composed of alpha and beta chains (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}.
Interaction partners:
- ATP-citrate synthase beta chain protein 2
- ATP-citrate synthase beta chain protein 1
- Citrate synthase 2, peroxisomal
- Citrate synthase 3, peroxisomal
- Succinate--CoA ligase subunit alpha-2, mitochondrial
- Citrate synthase 4, mitochondrial
- Citrate synthase 5, mitochondrial
- Citrate synthase 1, peroxisomal
- Succinate--CoA ligase subunit alpha-1, mitochondrial
- Aconitate hydratase 2, mitochondrial
Sequence:
MARKKIREYDSKRLVKEHFKRLSGQELPIRSVQINQETDLNELVEREPWLSSEKLVVKPDMLFGKRGKSGLVALNLDFADVATFVKERLGKEVEMSGCKGPITTFIVEPFVPHNEEFYLNIVSDRLGCSISFSECGGIDIEENWDKVKTITIPTGASLTFEICAPLVATLPLEIKGELEDFIQVIFTLFEDLDFTFLEMNPFTLVDGKPYPLDMRGELDDTAAFKNFKKWGDIEFPMPFGRVMSSTESFIHGLDEKTSASLKFTVLNPKGRIWTMVAGGGASVIYADTVGDLGYASELGNYAEYSGAPKEDEVLQYARVVIDCATANPDGKSRALVIGGGIANFTDVAATFNGIIRALKEKEAKLKAARMHIFVRRGGPNYQKGLAKMRSLGDEIGVPIEVYGPEATMTGICKEAIQYITAAA
Protein: Ecotropic viral integration site 5 ortholog (Q9VYY9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Functions as a GTPase-activating protein (GAP). During border cell migration in the ovary, acts as a GAP for Rab11 and is necessary for the maintenance of active receptor tyrosine kinases at the leading edge.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22778279}. Endosome {ECO:0000269|PubMed:22778279}.
Interaction partners:
- Rab11
Sequence:
MTLTTTTTASSAESQAKMDVKGGALPGEENLPTSEMDLLAKLEAANKLIESDAKSLNSLHSTHSRKNSDTSQISLTSSGNSVAEEDIWTTWATILNDWEGALKRKNPCVSELVRRGIPHHFRAIVWQQLSGASDGDKKQYAEYIKATSACEKVIRRDIARTYPEVEFFKEKDGPGQEALFNVIKAYSLHDREVGYCQGSGFIVGLLLMQMPEEEAFAVLVQIMQQHRMRHMFKPSMSELGLCMYQLENLVQEQIPDMHIHFQQQGFQTTMYASSWFLTLYTTTLNVNLSCRIMDVFLSEGMEFIFKVALALLLTGKDTLLCLDMEAMLKFFQKELPGRVEADVEGFFNLAYSIKLNTKRMKKMEKEYQDLKKKEQEEMAELRRLRRENCLLKQRNELLEAESAELADRLVRGQVSRAEEEETSYAIQTELMQLRRSYLEVSHQLENANEEVRGLSLRLQENNVSIDSNNSRQSSIDELCMKEEALKQRDEMVSCLLEELVKVRQGLAESEDQIRNLKAKVEELEEDKKTLRETTPDNSVAHLQDELIASKLREAEASLSLKDLKQRVQELSSQWQRQLAENQRSESERTTNAVDSTPKKLLTNFFDSSKSSEHTQKLEEELMTTRIREMETLTELKELRLKVMELETQVQVSTNQLRRQDEEHKKLKEELEMAVTREKDMSNKAREQQHRYSDLESRMKDELMNVKIKFTEQSQTVAELKQEISRLETKNSEMLAEGELRANLDDSDKVRDLQDRLADMKAELTALKSRGKFPGAKLRSSSIQSIESTEIDFNDLNMVRRGSTELST
Protein: DNA (cytosine-5-)-methyltransferase (EC 2.1.1.37) (A0A2R9YJL5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATNVSLEPNNPDDKCSRYEVLGWINETLQTNFTQVEQCRSGACFCQLIDLLFPGTINLKKVKFESQKRSDFMQNYGLLQAAFRDLEVTEPVPVNELLSGKFRPNFTYLKWFKKFFYANVKQERVYNAFEARDGQEIVPVDDVMKSPKALKSSYESGRAGEESDMEINGGRRSATYDPKWQRNLKWIRASDMGDNYAYCTTCDYNIILLAGFHDLKRHQLTQNHMKHETGRTNLPGRKQIEESISCSETMLLFIQSHCLSSLPSRINRVSQRTARCILGLKYPNDIVSACKLNPYCIYIYGQVPLDVKTGDKTNCHVVLAGFFEEKQARYCIRFLDVFQPEDSASSVSGGLFSILKKFEIPASNMVAVYINDHELTSESVVSQIRELNPQVIDLGGLYSIPDTACSAGLQTHSVQVQELIANIYRHFSTGSTSNDNLKMLFAGIDGLKVHSNPLSNSEEFCVLVKRIHEMWSDLVSYFSSCDENNDNVKQICSQLENPKIRLTLMFLDQALGPLRAFGQHLQQSKSSVRADLVEILREASGLLRSYASSFLRPQAVIRYLKEQDPAILDNEAFCLPAAELSLGGVLEDFISAREEELADFLSTFYNECLAIYKTLTTSIAASLPLSDSVLRAISQLLSPAGRLKVTGKNIVDLAVRFGFCSKPEDSAKLNDEFLEYQLAEEENLSSTHSIERYWCTVLKTFPPTSVFKRLVLCLLVLPSPSLDATKIFAQAIENGDADQLDDSSSESDTDMTKELDSNDDNSLDNSELQISPIKNGIMKKSRRSTSETVQHSNAVKPCVVRLEKITSQREVNLKNDGAKNDGTLTSNTLKEVKNDLSNSTPSPRRGKRDQAYNDGKGFAVGELVWGKVKDFSLWPGLVVPWKGRIVPVSMRRVEWFGDGMFSEIHTDGLLPFGAFSKNFCSKSYEGLPTYKNAIYQILELAAERSGKLFPPSEKKGEEVKAMMDWAFGGFQPMGADGFLPSADSSASNKTESDSSVSDYQPPAKRKYVFKNRPSTQECNRDQMVQEVTSKGRKIEDFCLSCGSSNTEIFHPLFKGSLCIKCKENFTETLYRYDDDGYQSYCTVCCAGLEVILCGNASCCRCFCKDCLNVLVGPGTFDKLKEVDPWSCYVCLPSKCYGVLKLRTDWSVRVQEFFANNSAFEFEPHRVYPSIPAHKRRPIRVLSLFDGIATGYLVLKDLGFKLERYIASEICEDSIAVGMVKHEGKIEYVKDVRTITRKHLAEWGPFDLLIGGSPCNDLSMVNPARKGLFEGTGRLFFEYYRMLTMMRPKEDDDRPFFWLFENVVAMSAHDKADICRFLECNPVMIDAVKVSPAHRARYFWGNLPGMNRPVATSLTDNVDLQDCLESGRTAMFSKVRTITTKSNSIKQGKTGPLPVTMNGKEDYLWCTEMEKIFGFPKHYTDVNNMGRGQRQKVLGRSWSVPVIRHLFAPLKDYFACE
Protein: DUF3631 domain-containing protein (P71952)
Organism: Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Interaction partners:
Sequence:
MADIPYGRDYPDPIWCDEDGQPMPPVGAELLDDIRAFLRRFVVYPSDHELIAHTLWIAHCWFMEAWDSTPRIAFLSPEPGSGKSRALEVTEPLVPRPVHAINCTPAYLFRRVADPVGRPTVLYDECDTLFGPKAKEHEEIRGVINAGHRKGAVAGRCVIRGKIVETEELPAYCAVALAGLDDLPDTIMSRSIVVRMRRRAPTEPVEPWRPRVNGPEAEKLHDRLANWAAAINPLESGWPAMPDGVTDRRADVWESLVAVADTAGGHWPKTARATAETDATANRGAKPSIGVLLLRDIRRVFSDRDRMRTSDILTGLNRMEEGPWGSIRRGDPLDARGLATRLGRYGIGPKFQHSGGEPPYKGYSRTQFEDAWSRYLSADDETPEERDLSVSAVSAVSPPVGDPGDATGATDATDLPEAGDLPYEPPAPNGHPNGDAPLCSGPGCPNKLLSTEAKAAGKCRPCRGRAAASARDGAR