wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine protein kinase (YPK1), putative (AFU_orthologue AFUA_2G10620) (Q5B0F7)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- non-specific serine/threonine protein kinase
- non-specific serine/threonine protein kinase
- Stress activated MAP kinase interacting protein, putative
Sequence:
MSWKLTKKLKETHLAPLTQTFTRSSSTSTIKGDSGEEAQAPAQTPTISSSASSNGIAASEALVSPPVAPVKPGILIVTLHEGRSFALPQHYQQVFSSHIQNGYSMRPSSSSSHSTHSQSSSFVPSNRPQSTSSGINAAPTIHGRYSTKYLPYALLDFDKNQVFVDAVSGTPENPLWAGDNTAFKFDVSRKTDLNVQLYLRNPAARPGAGRNDDIFLGAVKVHPRFEEEIQPYIDDPKLSKKDNQKAAAAHAEQERALGQVGAEWHDLQFGSGSLKISVSFVESKHRSLKLEDFDLLKVVGKGSFGKVMQVMKKDTGRIYALKTIRKAHIISRSEVTHTLAERSVLAQINNPFIVPLKFSFQSPEKLYFVLAFVNGGELFHHLQREQRFDVNRARFYTAELLCALECLHGFKVIYRDLKPENILLDYTGHIALCDFGLCKLDMKDEDRTNTFCGTPEYLAPELLLGQGYTKTVDWWTLGVLLYEMLTGLPPFYDENTNDMYRKILQEPLTFPSSDIVPPAARDLLTRLLDRDPNRRLGANGAAEIKSHHFFANIDWRKLLQRKYEPSFRPNVADARDTKNFDAEFTSEAPKDSYVDGPMLSSTQQQQFEGWSYNRPVAGLGDAGGSVKDPSFASIPEDSRF
Protein: Glutathione-specific gamma-glutamylcyclotransferase (Gamma-GCG) (EC 4.3.2.7) (P32656)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the cleavage of glutathione into 5-oxo-L-proline and a Cys-Gly dipeptide. Acts specifically on glutathione, but not on other gamma-glutamyl peptides. Allows utilization of gluthathione through subsequent cleavage of the Cys-Gly dipeptide by Cys-Gly metallodipeptidase DUG1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Glutathione hydrolase proenzyme
- 5-oxoprolinase
- Glutathione synthetase GSH2
- Cys-Gly metallodipeptidase DUG1
- Peroxiredoxin PRX1, mitochondrial
- Glutathione S-transferase 1
- Transcriptional regulator URE2
- Glutathione reductase
- J protein JJJ1
- 4-hydroxy-4-methyl-2-oxoglutarate aldolase
Sequence:
MTNDNSGIWVLGYGSLIYKPPSHYTHRIPAIIHGFARRFWQSSTDHRGTPANPGRVATLIPYEDIIRQTAFLKNVNLYSESAPIQDPDDLVTIGVVYYIPPEHAQEVREYLNVREQNGYTLHEVEVHLETNREHEAELGEALEQLPRHNKSGKRVLLTSVYIGTIDNEAFVGPETVDETAKVIAVSHGPSGSNYEYLAKLEQALAQMPIMKERGRITDHYLTALLETVNKYR
Protein: Uncharacterized protein (R9PY35)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- LD26135p
Sequence:
MENKCRVCLASSKNMVNIFEERQDLPVSIAHMIIECTGFKVEKGDSLPHSICPPCVKDAHNAFTIIKTYERSYQVFYEVQDTVLEEELSEDVIIELSDSDEVILIDEQEEKVHLSENKAPTNEVSTQEESKTAQSDNVSEDKGHICTQCHMSFRRPGLLELHILRHHTTDGPRPMSSTSEHAVKEELRTKARQLSRNSTHTCRLCNKTFCSKASCVRHQKTHTGEKPFACEICQKPFADLASVKRHLRTHTGERPFKCLTCQSAFSDGSALRQHIRIHTGERPYKCDMCDKFFRERSDARKHMMSHTAEKRFKCSQCERRFRQPKGLRRHVKLCHTDKVENAAIS
Protein: Nucleoplasmin-2 (Q86SE8)
Organism: Homo sapiens (Human)
Function: Core histones chaperone involved in chromatin reprogramming, specially during fertilization and early embryonic development. Probably involved in sperm DNA decondensation during fertilization.
Subcellular location: Nucleus {ECO:0000250}. Note=Found in the oocyte nucleus before nuclear membrane breakdown, after which it is redistributed to the cytoplasm. {ECO:0000250}.
Interaction partners:
- Nucleoplasmin-3
- Nucleophosmin
- Nucleolin
Sequence:
MNLSSASSTEEKAVTTVLWGCELSQERRTWTFRPQLEGKQSCRLLLHTICLGEKAKEEMHRVEILPPANQEDKKMQPVTIASLQASVLPMVSMVGVQLSPPVTFQLRAGSGPVFLSGQERYEASDLTWEEEEEEEGEEEEEEEEDDEDEDADISLEEQSPVKQVKRLVPQKQASVAKKKKLEKEEEEIRASVRDKSPVKKAKATARAKKPGFKK
Protein: Calpain-like cysteine peptidase, putative (Q381R3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPRKALLGNWFEEEAYMRDRKRLLDSCDRGVVDAARETQRIIAKVKHHNSAYPMAEPHEDGYLHFYAPLMLQNAATLGFLSLDLEDRTLRPTGWHVACSTAPAAGPALRNCFVLVPAPTGPTDMIPAPPDEQDIVHYGQPFFIMTVPELCDNPLSLLSEPKGPLSASKVTGKHQDVFFSPDGASAEAMWVADFANPDHREDMRDLPIKADAVLVIRHNHTNTPLASSKAVFFNDFGPENEVCCGRFVNNPGTPCGPMKDENYWTFVHSENGEGDVEKGGETTTPVAENEVSVMTSTNGDKL
Protein: stearoyl-CoA 9-desaturase (EC 1.14.19.1) (C0JXB7)
Organism: Ovis aries (Sheep)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
Sequence:
MPAHLLQEEISSSYTTTTTITAPPSRVLQNGGGKLEKTPLYLEEDIRPEMRDDIYDPTYQDKEGPKPKLEYVWRNIILMGLLHLGALYGITLIPTCKIYTFLWVLFYYVISALGITAGVHRLWSHRTYKARLPLRVFLIIANTMAFQNDVFEWSRDHRAHHKFSETDADPHNSRRGFFFSHVGWLLVRKHPAVREKGATLDLSDLRAEKLVMFQRRYYKPGVLLLCFILPTLVPWYLWGETFQNSLFFATFLRYAVVLNATWLVNSAAHMYGYRPYDKTINPRENILVSLGAVGEGFHNYHHTFPYDYSASEYRWHINFTTFFIDCMAAIGLAYDRKKVSKAAVLARMKRTGEESYKSG
Protein: Inner membrane protein YnjI (P76228)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Uncharacterized protein YecT
- Inner membrane protein YnbA
- Uncharacterized HTH-type transcriptional regulator YidL
- Inner membrane protein YgiZ
- Sugar fermentation stimulation protein B
- Uncharacterized protein YqhG
- Protein RhsB
Sequence:
MKKVLLQNHPGSEKYSFNGWEIFNSNFERMIKENKAMLLCKWGFYLTCVVAVMFVFAAITSNGLNERGLITAGCSFLYLLIMMGLIVRAGFKAKKEQLHYYQAKGIEPLSIEKLQALQLIAPYRFYHKQWSETLEFWPRKPEPGKDTFQYHVLPFDSIDIISKRRESLEDQWGIEDSESYCALMEHFLSGDHGANTFKANMEEAPEQVIALLNKFAVFPSDYISDCANHSSGKSSAKLIWAAELSWMISISSTAFQNGTIEEELAWHYIMLASRKAHELFESEEDYQKNSQMGFLYWHICCYRRKLTDAELEACYRYDKQFWEHYSKKCRWPIRNVPWGASSVKYS
Protein: ABC-type glutathione-S-conjugate transporter (EC 7.6.2.3) (A0A0S0WIA2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Vacuole membrane {ECO:0000256|ARBA:ARBA00004128}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004128}.
Interaction partners:
Sequence:
MADDTSSPMDRFCGSTFWNATETWYTNDPDFTPCFEQTALVWTPCAFYWAFVIFDFYYLKASLDRNIPWNKLNVSKALVNLGLLVITALDLIMALVKKGGDSELPLYDLDVWGPIIKFATFLLLFIFIPLNRKYGVQTTGCQFIFWFLLTVLSIPRCRTEVRLDAERQKILNSQQPSEQDFSWEEYQFVSFFIFFTFTSIMLILNCFADGMPRQTKYQRGENEIPELSASFLSRITYQWFDKMALKGYRNPLEEKDLWDLRPQDSCSEVMPIFAHHWNQNVRKNYKNKARVEPKAQFSNGNVTFENPHGEKNGRKKGMASIMPPIYKSFGGVFLFGALMKLFTDTLTFAQPQVLSLIISFVEAQDAEPEWKGILYAVLLFVLAAAQTFILGQYFHRMFIVGLRIRTALINAIYRKALRISNSTKKESTVGEIVNLMAVDAQRFMELTTYLNMIWSAPLQIGLALYFLWQQLGPSVLAGLAVMIILIPVNGVIASRIKTYQIRQMKYKDERVKLMNEVLSGIKVLKLYAWEPSFEKQVLDIRDKEIATLRSTAYLNAGTSFLWSCAPFLVSLVTFATYVLIDENNVLDATKTFVSLSLFNILRFPLTMLPMLITNLVQTQVSVNRINKFLNSEELDPNSVLHDSSKPHPMSIENGEFSWGDEITLRNINIEVKKGSLVALVGTVGSGKSSVVQAFLGEMEKLAGVVNTVGKLAYVPQQAWIQNATVRDNILFGQTYDRKRYNKVIDACALRADIDILSAGDLTEIGEKGINLSGGQKQRISLARAVYSDADLYLLDDPLSAVDAHVGKHIFEEVIGPKGILARKSRVLVTHGVTFLPQVDSIYVIKMGEISESGTFDQLVKNKGAFADFIIQHLQEGNEEEEELNQIKRQISSTADVPELLGTVEKAIKLARTESLSDSISVTSADSLMGGGGSLRRRTKRQDSHDSVASAASLKKKQEVEGKLIETEKSQTGGVEFAVYKHYIKSVGIFLSVATLVLNFVFQAFQIGSNLWLTQWANDQNVANDTGLRDMYLGVYGAFGFGQVATNFFSSLAISLGCLKCSQLLHQTLLYYNLRWPMELFDTTPLGRIVNRFSKDIDTIDNVLPFNIRVVIGQAYMVLATIVVISLSTPIFLAVIVPIAFLYYFAQRFYVATSRQLMRLESVSRSPIYSHFSETVTGASTIRAYNVGDRFIEESDAKVDKNQVCKYPSVIANRWLAIRLEMVGNLIILFASLFAVLGGQTNPGLVGLSVSYALQVTQTLNWLVRMSSDIETNIVSVERIKEYGETKQEAPWELEQDKNKPKNWPQEGRVEFQNFQVRYREGLDLVLRGVSFNIQGGEKVGIVGRTGAGKSSLTLALFRIIEAAGGRISIDGVDIASMGLHMLRSRLTIIPQDPVLFSGSLRINLDPFEIKTDDEIWKALELSHLKSFVKSLAAGLNHEIAEGGENLSVGQRQLVCLARALLRKTKVLVLDEATAAVDLETDDLIQIRHFCHP
Protein: Large ribosomal subunit protein eL38 (60S ribosomal protein L38) (Q9JJI8)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein uS7
- Elongation factor 2
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein uS2
Sequence:
MPRKIEEIKDFLLTARRKDAKSVKIKKNKDNVKFKVRCSRYLYTLVITDKEKAEKLKQSLPPGLAVKDLK
Protein: Tissue factor (TF) (Coagulation factor III) (CD antigen CD142) (P42533)
Organism: Rattus norvegicus (Rat)
Function: Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited proteolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade.
Subcellular location: Membrane {ECO:0000250|UniProtKB:P13726}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P13726}.
Interaction partners:
- Coagulation factor VII
- Tissue factor pathway inhibitor
- Prothrombin
- Coagulation factor X
- Thrombomodulin
- Tissue factor pathway inhibitor
- Coagulation factor IX
- Vitamin K-dependent protein C
- Coagulation factor XI
- von Willebrand factor
Sequence:
MAIPMRPRLLAALAPTFLGFLLLQVAVGAGTPPGKAFNLTWISTDFKTILEWQPKPTNYTYTVQISDRSRNWKYKCTGTTDTECDLTDEIVKDVNWTYEARVLSVPWRNSTHGKETLFGTHGEEPPFTNARKFLPYRDTKIGQPVIQKYEQGGTKLKVTVKDSFTLVRKNGTFLTLRQVFGNDLGYILTYRKDSSTGRKTNTTHTNEFLIDVEKGVSYCFFAQAVIFSRKTNHKSPESITKCTEQWKSVLGETLIIVGAVVFLVTVFIILLTISLCKRRKNRAGQKRKNTPSRLA
Protein: Inner kinetochore subunit MIF2 (CENP-C homolog) (Constitutive centromere-associated network protein MIF2) (Mitotic fidelity of chromosome transmission protein 2) (P35201)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the kinetochore, a multiprotein complex that assembles on centromeric DNA and attaches chromosomes to spindle microtubules, mediating chromosome segregation and sister chromatid segregation during meiosis and mitosis. Component of the inner kinetochore constitutive centromere-associated network (CCAN), which serves as a structural platform for outer kinetochore assembly.
Subcellular location: Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore {ECO:0000305|PubMed:22561346}.
Interaction partners:
- Histone H3-like centromeric protein CSE4
- Histone H4
- Histone H2A.1
- Histone H2A.2
- Inner kinetochore subunit CHL4
- Inner kinetochore subunit MCM21
- Kinetochore-associated protein DSN1
- Inner kinetochore subunit AME1
- COMPASS component BRE2
- Histone H2B.1
Sequence:
MDYMKLGLKSRKTGIDVKQDIPKDEYSMENIDDFFKDDETSLISMRRKSRRKSSLFLPSTLNGDTKNVLPPFLQSYKSQDDEVVQSPSGKGDGSRRSSLLSHQSNFLSPANDFEPIEEEPEQEENDIRGNDFATPITQKLSKPTYKRKYSTRYSLDTSESPSVRLTPDRITNKNVYSDVPDLVADEDDDDRVNTSLNTSDNALLEDELEDDGFIPESEEDGDYIESDSSLDSGSDSASDSDGDNTYQEVEEEAEVNTNDNEDDYIRRQASDVVRTDSIIDRNGLRKSTRVKVAPLQYWRNEKIVYKRKSNKPVLDIDKIVTYDESEDEEEILAAQRRKKQKKKPTPTRPYNYVPTGRPRGRPKKDPNAKENLIPEDPNEDIIERIESGGIENGEWLKHGILEANVKISDTKEETKDEIIAFAPNLSQTEQVKDTKDENFALEIMFDKHKEYFASGILKLPAISGQKKLSNSFRTYITFHVIQGIVEVTVCKNKFLSVKGSTFQIPAFNEYAIANRGNDEAKMFFVQVTVSEDANDDNDKELDSTFDTFG
Protein: Serine/threonine-protein kinase PBL27 (EC 2.7.11.1) (PBS1-like protein 27) (Receptor-like cytoplasmic kinase PBL27) (Q1PDV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Receptor-like cytoplasmic kinase involved in the transduction of signal between the host cell surface chitin receptor complex CERK1-LYK5 and the intracellular MAPKKK5-dependent mitogen-activated protein kinase (MAPK) cascade that leads to chitin-induced immunity. Phosphorylates and activates MAPKKK5 when phosphorylated by CERK1 after elicitation by chitin.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24750441, ECO:0000269|PubMed:27679653}; Lipid-anchor {ECO:0000269|PubMed:24750441}.
Interaction partners:
- S-type anion channel SLAH3
- U-box domain-containing protein 4
- LysM domain-containing GPI-anchored protein 1
- Chitin elicitor receptor kinase 1
Sequence:
MSGCLPCFGSSAKDAASKDSVKKELSAKDGSVTQSHHISLDKSKSRRGPEQKKELTAPKEGPTAHIAAQTFTFRELAAATKNFRPECLLGEGGFGRVYKGRLETTGQIVAVKQLDRNGLQGNREFLVEVLMLSLLHHPNLVNLIGYCADGDQRLLVYEYMPLGSLEDHLHDLPPDKEPLDWSTRMTIAAGAAKGLEYLHDKANPPVIYRDLKSSNILLGDGYHPKLSDFGLAKLGPVGDKTHVSTRVMGTYGYCAPEYAMTGQLTLKSDVYSFGVVFLELITGRKAIDNARAPGEHNLVAWARPLFKDRRKFPKMADPSLQGRYPMRGLYQALAVAAMCLQEQAATRPLIGDVVTALTYLASQTFDPNAPSGQNSRSGSGPPFIRTRDDRRSLGDGSSLDSPAETRSRLGSPATHKNSPDYRRRDMVREVNAGSEGGSETGGGSGRKWGLSDLEGQESQRGSPASVGRSSRGTPRNRDLDRERAVAEAKVWGENWRERKRATNGPGSFDSTND
Protein: 5-hydroxytryptamine receptor 1A (5-HT-1A) (5-HT1A) (x5-HT1A) (Serotonin receptor 1A) (Q98998)
Organism: Xenopus laevis (African clawed frog)
Function: G-protein coupled receptor for 5-hydroxytryptamine (serotonin). Also functions as a receptor for various drugs and psychoactive substances. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Beta-arrestin family members inhibit signaling via G proteins and mediate activation of alternative signaling pathways. Signaling inhibits adenylate cyclase activity and activates a phosphatidylinositol-calcium second messenger system that regulates the release of Ca(2+) ions from intracellular stores. Plays a role in the regulation of 5-hydroxytryptamine release and in the regulation of dopamine and 5-hydroxytryptamine metabolism. Plays a role in the regulation of dopamine and 5-hydroxytryptamine levels in the brain, and thereby affects neural activity and behavior. Activation of the receptor may play a role in the exit from G0 phase and in promoting DNA synthesis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9878840}; Multi-pass membrane protein {ECO:0000255, ECO:0000269|PubMed:9878840}.
Interaction partners:
Sequence:
MDASNNTTSWNILQRGRMGPSWRRCPVSYQIIASLFLGRSFSAGIFGNACVIAAIALERSLQNVANYLIGSLAVTDLMVSVLVLPMAAQNQVLNKWTLGQVTCDIFISLDVLCCTSSILHLCAIALDRYWAITDPIDYVNKRTPRRAAVLISITWIVGFSISIPPMLGWRTPEDRSDPNACRISEDPGYTIYSTFGAFYIPLILMLVLYGKIFKAARFRIRKTVKKAEKKKVADTCLSVSQQSPKEKQRGAQQELEEVGGAQAQRCVNGAIRHGEEGAVLEIIEVHHYVNSKCHLHCKPVPPPEQLPPALKNDRATEAKRKVALARERKTVKTLGIIMGTFILCWLPFFIVALVLPFCETCHMPHLLFDIITWLGYSNSLLNPIIYAYFNKDFQSAFKKIIKCKFCRQ
Protein: KRR1 small subunit processome component (KRR-R motif-containing protein 1) (Ribosomal RNA assembly protein KRR1) (P25586)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for 40S ribosome biogenesis. Involved in nucleolar processing of pre-18S ribosomal RNA and ribosome assembly. Essential for vegetative growth.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:11027267, ECO:0000269|PubMed:11996121, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15094838, ECO:0000269|PubMed:15590835}.
Interaction partners:
- Small ribosomal subunit protein uS7
- Probable ATP-dependent RNA helicase DHR1
- U3 small nucleolar RNA-associated protein 22
- Probable ATP-dependent RNA helicase DHR2
- Nucleolar complex protein 4
- U3 small nucleolar RNA-associated protein 21
- Protein BFR2
- U3 small nucleolar ribonucleoprotein protein IMP3
- U3 small nucleolar ribonucleoprotein protein LCP5
- rRNA biogenesis protein RRP5
Sequence:
MVSTHNRDKPWDTDDIDKWKIEEFKEEDNASGQPFAEESSFMTLFPKYRESYLKTIWNDVTRALDKHNIACVLDLVEGSMTVKTTRKTYDPAIILKARDLIKLLARSVPFPQAVKILQDDMACDVIKIGNFVTNKERFVKRRQRLVGPNGNTLKALELLTKCYILVQGNTVSAMGPFKGLKEVRRVVEDCMKNIHPIYHIKELMIKRELAKRPELANEDWSRFLPMFKKRNVARKKPKKIRNVEKKVYTPFPPAQLPRKVDLEIESGEYFLSKREKQMKKLNEQKEKQMEREIERQEERAKDFIAPEEEAYKPNQN
Protein: Endoplasmic reticulum resident protein 44 (ER protein 44) (ERp44) (Thioredoxin domain-containing protein 4) (Q9BS26)
Organism: Homo sapiens (Human)
Function: Mediates thiol-dependent retention in the early secretory pathway, forming mixed disulfides with substrate proteins through its conserved CRFS motif. Inhibits the calcium channel activity of ITPR1. May have a role in the control of oxidative protein folding in the endoplasmic reticulum. Required to retain ERO1A and ERO1B in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000269|PubMed:11847130, ECO:0000269|PubMed:15652484}.
Interaction partners:
- ERO1-like protein alpha
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Peroxiredoxin-4
- ERO1-like protein beta
- Protein ERGIC-53
- Thioredoxin
- Formylglycine-generating enzyme
- Zinc finger protein 385A
- Immunoglobulin J chain
- DnaJ homolog subfamily B member 11
Sequence:
MHPAVFLSLPDLRCSLLLLVTWVFTPVTTEITSLDTENIDEILNNADVALVNFYADWCRFSQMLHPIFEEASDVIKEEFPNENQVVFARVDCDQHSDIAQRYRISKYPTLKLFRNGMMMKREYRGQRSVKALADYIRQQKSDPIQEIRDLAEITTLDRSKRNIIGYFEQKDSDNYRVFERVANILHDDCAFLSAFGDVSKPERYSGDNIIYKPPGHSAPDMVYLGAMTNFDVTYNWIQDKCVPLVREITFENGEELTEEGLPFLILFHMKEDTESLEIFQNEVARQLISEKGTINFLHADCDKFRHPLLHIQKTPADCPVIAIDSFRHMYVFGDFKDVLIPGKLKQFVFDLHSGKLHREFHHGPDPTDTAPGEQAQDVASSPPESSFQKLAPSEYRYTLLRDRDEL
Protein: Alpha-amylase (EC 3.2.1.1) (A0A8I5ZY75)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MYFFLMKFFLLLSLIGLCWAQYDPHTFYGRSSIVHLFEWRWVDIAKECERYLAPNGFGGVQVSPPNENIVVNSPFRPWWERYQPISYKICSRSGNEDEFRDMVNRCNNVGVRIYVDAVINHMCGVGAEAGQSSTCGSYFNPNNRDFPGVPYSGFDFNDGKCKTGSGGIENYNDAAQVRDCRLSGLLDLALEKDYVRTKVADYMNHLIDIGVAGFRLDASKHMWPGDIKAVLDKLHNLNTKWFSEGSKPFIYQEVIDLGGEAVSSNEYFGNGRVTEFKYGAKLGKVLRKWDGEKMAYLKNWGEGWGFMPSDRALVFVDNHDNQRGHGAGGSSILTFWDARLYKMAVGFMLAHPYGFTRVMSSFHWPRYFENGKDVNDWVGPPNNNGATKEVTINSDSTCGNDWVCEHRWRQIRNMVAFRNVVNGQPFANWWDNGSNQVAFGRGNKGFIVFNNDDWDLSTTLQTGLPAGTYCDVISGDKVDGNCTGIKVYVGSDGNAYFSISNSAEDPFIAIHVESKI
Protein: 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic (EC 2.3.1.41) (Beta-ketoacyl-acyl-carrier-protein synthase II) (AtKAS2) (Beta-ketoacyl-ACP synthetase 2) (Protein FATTY ACID BIOSYNTHESIS 1) (Q9C9P4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein that catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Specific for elongation from C-16 and C-16 to unsaturated C-18 fatty acids. Confers resistance to low temperatures by maintaining chloroplast membranes integrity. Involved in the regulation of fatty acids ratios during seed metabolism. Required for embryo development, especially at the transition from the globular to the heart stage.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18431481}.
Interaction partners:
- Beta-ketoacyl-[acyl-carrier-protein] synthase III, chloroplastic
- EMBRYO DEFECTIVE 3147
- 3-oxoacyl-[acyl-carrier-protein] reductase, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, chloroplastic
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- 3-hydroxyacyl-[acyl-carrier-protein] dehydratase
- Biotin carboxylase, chloroplastic
- AT4g13180/F17N18_70
- NAD
Sequence:
MVGASSSYASPLCTWFVAACMSVSHGGGDSRQAVALQSGGRSRRRRQLSKCSVASGSASIQALVTSCLDFGPCTHYNNNNALSSLFGSNSVSLNRNQRRLNRAASSGGAMAVMEMEKEAAVNKKPPTEQRRVVVTGMGVETSLGHDPHTFYENLLQGNSGISQIENFDCSEFPTRIAGEIKSFSTEGWVAPKLSKRMDKFMLYLLTAGKKALADGGVTDEVMAEFDKTKCGVLIGSAMGGMKVFYDAIEALRISYKKMNPFCVPFATTNMGSAMLAMDLGWMGPNYSISTACATSNFCILNSANHIIKGEADVMLCGGSDAVIIPIGLGGFVACRALSQRNNDPTKASRPWDTNRDGFVMGEGAGVLLLEELEHAKKRGATIYAEFLGGSFTCDAYHMTEPHPDGAGVILCIERALASAGISKEQINYINAHATSTHAGDIKEYQALAHCFGQNPELKVNSTKSMIGHLLGAAGAVEAVATVQAIRTGWVHPNINLENPDSGVDTKLLVGPKKERLDIKAALSNSFGFGGHNSSIIFAPYK
Protein: Battenin (G5EBM4)
Organism: Caenorhabditis elegans
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}. Lysosome membrane {ECO:0000256|RuleBase:RU361113}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361113}.
Interaction partners:
- Alpha-mannosidase
- Battenin
- Battenin
- hydroxymethylglutaryl-CoA lyase
- Probable beta-mannosidase
- Palmitoyl-protein thioesterase 1
- Coelomocyte uptake defective protein 15
- Sulfatase N-terminal domain-containing protein
- Chloride channel protein
- Sphingomyelin phosphodiesterase 1
Sequence:
MVNWTNFRDILAFWLLGLCNNYGYVIMLSAAEDILDDQKGTNSSSTNSSTCETHLDSRHCQSISTGAVLLADNLPALVVQTTFPFFMHRFPFGFRAFLVFLLQASSYFVVAYSKNIAMSLAGVCMASLGQGIGEITFLAMAAHYIPETIASWSSGTGGAGLIGSFSYAFITQAGLSPSNTLLVQLFIPVVFAGAYFFLLTIPPTVYSPTIHPSTWIIPKNYDKDVFEAAEARGDVLNTKKVPQRELGPLERIKLIGPLLYLMVPLATVYTAEYMINQGLTELIIFNCSQGLSLPLSSQYRWYQVLYQLGVFISRSSVKFFEMPLWLIWCLPILQCVNMIFFFFEAVYWFTPTIIIIFVLIVFEGLLGGSAYVNTYNKIHKKVNPDVREYSLSAASMGNSLGTNIAAFLSIPLYNWVCTMKAPGR
Protein: ATP synthase subunit gamma, mitochondrial (F-ATPase gamma subunit) (O01666)
Organism: Drosophila melanogaster (Fruit fly)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(1) domain and the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha(3)beta(3). Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
Subcellular location: Mitochondrion. Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- ATP synthase subunit O, mitochondrial
- Small ribosomal subunit protein uS3
- ATPase protein 9
- ATP synthase subunit beta, mitochondrial
- ATP synthase subunit b, mitochondrial
- ATP synthase F
- ATP synthase subunit a
- ATP synthase subunit alpha, mitochondrial
- ATP synthase subunit d, mitochondrial
- ATP synthase subunit beta
Sequence:
MMMQRTQLLLPLAMEATMLAQQQRGMATLKMISIRLKSVKNIQKITQSMKMVSAAKYARAERDLKAARPYGIGAQQFFEKTEIQPDEKAEPKKLLIAVTSDRGLCGAVHTGVARLIRGELAQDEANTKVFCVGDKSRAILSRLYGKNILMVANEVGRLPPTFLDASKIANEVLQTGYDYTEGKIVYNRFKSVVSYQCSTLPIFSGSTVEKSEKLAVYDSLDSDVVKSYLEFSLASLIFYTMKEGACSEQSSRMTAMDNASKNAGEMIDKLTLTFNRTRQAVITRELIEIISGAAALT
Protein: Cytoplasmic FMR1-interacting protein (A5A5E1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MTTHVTLEDALSNVDLLEELPLPDQQPCIEPPPSSIMYQANFDTNFEDRNAFVTGIARYIEQATVHSSMNEMLEEGHEYAVMLYTWRSCSRAIPQVKCNEQPNRVEIYEKTVEVLEPEVTKLMKFMYFQRKAIERFCSEVKRLCHAERRKDFVSEAYLLTLGKFINMFAVLDELKNMKCSVKNDHSAYKRAAQFLRKMADPQSIQESQNLSMFLANHNRITQCLHQQLEVIPGYEELLADIVNICVDYYENKMYLTPSEKHMLLKVMGFGLYLMDGNVSNIYKLDAKKRINLSKIDKFFKLQVVPLFGDMQIELSRYIETSAHYEENKSKWTCTQSSISPQYNLCEQMVQIREDHIRFISELARYSNSEVVTGSGLDSQKSDEEYRELFDLALRGLQLLSKWSTHVMEVYSWKLVHPTDKFCNKDCPGTAEEYERATRYNYTSEEKFALVEVIAMIKGLQVLMGRMESVFNQAIRHTIYSALQDFAQVTLREPLRQAVRKKKNVLISVLQAIRKTICDWEGAREPPNDPCLRGEKDPKGGFDIKVPRRAVGPSSTQLYMVRTMLESLIADKSGSKKTLRSSLDGPIVQAIEDFHKQSFFFTHLLNFSEALQQCCDLSQLWFREFFLELTMGRRIQFPIEMSMPWILTDHILETKEPSMMEYVLYPLDLYNDSGYYALTKFKKQFLYDEIEAEVNLCFDQFVYKLADQIFAYYKAMAGSVLLDKRFRAECKNYGVIIPYPPSNRYETLLKQRHVQLLGRSIDLNRLITQRISAAMYKSLDQAISRFESEDLTSIVELEWLLEINRLTHRLLSKHMTLDSFDAMFREANHNVSAPYGRITLHVFWELNFDFLPNYCYNGSTNRFVRTAIPFTQEPQRDKPANVQPYYLYGSKPLNIAYSHIYSSYRNFVGPPHFKTICRLLGYQGIAVVMEELLKIVKSLLQGTILQYVKTLIEVMPKICRLPRHEYGSPGILEFFHHQLKDIIEYAELKTDVFQSLREVGNAVLFCLLIEQALVSQEEVCDLLHAAPFQNILPRVYIKEGERLEVRMKRLEAKYAPLHLVPLIERLGTPQQIAIAREGDLLTKERLCCGLSMFEVILTRIRSFLQDNVWRGPPPTNGVMHVDECMEFHRLWSAMQFVYCIPVGTHEFTAEQCFGDGLNWAGCAIIVLLGQQRRFDLFDFCYHLLKVQRQDGKDEIIKNVPLKKMADRIRKYQILNNEIFAILNKYMKAVETDSSTVEHVRCFQPPIHQSLATTC