wanglab/gogpt-training-data huggingface dataset:
Protein: Endonuclease 4 (AtENDO4) (EC 3.1.30.1) (Deoxyribonuclease ENDO4) (Single-stranded-nucleate endonuclease ENDO4) (F4JJL0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Endonuclease that can use single-stranded RNA and DNA as substrates. In contradiction with PubMed:23620482, cannot hydrolyze single-stranded DNA and does not cleave mismatches.
Interaction partners:
- Protein trichome birefringence-like 9
- Bifunctional nuclease 1
- Probable ADP-ribosylation factor GTPase-activating protein AGD8
- Bifunctional nuclease 2
- Microtubule-associated protein 70-4
- Thioredoxin O1, mitochondrial
- Ubiquitin-conjugating enzyme E2 variant 1D
- MAR-binding filament-like protein 1
- Beta-glucosidase 11
Sequence:
MSSSLRQWFARVLVLTQLINGALCWGKEGHYTVCKIAESYFEEETVAAVKKLLPKSADGDLASVCSWPDEIKHHWQWRWTSPLHYVDTPDYRCNYEYCRDCHDTHKNQDRCVTGAIFNYTMQLMSASENSDTIVHYNLTEALMFLSHFIGDIHQPLHVGFLGDEGGNTITVRWYRRKTNLHHVWDNMIIESALKTYYNKSLPLMIEALQANLTNDWSNDVPLWESCQLNQTACPNPYASESINLACKYAYRNATPGTTLGDDYFLSRLPIVEKRLAQGGIRLAATLNRIFSSKPKHAGS
Protein: Serine--tRNA ligase, mitochondrial (EC 6.1.1.11) (SerRSmt) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser/Sec) synthetase) (Q9NP81)
Organism: Homo sapiens (Human)
Function: Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q9N0F3}.
Interaction partners:
- L-seryl-tRNA
- O-phosphoseryl-tRNA
- Probable arginine--tRNA ligase, mitochondrial
- Arginine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, mitochondrial
- Isoleucine--tRNA ligase, mitochondrial
- serine--tRNA ligase
- Tyrosine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
Sequence:
MAASMARRLWPLLTRRGFRPRGGCISNDSPRRSFTTEKRNRNLLYEYAREGYSALPQLDIERFCACPEEAAHALELRKGELRSADLPAIISTWQELRQLQEQIRSLEEEKAAVTEAVRALLANQDSGEVQQDPKYQGLRARGREIRKELVHLYPREAQLEEQFYLQALKLPNQTHPDVPVGDESQARVLHMVGDKPVFSFQPRGHLEIGEKLDIIRQKRLSHVSGHRSYYLRGAGALLQHGLVNFTFNKLLRRGFTPMTVPDLLRGAVFEGCGMTPNANPSQIYNIDPARFKDLNLAGTAEVGLAGYFMDHTVAFRDLPVRMVCSSTCYRAETNTGQEPRGLYRVHHFTKVEMFGVTGPGLEQSSQLLEEFLSLQMEILTELGLHFRVLDMPTQELGLPAYRKFDIEAWMPGRGRFGEVTSASNCTDFQSRRLHIMFQTEAGELQFAHTVNATACAVPRLLIALLESNQQKDGSVLVPPALQSYLGTDRITAPTHVPLQYIGPNQPRKPGLPGQPAVS
Protein: Peptidyl-prolyl cis-trans isomerase FKBP14 (PPIase FKBP14) (EC 5.2.1.8) (22 kDa FK506-binding protein) (22 kDa FKBP) (FKBP-22) (FK506-binding protein 14) (FKBP-14) (Rotamase) (Q9NWM8)
Organism: Homo sapiens (Human)
Function: PPIase which accelerates the folding of proteins during protein synthesis. Has a preference for substrates containing 4-hydroxylproline modifications, including type III collagen. May also target type VI and type X collagens.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138, ECO:0000269|PubMed:22265013}.
Interaction partners:
- X-box-binding protein 1
Sequence:
MRLFLWNAVLTLFVTSLIGALIPEPEVKIEVLQKPFICHRKTKGGDLMLVHYEGYLEKDGSLFHSTHKHNNGQPIWFTLGILEALKGWDQGLKGMCVGEKRKLIIPPALGYGKEGKGKIPPESTLIFNIDLLEIRNGPRSHESFQEMDLNDDWKLSKDEVKAYLKKEFEKHGAVVNESHHDALVEDIFDKEDEDKDGFISAREFTYKHDEL
Protein: Probable membrane transporter protein MamO (Q2W8Q2)
Organism: Paramagnetospirillum magneticum (strain ATCC 700264 / AMB-1) (Magnetospirillum magneticum)
Function: Plays 2 roles; promotes magnetite nucleation/formation and activates the MamE protease (Probable). Despite its near conservation of a protease-like sequence, this is probably not a protease (Probable). Required in conjunction with MamP for proteolysis of at least MamE, itself and MamP. May transport a solute that controls MamE's protease activity. May place individual iron atoms into the magnetite lattice (Probable).
Subcellular location: Magnetosome membrane {ECO:0000269|PubMed:27302060}; Multi-pass membrane protein {ECO:0000305|PubMed:27302060}.
Interaction partners:
- Magnetosome protein MamN
- Magnetosome protein MamH
- Actin-like protein MamK
- Multi-heme protein MamP
- Magnetosome protein MamB
- Magnetosome protein MamM
- Magnetosome protein MamQ 1
- Magnetosome protein MamR
- Magnetosome protein MamL
- Magnetosome protein MamA
Sequence:
MIEVGETMGELPTNKIVFCERSWKTPVSILAFLIFVTFAWGIYLLDHYDEDDNFHGADDLSVGQFLVRNIAMPHVQRLYHTVPPAVVGVGGGGVNAGPVASGAIVGTNGYVITTLHSVSKLPEISVQVATTGGIRRFPAQVVKTIPGHDLALLKMQTTEKFLHFRMADVQTVVPGQQVFAFGRNMAGAPLVRQGLVQSADAPLAVGATQITHLLRSDAVYSWEQTGGPLVNAQGDLVGINIAATGPTGKVEGFTVPAQVIVSHLQDVVRFKKGSATAPGQPQTQTVAAGSTNWWSKARAVVGGPTAIPGMGMNVVQGNVVKGNVAPSIPSGMPFIDTDHVGGAKIGGYSVADIVGLVMLALAAGVTGGMMTMGGGVLQVAGMMVFFGYGMYLIRPVVFLTNVVVYGAASLRNDKAQLVQWDKVKPLIPWGIAGVILGYFIGNAIGDSVVGILLGLFALIMAGKAVMEILQPNAGEETAESISATEAEDEMDELMALADGTSRPKASGLALPEGHARSAVLGLPMGLFSGILGISGGVIEVPLQRYVGRISLQNAIANSSVLVFWASVAGSVVAFLHGSSTGLIHWEAPVTLALVMIPGAYVGGIIGARLMRVLPVRVLKGVYAATMAAIALKMLTSV
Protein: Hemoglobin subunit beta-2 (Beta-2-globin) (Hemoglobin beta-2 chain) (Hemoglobin beta-minor chain) (P02089)
Organism: Mus musculus (Mouse)
Function: Involved in oxygen transport from the lung to the various peripheral tissues.
Interaction partners:
Sequence:
MVHLTDAEKSAVSCLWAKVNPDEVGGEALGRLLVVYPWTQRYFDSFGDLSSASAIMGNPKVKAHGKKVITAFNEGLKNLDNLKGTFASLSELHCDKLHVDPENFRLLGNAIVIVLGHHLGKDFTPAAQAAFQKVVAGVATALAHKYH
Protein: Mast cell protease 1-like 3 (E9PTQ9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MQALLFLMALLLPSGAGAEEIIGGVESIPHSRPYMALLKIVTEEGHVTFCGGFLISHLFVMTAAHCRGKEITVILGAHDMSKRESTQQKIKVEKQIFYPKYNFFSNFHDIMLLKLEEKAVLTPTVNVIPLPQSSDFIKPGKMCWAAGWGRTGVTEPTSDTLREVKLRIMEKKACWYFWHYDNRFQICVGSPEMLKLTYKEDSGGPLVCAGVAHGIVSHGRGRGKPPIIFTRISSYVPWIDTVIKGN
Protein: X-prolyl aminopeptidase (Aminopeptidase P) 3, putative (Xaa-Pro aminopeptidase 3 (EC 3.4.11.9)) (Q6NYT0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MFHSSSGLLRAAVQCASRSYWCPGSVWCPCRHVSVKTEGWNSKKVPQRYLGQPSPYTHPHLIRHGEVTPGLTQTEYELRRQRLASLIEIQAERQTGSGASSNSSHIVIILSHPIRYMSNDIPYPFHQNQDFLYLTGITEPDSALVMYGSSKPDQAVLFVPRRDPARELWDGPRSGKDGAAALTGLERVHSTEELGVVLKSIKGGTVWYDNSQPCHQRLHQTHVRPLLEGGQLVKSLRPLTHSLRAIKSPAEVALMKEAGRITAQAFKKTMAMSRGNIDEAVLYAKFDYECRAHGANFLAYPPVVAGGNRANTLHYINNNQIVKDGEMVLLDGGCEYFGYVSDITRTWPVNGKFSAAQRELYEAVLEVQLACLSQCSPGVSLDYIYSTMLTLLARQLKELGIVPSHASDTDAMKAARQFCPHHVGHYLGMDVHDTPELSRSQPLQPGMVITIEPGLYISEDNRSCPERFRGLGVRIEDDVVIRDHGEPLILSANTPKTISEVERTCAHAED
Protein: ADP-ribosylation factor-like protein 6-interacting protein 1 (ARL-6-interacting protein 1) (Aip-1) (Apoptotic regulator in the membrane of the endoplasmic reticulum) (Q15041)
Organism: Homo sapiens (Human)
Function: Positively regulates SLC1A1/EAAC1-mediated glutamate transport by increasing its affinity for glutamate in a PKC activity-dependent manner. Promotes the catalytic efficiency of SLC1A1/EAAC1 probably by reducing its interaction with ARL6IP5, a negative regulator of SLC1A1/EAAC1-mediated glutamate transport (By similarity). Plays a role in the formation and stabilization of endoplasmic reticulum tubules. Negatively regulates apoptosis, possibly by modulating the activity of caspase-9 (CASP9). Inhibits cleavage of CASP9-dependent substrates and downstream markers of apoptosis but not CASP9 itself. May be involved in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:10995579}; Multi-pass membrane protein {ECO:0000269|PubMed:10995579}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12754298, ECO:0000269|PubMed:24076029, ECO:0000269|PubMed:24262037}; Multi-pass membrane protein {ECO:0000269|PubMed:24076029}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9JKW0}. Note=Predominantly localized to intracytoplasmic membranes. Preferentially localizes at the ER tubules and the edge of the ER sheets, both of which are characterized by a high membrane curvature. {ECO:0000269|PubMed:24262037}.
Interaction partners:
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL15
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein eS21
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS19
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein eS28
Sequence:
MAEGDNRSTNLLAAETASLEEQLQGWGEVMLMADKVLRWERAWFPPAIMGVVSLVFLIIYYLDPSVLSGVSCFVMFLCLADYLVPILAPRIFGSNKWTTEQQQRFHEICSNLVKTRRRAVGWWKRLFTLKEEKPKMYFMTMIVSLAAVAWVGQQVHNLLLTYLIVTSLLLLPGLNQHGIILKYIGMAKREINKLLKQKEKKNE
Protein: Glutamate receptor ionotropic, delta-2 (GluD2) (GluR delta-2 subunit) (Q63226)
Organism: Rattus norvegicus (Rat)
Function: Receptor for glutamate. L-glutamate acts as an excitatory neurotransmitter at many synapses in the central nervous system. The postsynaptic actions of Glu are mediated by a variety of receptors that are named according to their selective agonists. Promotes synaptogenesis and mediates the D-Serine-dependent long term depression signals and AMPA receptor endocytosis of cerebellar parallel fiber-Purkinje cell (PF-PC) synapses through the beta-NRX1-CBLN1-GRID2 triad complex.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q61625}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cerebellin-1
- Neurexin-3
- Glutamate receptor ionotropic, kainate 2
- Glutamate receptor 1
- Neurexin-2
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor 4
- Glutamate receptor ionotropic, NMDA 3A
- Glutamate receptor ionotropic, NMDA 2B
- Glutamate receptor ionotropic, NMDA 2A
Sequence:
MEVFPLLFFLSFWWSRTWDLATSDSIIHIGAIFDESAKKDDEVFRTAVGDLNQNEEILQTEKITFSVTFVDGNNPFQAVQEACELMNQGILALVSSIGCTSAGSLQSLADAMHIPHLFIQRSTAGTPRSGCGLTRSNRNDDYTLSVRPPVYLNEVILRVVTEYAWQKFIIFYDSEYDIRGIQEFLDKVSQQGMDVALQKVENNINKMITTLFDTMRIEELNRYRDTLRRAILVMNPATAKSFISEVVETNLVAFDCHWIIINEEINDVDVQELVRRSIGRLTIIRQTFPVPQNISQRCFRGNHRISSTLCDPKDPFAQNMEISNLYIYDTVLLLANAFHKKLEDRKWHSMASLSCIRKNSKPWQGGRSMLETIKKGGVNGLTGDLEFGENGGNPNVHFEILGTNYGEELGRGVRKLGCWNPVTGLNGSLTDKKLENNMRGVVLRVVTVLEEPFVMVSENVLGKPKKYQGFSIDVLDALSNYLGFNYEIYVAPDHKYGSPQEDGTWNGLVGELVFKRADIGISALTITPDRENVVDFTTRYMDYSVGVLLRRAEKTVDMFACLAPFDLSLWACIAGTVLLVGLLVYLLNWLNPPRLQMGSMTSTTLYNSMWFVYGSFVQQGGEVPYTTLATRMMMGAWWLFALIVISSYTANLAAFLTITRIESSIQSLQDLSKQTDIPYGTVLDSAVYQHVRMKGLNPFERDSMYSQMWRMINRSNGSENNVLESQAGIQKVKYGNYAFVWDAAVLEYVAINDPDCSFYTVGNTVADRGYGIALQHGSPYRDVFSQRILELQQSGDMDILKHKWWPKNGQCDLYSSVDAKQKGGALDIKSLAGVFCILAAGIVLSCLIAVLETWWSRRKGSRVPSKEDDKEIDLEHLHRRVNSLCTDDDSPHKQFSTSSIDLTPLDIDTLPTRQALEQISDFRNTHITTTTFIPEQIQTLSRTLSAKAASGFTFGSVPEHRTGPFRHRAPNGGFFRSPIKTMSSIPYQPTPTLGLNLGNDPDRGTSI
Protein: DNA alpha-glucosyltransferase (AGT) (Alpha-GT) (EC 2.4.1.26) (P04519)
Organism: Enterobacteria phage T4 (Bacteriophage T4)
Function: Catalyzes the transfer of glucose from uridine diphosphoglucose to 5-hydroxymethyl cytosine of T4 DNA to yield glucosyl 5-hydroxymethyl cytosine (glc-HMC). This DNA process seems to occur immediately after DNA synthesis since the DNA alpha-glucosyltransferase interacts with the clamp protein gp45. The glc-HMC modification protects the phage genome against its own nucleases and the host restriction endonuclease system. The glc-HMC modification also protects against the host CRISPR-Cas9 defense system.
Interaction partners:
Sequence:
MRICIFMARGLEGCGVTKFSLEQRDWFIKNGHEVTLVYAKDKSFTRTSSHDHKSFSIPVILAKEYDKALKLVNDCDILIINSVPATSVQEATINNYKKLLDNIKPSIRVVVYQHDHSVLSLRRNLGLEETVRRADVIFSHSDNGDFNKVLMKEWYPETVSLFDDIEEAPTVYNFQPPMDIVKVRSTYWKDVSEINMNINRWIGRTTTWKGFYQMFDFHEKFLKPAGKSTVMEGLERSPAFIAIKEKGIPYEYYGNREIDKMNLAPNQPAQILDCYINSEMLERMSKSGFGYQLSKLNQKYLQRSLEYTHLELGACGTIPVFWKSTGENLKFRVDNTPLTSHDSGIIWFDENDMESTFERIKELSSDRALYDREREKAYEFLYQHQDSSFCFKEQFDIITK
Protein: AT31643p (Q8T8S0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAKRDILPVFPSRANSVIMKQRVLAARRGVGLLKRKRDAIDMKLRELRRIRFDQDMHGDEAMRNAIFSMAKANLLGADFKPQMVSRSHVATVSLRRTEIKIVGVKLNTLELETKGVGAFPLAGLSCGGMQVSRIRDSYTKALKALVEFASLEYQVRMLEAASLQTNMRVNALEHVVIPILQNTYNYICGELEEFEREDFYRLKRSQAKQLEAKMAFTELIKTKNMTDEELETYIKRNINQTRPPAADTPFDQEQFEEREVKRRMREARLSLKQRREQERKEAIKRGEPPPPTSFITTHGASLSFAGRQRDPRASSGDLYSTKRMLLSSGPERKSASNVTERKSDTPPRNSQETQRRSSQMSKDVVNEDPPEES
Protein: FAD-linked oxidoreductase fmqD (EC 1.-.-.-) (Fumiquinazoline biosynthesis cluster protein D) (Q4WLW6)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of the antitumor fumiquinazolines that confer a dual-usage capability to defend against phagocytes in the environment and animal hosts. The simplest member is fumiquinazoline F (FQF) with a 6-6-6 tricyclic core derived from anthranilic acid (Ant), tryptophan (Trp), and alanine (Ala). The trimodular NRPS fmqA is responsible for FQF formation. Modules 1, 2 and 3 of fmqA are predicted to activate and load Ant, Trp and Ala, respectively, providing for the assembly of an Ant-Trp-Ala-S-enzyme intermediate that would undergo double cyclization for chain release and generation of the tricyclic 6-6-6 product fumiquinazoline F. The presence of an E domain predicted for module 2 of fmqA is consistent with epimerization of L-Trp to D-Trp during assembly to generate the R-stereocenter at C14 of FQF. The FAD-dependent monooxygenase fmqB and the monomodular NRPS fmqC then maturate FQF to FQA. FmqB oxidizes the 2',3'-double bond of the indole side chain of FQF, and fmqC activates L-Ala as the adenylate, installs it as the pantetheinyl thioester on its carrier protein domain, and acylates the oxidized indole for subsequent intramolecular cyclization to create the 6-5-5-imidazolindolone of FQA. The FAD-linked oxidoreductase fmqD introduces a third layer of scaffold complexity by converting FQA to the spirohemiaminal FQC, presumably by catalyzing the formation of a transient imine within the pyrazinone ring. FQC subsequently converts nonenzymatically to the known cyclic aminal FQD.
Subcellular location: Secreted {ECO:0000269|PubMed:24612080, ECO:0000305|PubMed:21899262}. Secreted, cell wall {ECO:0000269|PubMed:24612080}. Note=Localizes to the cell wall of the conidia and In to both the cell wall and septa in the hyphae (PubMed:24612080). {ECO:0000269|PubMed:24612080}.
Interaction partners:
- Nonribosomal peptide synthetase fmqC
- FAD-dependent monooxygenase fmqB
- MFS transporter fmqE
Sequence:
MQYIPFLISGLVPVALSKSLFEATSNTRIDGNDIAAIFGPVLTPEAHIFLPSDGDYDDNVMARWSTFNDPSYVATVKPATETDVQAIREYQVSTAASHNITFFATGGGHGVKLNFGNVQNAINIELSLLDFIDLDLDNEVVTIGPGVENAQLYDLLSSVGKETALTGERCVNTIGPTLGGGLGPLYGIRGPQVDSLVSARLVTASGDVITVSRSENRDLFWAIRGAGANFGIVTSATYRIYDQTNGGMAVSAQFAFAPAVNRSVFDLMESMNDEYPPGMSGGMILSYNHTTNEPSVQWNLLFMGSNEDAQPWLDKIQALGPIDSSIRNVPWHRRDEPEVPYCERGQHYILYNLNLRRTDAATLQSYFDSFVDFSSKNPWFDCDLMYERQATDAALAVPLSERGVGPWRDSKINANFLVVTPSEEYDEAADAFVRPFMDRFQAVMGFDTLHVYVNEALGDEGPASWYGEENLPRLVALKQQWDPENKFGAGAPIPLSL
Protein: Methyl-CpG-binding protein 2 (MeCp-2 protein) (MeCp2) (A0A140VKC4)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|PIRNR:PIRNR038006}. Note=Colocalized with methyl-CpG in the genome. {ECO:0000256|PIRNR:PIRNR038006}.
Interaction partners:
Sequence:
MAAAAAAAPSGGGGGGEEERLEEKSEDQDLQGLKDKPLKFKKVKKDKKEEKEGKHEPVQPSAHHSAEPAEAGKAETSEGSGSAPAVPEASASPKQRRSIIRDRGPMYDDPTLPEGWTRKLKQRKSGRSAGKYDVYLINPQGKAFRSKVELIAYFEKVGDTSLDPNDFDFTVTGRGSPSRREQKPPKKPKSPKAPGTGRGRGRPKGSGTTRPKAATSEGVQVKRVLEKSPGKLLVKMPFQTSPGGKAEGGGATTSTQVMVIKRPGRKRKAEADPQAIPKKRGRKPGSVVAAAAAEAKKKAVKESSIRSVQETVLPIKKRKTRETVSIEVKEVVKPLLVSTLGEKSGKGLKTCKSPGRKSKESSPKGRSSSASSPPKKEHHHHHHHSESPKAPVPLLPPLPPPPPEPESSEDPTSPPEPQDLSSSVCKEEKMPRGGSLESDGCPKEPAKTQPAVATAATAAEKYKHRGEGERKDIVSSSMPRPNREEPVDSRTPVTERVS
Protein: Lathosterol oxidase (EC 1.14.19.20) (Sterol-C5-desaturase (Fungal ERG3, delta-5-desaturase) homolog (S. cerevisae)) (Q66ID6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MDLVLKVADHYFFTPYVYPSSWPEDNPLRQIIGLMVVTNLGAAILYLGLGALSYFFVFDHKLKDHPQFLENQVQREIKYALWSLPWISIPTVALFFAEVRGYSKLYDRVDDSPLGWSGLIFSMVSFLFFTDMCIYWIHRFLHHKLIYKYFHKPHHVWKIPTPFASHAFHPVDGFLQGLPYHIYPFFFPLHKVLYLILYVFVNIWTISIHDGDYRVPNMVEEIINGSAHHTDHHLFFDYNYGQYFTLWDRIGGSYRYPSALMGKGPHDQIKKLMAEGKLISNSSKGHTNNNQKNGIHVKKE
Protein: Ganglioside GM2 activator (Cerebroside sulfate activator protein) (GM2-AP) (Sphingolipid activator protein 3) (SAP-3) [Cleaved into: Ganglioside GM2 activator isoform short] (P17900)
Organism: Homo sapiens (Human)
Function: The large binding pocket can accommodate several single chain phospholipids and fatty acids, GM2A also exhibits some calcium-independent phospholipase activity (By similarity). Binds gangliosides and stimulates ganglioside GM2 degradation. It stimulates only the breakdown of ganglioside GM2 and glycolipid GA2 by beta-hexosaminidase A. It extracts single GM2 molecules from membranes and presents them in soluble form to beta-hexosaminidase A for cleavage of N-acetyl-D-galactosamine and conversion to GM3 (By similarity). Has cholesterol transfer activity.
Subcellular location: Lysosome.
Interaction partners:
- Beta-hexosaminidase subunit beta
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Beta-hexosaminidase subunit alpha
- Protein O-GlcNAcase
- NPC intracellular cholesterol transporter 2
Sequence:
MQSLMQAPLLIALGLLLAAPAQAHLKKPSQLSSFSWDNCDEGKDPAVIRSLTLEPDPIIVPGNVTLSVMGSTSVPLSSPLKVDLVLEKEVAGLWIKIPCTDYIGSCTFEHFCDVLDMLIPTGEPCPEPLRTYGLPCHCPFKEGTYSLPKSEFVVPDLELPSWLTTGNYRIESVLSSSGKRLGCIKIAASLKGI
Protein: S-adenosyl-L-methionine-dependent methyltransferases superfamily protein (Q9SUW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- non-specific serine/threonine protein kinase
- F9L1.6
- At1g33030
- Paraxanthine methyltransferase 2
- Disease resistance protein ADR2
- Novel plant SNARE 12
- Folylpolyglutamate synthase
Sequence:
MSGVYDSQADIYLDARPTYPADWYSKLAALSHRHNLAWDAGTGNGQAAIGIAEHYERVVATDVSETMLNLGKPHPKVTYHHTPSSMTEDEMVDLIGGENSVDLITVATAVHWFDLPRFYAIANRLLRKPGGIIAVWSYNTDMVVNPEFDSVMTRFIAETLPYCKFPESQYFLDGYKTLPFPFESVGLGSEGKPMELEMKKTVSFEGFLRMLRSWSAVGAAKEKGVDLLSDNVVKELETAWGGYELVRTIVYKTFMLAGTVP
Protein: Heavy metal-associated isoprenylated plant protein 25 (AtHIP25) (AtHIPP25) (O49613)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heavy-metal-binding protein. Binds cadmium. May be involved in cadmium transport and play a role in cadmium detoxification.
Subcellular location: Membrane {ECO:0000250|UniProtKB:Q9SZN7}.
Interaction partners:
- Protein yippee-like At4g27740
- Filament-like protein
- Transmembrane protein, putative
- Haloacid dehalogenase-like hydrolase
- Heavy metal-associated isoprenylated plant protein 2
- C2 domain-containing protein At1g53590
- Protein NETWORKED 2D
- At3g45160
- Protein CutA, chloroplastic
- At1g64330
Sequence:
MGVLDHVSEYFDCSHGSSKRHKSLQTVDVRVLIDCEGCERKVRRALEGMRGIRDVTIEPNAQKVTVVGYVEPNKVVARIIHRTGKRAELYPFVPYDVVAHPYASGVYDNRAPTGYVRNTEYDPHVSRLARASSTEVRYTTAFSDENASACVVM
Protein: Phthiodiolone/phenolphthiodiolone dimycocerosates ketoreductase (EC 1.2.-.-) (P9WIB7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the reduction of the keto moiety of phthiodiolone dimycocerosates (DIM B) and glycosylated phenolphthiodiolone dimycocerosates to form the intermediate compounds phthiotriol and glycosylated phenolphthiotriol dimycocerosates during phthiocerol dimycocerosates (DIM A) and glycosylated phenolphthiocerol dimycocerosates (PGL) biosynthesis.
Interaction partners:
- Trans-acting enoyl reductase
- Phthiotriol/phenolphthiotriol dimycocerosates methyltransferase
- Bifunctional F420 biosynthesis protein FbiB
- Phosphoenolpyruvate transferase
- F420H
- Hypothetical oxidoreductase
- Putative F420H
- Possible oxidoreductase
- Deazaflavin-dependent nitroreductase
- Conserved protein
Sequence:
MGGLRFGFVDALVHSRLPPTLPARSSMAAATVMGADSYWVGDHLNALVPRSIATSEYLGIAAKFVPKIDANYEPWTMLGNLAFGLPSRLRLGVCVTDAGRRNPAVTAQAAATLHLLTRGRAILGIGVGEREGNEPYGVEWTKPVARFEEALATIRALWNSNGELISRESPYFPLHNALFDLPPYRGKWPEIWVAAHGPRMLRATGRYADAWIPIVVVRPSDYSRALEAVRSAASDAGRDPMSITPAAVRGIITGRNRDDVEEALESVVVKMTALGVPGEAWARHGVEHPMGADFSGVQDIIPQTMDKQTVLSYAAKVPAALMKEVVFSGTPDEVIDQVAEWRDHGLRYVVLINGSLVNPSLRKTVTAVLPHAKVLRGLKKL
Protein: Plant UBX domain-containing protein 10 (PUX10) (Q9M0N1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cell division control protein 48 homolog A
- Plant UBX domain-containing protein 3
- Protein OS-9 homolog
- Uncharacterized protein At2g04870
- Di-glucose binding protein with Leucine-rich repeat domain-containing protein
- DNA binding protein
- AT3g18860/MCB22_3
- Plant UBX domain-containing protein 1
- Plant UBX domain-containing protein 5
- Probable ubiquitin conjugation factor E4
Sequence:
MVDTVDKLGYFQAITGLEDADLCTEILQAHGWDLELAISSFTSSDQDASSSAVDGGGNNRDHDHNNATVTPDYPPRGIVDDTELVMRDDGGGNRGPGVAWRIITLPISIVSGSLGLVSGAIGLGIWAAGGVLSYSLGMLGFRSGRGGGSESARLVSVSSAVGEAMEFVALFDRDYGSNNAFKIDFVVEGFMDALQRSRSSFKLLFVYLHSPDHPDTPVFCGGTLCNEAVVAFVNENFVSWGGSIRSSEGFKMSNSLKASRFPFCAVVMPAANQRIALLQQVEGPKSPEEMLAILQRIVEDSSPTLVTARVEAEERRTNLRLREEQDAAYRAALEADQAREQQRQEEKERLEREAAEAERKLKEEEEARERAAREAEERQAARVRMRQEKALALGEEPEKGPDVTQVLVRFPNGERKGRMFKSETKIQTLYDYVDSLGLLDTEEYSLITNFPRTVYGRDKESMSLKDAGLHPQASLFIEIN
Protein: Large ribosomal subunit protein uL4 (60S ribosomal protein L1) (60S ribosomal protein L4) (P50878)
Organism: Rattus norvegicus (Rat)
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:0000250|UniProtKB:P36578}.
Interaction partners:
- Large ribosomal subunit protein uL13
- Small ribosomal subunit protein uS7
- Ubiquitin-like protein FUBI
- Large ribosomal subunit protein uL3
- Ubiquitin-ribosomal protein eL40 fusion protein
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL15
- Large ribosomal subunit protein uL18
- Large ribosomal subunit protein eL24
- Large ribosomal subunit protein uL14
Sequence:
MACARPLISVYSEKGESSGKNVTLPAVFKAPIRPDIVNFVHTNLRKNNRQPYAVSELAGHQTSAESWGTGRAVARIPRVRGGGTHRSGQGAFGNMCRGGRMFAPTKTWRRWHRRVNTTQKRYAICSALAASALPALVMSKGHCVEEVPELPLVVEDKVESYKKTKEAVQLLKKLKAWNDIKKVYASQRMRAGKGKMRNRRRIQRRGPCIIYNEDNGIIKAFRNIPGITLLNVSKLNILKLAPGGHVGRFCIWTESAFRKLDELYGTWRKAASLKSNYNLPMHKMMNTDLSRILKSPEIQRALRAPRKKIHRRVLKKNPLKNLRIMLKLNPYAKTMRRNTILRQARNHKLRVKKLEAAAAALAAKSEKIVPEKGAGDKKPAVGKKGKKPVDAKKLKKPAGKKVVTKKPAEKKPTTEEKKSAA
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0B4K697)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MQRRERQASGGGPQTTTAGPSAGNVANATTALAGGKSSSNNMYSTRQSVSTTTGVLMVGPNFRVGKKIGCGNFGELRLGRRMCCFGGGVGGRNGRGTTDNGGAGKNLYNNEHVAIKMEPMKSKAPQLHLEYRFYKLLGSHADNAPDGIPRIYHLGTCGGRYNAMVLELLGLSLEDLFNICARKFSLKTVLMIAKQLLHRIEYVHSRHLIYRDVKPENFLIGRTSTKREKIIHIIDFGLAKEYIDLDTNRHIPYREHKSLTGTARYMSINTHMGREQSRRDDLEALGHMFMYFLRGSLPWQGLKADTLKERYQKIGDTKRATPIEVLCDGHPEEFATYLRYVRRLDFFETPDYDFLRRLFQDLFDRKGYTDEGEFDWTGKTMSTPVGSLQTGHEVIISPNKDRHNVTAKDVSYFDFDDDVDDENEEYIILQTNAKGGVAAWPDVPKPGATLGNLTPADRHGSVQVVSSTNGELNPDDPTAGHSNTPITQQPEVEVVDETNGSLYSRCCCFFKRKKKKSTRQK
Protein: Heat shock protein 70 (Q8I2X4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Endoplasmic reticulum chaperone GRP170
- DnaJ protein, putative
- Endoplasmin, putative
- Hsp70 nucleotide exchange factor FES1
- Translocation protein SEC63, putative
- GrpE protein homolog
- Thioredoxin-like protein
- Heat shock 70 kDa protein
- non-specific serine/threonine protein kinase
- Protein disulfide isomerase
Sequence:
MKQIRPYILLLIVSLLKFISAVDSNIEGPVIGIDLGTTYSCVGVFKNGRVEILNNELGNRITPSYVSFVDGERKVGEAAKLEATLHPTQTVFDVKRLIGRKFDDQEVVKDRSLLPYEIVNNQGKPNIKVQIKDKDTTFAPEQISAMVLEKMKEIAQSFLGKPVKNAVVTVPAYFNDAQRQATKDAGTIAGLNIVRIINEPTAAALAYGLDKKEETSILVYDLGGGTFDVSILVIDNGVFEVYATAGNTHLGGEDFDQRVMDYFIKMFKKKNNIDLRTDKRAIQKLRKEVEIAKRNLSVVHSTQIEIEDIVEGHNFSETLTRAKFEELNDDLFRETLEPVKKVLDDAKYEKSKIDEIVLVGGSTRIPKIQQIIKEFFNGKEPNRGINPDEAVAYGAAIQAGIILGEELQDVVLLDVTPLTLGIETVGGIMTQLIKRNTVIPTKKSQTFSTYQDNQPAVLIQVFEGERALTKDNHLLGKFELSGIPPAQRGVPKIEVTFTVDKNGILHVEAEDKGTGKSRGITITNDKGRLSKEQIEKMINDAEKFADEDKNLREKVEAKNNLDNYIQSMKATVEDKDKLADKIEKEDKNTILSAVKDAEDWLNNNSNADSEALKQKLKDLEAVCQPIIVKLYGQPGGPSPQPSGDEDVDSDEL