wanglab/gogpt-training-data huggingface dataset:
Protein: Homer protein homolog 1 (PSD-Zip45) (VASP/Ena-related gene up-regulated during seizure and LTP 1) (Vesl-1) (Q9Z214)
Organism: Rattus norvegicus (Rat)
Function: Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Differentially regulates the functions of the calcium activated channel ryanodine receptors RYR1 and RYR2. Isoform 1 decreases the activity of RYR2, and increases the activity of RYR1, whereas isoform 3 counteracts the effects by competing for binding sites. Isoform 1 regulates the trafficking and surface expression of GRM5. Isoform 3 acts as a natural dominant negative, in dynamic competition with constitutively expressed isoform 1, and isoform 2 to regulate synaptic metabotropic glutamate function. Isoform 3, may be involved in the structural changes that occur at synapses during long-lasting neuronal plasticity and development. Forms a high-order complex with SHANK1, which in turn is necessary for the structural and functional integrity of dendritic spines. Negatively regulates T cell activation by inhibiting the calcineurin-NFAT pathway. Acts by competing with calcineurin/PPP3CA for NFAT protein binding, hence preventing NFAT activation by PPP3CA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Postsynaptic density {ECO:0000250}. Synapse {ECO:0000269|PubMed:10433269}. Cell projection, dendritic spine {ECO:0000269|PubMed:19345194, ECO:0000269|PubMed:30021165}. Note=Isoform 1 inhibits surface expression of GRM5 causing it to be retained in the endoplasmic reticulum. {ECO:0000250}.
Interaction partners:
- SH3 and multiple ankyrin repeat domains protein 1
- Homer protein homolog 3
- Metabotropic glutamate receptor 1
- SH3 and multiple ankyrin repeat domains protein 3
- Homer protein homolog 2
- Metabotropic glutamate receptor 5
- Glutamate receptor ionotropic, NMDA 1
- Disks large homolog 4
- Glutamate receptor ionotropic, NMDA 2A
- Vesicular glutamate transporter 1
Sequence:
MGEQPIFSTRAHVFQIDPNTKKNWVPTSKHAVTVSYFYDSTRNVYRIISLDGSKAIINSTITPNMTFTKTSQKFGQWADSRANTVYGLGFSSEHHLSKFAEKFQEFKEAARLAKEKSQEKMELTSTPSQESAGGDLQSPLTPESINGTDDERTPDVTQNSEPRAEPAQNALPFSHSAGDRTQGLSHASSAISKHWEAELATLKGNNAKLTAALLESTANVKQWKQQLAAYQEEAERLHKRVTELECVSSQANAVHSHKTELSQTVQELEETLKVKEEEIERLKQEIDNARELQEQRDSLTQKLQEVEIRNKDLEGQLSELEQRLEKSQSEQDAFRSNLKTLLEILDGKIFELTELRDNLAKLLECS
Protein: Calcium-independent phospholipase A2-gamma (EC 3.1.1.-) (EC 3.1.1.5) (Intracellular membrane-associated calcium-independent phospholipase A2 gamma) (iPLA2-gamma) (Patatin-like phospholipase domain-containing protein 8) (Q8K1N1)
Organism: Mus musculus (Mouse)
Function: Calcium-independent and membrane-bound phospholipase, that catalyzes the esterolytic cleavage of fatty acids from glycerophospholipids to yield free fatty acids and lysophospholipids, hence regulating membrane physical properties and the release of lipid second messengers and growth factors. Hydrolyzes phosphatidylethanolamine, phosphatidylcholine and probably phosphatidylinositol with a possible preference for the former. Has also a broad substrate specificity in terms of fatty acid moieties, hydrolyzing saturated and mono-unsaturated fatty acids at nearly equal rates from either the sn-1 or sn-2 position in diacyl phosphatidylcholine. However, has a weak activity toward polyunsaturated fatty acids at the sn-2 position, and thereby favors the production of 2-arachidonoyl lysophosphatidylcholine, a key branch point metabolite in eicosanoid signaling. On the other hand, can produce arachidonic acid from the sn-1 position of diacyl phospholipid and from the sn-2 position of arachidonate-containing plasmalogen substrates. Therefore, plays an important role in the mobilization of arachidonic acid in response to cellular stimuli and the generation of lipid second messengers. Can also hydrolyze lysophosphatidylcholine (By similarity). In the mitochondrial compartment, catalyzes the hydrolysis and release of oxidized aliphatic chains from cardiolipin and integrates mitochondrial bioenergetics and signaling. It is essential for maintaining efficient bioenergetic mitochondrial function through tailoring mitochondrial membrane lipid metabolism and composition.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q5XTS1}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5XTS1}. Mitochondrion membrane {ECO:0000269|PubMed:17213206, ECO:0000269|PubMed:17923475}; Single-pass membrane protein {ECO:0000305}. Peroxisome membrane {ECO:0000269|PubMed:17213206}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytosolic phospholipase A2 gamma
- Omega-hydroxyceramide transacylase
- Patatin-like phospholipase domain-containing protein 5
Sequence:
MSINLTLDIYIYFLNNARSLCGKQRSKQLHFVCSKQYWRMNHVNVHREFHTSKKSCKWNRSEAHCSKHWHSPSNHGLHFGIVRLSTSAPKGLTKVSIHMSRIKSTLNSVSKAIFGSQNEMVTRLAQFKPSSRILRKVSDKGWLKQKNVKQAVESLKNYSDKSAGKNSLAEQKSYFADKEEDSGKHSLFHYTYGITTRFGESFSVLANHINSYFKSKGKMSQTKEDKQLQDKPDLEERKSSSPGPDTVADRPDSESPLEVKDKLSSPTQMPEAHPVSAKQSIANFLSRPTEGVQALVGGYIGGLVPKLKSDPKSPPEEQEVSAKTEQAVNKDKKAEEKKRVLLQQEKIIARVSIDNRTRALVQALRRTADPKLCITRVEELTFHLLEFPEGKGVAIKEKIIPYLLRLRQVKDETLQAAVREILALIGYVDPVKGRGIRILTIDGGGTRGVVALQTLRKLVELTQKPIHQLFDYICGVSTGAILAFMLGLFHMPLDECEELYRKLGSDVFTQNVIVGTVKMSWSHAFYDSNTWEKILKDRIGSALMIETARNPACPKVAAISTIVNRGQTPKAFVFRNYGHFPGTNSHYLGGCQYKMWQAIRASSAAPGYFAEYALGSDLHQDGGLLLNNPSALALHECKCIWPDTPLECIVSLGTGRYESDVRNTSTYTSLKTKLSNVISSATDTEEVHIMLDGLLPSDTYFRFNPVICENIPLDESRDEKLDQLQLEGMKYIERNDQKMKKVAKILSQEKTTLQKINDWIKLKSDMYEGLPFFSKL
Protein: Leucine--tRNA ligase, cytoplasmic (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) (F4I116)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
Subcellular location: Cytoplasm, cytosol {ECO:0000305|PubMed:16251277, ECO:0000305|PubMed:16297076}.
Interaction partners:
- Isoleucine--tRNA ligase, cytoplasmic
- Methionine--tRNA ligase, cytoplasmic
- Glutamate--tRNA ligase, cytoplasmic
- Methionine-tRNA ligase
- ATP binding / aminoacyl-tRNA ligase/ nucleotide binding protein
- Arginine--tRNA ligase, chloroplastic/mitochondrial
- Lysine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
- Glutamine--tRNA ligase, cytoplasmic
Sequence:
MASESKSYARRDRLLEIEATVRKWWEDEDVFRAESCENLPKPGEKFFSTFPFPYMNGYLHIGHAFSLSKVDFASAYHRLRGANVLLPFGFHCTGMPIKASADKLRREIEQFGNPPVFTAEDTTKVPEVQEESSDTIALPIPGQFKGKKSKVAAKAGGQVYQWEIMRSFGLTDSEIANFREPSEWLYYFPPLAVEDLRAYGLGCDWRRSFVTTDVNPFFDAFVRWQMRKLKSMGKIVKDRRYTIFSPLDGQPCADHDRATGEGVQPQEYTLIKMEVVKPFPLKLGPLEGKRVFLAAATLRPETMYGQTNAWVLPDGKYGAYEISETEVFILTERAALNLAYQNFSKNPQEPSCLVELTGYDLIGLPLRSPLSVNEIIYALPMLTILTNKGTGIVTSVPSDAPDDYMALQDLIKKPALQDKYGVKTEWLPTEIIPIINIPEFGDKAAEKVCLDLKIKSQNDKEKLAEAKRLTYLKGFTEGTMLIGEFFGRKVQEIKPIIKTKLIETGEAIIYSEPEKPVMSRSGDECVVALTDQWYITYGESEWRKIAEECLSKMNLYSDETRHGFEHTLSWLNQWACSRSFGLGTRIPWDEQFLVESLSDSSLYMAYYTVAHIFHDGDMYKGSKSLIRPQQMNDEVWEYLFCDGPYPKSSDIPSAVLSEMKQEFDYWYPLDLRVSGKDLIQNHLTFFIYNHTALMANRNWPRGIRCNGHIMLNSEKMSKSTGNFRTLRQSIEEFSATGTRFCLADAGDGVDDANFAFETANAAILRLTKELTWMEEVLDVESSLRTGPPSTYADKVFENDMNIALRLTERAYKDCLFREALKNGFYDLQAARDEYRLSCGTGGMHHDLLLKFMDVQTRLIVPICPHFADYVWRKVLNKEGCVLTAGWPPSNEPDLVLKSANKYLQDSIVLMRKLLQKQLSGSKKGAKKGAQVTAVPEGKLKGLVYVNEQFDGWRAHCLRILQSRFDQQTCSFPPDTEMLAELSATLLQEGKNLKAIQKVCMPFLKFKKDEAISIGTQALNLRLPFGEIEVLQSNKDLIRRQLGLEEVEIYSASDPDDVSIAGPHASLLTQNPPSPGSPTAIFVTSTSVCPPS
Protein: Alpha-defensin 1 (A6YB85)
Organism: Equus caballus (Horse)
Function: Has broad-spectrum antimicrobial properties. The antimicrobial activity decreases in the present of salt in vitro. Binds anionic phospholipids, which leads to the aggregation of liposomes in vitro. Membrane permeabilization of the target cells is an essential part of the peptide's mode of antimicrobial activity. No hemolytic activity against sheep or horse erythrocytes. Has antibacterial activity against the bacterial horse pathogens Gram-positive R.equi ATCC 33701 P(-) (minimum bactericidal concentration or MBC=5 ug/ml) and R.equi ATCC 33701 P(+) (MBC=5 ug/ml), which are resistant against beta-lactam antibiotics. Also has antibacterial activity against highly infectious wild-type strain R.equi 85F P(+) (MBC=5 ug/ml), S.equi subsp. equi (MBC=5 ug/ml), S.equi subsp. zooepidemicus (MBC=5 ug/ml), S.dysgalactiae subsp. equisimilis (MBC=10 ug/ml), S.choleraesuis subsp. choleraesuis serovar Typhimurium (MBC=10 ug/ml), and P.multocida subsp. multocida (MBC=>10 ug/ml). Probably contributes to the antimicrobial barrier function of the small bowel mucosa (Probable).
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q01523}.
Interaction partners:
- Myeloid cathelicidin 3
Sequence:
MRTLTLLTALLLLALQVQTQSLEETADQVPAQDQPGAEAQDITISFAGDERSAREASKSLIGTASCTCRRAWICRWGERHSGKCIDQKGSTYRLCCRR
Protein: Protein NEOXANTHIN-DEFICIENT 1 (K4DEY3)
Organism: Solanum lycopersicum (Tomato) (Lycopersicon esculentum)
Function: Required for neoxanthin biosynthesis. Probably not involved directly in the enzymatic conversion of violaxanthin to neoxanthin. Is necessary but not sufficient for neoxanthin synthesis. Seems not required for abscisic acid (ABA) biosynthesis in response to drought stress.
Interaction partners:
Sequence:
MEVKDTNCTSLGYGKPPWIFKGSALYQLHLVKAENARAFIPKECKLVEAFGYTLGGFFLASYDDSPAGIFDELVVIAGLVWNPPTSCAWAARVLVGSDEACLHGRKVVGLPSQVARFSKKITALPQKPESKSSSFLRRIGLRTSSNYKNHMDVEVTEIKKQTAMSICNINVNATASQQDSKGWMGPLIKMSLPNFSGRTKYNSDLLKYSCQIECRVRAVQPAKVSGPSESDADKENSSEDQSSNVESVSRVPRGTKRNFSISVMLSKPILALEFNHLKMRVEAPTTVTACSHDTT
Protein: Methyltransferase type 11 domain-containing protein (Q38FT0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 40S ribosomal protein S15, putative
- 40S ribosomal protein S4
- 40S ribosomal protein S25
- 40S ribosomal protein S8
- Ribosomal protein S19, putative
- 40S ribosomal protein S18, putative
- 40S ribosomal protein S16, putative
- Small ribosomal subunit protein uS4
- 40S ribosomal protein S23, putative
- 40S ribosomal protein S24
Sequence:
MLALCKCTAPETRCLVGSVIFTAVVSSAATYAFRDVFDHFLRCRYKFLSWTDGVWVLRKLFGFFGKWFPHWALCRPSEPANVYESDASVRQYMEFHYTLSSESFAQNLRMISESFDYPIRVARKFHEFVPANDGKERRALDLGCAVGASSLEMSKYFSRVVGIDYSVAFIKMARNVVQSALNPNIQPIKYEAPLQGDITVERTACLPDGAVPQRCRFYRGDAMNLLDSDGDDGRGHIVPPVHHGDTNDEDITSWYRVPSGERFDAVLVANLLCRVPNPRKLLDMLPLLLVSGGILVISSPYSWEGSVEERDTWVGGRAEGSTSEILVKEILGANFDLLSETDEAFLIRDHVRRYQLGVAHCTVWRRR
Protein: Cubilin (P90732)
Organism: Caenorhabditis elegans
Interaction partners:
- Double-stranded RNA-specific adenosine deaminase adr-2
- A-to-I RNA editing regulator adr-1
- Protein kinase domain-containing protein
- C-type lectin domain-containing protein
- C-type lectin domain-containing protein 160
- Zinc finger transcription factor pqm-1
- C-type lectin domain-containing protein
Sequence:
MWFHSTLLLAILVAVSADTCPAGFTALSTSKKCVKLITDVAKHSDATANCSSYGGHLISVQNAIDNNAYLQLAAVSVTPYWLGIKCSLSGNPASCQWDDQSGNAGGYNGFAPGYPLVEVGNCVYVPTSGSFAGKWLSGDCNTMSLNFICETAPTSPITDTCSFQYNGNCYYPSLSALPKQDAQFSCQQACGNLVSIHSIEENNYVQSLFTTNAPTYIRIGAVANNQNSNSWIDGTSWNYDNIGYSNINLGMCWSMALSNDIVSTGKWISSYCDTSLPFVCKRKVGTQCGTTSGPTQTPGQCTSPMFMDNSGRFYSPSWPYSYIGEQNPCNYILDTPVGSLVQIRFPVMNLDSQASISIYSRIEDTTPLVVLQGNSASNQWYTSTTNTMKVVFRPCIANCPNDGVNYRWEADFKPSTDVTQPPVTVTPNPNNPSGCNSTILVAPGSISTPNYPNYYPNFLLCMYHLSTTGGYRINLDFGAIDTEQCCDIIEVHDGPLLGSPKLGIVSGTWPAHAKTYQSSSNSMLVTFSTDSSGQGSGFSANFWAL
Protein: Serpin domain-containing protein (A9Z1L1)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSDPKENMALLLQSETDFGLGLLRQQNISESLAFSPLSIALALSLVHVAAKGETRDQIREALVKGSTDEQLEQHFANISAALLAAERGTEVKLANHVFTRAGFKIKQSYLDDVKKLYNAGASSLDFDNKEATAEAINNFVRENTGDHIKKIIGSDSINSDLVAVLTNALYFKADWQNKFKKDSTFKSEFFSSADSKREIDFLHASSVSRDYAENDQFQVLSLPYKDNTFALTIFLPKTRFGLTESLKTLDSATIQHLLSNVSSTSVNVQIPKWKIETKLGLEEALQSLGIKKAFDNDADLGNMADGLYVSKVTHKALIEVDEEGTKAAAATTVSISLKSAMFVMEEPKDFTADHPFFFVLSKDNHPLFVGLHH
Protein: Meiotic drive suppressor wtf25 (U3H0P2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons (By similarity). Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote (By similarity).
Subcellular location: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Wtf element wtf14
- Meiotically up-regulated gene 146 protein
- Putative uncharacterized protein C32H8.15
- Putative uncharacterized protein SPCC794.16.
Sequence:
MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEEGALPPYSDHALVNNPLNTHRENHSYGTTDNSSPLLIILLISFTSIILFNAPAFCYLKYKDAFFKNYGAAEWTLFGFWCLVCTLALIFLTYFYETWSKACGKGIKHFLKNWRNMIFAFCKSSLFCLVLLKAENKLSSHLGDQRWGWKCSASAFTFMAVSSILIFIAETVEPGSCSTDLVKRTLAFYGYEIRQHVNEDATILLREMNPESEA
Protein: Archaetidylinositol phosphate synthase (AIP synthase) (EC 2.7.8.39) (O27726)
Organism: Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Function: Catalyzes the formation of archaetidylinositol phosphate (AIP) from CDP-archaeol (CDP-ArOH or CDP-2,3-bis-(O-phytanyl)-sn-glycerol) and 1L-myo-inositol 1-phosphate (IP or 1D-myo-inositol 3-phosphate). AIP is a precursor of archaetidyl-myo-inositol (AI), an ether-type inositol phospholipid ubiquitously distributed in archaea membranes and essential for glycolipid biosynthesis in archaea.
Subcellular location: Cell membrane {ECO:0000305|PubMed:19740749}; Multi-pass membrane protein {ECO:0000305|PubMed:19740749}.
Interaction partners:
- DUF357 domain-containing protein
- Conserved protein
- Putative archaetidylserine decarboxylase proenzyme
- UPF0111 protein MTH_1689
- Conserved protein
- Conserved protein
- DNA double-strand break repair protein Mre11
Sequence:
MPDINESMLNQFRPVIRRFIDPIADRIALPADYITLTGFLVACAASAGYASGSLITGAALLAASGFIDVLDGAVARRRFRPTAFGGFLDSTLDRLSDGIIIIGITAGGFTGLLTGLLALHSGLMVSYVRARAESLGIECAVGIAERAERIIIILAGSLAGYLIHPWFMDAAIIVLAALGYFTMIQRMIYVWQRLK
Protein: Small ribosomal subunit assembling AARP2 protein (Q8I275)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Periodic tryptophan protein 2, putative
- U3 small nucleolar RNA-associated protein 4, putative
- U3 small nucleolar RNA-associated protein 12, putative
- U3 small nucleolar ribonucleoprotein protein MPP10, putative
- U3 small nucleolar RNA-associated protein 20 C-terminal domain-containing protein
- U3 small nucleolar RNA-associated protein 13, putative
- Nucleolar protein 56
- KRR1 small subunit processome component
- WD repeat-containing protein, putative
- rRNA biogenesis protein RRP5, putative
Sequence:
MDDKKKHHKKKKVGKKSKKKKINKNGNNKKYHKAFAFSGGIKSAHRRKQHLFELEEKKLRVQKVYKEGNKSSPLIVVIQGAKGVGKSTLLKSLIKYYVGITINNIKGPISIFTKNLKRYTFIEVNDDILHMIDVAKIADICILVIDGSYGIELETLEFLNILYTHGLPKVLGVVTHLDKFKDSKSIRKRKKKLNKRYSEELVEGSKLFFLSGIQNNRYNKTEIRNLCKFLSVIKKPIISWREQHGYILGLKLDVDDLLINNQITSQKNNLQSEHVHNENYVNHASYDNDNDNDEENEKKLTNFLTNCDEKIKISIEGYVYGSKIYKNQKVHIPNIGDVEIDNIQILQEPFKLDEQKKNPNIYAPMSDVGNLTFDFDNMYIHIPKNKVNFTREEFLLADQREETIPGDHSGEKNGNTLKDDEGGGDGDDDDDDVGDDNVDDGDDDDDDVGDDNVDDDDGNDDDDDDNDDDDNDDDDNDDDDNDDDDDDDNENSDKSSHHNKQSNDNEKYITDSIKMIRELQKSNGVFSKQQKDNLILFNETNDNNGASNIRRKAPSNVYISEKQKKKKQQDSYVNEKAEEYNKLESILYEKKNNDEEYYCANNVTISSDDDKEENDASFREFYRKYGLNADMSDDGGNNDINIYNGQESEEKLKDTYDKLIDGGHDEDDYDDDENVGDENDDDEENDDDENDDDEENDDDENDDDEENDDDDDENDDDDENDDDDENDDDDENVGDDDENDDDDENVGDENIDDDDDDDYNNYNNKELKHKNTLDPNKSTVNRMEAHDIADILSFDNKISLDTFIYDFSYINRKNNLLYFRGDVINVIKREERKLDESCHLQEYEEHFYFIKNMLSTDIVEDKKRGCYSFMNEDNYYYDKLDTFRSDEEDIFIFNNLSISLYDIVDSNIVDNFFSRYDKVYRMFFKNRKRGNMGINSEGDDNNNNNSDDDNNINSDDNNSNSDDNNSNSDDNNSNSDDNNSNSDDNNINSDDNNINSGDDNNLKDKDKGNIGNEINIKENLKKLKEEKLIEKEKFRETEKIGVLNSGYGSSVNIGEYVRIELNIEKKKLAILKNNLIICGGIQTYEEKDSLIHCRIKKHRWFPKLLRSNDPLIFSVGWRRYQSIPIYSISERNNVRLRYLKYTTEHMHCNCTFYGPLASVNSGILALYNYKKVPFYRICINGLIIETNNNLNIMKKLKLIGEPYKIFKNTAFVKNMFNSDLEVCKFLNCPVVTPSGIKGLIKNKINNNGDFRCTFADKIRMSDIVILKLYVNVKIKKFYYFDIENKIKSINELRYLYNIYVNHNNNYRSIPFRHFYHTKIQIKSKLLKDLPFKSKPKLFKKLQNHANLNNKQLTNNINNKKTKTDQINFNALPNPKLAAKWYQMLHTIKKNILDQKKAKSQLSYHKKLKEKLKIQQAKTQVVKQRKKISYKKGRK
Protein: Aureochrome1 (A8QW55)
Organism: Vaucheria frigida (Yellow-green alga) (Conferva frigida)
Interaction partners:
Sequence:
MNGLTPPLMFCSRSDDPSSTSNINLDDVFADVFFNSNGELLDIDEIDDFGDNTCPKSSMSVDDDASSQVFQGHLFGNALSSIALSDSGDLSTGIYESQGNASRGKSLRTKSSGSISSELTEAQKVERRERNREHAKRSRVRKKFLLESLQQSVNELNHENNCLKESIREHLGPRGDSLIAQCSPEADTLLTDNPSKANRILEDPDYSLVKALQMAQQNFVITDASLPDNPIVYASRGFLTLTGYSLDQILGRNCRFLQGPETDPRAVDKIRNAITKGVDTSVCLLNYRQDGTTFWNLFFVAGLRDSKGNIVNYVGVQSKVSEDYAKLLVNEQNIEYKGVRTSNMLRRK
Protein: D-arabinose 1-dehydrogenase (EC 1.1.1.116) (NAD(+)-specific D-arabinose dehydrogenase) (Q04212)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- D-arabinose dehydrogenase [NAD
Sequence:
MVNEKVNPFDLASVSPLVLGGAILNQQYTDEPESIPLEDIIKYAFSHGINAIDTSPYYGPSEVLYGRALSNLRNEFPRDTYFICTKVGRIGAEEFNYSRDFVRFSVHRSCERLHTTYLDLVYLHDVEFVKFPDILEALKELRTLKNKGVIKNFGISGYPIDFITWLAEYCSTEESDIGSLDAVLSYCNLNLQNNKLLNFRERLLRNAKLKMVCNASILSMSLLRSQETRQFHPCSHELRECASQAAKYCQEQNVDLADLATRYAISEWVGKGPVVLGVSSMEELKLALDNYEIVKSNGNRLSSKDGQLVEYIQKNIFKEHFNEEWSSGIPHPEMI
Protein: Nipsnap homolog 3A (B1AWZ3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MLALRGSLRRLSQALVHQVEVCSPFTTGHRQQEGTFYEFCTYYLKPASVEEFLYNFKKNVHLRTAHSELVGYWTVGFGGRINTVFHIWKYDNFAHRAAVYKALAKDEDWQEQFLIPNLPLIDKQESEITYLVPWCKIGKPPKEGVYELATFLMKPGGPALWGEAFQRAVNAHADQGYIKLIGVFHAEYGLLNRVHVLWWCENADARAAGRRQAHEDPRVVSAVRESVNYLDVQQNMFLIPWSFSPLK
Protein: 1,8-cineol synthase, chloroplastic (EC 4.2.3.108) ((E)-beta-ocimene synthase) (EC 4.2.3.106) (Alpha-pinene synthase) (EC 4.2.3.-) (Alpha-terpineol synthase) (EC 4.2.3.111) (Beta-myrcene synthase) (EC 4.2.3.15) (Limonene synthase) (EC 4.2.3.-) (Sabinene synthase) (EC 4.2.3.-) (A5Y5L5)
Organism: Nicotiana suaveolens (Australian tobacco)
Function: Monoterpene synthase involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into 1,8-cineole and, as minor products, limonene, sabinene, (E)-beta-ocimene, beta-myrcene, alpha-pinene and alpha-terpineol.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MNHHLIITPIFHLQIMLPVATLKRPPPPAATCSIYSFSRGTPSLVSKARLSTAAVGGMKNEPSPNHYSDISSSDLNLTRRSGNYGPTMWDFEYIQSIHNDYTEKKYMNRLNKLKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLFREYGFHISQEIFGGLSETHTEDTKGMLYLYEASFLATEGESELEKARNWTEKHLREYLENKNDDQNVAELVHHALELPLHWRMLRIEARWFINFYKKKQDMIPLLLELAILDFNIVQAAHIEDLKYVARWWKETCLAENLPFARDRLVENFFWTIGVNFLPQYGYFRRIETKVNALVTTIDDVYDVFGTMDELQCFTHAFQRWNIDELDNLPDNMKMCYFALDNFINEVAGDAFEEHRVPILSYLRNAWTDLCKAYLREAKWYFSKYIPTMEEYMDNAWISISAPVILVHAYFLVANPVNKEVLHYLENYHDIIRWSALILRLANDLGTSSEELKRGDVPKSIQCYMNEKKVSEEEARQHIRLLISETWKKLNEAHNVAAHPFPKMFVKCAMNLARMAQCMYQHGDGHGHGDLNSETTNHIMALLFESIPPA
Protein: Methylesterase 10 (AtMES10) (EC 3.1.1.-) (Q8S9K8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Methylesterase shown to have methyl jasmonate (MeJA) esterase activity in vitro.
Interaction partners:
- Cytochrome P450 89A9
- Isoprenylcysteine alpha-carbonyl methylesterase ICME
- Leucine-rich repeat
- S-formylglutathione hydrolase
- Probable nucleoside diphosphate kinase 5
Sequence:
MTYQKQYQMQTHHMQQQQLHHFVFVHGSCHGAWCWFKLAAKLKLDGHRVTAIDLGGSGVDTRQLHEVRLVSAYLEPLMSFMESLPENEKVVLVGHSYGGIGTSLAMERFPTKVSVGIFLSAYMPHHDSPPAVLIQEYFTRLPEGFAMDCEFTFEEGLEHPPSSVLFGTSFLKEKAYSNCQLEDLELAMALMKPSWLYTKEMGGEDLITKERYGSGKRVFIVCEGDNVVPEEIQKWMISNYEPHEVKRIEEAGHMAMLTKPHELSQLLQEIAAKYN
Protein: Uncharacterized protein (Q38C76)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MFRQELRRCSVILFHGGLVPRRMIINEDPQERSRELALREKVAKKYKGLSISEFSGFSYGHFAMGGLATSAAFRAREASQGNAPNFGNLSQGERRVDWLMFFTGVVLVFVSSKIIIQRLFGGVSEDLALPLWIGSVDEQATYLLFTIQYDKSSRQRIKDEYLAERRINPFITFFPWLITRYPEYGRGVQFSRDVAFGTLREILSSGNQRSLLNLAGSTKDTLLRNDSPAHRVDYFLRRVGVVPMIQGVNSDSKAAAYVPPAVASNLQLMYGSEPEAIKTVLSVSPDERHGSVPFQ
Protein: Uncharacterized membrane protein YPR071W (Q12346)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Uncharacterized TLC domain-containing protein YPR114W
Sequence:
MQNGTEDKSNIPARSNDDVLPPLAVRLTMKVMRLIFIGKMFAYSFVPFPPFKLLTFDNTVGWFVAYSAIVSIWGFAVWMERGYRHKINLLPPRCTKIRCSRCNTRIRSPNWFKYKNWLYFFLLYVSLTTSNLIIQLASFMTEMSRRGISVPGTKDPGKRDYLGLIIPMRFIGAFIHYMTANLFKEYYLHNGPLEKNDRPSTDEKTSENETL
Protein: Accessory gland peptide Acp33A (O46227)
Organism: Drosophila melanogaster (Fruit fly)
Function: Responsible for physiological and behavioral changes in mated female flies.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Accessory gland protein Acp53Ea
- Accessory gland protein Acp76A
- Accessory gland protein Acp32CD
- Proteasome subunit beta
- Accessory gland protein Acp63F
- Accessory gland-specific peptide 95EF
- Accessory gland protein 98AB
- glutaminyl-peptide cyclotransferase
- Accessory gland protein Acp62F
- Accessory gland protein Acp29AB
Sequence:
MLPSKRVPFLFTIILFLAGLGQHTTESVLPDCVLYPRCLITKDPCCM
Protein: Glycine cleavage system H protein 2, mitochondrial (O82179)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The glycine decarboxylase (GDC) or glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).
Subcellular location: Mitochondrion {ECO:0000255}.
Interaction partners:
- Glycine dehydrogenase
- Glycine dehydrogenase
- Aminomethyltransferase, mitochondrial
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Serine--glyoxylate aminotransferase
- Putative transferase At1g60990, chloroplastic
- Serine hydroxymethyltransferase 4
Sequence:
MACRLFWASRVASHLRISVAQRGFSSVVLKDLKYADSHEWVKIDGNKATFGITDHAQDHLGDVVYVELPDVGHSVSQGKSFGAVESVKATSDINSPVSGKVVEVNEELTESPGLVNSSPYEQGWIIKVELSDAGEAEKLMDSDKYSKFCEEEDAKH
Protein: Glutathione S-transferase U13 (AtGSTU13) (EC 2.5.1.18) (GST class-tau member 13) (Glutathione S-transferase 12) (Q9FUS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: In vitro, possesses glutathione S-transferase activity toward 1-chloro-2,4-dinitrobenzene (CDNB) and benzyl isothiocyanate (BITC). May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase DHAR2
- Glutathione S-transferase F10
- Glutathione S-transferase F11
- Glutathione S-transferase F9
- Glutathione synthetase, chloroplastic
- Defensin-like protein 192
- Glutathione S-transferase F7
- Glutathione S-transferase DHAR1, mitochondrial
- Glutathione S-transferase F8, chloroplastic
- Glutathione S-transferase DHAR3, chloroplastic
Sequence:
MAQNDTVKLIGSWSSPYSLRARVALHLKSVKYEYLDEPDVLKEKSELLLKSNPIHKKVPVLLHGDLSISESLNVVQYVDEAWPSVPSILPSDAYDRASARFWAQYIDDKCFAAVDAVVGAKDDEGKMAAVGKLMECLAILEETFQKSSKGLGFFGGETIGYLDIACSALLGPISVIEAFSGVKFLRQETTPGLIKWAERFRAHEAVKPYMPTVEEVVAFAKQKFNVQ