wanglab/gogpt-training-data huggingface dataset:
Protein: Neural cell adhesion molecule L1-like protein (Cell adhesion molecule with homology to L1CAM) (Chl1-like protein) (Close homolog of L1) [Cleaved into: Processed neural cell adhesion molecule L1-like protein] (P70232)
Organism: Mus musculus (Mouse)
Function: Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neurons as well as in regulation of both the number of interneurons and the efficacy of GABAergic synapses. May play a role in regulating cell migration in nerve regeneration and cortical development. Potentiates integrin-dependent cell migration towards extracellular matrix proteins. Recruits ANK3 to the plasma membrane.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Note=Soluble forms produced by cleavage/shedding also exist.; SUBCELLULAR LOCATION: [Processed neural cell adhesion molecule L1-like protein]: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Contactin-6
- Neuropilin-1
- Stress-induced-phosphoprotein 1
- Contactin-associated protein-like 4
- Receptor-type tyrosine-protein phosphatase alpha
Sequence:
MMELPLCGRGLILSLIFLLLKLSAAEIPLSVQQVPTIVKQSYVQVAFPFDEYFQIECEAKGNPEPIFSWTKDDKPFDLSDPRIIAANNSGTFKIPNEGHISHFQGKYRCFASNRLGTAVSEEIEFIVPGVPKFPKEKIEPIDVEEGDSIVLPCNPPKGLPPLHIYWMNIELEHIEQDERVYMSQRGDLYFANVEENDSRNDYCCFAAFPKLRTIVQKMPMKLTVNSSNSIKQRKPKLLLPPAQMGSLSAKTVLKGDTLLLECFAEGLPTPHIQWSKPGSELPEGRATIEVHEKTLKIENISYQDRGNYRCTANNLLGKASHDFHVTVEEPPRWKKKPQSAVYSTGSSGILLCEAEGEPQPTIKWRLNGLPIEKHPFPGDFMFPREISFTNLLPNHTGVYQCEASNIHGTILANANIDVIDVIPLIKTKNEENYATVVGYSAFLHCEYFASPKATVVWEVADETHPLEGDRYHTHENGTLEIYRTTEEDAGSYSCWVDNAMGKAVITANLDIRNATKLRVSPKNPRIPKSHVLELYCESQCDSHLKHSLKLSWSKDGEAFEMNGTEDGRIVIDGAYLTISNITAEDQGVYSCSAQTSLDSTSEKTQVTVLGVPDPPGNLHLSERQNRSVRLSWEAGDDHNSKISEYIVEFEGNREEPGKWEELTRVQGEETDVVLSLAPYVRYQFRVTAVNEVGRSHASLPSDHHETPPAAPDKNPQNIRVQASQPKEMIIKWEPLKSMEQNGPGLEYKVSWKPQGAPEEWEEEIVTNHTLRVMTPTVYAPYDVKVQAINQLGSSPDPQPVTLYSGEDYPSTAPVIQRVDVMNSTLVKVTWSSIPKETVHGLLRGYQINWWKTKSLLDGRTHPKEVNILRFSGQRNSGMVPSLDPFSEFHLTVLAYNSKGAGPESEPYIFQTPEGVPEQPSFLKVIKVDKDTATLSWGLPKKLNGNLTGYLLQYQIINDTYELGELNEINVTTPSKSSWHLSNLNSTTKYKFYLRACTSRGCGKPISEEGATLGEGSKGIRKITEGVNVTQKIHPVEVLVPGAEHIVHLMTKNWGDNDSIFQDVIETRGREYAGLYDDISTQGWFIGLMCAIALLTLILLTICFVKRNRGGKYSVKEKEDLHPDPEVQSAKDETFGEYSDSDEKPLKGSLRSLNRNMQPTESADSLVEYGEGDQSIFNEDGSFIGAYTGAKEKGSVESNGSSTATFPLRA
Protein: Discs large 5, isoform A (Discs large 5, isoform B) (LD32687p) (Q9VKG8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Peripheral plasma membrane protein CASK
- LD33695p
- non-specific serine/threonine protein kinase
- DNA-directed RNA polymerases I, II, and III subunit RPABC2
- Calcium/calmodulin-dependent protein kinase type II alpha chain
- LD29223p
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MAKMASGDLSLTSTSSQEEESSEYVGYDNTLRPPSNSSGSTTAANMSNNNGPSKGVSSGVGVSGISGGNGANYDILQAQYKSALLELNTLRHQHANTKRRCDELATELTLYQEHYVADRNKFTDMVEESARFKRLLLETQNQQSQQAQNGNSQVPPVGSGNPYYFGKTQGCDGSCSEKLAELKKERNMVAVEREKYKKSYIELEKDRNYYRERGDENQKLKVLLSQESKNVLSLTEELNQLLSEKDNVLQEHQKMSDDLVLANKEIERLKKDEQLARAEIKVLQLANADLKKRDLLKSRDSSWSKEFPSGKELENSKELEKLRKSLEKALSEVERSSQDAEEAKRVRDWAISQREKIVQERDSVKTLCDKMRHERDKAISDSLMAIRDSEKIKKQKDEAQKKIDLLKEQMEQQERQNLDSNASGSRRSFRPSSYEGEDLLEVELSGYEHTSDLGIILDDSNKRKLVCGVTSSSPACGKLKINDVICKVNNLDCQSLSKRMVLDEIRACAPRSLLLVSRTRHSKRHAYSVQLKTRDRDCPHGLQLDMGVFIAKIEQNSLAFYEPELDVGDRVLSINNKSMDSVQSIEEVMQLMNDPRSDGLNLFALKYVQDQLPPGMTTSSAQTDSIDSMQHVSSAGGGGGSGPSSATKHPSRFAEFFFRKLKFSKPGTPEDNFEQEHDDAIAALDSVLSENSSEKSKENLFNRKKRTKKEKEASKSMGTWPRTNISHENPTGTMRGNEKKRALMSLFTAGPINVDKDDELMGEVGVPEKQPAALIQDQLPPPLPPQMSKPLAHIRGSNGGAIKTHPNRNSNPVSSGVSALFPPGPPNGMPNTSYPTHPRHSLYGVTAEEINQKPIQRAPLMGANARVKMPSQERYGTRPHSNHRLSLNITPSGDFYQPKTSGQQAQQQVMNASSTSAGFGVGSGSMVGGTGPAAGEFPVRKQQVYDVFHPPPLPKNSSGSNMFMPLHPTRGSHPPPVGQPPDVVSLKSQNSIESILSAKSPAISEYGMYAKRHVPQAVRHVPKYPSDSESIGSGVHGGYGGFLQSNHMPGNRHTQLFPTFGPGGRGNRRSSPLTLPSPPPQQQLQQLPAATAPHDSVGIPTDLDYHPHHHTQTNAMPHPHPHPHAPYLDYGHGLGIGPYMGVGGGVSGVGGAIYEGGTFPRKKDNQRLRIPSNPSVASKSSSMVKNSSGSIDHHYVTSTGPVSGGSMSASSSDRAPMSLMSSSIHNSYGANIAGGNGTGSSIGVGGGGGGGSGRGSPMPQVHVEVLSHGGGGSGKRNSNVPADFLCPGDLRRVTIDKRDKSLGITIQCNNNGGGIFVSTVADKSTAMRAGLQVGDQLLEVCGINMRAATQEIAANVLRQCGDSFTMLVQYNPEKFPSIEYEGAHNLEPESPINHSGSPTPRNSPRPPARNSLFPLPMQPQAPSTRPGSRAPLSHQSIKDQSFTDSLENQSDISSSQDMPSSAATTTTTTASATSTVYDEEPKPSLPPPPASVPAETLRYVTLHMDKSKNLGIKLFGGNKVGIYVHDVAVGSPSDHAGIRKGDQILEYNGVDLSGVTAEQAANEISKLTDTVTMLVQNKLHTLKQIKDEPGDSFYIRVGFDRTGELNEDDLRFVKDEVLYVDNTVFNGTFGLWRAWKLDAMGHRKECGIIPSQMKVEEELRSGEVVDCDTGTARRGSTSARRSFFRRKKNQRSSSRDSTEIASFSNTQLSFFPDLGLLNDDGGALSYQRVELLDSPIRRPVLIIGPLSECLMVRLTIDFSNLFKLCEVTAMDCSQEAMEEGLKENIFVDYRRRGNKFECTTVEAISNACKNDRRHCILDVSISAVERLQRLQIYPIVLLLRFKSAKQIRDIRDFGTDKISAKAAKEMYERAMKLETDYKQYISAVIPGVSIKHMCTQIKDAVDKEQDKLLWVPVSSG
Protein: Beta,beta-carotene 15,15'-dioxygenase (EC 1.13.11.63) (Beta-carotene dioxygenase 1) (Beta-carotene oxygenase 1) (Q91XT5)
Organism: Rattus norvegicus (Rat)
Function: Symmetrically cleaves beta-carotene into two molecules of retinal using a dioxygenase mechanism.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9I993}.
Interaction partners:
- Retinaldehyde dehydrogenase 3
- Retinol dehydrogenase 10
- NADP-retinol dehydrogenase
- Aldehyde dehydrogenase 1A1
- Dehydrogenase/reductase
- Retinal dehydrogenase 2
- Aldehyde oxidase 4
- Retinol dehydrogenase 16
- Dehydrogenase/reductase SDR family member 4
- Dehydrogenase/reductase SDR family member 9
Sequence:
MEIIFGRNKKEQLEPLRATVTGSIPAWLQGTLLRNGPGMHTVGDSKYNHWFDGLALLHSFSIRDGEVFYRSKYLQSDTYNANIEANRIVVSEFGTMAYPDPCKNIFSKAFSYLSHTIPDFTDNCLINIMKCGEDFYATTETNYIRKIDPQTLETLEKVDYRKYVAVNLATSHPHYDEAGNVLNMGTSIADKGGTKYVMFKIPATAPGSKKKGKNPLKHSEVFCSIPSRSLLSPSYYHSFGVTENYVVFLEQPFKLDILKMATAYMRGVSWASCMTFCKEDKTYIHIIDQKTRKPVPTKFYTDPMVVFHHVNAYEEDGCVLFDVIAYEDNSLYQLFYLANLNKDFEEKSRLTSVPTLRRFAVPLHVDKDAEVGSNLVKVSSTTATALKEKDDHVYCQPEVLYEGLELPRINYAHNGKPYRYIFAAEVQWSPVPTKILKYDVLTKSSLKWSEESCWPAEPLFVPTPGAKDEDDGVILSAIISTDPQKLPFLLILDAKSFTELARASVDVDMHLDLHGLFIPDAGWNAVKQTPAKTQEDENSDHPTGLTAPGLGHGENDFTAGHGGKSL
Protein: Probable G-protein coupled receptor 132 (Si:dkey-165a24.9) (E7F793)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MKHLKILKFKCHGSVTSIKTMLLNLTNGSCQIPLANDRVGLTYIYSLAFSIGLPANLLSLWGLYQLGRSGGGGCQLVYILNLLLSDLLQLLTLPLWILYLQGDHHWPYGSVTCQLVGYVFYVNLYASVIFLCLIALDRCLAIVYPLSSRGVRKVRVAAFSGVVVWTLIFLFCLTGLYPSVFEPQRELCLEQYPVSSRYAYFKIATVALGFLMPCSILGYTSARIGRTLRNSPSVADHERRRIVATLVVITVIFIVIFGPYHLVVGYRFVTLLLTESGKEQCSVEVSLYLYYRICYGLTSLNTLLDPLFYIFLCNDARQELRRSLLCPCRGHRVHRSSRVQTYPKGRLSLSADV
Protein: Filament-like plant protein 2 (AtFPP2) (Protein VESICLE TETHERING 2) (Q9SFF4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Ensures, when in complex with FPP3/VETH1 and COG2, the correct secondary cell wall (SCW) deposition pattern by recruiting exocyst components to cortical microtubules in xylem cells during secondary cell wall deposition by recruiting EXO70A1.
Subcellular location: Vesicle {ECO:0000269|PubMed:25541219}. Note=Present in vesicle-like small compartments which exhibit microtubule plus-end-directed and end-tracking dynamics. {ECO:0000269|PubMed:25541219}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At1g03540
- Conserved oligomeric Golgi complex subunit 2
- Cytochrome b561 and DOMON domain-containing protein At4g12980
- Microtubule-associated protein RP/EB family member 1C
- Interactor of constitutive active ROPs 1
- Cytochrome b561 and DOMON domain-containing protein At5g35735
- 65-kDa microtubule-associated protein 4
- Kinesin-like protein KIN-5A
- At5g64850
- Kinesin-like protein KIN-12A
Sequence:
MMTGTTLILEPVMDSKDELVKQHAKVAEDAVAGWEKAENEVVELKQKLEDAADKNIVLEDRVSHLDGALKECVRQLRQFRDEQEKNIQAAVTESTKELHSANTGLEKRVLELQKEAEAAKSENMMLRREFLTQREDLEIVMIERDLSTQAAETASKQHLDIIKKLAKLEAECRKLRILAKTSSSLSSNQSVDSHSDGGRERVEGSCSDSWASSAFISELDQIKNEKGGNRSLQGTTSSTEIDLMDDFLEMERLVALPTETQAKNSKDGYELSLMEKLEKIQAEKDDLEREVKCCREAEKRLSLEIEAVVGDKMELEDMLKRVEAEKAELKTSFDVLKDKYQESRVCFQEVDTKLEKLQAEKDELDSEVICCKEAEKRFSLELEAVVGDKIEMEDELEKMEAEKAELKISFDVIKDQYQESRVCFQEVEMKLEAMKRELKLANESKTQAESRVTRMEAEVRKERIVSDGLKEKCETFEEELRREIEEKTMIKREKVEPKIKQEDIATAAGKFADCQKTIASLGKQLQSLATLEEFLIDTASIPGSARSVHNKEALLGKDPHECIKTINGRSLEFLAIQNSNNKTSPPCSSSSDSTTVSLIMSSNRGSSEKNRNGFATVFTRSRNSVNLGI
Protein: Sushi domain-containing protein 3 (Q96L08)
Organism: Homo sapiens (Human)
Function: May play a role in breast tumorigenesis by promoting estrogen-dependent cell proliferation, cell-cell interactions and migration.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24413080}; Single-pass membrane protein {ECO:0000305}. Note=Prominently localized to cell-cell borders. {ECO:0000269|PubMed:24413080}.
Interaction partners:
Sequence:
MRWAAATLRGKARPRGRAGVTTPAPGNRTGTCAKLRLPPQATFQVLRGNGASVGTVLMFRCPSNHQMVGSGLLTCTWKGSIAEWSSGSPVCKLVPPHETFGFKVAVIASIVSCAIILLMSMAFLTCCLLKCVKKSKRRRSNRSAQLWSQLKDEDLETVQAAYLGLKHFNKPVSGPSQAHDNHSFTTDHGESTSKLASVTRSVDKDPGIPRALSLSGSSSSPQAQVMVHMANPRQPLPASGLATGMPQQPAAYALG
Protein: Protein qui-1 (Quinine non-avoider protein 1) (O62471)
Organism: Caenorhabditis elegans
Function: Involved in the avoidance response to the noxious chemicals and repellents such as quinine in ASH and ADL sensory neurons. In response to the noxious chemical quinine, promotes dauer formation induced by pheromones such as the ascaroside ascr#3 in ASH nociceptive neurons.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:14988722, ECO:0000269|PubMed:26976437}. Perikaryon {ECO:0000269|PubMed:14988722}. Nucleus {ECO:0000269|PubMed:14988722}. Cell projection, dendrite {ECO:0000269|PubMed:14988722}. Cell projection, axon {ECO:0000269|PubMed:14988722}.
Interaction partners:
- Serpentine Receptor, class H
- Inactive tau-tubulin kinase ttbk-6
- TPR_REGION domain-containing protein
- Helicase SKI2W
Sequence:
MFRGKGQQQVSSTDNIKAMMTAAIGNKLEKRLPLVSTIFVVGNDEEEFNIERRTLWQDVLPDLQNLAFQSNFDLEFCDVPLENGELTNSVAEHVLQMWKDNPRSWIVLLLGNRYGNVSVPTSLRKEEYESIRSSIFEENGNVRVFEKAYTINRNGAVEEYRLVPSAIKDKKQLAEIIKALQAGAKAAHEEGSINQVHEQRQNRFFSSPLETFVRSILQVSPCRCLFLLRKFDQLVADPNSPNAFLETNDQNSRKIEDLKNEITLKMNDRVMTHVLRPESTDINYFFNSRDGDKYREKIARQFNEKLKNHLADINPPVRPEPPKSPMVLAANEARTHQEFLENQLALGNLKRDYDKRLDELASVKVNRGVFLIQGTDLCGKTQALCRLYHKISDKDAYKVIFFTNLTYSSNFAHEAWRTICLNICSISNIDPKEVLEHFKLGGILKSLEELVQKADKPVCIFIDDVHLLKFGHLLSQIGRRTETAPDNLSLFMTSSNVAPVNAVFAVTQTVNVDVISENEVVGMVQKMAEKVDKKLTNEQISAIRPLMAAKDGILIAKSFTHEILFNGNSSMKGGMDGRMTRIEKEFGKLAVGNAVKFIAASSHGLTRLEIHDAISADREVLEEMNMSIVYSLLTLDGIIEALGPILRKVIIDDRQIIGIAHSGLISWLRNRYLTSSQDIRSAHLQLSDLFADLLIDNEQSPRHEIAYQSFSQGIKRDNGSPNFRRLRLLWYHCLHSGNLDRLKELSLCHFEYVDYVTRYFGISHLLSLYEECATQILHHDLQVISEQVLVPALVTMARDSEQLAAEVIGRLRFTRHENSHFLNSLVDQAMSWVDLYNRQPLLVPLTCWISPPATKVCRSFTLKDWKPGNTVLTLSANHQYILISGNQSDPGVIYAYHIASEQLIGTFKGHTAAVTCLCSSNDSSLFVSTSFDKTVNVWVFSQSTPTMSLTHHTAKVTCAILTSDDQYLITASADSSAKMIKLETGEVMRSFNDHTGSVVSLQLTSNNQFLITGSGDFVVQMWDVTNGKCISRMGGLMAPVSTLAITSNDAFVVVACEDETLKVFSTVGGQELHELMGHEGKVNSLVCAQDDCQLFAATKSKVFCYDIHNGQMIDVLDTAQPFPICSLKISSDNYFLISPCGPKVTIWNVTKRNHDAHDVHADKEGFLTAVALSNDDKYAACGTNNGIVALWDLEVCQCVFTTIQNKGDPITCIRYSVDSQYCISGNQAGCILILDAQNGGVVRELFMHSSEVLSIMSLVHNKMISCDIQGKMVIWELFGDDDTPEMVATGVKPPIFVPPTGRIMVGHCSLSNKEMKIWAFPEEGPPVTRAKLSHSDEITCFATSPKGGNFIATGSRDMSLKIWQIDKGFLTQVLVGHENVVTCCCISFDERLVVSGARDEKIIVWNVQSGDMVCTVNTTAAITSLSMTGDSTVVFSTTEDGWVETWSTTKGRLLSTFNAHRPIKKLINSYESHRMLLLLENCAQLPILCLHNTPAVGVEATRRRSARAQSVSSASNEPVASTSAGEIKKDPILSSNNGGNAQSAPRATAPKPTFDMLERSKSRTSLIEKDRTTTLTQSNAPPPQKSNMCTLL
Protein: Trace amine-associated receptor 12i (Q5QNN0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MTSNETDVYAENMFLCFPHLPNSCPKSQRFVVVKLAMYVCLLLMILTTVFGNLLIIISISHFKHLQSPTHLIVRSLAASDCLLGSLVMPYSMVRSVEGCWYLGDVVCKVHSSLDMTFCISSLLHLGLVSIDRYWAICDPLRYRIRVTNTTVTLYTIFIWLFSFLYSFVIVFSGVNRIGLETFIMQVYCVGSCVLFFNKEWGLICPVLTFFIPGAIMSSLYMKIFHVARKHAKVMSERVTGGLKSQSSAQRERKAAKTLAIVMGVFLLCWTPIFIASIIDSFLNFVTPAGVFDALIWFGYFNSTCNPLIYGFFYSCFQKAFKILLSSLFLGFGNSSTLTFE
Protein: 2-methylisoborneol synthase (2-MIB synthase) (EC 4.2.3.118) (Q9F1Y6)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Catalyzes the cyclization of 2-methylgeranyl diphosphate (2-MeGPP) to 2-methylisoborneol (2-MIB), which likely involves the intermediacy of 2-methyllinalyl diphosphate. Is also able to catalyze the cyclization of geranyl diphosphate (GPP), albeit with much lower efficiency, leading to the formation of a complex mixture of cyclic monoterpenes, consisting of alpha-pinene (6%), beta-pinene (23%), limonene (32%), gamma-terpinene (29%), and delta-terpinene (10%).
Interaction partners:
- Geranyl diphosphate 2-C-methyltransferase
- Germacradienol/geosmin synthase
- Nucleotide-binding protein
- Small ribosomal subunit protein uS10
- Isopentenyl-diphosphate Delta-isomerase
- Secreted metal-binding protein
Sequence:
MPDSGTLGTPPPEQGPTPPTTLPDVPAPVIPSASVTSAASDFLAALHPPVTVPDPAPPPPPAPAAGNPPDTVTGDSVLQRILRGPTGPGTTSLAPAVRYGRQPGPEAPASAPPAAGRAVPGLYHHPVPEPDPVRVEEVSRRIKRWAEDEVQLYPEEWEGQFDGFSVGRYMVGCHPDAPTVDHLMLATRLMVAENAVDDCYCEDHGGSPVGLGGRLLLAHTAIDHFHSTAEYTPTWQASLAADAPRRAYDSAMGYFVRAATPSQSDRYRHDMARLHLGYLAEGAWAQTGHVPEVWEYLAMRQFNNFRPCPTITDTVGGYELPADLHARPDMQRVIALAGNATTIVNDLYSYTKELNSPGRHLNLPVVIAEREQLCERDAYLKAVEVHNELQHSFEAAAADLAEACPLPPVLRFLRGVAAWVDGNHDWHRTNTYRYSLPDFW
Protein: Helix-loop-helix protein 6 (Q10007)
Organism: Caenorhabditis elegans
Function: Transcription factor that regulates the development of the g2 pharyngeal gland cells and pharyngeal gland function and thereby is required for feeding. Required for the expression of a number of genes in the pharyngeal gland, possibly by binding to the E box motif (5'-CANNTG-3') in the promoter region of these genes. Positively regulates the expression of genes encoding mucin-like proteins, which lubricate the pharyngeal tract to ensure efficient passage of the bacterial food source. Exhibits pharyngeal gland-specific positive autoregulation activity.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- ShKT domain-containing protein
- EB domain-containing protein
- ShKT domain-containing protein
- Flo11 domain-containing protein
- Helix-loop-helix protein hlh-2
- Defective pharyngeal development protein 4
- BTB domain-containing protein
- Homeobox protein ceh-22
- Zinc finger protein ztf-2
Sequence:
MSISQNNFLTMFPVTYTFENGVYSTIINQNTIQTPIPNPIQHHIQNHIQTSIPNTNLLLENVQTDVQKLMVPLIDQQFHIPTSTPLQLAPIPTQIQSQLQPQISQIPIHNQPQIQIQSQVQPQLPTQSQPKPSSKASLDTSSNAFKKYVNPFAPEATVPLPVELEDQYGPYSSSVWKRNERERCRVRNVNDGYERLRKHLPVHFDEKRISKVDTLRLAIRYIKHLDNLLRSELHQYNCKCFNGFQEESEGNILIDISTFNFNSSNNAM
Protein: 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha (OFOR1) (EC 1.2.7.11) (Q9YA13)
Organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Function: Catalyzes the coenzyme A-dependent oxidative decarboxylation of different 2-oxoacids such as pyruvate, 2-oxobutyrate and glyoxylate to form their CoA derivatives.
Interaction partners:
- 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta
- 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta
- Succinate--CoA ligase subunit beta
- Succinate--CoA ligase subunit alpha
- 2-oxoacid oxidoreductase
- Citrate synthase
- isocitrate dehydrogenase
- 2-oxoacid oxidoreductase
- Pyruvate dehydrogenase complex, E2 component
- Pyruvate kinase
Sequence:
MRKDVVLLVGGAQGSGLETTMQVLAPAYASLGYGVLANREYFSNIVGRHSYIHIRVSSSGEARPLYYPADFLGAMDAETVFTHWDDIGEGAFLLYDLGTARMRLQQIASMEPDLRSRLMQQYREAGIEPFTVEKVVEYLEREKRVRVIGLSFTALFDVLIKKHGLSRAQAQRFRSSILIGAIAGLTSLDREALDLGLQRRFGSRPKVLEINRDFIASVADEVEKEYGAQLKLEPAEPKSGEYVVASGNDVVAMGKVVGGVRYQAYYPITPASDESVLLEEFEGLKIDGESLGSIAILQTEDEIAAVSSVIGAALTGARASTATSGPGFSLMVEALGWAGKNDVPMVITYYQRGGPSTGLPTRGSQSDLLFSLFASHGEFPRIILSSGDHLEAFYDAIEAYNLAERFQMPVIHLLDKFLANMVASVPFPDWKAIKIDRGKTLFKAPTGPFKRFPRDQPLADRPVLGSGAITWYTGDENDEYGHIDEDPVNRLVMYERRWKKMEIADREIPEDFRVKYYGDEDAEVLLVGWGSVKIPALEAIERLREMGVNAAYLHLRMLSPLPKRRVSEVLSRFDADRVIAVEANYLGQASKIVTMETGFMFRKYILKWTGRPVYLHELVEGVLDIVRNGRDKVVLSYGK
Protein: Oxytocin-neurophysin 1 (OT-NPI) [Cleaved into: Oxytocin (Ocytocin); Neurophysin 1] (P01178)
Organism: Homo sapiens (Human)
Function: Neurophysin 1 specifically binds oxytocin.
Subcellular location: Secreted.
Interaction partners:
- Oxytocin receptor
- Vasopressin V1a receptor
- Vasopressin-neurophysin 2-copeptin
- Pro-opiomelanocortin
- Corticoliberin
- Neurotensin/neuromedin N
- Prolactin
- Vasopressin V1b receptor
- Leucyl-cystinyl aminopeptidase
- Protachykinin-1
Sequence:
MAGPSLACCLLGLLALTSACYIQNCPLGGKRAAPDLDVRKCLPCGPGGKGRCFGPNICCAEELGCFVGTAEALRCQEENYLPSPCQSGQKACGSGGRCAVLGLCCSPDGCHADPACDAEATFSQR
Protein: N-alpha-acetyltransferase 38, NatC auxiliary subunit (LSM domain-containing protein 1) (Phosphonoformate immuno-associated protein 2) (Q9BRA0)
Organism: Homo sapiens (Human)
Function: Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19398576}. Nucleus {ECO:0000269|PubMed:19398576}.
Interaction partners:
- N-alpha-acetyltransferase 35, NatC auxiliary subunit
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 10
- U6 snRNA-associated Sm-like protein LSm4
- U6 snRNA-associated Sm-like protein LSm5
- N-alpha-acetyltransferase 11
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
- U6 snRNA-associated Sm-like protein LSm7
- N-alpha-acetyltransferase 50
Sequence:
MAGAGPTMLLREENGCCSRRQSSSSAGDSDGEREDSAAERARQQLEALLNKTMRIRMTDGRTLVGCFLCTDRDCNVILGSAQEFLKPSDSFSAGEPRVLGLAMVPGHHIVSIEVQRESLTGPPYL
Protein: Asparagine synthetase [glutamine-hydrolyzing] (EC 6.3.5.4) (Cell cycle control protein TS11) (Glutamine-dependent asparagine synthetase) (P08243)
Organism: Homo sapiens (Human)
Interaction partners:
- Argininosuccinate synthase
- Aspartate aminotransferase, mitochondrial
- Aspartate aminotransferase, cytoplasmic
- Isoaspartyl peptidase/L-asparaginase
- Putative aspartate aminotransferase, cytoplasmic 2
- Multifunctional protein CAD
- Asparagine--tRNA ligase, cytoplasmic
- Adenylosuccinate synthetase isozyme 2
- N-acetylaspartate synthetase
- Cyclic AMP-dependent transcription factor ATF-4
Sequence:
MCGIWALFGSDDCLSVQCLSAMKIAHRGPDAFRFENVNGYTNCCFGFHRLAVVDPLFGMQPIRVKKYPYLWLCYNGEIYNHKKMQQHFEFEYQTKVDGEIILHLYDKGGIEQTICMLDGVFAFVLLDTANKKVFLGRDTYGVRPLFKAMTEDGFLAVCSEAKGLVTLKHSATPFLKVEPFLPGHYEVLDLKPNGKVASVEMVKYHHCRDVPLHALYDNVEKLFPGFEIETVKNNLRILFNNAVKKRLMTDRRIGCLLSGGLDSSLVAATLLKQLKEAQVQYPLQTFAIGMEDSPDLLAARKVADHIGSEHYEVLFNSEEGIQALDEVIFSLETYDITTVRASVGMYLISKYIRKNTDSVVIFSGEGSDELTQGYIYFHKAPSPEKAEEESERLLRELYLFDVLRADRTTAAHGLELRVPFLDHRFSSYYLSLPPEMRIPKNGIEKHLLRETFEDSNLIPKEILWRPKEAFSDGITSVKNSWFKILQEYVEHQVDDAMMANAAQKFPFNTPKTKEGYYYRQVFERHYPGRADWLSHYWMPKWINATDPSARTLTHYKSAVKA
Protein: Epididymis secretory protein Li 1 (V9HWD6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTMDKSELVQKAKLAEQAERYDDMAAAMKAVTEQGHELSNEERNLLSVAYKNVVGARRSSWRVISSIEQKTERNEKKQQMGKEYREKIEAELQDICNDVLELLDKYLIPNATQPESKVFYLKMKGDYFRYLSEVASGDNKQTTVSNSQQAYQEAFEISKKEMQPTHPIRLGLALNFSVFYYEILNSPEKACSLAKTAFDEAIAELDTLNEESYKDSTLIMQLLRDNLTLWTSENQGDEGDAGEGEN
Protein: Proline-rich region:Proline-rich extensin (Q2YQ34)
Organism: Brucella abortus (strain 2308)
Interaction partners:
- Uncharacterized protein
Sequence:
MKEWLSGIIGESAANIVGFVLIFAIILGGIFVVLGIIRRFSGGTFVSSGRMRQPRLSVMDAAAVDSRRKLVLIRRDDVEHLLLIGGPTDVVVEQNIVLESRAGTHAPGTHALGTHAQSSRIEPEHIERFRQHEVLANEKTERPALSVQSQPGDEREETIQLSSAIAAPVYRKPEPPKAENVRPAPSEPAPMRAPQPPVTPPPAAPRPEAPASQVSEPHPRPASNYPSQPRTVLPPRPAPSAAPNSVRAHPAYPLSQVSRGVVSSTSNIQAATVASAATANLGSIVPERESAAPAKPAAPAPNQPERSERPERPERPQQRIEPVVPFVAQEVRQPESADDDLDDLGGTLHDAIMADLGSNAGKDENMEELDTASLEDELLSSLDISPTDEQPEDAKAEETIEDEMEKLLGELTKGETRN
Protein: Dihydrofolate reductase (EC 1.5.1.3) (P36591)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Key enzyme in folate metabolism. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis (By similarity).
Interaction partners:
- Probable thymidylate synthase
- Serine hydroxymethyltransferase, mitochondrial
- Probable serine hydroxymethyltransferase, cytosolic
- Probable dihydrofolate synthetase
- Probable folylpolyglutamate synthase
- Thymidylate kinase
- Probable aminomethyltransferase, mitochondrial
- C-1-tetrahydrofolate synthase, cytoplasmic
- Putative methionyl-tRNA formyltransferase
- Phosphoribosylglycinamide formyltransferase
Sequence:
MSKPLKVLCLHGWIQSGPVFSKKMGSVQKYLSKYAELHFPTGPVVADEEADPNDEEEKKRLAALGGEQNGGKFGWFEVEDFKNTYGSWDESLECINQYMQEKGPFDGLIGFSQGAGIGAMLAQMLQPGQPPNPYVQHPPFKFVVFVGGFRAEKPEFDHFYNPKLTTPSLHIAGTSDTLVPLARSKQLVERCENAHVLLHPGQHIVPQQAVYKTGIRDFMFSAPTKEPTKHPRDLTMIVAVSSPNLGIGKKNSMPWHIKQEMAYFANVTSSTESSGQLEEGKSKIMNVVIMGRSCYDSLPKKNRPLKDRINIVITRNSNYNFGLTKKEKMPENLYAADCIDSALDLVAEKYGADSDIQVGKVFIIGGSFLYGSALYHPLTKNLLFTRIHKEYPCDSFFPFEPAESSDWVRKAHPELEKFVGIPVEEGRLKAASSNKEEVEIEFELYGKNDDVNVALEKLSIC
Protein: GPI ethanolamine phosphate transferase 2 (EC 2.-.-.-) (Glycosylphosphatidylinositol-anchor biosynthesis protein 7) (Q09782)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the GPI second mannose (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Endoplasmic reticulum vesicle protein 25
- Actin-related protein 2/3 complex subunit 3
- Large ribosomal subunit protein eL19B
Sequence:
MRFAFFGIFWLQIFGSILFLLGFFPHKNDSTGKAMSNQFSPPAVIDQVVFVMVDALRADFVFSKSHNMPFTQSLLYNSTHGIGFSAFARSPTVTMPRLKALTTGTIPGFLDVLLNIAESDTGSSIEAQDSWVYQLNSFNKKIEFYGDDTWLKLFPSAFSKFEGTTSFFVSDYTEVDNNVTRNFDHALPSSLSHSWDALILHYLGVDHIGHLYGPSSPLLNIKLLEIDTIISRIYKYLQEYDEKTNTHSLIVLCGDHGMNEVGNHGGSSSGETTAALSLLFPSNELSHINKPILNMDDNPYSILERVEQVDVVPTICLLLGIPIPKGNMGKVLSPVTELWKDTKTAKMAALSNLFQLSLLKNPSLTTSELSTQFQDSDLNDIRLALENLQSQMVAQSSSYSLDRMLVAISILGACSILSLILFRNLYNYKELLAFAPFVVQNIIIVFSSSFIEEEHVIWYFAAVSLSLLQLLNPKTRLAGSLQLFCLSIIKRWNQTGQKYSDLRDIVDDFIAPSTFMKTILCVTSAFMPAIRSPSPINFLSSMFIAFYKLMPIISKHLNELPIIASFDYTFFVRIIWSLLLISFLSKPTFKQLRCQLSLFILLLTRLENMGLYLLYDIWQRTMPEEGTLASVMYYVAEQVAFFSLGNSNSLATVDLSQAYTGLDSYNIFAVGILLFTSVFAGALWWCLHQPKRMMDRSVKTFWIMSSISLTFLCISCFIMRHHLFVWSVFSPKLLYNASWASMYFLAKCLISTIMVRLR