wanglab/gogpt-training-data huggingface dataset:
Protein: Non-reducing polyketide synthase pkdA (NR-PKS pkdA) (EC 2.3.1.-) (Pkd biosynthesis cluster protein A) (Q5BG07)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Non-reducing polyketide synthase that synthesizes 6-ethyl-2,4-dihydroxy-3,5-dimethylbenzaldehyde via condensation of one propanoyl-CoA starter unit with 3 malonyl-CoA units, as well as 2 methylation steps.
Interaction partners:
Sequence:
MASSSSSTQAENLILIFGPQDPNLNDAYLQSLRTNLLDSPFLQWIVHTLIQLPQEWQRIAPTHTELGSFQGQKYLQLLSEWMRKGTLPGNIFPLPNILVTPLVVTTHLAQYTKLLEQLNPAIATNDMLSGIVKHDIQTVGLCTGLLSSAAVASSATLAELEKHGAAAIRMAMAIGALVDAGDTEVEDGDKWQSLAVGWTTQNGDAELEGISKQFSHAYVSVISEARLATLTMLKNDANAIQRELTNAGFIYTKTALRGPFHCGSREDQAVSLMRLFDSDPSFQFPGASTLVFRTRAPDGEEFPLDRSLHGAAARAMLTDQADWHKLYTKLHESTNSHPGIVITFGSQRFIPQWFLRKLGPRLAHVLDLDVGSGHWPAPLYTLQDSGQDESIAVVGMACNFPGGSDLDEFWDTVCAAKSQCTEVPPERVDFDYEAWRENDTQRKWFGNFIREYDTFDHKFFQKSPREMISTDPQHRIMLQVAYQAVQQSGYFNRPGRSKHVGCYVGIGVTDYENNVACHPPTAYTATGNLKSFAAGKISHFFGWSGPGVTVDTACSSSALAIHLACKAILSGECDASLAGGVNVITSPEWYQNLDGASFLSPTGQCKPFDAAADGYCRGEGAGAVFLKRLSSAVEDGDQIVGVIRATSVNQNENCSAITAPSVRSLANVFNGVIRKARVDPKQISVVEAHGTGTQVGDRAEYDSIRTVLGGPGRAYPLSLGSVKGLIGHLECASGIAALIKVLLMVQNGIIPPQPGFSKINPKLEALPSDNIEIPTSLRPWNPGFRAALLNNYGASGSNASLVVTQAGVPHLNQSAIPKGASAGRRPFWLSGTDVQSLRSYAAKLVQMLRSRKADDPRFTVANLSFQLARQSNRNLGQALIFSCASVDELEAKLADFASGGNTLTSVPRPDSSRPVILCFGGQRSSFVGLDREAFDSFKLLKSHLTHCHETSLALGLGGILPAIFDRTPRSSIVELQLMQFALQYSCAKTWIDSGIHVAALVGHSFGELTAMCVSGTLSLQDTLRMIAGRARIIEEKWGPDRGSMMAVDGELELVQRLLHNAHEASPNEPAVNIACFNGPRLFTLAGTTKAMRVVREVLSKDNRLSSIKVKSLETSHAFHSTLVEPLIPDLEELGEESIFRKPVVVHERATQNSVAGPPPFSIFASHMRDPVYFDRAVQRLANRYPSSIWLEAGSGSGVTNLASRAAGSRAMAFQSINITSSSAVQNVADATLNLWKEGLQVMFWEHVRPSPKFPLLLLPPYQFAKSRHWLERRKLKTKVFVPASPVQEAQKGLWTFVGYQDSDRCQARFQIHITSDEFQNYVSAHVIAQTAPICPSMFQQVIARDALATLVDGDMIPELEGMENDTPLCLDGSKSVWLVAERPSDRSSAWDFRITSSDSGNTTQHVSGRITFQTPKQSMQAFAAYERLVDHRRALALLNGQEAEQTIQGSRNIYKLFSNVVNYKEDGYRGLQKLAATSNESAGRIIKQDSSKSILGVGLGDTFCQVAGIFLNCMTDCDEGKMYLSNRVERWIRSPTVPLDLRPEQWEVYARHHQPSPKEYVSDIFVFDATNGKLVWVILGLHFVEVSIAGMSRFLTRLSGGQLEPQEKCLATVEFKEVPEPVFTKDVSKNEKDAKAPSKKKESTSKSPGHDILARVRTLFCNLLGLEPVEIQPGADLVELGIDSLLAMEVAREVEKEFSIKFELDELMDMTDVHSLVKCIGANMMASDTSRTGDDSSDDLETASAESETSSGINNEDSHNIDRQQIPASSIVDSFTETKLLTDRFIEANKLSGYSNNVQPRLTELVIVHTLDAFDQMGCSIRAAQPGQTVRRISHLPKHNQVVAVLYGLLEKASLVDVDGPRMTRTAVPVPSKSAEQILQELLRQYPEHAYDHKLTSLTGCKLADCLTGKTEAIQLLFGTPEGRDLAAGMYGKSPINVAWLRQLQHFWEHFLAQLPQHRTEPINILEMGAGTGGTTAALVPLLSRSRIPVRYTATDISPSLVAGLRKRFKDHTWMRFEVVDCEKTPSSHLFESQHVVLAVAIIPPAPSKMSTADIASRQAIIDTLVEKHTSHFSAPTCLPPNQVIDGSPHCVLVTGATGSLGSHLVAHLVKQSSVTKVVCLNRVSGSDATSRQLDAFQSKGLILDSESLSKLEVIETDSSAPSLGLVPERYQHLVNTVTDVVHNAWAMSMTRPVRGFEPQFKTMRNLIDLCRDCANRRHSDTGKVGFQFVSSVSVVGCHPFITKKAIVPEQPVNAESALPMGYADAKLVCEHILDETLHMHPDIFRTMSVRVGQISGSKINGYWNPVEHLVHLIKSSKTLNVLPDLEGVLSWCPVDDVAAALGDLLLTNKPAYSVYHIENPVRQPWPDMLTILADALDIPRTNAVPFKEWLRRVRHFPPSLGFSENPAARLADFFETDFLRMSCGGMILDTTRSREHSATLRSLGPIDQDLVMKITFKRIYAIFAKSSEVKIKKSS
Protein: Nuclear receptor subfamily 1 group I member 3 (D6REZ7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRKDMILSAEALALRRAKQAQRRAQQTPVQLSKEQEELIRTLLGAHTRHMGTMFEQFVQFRPPAHLFIHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLPVFRSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPLRYTIEDGARVGFQVEFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYIKGQQRRPRDRFLYAKLLGLLAELRSINEAYGYQIQHIQGLSAMMPLLQEICS
Protein: Transmembrane protein 245 (Q21453)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MMSSEGIERYFGAGDSEQRTALQFAFYNVLLFVLLGVSLCGLAALYNMMYMFLSPMLWAVLVGTVLFPFKKKVADTVQHWLRNLQKSNQTLAKSVITLPFTGFSKISEKIYTTFASPNGAIIVIAYTALKILSYERTFMYIISWMGRLYGYLDSFIVFFARPWVLPLIIVYFCCYAAWIYVQNPKEINKKLARSFSLPIWIYVISYASLYFGPLRAGVFGVSAAVLGMLSAGLIGGHRPSEELLEKENSSENLDESILPPNVEKVLETAKEKLDATEQSLLDNSLLSTSTVDEAITGDWLIRCVFGLCALLWVVRHDGALILLAIPFVLAVISRTAEQLGITAAIHNFLDSTWQKMSPSVTKIVEITVAGPLRQFVKMLFSSDKYIVDTLHDKMDVLSSVIVMALLAFSAIFSVFFFGFQLHGETVHLVRLTSNVVNSRPDWLAAAMDYTEDQLEENNIDIDDYVQQAYEQGRTWLASNVRSLANAKDTKRADMLEEQVKQVVDKLYNMWEERNNNFTVAVNQEPRGDVWTQLKGVTDLTALKDELTLIVKENLDTLMGIAQSIGAILAVNVSIFSSLLVSLAGIILSFGMDLLNTFIEMIVFLTMVYYLLSASRTRWLPLQWASDLSAVTTADGSSAGNQHHITVAIEHAIFGVFVLSAKMAVFYGLYTYFVHSLFDLNIVFVPSMAATVFAAIPIMPPYIVAIFGIVELWLVRGEGAAALVFTVASFAPVMFADATFYREVKGSHPYVTGLAIIGGMYWLGLQGAIIGPIVLCLCLVLVNVYLQHVKPTALYTPAPSPRNVKLHNH
Protein: Cold shock domain-containing protein C2 (RNA-binding protein PIPPin) (Q9Y534)
Organism: Homo sapiens (Human)
Function: RNA-binding factor which binds specifically to the very 3'-UTR ends of both histone H1 and H3.3 mRNAs, encompassing the polyadenylation signal. Might play a central role in the negative regulation of histone variant synthesis in the developing brain (By similarity).
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=PIPPin-RNA complexes are located to the nucleus. {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
Sequence:
MTSESTSPPVVPPLHSPKSPVWPTFPFHREGSRVWERGGVPPRDLPSPLPTKRTRTYSATARASAGPVFKGVCKQFSRSQGHGFITPENGSEDIFVHVSDIEGEYVPVEGDEVTYKMCPIPPKNQKFQAVEVVLTQLAPHTPHETWSGQVVGS
Protein: CUGBP Elav-like family member 1 (CELF-1) (Bruno-like protein 2) (CUG triplet repeat RNA-binding protein 1) (CUG-BP1) (CUG-BP- and ETR-3-like factor 1) (EDEN-BP/Bruno-like protein) (RNA-binding protein BRUNOL-2) (Q9IBD0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: RNA-binding protein implicated in the regulation of several post-transcriptional events. May be involved in mRNA translation activation and stability (By similarity). Involved in the regulation of muscle-specific splicing of alpha actinin pre-mRNAs via the binding to the UR-repeat element (URE) at the branch point of the non-muscle (NM) exon.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
Interaction partners:
- Muscleblind-like-splicing regulator 1.
- Muscleblind-like protein 3 isoform X2
- Pur-alpha
- Muscleblind-like protein 2 isoform C
- Uncharacterized protein
Sequence:
MNGSLDHPDQPDIDSIKMFVGQIPRTWSEDQLRELFEPYGAVYEINVLRDRSQNPPQSKGCCFVTYYTRKSALEAQNALHNMKILPGMHHPIQMKPADSEKNNAVEDRKLFVGMISKKCNENDIRLMFSPYGQIEECRILRGPDGLSRGCAFVTFTARQMAQSAIKSMHQSQTMEGCSSPIVVKFADTQKDKEQKRIAQQLQQQMQQLNAASMWGNLTGLNSLGPQYLALYLQLLQQSASSGNALNNLHPMSGLNAMQNLAALAAAASATQATPTGSSALTTSSSPLSVLTSSGTPSGQPAQSAWDAYKAGSSPTSSTSSSVNPMASLGALQSLAAGAGAGLNMSSLASMAALNGGLGSGGLSNGSGSTMEALTQAAYSGIQQYAAAALPSLYSQSLLSQQNVSAAGSQKEGPEGANLFIYHLPQEFGDQDLLQMFMPFGNVISAKVFIDKQTNLSKCFGFVSYDNPVSSQAAIQSMNGFQIGMKRLKVQLKRSKNDSKPY
Protein: Candida glabrata strain CBS138 chromosome M complete sequence (Q6FJ79)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MQFNKISLLAMASAASAATTSPTTTETKPTTTKFFTPGDNFSTFAPNATFSGAAVNFTSTFGIAVQSIDSKSVVSKSLVSTSTTSTLAPSSSTSSAASSTTSSPNITIVNKSCKADGTLVMELENGILRDGKGRIGSIVSNRQFQFDGPPPQAGAIYAAGWSVTPEGNLALGDSDVFYQCSSGNFYNLYDEYIAEQCHPIHLEVLSLVDC
Protein: 3-ketoacyl-CoA thiolase A, peroxisomal (EC 2.3.1.16) (Acetyl-CoA C-myristoyltransferase) (EC 2.3.1.155) (Acetyl-CoA acyltransferase A) (EC 2.3.1.9) (Beta-ketothiolase A) (Peroxisomal 3-oxoacyl-CoA thiolase A) (Q921H8)
Organism: Mus musculus (Mouse)
Function: Responsible for the thiolytic cleavage of straight chain 3-keto fatty acyl-CoAs (3-oxoacyl-CoAs) (Probable). Plays an important role in fatty acid peroxisomal beta-oxidation (Probable). Catalyzes the cleavage of short, medium, long, and very long straight chain 3-oxoacyl-CoAs (By similarity).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:P09110}. Note=Transported into peroxisomes following association with PEX7. {ECO:0000250|UniProtKB:P09110}.
Interaction partners:
- Peroxisomal acyl-coenzyme A oxidase 1
- Peroxisomal bifunctional enzyme
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Peroxisomal multifunctional enzyme type 2
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
Sequence:
MHRLQVVLGHLAGRPESSSALQAAPCSARFPQASASDVVVVHGRRTPIGRASRGGFKNTTPDELLSAVLTAVLQDVRLKPEQLGDISVGNVLEPGAGAVMARIAQFLSGIPETVPLSTVNRQCSSGLQAVANIAGGIRNGSYDIGMACGVESMSLSGMGNPGNISSRLLESEKARDCLTPMGMTSENVAERFGISRQKQDDFALASQQKAASAQSRGCFRAEIVPVTTTVLDDKGDKKTITVSQDEGVRPSTTMQGLAKLKPAFKDGGSTTAGNSSQVSDGAAAVLLARRSKAEELGLPILGVLRSYAVVGVPPDVMGIGPAYAIPAALQKAGLTVNDIDIFEINEAFASQAVYCVEKLGIPAEKVNPLGGAIALGHPLGCTGARQVVTLLNELKRRGRRAYGVVSMCIGTGMGAAAVFEYPGN
Protein: Protein S100-A10 (Calpactin I light chain) (Calpactin-1 light chain) (Cellular ligand of annexin II) (Nerve growth factor-induced protein 42C) (S100 calcium-binding protein A10) (p10 protein) (p11) (P05943)
Organism: Rattus norvegicus (Rat)
Function: Because S100A10 induces the dimerization of ANXA2/p36, it may function as a regulator of protein phosphorylation in that the ANXA2 monomer is the preferred target (in vitro) of tyrosine-specific kinase.
Interaction partners:
- Annexin A2
- AHNAK nucleoprotein
- Uncharacterized protein.
- Annexin A1
- Plasminogen
- Tissue-type plasminogen activator
- Protein S100-A6
- 5-hydroxytryptamine receptor 1B
- Protein S100-A4
- Helicase-like transcription factor
Sequence:
MPSQMEHAMETMMLTFHRFAGEKNYLTKEDLRVLMEREFPGFLENQKDPLAVDKIMKDLDQCRDGKVGFQSFLSLVAGLIIACNDYFVVHMKQKK
Protein: Triadin (Q9QX75)
Organism: Rattus norvegicus (Rat)
Function: Contributes to the regulation of lumenal Ca2+ release via the sarcoplasmic reticulum calcium release channels RYR1 and RYR2, a key step in triggering skeletal and heart muscle contraction. Required for normal organization of the triad junction, where T-tubules and the sarcoplasmic reticulum terminal cisternae are in close contact. Required for normal skeletal muscle strength. Plays a role in excitation-contraction coupling in the heart and in regulating the rate of heart beats.
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q28820}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q28820}. Microsome {ECO:0000269|PubMed:15927957}. Cell membrane, sarcolemma {ECO:0000269|PubMed:15927957}.
Interaction partners:
- Calsequestrin-2
- Ryanodine receptor 2
- Calsequestrin-1
- Histidine rich calcium binding protein
- Ryanodine receptor 1
- Junctophilin-2
- Junctophilin
- Peptidyl-prolyl cis-trans isomerase FKBP1B
- Inositol 1,4,5-trisphosphate/ryanodine receptor domain-containing protein
- Junctophilin
Sequence:
MTEITAEGNASITTTVIDNKNGSVPKSPGKVLKRTVTEDIVTTFSSPAAWLLVIALIITWSAVAIVMFDLVDYKNFSASSIAKIGSDPLKLVNDAVEETTDWIYGFFSLLSDIISSDGDEDDEDADEDIDKGEIEEPPLKRKEIQKEKAEKQEKPEKKIQTKVSHREKEKGKEKLKGEKPEKKATHKEKLEKKERTETKMAAKEDKKIKTKEKTEEKAKKEMKVGKQEKAKPAAAKAKETPKTTPKAREKDDKETPAVPKHEQKDQYAFCRYMIDMFVHGDLKPGQSPAVPPPSLTASRPALSTPSLEEKEKEEKKKVEKKVTSDTKKKEKGEAKKKSEKETVIDGKGKEPGKPPETKQTTTKLTTQAAATKDEKKEDSKKMKKPPEEKPKGKKQEKKEKHIEPAKTPKKEHPAPSEKHRKAKAEQAKEEIAPASTKKALHGKKEEKAKTVEQGKDVKPKLPQPQLKKEEKSEPQPKKEVKLETQLKKEEKSEPQVKKEAKLASSEKGQTRKQNITRPEQVIPHGKPEQKVPKQIKAITAEKTEKAERQEKYHPSIKTEGKPEVTDSGKKKIEKPEKESKVPPKQENLQVRNVTRAEKRGKISKDSKDAPAPKKDKDSKDVLHSKKDKEVTNNVSSPKKQKSPISFFQCVYLDGYNGYGFQFPVTPVQHSGENPGKSNSPGQKQQEQ
Protein: RE15841p (Zinc/iron regulated transporter-related protein 42C.1) (Q7JZR2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Zinc transporter 63C, isoform F
- IP18018p
- LD23375p
- Crossover suppressor on 3 of Gowen
- FI23527p1
- Zinc transporter ZIP11
- Zinc transporter foi
Sequence:
MSATATMSQEQTQDVDHHALLVAKIVSMVVLVVITVLCGSLPYVLNRCFHWTKASPEETRSSLVVRCLLFFGGGVLICTTFLHMLPEVIEVVEALQECGSLVKTPFALAEMLLCTGFFLMYALDELMTSLVRHHQGKLSRKESVASLAFERGRSIRHSVLLNPQAKEEVEVKDTEPQPHKDHHGHSHMPVPADDGSSARGLGIILALSLHELFEGMAIGLEGTVSTVWFMFGAVSAHKLVLAFCVGMELLVARTRSSLAILYLVTFSIVTPIGIGVGLGISQQVAAGQPSLPSGVLQGIACGTLLYVVFFEILIESHAGWRALVAAVAGFALMFGLQILSDEAEGDDSLTCS
Protein: Similar to part of disease resistance protein (Toll-Interleukin-Resistance (TIR) domain-containing protein) (Q9SSN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Leucine-rich repeat
- Leucine-rich repeat
- Leucine-rich repeat
- Probable methyltransferase PMT15
- Leucine-rich repeat
- Repressor ROX1-like protein
- Probable disease resistance protein At5g45510
- Leucine-rich repeat
- At5g09570
- Lysophospholipid acyltransferase LPEAT2
Sequence:
MSSHTATKYDVFLSFRGHDTRQNFISFLYKELVRRSIRTFKDDKELENGQRISSELKRTIEVSRFAVVVVSETYAASSWCLDELVTIMDFEKKGSITVMPIFYGVEPNHVRWQTGVLAEQFKKHGSREDHEKVLKWRQALTNFAQLSGDCSGDDDSKLVDKIANEISNKKTIYATINNGKNLVGIDTHMKELNRLMHMNCNKVTVRMVGIWARGGDGRSALAKYVYQTSCQQFDSHCFLGNVKTISQGRHSAHLHDEFLRNIKREDSNKQCLKNQKVLLVADNVTKVKQLEALAGDFSSFGPGSVVIITTDNKGLLNSYGITDVYEVEHLKFCGILRSLGFKKRAAAFQRALCRAKSFATECFCCQSSSISGYGKVTDLV
Protein: Chalcone isomerase-like protein 1 (HlCHIL1) (EC 5.5.1.6) (A0A2U7XUH7)
Organism: Humulus lupulus (European hop)
Function: Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Involved in anthocyanin biosynthesis (By similarity). Polyketide binding proteins (PBP) which reduces the catalytic activities of CHS_H1 and PT1L and prevents demethylxanthohumol (DMX) production, by binding to DMX and naringenin chalcone (NC) to stabilize the chalconoids ring-opened structure.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29760092}.
Interaction partners:
Sequence:
MATALNSKNASSNTAVHIEPKTGIAFPVKLDDGKSLNSVGLRKKSLLGMGIKVFGFGLYADNEKLKNLLKLKIGKSPAKPTEEMYQLVIDGDIGLTHKIVIAYSGLKMNMFKKAFSEALGESIMKLNGGRKNEELANKVLGPASDQIKLATGSEMEISKLPGYVLETKVHGELASRVESELLCRAYFGIYLGEITMECYKESKEMFGQSMLSLF
Protein: Isocitric dehydrogenase subunit beta (NAD(+)-specific ICDH subunit beta) (Q9VD58)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Isocitrate dehydrogenase
- Probable isocitrate dehydrogenase subunit alpha, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Dihydrolipoyl dehydrogenase
- isocitrate dehydrogenase
- Glutamate dehydrogenase, mitochondrial
- Malate dehydrogenase, mitochondrial
- Aconitate hydratase, mitochondrial
- ATP synthase subunit gamma, mitochondrial
- Glutamate dehydrogenase
Sequence:
MSMLARTVGRTFMQAAAARSLHTTSTLRATDNYGANRTTCTLIPGDGVGPELVYSLQEVFKAASVPVDFECYFLSEINPVLSAKLEDVVASIQKNKVCIKGVLATPDYSNVGDLQTLNMKLRNDLDLYANVVHVRSLPGVKTRHTNIDTVIIREQTEGEYSALEHESVPGIVECLKIITAKKSMRIAKFAFDYATKNQRKKVTAVHKANIMKLGDGLFLRSCEEVSRLYPRIQFEKMIVDNTTMQMVSNPNQFDVMVTPNLYGAIVDNLASGLVGGAGVVAGASYSSESVVFEPGARHTFAEAVGKNVANPTAMLLCGVKLLRHINLPTYGEIIQNAINKVLNDGKVRTKDLGGQSTTQDFTRAIILNMS
Protein: Semaphorin-6C (Semaphorin-Y) (Sema Y) (Q9WTL3)
Organism: Rattus norvegicus (Rat)
Function: Shows growth cone collapsing activity on dorsal root ganglion (DRG) neurons in vitro. May be a stop signal for the DRG neurons in their target areas, and possibly also for other neurons. May also be involved in the maintenance and remodeling of neuronal connections.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Semaphorin-6B
- Semaphorin-6A
- Plexin-A1
- Plexin-A2
- Plexin-A3
- Plexin-C1
- Plexin-A4
- Plexin-D1
Sequence:
MPRAPHSMPLLLLLLLSLPQAQTAFPQDPIPLLTSDLQGTSPSSWFRGLEDDAVAAELGLDFQRFLTLNRTLLVAARDHVFSFDLQAQEEGEGLVPNKFLTWRSQDMENCAVRGKLTDECYNYIRVLVPWDSQTLLACGTNSFSPVCRSYGITSLQQEGEELSGQARCPFDATQSTVAISAEGSLYSATAADFQASDAVVYRSLGPQPPLRSAKYDSKWLREPHFVYALEHGDHVYFFFREVSVEDARLGRVQFSRVARVCKRDMGGSPRALDRHWTSFLKLRLNCSVPGDSTFYFDVLQSLTGPVNLHGRSALFGVFTTQTNSIPGSAVCAFYLDDIERGFEGKFKEQRSLDGAWTPVSEDKVPSPRPGSCAGVGAAALFSSSQDLPDDVLLFIKAHPLLDPAVPPATHQPLLTLTSRALLTQVAVDGMAGPHRNTTVLFLGSNDGTVLKVLPPGGQSLGPEPIILEEIDAYSHARCSGKRSPRAARRIIGLELDTEGHRLFVAFPGCIVYLSLSRCARHGACQRSCLASLDPYCGWHRFRGCVNIRGPGGTDVDLTGNQESMEHGDCQDGATGSQSGPGDSAYVLLGPGPSPETPSSPSDAHPGPQSSTLGAHTQGVRRDLSPASASRSIPIPLLLACVAAAFALGASVSGLLVSCACRRANRRRSKDIETPGLPRPLSLRSLARLHGGGPEPPPPPKDGDAAQTPQLYTTFLPPPEGGSPPELACLPTPETTPELPVKHLRASGGPWEWNQNGNNASEGPGRPRGCSAAGGPAPRVLVRPPPPGCPGQEVEVTTLEELLRYLHGPQPPRKGSEPLASAPFTSRPPASEPGAALFVDSSPMPRDCVPPLRLDVPPDGKRAAPSGRPALSAPAPRLGVSGSRRLPFPTHRAPPGLLTRVPSGGPSRYSGGPGRHLLYLGRPDGHRGRSLKRVDVKSPLSPKPPLATPPQPAPHGSHFNF
Protein: Furin-like protease kpc-1 (EC 3.4.21.-) (CelfurPC protein) (O17798)
Organism: Caenorhabditis elegans
Function: Furin-like protease which cleaves proproteins at the RX(K/R)R consensus motif. During neuronal development, regulates the formation and extension of dendrite branches and cellular positioning of various type of neurons. Together with chin-1 and cdc-42, plays a role in the development of the neuropil and is required for the guidance of axons from neurons, including SubL pioneer neurons and AIY interneurons, into the nerve ring. Its role in axon guidance in glia and pioneer neurons may be through ensuring the fmi-1 protein is correctly localized to the nerve ring. Promotes the formation, extension and self-avoidance of dendritic branches of PVD and FLP mechanosensory neurons. In PVD neurons, regulates plasma membrane levels of branching receptor dma-1 by targeting it to late endosomes and thus promotes normal dendrite branching and dendrite self-avoidance. Also controls dendrite extension in AIY and D-type motoneurons, dendrite branching in AQR sensory neurons and VC4/5 motoneurons, the normal number of dendritic branches in AVL neurons and the positioning of HSN and ALM/PLM neurons. Dispensable for maintaining dendrite branching in adults. Also regulates dauer-specific dendritic branching of IL2 neurons and dauer-specific nictation behavior. Under adverse environmental conditions, may promote dauer formation by processing insulin-like proteins ins-1 and ins-18, two daf-2/InsR antagonists.
Subcellular location: Cell membrane {ECO:0000305|PubMed:26974341}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:23932402}. Cell projection, axon {ECO:0000269|PubMed:23932402}. Note=In most neurons, localizes exclusively within the cell bodies, but in ventral cord neurons, localizes in both the neuronal cell bodies and processes. {ECO:0000269|PubMed:23932402}.
Interaction partners:
- Protein lin-12
- LRRCT domain-containing protein
- AO66 ankyrin
- Menorin
- Platelet-derived growth factor
- Nicastrin
- Teneurin-1
- Frizzled-4
- Clc-like protein
Sequence:
MSNISWYRHCSVRLQLVTLALFLLLGSASLGSAHIDEEFEDDVTTTISSIASPMRRTYTNEWAVRIAGGKVEEANRLANKYGYTNLGPIIPGDEYYLFRDDRKKSRSSRKTRSLSANQLQHEEDVMWMEQQVAKRRVKRGYRRIRRHTDDNDIFEEDDDGTQISKSRNRKHPDPNDPLWTDMWYLNRGEHHSDSTTRMDHNVKEAWDLGYTGKGVVVTILDDGLERTHPDISPNYDERASYDVNDRDNDPMPRYEFSDENRHGTRCAGEVAAIFNNSLCIVGIAYNANIGGIRMLDGDVTDAVEAASVGHNADYIDIYSASWGPDDDGRTVDGPAKLTRSAFEKGITMGRKGKGSIFVWASGNGGKDADSCNCDGYTNSIYTLSISSATENGNIPWYSEACSSTLATTYSSGATGEKMILTTDLHHACTNMHTGTSASAPLAAGIVALALEANPNLTWRDLQHIVIRTAKPINLRAGDWTTNGVGRNVSHSFGYGLMDAGAMVKLAKIWKKVDEQHRCRQFYPSRYKNIPNGNRLQLQLYSDGCYGGADENKVSYVEHVQAIVTLKAPKRGDLQIYLTSPSGTKSTLLTKRARDTSRSGFTDWAFMTTHNWGEQAAGLWILEIDNDGWDDAELVKWELVLYGTDRETGDFGGQHASPLAVRSVQMEATSSGTQYSIFHVITLVILTFSQILY
Protein: Single-strand selective monofunctional uracil DNA glycosylase (EC 3.2.2.-) (Q59I47)
Organism: Bos taurus (Bovine)
Function: Recognizes base lesions in the genome and initiates base excision DNA repair. Acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA with a preference for single-stranded DNA substrates. The activity is greater toward mismatches (U/G) compared to matches (U/A). Excises uracil (U), 5-formyluracil (fU) and uracil derivatives bearing an oxidized group at C5 [5-hydroxyuracil (hoU) and 5-hydroxymethyluracil (hmU)] in ssDNA and dsDNA, but not analogous cytosine derivatives (5-hydroxycytosine and 5-formylcytosine), nor other oxidized bases. The activity is damage-specific and salt-dependent. The substrate preference is the following: ssDNA > dsDNA (G pair) = dsDNA (A pair) at low salt concentration, and dsDNA (G pair) > dsDNA (A pair) > ssDNA at high salt concentration.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q53HV7}.
Interaction partners:
- G/T mismatch-specific thymine DNA glycosylase
- Thymidylate synthase
- Methyl-CpG-binding domain protein 4
- Thymidine kinase, cytosolic
- Uracil phosphoribosyltransferase homolog
- 5'-nucleotidase
- Endonuclease 8-like 1 lyase Neil1)
- DNA-3-methyladenine glycosylase
- Thymidylat_synt domain-containing protein.
- Ornithine aminotransferase, mitochondrial
Sequence:
MAVPQPFPSGPHLQPAGALMEPQPSPRSLAEGFLQEELRLNDELRQLQFSELVGIVYNPVEYAWEPHRSYVTRYCQGPKQVLFLGMNPGPFGMAQTGVPFGEVSVVRDWLGLGGPVRTPPQEHPKRPVLGLECPQSEVSGARFWGFFRNLCGQPEVFFRHCFVHNLCPLLLLAPSGRNITPAELPAKQREQLLGVCDAALCRQVQLLGVRLVVGVGRVAEQRARRALASLMPEVQVEGLLHPSPRSPQANKGWEAVAKERLNELGLLPLLTS
Protein: Sentrin-specific protease 7 (EC 3.4.22.-) (SUMO-1-specific protease 2) (Sentrin/SUMO-specific protease SENP7) (Q9BQF6)
Organism: Homo sapiens (Human)
Function: Protease that acts as a positive regulator of the cGAS-STING pathway by catalyzing desumoylation of CGAS. Desumoylation of CGAS promotes DNA-binding activity of CGAS, subsequent oligomerization and activation (By similarity). Deconjugates SUMO2 and SUMO3 from targeted proteins, but not SUMO1. Catalyzes the deconjugation of poly-SUMO2 and poly-SUMO3 chains. Has very low efficiency in processing full-length SUMO proteins to their mature forms.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8BUH8}.
Interaction partners:
- Small ubiquitin-related modifier 2
- Small ubiquitin-related modifier 1
- Ran GTPase-activating protein 1
- Chromobox protein homolog 5
- Small ubiquitin-related modifier 4
- SUMO-conjugating enzyme UBC9
Sequence:
MDKRKLGRRPSSSEIITEGKRKKSSSDLSEIRKMLNAKPEDVHVQSPLSKFRSSERWTLPLQWERSLRNKVISLDHKNKKHIRGCPVTSKSSPERQLKVMLTNVLWTDLGRKFRKTLPRNDANLCDANKVQSDSLPSTSVDSLETCQKLEPLRQSLNLSERIPRVILTNVLGTELGRKYIRTPPVTEGSLSDTDNLQSEQLSSSSDGSLESYQNLNPHKSCYLSERGSQRSKTVDDNSAKQTAHNKEKRRKDDGISLLISDTQPEDLNSGSRGCDHLEQESRNKDVKYSDSKVELTLISRKTKRRLRNNLPDSQYCTSLDKSTEQTKKQEDDSTISTEFEKPSENYHQDPKLPEEITTKPTKSDFTKLSSLNSQELTLSNATKSASAGSTTETVENSNSIDIVGISSLVEKDENELNTIEKPILRGHNEGNQSLISAEPIVVSSDEEGPVEHKSSEILKLQSKQDRETTNENESTSESALLELPLITCESVQMSSELCPYNPVMENISSIMPSNEMDLQLDFIFTSVYIGKIKGASKGCVTITKKYIKIPFQVSLNEISLLVDTTHLKRFGLWKSKDDNHSKRSHAILFFWVSSDYLQEIQTQLEHSVLSQQSKSSEFIFLELHNPVSQREELKLKDIMTEISIISGELELSYPLSWVQAFPLFQNLSSKESSFIHYYCVSTCSFPAGVAVAEEMKLKSVSQPSNTDAAKPTYTFLQKQSSGCYSLSITSNPDEEWREVRHTGLVQKLIVYPPPPTKGGLGVTNEDLECLEEGEFLNDVIIDFYLKYLILEKASDELVERSHIFSSFFYKCLTRKENNLTEDNPNLSMAQRRHKRVRTWTRHINIFNKDYIFVPVNESSHWYLAVICFPWLEEAVYEDFPQTVSQQSQAQQSQNDNKTIDNDLRTTSTLSLSAEDSQSTESNMSVPKKMCKRPCILILDSLKAASVQNTVQNLREYLEVEWEVKLKTHRQFSKTNMVDLCPKVPKQDNSSDCGVYLLQYVESFFKDPIVNFELPIHLEKWFPRHVIKTKREDIRELILKLHLQQQKGSSS
Protein: Macrophage immunometabolism regulator (Q8VEB3)
Organism: Mus musculus (Mouse)
Function: Regulates the macrophage function, by enhancing the resolution of inflammation and wound repair functions mediated by M2 macrophages. The regulation of macrophage function is, due at least in part, to its ability to inhibit glycolysis. May also play a role in trafficking of proteins via its interaction with UNC119 and UNC119B cargo adapters: may help the release of UNC119 and UNC119B cargo or the recycling of UNC119 and UNC119B. May play a role in ciliary membrane localization via its interaction with UNC119B and protein transport into photoreceptor cells.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96GV9}. Cell projection, cilium {ECO:0000250|UniProtKB:Q96GV9}. Note=Localizes to the transition zone and proximal cilium in addition to being found throughout the cytoplasm. {ECO:0000250|UniProtKB:Q96GV9}.
Interaction partners:
Sequence:
MEVDINGDSRSTLTTLPLPVAEGSSPGKAEAEKPRCSSTPCSPMRRTVSGYQILHMDSNYLVGFTTGEELLKLAQKCTGGEDSKGEAMPALRAKQLDTGLARSSRLYKTRSRYYQPYEIPAVNGRRRRRMPSSGDKCTKPLPYEPYKALHGPLPLCLLKGKRAHSKSLDYLNLDKMNIKEPADTEVLQYQLQHLTLRGDRVFARNNT