wanglab/gogpt-training-data huggingface dataset:
Protein: chitin synthase (EC 2.4.1.16) (A0A1D8PTV3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- UDP-N-acetylglucosamine diphosphorylase
- Chitin synthase export chaperone
- chitin deacetylase
- NEDD8-conjugating enzyme UBC12
- Bni4p
- Chs4p
- Chitin biosynthesis protein CHS5
Sequence:
MSYNNPNNSNSHLRPHAYNNSRRDDSDGDESSIEFLNQRSNTPLTQGTYNYHNTSTNSLNFQQPEPIYRNQTRTSLSDSYYDHPIFDTSQTQIQPPHDNPFTESYEMTDTSYQGNDHHYRTGQPNHLMNPTYNQAFIPHVYDEEDNDEQEYDQRIQYNQFQGDHFDLAAISYADDESQSQLDYVPTERVIPEGEEEEEEGETSFEKEPGSETISGPFGEERSFEEPPPQQEVRSKKLTRATGLNGHLVLDCPVADELLSKFPDYNPAEKSGGLSREFAFMRYTAVTCGPSNFYRDAYILRPVHYPIPRQTELMIVITMYNEDDILLGRTLKGVFKNIKYLESKARSSTWGKDSWKKIVVCIVSDGRTKINERAQALLAGLGVYQEGLAKSRVDDKKVQAHMFEYTTRVGISKVTDDVVKLTTEKVVPVQMLFCLKETNAKKINSHRWCFQAIGQVLDPKIVVLLDCGTQPSGRSLYELWKEFDRDHRVAGACGEITTSLKKRQMITNPLVYGQNFEYKISNILDKPTESSFGFISVLPGAFSAYRFIALQNDINGVGPLEKYFKGEFLHSSGELDPNDDEFQMKHLMLKEEAGIFTSNMYLAEDRILCFELVAKRGCNWLLRYCKSARAETDVPEGLAEFILQRRRWLNGSFFAAIYSLVHFYKVWTSSHSFGRKIFLHIEFFYQLINLIVSWFSIGSYFLVFRILTTSLGDKALGFAPGKILSVIFLWLYLASIVTTFVLSFGNKPKGTEKFYVTIVIFFAILMAYMIFAAIFMAVHSIQDIYRSGTRITVSLFFQNSEFRDLVVATSSTYALYFLASFLYFEPWHMFTSFVQYILLSPSYVNVLNIYAFCNIDDISWGTKGEVGGKSLGEAKLREDGTFDVSVPISKEQINQSYLDQLEKIRDPAPPEEKVLVTNTEDYYAFIRSMTVLVWMFTNFVVIALVLETGGFNQFVEATDLANLKSNRAAVFLTVILWTVAFMALFRFIGCIYYLITRLGREIKASEHATK
Protein: Transmembrane protein 100 (Q9NV29)
Organism: Homo sapiens (Human)
Function: Plays a role during embryonic arterial endothelium differentiation and vascular morphogenesis through the ACVRL1 receptor-dependent signaling pathway upon stimulation by bone morphogenetic proteins, such as GDF2/BMP9 and BMP10. Involved in the regulation of nociception, acting as a modulator of the interaction between TRPA1 and TRPV1, two molecular sensors and mediators of pain signals in dorsal root ganglia (DRG) neurons. Mechanistically, it weakens their interaction, thereby releasing the inhibition of TRPA1 by TRPV1 and increasing the single-channel open probability of the TRPA1-TRPV1 complex.
Subcellular location: Cell membrane; Multi-pass membrane protein. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Perikaryon. Cytoplasm, perinuclear region. Endoplasmic reticulum. Note=Colocalized with HSPA5 in the endoplasmic reticulum (ER). Enriched in ER microsome. Colocalized with BMP4 in neural cell bodies and neural fibers of the enteric nervous system.
Interaction partners:
Sequence:
MTEEPIKEILGAPKAHMAATMEKSPKSEVVITTVPLVSEIQLMAATGGTELSCYRCIIPFAVVVFIAGIVVTAVAYSFNSHGSIISIFGLVVLSSGLFLLASSALCWKVRQRSKKAKRRESQTALVANQRSLFA
Protein: Tubulin polyglutamylase TTLL11 (EC 6.3.2.-) (Tubulin--tyrosine ligase-like protein 11) (A4Q9F4)
Organism: Mus musculus (Mouse)
Function: Polyglutamylase which modifies tubulin, generating polyglutamate side chains of variable lengths on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of tubulin. Preferentially mediates ATP-dependent polyglutamate long side-chain elongation over the initiation step of the polyglutamylation reaction. Preferentially modifies the alpha-tubulin tail over a beta-tail. Required for CCSAP localization to both spindle and cilia microtubules (By similarity). Promotes tubulin polyglutamylation which stimulates spastin/SPAST-mediated microtubule severing, thereby regulating microtubule functions.
Subcellular location: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton {ECO:0000305|PubMed:20530212}.
Interaction partners:
Sequence:
MRRSSPEKKPEAEWEADAAAAAAATAAATESLPAETEKQQGVDAGAAGDPERLELEEQPKDVGRIPTPTRRHAPEEGEARVVRRLPPALPLAQPRPAARALSQLVKARGRSRSRVYRRSAGSMRPVTVDSSKARTSLDALKISLRQLRWKEFPFGRRLPCDIYWHGVSFRDSDILSGQVNKFPGMTEMVRKVTLSRALRIMQNLFPEEYNFYPRSWILPEEFQLFVSQVQTVKEGDPSWKPTFIVKPDSGCQGDGIYLIKDPCDGRLTGTLHNRPAVVQEYIRKPLLIDKLKFDIRLYVLLKSLDPLEIYIAKDGLSRFCTEPYQEPNPQNLHHVFMHLTNYSLNIHSGKFVHSDSASTGSKRTFSSILCRLSSKGVDIKKVWSDIISLVIKTVIALTPELKVFYQSDIPTGRPGPTCFQILGFDILLMKNLKPMLLEVNANPSMRIEHEYELSPGVFENIPSLVDEEVKVAVIRDTLRLMDPLKKKKEIHFPDIYMDRKHRIPPVSDRMSSWKHKGSSLSIVRSQQMEKSFTSKEDLNCDPTGGDSEPNPEAHLPSICLKQVFPKYAKQFNYLRLVDRMANLFIRFLGIKGTMKLGPTGFRTFIRNCKLSSSSLSMAAVDILYIDITRRWNSVTVDQRDSGMCLQAFVEAFFFLAQRKFKLQPLHEQVASLIDLCEYHLSVLDEKRLLCHRGRPLQRNPPQMNRPEHSATGSSAPRVIGASKLSQS
Protein: Hector, isoform A (Hector, isoform B) (Q9VYH9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Furrowed, isoform A
- DNA-directed RNA polymerase III subunit RPC9
Sequence:
MATTSSDSESQNVDVASQAQTQDNLRIFLKHLYAECVFRYQNVTYDTDDPSFSLGPATDYDSDLPENFSPVPRYLENAAMNEGVIDMRNVDEELAEKEELMATVVSATMATNQKENRLFCPLNFDGYLCWPRTPAGTVLSQYCPDFVEGFNRKFLAHKTCLENGSWYRHPVSNQTWSNYTNCVDYEDLEFRQFINELYVKGYALSLLALLISIIIFLGFKSLRCTRIRIHVHLFASLACTCVAWILWYRLVVERSETIAENPLWCIGLHLVVHYFMLVNYFWMFCEGLHLHLVLVVVFVKDTIVMRWFIVISWFSPIPIAIVYGLARHFSSPDNKHCWITDSLYLWIFSVPITLSLLASFIFLINVLRVIVRKLHPQSAQPAPLAIRKAVRATIILVPLFGLQHFLLPYRPDAGTQLDHFYQMLSVVLVSLQGFVVSFLFCFANHDVTFAIRTLLNKLLPSLVTPPPAGSNTGQMATTTPSRELGV
Protein: Lecithin retinol acyltransferase b, tandem duplicate 1 (Lecithin retinol acyltransferase-like) (A0A2R8PZT4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MLDSLSLLLEKTLLLAHFNFFSTTSSKQERCTKRREESTYFQRGDLLEVPRTLFTHFGIYLGDNKVAHLMPDILPVLTSNKSHLQNVVTNKRLLLGVLYKYASVRVDTVEDFAYGSNILLNTMDTTLRKQPLAAEEVARRAEKLVGHFPYSLMWNNCEHFVTYCRYGTAVSLQTDQFCESLKSIIRDQRSILLTTVIGMLSMFFVGIAPSTALPTFIIPFILWMAG
Protein: tRNA wybutosine-synthesizing protein 4 (tRNA yW-synthesizing protein 4) (EC 2.1.1.290) (EC 2.3.1.231) (tRNA(Phe) (7-(3-amino-3-(methoxycarbonyl)propyl)wyosine(37)-N)-methoxycarbonyltransferase) (tRNA(Phe) (7-(3-amino-3-carboxypropyl)wyosine(37)-O)-methyltransferase) (Q08282)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: S-adenosyl-L-methionine-dependent methyltransferase that acts as a component of the wybutosine biosynthesis pathway. Wybutosine is a hyper modified guanosine with a tricyclic base found at the 3'-position adjacent to the anticodon of eukaryotic phenylalanine tRNA. Catalyzes the final 2 independent reactions, methylation of the alpha-carboxy group of wybutosine-72 to form wybutosine-58, and methoxycarbonylation of alpha-amino group of wybutosine-58 through the fixation of CO(2) to complete wybutosine.
Subcellular location: Cytoplasm. Mitochondrion.
Interaction partners:
- tRNA wybutosine-synthesizing protein 2
- tRNA wybutosine-synthesizing protein 3
- S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase
- tRNA
- Large ribosomal subunit protein mL49
Sequence:
MKNLTTIKQTNKNVKQERRKKYADLAIQGTNNSSIASKRSVELLYLPKLSSANNFQMDKNNKLLEYFKFFVPKKIKRSPCINRGYWLRLFAIRSRLNSIIEQTPQDKKIVVVNLGCGYDPLPFQLLDTNNIQSQQYHDRVSFIDIDYSDLLKIKIELIKTIPELSKIIGLSEDKDYVDDSNVDFLTTPKYLARPCDLNDSKMFSTLLNECQLYDPNVVKVFVAEVSLAYMKPERSDSIIEATSKMENSHFIILEQLIPKGPFEPFSKQMLAHFKRNDSPLQSVLKYNTIESQVQRFNKLGFAYVNVGDMFQLWESADEATKKELLKVEPFDELEEFHLFCHHYVLCHATNYKEFAFTQGFLFDRSISEINLTVDEDYQLLECECPINRKFGDVDVAGNDVFYMGGSNPYRVNEILQLSIHYDKIDMKNIEVSSSEVPVARMCHTFTTISRNNQLLLIGGRKAPHQGLSDNWIFDMKTREWSMIKSLSHTRFRHSACSLPDGNVLILGGVTEGPAMLLYNVTEEIFKDVTPKDEFFQNSLVSAGLEFDPVSKQGIILGGGFMDQTTVSDKAIIFKYDAENATEPITVIKKLQHPLFQRYGSQIKYITPRKLLIVGGTSPSGLFDRTNSIISLDPLSETLTSIPISRRIWEDHSLMLAGFSLVSTSMGTIHIIGGGATCYGFGSVTNVGLKLIAIAK
Protein: mRNA decay factor CTH2 (Cysteine-three-histidine protein 2) (Protein TIS11 homolog) (Protein YTIS11) (TPA-induced sequence protein 11) (P47977)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to specific AU-rich elements (ARE) in the 3'-untranslated region of target mRNAs and promotes their degradation. In response to iron deficiency, promotes the decay of many mRNAs encoding proteins involved in iron-dependent pathways. Recruits the DHH1 helicase to the SDH4 mRNA and promotes SDH4 mRNA decay. Also destabilizes target mRNA by modulating 3'-end processing, creating extended transcripts that are prone for degradation.
Subcellular location: Nucleus {ECO:0000269|PubMed:18923425}. Cytoplasm, P-body {ECO:0000269|PubMed:18715869}.
Interaction partners:
- Iron-regulated transcriptional activator AFT1
- NifU-like protein
- ATP-dependent RNA helicase DHH1
- Aconitate hydratase, mitochondrial
- Facilitator of iron transport 2
- Iron-regulated transcriptional activator AFT2
- Iron transport multicopper oxidase FET3
- 5'-3' exoribonuclease 1
- Siderophore iron transporter ARN1
- Siderophore iron transporter 1
Sequence:
MWAQLSYTRPESQKTDLTSLFSTDQEQNPLNDYQYQINIRELEEYYNKTILNEDNIQETSSEISSAVSFSPPKNTNAIQPGLLYDPQLMNPFLPSAHLNSTAPTTFKKKLEVQINPDYVPKSSQLPLTSQNLQQLSQQKPKNDASFSSEKESSAQPKVKSQVQETPKQLYKTELCESFTLKGSCPYGSKCQFAHGLGELKVKKSCKNFRTKPCVNWEKLGYCPYGRRCCFKHGDDNDIAVYVKAGTYCNVSSTSKQSDEKRSNGRGSAKKKNLNVKVKALQRMTW
Protein: Protein TPLATE (F4J8D3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions in vesicle-trafficking events required for site-specific cell wall modifications during pollen germination and for anchoring of the cell plate to the mother wall at the correct cortical position.
Subcellular location: Cytoplasm, cytoskeleton, phragmoplast {ECO:0000269|PubMed:15469496, ECO:0000269|PubMed:17189342, ECO:0000269|PubMed:21187379}. Note=Localized in the forming cell plate and the cortical division zone (CDZ) during cytokinesis.
Interaction partners:
- Bystin
- Periodic tryptophan protein 2
- At3g49990
- Putative U3 small nucleolar ribonucleoprotein
- Transducin family protein / WD-40 repeat family protein
- Putative WD-repeat membrane protein
- At1g42440/F7F22_7
- Probable cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG6
- Protein NUCLEOLAR COMPLEX ASSOCIATED 4
- At3g13230
Sequence:
MDILFAQIQADLRSNDALRQSSALLQALQQSAAGRDISVIAKSAVEEIVASPASAVCKKLAFDLIRSTRLTPDLWDTVCSGVKTDLHFPDPDVTAAAVSILAALPAFSLPKLISDCSSEIASCFDSPSDNLRFSITETLGCILARDDLVTLCENNVGLLDKVSNWWARIGQNMLDKSDAVSKVAFESVGRLFQEFDSKRMSRLAGDKLVDSENSLAIRSKWVSSMVDIVWRKRSALMARSLVLPVETFRATVFPLVFAVKAVASGSVEVIRQLSKASSAAAAANATVVDSNAEKLVGVSDLVTHLAPFLASSLDPALIFEVGINMLYLADVAGGKPEWASQSIIAILTLWDRQEFSSARESIVRAVVTNLHLLDLHMQVSLFRRLLLMVRNLRAESDRMHALACICRTALCVHLFARESARRGQKPLPGTDIISLFEDARIKDDLNSVTSKSLFREELVAMLVESCFQLSLPLPEQKNSGMESRVIGALAYGTGYGALNWTEPALEVVEVCRPCVKWDCDGRTYAVDCYLKLLVRLCHIYDTRGGVKRLKDGASQDQILNETRLQNLQRELVKDLQEVNTPRILGRLIWTIAEHIDLEGLDPLLADDPDDPLNIIIANIHKVLFNLDAAATTSNRLQDVQAVLLCAQRMGSRHARAGQLLTKELEEYRNHAAADTVSKHQTRLILQRIKYVSNLPERKWAGVSETRGDYPFSHHKLTVQFYEPSAAQDRKLEGLIHKAILELWRPKPTELTLFLTKGVDSTSIKVPPTAYPLTGSSDPCYIEAYHLADTNDGRVTLHLKIINLTELELNRVDIRVGLSGALYFMDGSPQAVRQLRNLVSQDPVQCSVTVGVSQFERCGFWVQVLYYPFRGARGEYDGDYIEEDPQIMKQKRGSKAELGEPVILRCQPYKIPLTELLLPHKISPVEFFRLWPSLPAVAEYTGTYMYEGSGFMATAAQQYGASPFLSGLKSLSSKPFHRVCSHIIRTVAGFQLCYAAKTWHGGFVGMMIFGASEVSRNMDLGDETTTMMCKFVVRASEASITKQIESDIQGWCDDLTDGGVEYMPEDEVKATAAEKLKISMERIALLKAAQPKKTSKIEEESENEEEEEGEEEDDDEEVKEKKEKEEGKDKEEKKKKEKEKGTFSKLTAEETEHMALQAAVLQEWHILCKDRKYTKVN
Protein: 5-amino-6-(5-phospho-D-ribitylamino)uracil phosphatase YigB (EC 3.1.3.104) (P0ADP0)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dephosphorylation of 5-amino-6-(5-phospho-D-ribitylamino)uracil, and thus could be involved in the riboflavin biosynthesis pathway. Is also able to dephosphorylate flavin mononucleotide (FMN) and other phosphoric acid esters. YigB is important for the formation of dormant persister cells.
Interaction partners:
- 5-amino-6-
- Riboflavin biosynthesis protein RibD
- 6,7-dimethyl-8-ribityllumazine synthase
- Bifunctional riboflavin kinase/FMN adenylyltransferase
- Riboflavin synthase
- FMN reductase
- NAD
- Class B acid phosphatase
- Phytase AppA
- Tyrosine recombinase XerC
Sequence:
MRFYRPLGRISALTFDLDDTLYDNRPVILRTEREALTFVQNYHPALRSFQNEDLQRLRQAVREAEPEIYHDVTRWRFRSIEQAMLDAGLSAEEASAGAHAAMINFAKWRSRIDVPQQTHDTLKQLAKKWPLVAITNGNAQPELFGLGDYFEFVLRAGPHGRSKPFSDMYFLAAEKLNVPIGEILHVGDDLTTDVGGAIRSGMQACWIRPENGDLMQTWDSRLLPHLEISRLASLTSLI
Protein: Butyrate kinase 1 (BK 1) (BKI) (EC 2.7.2.7) (Q45829)
Organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)
Function: Catalyzes the conversion of butyryl-CoA through butyryl phosphate to butyrate.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Phosphate butyryltransferase
- Phosphate acetyltransferase
- Butyrate kinase 2
- Pyruvate:ferredoxin oxidoreductase
- Acetyl-CoA acetyltransferase
- Acyl-CoA dehydrogenase, short-chain specific
- 3-hydroxybutyryl-CoA dehydrogenase
- Short-chain-enoyl-CoA hydratase
- Pyruvate:ferredoxin oxidoreductase
- NADH-dependent butanol dehydrogenase A
Sequence:
MYRLLIINPGSTSTKIGIYDDEKEIFEKTLRHSAEEIEKYNTIFDQFQFRKNVILDALKEANIEVSSLNAVVGRGGLLKPIVSGTYAVNQKMLEDLKVGVQGQHASNLGGIIANEIAKEINVPAYIVDPVVVDELDEVSRISGMADIPRKSIFHALNQKAVARRYAKEVGKKYEDLNLIVVHMGGGTSVGTHKDGRVIEVNNTLDGEGPFSPERSGGVPIGDLVRLCFSNKYTYEEVMKKINGKGGVVSYLNTIDFKAVVDKALEGDKKCALIYEAFTFQVAKEIGKCSTVLKGNVDAIILTGGIAYNEHVCNAIEDRVKFIAPVVRYGGEDELLALAEGGLRVLRGEEKAKEYK
Protein: Cystatin cpi-2 (Ce-cpi-2a) (Cysele2) (G5ECM9)
Organism: Caenorhabditis elegans
Function: Cysteine protease inhibitor which inhibits members of the peptidase C1 family. Does not inhibit asparaginyl endopeptidase. Required for the uptake and/or processing of yolk proteins during the development of oocytes, probably by regulating the catalytic activity of cysteine proteases cpl-1 and cpz-1. May play a protective role against exogenous cysteine proteases derived from soil bacteria or fungi, or rotting fruits and vegetation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16857685}. Secreted {ECO:0000269|PubMed:16857685}. Cytoplasmic granule {ECO:0000269|PubMed:16857685}. Note=Localizes to the sheath cell cytoplasm surrounding germ cells and oocytes. Localizes to yolk granules in the developing oocyte. {ECO:0000269|PubMed:16857685}.
Interaction partners:
- Neuropeptide-Like Protein
- Macrophage migration inhibitory factor
- legumain
- SCP domain-containing protein
- Cathepsin Z-1
Sequence:
MKAILVFALIAISIISVNAGMMTGGSVEQDASQKEYSDKAWKAVKGINDQASNNGPYYYAPIKVTKASTQVVAGISTKLEVLVGESNCKKGELQAHEITSSNCQIKDGGSRALYQVTIWEKPWENFEQFTVEKIRDVTADEQF
Protein: Toll-like receptor 9 (Q80XA5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046288}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00046288}.
Interaction partners:
Sequence:
SLIHLDLSQNKLHILRPQNLNYLPKSLTKLSFRDNHLSFFNWSSLAFLPNLRDLDLAGNLLKALTNGTLPNGTLLQKLDVSSNSIVFVVPAFFALAVELKEVNLSHNILKTVDRSWFGPIVMNLTVLDVSSNPLHCACGAPFVDLLLEVQTKVPGLANGVKCGSPRQLQGRSIFAQDLRLCLDDVLSRDCFGLSLLAVAVGTVLPLLQHLCGWDVWYCFHLCLAWLPLLTRGRRSAQALPYDAFVVFDKAQSAVADWVYNELRVRLEERRGRRALRLCLEDRDWLPGQTLFENLWASIYGSRKTLFVLAHTDKVSGLLRTSFLLAQQRLLEDRKDVVVLVILRPDAHRSRYVRLRQRLCRQSVLFWPHQPNGQGSFWAQLSTALTRDN
Protein: Adenosine receptor A1 (P30542)
Organism: Homo sapiens (Human)
Function: Receptor for adenosine. The activity of this receptor is mediated by G proteins which inhibit adenylyl cyclase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27134041}; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Kininogen-1
- Guanine nucleotide-binding protein G
- Adenosine receptor A3
- Equilibrative nucleoside transporter 1
- Adenosine deaminase
- Guanine nucleotide-binding protein G
- Adenosine receptor A2a
Sequence:
MPPSISAFQAAYIGIEVLIALVSVPGNVLVIWAVKVNQALRDATFCFIVSLAVADVAVGALVIPLAILINIGPQTYFHTCLMVACPVLILTQSSILALLAIAVDRYLRVKIPLRYKMVVTPRRAAVAIAGCWILSFVVGLTPMFGWNNLSAVERAWAANGSMGEPVIKCEFEKVISMEYMVYFNFFVWVLPPLLLMVLIYLEVFYLIRKQLNKKVSASSGDPQKYYGKELKIAKSLALILFLFALSWLPLHILNCITLFCPSCHKPSILTYIAIFLTHGNSAMNPIVYAFRIQKFRVTFLKIWNDHFRCQPAPPIDEDLPEERPDD
Protein: Endonuclease 3 (AtENDO3) (EC 3.1.30.1) (Deoxyribonuclease ENDO3) (Single-stranded-nucleate endonuclease ENDO3) (Q8LDW6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Endonuclease that can use RNA and single-stranded DNA as substrates. In contradiction with PubMed:23620482, cannot hydrolyze single-stranded DNA and does not cleave mismatches.
Interaction partners:
- DNA damage-repair/toleration protein DRT100
- DNA topoisomerase 1 beta
- Nucleolar-like protein
Sequence:
MGWSLRMWIVSILVLTQLVNGALCWGDAGHYAVCKIAQSYFEEDTVVAVKKLLPESANGELAAVCSWPDEIKKLPQWRWTSALHFADTPDYKCNYEYSRDCPKDWCVTGAIFNYTNQLMSTSENSQSIVHYNLTEALMFLSHYMGDIHQPLHEGFIGDLGGNKIKVHWYNQETNLHRVWDDMIIESALETYYNSSLPRMIHELQAKLKNGWSNDVPSWESCQLNQTACPNPYASESIDLACKYAYRNATAGTTLGDYYFVSRLPVVEKRLAQGGIRLAGTLNRIFSAKRKLARA
Protein: Plexin domain-containing protein 2 (Tumor endothelial marker 7-related protein) (Q9DC11)
Organism: Mus musculus (Mouse)
Function: May play a role in tumor angiogenesis.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Pigment epithelium-derived factor
Sequence:
MARFRRADLAAAGVMLLCHFLTDRFQFAHGEPGHHTNDWIYEVTNAFPWNEEGVEVDSQAYNHRWKRNVDPFKAVDTNRASMGQASPESKGFTDLLLDDGQDNNTQIEEDTDHNYYISRIYGPADSASRDLWVNIDQMEKDKVKIHGILSNTHRQAARVNLSFDFPFYGHFLNEVTVATGGFIYTGEVVHRMLTATQYIAPLMANFDPSVSRNSTVRYFDNGTALVVQWDHVHLQDNYNLGSFTFQATLLMDGRIIFGYKEIPVLVTQISSTNHPVKVGLSDAFVVVHRIQQIPNVRRRTIYEYHRVELQMSKITNISAVEMTPLPTCLQFNGCGPCVSSQIGFNCSWCSKLQRCSSGFDRHRQDWVDSGCPEEVQSKEKMCEKTEPGETSQTTTTSHTTTMQFRVLTTTRRAVTSQMPTSLPTEDDTKIALHLKDSGASTDDSAAEKKGGTLHAGLIVGILILVLIIAAAILVTVYMYHHPTSAASIFFIERRPSRWPAMKFRRGSGHPAYAEVEPVGEKEGFIVSEQC
Protein: NEDD4-binding protein 2-like 2 (Phosphonoformate immuno-associated protein 5) (Q92802)
Organism: Homo sapiens (Human)
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 7
Sequence:
MSYGEIEGKFLGPREEVTSEPRCKKLKSTTESYVFHNHSNADFHRIQEKTGNDWVPVTIIDVRGHSYLQENKIKTTDLHRPLHDEMPGNRPDVIESIDSQVLQEARPPLVSADDEIYSTSKAFIGPIYKPPEKKKRNEGRNEAHVLNGINDRGGQKEKQKFNSEKSEIDNELFQFYKEIEELEKEKDGFENSCKESEPSQEQFVPFYEGHNNGLLKPDEEKKDLSNKAMPSHCDYQQNLGNEPDKYPCNGQVIPTFCDTSFTSFRPEWQSVYPFIVPYGPPLPSLNYHLNIQRFSGPPNPPSNIFQAQDDSQIQNGYYVNNCHVNWNCMTFDQNNEYTDCSENRSSVHPSGNGCSMQDRYVSNGFCEVRERCWKDHCMDKHNGTDRFVNQQFQEEKLNKLQKLLILLRGLPGSGKTTLSRILLGQNRDGIVFSTDDYFHHQDGYRYNVNQLGDAHDWNQNRAKQAIDQGRSPVIIDNTNIQAWEMKPYVEVAIGKGYRVEFHEPETWWKFDPEELEKRNKHGVSRKKIAQMLDRYEYQMSISIVMNSVEPSHKSTQRPPPPQGRQRWGGSLGSHNRVCVTNNH
Protein: Protein ORANGE-ORANGE, chloroplastic (CmOr-orange) (DnaJ-like cysteine-rich domain-containing protein Or) (A0A0D3MU50)
Organism: Cucumis melo (Muskmelon)
Function: Triggers accumulation of carotenoids, mainly beta-carotene, in fruit flesh.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305|PubMed:25754094}.
Interaction partners:
Sequence:
MDRVLVASYPINHLIRPHSFRIDYCWSTCFTSRLNSGKERQKLSSRWRWRSMASDSTDSSSSSSFAPSVESDPSDKTSASFCIIEGPETVQDFAKMELQEIQENIRSHRNKIFLHMEEVRRLRIQQRIKNAELGISKEERENELPNFPSFIPFLPPLSSENLKLYYVTCYSLIAGIILFGGLLAPTLELKLGLGGTSYEDFIRSVHLPMQLSQVDPIVASFSGGAVGVISALMVVEVNNVKQQEHKRCKYCLGTGYLACARCSNTGALVLIEPVSTLNGEHQPLSLPKTERCQNCSGSGKVMCPTCLCTGMAMASEHDPRIDPFD
Protein: LD45876p (Q8MSA6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MVRNSFIVELVDGHRKLRHLFLFNDVIACAKYKALGRDRIDYELKWFIPLKDVSIYEEADPAVELKESSPANISQVKRNLRSVRDQLAMEVANSGSGAFRSGDKYRRKLADLESQLVLATPNLVLRLGNKANNKTITFFLSSDFERTQWIDSILSLKQKCNLPGANTINSLEVTAFIVAMQKGMKTEMGSYLMRNTNDESLLVGDLYMGVHGLEGLEQANDLYICVEVDSYGHYFRKATTKKICRSQTPLWNESFMLELEGSQNVRILLYEAKERPLLKAKHILKLSLSWLTETTQPKSIKLTETLELGCSFRFIPGELFRGSTKPGALFGAKMSQVLKREKRDIPFIIGACIREVERRGMLEVGCYRVSGSASDLAKLKKAFESDAYEAEQLLREVDIHSVTGILKTFLRELPEALFTDQLYPRFFDTFSAFSNNNESTRINELLKVFEELPQANKASITSILDHLIRVHEKETDNKMSLHNLAMVFGPTLLRPGQTQVKQKDPLAASTVDVMAQAGILYCFLQARIKKD
Protein: Probable conserved transmembrane protein (O05579)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable conserved lipoprotein LppL
- Probable membrane protein
- Conserved alanine valine rich protein
- Molybdopterin molybdenumtransferase 1
- Probable conserved transmembrane protein
- Conserved protein
- Heparin-binding hemagglutinin
- Possible conserved secreted protein
- Conserved protein
- Uncharacterized protein Rv0481c
Sequence:
MPSIPQSLLWISLVVLWLFVLVPMLISKRDAVRRTSDVALATRVLNGGAGARLLKRGGPAAGHRWGYLPPEGQGDDPDWKPEEDWRDDPVEDGFADVEHDIDEDQEADDARRRGAVVMKVAAPQTAGADEPDYLDVDVVEEDSEALPVGAGAAVGESADEADAEAADGVAGHADPEADPVEYEYEYEYVEDTCGLELEEDDQEAPPTVASGTSRRRRFDTKTAAAVSARKYTFRKRALIVMAVILVGSAAAAFELTPVAWWICGSATGVTVLYLAYLRRQTRIEEKVRRRRMQRIARARLGVENTRDREYDVVPSRLRRPGAVVLEIDDEDPIFTHLESAAPIRNYGWPRDLPRAVGQ
Protein: histidine kinase (EC 2.7.13.3) (G3XCM7)
Organism: Pseudomonas aeruginosa
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLTSFSLTQLILISVTYLSTLFGIAWITERGYVPRRLVRHPLVYTLSLGVYASAWAFYGTVGLAYQYGYGFLAIYLGISGAFLLAPVLLYPILRVTRAYQLSSLADLFAFRFRSTWAGALTTLFMLIGVLPMLALQIQAVTDSISILTRDPAQERVAFVFCTLITLFAILFGARHIATRERHEGLVFAIAFESLVKLVMLGSIGLYALYGVFGGPEGLEVWLLQNQTALTTLHTPLAEGPWRTLLLVFFAAAIVMPHMFHMIFTENLNPRALISASWGLPLFLLLMSLAVPPILWAGLRLGASTTPEYYTIGLGLAVDSPALALAAFIGGISAASGLTIVMTLALSGMVLNHLVLPLYQPPAQGNIYRWLKWTRRLLIVAIIMASYAFYLLLGAEQDLSNLGIVSFVATLQFLPGALSVLYWPTANRRGFISGLIAGMLVWAITMLLPLMGNVQGLYLPLFDVIYVLDDSNWHLAALSSLAANVLVFTLVSLFTEASDEEKGAAEACAVDNVRRPQRRELFAGSPQEFASQLAKPLGAKTAQKEVEQALRDLHLPFDERRPYALRRLRDRIEANLSGLMGPSVAQDIVETFLPYKTSEESYVTEDIHFIESRLEDYHSRLTGLAAELDTLRRYHRQTLQDLPMGVCSLAKDQEVLMWNRAIEELTGVGAQKVVGSRLSALPEPWKGLLERFIDAPDEHLHKQRLVYDGHTRWLNLHKAAIEEPLAPGNSGLVLLVEDLTETQLLEDKLVHSERLASIGRLAAGVAHEIGNPITGIACLAQNLREEREGDGELTEISEQILDQTKRVSRIVQSLMSFAHSGSHLQALEPVCLSEVAQEAIGLLSLNRRSVEVEFFNLCDPAHWVEGDSQRLAQVLINLLSNARDASPPGGAIRVRSEASEHTVDLVVEDEGSGIPKAIMDQLFEPFFTTKDPGKGTGLGLALVYSIVEEHYGQITIESPTDHQREGGTRFRVTLPRHPGPTAEL
Protein: GH22749p (Q9VUL6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSCLVGNRKRNSGSTADEFDKVSTLANADDTECVSPDPGREPESNKPDSQTEPEFGHLNETRRKILDAIAALNDDSFDKRMARLLMQYEGAIREEFQRAQYLPQKCRKLARILTGLTDVIHTMVQGRALQRDESYRQRMCNIVGFYISCELCSAQEPVEKEETIINRINSCLKLYVEYGDGGAGVHREHVLRTLLAAPKLFNRASILSMLYSRLFPHWSVPSVMIQAELPDKLYIEYILIFYYWQRLESDESVKERIVQFAEKFMRPSRSLAIKSVYAHYLPKFTDQNAATRTILNHLRMSSCTSLHVVSKVDNRPPQSNEVVLSSDDEDSCPMWDISGTPTSSIYNHPPVFLQNLCQNARQLEPCKRANVLFSGIDNSMEIVELRDSDDDVEMFSVNFNVPANVDGINSNSNSNDSANQTSTTILCDDDSVPVTRIYPSNLRTYERTVLPPTTYTVPRIVNSYSCRRDSLHLVSTTAPHLVDQCVQTLDDEEQDLVEEDQYSGAHSHGFFPRSSNASYASGQRTPLYHCRQTSSQNSNCSESSLLKKQVTFSPRHLGAATPNAKTGTSKKPSIKQYKPSSSNATESQRWKEEHRKASAKMFAKLDAKIKARSEAENVSTSQLTPTTSNASSSTPTKISGTPTRIRSTQRGQRVALPTPPASTHSSSSPCQIRSASTDNHNYNVDSDYSRRCFSKAAGDEVSYYNHLLTLQRENIRRRRLNNQKKKKNRKVSQKVQKKDDKLNMLKQATKRCRKLRALNAKRKNEVQKLEQDLDTIRKSAPHKLPIIRLKRCNLKTQKRSLKAEEAPSVQEDILSMNSDRELQEQKKAQKPKRKRYKKVQKEQENEKYLREQEIIISQSQMVEEDKVEEHHAHEAPSEQQRELDLEHQQFLEEQLLQEEHQLAMHEEEHHQMDDEQESHEVARLLEDQQPAEGTHLHVENEMLAEKEQPLIEDDDQEADDQNQNEHLSDDQQQEADQQLSIEQPQEHEENQSLSQDPLDEQCTPTPNGKRRKRRRRFKRRCWTHVKNKKKKQWLIDYPLEFEADPALDTPPIQPEPAPDEQQAELVTGPVSESVAEPVAEPVAEPVSEPFAEQIAEPIAQPTPEPAYDFDQDLVPEVGNELEIAAPIRVAEDEDSTAILSPSHNLELVTSHVPVYLLNGESRDVSTPLSSSSYSAGGSEIYASSKDLV
Protein: Large ribosomal subunit protein uL23 (60S ribosomal protein L23a) (P62750)
Organism: Homo sapiens (Human)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds a specific region on the 26S rRNA. May promote p53/TP53 degradation possibly through the stimulation of MDM2-mediated TP53 polyubiquitination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:9687515}. Nucleus {ECO:0000269|PubMed:9687515}. Note=Although RPL23A is functional within the cytoplasm, the assembly of ribosomal subunits occurs in the nucleus. RPL23A nuclear import is mediated by IPO5/RanBP5, IPO7/RanBP7, KPNB1/importin-beta or TPNO1/Trn. {ECO:0000269|PubMed:11682607, ECO:0000269|PubMed:9687515}.
Interaction partners:
- Small ribosomal subunit protein eS17
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein bL36m
- Small ribosomal subunit protein eS7
- Small ribosomal subunit protein eS4, X isoform
- Large ribosomal subunit protein uL4
- Large ribosomal subunit protein P1
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein eS28
- Proliferation-associated protein 2G4
Sequence:
MAPKAKKEAPAPPKAEAKAKALKAKKAVLKGVHSHKKKKIRTSPTFRRPKTLRLRRQPKYPRKSAPRRNKLDHYAIIKFPLTTESAMKKIEDNNTLVFIVDVKANKHQIKQAVKKLYDIDVAKVNTLIRPDGEKKAYVRLAPDYDALDVANKIGII