wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein ligase TRIM23 (EC 2.3.2.27) (ADP-ribosylation factor domain-containing protein 1) (GTP-binding protein ARD-1) (RING-type E3 ubiquitin transferase TRIM23) (Tripartite motif-containing protein 23) (P36407)
Organism: Rattus norvegicus (Rat)
Function: Acts as an E3 ubiquitin-protein ligase. Plays an essential role in autophagy activation during viral infection. Mechanistically, activates TANK-binding kinase 1/TBK1 by facilitating its dimerization and ability to phosphorylate the selective autophagy receptor SQSTM1. In order to achieve this function, TRIM23 mediates 'Lys-27'-linked auto-ubiquitination of its ADP-ribosylation factor (ARF) domain to induce its GTPase activity and its recruitment to autophagosomes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P36406}. Endomembrane system {ECO:0000250|UniProtKB:P36406}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P36406}. Lysosome membrane {ECO:0000250|UniProtKB:P36406}. Note=Membrane-associated with the Golgi complex and lysosomal structures. {ECO:0000250|UniProtKB:P36406}.
Interaction partners:
- Ubiquitin-ribosomal protein eL40 fusion protein
- Thioredoxin domain-containing protein 3
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Intersectin 2
- Intersectin-1
- Polyubiquitin-C
Sequence:
MAALAVNKPGAGVDSGRQGSRGTAVVKVLECGVCEDVFSLQGDKVPRLLLCGHTVCHDCLTRLPLHGRAIRCPFDRQVTDLGDSGVWGLKKNFALLELLERLQNGHIGQYGAAEEALGISGESIIRCDEDEAHVASVYCTVCATHLCSECSQVTHSTKTLAKHRRVPLADKPHEKTMCCQHQVHAIEFVCLEEACQTSPLMCCVCKEYGKHQGHKHSVLEPEANQIRASILDMAHCIRTFTEEISDYSRKLVGIVQHIEGGEQIVEDGIGMAHTEHVPGTAENARSCVRAYFSDLHETLCRQEEMALSVVDAHVREKLIWLRQQQEDMTILLSQVSTACLHCKTLQQDDCRVVLAKQEITRLLETLQKQQQQFTEVADHIQLDASIPVTFTKDNRVYHGPKMEIRVVTLGLDGAGKTTILFKLKQDEFMQPIPTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVVDSSHRDRISEAHSELAKLLTEKELRDALLLIFANKQDVAGALSVEEITELLSLHKLCCGRSWYIQGCDARSGMGLYEGLDWLSRQLVAAGVLDVA
Protein: tRNA methyltransferase 10 homolog C (HBV pre-S2 trans-regulated protein 2) (Mitochondrial ribonuclease P protein 1) (Mitochondrial RNase P protein 1) (RNA (guanine-9-)-methyltransferase domain-containing protein 1) (Renal carcinoma antigen NY-REN-49) (mRNA methyladenosine-N(1)-methyltransferase) (EC 2.1.1.-) (tRNA (adenine(9)-N(1))-methyltransferase) (EC 2.1.1.218) (tRNA (guanine(9)-N(1))-methyltransferase) (EC 2.1.1.221) (Q7L0Y3)
Organism: Homo sapiens (Human)
Function: Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation. Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends. Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity. The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N(1)-methyltransferase subunit. The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme. In addition to tRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA. Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly.
Subcellular location: Mitochondrion matrix, mitochondrion nucleoid {ECO:0000269|PubMed:18984158, ECO:0000269|PubMed:23473034, ECO:0000269|PubMed:24703694}.
Interaction partners:
- 3-hydroxyacyl-CoA dehydrogenase type-2
- Mitochondrial ribonuclease P catalytic subunit
- tRNA
- tRNA
- Ribosome production factor 1
- tRNA
- tRNA
- Zinc phosphodiesterase ELAC protein 2
- tRNA
- Fibrous sheath-interacting protein 1
Sequence:
MAAFLKMSVSVNFFRPFTRFLVPFTLHRKRNNLTILQRYMSSKIPAVTYPKNESTPPSEELELDKWKTTMKSSVQEECVSTISSSKDEDPLAATREFIEMWRLLGREVPEHITEEELKTLMECVSNTAKKKYLKYLYTKEKVKKARQIKKEMKAAAREEAKNIKLLETTEEDKQKNFLFLRLWDRNMDIAMGWKGAQAMQFGQPLVFDMAYENYMKRKELQNTVSQLLESEGWNRRNVDPFHIYFCNLKIDGALHRELVKRYQEKWDKLLLTSTEKSHVDLFPKDSIIYLTADSPNVMTTFRHDKVYVIGSFVDKSMQPGTSLAKAKRLNLATECLPLDKYLQWEIGNKNLTLDQMIRILLCLKNNGNWQEALQFVPKRKHTGFLEISQHSQEFINRLKKAKT
Protein: NHS-like protein 2 (Q5HYW2)
Organism: Homo sapiens (Human)
Interaction partners:
- Actin-binding protein WASF2
- Nck-associated protein 1
- Cytoplasmic FMR1-interacting protein 1
Sequence:
MPFYRRTVVPQRLCPRNPPQQLAELRDVSHLAALSLLRQLADLCGHSLALLEDLEGHLLALGRRTDSLYRRTVRLRRRLPCRLLGPEEDEEELAAANSGRENATATAHSRSSWRQPVNVFLSSGRPPSVEELLREAQLNLQSLLQEEYEEQYSEARLVGQTFRSSDEATKPTPNPRPQSARRLEFILMPTKRQLSEDETTTQGVRAPEASLSLSTTADKQTAWNSLFPLPILEEKRWPQLCSTQSDIVPINISGQQFDKHASLRHSLFNTETAVNPKSTLRRRRTIIGFSNFSQRDQGHSNSPAGSVAHSTTSDIRPSHSVPEGVHGRVAVGQDARFPSLTSPVLRTPSSEPDEPHQARSGPNPPGMESMGMVYSVPSSCNGPTESTFSTSWKGDAFTYMTPSATSQSNQVNENGKNPSCGNSWVSLNKVPPLVPKEAATLLVARDNPAGCSGSAGYPERLIQQRHMPERPSKIGLLTSGTSRLETGPGGASRFRERSLSVPTDSGTTDVDYDEEQKANEACALPFASTSSEGSNSADNIASLSAQQEAQHRRQRSKSISLRKAKKKPSPPTRSVSLVKDEPGLLPEGGSALPKDQRPKSLCLSLEHQGHHSSHPDAQGHPAIPNHKDPESTQFSHHWYLTDWKSGDTYQSLSSSSTATGTTVIECTQVQGSSESLASPSTSRATTPSQLSIEVEAREISSPGRPPGLMSPSSGYSSQSETPTPTVSMSLTLGHLPPPSSSVRVRPVVPERKSSLPPTSPMEKFPKSRLSFDLPLTSSPNLDLSGMSISIRSKTKVSRHHSETNFGVKLAQKTNPNQPIMPMVTQSDLRSVRLRSVSKSEPEDDIESPEYAEEPRAEEVFTLPERKTKPPVAEKPPVARRPPSLVHKPPSVPEEYALTSPTLAMPPRSSIQHARPLPQDSYTVVRKPKPSSFPDGRSPGESTAPSSLVFTPFASSSDAFFSGTQQPPQGSVEDEGPKVRVLPERISLQSQEEAEKKKGKIPPPVPKKPSVLYLPLTSPTAQMEAYVAEPRLPLSPIITLEEDTKCPATGDDLQSLGQRVTSTPQADSEREASPLGSSVEPGTEEKSLISDKTAEWIAEDDDDVFVASRTTEDLFTVIHRSKRKLLGWKEPGEAFVGGRTSSHSPIKNTAESPISESTATAGSGSSANLDAGRNDDFKALLQKKGSKATPRSRPSAAELLKTTNPLARRIIAQFSKDYETTDNPST
Protein: Proline-rich receptor-like protein kinase PERK10 (EC 2.7.11.1) (Proline-rich extensin-like receptor kinase 10) (AtPERK10) (Q9C660)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Could be involved in the negative regulation of root growth.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass membrane protein {ECO:0000250}.
Interaction partners:
- Serine/threonine-protein kinase KIPK2
- Serine/threonine-protein kinase KIPK1
- RING-H2 finger protein ATL72
- Kinesin-like protein KIN-14E
Sequence:
MTTPAQAPREEVSLSPSLASPPLMALPPPQPSFPGDNATSPTREPTNGNPPETTNTPAQSSPPPETPLSSPPPEPSPPSPSLTGPPPTTIPVSPPPEPSPPPPLPTEAPPPANPVSSPPPESSPPPPPPTEAPPTTPITSPSPPTNPPPPPESPPSLPAPDPPSNPLPPPKLVPPSHSPPRHLPSPPASEIPPPPRHLPSPPASERPSTPPSDSEHPSPPPPGHPKRREQPPPPGSKRPTPSPPSPSDSKRPVHPSPPSPPEETLPPPKPSPDPLPSNSSSPPTLLPPSSVVSPPSPPRKSVSGPDNPSPNNPTPVTDNSSSSGISIAAVVGVSIGVALVLLTLIGVVVCCLKKRKKRLSTIGGGYVMPTPMESSSPRSDSALLKTQSSAPLVGNRSSNRTYLSQSEPGGFGQSRELFSYEELVIATNGFSDENLLGEGGFGRVYKGVLPDERVVAVKQLKIGGGQGDREFKAEVDTISRVHHRNLLSMVGYCISENRRLLIYDYVPNNNLYFHLHAAGTPGLDWATRVKIAAGAARGLAYLHEDCHPRIIHRDIKSSNILLENNFHALVSDFGLAKLALDCNTHITTRVMGTFGYMAPEYASSGKLTEKSDVFSFGVVLLELITGRKPVDASQPLGDESLVEWARPLLSNATETEEFTALADPKLGRNYVGVEMFRMIEAAAACIRHSATKRPRMSQIVRAFDSLAEEDLTNGMRLGESEIINSAQQSAEIRLFRRMAFGSQNYSTDSLTRNSYISKDENL
Protein: Exodeoxyribonuclease 7 large subunit (EC 3.1.11.6) (Exodeoxyribonuclease VII large subunit) (ExoVII large subunit) (Exonuclease VII large subunit) (P04994)
Organism: Escherichia coli (strain K12)
Function: Bidirectionally degrades single-stranded DNA into large acid-insoluble oligonucleotides, which are then degraded further into small acid-soluble oligonucleotides. It can degrade 3' or 5' ss regions extending from the termini of duplex DNA molecules and displaced ss regions. It can also excise thymine dimers in vitro (Probable). ssDNA-binding requires both subunits. Required for production of the mature 5'-end of retron Ec78 or Ec83 msDNA. Overproduction of this subunit in the absence of an equivalent quantity of the small subunit is toxic, causing cell elongation and chromosome fragmentation or loss; its toxicity is mostly suppressed by RecA.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:6284744}.
Interaction partners:
- Exodeoxyribonuclease 7 small subunit
- Bifunctional protein FolD
- Single-stranded-DNA-specific exonuclease RecJ
- Exodeoxyribonuclease I
- Exodeoxyribonuclease 10
- DNA repair protein RecN
- ATP-dependent DNA helicase RecG
- Holliday junction branch migration complex subunit RuvA
Sequence:
MLPSQSPAIFTVSRLNQTVRLLLEHEMGQVWISGEISNFTQPASGHWYFTLKDDTAQVRCAMFRNSNRRVTFRPQHGQQVLVRANITLYEPRGDYQIIVESMQPAGEGLLQQKYEQLKAKLQAEGLFDQQYKKPLPSPAHCVGVITSKTGAALHDILHVLKRRDPSLPVIIYPAAVQGDDAPGQIVRAIELANQRNECDVLIVGRGGGSLEDLWSFNDERVARAIFTSRIPVVSAVGHETDVTIADFVADLRAPTPSAAAEVVSRNQQELLRQVQSTRQRLEMAMDYYLANRTRRFTQIHHRLQQQHPQLRLARQQTMLERLQKRMSFALENQLKRTGQQQQRLTQRLNQQNPQPKIHRAQTRIQQLEYRLAETLRAQLSATRERFGNAVTHLEAVSPLSTLARGYSVTTATDGNVLKKVKQVKAGEMLTTRLEDGWIESEVKNIQPVKKSRKKVH
Protein: cAMP-dependent protein kinase inhibitor alpha (PKI-alpha) (cAMP-dependent protein kinase inhibitor, muscle/brain isoform) (P63249)
Organism: Rattus norvegicus (Rat)
Function: Extremely potent competitive inhibitor of cAMP-dependent protein kinase activity, this protein interacts with the catalytic subunit of the enzyme after the cAMP-induced dissociation of its regulatory chains.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Exportin-1
- Protein kinase cAMP-dependent X-linked catalytic subunit
- cAMP-dependent protein kinase inhibitor
Sequence:
MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEDDGQRSSTEQSGEAQGEAAKSES
Protein: CcsA (Cytochrome c biogenesis protein) (C5MRH2)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLFATLEHILTHISFSTISIVITIHLITLLVRELGGLRDSSEKGMIATFFCITGFLVSRWASSGHFPLSNLYESLIFLSWALYILHMIPKIQNSKNDLSTITTPSTILTQGFATSGLLTEMHQSTILVPALQSQWLMMHVSMMLLSYATLLCGSLLSAALLMIRFRKNLDFFSKKKKNVLLKTFFFNEIEYFYAKRSALKSTFFPLFPNYYKYQLIERLDSWSYRVISLGFTLLT
Protein: DnaJ heat shock protein family (Hsp40) member C7 (K7EIH8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSTTGWEAETFKEQGNAYYAKKDYNEAYNYYTKAIDMCPKNASYYGNRAATLMMLGRFREALGDAQQSVRLDDSFVRGHLREGKCHLSLGNAMAACRSFQRALELDHKNAQAQQEFKNANAVMEYEKIAETDFEKRDFRKVVFCMDRALEFAPACHRFKILKAECLAMLGRYPEAQSVASDILRMDSTNADALYVRGLCLYYEDCIEKAVQFFVQALRMAPDHEKACIACRNAKALKAKKEDGNKAFKEGNYKLAYELYTEALGIDP
Protein: p140 (Q66542)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Subcellular location: Virion tegument {ECO:0000256|ARBA:ARBA00004535}.
Interaction partners:
Sequence:
MEERGRETQMPVARYGGPFIMVRLFGQDGEANIQEQRLYELLSDPRSALGLDPGPLIAENLLLVALRGTNNDPRPQRQERARELALVGILLGNGEQGEHLGTESALEASGNNYVYAYGPDWMARPSTWSAEIQQFLRLLGAAYVLRVEMGRQFGFEVHRSRPSFRQFQAINHLVLFDNALRKYDSGQVAAGFQRALLVAGPETADTRPDLRKLNEWVFGGRAAGGRQLADELKIVSALRDTYSGHLVLQPTETLDTWKVLSRDTRTAHSLEHGFIHAAGTIQANCPQLFMRRQHPGLFPFVNAIASSLGWYYQTATGPGADARAAAQRQQAFQTRAAAECHAKSGVPVVAGFYRTINATLKGGEGLQPTMFSGELGAIKHQALDTVRYDYGHYLIMLGPFQPWSGLTAPPCPYAESSWAQAAVQTALELFSALYPAPCISGYARPPGPSAVIEHLGSLVPKGGLLLFLSHLPDDVKDGLGEMGPARATGPGMQQFVSSYFLNPACSNVFITVRQRGEKINGRTVLQALGRACDMAGCQHYVLGSTVPLGGLNFVNDLASPVSTAEMMDDFSPFFTVEFPPIQEEGASSPVPLDVDESMDISPSYELPWLSLESCLTSILSHPTVGSKEHLVRHTDRVSGGRVAQQPGVGPLDLPLADYAFVAHSQVWTRPGGAPPLPYRTWDRMTEKLLVSAKPGGENVKVSGTVITLGEQGYKVSLDLREGTRLAMAEALLNAAFAPILDPEDVLLTLHLHLDPRRADNSAVMEAMTAASDYARGLGVKLTFGSASCPETGSSASNFMTVVASVSAPGEFSGPLITPVLQKTGSLLIAVRCGDGKIQGGSLFEQLFSDVATTPRAPEALSLKNLFRAVQQLVKSGIVLSGHDISDGGLVTCLVEMALAGQRGVTITMPVASDYLPEMFAEHPGLVFEVEERSVGEVLQTLRSMNMYPAVLGRVGEQGPDQMFEVQHGPETVLRQSLRLLLGTWSSFASEQYECLRPDRINRSMHVSDYGYNEALAVSPLTGKNLSPRRLVTEPDPRCQVAVLCAPGTRGHESLLAAFTNAGCLCRRVFFREVRDNTFLDKYVGLAIGGVHGARDSALAGRATVALINRSPALRDAILKFLNRPDTFSVALGELGVQVLAGLGAVGSTDNPPAPGVEVNVQRSPLILAPNASGMFESRWLNISIPATTSSVMLRGLRGCVLPCWVQGSCLGLQFTNLGMPYVLQNAHQIACHFHSNGTDAWRFAMNYPRNPTEQGNIAGLCSRDGRHLALLCDPSLCTDFWQWEHIPPAFGHPTGCSPWTLMFQAAHLWSLRHGRPSE
Protein: At1g49750 (F14J22.4 protein) (Leucine-rich repeat (LRR) family protein) (Q9FXA1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- AT3g15450/MJK13_11
- Beta-glucosidase 16
- Actin-related protein 4
- Probable xyloglucan endotransglucosylase/hydrolase protein 6
Sequence:
MASILSILLLILSLSNLHFTSTTGNNHINDRKSLEIIIGGGNDNNPPPSPSPEPEPEPADCPPPPPPPPCPPPPSPPPCPPPPSPPPSPPPPQLPPPPQLPPPAPPKPQPSPPTPDLPFASSLLKKVYPVLQRFKDLVADDKLKSWEGPDICNKYLGLKCAIFPKTKHLALASVQFNGLNLRGKIGKILKLDNFLDKLEEVTIFHANSNGFTGSVPDFSNLKFLYELDLSNNKLTGDFPTSVLKGNNLTFLDLRFNSFSGSVPPQVFNLDLDVLFINNNNLVQKLPLNLGSITALYLTFANNRFTGPIPESIGNIKYLQEVLFLNNKLTGCLPYQIGNLTRATVFDVGFNQLTGPIPYSFGCLETMEQLNLAGNKFYGTIPEIVCEIACLQNVSLSNNYFTQVGPKCRKLIKRKIMDVSMNCILDLPNQKTPSECAKFFMRKQTCPNSKSLFTVPCDKNPNRGKPDQERLEEEKAQVSHPVTYNTLNPDRLRNL
Protein: Axial budding pattern protein 2 (Bud site selection protein 10) (Suppressor of RHO3 protein 4) (P38928)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for haploid cells axial budding pattern. Acts as an anchor to help direct new growth components and/or polarity establishment components like the BUD5 GTP/GDP exchange factor to localize at the cortical axial budding site. Regulates septin organization in late G1 independently of its role in polarity-axis determination.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10366591, ECO:0000269|PubMed:11065362, ECO:0000269|PubMed:11134078, ECO:0000269|PubMed:12221111, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:17460121, ECO:0000269|PubMed:8805277, ECO:0000269|PubMed:8846915, ECO:0000269|PubMed:9732282}; Single-pass type I membrane protein {ECO:0000269|PubMed:10366591, ECO:0000269|PubMed:11065362, ECO:0000269|PubMed:11134078, ECO:0000269|PubMed:12221111, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15282802, ECO:0000269|PubMed:17460121, ECO:0000269|PubMed:8805277, ECO:0000269|PubMed:8846915, ECO:0000269|PubMed:9732282}. Note=In small buds, localizes to incipient bud sites, emerging buds and to the bud periphery. In large buds, localizes as a ring at the bud neck. Requires ERV14 to be efficiently delivered to the cell surface. Recruitment to the bud neck after S/G2 phase of the cell cycle depends on BUD3 and BUD4.
Interaction partners:
- Bud site selection protein 4
- Bud site selection protein 5
- Bud site selection protein 3
- Putative protease AXL1
- Ras-related protein RSR1
- Bud site selection protein 9
- Bud site selection protein RAX2
- ER-derived vesicles protein ERV14
- Bud site selection protein RAX1
- Cell division control protein 42
Sequence:
MTQLQISLLLTATISLLHLVVATPYEAYPIGKQYPPVARVNESFTFQISNDTYKSSVDKTAQITYNCFDLPSWLSFDSSSRTFSGEPSSDLLSDANTTLYFNVILEGTDSADSTSLNNTYQFVVTNRPSISLSSDFNLLALLKNYGYTNGKNALKLDPNEVFNVTFDRSMFTNEESIVSYYGRSQLYNAPLPNWLFFDSGELKFTGTAPVINSAIAPETSYSFVIIATDIEGFSAVEVEFELVIGAHQLTTSIQNSLIINVTDTGNVSYDLPLNYVYLDDDPISSDKLGSINLLDAPDWVALDNATISGSVPDELLGKNSNPANFSVSIYDTYGDVIYFNFEVVSTTDLFAISSLPNINATRGEWFSYYFLPSQFTDYVNTNVSLEFTNSSQDHDWVKFQSSNLTLAGEVPKNFDKLSLGLKANQGSQSQELYFNIIGMDSKITHSNHSANATSTRSSHHSTSTSSYTSSTYTAKISSTSAAATSSAPAALPAANKTSSHNKKAVAIACGVAIPLGVILVALICFLIFWRRRRENPDDENLPHAISGPDLNNPANKPNQENATPLNNPFDDDASSYDDTSIARRLAALNTLKLDNHSATESDISSVDEKRDSLSGMNTYNDQFQSQSKEELLAKPPVQPPESPFFDPQNRSSSVYMDSEPAVNKSWRYTGNLSPVSDIVRDSYGSQKTVDTEKLFDLEAPEKEKRTSRDVTMSSLDPWNSNISPSPVRKSVTPSPYNVTKHRNRHLQNIQDSQSGKNGITPTTMSTSSSDDFVPVKDGENFCWVHSMEPDRRPSKKRLVDFSNKSNVNVGQVKDIHGRIPEML
Protein: GH23001p (Q8MQR6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
DLGFVKTNASTDVIFSPFNYKMTMDGATGSTSSSGSLRKQRNSSQSVSEDEILKTLDYKHVADWQSLATLLPSEYRRRLQHIPEVKHLVRQLDAELSQRPLFCMSPPLRRNRTHICDCAKYFQGQQTQTDEASSSGSSQQPSSGYRGSSTLLTDSELDVDPLKQMYVYQYDQQRMDSGVETSPGSQLTQTPPQPMPRSILRKAHSAQSRSKRNSMIEAQQTQKLTKLEKRRSLQEPPNNYGLGSTDELADVFEEEEHSQPAPPVKQRLSRKDLDARARAESFLASLPRSELKYYAEIASILESSGEHVTYDAAALKKEVSRVLSQQNKVSFNDEGVAAGLQQHAKRFATPPNSPNISMGALKRDTVDVLEQRKIESNRFKRLQIQWELMSKDSSMLKELASEAATKSGGSTPTSGNSTGSNSAPRSRIPRPVSYPAGRSSTPTSSRTAPVLATPSPARPATPKTVTKSHNKPGLFTSPRPSRLTSAQEAAGGNKVSTRSPSRIVQPKRYSLAGATTPTSTTPTSARARTPTNPVAVTAPNTPKRQAVAQSPRPTSRVR
Protein: Transmembrane protein 101 (Putative NF-kappa-B-activating protein 130) (Q96IK0)
Organism: Homo sapiens (Human)
Function: May activate NF-kappa-B signaling pathways.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MASKIGSRRWMLQLIMQLGSVLLTRCPFWGCFSQLMLYAERAEARRKPDIPVPYLYFDMGAAVLCASFMSFGVKRRWFALGAALQLAISTYAAYIGGYVHYGDWLKVRMYSRTVAIIGGFLVLASGAGELYRRKPRSRSLQSTGQVFLGIYLICVAYSLQHSKEDRLAYLNHLPGGELMIQLFFVLYGILALAFLSGYYVTLAAQILAVLLPPVMLLIDGNVAYWHNTRRVEFWNQMKLLGESVGIFGTAVILATDG
Protein: UPF0649 protein C1442.02 (Q76PC4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- COP9 signalosome complex subunit 7
Sequence:
MDWKEAIPGAAKVAIETKDYITYSTLLELILEEARIKDIDEQRELIKCLHEELKQEKNDHITREISWDIIGMVLPYVGKVQNEADEFVDFLAKNGNPREVFLKCCELLINGGFESPQQFISLNSAILSALHRISTKRPVLFVNNFLISLFSGLANILQIDSDELYCVWKISISSIQDAMHRFPVSECYLACLKACSILAQLFLSKETLMLSFRSLLQTKDQYAEFREELSGATTNCDKLDTLSKSIINIFDYLLSHLPESWSIITEHMAQELTKATYVSQSSSISSEDEEIAKNADVPAEVDNNSTKADDKRDEIEFDTKGCLALLTIKSFYQSGNFFLDFLKEKFPSTILETLQQLVSWEIQLDSVGFKDIAVYQGYLLDLPHFQVPDSELEHLSSLLHGYHFMASSTELPWLRVTCNAIVTKCLDSQLPSVRLSYILDTLEECPLLNIKTAILNYYQKQCSLVKDSNEEGLKNFVSPNTLLDVFKVFDAMEDVELDSQSLSYIHQTLVFLYSLEIQNLLSQNQFPTVYFTKISDQINNYEGELPTDGLKYYIELLNSRNK
Protein: Cytosolic sulfotransferase 13 (AtSOT13) (EC 2.8.2.-) (Q9ZPQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- BPS1-like protein
- At2g15730
- P-loop containing nucleoside triphosphate hydrolases superfamily protein
- Putative cytosolic sulfotransferase 2
- Protein IMPAIRED IN BABA-INDUCED STERILITY 1
- Protein BPS1, chloroplastic
- Sulfotransferase
Sequence:
MTKSETTLSKLLVESELVQECEELLSSLPRDRSVFAEYLYQYQGFWYPPNLLEGVLYSQKHFQARDSDIVLASIPKSGTTWLKSLVFALIHRQEFQTPLVSHPLLDNNPHTLVTFIEGFHLHTQDTSPRIFSTHIPVGSLPESVKDSSCKVVYCCRNPKDAFVSLWHFMKNLIVKEMVGCTMEEMVRFFCRGSSIYGPFWDHVLQYWKESRENPKKVMFVMYEEMREQPQEWVMRIAEFLGYSFTEEEIENGVLEDIIKLCSLENLSKLEVNEKGKLLNGMETKAFFRKGEIGGWRDTLTPLLAEEIDKTTKEKLIGSDFRFFC
Protein: PHD finger protein MALE STERILITY 1 (Q9FMS5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcriptional activator required for anther and post-meiotic pollen development and maturation. Seems to regulate inflorescence branching and floral development. May control tapetal development by directly regulating tapetal programmed cell death (PCD) and breakdown. Implicated in pollen cytosolic components and wall development (e.g. exine and intine formation).
Subcellular location: Nucleus {ECO:0000269|PubMed:12461128, ECO:0000269|PubMed:18032629}.
Interaction partners:
- Aspartyl protease UND
- MYB transcription factor
- Cysteine-rich repeat secretory protein 41
- Probable inactive peroxygenase-like protein
- Tapetal oleosin GRP-16
- Probable peroxygenase 7
- Alpha/beta-Hydrolases superfamily protein
- Glycine-rich protein
- GDSL esterase/lipase EXL5
- Glycine-rich protein
Sequence:
MANLIRTDHQQHIPKKRKRGESRVFRLKTFGESGHPAEMNELSFRDNLAKLLEFGHFESSGLMGSWSFQLEIQRNPNPLYVLLFVVEEPIEASLNLRCNHCQYVGWGNQMICNKKYHFVIPSKETMAAFLKLEGGGYAFPEKESFSHLVELQGHVLHGFFHSNGFGHLLSLNGIETGSDLTGHQVMDLWDRLCTGLKARKIGLNDASHKKGMELRLLHGVAKGEPWFGRWGYRFGSGTYGVTQKIYEKALESVRNIPLCLLNHHLTSLNRETPILLSKYQSLSTEPLITLSDLFRFMLHLHSRLPRDNYMSNSRNQIISIDSTNCRWSQKRIQMAIKVVIESLKRVEYRWISRQEVRDAARNYIGDTGLLDFVLKSLGNQVVGNYLVRRSLNPVKKVLEYSLEDISNLLPSSNNELITLQNQNSMGKMATNGHNKITRGQVMKDMFYFYKHILMDYKGVLGPIGGILNQIGMASRAILDAKYFIKEYHYIRDTSAKTLHLDRGEELGIFCTIAWKCHHHNNEIKVPPQECIVVKKDATLSEVYGEAERVFRDIYWELRDVVVESVVGGQIEITRVDEMALNGNKGLVLEGNVGMMMNIEVTKCYEDDDKKKDKRIECECGATEEDGERMVCCDICEVWQHTRCVGVQHNEEVPRIFLCQSCDQHLIPLSFLP
Protein: Guanine nucleotide-binding protein G(t) subunit alpha-3 (Gustducin alpha-3 chain) (P0C7Q4)
Organism: Bos taurus (Bovine)
Function: Guanine nucleotide-binding protein (G protein) alpha subunit playing a prominent role in bitter and sweet taste transduction as well as in umami (monosodium glutamate, monopotassium glutamate, and inosine monophosphate) taste transduction.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Taste receptor type 1 member 3
- Taste 1 receptor member 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Taste receptor type 1 member 2
- Chaperone Ric-8A
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1A
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4
- Guanine nucleotide-binding protein G
Sequence:
MGIGISSESKESAKRSKELEKKLQEDAERDARTVKLLLLGAGESGKSTIVKQMKIIHKNGYSEQECMEFKAVIYSNTLQSILAIVKAMATLEIDYVNPRSAEDQQQLCAMANTLEDGSMTPELAEIIKRLWRDPGVQACFERASEYQLNDSAAYYLNDLDRIAAPGYVPNEQDVLHSRVKTTGIIETQFSFKDLHFRMFDVGGQRSERKKWIHCFEGVTCIIFCAALSAYDMVLVEDEEVNRMHESLHLFNSICNHKYFATTSIVLFLNKKDLFQEKVTKVHLSICFPEYTGPNTFEDAGNYIKNQFLDLNLKKEDKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Protein: SPRY domain-containing SOCS box protein 2 (SSB-2) (Gene-rich cluster protein C9) (O88838)
Organism: Mus musculus (Mouse)
Function: Substrate recognition component of a SCF-like ECS (Elongin BC-CUL2/5-SOCS-box protein) E3 ubiquitin-protein ligase complex which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Negatively regulates nitric oxide (NO) production and limits cellular toxicity in activated macrophages by mediating the ubiquitination and proteasomal degradation of NOS2. Acts as a bridge which links NOS2 with the ECS E3 ubiquitin ligase complex components ELOC and CUL5 (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q99619}. Note=Exhibits a diffuse cytosolic localization. {ECO:0000250|UniProtKB:Q99619}.
Interaction partners:
- Elongin-C
- Cullin-5
Sequence:
MGQTALARGSSSTPTSQALYSDFSPPEGLEELLSAPPPDLVAQRHHGWNPKDCSENIDVKEGGLCFERRPVAQSTDGVRGKRGYSRGLHAWEISWPLEQRGTHAVVGVATALAPLQADHYAALLGSNSESWGWDIGRGKLYHQSKGLEAPQYPAGPQGEQLVVPERLLVVLDMEEGTLGYSIGGTYLGPAFRGLKGRTLYPSVSAVWGQCQVRIRYMGERRVEEPQSLLHLSRLCVRHALGDTRLGQISTLPLPPAMKRYLLYK
Protein: Dihydroorotate dehydrogenase (quinone), mitochondrial (DHOdehase) (EC 1.3.5.2) (Dihydroorotate oxidase) (Q63707)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor. Required for UMP biosynthesis via de novo pathway.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:10727948}; Single-pass membrane protein {ECO:0000269|PubMed:10727948}.
Interaction partners:
- Uridine monophosphate synthetase, isoform CRA_a.
- Multifunctional protein CAD
- Cytochrome b5 reductase 4
- NADH-cytochrome b5 reductase 2
- NADH-cytochrome b5 reductase-like
- NADH-cytochrome b5 reductase 1
- NADH-cytochrome b5 reductase 3
- GMP synthase
- Oxidoreductase NAD-binding domain-containing protein 1
- Trifunctional purine biosynthetic protein adenosine-3
Sequence:
MAWRQLRKRALDAVIILGGGGLLFTSYLTATGDDHFYAEYLMPGLQRLLDPESAHRLAVRVTSLGLLPRATFQDSDMLEVKVLGHKFRNPVGIAAGFDKNGEAVDGLYKLGFGFVEVGSVTPQPQEGNPRPRVFRLPEDQAVINRYGFNSHGLSVVEHRLRARQQKQAQLTADGLPLGINLGKNKTSEDAAADYAEGVRTLGPLADYLVVNVSSPNTAGLRSLQGKTELRHLLSKVLQERDALKGTRKPAVLVKIAPDLTAQDKEDIASVARELGIDGLIVTNTTVSRPVGLQGALRSETGGLSGKPLRDLSTQTIREMYALTQGRIPIIGVGGVSSGQDALEKIQAGASLVQLYTALIFLGPPVVVRVKRELEALLKERGFTTVTDAIGADHRR