wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin-ribosomal protein eL40 fusion protein (Ubiquitin A-52 residue ribosomal protein fusion product 1) [Cleaved into: Ubiquitin; Large ribosomal subunit protein eL40 (60S ribosomal protein L40) (CEP52)] (P62986)
Organism: Rattus norvegicus (Rat)
Function: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in proteotoxic stress response and cell cycle; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.
Subcellular location: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40]: Cytoplasm {ECO:0000250|UniProtKB:P62984}.
Interaction partners:
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS4
- Large ribosomal subunit protein uL4
- Small ribosomal subunit protein uS14
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein uL14
- FAU ubiquitin like and ribosomal protein S30 fusion like 2
- Large ribosomal subunit protein eL18
Sequence:
MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLRQLAQKYNCDKMICRKCYARLHPRAVNCRKKKCGHTNNLRPKKKVK
Protein: Complement factor B (EC 3.4.21.47) (C3/C5 convertase) (Q6MG74)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MEGPQLCLVLLVLGLSSGGVSATPVLEARPQVSCSLEGVEIKGGSFQLLQDGQALEYLCPSGFYPYPVQTRTCKSTGSWSVLQTRDQKIVKKAECRAIRCPRPQDFENGEFWPRSPYYNLSDQISFQCYDGYTLRGSANRTCQENGRWDGQTAICDDGAGYCPNPGIPIGTRKVGSQYRLEDTVTYHCSRGLVLRGSQQRRCQEGGSWSGTEPSCQDSFMYDSPQEVAEAFLSSLTETIEGADAEDGHSPGEQQKRKIILDPSGSMNIYMVLDGSDSIGASNFTGAKRCLANLIEKVASYGVKPRYGLVTYATVPKVLVRVSEERSSDADWVTEKLNQISYEDHKLKSGTNTKKALQAVYSMMSWPGDAPPEGWNRTRHVIIIMTDGLHNMGGDPVTVIEDIRDLLDIGRDRKNPREDYLDVYVFGVGPLVDPVNINALASKKNNEQHVFKVKDMEDLENVFYKMIDETKSLGLCGMVWEHQKGGDYYKQPWQAKISVTRPLKGHENCMGAVVSEYFVLTAAHCFTVEDQKHSIKVNVEGKRRDLEIEEVLFHPNYDINGKKAEGISEFYDYDVALIKLKTKLKYSQTLRPICLPCTEGTTRALRLPQTATCKQHKEELLPMKDVKALFVSEEGKKLTRKEVYIKNGEKKASCERDATKAQGYEKVKVASEVVTPRFLCTGGVDPYADPNTCKGDSGGPLIVHKRSRFIQVGVISWGVVDVCKDPRRQQLVPSYARDFHINLFQVLPWLKEKLKDEDLGFL
Protein: Serine/threonine-protein kinase ATG1 (EC 2.7.11.1) (Autophagy-related protein 1) (W0T9X4)
Organism: Kluyveromyces marxianus (strain DMKU3-1042 / BCC 29191 / NBRC 104275) (Yeast) (Candida kefyr)
Function: Serine/threonine protein kinase involved in the cytoplasm to vacuole transport (Cvt) and found to be essential in autophagy, where it is required for the formation of autophagosomes (By similarity). Involved in the clearance of protein aggregates which cannot be efficiently cleared by the proteasome (By similarity). Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production (By similarity). Also involved in endoplasmic reticulum-specific autophagic process, in selective removal of ER-associated degradation (ERAD) substrates (By similarity). Plays a key role in ATG9 and ATG23 cycling through the pre-autophagosomal structure and is necessary to promote ATG18 binding to ATG9 through phosphorylation of ATG9. Catalyzes phosphorylation of ATG4, decreasing the interaction between ATG4 and ATG8 and impairing deconjugation of PE-conjugated forms of ATG8 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53104}. Preautophagosomal structure membrane {ECO:0000250|UniProtKB:P53104}; Peripheral membrane protein {ECO:0000250|UniProtKB:P53104}.
Interaction partners:
Sequence:
MSSESHGKAVAKAIRLPTENYTVEKEIGKGSFAIVYKGVSLRDGRNIAIKAVSRSKLKNKKLLENLEVEIAILKKIKHPHIVGLIDCERTSTDFYLIMEYCALGDLTFFIKKRRSLVMKHPLIKTVFDLYPPPSAEHNGLNRVLVVNYLQQLSSALKFLRSKNLVHRDIKPQNLLLCTPLQDYSDPKTFHEMGFIGIYNLPVLKIADFGFARFLPNTSLAETLCGSPLYMAPEILNYQKYNAKADLWSVGTVLYEMCCGRPPFKASNHLELFQKIKKANDEVTVPSNCYIEPKIFKLIKGLLTFDPEARMGFNEFFNNEVVTEDLSRYEASYEPDLESKSKDVAESNMFVSEYLVRPAAQEKANGGLRTDEGSAMPGAEHTYNKEREHYRERQDLQGQQQQQQQHPDSPPRGSTQGYQSSAGQTRMKSSYNDLILEKEYVVVEKKTVEVNSLADDFANNGPTTNNQGAQIIKPLRYRTSSSSDGHGGRRASLVERRLSISSLSPSNALSKALGLASVRLFGYQQPNTQTTSTSTHPTLLNPQIFHELTENAVLRADHHLNLFNEQISDSNITPFVESLSAKAFVMYSFAEMKFSQILPSPPSSTDYYSQSDKRLSNGSCAIDDDDDLDSGNPSSNQTLTPGANKVSAANVDNLIPAPELKKLCMESLLLYLKSLTILASSMKLTSKWWYENESKNCTLKLNILVQWIRDRFNECLDKAEFLRLKLHTLNQSEDPQVLDDEPTIFVEKLIYDRALDISRNAARLEMEGGNYNTCELAYATSLWMLEILLDEHLSSNEVYDDGYSSNITSLDESDKEMIRKYVSSIANRLKALKSKMS
Protein: Zinc finger protein 557 (Q8N988)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MAAVVLPPTAASQREGHTEGGELVNELLKSWLKGLVTFEDVAVEFTQEEWALLDPAQRTLYRDVMLENCRNLASLGNQVDKPRLISQLEQEDKVMTEERGILSGTCPDVENPFKAKGLTPKLHVFRKEQSRNMKMERNHLGATLNECNQCFKVFSTKSSLTRHRKIHTGERPYGCSECGKSYSSRSYLAVHKRIHNGEKPYECNDCGKTFSSRSYLTVHKRIHNGEKPYECSDCGKTFSNSSYLRPHLRIHTGEKPYKCNQCFREFRTQSIFTRHKRVHTGEGHYVCNQCGKAFGTRSSLSSHYSIHTGEYPYECHDCGRTFRRRSNLTQHIRTHTGEKPYTCNECGKSFTNSFSLTIHRRIHNGEKSYECSDCGKSFNVLSSVKKHMRTHTGKKPYECNYCGKSFTSNSYLSVHTRMHNRQM
Protein: Pentatricopeptide repeat-containing protein At1g79080, chloroplastic (A3KPF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast {ECO:0000305}.
Interaction partners:
Sequence:
MSTLLNSVLSMASPESSPRKAVGFVSHIPSGFLHFSSVSKGVARVLASTQITLSPKDSAFTITGSSWKPDLDSGSFSDDPRSDEPNLSDSFSHLESLVTGGHKPNVAHSTQLLYDLCKANRLKKAIRVIELMVSSGIIPDASAYTYLVNQLCKRGNVGYAMQLVEKMEDHGYPSNTVTYNALVRGLCMLGSLNQSLQFVERLMQKGLAPNAFTYSFLLEAAYKERGTDEAVKLLDEIIVKGGEPNLVSYNVLLTGFCKEGRTDDAMALFRELPAKGFKANVVSYNILLRCLCCDGRWEEANSLLAEMDGGDRAPSVVTYNILINSLAFHGRTEQALQVLKEMSKGNHQFRVTATSYNPVIARLCKEGKVDLVVKCLDEMIYRRCKPNEGTYNAIGSLCEHNSKVQEAFYIIQSLSNKQKCCTHDFYKSVITSLCRKGNTFAAFQLLYEMTRCGFDPDAHTYSALIRGLCLEGMFTGAMEVLSIMEESENCKPTVDNFNAMILGLCKIRRTDLAMEVFEMMVEKKRMPNETTYAILVEGIAHEDELELAKEVLDELRLRKVIGQNAVDRIVMQFNLD
Protein: 3-ketoacyl-CoA thiolase, mitochondrial (EC 2.3.1.16) (Acetyl-CoA acetyltransferase) (EC 2.3.1.9) (Acetyl-CoA acyltransferase) (Acyl-CoA hydrolase, mitochondrial) (EC 3.1.2.-, EC 3.1.2.1, EC 3.1.2.2) (Beta-ketothiolase) (Mitochondrial 3-oxoacyl-CoA thiolase) (Q8BWT1)
Organism: Mus musculus (Mouse)
Function: In the production of energy from fats, this is one of the enzymes that catalyzes the last step of the mitochondrial beta-oxidation pathway, an aerobic process breaking down fatty acids into acetyl-CoA. Using free coenzyme A/CoA, catalyzes the thiolytic cleavage of medium- to long-chain unbranched 3-oxoacyl-CoAs into acetyl-CoA and a fatty acyl-CoA shortened by two carbon atoms. Also catalyzes the condensation of two acetyl-CoA molecules into acetoacetyl-CoA and could be involved in the production of ketone bodies. Also displays hydrolase activity on various fatty acyl-CoAs (By similarity). Thereby, could be responsible for the production of acetate in a side reaction to beta-oxidation (By similarity). Abolishes BNIP3-mediated apoptosis and mitochondrial damage (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:P42765}.
Interaction partners:
- Trifunctional enzyme subunit alpha, mitochondrial
- Medium-chain specific acyl-CoA dehydrogenase, mitochondrial
- Very long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, mitochondrial
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Hydroxymethylglutaryl-CoA synthase, cytoplasmic
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Long-chain specific acyl-CoA dehydrogenase, mitochondrial
- Peroxisomal bifunctional enzyme
- Peroxisomal acyl-coenzyme A oxidase 1
Sequence:
MALLRGVFIVAAKRTPFGAYGGLLKDFSATDLTEFAARAALSAGKVPPETIDSVIVGNVMQSSSDAAYLARHVGLRVGVPTETGALTLNRLCGSGFQSIVSGCQEICSKDAEVVLCGGTESMSQSPYCVRNVRFGTKFGLDLKLEDTLWAGLTDQHVKLPMGMTAENLAAKYNISREDCDRYALQSQQRWKAANEAGYFNEEMAPIEVKTKKGKQTMQVDEHARPQTTLEQLQKLPSVFKKDGTVTAGNASGVSDGAGAVIIASEDAVKKHNFTPLARVVGYFVSGCDPTIMGIGPVPAINGALKKAGLSLKDMDLIDVNEAFAPQFLSVQKALDLDPSKTNVSGGAIALGHPLGGSGSRITAHLVHELRRRGGKYAVGSACIGGGQGIALIIQNTA
Protein: Alanine--glyoxylate aminotransferase 1 (EC 2.6.1.44) (P43567)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Has alanine:glyoxylate aminotransferase activity.
Interaction partners:
- Low specificity L-threonine aldolase
- Serine hydroxymethyltransferase, cytosolic
- Phosphoserine phosphatase
- Serine hydroxymethyltransferase, mitochondrial
- Isocitrate lyase
- Aminomethyltransferase, mitochondrial
- Glyoxylate reductase 1
- Mitochondrial 2-methylisocitrate lyase ICL2
- Glycine dehydrogenase
- Malate synthase 1
Sequence:
MTKSVDTLLIPGPIILSGAVQKALDVPSLGHTSPEFVSIFQRVLKNTRAVFKSAAASKSQPFVLAGSGTLGWDIFASNFILSKAPNKNVLVVSTGTFSDRFADCLRSYGAQVDVVRPLKIGESVPLELITEKLSQNSYGAVTVTHVDTSTAVLSDLKAISQAIKQTSPETFFVVDAVCSIGCEEFEFDEWGVDFALTASQKAIGAPAGLSISLCSSRFMDYALNDSKNGHVHGYFSSLRRWTPIMENYEAGKGAYFATPPVQLINSLDVALKEILEEGLHKRWDLHREMSDWFKDSLVNGLQLTSVSRYPSNMSAHGLTAVYVADPPDVIAFLKSHGVVIAGGIHKDIGPKYIRIGHMGVTACNKNLPYMKNCFDLIKLALQRKK
Protein: Fusion glycoprotein F0 [Cleaved into: Fusion glycoprotein F2 (F2); p27 (Intervening segment) (Pep27) (Peptide 27); Fusion glycoprotein F1 (F1)] (P03420)
Organism: Human respiratory syncytial virus A (strain A2)
Function: Inactive precursor that is cleaved at two sites by a furin-like protease to give rise to the mature F1 and F2 fusion glycoproteins.
Subcellular location: [Fusion glycoprotein F0]: Host Golgi apparatus membrane {ECO:0000305|PubMed:16160180}; Single-pass membrane protein {ECO:0000269|PubMed:16160180}.; SUBCELLULAR LOCATION: [Fusion glycoprotein F1]: Virion membrane {ECO:0000269|PubMed:23776214}; Single-pass type I membrane protein {ECO:0000269|PubMed:16160180}. Host cell membrane {ECO:0000269|PubMed:16160180}; Single-pass membrane protein {ECO:0000269|PubMed:16160180}. Note=Localized at the host apical membrane. {ECO:0000269|PubMed:16160180}.; SUBCELLULAR LOCATION: [Fusion glycoprotein F2]: Virion membrane {ECO:0000269|PubMed:23776214}. Host cell membrane {ECO:0000305}. Note=Localized at the host apical membrane. {ECO:0000305}.
Interaction partners:
Sequence:
MELLILKANAITTILTAVTFCFASGQNITEEFYQSTCSAVSKGYLSALRTGWYTSVITIELSNIKENKCNGTDAKVKLIKQELDKYKNAVTELQLLMQSTPPTNNRARRELPRFMNYTLNNAKKTNVTLSKKRKRRFLGFLLGVGSAIASGVAVSKVLHLEGEVNKIKSALLSTNKAVVSLSNGVSVLTSKVLDLKNYIDKQLLPIVNKQSCSISNIETVIEFQQKNNRLLEITREFSVNAGVTTPVSTYMLTNSELLSLINDMPITNDQKKLMSNNVQIVRQQSYSIMSIIKEEVLAYVVQLPLYGVIDTPCWKLHTSPLCTTNTKEGSNICLTRTDRGWYCDNAGSVSFFPQAETCKVQSNRVFCDTMNSLTLPSEINLCNVDIFNPKYDCKIMTSKTDVSSSVITSLGAIVSCYGKTKCTASNKNRGIIKTFSNGCDYVSNKGMDTVSVGNTLYYVNKQEGKSLYVKGEPIINFYDPLVFPSDEFDASISQVNEKINQSLAFIRKSDELLHNVNAGKSTTNIMITTIIIVIIVILLSLIAVGLLLYCKARSTPVTLSKDQLSGINNIAFSN
Protein: Cytochrome b5 B (Q86L22)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004131}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004131}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004131}. Microsome membrane {ECO:0000256|ARBA:ARBA00037877}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00037877}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00037877}.
Interaction partners:
Sequence:
MSEDKQYTMEEVSKHDKVDDLWMVINQKVYDVTSFVNDHPGGGDYLIQNAGKEATNEFLDVGHSQKAVDMLKDYYIGVCTDSKPLQNPLSSNPIPISTESPVIKSTESSSNNNNNEDKNKDVTTTIALVGGIVVAVASIAFFTFAKIKK
Protein: Beta-hexosaminidase subunit A1 (EC 3.2.1.52) (Beta-N-acetylhexosaminidase subunit A1) (N-acetyl-beta-glucosaminidase subunit A1) (P13723)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Responsible for the degradation of GM2 gangliosides, and a variety of other molecules containing terminal N-acetyl hexosamines. This enzyme plays a role during the slug stage of development in the maintenance of pseudoplasmodia of normal size.
Subcellular location: Lysosome {ECO:0000269|PubMed:2972716}.
Interaction partners:
- Beta-galactosidase 1
- Probable alpha-galactosidase
- Alpha-galactosidase
- Beta-hexosaminidase subunit B2
- Beta-hexosaminidase subunit A2
Sequence:
MIKKIILFFAVLIAIVIGQQPLNVVPYPQQVSIGTCVIPVAPGSILIESNIESATFSVSMDRYTNLFFPFSNESEPSSNESFLLSVTIYSDDETLQLGIDESYSLSIEQGSYQLKATNIYGAMRGLETFKQLIVYNELENSYSIVCVSISDSPRYPWRGFMVDSARHYIPKNMILHMIDSLGFSKFNTLHWHMVDAVAFPVESTTYPDLTKGAFSPSATFSHDDIQEVVAYAKTYGIRVIPEFDIPGHAAAWGIGYPELVATCPDYAANVNNIPLDISNPATFTFIQNLFTEIAPLFIDNYFHTGGDELVTGCWLEDPAIANWMTKMGFSTTDAFQYFENNLDVTMKSINRTKITWNDPIDYGVQLNPETLVQVWSSGSDLQGIVNSGYKALVSFAWYLDKQNPDNNIHYEWQDTWQDFYAADPTNNISTNAENIIGGEATMWAEQINQVNWDVRVWPRAIGIAERLWSAQSVNSVSLALPRIGHFTCDLSRRGIQSGPLFPDYCPMQDDLVFTMKPNTKLSKSEIKLILNK
Protein: ABC transporter G family member 6 (ABC transporter ABCG.6) (Q54TV1)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAKQDPKDKNSDSPNLSIPINNNNNENLDNDQELLNNNNNNNNNNNNNNNNNNNNNNNNNNNNNLISSSRKHKDEESNYDSDDEKSVYQIAKEHEGEDDGDDEYFPIPLDELMPNHENDELTKKIKQTRPEDKTGLYVYCRNATYTVKHRENKKVKIKLIDDISFYLKPKEMTLILGTPGCGKSTIFQMLAGQLKDKHFKGELLFNGHPINHKNHHRDISYVTQDDIHVPTLTVKETFRFALDCLGRKELTNEEKKETVDNCMNLLGLKESENTVVGDNFVRGISGGQKKRVTIGVGVIKGSNLLLMDEPTSGLDSSTSFEILSDVKKFVTYGYSPALITLLQPSVQLTSLFDNLMILNKGRICYFGPMNKALGYFKKLGFACPSHNNPAEFFQEVVDAPERYSFIHPPKCKTSKDFVRAYRESEFYKDLMEKMDANKDGIVDDNKPKVLVDSTAKELGMYPHGIGYQTKICMKRGFTMIRRNYYNFLTRVAKGIFFGLLLGTLYWRIGHNQSGGMERFGLLFFIMVTIIFSSFAAVNSFFGERKVFYSQKALYYYKTGAYFISSIICDIPAGILEVAFFGPIVYWLANLRPVFIRFVYFMLLLIMTDNLSLSFAKMCAAISPTIEIANVIASVILSIWLLFSGFTAPKNDIGGWWIWLYYISPYTWIFQGLSINEFTYQEYGCKTSELIPPRTPQNLLPYPEGFGGNQVCQFTSGEQIMDAFGITNPNYFKWVVFGILSAYIVFFYVVCFFALKYFNFEDKKSKLAVKKLKKKKKVKTTKQDEESAAISSEALERIDDDNDDDADYETEIKKKKSHKKQKEDTVIDVKSPSSLTTGSPYYNINNNNNNLSGSGNNIKKRKVKTPSNLSPSVNSPITINSPMPTSPSNNNNNNNSNEKSKNGKDIGSETGSYLQFKKLCYAVDVKVDDPDNPKKKKSQRLQLLTDIDGYVKPGQMLALMGPSGAGKSTLLDVLAQRKTGGHITGEILINGKPPSEFTNRIRAYVEQMDVLPPTQTVREAIAFSARCRLPPEVTKEERESYVDKIVEVLSLSSIKDLKIGVLGDGLSVSQRKRVNIGVELASNPEILFLDEPTSGLDSGDAFKVIDVVNKIAKVMNRTVICTVHQPSAAIFEFFDQLLLLKQGGETIYFGPLGNQSSVILDYCDKLGMHIKPHINPADFVMTLADQGKMVEGPNGEQVPLDAKKAYFESDICKKEYEIMEGQLIPDDFVIKTYDSRFASSWMTQFRALCMRSWLSRLRRPAIFVSNCIRSILLAVLLGTLFVRMDYEQKDARSRVSLLFFSFLFAGMVAIGNIPTTVLERGVFYREVTAGFYHSTAYMTSYVLTSYPFTLSTGILYIIPTFWIAGLDSGRHSSKFWYCLFIFIITYVMYDAFGLCLAVCLPNEVMASTICGIGLSLSTLFGGFVIARPNYPSAYYWCHYLDWLRYPLEASCTNEFTGLTFVCTNNKGAVPIPIIENGVQIAIKYYCPITNGDDFMLTYGFHKFMRYIDIAAIFGYIFIFVGLSFWGFKKIRWFNR
Protein: E3 ubiquitin-protein ligase RMA1H1 (EC 2.3.2.27) (Protein RING membrane-anchor 1 homolog 1) (RING-type E3 ubiquitin transferase RMA1H1) (Q6R567)
Organism: Capsicum annuum (Capsicum pepper)
Function: E3 ubiquitin-protein ligase required for aquaporin levels regulation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19234086}; Single-pass type IV membrane protein {ECO:0000269|PubMed:19234086}. Note=Localization experiments made in a heterologous system.
Interaction partners:
Sequence:
MNQDMALEQLDTTFNKHDTPLGKWKSMNDEVEENISGGFDCNICLDCVHEPVITLCGHLYCWPCIYKWIYFQSVSSENSDQQQPQCPVCKAEVSEKTLIPLYGRGGQSTKPSEGKAPNLGIVIPQRPPSPRCGGHFLLPTTDSNPSQLLQRRGYQQQSQTRQPAYQGSYMSSPMLSPGGATANMLQHSMIGEVAYARIFGNSSTTMYTYPNSYNLAISSSPRMRRQLSQADRSLGRICFFLFCCFVTCLILF
Protein: Prolyl aminopeptidase papA-Aspergillus niger (EC 3.4.11.5) (A2QWD1)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MGQLREGVETDGKLNRGSTYRIVKRRYRYSLQLLPKRRLNGRPPPAAVGPILPVTPPQIAPSLRKNVANDRWGYPGRLRVAELFFDVPLNYSKPNEGTLRLFARSVRRLVTPAEPSETPKDDKQLPFLVYLQGGPGMGCRPPQEYGWIGTVLEKGYQVLFLDQRGTGLSSTVTAGTLARQGNAIKQAEYMKNFRADNIVRDCEAVRRCLMTDYPEDKRKWSIIGQSFGGFCAVTYLSMFPEGLAEAFICGGLPPLVDNPDPVYARTYEKVLERNKAYYAKFPEDVERVKQIIQYLKDNEVALPTGTLTPERFQQMGILFGMHGGLDSIHDLVLRAWNDLDVFGFLTHPTLTSIDSFGGMDNNIIYAILHEAIYCQGKPSNWSADRLRASNPDFQIDSNKSEILFTGEMVYKDMFDSYTELSQIRDAADILASTDDWPALYDEAQLARNEVPVYAATYIDDMYVHFDHAQNTAAKIKGAKQFITNVMYHNAIRSKSDELIQQLFALREDTID
Protein: PHD finger-like domain-containing protein 5A (Q9VMC8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Splicing factor 3B subunit 5
- Splicing factor 3B subunit 6
- Splicing factor 3B subunit 3
- LD45152p
- Splicing factor 3B subunit 4
- Splicing factor 3B subunit 1
- Probable small nuclear ribonucleoprotein G
- Splicing factor 3A subunit 2
- RNA-binding motif protein, X-linked 2
- U1 small nuclear ribonucleoprotein A
Sequence:
MAKHHPDLIFCRKQPGVAIGRLCEKDDGKCVICDSYVRPCTLVRICDECNYGSYQGRCVICGGPGVSDAYYCKSCTIQEKDRDGCPKIVNLGSSKTDLFYERKKYGFKQNY
Protein: DNA packaging protein (ATPase gp16) (EC 3.6.4.-) (Gene product 16) (gp16) (Protein p16) (P11014)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: ATPase required for the genome encapsidation reaction. Part of the active packaging motor via the binding to the packaging RNA (pRNA), itself fixed to the head-tail connector at the unique portal vertex of the prohead. Binds and supercoils the DNA-gp3 to produce an initiation complex for DNA packaging. Provides the energy to actively pump the viral DNA into the prohead. Approximately one molecule of ATP is used in the packaging of 2 bp of viral DNA. After packaging, the ATPase and the pRNA are released from the prohead.
Interaction partners:
Sequence:
MDKSLFYNPQKMLSYDRILNFVIGARGIGKSYAMKVYPINRFIKYGEQFIYVRRYKPELAKVSNYFNDVAQEFPDHELVVKGRRFYIDGKLAGWAIPLSVWQSEKSNAYPNVSTIVFDEFIREKDNSNYIPNEVSALLNLMDTVFRNRERVRCICLSNAVSVVNPYFLFFNLVPDVNKRFNVYDDALIEIPDSLDFSSERRKTRFGRLIDGTEYGEMSLDNQFIGDSQVFIEKRSKDSKFVFSIVYNGFTLGVWVDVNQGLMYIDTAHDPSTKNVYTLTTDDLNENMMLITNYKNNYHLRKLASAFMNGYLRFDNQVIRNIAYELFRKMRIQ
Protein: Sensor protein KdpD (EC 2.7.13.3) (P9WGL3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Member of the two-component regulatory system KdpD/KdpE involved in the regulation of the kdp operon. Functions as a sensor protein kinase which is autophosphorylated at a histidine residue and transfers its phosphate group to the conserved aspartic acid residue in the regulatory domain of KdpE in response to environmental signals such as low levels of potassium ion, osmotic imbalance, acid and nutrient stresses. In turn, KdpE binds to the upstream promoter regions of target genes to positively regulate their expression.
Subcellular location: Cell membrane {ECO:0000305|PubMed:12581360}; Multi-pass membrane protein {ECO:0000305|PubMed:12581360}.
Interaction partners:
- Transcriptional regulatory protein KdpE
- Potassium-transporting ATPase KdpC subunit
- Potassium-transporting ATPase ATP-binding subunit
- Potassium-transporting ATPase potassium-binding subunit
- Putative diacylated glycolipid transporter LprF
- Putative lipoprotein LprJ
- Transcriptional regulatory protein TrcR
- Probable membrane protein KdpF
- DNA-binding response regulator MtrA
- Transcriptional regulatory protein PrrA
Sequence:
MTLLFADLCAIFTPYRWMIEHVTTKRGQLRIYLGAAPGVGKTYAMLGEAHRRLERGTDVVAAVVETHGRNKTAKLLEGIEMIPPRYVEYRGARFPELDVEAVLRRHPQVVLVDELAHTNTPGSKNPKRWQDVQEILDAGITVISTVNIQHLEGLNDVVEQITGIEQKEKIPDEIVRAADQVELVDITPEALRRRLAHGNVYAAERVDAALSNYFRTGNLTALREIALLWLADQVDAALEKYRADKKITATWEARERVVVAVTGGPESETLVRRASRIASKSSAELMVVHVIRGDGLAGVSAPQLGRVRELATSLGATMHTVVGDDVPTALLDFAREMNATQLVVGTSRRSRWARLFDEGIGARTVQEPGGIDVHMVTHPAASRASGWSRVSPRERHIASWLAALVVPSVICAITVAWLDRFMGIGGESALFFIGVLIVALLGGVAPAALSALLSGMLLNYFLTEPRYTWTIAEPDAAVTEFVLLAMAVAVAVLVDGAASRTREARRASQEAELLALFAGSVLRGADLATLLQRVRETYSQRAVTMLRVRQGASTGETVACVGTNPCRDVDSADTAIEVGDDEFWMLMAGRKLAARDRRVLTAVATQAAGLVKQRELAEEAGQAEAIARADELRRSLLSAVSHDLRTPLAAAKVAVSSLRTEDVAFSPEDTAELLATIEESIDQLTALVANLLDSSRLAAGVIRPQLRRAYLEEAVQRALVSIGKGATGFYRSGIDRVKVDVGDAVAMADAGLLERVLANLIDNALRYAPDCVVRVNAGRVRERVLINVIDEGPGVPRGTEEQLFAPFQRPGDHDNTTGVGLGMSVARGFVEAMGGTISATDTPGGGLTVVIDLAAPEDRP
Protein: Flavin-containing monooxygenase FMO GS-OX2 (EC 1.14.13.237) (Flavin-monooxygenase glucosinolate S-oxygenase 2) (Q94K43)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the conversion of methylthioalkyl glucosinolates of any chain length into methylsulfinylalkyl glucosinolates.
Interaction partners:
- Probable inactive 2-oxoglutarate-dependent dioxygenase AOP2
- Cytochrome P450 81F3
- Cytochrome P450 81F1
- Cytochrome P450 81F4
- Probable 2-oxoacid dependent dioxygenase
- Transcription factor MYB28
- Transcription factor MYB29
- Methylthioalkylmalate synthase 1, chloroplastic
- UDP-glycosyltransferase 74C1
- Cytosolic sulfotransferase 17
Sequence:
MAPAQNPISSQHVVVIGAGAAGLVAARELSREGHTVVVLEREKEVGGLWIYSPKAESDPLSLDPTRSIVHSSVYESLRTNLPRECMGFTDFPFVPRFDDESRDSRRYPSHMEVLAYLQDFAREFNLEEMVRFEIEVVRVEPVNGKWRVWSKTSGGVSHDEIFDAVVVCSGHYTEPNVAHIPGIKSWPGKQIHSHNYRVPGPFENEVVVVIGNFASGADISRDIAKVAKEVHIASRASEFDTYEKLPVPRNNLWIHSEIDTAYEDGSIVFKNGKVVYADSIVYCTGYKYRFTFLETNGYMNIDENRVEHLYKHVFPPALSPGLSFVGLPSMGIQFVMFEIQSKWVAAVLSRRVTLPTEDKMMEDISAWYASLDAVGIPKRYTHKLGKIQSEYLNWVAEECGCPLVEHWRNQQIVRGYQRLVSHPETYRDEWDDNDLMEEAYEDFARKKLISFHPSHIL
Protein: Platelet-derived growth factor receptor-like protein (F1QBD0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MFDILFVMIFGLSGRVLTKDTDTKGRFSSPVLDVTEKQLVIERNQTLQLSCRGRWELQWVLPSGVPKLYPDTHIVNTQCGKKSNQYCSRLTLSPALTQHTGSYRCRYRQKERKQTSVYIYITDSQRPFVKVQSEIPDVVYMKEGEPLVFPCRVTNPDAKVSLVKFPLHRITPDHRNIIWNSRQGFIIRSPTFFYIGLFSCETIVDGVKYTNKFLTHRPVNKILDVYLNSTGLVHTLQGEMLALNCTVTAEWNSRVSISWTYPQKANGSAIISKRISRSRSNMLFYSVLTIPSLSKADKGLYKCQVTSGPSKRETNTTVIVYDQPFIRLKHRNGPVVQAFAGQKSFRLTPKLKAFPAPEIIWLKDGMVAAERCSRYHVDGFSLVIRDVAEEDAGIYTILTGIQQYGLFQNLTITLVVNVKPQIGEKSVSSQQPGTVQRGSRQALHCTSHGVPPPQIQWLWHPCPPKGLGPARLA
Protein: Probable arginine--tRNA ligase, cytoplasmic (EC 6.1.1.19) (Arginyl-tRNA synthetase) (ArgRS) (Q19825)
Organism: Caenorhabditis elegans
Function: Forms part of a macromolecular complex that catalyzes the attachment of specific amino acids to cognate tRNAs during protein synthesis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P54136}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P54136}.
Interaction partners:
- Probable glutamine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase
- Leucine--tRNA ligase
- glutamate--tRNA ligase
- proline--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
- serine--tRNA ligase
- Histidine--tRNA ligase
Sequence:
MSANKELQQGYSDYSAASDQAALLNRLITAMQKGELTDELLEHIPELGDAKKLNDKLKYRKSILEKSIAEQAAKNKKNGVKATSTSSPSSSTSAPAEKKAKKDGKTGGAPPKQAKKVDYVTVEDYGSSIFGRLQSLFKKAIEDAFPGLDVPLLLAETPNPQFGDYQCNSAMPIAAKLKANKINKRPGDVAKEIQAKLPTKIDFVEKIDVMPAGFINIFLNTDYLRRQISLLASEGVKLPKLTRKRVLVDFSSPNIAKEMHVGHLRSTIIGDSICRLFEAVGFDVLRVNHIGDWGTQFGMLIAHLYDRFPDFLKKLPDISDLQAFYKESKKRFDEDEQFKKRAYEYVVKLQSHDGDIVKAWNTICDVSKKYNQIVYNYLDIKIKDVGESFYQDKMIELVKWVKTNKPDMLREEDGRQIMFPTGCDIPLTVVKSDGGFTYDTSDLAALKYRMLEEKCDWNIYVVDSGQSLHLETVYAAGRDFGWYDESIQRVEHVAFGLVLGDDKKKFKTRSGETVRLLDLLSEGVKRATEKLIEKGRETAMSEEQLVAARDAVAFGCVKYADLSHTRTQDYVFSFDRMLEDRGNTAVYLLYAYTRIQSIFEKDEVKNVDLVKYIASTPTLPLDHPGEFKLAKQLLKLSDCVLLVLDSLMLHQMCDYVYQLATLFHDFYNECYVIENKEGEKPFVHMHRLALCDVTRKVMSTCFKILGLREVNKM