wanglab/gogpt-training-data huggingface dataset:
Protein: Interferon-gamma binding protein C4R (Q66793)
Organism: Ectromelia virus (strain Moscow) (ECTV) (Mousepox virus)
Interaction partners:
Sequence:
MRAIILTVLFINSINATITSYKFESVNFDSKIEWTGNGLYNISLRNYGIKTWQTMYTNVPEGTYDISGFPNNDFVSFWVKFEQGDYKVDKYCTGLCIEVKIGPPTVTLTEYDDHINLYIEHPYATRGSKKIPIYKRNDMCDIYLLYTANFTFGDSEEPVIYDIDDYDCTSTGCSIDFATTEKVCVMAQGATEGLLDKITPWSSEVCLTPKKNVYTCAIRSKEDVPNFKEKMTRVIKRKFNKQSHSYLTKFLGSTSNDITTFLSMLD
Protein: Uncharacterized protein (Q38EI6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MAKSTRSKWKKAHRRQRAQLEAATVSKRIGRLNGKLKLAAEGGLSEVPLQDPETRFHFVNPQMDHNVPHTCKGLNNNYEQLIRESPDFNKPLKLKPPTTNYYGKSNPDAPHPVTCQYEVISATTPVAGHALSVEDVARMTKEQVEHNQSKPEEARNDKGMRTEENEENDMEEFVLGCNDAAKETTVKTKALLAGKTTISPLPKKSRKAPVKSVTTALKRNGQLRSSKEKKKVQWR
Protein: Junctional sarcoplasmic reticulum protein 1 (Junctional-face membrane protein of 45 kDa homolog) (JP-45) (Q3MI48)
Organism: Mus musculus (Mouse)
Function: Involved in skeletal muscle excitation/contraction coupling (EC), probably acting as a regulator of the voltage-sensitive calcium channel CACNA1S (By similarity). EC is a physiological process whereby an electrical signal (depolarization of the plasma membrane) is converted into a chemical signal, a calcium gradient, by the opening of ryanodine receptor calcium release channels. May regulate CACNA1S membrane targeting and activity.
Subcellular location: Sarcoplasmic reticulum membrane. Endoplasmic reticulum membrane. Note=Colocalizes with ryanodine receptors at the sarcoplasmic reticulum triad membranes.
Interaction partners:
- Voltage-dependent L-type calcium channel subunit alpha-1S
- Ryanodine receptor 1
- SH3 and cysteine-rich domain-containing protein 3
- Triadin
- Calsequestrin-1
- Aspartyl/asparaginyl beta-hydroxylase
Sequence:
MTTRGLEDLDGGLGSCLPSDDLPFLEEPASGRRRESKARGTSRRADSSDWTHVLQDPVAAGAGDAGLKKMEKELAGKESTAGKAGTSPRIVPARRKPQAPPPLQPPPPPLQPPPRTPSDDLPWGDLTLNKCLVLASLVALLGSALQLCRDAVAGEVVAAPHPWVPPSSPPKKEASPAPKPPVLVSPSGSPQPKPGPPQARMQDEPELPGSPEATETRVERGGSISEASGEESVPLGDRGSQEKPRKEKPSKGEKLKKEKPRREKPRREDKSQVTGEPRQSLPRRWEAREGGRRPWGRDSRDLLEHGKLQAWAPRRRHDRDDRPRQKRGKGRD
Protein: Putative transposase InsK for insertion sequence element IS150 (P19769)
Organism: Escherichia coli (strain K12)
Function: Involved in the transposition of the insertion sequence IS150.
Interaction partners:
- Insertion element IS150 protein InsJ
- Uncharacterized oxidoreductase YhhX
- Uncharacterized protein YccE
Sequence:
MKVLNELRQFYPLDELLRAAEIPRSTFYYHLKALSKPDKYADVKKRISEIYHENRGRYGYRRVTLSLHREGKQINHKAVQRLMGTLSLKAAIKVKRYRSYRGEVGQTAPNVLQRDFKATRPNEKWVTDVTEFAVNGRKLYLSPVIDLFNNEVISYSLSERPVMNMVENMLDQAFKKLNPHEHPVLHSDQGWQYRMRRYQNILKEHGIKQSMSRKGNCLDNAVVECFFGTLKSECFYLDEFSNISELKDAVTEYIEYYNSRRISLKLKGLTPIEYRNQTYMPRV
Protein: dTDP-4-dehydrorhamnose reductase (EC 1.1.1.133) (dTDP-4-keto-L-rhamnose reductase) (dTDP-6-deoxy-L-lyxo-4-hexulose reductase) (dTDP-6-deoxy-L-mannose dehydrogenase) (dTDP-L-rhamnose synthase) (P9WH09)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of the dTDP-L-rhamnose which is a component of the critical linker, D-N-acetylglucosamine-L-rhamnose disaccharide, which connects the galactan region of arabinogalactan to peptidoglycan via a phosphodiester linkage. Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose (By similarity).
Interaction partners:
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Glucose-1-phosphate thymidylyltransferase
- N-acetylglucosaminyl-diphospho-decaprenol L-rhamnosyltransferase
- dTDP-glucose 4,6-dehydratase
- Possible dTDP-glucose 4,6-dehydratase
- Mannose-1-phosphate guanylyltransferase
- Probable UDP-glucose 4-epimerase GalE3
- Conserved protein
- Galactofuranosyltransferase GlfT2
- Glutamate-1-semialdehyde 2,1-aminomutase
Sequence:
MAGRSERLVITGAGGQLGSHLTAQAAREGRDMLALTSSQWDITDPAAAERIIRHGDVVINCAAYTDVDGAESNEAVAYAVNATGPQHLARACARVGARLIHVSTDYVFDGDFGGAEPRPYEPTDETAPQGVYARSKLAGEQAVLAAFPEAAVVRTAWVYTGGTGKDFVAVMRRLAAGHGRVDVVDDQTGSPTYVADLAEALLALADAGVRGRVLHAANEGVVSRFGQARAVFEECGADPQRVRPVSSAQFPRPAPRSSYSALSSRQWALAGLTPLRHWRSALATALAAPANSTSIDRRLPSTRD
Protein: Homeobox protein Wariai (Homeobox protein 1) (DdHbx-1) (Q54F46)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Putative transcription factor, that seems to be involved in anterior-posterior patterning of the slug, probably by controlling the proportions of prestalk and prespore cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
- Uncharacterized protein
Sequence:
MASIVMKSQHSLGYPNIGNINRSDYDSYEQQYNNPTGSKQYNNNNNNNTNTNEINNGTNTNLNPNNMYGMYNNNNNNNNNNNNNNNNNNNNNNSNNNNNNNNNNNINNNNNNNNNNNNNNNNNNQHLSQSQQLSPTPYSSNSFSKLLSRSTNDLMLDQDDPSKKKRKRTSPDQLKLLEKIFMAHQHPNLNLRSQLAVELHMTARSVQIWFQNRRAKARNMEFKPQLSHGGSDLIYNALGSQNGMNSMGGGGGNGGGNGGGGMNGINNILNGNHNRNLNKYIPHGGNSINGNMGGGGGGGGGSHNHHHHNHNHNHHNHNHNHNHNQPLSNGDCGEKFSVASAWNKILLHPNNIDFLIRYNPDDPNSIDVNARDSKGLSLLFTAAFLGYEYQVRRLIESGANPNIKDNQGNTPLIAASVLGNQPIVELLLEHRADPNLVNDEGVSPLFSACKGGHLQIASSLLDHDAEVSVKTKINGETPLHIASLKGFEKICKLLIETEAKASVIDSNNRTPLHHACIMGYFSIAKLLICNGADMNAIDIDGHTPLHTSSLMGHDLITRLLLENGADPNIQDSEGYTPIHYAVRESRIETVKFLIKFNSKLNIKTKNGQNLIHLSVQFASLMMGQMIFESKGCEIAADDSDDQGYTPLYLAAKAGKTNFVKYLLSKGASKKIALEKLIQENQDKEIIQMLESTVTKSSNNNNSNSNINNINNINNINNINSQPNTNSDNNNNNNNNNFNENYSNGNNEQSQPPGNKFEEDDEDDFYDRVYKKSYTNRIISNSFSYQQKLNSGNGISVNSGNLED
Protein: Ovochymase (HrOVCH) (EC 3.4.21.-) (A0A182C2Z2)
Organism: Halocynthia roretzi (Sea squirt) (Cynthia roretzi)
Function: May be responsible for elevation of the vitelline coat at the late developmental stage of oogenesis and during fertilization in ovarian eggs.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P79953}.
Interaction partners:
Sequence:
MIVTFVALALSCCTPQVTADCGLRPRLQSAIITGRIVGGEMAKLGEFPWQAAFLYKHVQVCGGTIIDTTWILSAAHCFDPHMYKLQSIKKEDALIRVADLDKTDDTDEGEMTFEVKDIIIHEQYNRQTFDNDIMLIEILGSITYGPTVQPACIPGANDAVADGTKCLISGWGDTQDHVHNRWPDKLQKAQVEVFARAQCLAAYPESTENMICAGLRTGGIDSCQGDSGGPLACPFTENTAQPTFFLQGIVSWGRGCALDGFPGVYTEVRKYSSWIANYTQHLLQDRNADVATFTITGDPCSSNGSIISGSEGDFSSPGFYSGSYTDNLDCKWIIQIPDIGSRIQLSFTEFGVEYHTFCWYDDVKVYSGAVGNIASADAADLLGSHCGMNIPSDLLSDGSSMTVIFHSDYMTHTLGFRAVFHAVSADVSQSGCGGIRELLTDHGEFSSKHYPNYYDADSICECFITAPTGKTIELNFLSFRLAGSDCADNVAIYDGLNSSYPRIIRLCINQGFNVTVPSSSNTMFVSFKTDGQVQDVGFEAYYYFSSNGNSTDDTDYSQCGFSSTPINADQTAARIVNGDIAIAGSWPWQISIRLCDTCNHYCGGSIISPSWIVTAAHCIESSAHITYIRAGDFDRFTIEISETIVPVAQIFIHPDYQKDLPNNADIALLKLANPLSYSSTIRPVCFPSQISTIPEENAECYVTGWGLTEENVMAQKLREAKLPLMPYDQCLNVYTSYVLNENMLCAGNISSGIDTCLGDSGGPFVCRKSRNDPWILYGVSAFGRECGSSRYPGVYTKVTRYIDWIIATANVSTVTSVVEEHDPTEFEQGCIQLLVLSNHEGDLSSPEYPELYGEGMLDCQWKIVLMDRTKSLNINFRFSHSQQDTAAACSLANIRISESYSDGTVGRQYGPYCGSSESILISSLHDLVVSLHNSQSQVKIGLKLEYRLEELEQSGCGQLKHLIENKGNFSSINYPNIYSANSHCEWYLHASIATHYLQISLSQFSLENAYQCRYDFLTVIDVTENGNISHGPYCGNSIPHVITGHGLFHIKFRSDASLNYKGFFASFVELNERPQEESGCGGVKFLNGTNGTFQTAGFPLAYEANLDCTWVIEVEDGYKVRLNFQQFSLESSSSCKYDWAMLYNGEFAFEAQRIDTLCGYDVKLEDIFESTSNVMRIDFHSDFSFNKQGFLAMYTAVSPGSSRSSVHQRENHLQEKRSGGCQDSIFTDEEGVIEYKQGDHTGNTRCLFRILTNHLHVIRLWLRKLSSLNLHENDSIKIYDKIDVDDIYSGVVKPVFQFTGIIGYLDSLPAYLDYNGGEISMLFSSDGQHGDTSFELIYKLMQDKSSTTNPKQLWNDHHGKWPWMVSLFGSSKYYFCSGVIISSRWIATAATCNLRSSEIHIIFPEGTNPKKIWEVEKIVVHPEFKMIYNVPQNDLALIQLVDPIEHIPPVCLPVASNIYSDCHVLKIPRLAGSAAFPDIVRISSVDTLAHDICMREWHLRITDDMLCGRINGTNSCQRDVGGPLVCQSPSDDAWYFVGISSWGPKICNDNTAHHRLPDVYVSVAYFLKWITKIIQ
Protein: SET domain-containing protein (Q388V8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPTQSPPALLRNLHCSLPTIVRLYKDIASSLNCPSREDSIKMLLPLEISTAADGEEVINFFCRELGMSVTSLRRWRCAVMSGMRRNWWRDCMRNKLAVVPTGTLSPNMDDFLFARSCITDLKAVISPFLTLAQPEAANAPRGSSFVATRNILPGVFLLSVPTSAIFFSSPPPATDPLTSFFMHVEDLVGQLVAVECSGDPPPSHAGYVDYLKKSVTPCNNLPFLEMGEVTQLLGKAKSSVGVTTGLEDTSSPALQLWEYFHRDMEGLPLSVFLRERLTKEEYAWWVSLVLSRRTGAATLIPVVDKLNHSPEPNCYYTMATEESFCGIDVFDNMLAGVDSELLYEPYLHTFSIREIKEGEELSLCYASPATNPKQRGVVGAPVSGGGDGISVATGEGRAAWQLQWGFIPSIDSPYTSADLLEVATIVAERRVDIRQKLFPP
Protein: Serine/threonine-protein kinase ppk33 (EC 2.7.11.1) (O74426)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- cAMP-dependent protein kinase regulatory subunit
- Meiotically up-regulated gene 112 protein
- Meiotically up-regulated gene 133 protein
Sequence:
MGNSNSKSVKNDKENFEDPNATNFESVSQFKIRNVIGKGSWSTVFVVKHRQTKQRFALKCINKKKHDEHKIKKLRNEVLLLQSLNHPLLCKFYSEFEDETKIYLVTDLMLGGDLRYHISQRKFNESVIRIWMVELVSALIYIHSKGVLHRDVKPDNILLDEKGHCKLADFNVAAKVHTSSSPSKSNMTVGRVGTPVYMAPETLIHAVSYKESDWWSLGITFYECLFQVRPFPNHLLINWIRASEEEKASSADRLSSALHISRDKKLTTISKDARSAVMAFLEMDIKKRLGHSSKKLQTHPFFCSISLETVSKGNLTPIFRPKSGKVYVDPILDLEATF
Protein: Glutamate--cysteine ligase, chloroplastic (EC 6.3.2.2) (Gamma-ECS) (GCS) (Gamma-glutamylcysteine synthetase) (Protein ROOT MERISTEMLESS 1) (AtGCL) (Protein cadmium-sensitive 2) (Protein phytoalexin-deficient 2) (P46309)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Seems to play an important role in controlling the expression of resistance responses like the regulation of salicylic acid (SA) and phytoalexin (camalexin) production. Involved in resistance to fungal and bacterial pathogens. Required for the regulation of cell proliferation in root apical meristems through the GSH-dependent developmental pathway. Also participates in the detoxification process, the antioxidant response and is essential for embryo development and proper seed maturation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15610346}.
Interaction partners:
- Glutathione synthetase, chloroplastic
- Bifunctional cystathionine gamma-lyase/cysteine synthase
- Cysteine synthase 1
- 5-oxoprolinase 1
- Gamma-glutamylcyclotransferase 2-1
- Glutathione hydrolase 1
- Branched-chain-amino-acid aminotransferase 3, chloroplastic
- Glutathione hydrolase 3
- Putative inactive glutathione hydrolase 4
- Cystathionine beta-lyase, chloroplastic
Sequence:
MALLSQAGGSYTVVPSGVCSKAGTKAVVSGGVRNLDVLRMKEAFGSSYSRSLSTKSMLLHSVKRSKRGHQLIVAASPPTEEAVVATEPLTREDLIAYLASGCKTKDKYRIGTEHEKFGFEVNTLRPMKYDQIAELLNGIAERFEWEKVMEGDKIIGLKQGKQSISLEPGGQFELSGAPLETLHQTCAEVNSHLYQVKAVAEEMGIGFLGIGFQPKWRREDIPIMPKGRYDIMRNYMPKVGTLGLDMMLRTCTVQVNLDFSSEADMIRKFRAGLALQPIATALFANSPFTEGKPNGFLSMRSHIWTDTDKDRTGMLPFVFDDSFGFEQYVDYALDVPMYFAYRKNKYIDCTGMTFRQFLAGKLPCLPGELPSYNDWENHLTTIFPEVRLKRYLEMRGADGGPWRRLCALPAFWVGLLYDDDSLQAILDLTADWTPAEREMLRNKVPVTGLKTPFRDGLLKHVAEDVLKLAKDGLERRGYKEAGFLNAVDEVVRTGVTPAEKLLEMYNGEWGQSVDPVFEELLY
Protein: Protein phosphatase 2C homolog 3 (PP2C-3) (EC 3.1.3.16) (P34221)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible, together with PTC2, for the dephosphorylation of the cyclin-dependent protein kinase CDC28.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12477803, ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:12477803, ECO:0000269|PubMed:14562095}.
Interaction partners:
- Polyamine N-acetyltransferase 1
- Serine/threonine-protein phosphatase 4 catalytic subunit
- Protein phosphatase 2C homolog 2
- Tyrosine-protein phosphatase 3
- Mitogen-activated protein kinase HOG1
- Tyrosine-protein phosphatase 2
- Ribosome biogenesis protein TSR1
- Protein phosphatase 2C homolog 7, mitochondrial
Sequence:
MGQILSNPIIDKEHHSGTDCLTAFGLCAMQGWRMSMEDAHIVEPNLLAESDEEHLAFYGIFDGHGGSSVAEFCGSKMISILKKQESFKSGMLEQCLIDTFLATDVELLKDEKLKDDHSGCTATVILVSQLKKLLICANSGDSRTVLSTGGNSKAMSFDHKPTLLSEKSRIVAADGFVEMDRVNGNLALSRAIGDFEFKSNTKLGPHEQVVTCVPDIICHNLNYDEDEFVILACDGIWDCLTSQECVDLVHYGISQGNMTLSDISSRIVDVCCSPTTEGSGIGCDNMSISIVALLKENESESQWFERMRSKNYNIQTSFVQRRKSIFDFHDFSDDDNEVFAITTKKLQDRLNRSKDNDDMEIDDLDTELGSSATPSKLSGEDRTGPIDLFSLEALLEAGIQIRQRPSSDSDGNTSYFHGASLSDMLASLSNAAAGETEPNDADDNDDNDGEENGKNENAKKGSKIEEIE
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 2 (Complex I-B8) (CI-B8) (NADH-ubiquinone oxidoreductase B8 subunit) (O43678)
Organism: Homo sapiens (Human)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:12611891}; Peripheral membrane protein {ECO:0000305}; Matrix side {ECO:0000305}.
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 1
- NADH dehydrogenase iron-sulfur protein 8, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 10, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 6
- Cytochrome b-c1 complex subunit 9
- NADH dehydrogenase iron-sulfur protein 2, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- NADH dehydrogenase 1 alpha subcomplex subunit 8
Sequence:
MAAAAASRGVGAKLGLREIRIHLCQRSPGSQGVRDFIEKRYVELKKANPDLPILIRECSDVQPKLWARYAFGQETNVPLNNFSADQVTRALENVLSGKA
Protein: WD repeat-containing protein 55 (Protein hokecha) (B2ZZS9)
Organism: Oryzias latipes (Japanese rice fish) (Japanese killifish)
Function: Nucleolar protein that acts as a modulator of rRNA synthesis. Plays a central role during organogenesis, including thymus development.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:18769712}.
Interaction partners:
- RED-like N-terminal domain-containing protein
- Ribosome biogenesis protein WDR12
- Protocadherin 2 alpha a 1
- Lymphocyte cytosolic protein 2a
Sequence:
MAAPPEHAATGSEQTDPPETNSEPDLSQPEPADSDADEPVGPKIRETPEDIRLEAIANTVALHPSRDVLVCGDVDGDVYAYAYSCTEGETRELWSSGHHLKSCRQVRFSADGLKLYSVSRDKAVHQLDVERGQLVSRIRGAHAAAINSLLLVDENILATGDDRGTLKVWDMRKGEAFMDLKHHDDYISDIAVDQAKRILLTTSGDGTMGVFNIKRRRFELLSEFQSGDLTSVALMKRGKKVVCGSSEGTVYIFNWNGFGATSDRFAVKAESVDCIVPITDSIMCTASMDGYIRAINLLPNRVIGCIGQHVGEPIEEINKSWDSRFLVSCAHDQLIKFWEISNLQKTTVSDYRKRKKKDGRMKSLTKKALGDNDFFSGLVEETEKKEEEEEEEEDSDSDSD
Protein: Thymosin beta (A2AF31)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245, ECO:0000256|PIRNR:PIRNR001828}.
Interaction partners:
Sequence:
MSDKPDLSEVETFDKAKLKKTNTEVKNTLPSKETIQQEKEHNERT
Protein: Cell division protein FtsX (P95357)
Organism: Neisseria gonorrhoeae
Function: Part of the ABC transporter FtsEX involved in cellular division.
Subcellular location: Cell inner membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MSIIHYFSLHVESARSALKQLLRQPFGTLLTLIMLAVAMTLPLFMYLGIQSGQSVLGKLNESPQITVYMETAAAQSDSDTVRSLLTRDKRLDNIRFIGKEDGLAELQSNLDQNLISMLDGNPLPDVFIVTPDPATTPAQMQAIYRDITKLPMVESASMDTEWVQTLYQINEFIRKILWFLSLTLGMAFVLVAHNTIRLQILSRKEEIEITKLLGAPASFIRRPFLYQAMWQSIFSAAVSLGLCGWLLSAVRPLVDAIFKPYGLNIGWRFFYVGELGLVFGFVIALGVFGAWLATTQHLLCFKAKK
Protein: GDNF family receptor alpha-4 (GDNF receptor alpha-4) (GDNFR-alpha-4) (GFR-alpha-4) (Persephin receptor) (Q9EPI2)
Organism: Rattus norvegicus (Rat)
Function: Receptor for persephin. Mediates the GDNF-induced autophosphorylation and activation of the RET receptor. May be important in C-cell development and, in the postnatal development of the adrenal medulla.
Subcellular location: [Isoform A]: Cell membrane {ECO:0000269|PubMed:10958791}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:Q9GZZ7}.; SUBCELLULAR LOCATION: [Isoform B]: Secreted {ECO:0000305|PubMed:10958791}.
Interaction partners:
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Persephin
- Neurturin
- Artemin
- Glial cell line-derived neurotrophic factor
- Growth/differentiation factor 15
Sequence:
MLSGAYLRVLNERPGQAVLWSLGCQRGSASSTEGNRCVEAAEACTADEQCQQLRSEYVAQCLGRAGWRGPGSCVRSRCRRALRRFFARGPPALTHALLFCGCEGPACAERRRQTFAPACAFSGPQLAPPSCLKPLDRCERSRRCRPRLFAFQASCAPAPGSRDGCPEEGGPRCLRAYAGLVGTVVTPNYLDNVSARVAPWCGCEASGNRREECEAFRKLFTRNPCLDGAIQAFDSSQPSVLQDQWNPYQNAGCCFLWVSSMSILTALALQALL
Protein: PcfG (Putative relaxase) (Q7X5P3)
Organism: Enterococcus faecalis (Streptococcus faecalis)
Interaction partners:
Sequence:
MVYTKHFVIHTFDKLNNACSYIENAEKTEVTNDNPSEHLEHLFQYIVNDDKTYMKKLVSGHGIVDPTNPYEEFKLTKLQAAIQRKIGYTFDPKSERLLPPTLTELEKGNAVLAHHLIQSFSPEDDLTPEKIHEIGYNTVMELTGGKYEFVIATHVDKEHLHNHIIFSSTNLKTGKAFRWQKGTKRVFEQISDKIAAKEGAKIIEKSPKQTHTKYTKWQTESIYKQKIKSRLDFLLEQSSSINDFLEKAEALNLSADFSNKWTTYRLLDEPQIKNTRSRSLSKSDPTRYNYEKIIERLKENKNVLTVEECVKRYEEKNEQEKNNFDYQFTIEPWQLSHKTERGYYINIDYGYGNSGKLFVGGYKVDPLDNGNYNIYIKRNEYFYFMSDKDATKSKYLTGASLIKQLRLYNGQTPLKREPVMQTIDELVSAINFLAANEIEDTRQLKLLEEKLEVAFLEAEKTLETLDEKMLELHQLSNLLLENELQGDPELIQKKLKTLLPDATLAEFSYEDVRGEIEAIKTSQTLLESKLERTRNEINQLHEIQAVQEKEPEKQTDIKPKL
Protein: Enhancer of mRNA decapping 3 (H3BSQ0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKNKDDECFGDDIEEIPDTDFDFEGNLALFDKAAVFEEIDTYERRSGTRSRGIPNERPTRYRHDENILESEPIVYRRIIVPHNVSKEFCTDSGLVVPSISYELHKKLLSVAEKHGLTLERRLEMTGVCASQMALTLLGGPNRLNPKNVHQRPTVALLCGPHVK
Protein: Purine nucleoside phosphorylase LACC1 (EC 2.4.2.1) (Adenosine deaminase LACC1) (EC 3.5.4.4) (Fatty acid metabolism-immunity nexus) (Guanosine phosphorylase LACC1) (Laccase domain-containing protein 1) (S-methyl-5'-thioadenosine phosphorylase LACC1) (EC 2.4.2.28) (Q8BZT9)
Organism: Mus musculus (Mouse)
Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine, guanosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine, guanine and hypoxanthine (By similarity). Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate (By similarity). Also has adenosine deaminase activity (By similarity). Acts as a regulator of innate immunity in macrophages by modulating the purine nucleotide metabolism, thereby regulating the metabolic function and bioenergetic state of macrophages. Enables a purine nucleotide cycle between adenosine and inosine monophosphate and adenylosuccinate that prevents cytoplasmic acidification and balances the cytoplasmic-mitochondrial redox interface. The purine nucleotide cycle consumes aspartate and releases fumarate in a manner involving fatty acid oxidation and ATP-citrate lyase activity. Participates in pattern recognition receptor-induced cytokines in macrophages: associates with the NOD2-signaling complex and promotes optimal NOD2-induced signaling, cytokine secretion and bacterial clearance (By similarity). Localizes to the endoplasmic reticulum upon PRR stimulation of macrophages and associates with endoplasmic reticulum-stress sensors, promoting the endoplasmic reticulum unfolded protein response (UPR) (By similarity). Does not show laccase activity (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30510070}. Nucleus {ECO:0000269|PubMed:30510070}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8IV20}. Peroxisome {ECO:0000250|UniProtKB:Q8IV20}. Note=Upon stimulation of the pattern-recognition receptor (PRR) NOD2, localizes to the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q8IV20}.
Interaction partners:
- Pyridoxal phosphate homeostasis protein
Sequence:
MAEAVLIDLSGLQLNAQKNCHETLLETLDGIHYHHAPKAKFLCIICCRNASKEKDGEYGLCELEAGNGFSRLAGKFETVSHPCLAASLYTIKQKIDEENLSCIKVIVPEHRKLLMKAYVGQLFTEVYEFEFEDLQGAWRDSLLKPSTGINVTTTQELEDIQHEIETYLRSLPALKGDLTIVTSPLIPDNFLHGFTTRTGGISSVPTLSSLNLFSSSKRRDPKVVVQENVRRLANAAGFNAEKFYRIKTDHASEVWVMGKKEPESYDGIVTNQRGVTITALGADCIPIVFADPVKKACGVAHSGWKGTLLGVAMATVNAMIAEYGCDVEDIIVVLGPSVGSCCFTLPKESAVSFHSLHPSCVRHFDSPRPYVDIRKATRILLERGGILPQNIQDQKEDLDLCTSCHPEKFFSHVRDGLNFGTQIGFISLRE
Protein: Double C2 domain alpha (H3BSH4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MRGRRGDRMTINIQEHMAINVCPGPIRPIRQISDYFPRGPGPEGGGGGGGEAPAHLVPLALAPPAALLGATTPEDGAEVDSYDSDDATALGTLEFDLLYDRASCTLHCSILRAKGLKPMDFNGLADPYVKLHLLPGACKANKLKTKTQRNTLNPVWNEDLTYSGITDDDITHKVLRIAVCDEDKLSHNEFIGEIRVPLRRLKP
Protein: Eukaryotic translation initiation factor 1A, Y-chromosomal (eIF-1A Y isoform) (eIF1A Y isoform) (Eukaryotic translation initiation factor 4C) (eIF-4C) (O14602)
Organism: Homo sapiens (Human)
Function: Seems to be required for maximal rate of protein biosynthesis. Enhances ribosome dissociation into subunits and stabilizes the binding of the initiator Met-tRNA(I) to 40 S ribosomal subunits (By similarity).
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Lysine-specific demethylase 5D
- Small ribosomal subunit protein eS4, Y isoform 1
- Ubiquitin carboxyl-terminal hydrolase 9Y
- ATP-dependent RNA helicase DDX3Y
- Eukaryotic translation initiation factor 1
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS19
- Eukaryotic translation initiation factor 1b
- Small ribosomal subunit protein uS17
- Small ribosomal subunit protein uS3
Sequence:
MPKNKGKGGKNRRRGKNENESEKRELVFKEDGQEYAQVIKMLGNGRLEALCFDGVKRLCHIRGKLRKKVWINTSDIILVGLRDYQDNKADVILKYNADEARSLKAYGELPEHAKINETDTFGPGDDDEIQFDDIGDDDEDIDDI
Protein: NYN domain-containing protein (P96389)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- tRNA
- Trehalose monomycolate exporter MmpL3
- protein adenylyltransferase
- Ribonuclease VapC51
- Conserved protein
- Transmembrane protein
- Carboxylesterase/lipase Culp6
- Alpha-
- Terminal beta-
- Putative antitoxin Rv0268c
Sequence:
MSLTEDVTSQTSESLARHSVLAEDLSQDGLTSLGAPGARVLLVWDAPNLDMGLGSILGRRPTALERPRFDALGRWLLARTAEIVAGRPGISTEPEATVFTNIAPGSAEVVRPWVDALRNVGFAVFAKPKVDEDSDVDRDMLAHIDERYREGLAALVVASADGQAFRQPLEAVARSGTPVQVLGFREHASWALASDTLEFVDLEDIAGVFREPLPRIGLDSLPEQGAWLQPFRPLSSLLTSRV
Protein: Transcription factor 3 (K7EPH6)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
IYSPDHSSNNFSSSPSTPVGSPQGLAGTSQWPRAGAPGALSPSYDGGLHGLVGGSHPEDGLAGSTSLMHNHAALPSQPGTLPDLSRPPDSYSGLGR
Protein: Missing-in-metastasis, isoform H (A0A0B4K822)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLSLERDSSALGSLFQQIINDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGASKEIGTALTRVCLRHKAVETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTDGLQSLMDSHMQDVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSELGHLQEAMQSIALVTKEPSVLPQASEELIHDAKASINLYPESPGGGSGSQGGGCSNSLGSRKSSVCSISSMNSSGSSNSPGHHHYPRSLSQFVTPAIRLKPGESSDSGFCSSPALTTQTSNATNQTANVSTWPPHSQDGVDTLPPTADRPHTISTAYEKGHQRPPLTVYTFQNPETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSSLERPLSAQSNHRQGSGNNLLQRQCPSPIPAHITKELSAAHHAQQQQQQQNQQPQTPPTYVNMSELATMAALKQTNQQQKPSTPPLQQQSSIDSTSSQHSNDSTGSHQLLQQQQQHHQSQQNHHSATATRSHSISSTASSLHSHPSIDSTVACGSLVGQHNHSTSTNTNTTSPSSGSSTPQNHYSPLLTNSPTSTAAGTPSGSSLGPGSGLGFVYQVSSPTPPSSEVLKITEQAAAGQDQGPANSVADETDERSRASVLQKASMFEKAAAAAAVSPPAPMQIASGSPASGGGTRRSEAEQQEMGGAAGGGSTRIGRRSSINQSKPPPPVRRSSSVTPSPNASVGLQQQPQHATLSQQNHQLSSSSEHLPPPPPFMLDAMPQIPSSALKVSETVRALAAMRHQPASPVSLRRMQQQQQQQLQQQQQQQVQQQQPLLQSAHNSPLKEDLTVYYDSYLDLHAYAQALASGQQPGGQQMANQQRFTLQQQHQHLHQPQQPPVYQVDATFRTSSPAAGGGGGGGIYAQPKLVNSMSSFRTSSPSPNGHAHPLPPTQPKANPNLIAQLNARLSGKQQQHQQQQHIEGIYGNQQAPGGESIYMRSGLSMSQPQQQQHFDDYATSTNIEKTGSIRAKTKAEFLENLNAKLAKQGMSGRAFAVRNLINSKALPDPRICHESLMDQIKRGATLKRNQKINDRSAPKIH
Protein: Ketosamine-3-kinase (EC 2.7.1.172) (Fructosamine-3-kinase-related protein) (FN3K-RP) (FN3K-related protein) (Protein-psicosamine 3-kinase FN3KRP) (EC 2.7.1.-) (Q9HA64)
Organism: Homo sapiens (Human)
Function: Ketosamine-3-kinase involved in protein deglycation by mediating phosphorylation of ribuloselysine and psicoselysine on glycated proteins, to generate ribuloselysine-3 phosphate and psicoselysine-3 phosphate, respectively. Ribuloselysine-3 phosphate and psicoselysine-3 phosphate adducts are unstable and decompose under physiological conditions. Not able to phosphorylate fructoselysine.
Interaction partners:
Sequence:
MEELLRRELGCSSVRATGHSGGGCISQGRSYDTDQGRVFVKVNPKAEARRMFEGEMASLTAILKTNTVKVPKPIKVLDAPGGGSVLVMEHMDMRHLSSHAAKLGAQLADLHLDNKKLGEMRLKEAGTVGRGGGQEERPFVARFGFDVVTCCGYLPQVNDWQEDWVVFYARQRIQPQMDMVEKESGDREALQLWSALQLKIPDLFRDLEIIPALLHGDLWGGNVAEDSSGPVIFDPASFYGHSEYELAIAGMFGGFSSSFYSAYHGKIPKAPGFEKRLQLYQLFHYLNHWNHFGSGYRGSSLNIMRNLVK