wanglab/gogpt-training-data huggingface dataset:
Protein: GH13988p (Q8SWX5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLVEGLYLYMLVVKTFSGDNLRFNIYASIGWGGPALFVVTWAVAKSLTVTYSTPEKYEINCPWMQETHVDWIYQGPVCAVLIINLTFLLRIMWVLITKLRSANTVETRQYRKAAKALLVLIPLFGITYLVVLAGPSESGLMGHMFAVLRAVLLSTQGFSVSLFYCFLNSEVRNALRHHISTWRDTRTIQLNQNRR
Protein: Dual-specificity RNA methyltransferase RlmN (EC 2.1.1.192) (23S rRNA (adenine(2503)-C(2))-methyltransferase) (23S rRNA m2A2503 methyltransferase) (Ribosomal RNA large subunit methyltransferase N) (tRNA (adenine(37)-C(2))-methyltransferase) (tRNA m2A37 methyltransferase) (P36979)
Organism: Escherichia coli (strain K12)
Function: Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity. Unmodified tRNA is not a suitable substrate for RlmN, which suggests that RlmN works in a late step during tRNA maturation.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- tRNA-2-methylthio-N
- Ribosomal RNA small subunit methyltransferase B
- Ribosomal protein uS12 methylthiotransferase RimO
- Ribosomal large subunit pseudouridine synthase B
- Ribosomal RNA large subunit methyltransferase M
- Ribosomal RNA small subunit methyltransferase A
- Ribosomal RNA large subunit methyltransferase K/L
- Dual-specificity RNA pseudouridine synthase RluA
- Ribosomal RNA small subunit methyltransferase F
- Heme chaperone HemW
Sequence:
MSEQLVTPENVTTKDGKINLLDLNRQQMREFFKDLGEKPFRADQVMKWMYHYCCDNFDEMTDINKVLRGKLKEVAEIRAPEVVEEQRSSDGTIKWAIAVGDQRVETVYIPEDDRATLCVSSQVGCALECKFCSTAQQGFNRNLRVSEIIGQVWRAAKIVGAAKVTGQRPITNVVMMGMGEPLLNLNNVVPAMEIMLDDFGFGLSKRRVTLSTSGVVPALDKLGDMIDVALAISLHAPNDEIRDEIVPINKKYNIETFLAAVRRYLEKSNANQGRVTIEYVMLDHVNDGTEHAHQLAELLKDTPCKINLIPWNPFPGAPYGRSSNSRIDRFSKVLMSYGFTTIVRKTRGDDIDAACGQLAGDVIDRTKRTLRKRMQGEAIDIKAV
Protein: Ketohexokinase (EC 2.7.1.3) (Hepatic fructokinase) (P50053)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of the ketose sugar fructose to fructose-1-phosphate.
Interaction partners:
- Fructose-bisphosphate aldolase B
- Sorbitol dehydrogenase
- Fructose-bisphosphate aldolase C
- Fructose-bisphosphate aldolase A
- Hexokinase-2
- Hexokinase-1
- Hexokinase HKDC1
- Hexokinase-3
- Hexokinase-4
- Glucokinase regulatory protein
Sequence:
MEEKQILCVGLVVLDVISLVDKYPKEDSEIRCLSQRWQRGGNASNSCTVLSLLGAPCAFMGSMAPGHVADFLVADFRRRGVDVSQVAWQSKGDTPSSCCIINNSNGNRTIVLHDTSLPDVSATDFEKVDLTQFKWIHIEGRNASEQVKMLQRIDAHNTRQPPEQKIRVSVEVEKPREELFQLFGYGDVVFVSKDVAKHLGFQSAEEALRGLYGRVRKGAVLVCAWAEEGADALGPDGKLLHSDAFPPPRVVDTLGAGDTFNASVIFSLSQGRSVQEALRFGCQVAGKKCGLQGFDGIV
Protein: ATP synthase peripheral stalk subunit b, mitochondrial (ATP synthase F(0) complex subunit B1, mitochondrial) (ATP synthase peripheral stalk-membrane subunit b) (ATP synthase subunit b) (ATPase subunit b) (Q9CQQ7)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha(3)beta(3) subcomplex and subunit a/ATP6 static relative to the rotary elements.
Subcellular location: Mitochondrion. Mitochondrion inner membrane.
Interaction partners:
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
Sequence:
MLSRVVLSAAATAAPCLKNAAALGPGVLQATRAFHTGQPRLAPLPPLPEYGGKVRLGLIPEEFFQFLYPKTGVTGPYVLGTGLSLYFLSKEIYVITPETFSTISVVGLIVYVIKKYGASFGEFIDKLNEEKIAQLEEVKQSSMKQIQDAIDMEKAQQALVQKRHYLFDVQRNNIALALEVTYRERLHKAYKEVKNRLDYHISVQNMMRRKEEEHMIDWVEKHVVKSISVQQEKETIAKCIEDLKLLAKKAQAQPIM
Protein: Pyruvate kinase (EC 2.7.1.40) (Q7SXK3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGARIRRYSEVMALPDSFIQKQQLDASMADTFLEHLCLLDIDQEPITARNTSIICTIGPASRSITKLQEMVKAGMNIARLNFSHGTHQYHAETIRNVREAVETLTSDPLYYRPVAIALDTKGPEIRTGLVKGRADAEVTLERGALVRVVTAECEREQTDGSVIWMDYPSLTRVLKKDSRIYIDDGLLALRVLEIGDSWLQARVENGGVLGSSKGVNLPGAELLDLPAVSERDRSDLQFGVEQQVDMIFASFIRCAEDVRAVRDALGPQGHDIKIISKVESRQGVRNFEQVLQESDGVMVARGDLGIEIPAEKVFIAQKMMIGRCNSAGKPVICATQMLESMVHHARPTRAESSDVANAVLDGADCVMLSGETAKGHFPVEAVAMMHSICREAEAAIFHQQLFEELRRLTPLSSDPTEVTAIGAVESSYKCCAGAIIILTTSGRSAQLLSRYRPRCPIIAVTRNAQVARQSQLLRGVFPALFRAPPAEVWADDVDNRVTFAMDIGKARGFFRSGDMVIVVTGWSPGSGHTNIMRAVTVP
Protein: 6-phosphogluconolactonase 4 (6PGL) (EC 3.1.1.31) (P53315)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in the pentose phosphate pathway via hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15454531}.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- 6-phosphogluconate dehydrogenase, decarboxylating 1
- Probable gluconokinase
- Phosphoglucomutase 2
- Inactive diphosphatase DCS2
- Exportin-T
- Transaldolase NQM1
- Glutamate decarboxylase
- Transketolase 2
Sequence:
MVKLQRFSEKKSLIHEFGKFILEKQESALTGDADAVFNIAISGGSMNQALYESLVNDKNIFPHIKWPQWRIFFCDERLVPFEDPQSNYGQFKKTVLDPLVHQGNQLNLGPTVYTINESLIGGGETANRKIAEEYASMLPASFDLILLGCGEDGHTCSLFPGVEFNYLVEEMDRKVLWCNNSPKAPKDRITFTLAVVAEAKSVCFLVRGAAKKAIMHDVLIVKNSELPSVLVNEMVGTKVTWFLDDEAGALIPENC
Protein: At3g52660 (Putative RNA-binding protein) (RNA-binding (RRM/RBD/RNP motifs) family protein) (Q9LXJ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Light-harvesting complex-like protein OHP1, chloroplastic
- Protein BROTHER of FT and TFL 1
- Protein CENTRORADIALIS-like
- F-box protein At4g00893
- E3 ubiquitin-protein ligase RKP
Sequence:
MSRTRTAASEAHDSMESEERVDLDGDNDPEEILEEEVEYEEVEEEEIEEIEEEIEEEVEVEEEEEEEDAVATEEEEEKKRHVELLALPPHGSEVYLGGIPTDATEGDLKGFCGSIGEVTEVRIMREKDSGDGKGYAFVTFRSKDLAAEAIDTLNNTDFRGKRIKCSTTQAKHRLFLGNVPRNWMESDIKKAANRIGPGVQIVELPKEPQNMGRNRGFAFIEYYNHACAEYSKQKMSNPSFKLDDNAPTVSWAESRSGGGGDSSASQVKALYIKNLPRDITQERLKALFEHHGKILKVVIPPAKPGKEDSRYGFVHYAERTSVMRALKNTERYEIDGHMLDCTLAKPQADQKTNTNTVQNVQKSQLQPNYPPLLSYGMAPSPFGALGGFGASAYSQPLMHAGGHAAGGMSMMPIMLPDGRIGYVLQQPGLAAMPQPPPRHSPPYRGGSGSSSSSGSKRSSDNGRGRSRYNPY
Protein: Bidirectional sugar transporter SWEET15 (AtSWEET15) (Protein SUGARS WILL EVENTUALLY BE EXPORTED TRANSPORTERS 15) (Senescence-associated protein 29) (Q9FY94)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates both low-affinity uptake and efflux of sugar across the plasma membrane. Regulates cell viability under high salinity. Promotes senescence and sensitivity to salt stress. Contributes to seed filling by triggering sucrose efflux involved in the transfer of sugars from seed coat to embryos.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20963606}; Multi-pass membrane protein {ECO:0000269|PubMed:20963606}. Golgi apparatus membrane {ECO:0000269|PubMed:25794936}.
Interaction partners:
- Senescence-specific cysteine protease SAG12
- NAC domain-containing protein 92
- Magnesium dechelatase SGR1, chloroplastic
- Transcription factor bHLH14
- Transcription factor bHLH13
- Transcription factor ABA-INDUCIBLE bHLH-TYPE
- Senescence-associated protein 13
- Probable chlorophyll
- Transcription factor MYC3
- Magnesium dechelatase SGR2, chloroplastic
Sequence:
MGVMINHHFLAFIFGILGNVISFLVFLAPVPTFYRIYKRKSTESFQSLPYQVSLFSCMLWLYYALIKKDAFLLITINSFGCVVETLYIAMFFAYATREKRISAMKLFIAMNVAFFSLILMVTHFVVKTPPLQVSVLGWICVAISVSVFAAPLMIVARVIKTKSVEYMPFTLSFFLTISAVMWFAYGLFLNDICIAIPNVVGFVLGLLQMVLYLVYRNSNEKPEKINSSEQQLKSIVVMSPLGVSEVHPVVTESVDPLSEAVHHEDLSKVTKVEEPSIENGKCYVEATRPETV
Protein: Pteridine reductase, putative (EC 1.5.1.33) (Q581W1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleoside 2-deoxyribosyltransferase
- Heat shock protein 83
- Sugar transporter, putative
- Adenosine kinase
- 4a-hydroxytetrahydrobiopterin dehydratase
- Glycine cleavage system P protein
- Nucleoside hydrolase, putative
Sequence:
MYCTEYKFPCFRHTHTIKLVLLHLRECNGVHPPQFYRRMYEWVGSVVIFSPTIIFAPIHDPYLEGGEKWRINNIVQGASISVAVKKKRKSPTYPLFRVKGVMEAPAAVVTGAAKRIGRAIAVKLHQTGYRVVIHYHNSAEAAVSLADELNKERSNTAVVCQADLTNSNVLPASCEEIINSCFRAFGRCDVLVNNASAFYPTPLVQGDHEDNSNGKTVETQVAELIGTNAIAPFLLTMSFAQRQKGTNPNCTSSNLSIVNLCDAMVDQPCMAFSLYNMGKHALVGLTQSAALELAPYGIRVNGVAPGVSLLPVAMGEEEKDKWRRKVPLGRREASAEQIADAVIFLVSGSAQYITGSIIKVDGGLSLVHA
Protein: Amino acid transporter (A0A3Q1MR13)
Organism: Bos taurus (Bovine)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU361216}.
Interaction partners:
- Excitatory amino acid transporter 1
- Amino acid transporter
- Sodium-coupled neutral amino acid symporter 2
- SLC3A2 protein
- Solute carrier family 7 member 5
- Aquaporin-4
- Neutral amino acid transporter 9
- Transporter
- Solute carrier family 7 member 1
- Glutamine synthetase
Sequence:
MPALRGQRIPGDESMVSANNMPKQVEVRMHDSHLSAEEPKPRHLGLRLCDKLGKNLLLTLTVFGVILGAVCGGLLRLASPIHPDVVMLIAFPGDILMRMLKMLILPLIISSLITGLSGLDAKASGRLGTRAMVYYMSTTIIAAVLGVILVLAIHPGNPKLKKQLGPGKKNDEVSSLDAFLDLIRNLFPENLVQACFQQIQTVTKKVLVAPPSDEDGNATNAVLSLLNETVTEVPEETQVVIKKGLEFKDGMNVLGLIGFFIAFGIAMGKMGEQAKLMVEFFNILNEIVMKLVIMIMWYSPLGIACLICGKIIAIKDLEVVARQLGMYMITVIVGLIIHGGIFLPLIYFLVTRKNPFSFFAGIFQAWITALGTASSAGTLPVTFRCLEENLGIDKRVTRFVLPVGATINMDGTALYEAVAAIFIAQMNGVVLDGGQIVTVSLTATLASVGAASIPSAGLVTMLLILTAVGLPTEDISLLVAVDWLLDRMRTSVNVVGDSFGAGIVYHLSKSELDTIDSQHRVHEDIEMTKTQSIYDDLKNHRESNSNQCVYAAHNSVIVDECKLSDRVQLCGDREVRQLTLLVLDQSAGLTPMHRGGSQSYRDEFAGFTQSIGVTFTPAFETLSGSVWFSKGTTLRFMMLHSC
Protein: Inward rectifier potassium channel 4 (BIR11) (Brain inwardly rectifying K(+) channel 2) (Inward rectifier K(+) channel Kir2.3) (IRK-3) (Potassium channel, inwardly rectifying subfamily J member 4) (P52190)
Organism: Rattus norvegicus (Rat)
Function: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. Can be blocked by extracellular barium and cesium (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:14960569}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle membrane {ECO:0000250|UniProtKB:P52189}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:P52189}; Multi-pass membrane protein {ECO:0000255}. Note=TAX1BP3 binding promotes dissociation of KCNJ4 from LIN7 famaly members and KCNJ4 internalization. {ECO:0000250|UniProtKB:P52189}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 12
- Potassium voltage-gated channel subfamily KQT member 3
- Potassium voltage-gated channel subfamily KQT member 2
- Inward rectifier potassium channel 2
- Potassium voltage-gated channel subfamily KQT member 4
- Potassium voltage-gated channel subfamily KQT member 1
- Potassium voltage-gated channel subfamily Q member 5
- Guanine nucleotide-binding protein G
- ATP-sensitive inward rectifier potassium channel 14
- Disks large homolog 4
Sequence:
MHGHSRNGQAHVPRRKRRNRFVKKNGQCNVYFANLSNKSQRYMADIFTTCVDTRWRYMLMIFSAAFLVSWLFFGLLFWCIAFFHGDLEPSPSGPTAGGPGGNGGGAAPTAAKPCIMHVNGFLGAFLFSVETQTTIGYGFRCVTEECPLAVIAVVVQSIVGCVIDSFMIGTIMAKMPRPKKRAQTLLFSHHAVISVRDGKLCLMWRVGNLRKSHIVEAHVRAQLIKPYMTQEGEYLPLDQRDLNVGYDIGLDRIFLVSPIIIVHEIDEDSPLYGMGKEELESEDFEIVVILEGMVEATAMTTQARSSYLASEILWGHRFEPVVFEEKSHYKVDYSRFHKTYEVAGTPCCSARELQESKITVLPAPPPPPSAFCYENELALMSQEEEEMEEEAAAAAAVAAGLGLEAGSKEETGIIRMLEFGSHLDLERMQAATLPLDNISYRRESAI
Protein: Uncharacterized protein CC285.14 (O74501)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Transport protein particle subunit trs120
- Transport protein particle subunit bet3
- Uncharacterized protein C15A10.12c
- Transport protein particle 20 kDa subunit
- Transport protein particle subunit trs31
- Transport protein particle subunit bet5
- Uncharacterized protein C13G6.05c
- Transport protein particle subunit trs23
- Transport protein particle subunit trs85-2
- GTP-binding protein ypt1
Sequence:
MSKKKPIVQYYDPFDLWPSIATDIESKIPLRNLQWVESYQYKKHTITSLDLEFLPWLEEFSSQDTSKDPTLLNIPLVNMLFLPEQDGEIYKTQHKPLATKWFQKVSKNENQSWMIVLVAEAQQAKRSNSLRRTHSRSSSYFAVKSTIDRVRGDFNTGNINHCVRLDYVRFGTPDAEGWNEFLKCLEWAVLSSLDSRFLQLSEQIRSIKLFDSSIFSDYLLFFLQKERLAASFFDLVLYRESLEQCEDMFSTLSKIISAIDGKKENISKYLGEGSDAQPDLKDFNSSFLILGSRYNTLHNLLADGDFTLFHFTLFLLSKIILLNLKISDYEKAFSTLQQALLFLTSSFFNEFVQNNLEIIAAFNYDCYTLLFKKITEAIHNNDTPIPLCCAKILLYARRQLTRMARWNNLIDDSSPLLWREPSFPLIEHHDNSLLDNRFQKLSETISSTSSFLSEYYRLSSEALSIFKAYKNRYSFVNTACDTGLAQYLLEDYENAYASLKNVDVQTAWSNDPLEEKWSKFYVDLLEKLEKFDEALEFASAISKGKVSIYNKNKILELSKKTAKSKVWNLDDFFTIEIPHMMAVVPHDDGINLSFMCESKVFDLESVDSVTCNYVLSSSKNPMNLLFTLHNSITDGKLNVHCNDIIPGRYHLKTIVFKLKDSVLSFQKDCLHSNKQIEVLNPTKHSNHLYILQSKISQQFQNDGIFACIPIMFGERFYKASCSEIKLSYIENSGFTNLEKSFLSEESHCGLESKTDSLVIKNIQKVPGVAKLYIPLTNTPVEGNEFLINLSYILESGQTVRFGKVLHIENAGIVEANCEKTNNMRDPLTSTIFLHIQPKEPIIFCSWNCMRKTKQGTYDNVFDIPYNIPVLSPMDCFTSCHFDSDMSIDLKFSMNCLRLADVVFMKLCVNIWERFDFIDIEHIMPLLDHACQQISLSNITQGTVVLPEEIRKLNGKKILNSFFDNEELRNEFSEFIQHLESEVSFNSLRSFVQEFEKKERLKNLPFYFSLHQTIGPLPFKDEMQSTTIEYIWKIPQKVLLNKPTEITLTFLRSLTHSKKEKQGQSFEIFYNFPAYTTTILFAGPTQRKIVWEKNQTTAQEQVTAVFLTAGRVMLPEVVVHSKDDDISILKNTKYTLVGRPLNDQPDLDYAP
Protein: Coilin (E9PTJ1)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar and coiled-body phosphoprotein 1
- Survival motor neuron protein
- Telomerase Cajal body protein 1
Sequence:
MSKMAASETVRVRLQFDYPPPATPHCTVFWLLVDLNRCRVVTDLISLIRQRFGFSSGALLGLYLEGGLLPPSESARLVRDNDCLRVKLEDQGLPEALIVSNGGDSNFPCRKSKKRAFKLVEDEETDQGYKYPDKYWKRQEDSGPNEKASDLETKLFPDEVRRTKNKRKSKVAGIPAEEDEEETKKKSSKRKEKCEQKKQTRASKSPKQQTHKEGGSQNCSFPRASYRSSLAKARRRSSTGAKGSPSYLSESESCPDSVSDGHCSVTTMQGVTLSEKLSAELLKDGATKTAAANRQSSKPSFTFSSGKGKASRASSSSSDSSSESEDQFLVSKNMLEGASDFLKTTGLFAGQGCSSPGLSLETPGIMGWKPSDSNRGRQAPGPNVPVPTSLGRGWGRGEDFLFGKGLRGRGIRGRGRGRGQTVSCILNRSSESQKQKQLNDILTNSSTVIQNPVETSKKDYSLLPLLAAAPQVGEKIAFKLLELTSDYSPDVSDYKEGKILSHDPETQQVDIEVLSSLPALKEPGKFDLVYHNENGTEVVEYAVTQEKRITVFWKELIDPRLIIDSSSSISNETQYPLQGREDSKACVRTTAQV
Protein: Brain serine protease (Serine protease (BSP)) (Serine protease (BSSP)) (O88301)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MKMLALCLVLAKSAWSEEQEKVVHGGPCLKDSHPFQAALYTSGHLLCGGVLIDPQWVLTAAHCKKPNLQVILGKHNLRQTETFQRQISVDRTIVHPRYNPETHDNDIMMVHLKNPVKFSKKIQPLPLKNDCSEENPNCQILGWGKMENGDFPDTIQCADVHLVPREQCERAYPGKITQSMVCAGDMKEGNDSCQGDSGGPLVCGGRLRGLVSWGDMPCGSKEKPGVYTDVCTHIRWIQNILRNKWL
Protein: Sphingosine kinase 2 (SK 2) (SPK 2) (EC 2.7.1.91) (Q9JIA7)
Organism: Mus musculus (Mouse)
Function: Catalyzes the phosphorylation of sphingosine to form sphingosine-1-phosphate (SPP), a lipid mediator with both intra- and extracellular functions. Also acts on D-erythro-dihydrosphingosine, D-erythro-sphingosine and L-threo-dihydrosphingosine. Binds phosphoinositides. In contrast to prosurvival SPHK1, has a positive effect on intracellular ceramide levels, inhibits cells growth and enhances apoptosis. In mitochondria, is important for cytochrome-c oxidase assembly and mitochondrial respiration. The SPP produced in mitochondria binds PHB2 and modulates the regulation via PHB2 of complex IV assembly and respiration. In nucleus, plays a role in epigenetic regulation of gene expression. Interacts with HDAC1 and HDAC2 and, through SPP production, inhibits their enzymatic activity, preventing the removal of acetyl groups from lysine residues with histones. Up-regulates acetylation of histone H3-K9, histone H4-K5 and histone H2B-K12. In nucleus, may have an inhibitory effect on DNA synthesis and cell cycle (By similarity). In mast cells, is the main regulator of SPP production which mediates calcium influx, NF-kappa-B activation, cytokine production, such as TNF and IL6, and degranulation of mast cells. In dopaminergic neurons, is involved in promoting mitochondrial functions regulating ATP and ROS levels. Also involved in the regulation of glucose and lipid metabolism.
Subcellular location: Lysosome membrane {ECO:0000250|UniProtKB:Q9NRA0}. Cytoplasm {ECO:0000269|PubMed:12954646, ECO:0000269|PubMed:16118219}. Cell membrane {ECO:0000269|PubMed:16118219}. Endoplasmic reticulum {ECO:0000269|PubMed:16118219}. Nucleus {ECO:0000269|PubMed:12954646, ECO:0000269|PubMed:20959514}. Mitochondrion inner membrane {ECO:0000269|PubMed:20959514, ECO:0000269|PubMed:25637806}. Note=In nucleus, is located in nucleosomes where it associates with core histone proteins such as histone 3. In apoptotic cells, colocalizes with CASP1 in cell membrane where is cleaved and released from cells in an active form. {ECO:0000250|UniProtKB:Q9NRA0}.
Interaction partners:
- Sphingosine-1-phosphate lyase 1
- Sphingosine-1-phosphate phosphatase 1
- Neutral ceramidase
- Acid ceramidase
- Sphingosine-1-phosphate phosphatase 2
- Alkaline ceramidase 2
- Ceramide synthase 2
- Alkaline ceramidase 1
- Alkaline ceramidase 3
- Ceramide synthase 5
Sequence:
MAPPPLLPVAASTPILHGEFGSYPANGPRFALTLTTQALHIQRLRPKPEARPRDGLVSLDEVSGCGTLQSRSPEDTAAYFCIYTYPRGRRGGRRRATRTFRADGATTYEENRAEAQRWATALTCLLRGVPLSGDQEITPELLPRKPRLLILVNPFGGRGLAWQRCMDHVVPMISEAGLSFNLIQTERQNHARELVQGLSLSEWEGIVTVSGDGLLYEVLNGLLDRPDWEDAVRMPIGVLPCGSGNALAGAVNHHGGFEQVVGVDLLLNCSLLLCRGGSHPLDLLSVTLASGSRCFSFLSVAWGFLSDVDIHSERFRALGSARFTLGAVLGLASLHTYRGRLSYLPATTEPALPIPGHSLPRAKSELVLAPAPAPAATHSPLHRSVSDLPLPLPQPALVSPGSPEPLPDLSLNGGGPELTGDWGGAGDAPLSPDPLLPSSPNALKTAQLSPIAEGPPEMPASSGFLPPTHSAPEASTWGPVDHLLPPLGSPLPQDWVTIEGEFVLMLGILPSHLCADLMAAPHARFDDGVVHLCWVRSGISRAALLRILLAMEHGNHFSLGCPHLGYAAARAFRLEPLTPRGLLTVDGELVEYGPIQAQVHPGLATLLTGPAGQKPQA
Protein: Cytochrome c oxidase subunit 2 (Q2F926)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}. Mitochondrion inner membrane {ECO:0000256|RuleBase:RU000457}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU000457}.
Interaction partners:
Sequence:
MILRSLECRFLTIALCDAAEPWQLGSQDAATPMMQGIIDLHHDIFFFLILILVFVSRMLVRALWHFNEQTNPIPQRIVHGTTIEIIRTIFPSVILLFIAIPSFALLYSMDGVLVDPAITIKAIGHQWYRPYEYSDYNSSDEQSLTFDSYTIPEDDPELGQSRLLEVDNRVVVPAKTHLRMIVTPADVPHSWAVPSSGVKCDAVPGRSNLTSISVQREGVYYGQCSEICGTNHAFTPIVVEAVTLKDYADWVSNQLILQTN
Protein: mRNA-capping enzyme regulatory subunit OPG124 (Virus termination factor small subunit) (VTF small subunit) (mRNA-capping enzyme 33 kDa subunit) (mRNA-capping enzyme D12 subunit) (mRNA-capping enzyme small subunit) (P04318)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: Regulatory subunit of the mRNA cap enzyme which stabilizes the catalytic subunit and enhances its methyltransferase activity through an allosteric mechanism. Heterodimeric mRNA capping enzyme catalyzes the linkage of a N7-methyl-guanosine moiety to the first transcribed nucleotide (cap 0 structure), whereas the methyltransferase OPG102 is responsible for a second methylation at the 2'-O position of the ribose (cap 1 structure). Also involved in early viral gene transcription termination and intermediate viral gene transcription initiation. Early gene transcription termination requires the termination factor VTF, the DNA-dependent ATPase NPH-I/OPG123 and the RAP94/OPG109 subunit of the viral RNA polymerase, as well as the presence of a specific termination motif. Binds, together with RAP94/OPG109, to the termination motif 5'-UUUUUNU-3' in the nascent early mRNA.
Subcellular location: Virion {ECO:0000305}. Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome.
Interaction partners:
Sequence:
MDEIVKNIREGTHVLLPFYETLPELNLSLGKSPLPSLEYGANYFLQISRVNDLNRMPTDMLKLFTHDIMLPESDLDKVYEILKINSVKYYGRSTKADAVVADLSARNKLFKRERDAIKSNNHLTENNLYISDYKMLTFDVFRPLFDFVNEKYCIIKLPTLFGRGVIDTMRIYCSLFKNVRLLKCVSDSWLKDSAIMVASDVCKKNLDLFMSHVKSVTKSSSWKDVNSVQFSILNNPVDTEFINKFLEFSNRVYEALYYVHSLLYSSMTSDSKSIENKHQRRLVKLLL
Protein: Protein unc-93 homolog B1 (Unc-93B1) (hUNC93B1) (Q9H1C4)
Organism: Homo sapiens (Human)
Function: Plays an important role in innate and adaptive immunity by regulating nucleotide-sensing Toll-like receptor (TLR) signaling. Required for the transport of a subset of TLRs (including TLR3, TLR7 and TLR9) from the endoplasmic reticulum to endolysosomes where they can engage pathogen nucleotides and activate signaling cascades. May play a role in autoreactive B-cells removal.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Endosome {ECO:0000250}. Lysosome {ECO:0000250}. Cytoplasmic vesicle, phagosome {ECO:0000250}. Note=Relocalizes from endoplasmic reticulum to endosome and lysosome upon cell-stimulation with CpG dinucleotides (By similarity). Colocalizes with LAMP5 in large endosomal intracellular vesicles. {ECO:0000250, ECO:0000269|PubMed:18082565, ECO:0000269|PubMed:21642595}.
Interaction partners:
- Toll-like receptor 3
- Toll-like receptor 7
- Toll-like receptor 9
- Toll-like receptor 8
- Protein canopy homolog 3
- Myeloid differentiation primary response protein MyD88
- Interferon beta
- Syntenin-2
- Serine/threonine-protein kinase TBK1
- Endoplasmin
Sequence:
MEAEPPLYPMAGAAGPQGDEDLLGVPDGPEAPLDELVGAYPNYNEEEEERRYYRRKRLGVLKNVLAASAGGMLTYGVYLGLLQMQLILHYDETYREVKYGNMGLPDIDSKMLMGINVTPIAALLYTPVLIRFFGTKWMMFLAVGIYALFVSTNYWERYYTLVPSAVALGMAIVPLWASMGNYITRMAQKYHEYSHYKEQDGQGMKQRPPRGSHAPYLLVFQAIFYSFFHLSFACAQLPMIYFLNHYLYDLNHTLYNVQSCGTNSHGILSGFNKTVLRTLPRSGNLIVVESVLMAVAFLAMLLVLGLCGAAYRPTEEIDLRSVGWGNIFQLPFKHVRDYRLRHLVPFFIYSGFEVLFACTGIALGYGVCSVGLERLAYLLVAYSLGASAASLLGLLGLWLPRPVPLVAGAGVHLLLTFILFFWAPVPRVLQHSWILYVAAALWGVGSALNKTGLSTLLGILYEDKERQDFIFTIYHWWQAVAIFTVYLGSSLHMKAKLAVLLVTLVAAAVSYLRMEQKLRRGVAPRQPRIPRPQHKVRGYRYLEEDNSDESDAEGEHGDGAEEEAPPAGPRPGPEPAGLGRRPCPYEQAQGGDGPEEQ
Protein: Vesicle transport protein USE1 (USE1-like protein) (Q5I940)
Organism: Mus musculus (Mouse)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004163}.
Interaction partners:
Sequence:
AQAEGAYHRPLATSRLELNLVRLLCRCESMAAEKREPDEWRLEKYVGALEDMLQALKVQASKPASEVISEYSRKVDFLKGMLQAEKLTSSSEKALANQLLAPGRVPTTAKERVPATKTVHLQSRARYTSEMRSELLGMEPSGECEVDMRKRAAKGSRPADERQSASELDLVLQRHQGLQEKLAEEMLGLARSLKTNTLAAQSVIKKDNQTLSHSLKMADQNLEKLKLESERLEQHAQKSVNWLLWAMLIVVCFVFISMILFIRIMPRLK
Protein: ENAH, actin regulator (A0A8I6G5W6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQEAVFYLGPTLPRQNSQLPAQVQNGPSQEEMEIQRRQLQEQQRQKELERERMERERLERERLERERLERERLEQEQLERQRQEREHVERLERERLERLERERQDRERERERLEQLEREQVEWERERRMSNAAPSSDSSLYSAPLPEYSSCQPPSAPPPSYAKVISAPVSDAAPDYAVVTALPPTSTPPTPPLRHSATRFATSLGSAFHPVLPHYATVPRPLNRNSRPSSPVNTPSSQPPAAKSCAWPTSNFSPLPPSPPIMISSPPGKATGPRPVLPVCVSSPVPQMPPSPTAPNGSLDSVTYPVSPPPTSGPAAPPPPPPPPPPPPPPPPPPPLPPLASLSHCGSQASPPPGTPLASTPSSKPSVLPSPSAAAPASVETPLNPELGDSSASEPGLQAASQPAETPAPQGHVLGPPAPPPPPPLPSGPAYASALPPPPGPPPPPPLPSAGPPPPPPPPPPLPNQVPPPPPPPPAPPLPASGIFSGSMSEDNRPLTGLAAAIAGAKLRKVSRVEDGSFPSGGNTVSVNLASSKTDSGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDRSEDAEPVTSKAASTSTPEPTRKPWERTNTMNGSKSPVISRPKSTPSSQPSANGVQTEGLDYDRLKQDILDEMRKELAKLKEELIDAIRQELSKSNTA