wanglab/gogpt-training-data huggingface dataset:
Protein: Bud site selection protein 20 (Q08004)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome. Involved in positioning the proximal bud pole signal.
Subcellular location: Nucleus {ECO:0000269|PubMed:11452010, ECO:0000269|PubMed:23045392}. Cytoplasm {ECO:0000269|PubMed:23045392}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000269|PubMed:23045392}.
Interaction partners:
- Eukaryotic translation initiation factor 6
- Proteasome-interacting protein CIC1
- Ribosome biogenesis protein RLP7
- Ribosome biogenesis protein RPF2
- Ribosome biogenesis protein 15
- Nucleolar GTP-binding protein 2
- Nuclear GTP-binding protein NUG1
- Ribosome biogenesis protein RLP24
- Nucleolar GTP-binding protein 1
- Ribosome assembly factor MRT4
Sequence:
MGRYSVKRYKTKRRTRDLDLIYNDLSTKESVQKLLNQPLDETKPGLGQHYCIHCAKYMETAIALKTHLKGKVHKRRVKELRGVPYTQEVSDAAAGYNLNKFLNRVQEITQSVGPEKESNEALLKEHLDSTLANVKTTEPTLPWAAADAEANTAAVTEAESTASAST
Protein: Auxin-responsive protein IAA26 (Indoleacetic acid-induced protein 26) (Q652A1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Aux/IAA proteins are short-lived transcriptional factors that function as repressors of early auxin response genes at low auxin concentrations.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Transport inhibitor response 1-like protein Os05g0150500
- Auxin response factor 11
- Auxin response factor 9
- Auxin response factor 7
- Auxin response factor 1
- Auxin response factor 14
- Auxin response factor 3
- Auxin response factor 2
- Auxin response factor 15
- Auxin response factor 16
Sequence:
MASYGDDGVELTELTLGPPGASARRARRGRKNGHPPPSSSMIQAAYFVKVSMDGTPYLRKVDVAAYGDYLELVEALNDMFYCSTIGLMDGYGEWEHAVVYEDGDGDWMLVGDVPWEMFVSSCKRMRVMRACEARGLSSNA
Protein: Transthyretin (Prealbumin) (TBPA) (P02767)
Organism: Rattus norvegicus (Rat)
Function: Thyroid hormone-binding protein. Probably transports thyroxine from the bloodstream to the brain.
Subcellular location: Secreted {ECO:0000269|PubMed:2309926, ECO:0000269|PubMed:873934}.
Interaction partners:
- Albumin
- Retinol-binding protein 4
- Thyroxine-binding globulin
- Vitamin D-binding protein
- Amyloid-beta precursor protein
- Low-density lipoprotein receptor-related protein 2
- Haptoglobin
- Alpha-1-antiproteinase
- Apolipoprotein E
- Uricase
Sequence:
MASLRLFLLCLAGLIFASEAGPGGAGESKCPLMVKVLDAVRGSPAVDVAVKVFKKTADGSWEPFASGKTAESGELHGLTTDEKFTEGVYRVELDTKSYWKALGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN
Protein: Nucleoporin SEH1 (Nuclear pore protein SEH1) (SEC13 homolog 1) (P53011)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. It is also required for normal nuclear morphology. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247}. Nucleus membrane {ECO:0000269|PubMed:10684247}; Peripheral membrane protein {ECO:0000269|PubMed:10684247}; Cytoplasmic side {ECO:0000269|PubMed:10684247}. Vacuole membrane {ECO:0000269|PubMed:21454883}; Peripheral membrane protein {ECO:0000269|PubMed:21454883}. Nucleus membrane {ECO:0000269|PubMed:10684247}; Peripheral membrane protein {ECO:0000269|PubMed:10684247}; Nucleoplasmic side {ECO:0000269|PubMed:10684247}. Note=Symmetric distribution. {ECO:0000269|PubMed:10684247}.
Interaction partners:
- Maintenance of telomere capping protein 5
- Nucleoporin NUP85
- SEH-associated protein 4
- Nucleoporin NUP120
- Nucleoporin NUP133
- Protein transport protein SEC13
- Nucleoporin NUP145
- Nitrogen permease regulator 2
- Restriction of telomere capping protein 1
- Nucleoporin NUP84
Sequence:
MQPFDSGHDDLVHDVVYDFYGRHVATCSSDQHIKVFKLDKDTSNWELSDSWRAHDSSIVAIDWASPEYGRIIASASYDKTVKLWEEDPDQEECSGRRWNKLCTLNDSKGSLYSVKFAPAHLGLKLACLGNDGILRLYDALEPSDLRSWTLTSEMKVLSIPPANHLQSDFCLSWCPSRFSPEKLAVSALEQAIIYQRGKDGKLHVAAKLPGHKSLIRSISWAPSIGRWYQLIATGCKDGRIRIFKITEKLSPLASEESLTNSNMFDNSADVDMDAQGRSDSNTEEKAELQSNLQVELLSEHDDHNGEVWSVSWNLTGTILSSAGDDGKVRLWKATYSNEFKCMSVITAQQ
Protein: UV radiation resistance-associated gene protein-like (A7DT33)
Organism: Caenorhabditis elegans
Interaction partners:
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Beclin homolog
- non-specific serine/threonine protein kinase
- SH3 domain-containing GRB2-like protein B1
- Vacuolar protein sorting-associated protein 16 homolog
- Ubiquitin-like protein atg-12
- Autophagy-related protein 5
- MRG domain-containing protein
- t-SNARE coiled-coil homology domain-containing protein
- Autophagy-related protein 9
Sequence:
MTTKNSTEDVAVDSDSLEKLQQVIKEVKEKETHLKTLRETIDDEDGLVVRYQMAQDLAIRVEEKEVKCKSYKTQIEMVQKLILAKRRIIYEVQEKIDKKNYDKMKLVEKTEGLGTQADNNVDTKLKNIKITRIMNRLVAYRKTFLLQEIMDVFKIDIDGGPASMKQNRVRSDCKCVLVDTIRGLHLPHIASIQLSPHNERETTAAIGLLIQMLHVISRVLEYSLRYPIVPAASFSKVYCPIDDKWATLSGWKKRSERERFLEGLSWLAKNIAQLRSDCGIPTPMADKTLSVLADWIRSVVEGKYVCIYDRPINNTSSPSSLLVNFQPPQDALPTDLPVP
Protein: Anastral spindle 2, isoform A (Q9XZ31)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Spindle assembly abnormal protein 6 homolog
- Spindle assembly abnormal 4
- Serine/threonine-protein kinase PLK4
- Centrosomal protein 135kDa, isoform B
- BcDNA.LD24702
- Asterless
- Anastral spindle 1, isoform A
- Centriolar coiled coil protein 110kDa, isoform B
- Centrosomin
- Pericentrin-like protein, isoform F
Sequence:
MFVPETEDMLPRLAPRPSAAVPMGHTNEIIGPTVPEVSILFGQPPQDPQMQPQQPNHAHQESSPRAAPTFASWKKQMLPRVNFSPILATELGPRTAPSSNSPCSSKEYQVMPRDRNYASDAQQTTNHMNCNAGGYNAEPKQQAYQSRRLSSSSNADVLTICAGTQTDPFNPSPPRKSLPQVVYSDIDVSNLANKSDLAALVSLVESVRHEQQQLRNLCEMILEQQQRAKPEAISKASSTTGTQCDILTTNQAGRRLSPIMQDYIAEEEEPLPPPQARVIPQFPSPRPHPPIAQSTGYRANTPQAKRIPQLAKPNTEKSMVMNELALKYLRQPVDELMKDMRLGASPKSPNPEPLRPIDNIGHAQSPNDISNASYKYLKKYRLLPEEQLEPVCPQSPMAATAPSPHIQLDLENIRNQPKLL
Protein: Adenylyl cyclase-associated protein (Q6YBS2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- PH domain and leucine-rich repeat protein phosphatase 1.
- PH domain and leucine-rich repeat protein phosphatase 2
- Profilin
- Family with sequence similarity 122B.
- Si:ch211-85n16.4.
- WD repeat domain 1.
- Cfl1 protein
- Cofilin-1
- Cofilin 2
- Cathepsin Lb
Sequence:
MADLAGLVQRLEVAVGRLESMSSSGSGGGPAAGSGAVGVYVEAYDGLISGPLAQYFTLSQKIGGDVLKHAEMMKQAFTSQRQLLATASCSQKPSDPVLNALLAPVSKAIQDVQAFREKNRSSPFFNHLSAVSESVPALGWVAMAPKPGPYVKEMQDAAMFYTNRVLKDYKEKDKTHVEWVNAYVTIWTELQAYIKQHHTTGLSWSKTGPVAAAAGGGAPAPPPPGPPPPPMDLNKSSGGDSEPTNRNALFASINKGSDITKGLKHVSDDQKTHKNPGLRGQTGPSVSGPKPFTPRPTATASPARSLPPVLELDGKKWKVENQEGAQNLVISDTELKQVVYGFKCNNSTLQVKGKINSITLDNCKKMGLVFDDVVGIVEVINCRDVKIQVIGKVPTISINKTDGCHVYLSKDSLSCEIVSAKSSEMNVLVPNKDGEFTEIPVPEQFKTVWDGSKLVTTATEIAG
Protein: DNA-binding protein HU-beta (HU-1) (NS1) (P0ACF4)
Organism: Escherichia coli (strain K12)
Function: Histone-like DNA-binding protein which is capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions.
Interaction partners:
- DNA-binding protein HU-alpha
- Integration host factor subunit alpha
- Chromosomal replication initiator protein DnaA
- DNA-binding protein H-NS
- Lon protease
- DNA-binding protein Fis
- Integration host factor subunit beta
- DNA topoisomerase 1
Sequence:
MNKSQLIDKIAAGADISKAAAGRALDAIIASVTESLKEGDDVALVGFGTFAVKERAARTGRNPQTGKEITIAAAKVPSFRAGKALKDAVN
Protein: Triose phosphate transporter (Q8I420)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKDNEKKNEYGTFPITINEGYSDNVGDNKLKSKGIYHKLFEKLKLALLFLTWYTLNVLYNVDNKKALNMVKLPWFISSMQLYVGWIFIFIYWISGMKKIPKIYSYDIFIRNILIQSVCHIFVHFGAVMAMSATSVSFTHVVKACEPVFTAIFSILLLKQYLKINKYIALLIIVGGVVCASMKELHFTWIAFWCATLSNFGSSIRSIYAKKMMTQKSLIGENLNASNIYAFITIISALISLPLVLAFEGKETYNFLVNYQGTNYTFKDVIFKIILSGMWYYFNNEVAFMCLERVNQITHALANSIKRVVIIVSSIIIFKTQITLLGAIGSAVAIFGAFLYSIF
Protein: Endoglucanase 1 (EC 3.2.1.4) (Cellulase I) (Endo-1,4-beta-glucanase) (Endoglucanase I) (EGI) (Q02934)
Organism: Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372) (Clostridium thermocellum)
Function: This enzyme catalyzes the endohydrolysis of 1,4-beta-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Principally active against barley beta-glucan.
Interaction partners:
- Cellulose 1,4-beta-cellobiosidase
- cellulase
- Endoglucanase B
- Beta-glucosidase A
- Cellulose 1,4-beta-cellobiosidase
- Cellulase/esterase CelE
- Xyloglucanase Xgh74A
- Glycosyltransferase 36
- Endoglucanase G
Sequence:
MRLVNSLGRRKILLILAVIVAFSTVLLFAKLWGRKTSSTLDEVGSKTHGDLTAENKNGGYLPEEEIPDQPPATGAFNYGEALQKAIFFYECQRSGKLDPSTLRLNWRGDSGLDDGKDAGIDLTGGWYDAGDHVKFNLPMSYSAAMLGWAVYEYEDAFKQSGQYNHILNNIKWACDYFIKCHPEKDVYYYQVGDGHADHAWWGPAEVMPMERPSYKVDRSSPGSTVVAETSAALAIASIIFKKVDGEYSKECLKHAKELFEFADTTKSDDGYTAANGFYNSWSGFYDELSWAAVWLYLATNDSSYLDKAESYSDKWGYEPQTNIPKYKWAQCWDDVTYGTYLLLARIKNDNGKYKEAIERHLDWWTTGYNGERITYTPKGLAWLDQWGSLRYATTTAFLACVYSDWENGDKEKAKTYLEFARSQADYALGSTGRSFVVGFGENPPKRPHHRTAHGSWADSQMEPPEHRHVLYGALVGGPDSTDNYTDDISNYTCNEVACDYNAGFVGLLAKMYKLYGGSPDPKFNGIEEVPEDEIFVEAGVNASGNNFIEIKAIVNNKSGWPARVCENLSFRYFINIEEIVNAGKSASDLQVSSSYNQGAKLSDVKHYKDNIYYVEVDLSGTKIYPGGQSAYKKEVQFRISAPEGTVFNPENDYSYQGLSAGTVVKSEYIPVYDAGVLVFGREPGSASKSTSKDNGLSKATPTVKTESQPTAKHTQNPASDFKTPANQNSVKKDQGIKGEVVLQYANGNAGATSNSINPRFKIINNGTKAINLSDVKIRYYYTKEGGASQNFWCDWSSAGNSNVTGNFFNLSSPKEGADTCLEVGFGSGAGTLDPGGSVEVQIRFSKEDWSNYNQSNDYSFNPSASDYTDWNRVTLYISNKLVYGKEP
Protein: Uncharacterized protein (Q382M8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MEGFCYTAAADAASEAKGGVPQLPHLSAAALGKASSRPLPHPAAAITTVELPSGSVVIAGGGSVISVEPLSSLLQSCSKEGECEACNDPLLGGVAVHSTVPGEKVTLTISSGLVSCIGTALLPGGTAAMCAVGTSAGSLCLFVVESRTGGNALALCKVCEASLCEYTDGLISADDIVLDVCVGLDPAGRPEFVAVATATVVVVIDTQCFNESLRANATEAVLRETVGSWQRTPCPTEKPVNETFYASFTASEVVRLLVPQRYRASFAVDIALLIVFDNGELRYVARRVVGGSLQLLTEHHRQRQLRHSTVGLGMLQHNSEGPIDGSHGSLALPHVLYAYSLSSVVHNVCTAAVGVSAATYKVVNNAALFFDDMSQTMRIIVVGAGTQLAECYGHQLRGTTGWWAITGAAVLARGTLDQRQLAAWGFDVPCSGALPRDRRGLACITVLEGGRVLFACGNELYVCTMADATTAVVDGSSGGGGGAYVALRQVHTCGSVVCGVACTGTRIDGRNVGVIGFGASLAALLF
Protein: Probable monooxygenase (O53762)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Nucleotide-binding protein Rv0566c
- Glycerol-3-phosphate dehydrogenase [NAD
- Putative S-adenosyl-L-methionine-dependent methyltransferase Rv0726c
Sequence:
MSVTPNAGCVDVVIVGAGISGLGAAYRIIERNPQLTYTILERRARIGGTWDLFRYPGVRSDSSIFTLSFPYEPWTREEGIADGAHIREYLTDMAHKYGIDRHIEFNSYVRAADWDSSTDTWTVTFEQNGVHKHYRSRFVFFGSGYYNYDEGYTPDFGGIEKFGGAVVHPQHWPEDLDYTGKKIVVIGSGATAVTLIPSLTDRAEKVTMLQRSPTYLISASKYSTFAAVVRKALPPKTSHLIVRMYNALLEAVFWFLSRKTPVFVKWLLRRTAIKNLPEGYDIETHFTPRYNPWDQRLCLIPDADLYNAITSGRAEVVTDHIDHFDATGIALKSGGHLDADIIVTATGLQLQALGGAAISLDGVEIDPRDRFVYKAHMLEDVPNLFWCVGYTNASWTLRADMTARATAKLLAHMAAHGHTRAAPHLGDEPMDEKPSWDIQAGYVKRAPYALPKSGTKRPWNVRQNYLADAIDYRFDRIEEAMVFGAA
Protein: Large ribosomal subunit protein eL20 (60S ribosomal protein L20-B) (A0A1D8PLC9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:35613268}.
Interaction partners:
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein eL15
- 60S acidic ribosomal protein P0
- Small ribosomal subunit protein eS1
- Large ribosomal subunit protein eL27
- Large ribosomal subunit protein uL5
- Small ribosomal subunit protein eS26
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein eS10
- Small ribosomal subunit protein uS10
Sequence:
MSRLNEYQVIGRNLPTESVPEPKLFRMRIFAPNTVVAKSRYWYFLQKLHKVKKASGEIVSVNIISEAKPTKVKTFGIWLRYESRSGIHNMYKEYRDVTRVGAVETMYQDLAARHRARFRSIHILKVVELEKTDDVKRQYVKQFLTKDLKFPLPHRVQKSKKLFQATAPTTFY
Protein: Probable plastid-lipid-associated protein 4, chloroplastic (Fibrillin-3a) (Plastoglobulin 25) (AtPGL25) (Q9LU85)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast thylakoid {ECO:0000269|PubMed:22274653}. Note=Located in thylakoid as a peripheral protein at the stromal side. {ECO:0000269|PubMed:22274653}.
Interaction partners:
- Probable plastid-lipid-associated protein 11, chloroplastic
- FAM10 family protein At4g22670
- Probable plastid-lipid-associated protein 9, chloroplastic
- Probable plastid-lipid-associated protein 3, chloroplastic
- Dihydrolipoyllysine-residue acetyltransferase component 3 of pyruvate dehydrogenase complex, mitochondrial
- Phytyl ester synthase 1, chloroplastic
Sequence:
MALPSCLKTGALMSPATGFNFSGSLMKSDSGFAVPTKLQSTRKGDRERLRVQAIFSFPPAFLTRNGRAEKQKQLKQELLEAIEPLERGATASPDDQLRIDQLARKVEAVNPTKEPLKSDLVNGKWELIYTTSASILQAKKPRFLRSITNYQSINVDTLKVQNMETWPFYNSVTGDIKPLNSKKVAVKLQVFKILGFIPIKAPDSARGELEITYVDEELRLSRGDKGNLFILKMFDPTYRIPL
Protein: Acyl-CoA 6-desaturase (EC 1.14.19.3) (Delta(6) fatty acid desaturase) (D6D) (Delta(6) desaturase) (Delta-6 desaturase) (Fatty acid desaturase 2) (Q9Z0R9)
Organism: Mus musculus (Mouse)
Function: Involved in the biosynthesis of highly unsaturated fatty acids (HUFA) from the essential polyunsaturated fatty acids (PUFA) linoleic acid (LA) (18:2n-6) and alpha-linolenic acid (ALA) (18:3n-3) precursors, acting as a fatty acyl-coenzyme A (CoA) desaturase that introduces a cis double bond at carbon 6 of the fatty acyl chain. Catalyzes the first and rate limiting step in this pathway which is the desaturation of LA (18:2n-6) and ALA (18:3n-3) into gamma-linoleate (GLA) (18:3n-6) and stearidonate (18:4n-3), respectively. Subsequently, in the biosynthetic pathway of HUFA n-3 series, it desaturates tetracosapentaenoate (24:5n-3) to tetracosahexaenoate (24:6n-3), which is then converted to docosahexaenoate (DHA)(22:6n-3), an important lipid for nervous system function (By similarity). It can also desaturate (11E)-octadecenoate (trans-vaccenoate) at carbon 6 generating (6Z,11E)-octadecadienoate (By similarity). In addition to Delta-6 activity, this enzyme exhibits Delta-8 activity with slight biases toward n-3 fatty acyl-CoA substrates (By similarity).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cytosolic phospholipase A2
- 85/88 kDa calcium-independent phospholipase A2
- Group XIIB secretory phospholipase A2-like protein
- Phospholipase A2 group V
- Group XIIA secretory phospholipase A2
- Group IIC secretory phospholipase A2
- Group IIF secretory phospholipase A2
- Cytosolic phospholipase A2 gamma
- Group IID secretory phospholipase A2
- Phospholipase A and acyltransferase 3
Sequence:
MGKGGNQGEGSTERQAPMPTFRWEEIQKHNLRTDRWLVIDRKVYNVTKWSQRHPGGHRVIGHYSGEDATDAFRAFHLDLDFVGKFLKPLLIGELAPEEPSLDRGKSSQITEDFRALKKTAEDMNLFKTNHLFFFLLLSHIIVMESLAWFILSYFGTGWIPTLVTAFVLATSQAQAGWLQHDYGHLSVYKKSIWNHVVHKFVIGHLKGASANWWNHRHFQHHAKPNIFHKDPDIKSLHVFVLGEWQPLEYGKKKLKYLPYNHQHEYFFLIGPPLLIPMYFQYQIIMTMISRRDWVDLAWAISYYMRFFYTYIPFYGILGALVFLNFIRFLESHWFVWVTQMNHLVMEIDLDHYRDWFSSQLAATCNVEQSFFNDWFSGHLNFQIEHHLFPTMPRHNLHKIAPLVKSLCAKHGIEYQEKPLLRALIDIVSSLKKSGELWLDAYLHK
Protein: Nucleoporin (Q57U40)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MHRKSIVSNYFISPEYSVAGSRVFTPNASAEEVTLSDAPTQLSLQITSPKTSIRPSAVSSLRFKRGREASWHGRYHNGSAGENTMGFMEAVAASVSRRGDVVAHSSCESHQNFMSRAGNFVESTTHSDSSDGYRYAKLPRKELIMIAGGEDSGEKEDLASFRKDLRRLQERHEQLNKVVEETREELRRSWEENDRLKMRADQSVKELRLEVAQLSKHVQLLEGRSTSVERSLASLNGMESLVECVQGELPSLRKEIGRNTTSIAVLERLLEDMKHQPRVSQVAVNSVSASASGQVTSLGAPPPALLNDERATSHSSTTPFSFGGAKPNANLSGQLTSSPAASNSVAGSKPEPASASAPSFTGVSATAGSVDKPSNPFGVSAASATTAGGSAPAPASNGTPSFGSAVTTTAPGGNASSPFDSSKNAGVSATATASSASYTFGGASTPASSTNKPPNPFAATVSFSPADGKGATPALAGTFSFSATGAADTLSDKPPTTPGAAPPVASPATSALPTNPFSPGSTTATAPTAGKPTTLFGGYATGDSSAATSAPAPGSAFSFGGIGTTAPASTVGFSFGGMPKVAETSTAGVNTTISPFSRAGSTAVTGATGSLGGFLFPSSSSATAAPLARGSEVKNDVFSNAKAVASSGASSVFGTGALMSAGVLSPPTPFGASAGVTNPFASSQRDGENASNPFGQGVQGLAAASTGTALPLLSQPPIGFSAPTVNANLGARRRTPKRF
Protein: Sodium/hydrogen exchanger 8 (Na(+)/H(+) exchanger 8) (NHE-8) (Solute carrier family 9 member 8) (Q9Y2E8)
Organism: Homo sapiens (Human)
Function: Na(+)/H(+) antiporter. Mediates the electoneutral exchange of intracellular H(+) ions for extracellular Na(+) in 1:1 stoichiometry. Acts as an Na(+)/H(+) exchanger in the trans-Golgi. Contributes to the regulation of pH regulation of Golgi apparatus, and consequently, in protein trafficking and endosomal morphology. In germ cells, plays a crucial role in acrosome biogenesis and sperm development, probably by playing a role in the fusion of the Golgi-derived vesicles that form the acrosomal cap (By similarity). Can also be active at the cell surface of specialized cells. In the small intestine, at the cell membrane, plays a major physiological role in transepithelial absorption of Na(+) and regulates intracellular pH homeostasis of intestinal epithelial cells. Acts as an important regulator of mucosal integrity in the intestine and in the stomach, could mediate the pH fluctuation necessary for mucin exocytosis or assist membrane trafficking of other proteins (By similarity). Plays a role in photoreceptor survival and in the maintenance of intracellular pH homeostasis in retinal pigment epithelium (RPE cells) (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:15522866}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus, trans-Golgi network membrane {ECO:0000269|PubMed:15522866, ECO:0000269|PubMed:20719963}; Multi-pass membrane protein {ECO:0000255}. Endosome, multivesicular body membrane {ECO:0000269|PubMed:20719963}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000269|PubMed:34288721}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, secretory vesicle, acrosome {ECO:0000250|UniProtKB:Q8R4D1}. Note=Intracellular versus plasma membrane-resident location may vary with cell type. Mainly localized to the mid- to trans-Golgi compartments but a proportion is also localized to multivesicular bodies (PubMed:15522866, PubMed:20719963). Localized at the apical membrane of polarized gastrointestinal epithelial cells (By similarity). Recruitment to the plasma membrane upon acid stimulation (By similarity). {ECO:0000250|UniProtKB:Q4L208, ECO:0000269|PubMed:15522866, ECO:0000269|PubMed:20719963}.
Interaction partners:
- Sodium/hydrogen exchanger 9B2
- Small ribosomal subunit protein RACK1
Sequence:
MGEKMAEEERFPNTTHEGFNVTLHTTLVVTTKLVLPTPGKPILPVQTGEQAQQEEQSSGMTIFFSLLVLAICIILVHLLIRYRLHFLPESVAVVSLGILMGAVIKIIEFKKLANWKEEEMFRPNMFFLLLLPPIIFESGYSLHKGNFFQNIGSITLFAVFGTAISAFVVGGGIYFLGQADVISKLNMTDSFAFGSLISAVDPVATIAIFNALHVDPVLNMLVFGESILNDAVSIVLTNTAEGLTRKNMSDVSGWQTFLQALDYFLKMFFGSAALGTLTGLISALVLKHIDLRKTPSLEFGMMIIFAYLPYGLAEGISLSGIMAILFSGIVMSHYTHHNLSPVTQILMQQTLRTVAFLCETCVFAFLGLSIFSFPHKFEISFVIWCIVLVLFGRAVNIFPLSYLLNFFRDHKITPKMMFIMWFSGLRGAIPYALSLHLDLEPMEKRQLIGTTTIVIVLFTILLLGGSTMPLIRLMDIEDAKAHRRNKKDVNLSKTEKMGNTVESEHLSELTEEEYEAHYIRRQDLKGFVWLDAKYLNPFFTRRLTQEDLHHGRIQMKTLTNKWYEEVRQGPSGSEDDEQELL
Protein: NUDIX domain, putative (AFU_orthologue AFUA_5G13840) (Q5BE28)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Glutamine-dependent NAD
- GTP cyclohydrolase 1
- nicotinate phosphoribosyltransferase
- Dihydroorotate dehydrogenase
- Flavoprotein, putative
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Sequence:
MPTETKSVRVGVAVFALSPENKFILGKRIGSHGADTWGLPGGHLEFGESWEECAARELIEETGVHVDKNSVQYLTATNDVFEKDGKHYVTIFVGVRVDGGQEPEIKEQLKCAEWRWVSWEELADDRKKQVEADQAKRETEGKKLFVPLLSLFEQRCGFQPVLN
Protein: Glutathione S-transferase F11 (AtGSTF11) (EC 2.5.1.18) (AtGSTF6) (GST class-phi) (GST class-phi member 11) (Q96324)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles and have a detoxification role against certain herbicides.
Subcellular location: Cytoplasm, cytosol {ECO:0000305}.
Interaction partners:
- Glutathione S-transferase U20
- Cytochrome P450 83A1
- Methionine--tRNA ligase, cytoplasmic
- Methylthioalkylmalate synthase 1, chloroplastic
- Cytosolic sulfotransferase 18
- Methionine aminotransferase BCAT4
- S-alkyl-thiohydroximate lyase SUR1
- Cytosolic sulfotransferase 17
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic
Sequence:
MVVKVYGQIKAANPQRVLLCFLEKDIEFEVIHVDLDKLEQKKPQHLLRQPFGQVPAIEDGYLKLFESRAIARYYATKYADQGTDLLGKTLEGRAIVDQWVEVENNYFYAVALPLVMNVVFKPKSGKPCDVALVEELKVKFDKVLDVYENRLATNRYLGGDEFTLADLSHMPGMRYIMNETSLSGLVTSRENLNRWWNEISARPAWKKLMELAAY
Protein: E3 ubiquitin-protein ligase EL5 (EC 2.3.2.27) (Protein ELICITOR 5) (RING-type E3 ubiquitin transferase EL5) (Q9LRB7)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Functions as a E3 ubiquitin-protein ligase in cooperation with the E2 ubiquitin conjugating enzymes UBC5A and UBC5B. Involved in root development. Required for the maintenance of cell viability after the initiation of root primordial formation. May mediate the degradation of cytotoxic proteins produced in root cells after the actions of auxin, cytokinin and jasmonic acid. Mediates 'Lys-48'-linked polyubiquitination of MBP in vitro.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17559513}; Single-pass membrane protein {ECO:0000269|PubMed:17559513}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 5B
Sequence:
MVRGVEQGGPAMDESSSSSSPSPVSAPAGQAAMTAGGIATVAAVLIVFAALTLAFVLLQCYCDERRRAVTTTSTSGRGRRPRPRRRSGSGGDGGTGGGVDPEVLRSLPVTVYSRSTAAAAAKEEEEEDDDGVECAVCLAELEDGEEARFLPRCGHGFHAECVDMWLGSHSTCPLCRLTVVVPPPPLPPVPPEPPASYTVSLPASVLLGLSDHGAGAVTMTAEGRSTLVIEIPESAASTTPRDAAARSSPSLARLRSLRRLWSFGRQGAAGSTSSCSCATGGDNDDGDVEHGVSVTVAIRAVEAATPARPPEAEAGARTAAAHVRN
Protein: Ubiquinone biosynthesis O-methyltransferase (2-octaprenyl-6-hydroxyphenol methylase) (EC 2.1.1.222) (3-demethylubiquinone-8 3-O-methyltransferase) (EC 2.1.1.64) (P17993)
Organism: Escherichia coli (strain K12)
Function: O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30686758}.
Interaction partners:
- 3-demethoxyubiquinol 3-hydroxylase
- 2-octaprenyl-6-methoxyphenol hydroxylase
- Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE
- 2-octaprenylphenol hydroxylase
- Ubiquinone biosynthesis accessory factor UbiJ
- Ubiquinone biosynthesis accessory factor UbiK
- 4-hydroxybenzoate octaprenyltransferase
- Ribose-5-phosphate isomerase B
- 3-octaprenyl-4-hydroxybenzoate carboxy-lyase
- Probable protein kinase UbiB
Sequence:
MNAEKSPVNHNVDHEEIAKFEAVASRWWDLEGEFKPLHRINPLRLGYIAERAGGLFGKKVLDVGCGGGILAESMAREGATVTGLDMGFEPLQVAKLHALESGIQVDYVQETVEEHAAKHAGQYDVVTCMEMLEHVPDPQSVVRACAQLVKPGGDVFFSTLNRNGKSWLMAVVGAEYILRMVPKGTHDVKKFIKPAELLGWVDQTSLKERHITGLHYNPITNTFKLGPGVDVNYMLHTQNK