wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase TOS3 (EC 2.7.11.1) (Target of SBF protein 3) (P43637)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: One of the three SNF1 protein kinases (with SAK1 and ELM1) which are required for growth on nonfermentable carbon sources and nonpreferred sugars and for response to environmental stress. Activates SNF1 by phosphorylation of its activation-loop 'Thr-210'. Required for the regulation by SNF1 of the transcription of a large set of genes, the modification the activity of metabolic enzymes, and the control of various nutrient-responsive cellular developmental processes. Phosphorylates also GAL83, MIG1 and SIP2.
Interaction partners:
- Carbon catabolite-derepressing protein kinase
- 5'-AMP-activated protein kinase subunit gamma
- SNF1 protein kinase subunit beta-3
- Serine/threonine-protein kinase ELM1
- SNF1 protein kinase subunit beta-1
- SNF1 protein kinase subunit beta-2
- SNF1-activating kinase 1
- Serine/threonine-protein phosphatase PP1-2
- Regulatory protein MIG1
Sequence:
MVLLKEPVQPLPRSSLLYNNASNSSSRIKETRKVKLLYNPLTKRQILNNFEILATLGNGQYGKVKLARDLGTGALVAIKILNRFEKRSGYSLQLKVENPRVNQEIEVMKRCHHENVVELYEILNDPESTKVYLVLEYCSRGPVKWCPENKMEIKAVGPSILTFQQSRKVVLDVVSGLEYLHSQGITHRDIKPSNLLISSNGTVKISDFGVAMSTATGSTNIQSSHEQLLKSRALGTPAFFAPELCSTEKEYSCSSAIDIWSLGVTIYCLLFGKLPFNANSGLELFDSIINKPLEFPSYEEMLNGATSGITMEEYTDAKDLLKKLLQKDPDKRIKLADIKVHPFMCHYGKSDAASVLTNLETFHELKVSPPSSCKRVELVSLPVNSSFASLDSVYMENFDHNNLRTGADRNSTYSPSIYDANTLSPSAYHNIGSRESSYSSFSSFTSSTAFASQISIQDAPAIGDQQCLIGESGSSLRVNSCEFPQYTTMSPVGEYPFESTEASLSSTLTPVGNVPQRIKAHLVEGKSNSKDDLRIEADASLVFEASDAQRTRRRMSLYKL
Protein: S-adenosylmethionine synthase isoform type-2 (AdoMet synthase 2) (EC 2.5.1.6) (Methionine adenosyltransferase 2) (MAT 2) (Methionine adenosyltransferase II) (MAT-II) (P31153)
Organism: Homo sapiens (Human)
Function: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate.
Interaction partners:
- Methionine adenosyltransferase 2 subunit beta
- S-adenosylmethionine synthase isoform type-1
- Betaine--homocysteine S-methyltransferase 1
- Methionine synthase
- S-methylmethionine--homocysteine S-methyltransferase BHMT2
- Tyrosine aminotransferase
- DNA
- DNA
- DNA
- Methylenetetrahydrofolate reductase
Sequence:
MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
Protein: Syntaxin 16 (A0A8I5ZW54)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004409}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004409}.
Interaction partners:
Sequence:
MALCVCLPMPFFCSSCADGPTATPQPQELDELADDRMALVSGISLDPEAAIGVTKRSPPKWVDGVDEIQYDVGRIKQKMRELASLHDKHLNRPTLDDSSEEEHAIEITTQEVTQLFHRCQRAVQALPSRARRTCSEQEERLLRNVVASLAQALQELSTSFRHAQSDYLKRMKNREERSQHFFDTPVPLMDDGDDATLYGQGFTDDQLVLVEQNTLVVEEREREIRQIVQSISDLNEIFRDLGAMIVEQGTVLDRIDYNVEQSCVKTEDGLKQLHKAEQYQKKNRKMLVILILVAVIVVLIVVLIAVKSR
Protein: Glucosidase II subunit alpha (Q9U3F8)
Organism: Caenorhabditis elegans
Subcellular location: Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MTAGSSWIVPIILLATPLAVQMVKRDDFKTCEQSAFCKQHRAITEPTGYELLADSITHHGAVWTANVRNSQNTLKINVIGLADSTVRVQIDEPESAIRKRYVPNPALVSLPEELEFSSVENGDQEAKIIGGNKKLKVVVTYKPFLVSIFNEFDELVAQLNRDGKLKVEEFRTKEEGKEYPEGFWEERFKGFTDHKQHGSSSVGVDISFVNFKTAYGLPEHADAFALRNTVGNSDPYRLYNLDVFEYELNNPMALYVSIPYILAHRANRSVGALWFNAAETWVDTQSSVTSKGLFGKMLDKVTGSSDNVPHFDAHFISESGLVDVFFFVGPTVKDVQRQNSKLTGVTPLPPLFSIGYHQCRWNYNDEQDVATVNQGFDDHDMPMDVIWLDIEHTDGKKYFTWDKHKFPTPNDMVDKVAAKGRKMVTIVDPHIKKDDGYYVYKDAKDKGLFVKRVDGSDFEGHCWPGSSEYLDFWHPDTRSYWKDQFAFDRYTGSSSNLHIWNDMNEPSVFSGPEITMDKESIHYGGIEHREIHNMYGMMYTSATFDGMIARTGGKERPFLLSRAGFIGTQRTAAIWTGDNTADWGHLEIAAPMTLSLSIAGVPFVGADVGGFFGNPDEQLLSRWYQTAAFQPFFRAHAHIDTRRREPWLFSEQTQQIIREALRTRYALLPYWYTLFQQHTENGVPPMRPLFYEFENDDLLLEEQKQWMVGSGILARPVVEKDTFNVQVKLPRGEHKTERWFEWVSGNEVRGESIYVDAPITFTPIYQRGGTIIPTWQRIRRSATLMKDDPITLFVALDSNENSNGEIYLDDGNTHDYQSGQFVKASFKYTTLSKNSAMLEGEHLDGKYAAKNWIERVVVRGVESSPKKVEITRVSDPVQSLEFSYDHDSKVLVIRKPEALLTSSFKVHIEF
Protein: Penicillin-insensitive murein endopeptidase (EC 3.4.24.-) (D-alanyl-D-alanine-endopeptidase) (DD-endopeptidase) (P0C0T5)
Organism: Escherichia coli (strain K12)
Function: Murein endopeptidase that cleaves the D-alanyl-meso-2,6-diamino-pimelyl amide bond that connects peptidoglycan strands. Likely plays a role in the removal of murein from the sacculus and could also play a role in the integration of nascent murein strands into the sacculus.
Subcellular location: Periplasm {ECO:0000305|PubMed:15292190}.
Interaction partners:
- Probable membrane transporter protein YfcA
- Chorismate synthase
- Ribosomal protein uL3 glutamine methyltransferase
- Multidrug resistance protein MdtK
- DNA gyrase subunit A
- Elongation factor P lysine hydroxylase
- Peptidoglycan L,D-endopeptidase MepK
- Uncharacterized protein YfcL
- L-glyceraldehyde 3-phosphate reductase
Sequence:
MNKTAIALLALLASSASLAATPWQKITQPVPGSAQSIGSFSNGCIVGADTLPIQSEHYQVMRTDQRRYFGHPDLVMFIQRLSSQVSNLGMGTVLIGDMGMPAGGRFNGGHASHQTGLDVDIFLQLPKTRWTSAQLLRPQALDLVSRDGKHVVSTLWKPEIFSLIKLAAQDKDVTRIFVNPAIKQQLCLDAGTDRDWLRKVRPWFQHRAHMHVRLRCPADSLECEDQPLPPSGDGCGAELQSWFEPPKPGTTKPEKKTPPPLPPSCQALLDEHVI
Protein: Rho-type guanine nucleotide exchange factor, isoform H (M9PBE8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, lamellipodium {ECO:0000256|ARBA:ARBA00004510}.
Interaction partners:
Sequence:
MDQPLVVQAEYSFMGSNNDELCFQKGDVITVTQREDGGWWEGTLNDKTGWFPSNYVNECKVQLPLTETIRPPEEIQEYRSVVLKDLLDSERAHVAELQGLLENFLEPMQQTQILSQDEYAQLMCNFVEIVRTHEDLLIQIEECNDRVGKLFLTSAPLMKKVHQAYCAAHPKAIVILDKYKDELEKYMERQGAATPGLLVLTTGLSKPFRRLDKYSAMLQELERHMESSHPDRGDTQRSVAVYKDIAATCSATRRQKELELQVLTGPVRGWQGQELSTLGDIIHMGSVAVGADHRDRYFVLFPQTLLFLSVSQRMSAFIYEGKLPLTGIIVNRLEDTDALKNAFEISSPLIDRIVAVCQGPNEANKWVELLNANNPSLPMGIKRQLSNLSNSSLGHLNAAHLSQHLDSRGYCTRFSLCAYYSSPPCHVRPLRVTLPPSNYPATAPYANLSAHFARLVKGGGLRSAIVKMLLYPQARQSIDLKRIALRKRRCHKASAKLKDLNTNQDSGQSELERQDAIELPTDSESYDDDFEDDFLHSCDSDPFEYVQFYQNKRNDSMCNSTGTFVDHGTGARRHCSSINLIKLDSADTDEVLALNELKKESLVIGSRALRALARKSTTRNSSVHTSTATLELGVGGSITNCVEEEPILKVKPSFSLQQQSSDASSIFAARLGGAFTACENLASMPDDLSRESSIQEPPTPLPASPTERHSMPTIFVGNRFNHSKNTEVYVPTWRDRQEMQNQSVDAKQDEELHSSSIDLPAACLSAPDKLQAELLYNYDEILEKPLQLHRELTPFPGHNLNSDKRVSHKSDSPSTGNAKTDPNLATRSSSTTELCIDTTSKKRTTPSERSRDSIRRCISYQFLQMSNRPPPPPPPRRDPDLHLDTKCRCCENSQCPSPRSSDSGMAGSCTITSPDPPNPESYFPMEAAGHDMLDNVEPERFDVCGMFREKFLTPEATQDVVDLSEEQPQLSDEPTTPTNRKEEPTCITSAQVQVNTRSIFLPSSSSMDETNRNVPANNILFSSSSADQLEPQATFRSGMYAHWWKKERLPPEVVRGIAHAYNKSLPSKDSKDSGSVCSSCFCSLGASGYSEGALYCSVCQNCADYYNGSVTSTTNTTTTTSSASCPLCSEDEGMIAPTHDSSSLDCPICNGRIASGAEEGKQSEMDRRPGNLRIPVEWYPVYLAGGVCSVHVLRLIVL
Protein: Linoleate 10R-lipoxygenase (EC 1.13.11.62) (Cyclooxygenase-like fatty acid oxygenase) (Fatty acid oxygenase ppoC) (Linoleate 10R-dioxygenase) (10R-DOX) (Psi-producing oxygenase C) (AfPpoC) (Q4WY82)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Responsible for the synthesis of various fatty acid-derived oxylipins. Oxidizes linoleic acid primarily to 10R-hydroperoxy-8,12-octadecadienoic acid (10R-HPODE) and, to a lesser extent, 8R-hydroperoxylinoleic acid (8R-HPODE). Also synthesizes 10-hydroxy-octadeca-8,12-dienoic acid (10-HODE) from linoleic acid and primarily 8R-hydroxy-octadeca-9-monoenoic acid (8-HOME, also known as psiB beta) from oleic acid. 8-HOME forms part of psi factor, a mixture of oxylipins that regulates the balance between sexual and asexual spore production. Displays epoxyalcohol synthase activity. Plays a role in the synthesis of prostaglandins which may be required for pathogenicity.
Interaction partners:
- Psi-producing oxygenase A
- Fatty acid oxygenase, putative
- Lysophospholipase
- Patatin-like phospholipase domain-containing protein
Sequence:
MLRRFSSTFKKKGDRESKQNGTASSSSAAVANTNNNDNKRHSKISAARKSSSDDDRNEKKGNSVSPFEKYASVLHASRSPIPNQTGDGAYLEHEHTTSLLQDARHLGFKDFKTLKEVIESKLPGGQLIDDKTMLMERIIQLVSRLPHNSKHREELTNAFLTELWDSLPHPPLSYMGNDYAYRSADGSNNNPTLPRLGAANTLYARTIPPLIIQPGGLPDPGLVFDTLFARQTFKPHPNKVSSVFFYWASLIIHDIFQTDYKNPNMNKTSGYLDLSILYGDVQEEQNLIRTFKDGKLKPDSFSEPRLQAFPATCCVLMVMLNRFHNYAVEQLAAINENGRFTKPADNLSEEEAKKAWAKYDEDLFQTGRLITCGLYINITLYDYLRTIVNLNRTNSTWCLDPRAQMEGSHTAPSGLGNQCSVEFNLAYRWHSATSATDEKWTEDVYERLMGKPASEVSMTELLMGLGKYQAELPKDPSKRTFADLERQADGRFKDEDLVNLLVNAVEDVAGSFGARNVPKVLKNVEILGIIQSRKWNVGSLNEFRKFFGLKPYETFEEINSDPDVAESLRSLYDHPDFVELYPGIVAEEAKQPMVPGVGIAPTYTISRAVLSDAVALVRGDRFYTIDYNPRNLTNWGYSEVRYDLSINQGCIFYKLATRAFPNWFKPDSIYAHYPMTIPSENRKIMKDLGREIHYSWDRPQYTPPRVDLVSYSNAKLVAEQQNQFRAAWGDTVEFVFGKASKEFKLYQDSAFIQKHADVMSKLLNKEEWHRSVKEFYEDITAKLLEDKTRRFGGINQVDITNDVGNLTPVIFAANVFSLPLKSKENPRGIYTEHEMFKVLAALYNCLYFDIDKTKSYPLHHASQAVGEPLGKALEANVKALGGSSLLSGIFRSFRENKNALKEYGVHLTKQLLENGLGAHEIAWAQFLPTVIAMVPAQAQAFTQIVDFYLSKEGSKHLPAIQRLAKQDTKKSDEQLLHYCLEAVRLNDMSGLYRQSETTLAVTDEAVEVTIQPGDKVFVSFAKANRDASVFPDPAEVRLDRPMNSYINPTLGPHGFLSKETSHIALTAMLRAVGRLNNLRVAPGVQGQLKKIPQPGGYSAYLREDHGSYSIFPTTFRVQYDA
Protein: Alpha/beta hydrolase domain-containing protein 17A (Abhydrolase domain-containing protein 17A) (EC 3.1.2.22) (Q5XIJ5)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards NRAS (By similarity). Has depalmitoylating activity towards DLG4/PSD95. May have depalmitoylating activity towards MAP6.
Subcellular location: Cell membrane {ECO:0000269|PubMed:27307232}; Lipid-anchor {ECO:0000250|UniProtKB:Q96GS6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GS6}. Recycling endosome membrane {ECO:0000269|PubMed:27307232}; Lipid-anchor {ECO:0000250|UniProtKB:Q96GS6}; Cytoplasmic side {ECO:0000250|UniProtKB:Q96GS6}. Cell projection, dendritic spine {ECO:0000269|PubMed:27307232}. Postsynaptic density membrane {ECO:0000269|PubMed:27307232}.
Interaction partners:
- Acyl-protein thioesterase 1
- GTPase NRas
- Palmitoyl-protein thioesterase ABHD10, mitochondrial
Sequence:
MNGLSVSELCCLFCCPPCPGRIAAKLAFLPPEPTYSLVPEPEPGPGGAGAAPSGPLRTSAATPGRWKIHLTERADFQYGQRELDTIEVFVTKSARANRIACMYVRCVPGARYTVLFSHGNAVDLGQMCSFYVGLGTRIGCNIFSYDYSGYGISSGRPSEKNLYADIDAAWQALRTRYGISPDSIILYGQSIGTVPTVDLASRYECAAVVLHSPLTSGMRVAFPDTKKTYCFDAFPNIEKVSKITSPVLIIHGTEDEVIDFSHGLALYERCPKAVEPLWVEGAGHNDIELYSQYLERLRRFISQELPSQRT
Protein: MLP-like protein 328 (Q9ZVF3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transport/golgi organization-like protein
- F13F21.11 protein
- Protein rolling protein
- At2g17710/T17A5.17
- AT5g51950/MSG15_3
- Glycerophosphodiester phosphodiesterase GDPDL5
- GDSL esterase/lipase At1g29660
- AT3G11930 protein
- E3 ubiquitin-protein ligase ORTHRUS 3
- Protein trichome birefringence-like 38
Sequence:
MATSGTYVTEVPLKGSAEKHYKRWRSENHLFPDAIGHHIQGVTIHDGEWDSHGAIKIWNYTCDGKPEVFKERREIDDENMAVTFRGLEGHVMEQLKVYDVIFQFIQKSPDDIICKITMIWEKQNDDMPEPSNYMKFVKSLAADMDDHVLKA
Protein: Cytochrome c1 1, heme protein, mitochondrial (Complex III subunit 4-1) (Complex III subunit IV-1) (Cytochrome b-c1 complex subunit 4-1) (Ubiquinol-cytochrome c reductase complex cytochrome c1 subunit 1) (Cytochrome c-1 1) (Q9LK29)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. Cytochrome c1 is a catalytic core subunit containing a c-type heme. It transfers electrons from the [2Fe-2S] iron-sulfur cluster of the Rieske protein to cytochrome c.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:18189341}; Single-pass membrane protein {ECO:0000269|PubMed:18189341}.
Interaction partners:
- Cytochrome b-c1 complex subunit 7-2, mitochondrial
- Cytochrome b-c1 complex subunit 9, mitochondrial
- Cytochrome b-c1 complex subunit Rieske-1, mitochondrial
- Cytochrome b-c1 complex subunit 7-1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- Cytochrome b
- Cytochrome b-c1 complex subunit Rieske-2, mitochondrial
- Cytochrome b-c1 complex subunit 6-1, mitochondrial
- Cytochrome b-c1 complex subunit 6-2, mitochondrial
Sequence:
MVGGGVIQQILRRKLHSQSLATPVLSWFSSKKAHEDAGSSGVRALALLGAGVTGLLSFSTVASADEAEHGLESPEYPWPHDGILSSYDHASIRRGHQVYQQVCASCHSMSLISYRDLVGVAYTEEEAKAMAAEIEVVDGPNDEGEMFTRPGKLSDRFPQPYANESAARFANGGAYPPDLSLITKARHNGPNYVFALLTGYRDPPAGISIREGLHYNPYFPGGAIAMPKMLNDEAVEYEDGVPATEAQMGKDIVSFLAWAAEPEMEERKLMGFKWIFLLSLALLQAAYYRRLKWSVLKSRKLVLDVVN
Protein: L-tartrate/succinate antiporter (Tartrate carrier) (Tartrate transporter) (P39414)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the uptake of tartrate in exchange for intracellular succinate. Essential for anaerobic L-tartrate fermentation.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- L
- L
- HTH-type transcriptional activator TtdR
Sequence:
MKPSTEWWRYLAPLAVIAIIALLPVPAGLENHTWLYFAVFTGVIVGLILEPVPGAVVAMVGISIIAILSPWLLFSPEQLAQPGFKFTAKSLSWAVSGFSNSVIWLIFAAFMFGTGYEKTGLGRRIALILVKKMGHRTLFLGYAVMFSELILAPVTPSNSARGAGIIYPIIRNLPPLYQSQPNDSSSRSIGSYIMWMGIVADCVTSAIFLTAMAPNLLLIGLMKSASHATLSWGDWFLGMLPLSILLVLLVPWLAYVLYPPVLKSGDQVPRWAETELQAMGPLCSREKRMLGLMVGALVLWIFGGDYIDAAMVGYSVVALMLLLRIISWDDIVSNKAAWNVFFWLASLITLATGLNNTGFISWFGKLLAGSLSGYSPTMVMVALIVVFYLLRYFFASATAYTSALAPMMIAAALAMPEIPLPVFCLMVGAAIGLGSILTPYATGPSPIYYGSGYLPTADYWRLGAIFGLIFLVLLVITGLLWMPVVLL
Protein: Polypeptide N-acetylgalactosaminyltransferase 35A (EC 2.4.1.41) (Protein l(2)35Aa) (Protein-UDP acetylgalactosaminyltransferase 35A) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 35A) (pp-GaNTase 35A) (dGalNAc-T1) (Q8MVS5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Polypeptide N-acetylgalactosaminyltransferases catalyze the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Displays the same enzyme activity toward MUC1, MUC4, and EA2. Not involved in glycosylation of erythropoietin (EPO). It can both act as a peptide transferase that transfers GalNAc onto unmodified peptide substrates, and as a glycopeptide transferase that requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Protein modification by this enzyme might be important for cytokinesis and tube formation during embryogenesis. Together with Pgant3, regulates integrin levels and activity-dependent integrin signaling at the synapse in neurons and muscles.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- GDP-fucose protein O-fucosyltransferase 2
- Transmembrane protein 11 homolog, mitochondrial
- Mannose-P-dolichol utilization defect 1 protein homolog
Sequence:
MMQIKRLLCKSCGLGTLLVAVVWLLALLFYSHSLRSSIRSAGWRIDEGNATPRAELSYQARVTVGCTPNASITTGESPAAPKPPSDPEQLELLGVVRNKQDKYIRDIGYKHHAFNALVSNNIGLFRAIPDTRHKVCDRQETTEAENLPQASIVMCFYNEHKMTLMRSIKTVLERTPSYLLREIILVDDHSDLPELEFHLHGDLRARLKYDNLRYIKNEQREGLIRSRVIGAREAVGDVLVFLDSHIEVNQQWLEPLLRLIKSENATLAVPVIDLINADTFEYTPSPLVRGGFNWGLHFRWENLPEGTLKVPEDFRGPFRSPTMAGGLFAVNRKYFQHLGEYDMAMDIWGGENIEISFRAWQCGGAIKIVPCSRVGHIFRKRRPYTSPDGANTMLKNSLRLAHVWMDQYKDYYLKHEKVPKTYDYGDISDRLKLRERLQCRDFAWYLKNVYPELHVPGEESKKSAAAPIFQPWHSRKRNYVDTFQLRLTGTELCAAVVAPKVKGFWKKGSSLQLQTCRRTPNQLWYETEKAEIVLDKLLCLEASGDAQVTVNKCHEMLGDQQWRHTRNANSPVYNMAKGTCLRAAAPTTGALISLDLCSKSNGAGGSWDIVQLKKPTEAEGRAKEARNSDKAL
Protein: Nuclear RNA export factor 3 (TAP-like protein 3) (TAPL-3) (Q9H4D5)
Organism: Homo sapiens (Human)
Function: May function as a tissue-specific nuclear mRNA export factor.
Subcellular location: Nucleus. Cytoplasm. Note=Shuttles between the nucleus and the cytoplasm.
Interaction partners:
- NTF2-related export protein 1
- NTF2-related export protein 2
- THO complex subunit 4
- mRNA export factor RAE1
- Exportin-1
- THO complex subunit 5
- Eukaryotic initiation factor 4A-III
- Nucleoporin NUP42
- Nuclear transport factor 2
- Regulator of nonsense transcripts 3A
Sequence:
MSLPSGHTTGHTDQVVQRRARCWDIYQRRFSSRSEPVNPGMHSSSHQQQDGDAAMHGAHMDSPVRYTPYTISPYNRKGSFRKQDQTHVNMEREQKPPERRMEGNMPDGTLGSWFKITVPFGIKYNEKWLLNLIQNECSVPFVPVEFHYENMHASFFVENASIAYALKNVSGKIWDEDNEKISIFVNPAGIPHFVHRELKSEKVEQIKLAMNQQCDVSQEALDIQRLPFYPDMVNRDTKMASNPRKCMAASLDVHEENIPTVMSAGEMDKWKGIEPGEKCADRSPVCTTFSDTSSNINSILELFPKLLCLDGQQSPRATLCGTEAHKRLPTCKGSFFGSEMLKNLVLQFLQQYYLIYDSGDRQGLLSAYHDEACFSLSIPFNPEDSAPSSFCKFFKDSRNIKILKDPYLRGELLKHTKLDIVDSLSALPKTQHDLSSFLVDMWYQTEWMLCFSVNGVFKEVEGQSQGSVLAFTRTFIATPGSSSSLCIVNDKLFVRDTSHQGTQSALFTLVPTAFSSSVPAFSQEQQKMLPS
Protein: Aspartate aminotransferase (EC 2.6.1.1) (Q8T0M9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGPPDAILGVTEAFKKDTNPKKINLGAGAYRDDNTQPFVLPSVREAEKRVVSRSLDKEYATIIGIPEFYNKAIELALGKGSKRLAAKHNVTAQSISGTGALRIGAAFLAKFWQGNREIYIPSPSWGNHVAIFEHAGLPVNRYRYYDKDTCALDFGGLIEDLKKIPEKSIVLLHACAHNPTGVDPTLEQWREISALVKKRNLYPFIDMAYQGFATGDIDRDAQAVRTFEADGHDFCLAQSFAKNMGLYGERAGAFTVLCSDEEEAARVMSQVKILIRGLYSNPPVHGARIAAEILNNEDLRAQWLKDVKLMADRIIDVRTKLKDNLIKLGSSQNWDHIVNQIGMFCFTGLKPEQVQKLIKDHSVYLTNDGRVSMAGVTSKNVEYLAESIHKVTK
Protein: Syndecan-3 (SYND3) (O75056)
Organism: Homo sapiens (Human)
Function: Cell surface proteoglycan that may bear heparan sulfate (By similarity). May have a role in the organization of cell shape by affecting the actin cytoskeleton, possibly by transferring signals from the cell surface in a sugar-dependent mechanism.
Subcellular location: Cell membrane; Single-pass type I membrane protein.
Interaction partners:
- Pleiotrophin
- Src substrate cortactin
- Glial cell line-derived neurotrophic factor
- Proto-oncogene tyrosine-protein kinase Src
- Fibroblast growth factor 2
- Syndecan-1
- Syndecan-2
- Inter-alpha-trypsin inhibitor heavy chain H4
- Neurturin
- Artemin
Sequence:
MKPGPPHRAGAAHGAGAGAGAAAGPGARGLLLPPLLLLLLAGRAAGAQRWRSENFERPVDLEGSGDDDSFPDDELDDLYSGSGSGYFEQESGIETAMRFSPDVALAVSTTPAVLPTTNIQPVGTPFEELPSERPTLEPATSPLVVTEVPEEPSQRATTVSTTMATTAATSTGDPTVATVPATVATATPSTPAAPPFTATTAVIRTTGVRRLLPLPLTTVATARATTPEAPSPPTTAAVLDTEAPTPRLVSTATSRPRALPRPATTQEPDIPERSTLPLGTTAPGPTEVAQTPTPETFLTTIRDEPEVPVSGGPSGDFELPEEETTQPDTANEVVAVGGAAAKASSPPGTLPKGARPGPGLLDNAIDSGSSAAQLPQKSILERKEVLVAVIVGGVVGALFAAFLVTLLIYRMKKKDEGSYTLEEPKQASVTYQKPDKQEEFYA
Protein: Kidins220 protein (Q52KP9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
TPVLVARDVKTFLPCTVNLDPKLREIIADVRAAREQINIGGLAYPPLPLHEAPPRPPSGYSQPASVCSSSASFNGPFPGGVVSPQPHSSYYSGLSGPQHPFYNRASVPATGTSLLLSSMTVDIVCEKLRQIEGLDQGMLPQYCTTIKKANINGRVLAQCNIDELKKEMAMNFGDWHLFRSMVLEMRSVENQVVPEDPRFLNENSSAPVAHGESARRTSHSELPHTELSSQTPYTLNFSFEELNTLGLDEGAPRHSNLSWQSQTRRTPSLSSLNSQDSSIEISKLTDKVQAEYRDAYREYIAQMSQLEGGTGSSTISGRSSPHSTYYIGQSSSGGSIHSNLEQERGKENELKQEEGRKSFLMKRGDVLDYSSSGVSTNEASPLDPITEEDEKSDQSGSKLLPGKKSSERPSLFQTDLKLKGSGLRYQKLPSDEDESGTEESDNTPLLKDDKDKKAEGKAERVAKSPEHSVEPIRTFIKAKEYLSDALLDKKDSSDSGVRSNESSPNHSLHNEAADDSQLEKANLIELEDEGHSGKRGMPHSLSGLQDPVIARMSICSEDKKSPSECSLIASSPEESWPSCQKAYNLNRTPSTVTLNNNTAPTNRANQNFDEIEGVRETSQVILRPGPSPNPTAVQNENLKSMAHKRSQRSSYTRLSKDASELHAASSDSTGFGEERESIL
Protein: G-protein coupled receptor 183-A (A5PLE7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: G-protein coupled receptor expressed in lymphocytes that acts as a chemotactic receptor for B-cells, T-cells, splenic dendritic cells, monocytes/macrophages and astrocytes (By similarity). Receptor for oxysterol 7-alpha,25-dihydroxycholesterol (7-alpha,25-OHC) and other related oxysterols (By similarity). Mediates cell positioning and movement of a number of cells by binding the 7-alpha,25-OHC ligand that forms a chemotactic gradient (By similarity). Binding of 7-alpha,25-OHC mediates the correct localization of B-cells during humoral immune responses (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P32249}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Beta-arrestin-1
Sequence:
METTSANFTQNDSNVCTNLYNHRGWAQYFLPAMYSLICIVGLLGNVLALHVIWPNLKKINSTTLYSANLVVSDILFSLALPLRVVYYARGFDWPMGEGLCKAVALLFYINMYAGVNFMTCLSVDRFIAVVLPLRFSRFRKVQKVRYICGVVWVVVLMQTLPLLSMPMTNIEQSGHITCMEYPNFEKIDNLPVMLIGAVVLGFGIPVITILVCYTALCLKLRHLAKSNKLTEKSGRSSKAIGVICTVILVFVVCYSPYHVDLLQYMIKKLRYDPDCSELHKFQISLHITVCFMNLNSCLDPFIYFFACKGYKKKVLKLLKKQVSMSFSSVVRTSPEGSSKDVFGNDKIQMNSRSFQKERSSVLLNSLEQ
Protein: Protein transport protein BOS1, putative (Q8IIP9)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00046280}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00046280}.
Interaction partners:
- Syntaxin, Qa-SNARE family
- Sec1 family protein, putative
- Protein transport protein SEC22
- BET1-like protein, putative
- SNARE protein, putative
- SNARE protein
- Alpha-soluble NSF attachment protein, putative
- Syntaxin-6, putative
- SNARE protein, putative
- Syntaxin, Qa-SNARE family
Sequence:
MNKKYEPILDNELLSSNNENENFVNSKKKDNENDKIQDTSLNNIYGKIVKIRKELEKSYNLFYSYNLIVSNNKEHDPNSPYNNVYARSDIININNNTKNNLTLNKINALTNSFYMNVQTLKNTYSFINTNNVNNKIINNDNIIWERRIETLSNEANSYIKTLDNIYKTNLKQSEMKNNKKSNYTKSNKRHDGDDAINYLHKENEILKQVEDHLNIFHVQGMNTLNMLRKQNKFLKNVRKKVIDMYNYVGLSSSLVDTIKKAHKQNLIIVIVGIILSLIFFYVIYSYFKR
Protein: Enhancer of mRNA-decapping protein 1 (P53080)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: mRNA-binding protein which stimulates mRNA decapping by DCP1 and DCP2. Involved in the regulation of expression of multiple genes involved in glycolysis and gluconeogenesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- mRNA-decapping enzyme subunit 1
- m7GpppN-mRNA hydrolase
- Enhancer of mRNA-decapping protein 2
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein complex subunit 1
- ATP-dependent RNA helicase DHH1
- LSM1-LSM7 complex subunit LSM1
- Enhancer of mRNA-decapping protein 3
Sequence:
MSTDTMYFNSSRLLPSAGRNKTNNLIKQKTRNNRARGNAAKNANNNNYITDIPPPQTLPNGQKPNFGHSSNKKPSFNQKKHSPPSSPSSTTTLGKKNRQNNKETPRQNNKDDTRLLSQNLKNLLLNQKQSPHGSQGIIPMGCNGSAKKLSHSYAGSTFATNGPREAKNLPKPSFL
Protein: Receptor-like protein 55 (AtRLP55) (Protein SUPPRESSOR OF NPR1-1, CONSTITUTIVE 3) (Q9FK66)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plant defense.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9SN38}; Single-pass type I membrane protein {ECO:0000255}.
Interaction partners:
- Receptor-like kinase
- Protein SUPPRESSOR OF NIM1 1
Sequence:
MKPQQPQPPLLLLLLLPLLLTTVSSYPLNPKQLKALQSLNISTPTNDPCNNNNNQSSSSSITCDDASPYRHITSISFTNCSSTLSLPSKTLKPLSKSLISLSFTNCPSLSPPYHLPISLHSFSAVSSFLQNNRTKLSGLFLARLKNLKTLYISSTPIQTSRRLYVILGNMHKLTSLTISNSNLTGLIPKSFHSNLRYIDLSNNSLKGSIRISITRLKNLKSLNLSHNSLSGQIPNKIKSLTFLKNLSLASNKLSGTIPNSLSSISELTHLDLSMNQLNGTVPSFFSEMKNLKHLNLADNSFHGVLPFNESFIKNLNFFEIGRNSELCYNKTVLSSNLKLEGLAPCDKYGFPLWSPSQKEESLSGENDYDVEGGNEEKTENLKTKEEEEEEHKGSNKTLFGLGIGLFSLVFLILFLFYLAKRCRLI