wanglab/gogpt-training-data huggingface dataset:
Protein: NKG2-C type II integral membrane protein (CD159 antigen-like family member C) (NK cell receptor C) (NKG2-C-activating NK receptor) (CD antigen CD159c) (P26717)
Organism: Homo sapiens (Human)
Function: Immune activating receptor involved in self-nonself discrimination. In complex with KLRD1 on cytotoxic lymphocyte subsets, recognizes non-classical major histocompatibility (MHC) class Ib HLA-E loaded with signal sequence-derived peptides from non-classical MHC class Ib HLA-G molecules, likely playing a role in the generation and effector functions of adaptive natural killer (NK) cells and in maternal-fetal tolerance during pregnancy. Regulates the effector functions of terminally differentiated cytotoxic lymphocyte subsets, and in particular may play a role in adaptive NK cell response to viral infection. Upon HLA-E-peptide binding, transmits intracellular signals via the adapter protein TYROBP/DAP12, triggering the phosphorylation of proximal signaling molecules and cell activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20952657, ECO:0000269|PubMed:21825173}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- TYRO protein tyrosine kinase-binding protein
- HLA class I histocompatibility antigen, alpha chain E
- Natural killer cells antigen CD94
- Killer cell immunoglobulin-like receptor 2DL1
- Killer cell immunoglobulin-like receptor 2DL3
- Killer cell immunoglobulin-like receptor 3DL1
- NKG2-F type II integral membrane protein
- NKG2-E type II integral membrane protein
- NKG2-A/NKG2-B type II integral membrane protein
- Killer cell immunoglobulin-like receptor 3DL2
Sequence:
MNKQRGTFSEVSLAQDPKRQQRKPKGNKSSISGTEQEIFQVELNLQNPSLNHQGIDKIYDCQGLLPPPEKLTAEVLGIICIVLMATVLKTIVLIPFLEQNNFSPNTRTQKARHCGHCPEEWITYSNSCYYIGKERRTWEESLLACTSKNSSLLSIDNEEEMKFLASILPSSWIGVFRNSSHHPWVTINGLAFKHKIKDSDNAELNCAVLQVNRLKSAQCGSSMIYHCKHKL
Protein: FXYD domain-containing ion transport regulator 7 (P58549)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P59648}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P59648}. Note=Able to translocate to the plasma membrane independent of its association with NKA (in vitro). {ECO:0000250|UniProtKB:P59649}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta-1
- FXYD domain-containing ion transport regulator 4
- FXYD domain-containing ion transport regulator 3
Sequence:
MATPTQTPTKAPEEPDPFYYDYNTVQTVGMTLATILFLLGILIVISKKVKCRKADSRSESPTCKSCKSELPSSAPGGGGV
Protein: dihydropyrimidinase (EC 3.5.2.2) (Q8IPQ2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dihydropyrimidine dehydrogenase [NADP
- Beta-ureidopropionase
- Multifunctional protein r
- Uncharacterized protein, isoform B
- LD30822p
- Uridine 5'-monophosphate synthase
- Dihydroorotate dehydrogenase
- FI17329p1
- Cyclin-dependent kinase 5 homolog
- FI21247p1
Sequence:
MSTSPKPVKKVPIHLQSAQNRVYIKNGEIVNHDKSFKADVYIEDGIIKFVGPSSEITIPGGVRTIDASGLMIIPGGIDPHTHMQLPFGGAVAVDDFYHGTKAAVAGGTTMIIDFVLPNKHESMIEAYDKWRSWADPKVCCDYGLHVGITWWSKSVSEEIGILCKELGVNSFKTFMAYKGLYQLNDSDLLDVFERIRHLNGVAMVHAENGDIIAKNTQRLLAEGINGPEGHELSRPEEVEAEAVHRACVLAHQADCPLYVVHVMSKSAGIELARARHRYRGRYIMGETLAAALGTDATCCQHLGFDAEAAHVLSPPLRPDKTTPEFLMKLLANDDLQLTGSDNCTFNKEHKALGKGDFTKIPNGVNGVEDRMSLVWEKGVHAGLLDPCRFVAVTSTNAAKIFNIYPQKGRIAVGSDADIVIWNPNATRTISKDTHHHACDFNIFEGMTVHGVCEFVLVRGRICAERGNVRVAEGFGRFIPTPVRPPFVYDIIEGKVQSQPEEQHEEKQNGSMAKRFAELDIQIPVQEPISAMLAGNLAMPAEGSLCSTPSVRGRVDGKRDLQESSFSISEELDRSGVRACIKVKNPPGGKSSGFW
Protein: Ubiquitin-fold modifier 1 (P61961)
Organism: Mus musculus (Mouse)
Function: Ubiquitin-like modifier which can be covalently attached via an isopeptide bond to lysine residues of substrate proteins as a monomer or a lysine-linked polymer. The so-called ufmylation, requires the UFM1-activating E1 enzyme UBA5, the UFM1-conjugating E2 enzyme UFC1, and the UFM1-ligase E3 enzyme UFL1. Ufmylation is involved in reticulophagy (also called ER-phagy) induced in response to endoplasmic reticulum stress. Ufmylation of TRIP4 regulates nuclear receptors-mediated transcription (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:21494687}. Cytoplasm {ECO:0000269|PubMed:21494687}.
Interaction partners:
- Ubiquitin-like modifier-activating enzyme 5
- Ufm1-specific protease 2
- Ubiquitin-fold modifier-conjugating enzyme 1
- Ufm1-specific protease 1
- E3 UFM1-protein ligase 1
- DDRGK domain-containing protein 1
- Ubiquitin-like protein NEDD8
- Adenylyltransferase and sulfurtransferase MOCS3
- Ubiquitin-related modifier 1
- CDK5 regulatory subunit-associated protein 3
Sequence:
MSKVSFKITLTSDPRLPYKVLSVPESTPFTAVLKFAAEEFKVPAATSAIITNDGIGINPAQTAGNVFLKHGSELRIIPRDRVGSC
Protein: Probable Dol-P-Man:Man(7)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase (EC 2.4.1.260) (Asparagine-linked glycosylation protein 12 homolog) (Dolichyl-P-Man:Man(7)GlcNAc(2)-PP-dolichyl-alpha-1,6-mannosyltransferase) (Mannosyltransferase ALG12 homolog) (Q9USD4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Adds the eighth mannose residue in an alpha-1,6 linkage onto the dolichol-PP-oligosaccharide precursor (dolichol-PP-Man(7)GlcNAc(2)) required for protein glycosylation.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:10759889}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Alpha-1,2-mannosyltransferase alg9
- Dol-P-Man:Man
- Dolichyl-phosphate beta-glucosyltransferase
- Dol-P-Glc:Glc
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl pyrophosphate Glc1Man9GlcNAc2 alpha-1,3-glucosyltransferase
- GPI mannosyltransferase 3
- UDP-N-acetylglucosamine transferase subunit alg13
- UDP-N-acetylglucosamine transferase subunit alg14
- GDP-Man:Man
Sequence:
MTSKESICWYLANILLVTCIGYYSYKTPFTKVEESFAMQAIHDIQTYRWDLSKYDHLEFPGAVKRSFIPSLFIAVLSYIPSWFVNPLLAARWTIGYLSWESMNSVSCSISKRFGTLSGALFILFSCAQFHLVYYMSRPLSNIFGLIATNHSLSLLLKNNYYGSISILVFAAAIVRSEIALLLMCLILPLLLQRRITLSKLLLVGISSSLAAVGASFLIDSYFWGAWCWPELEAFLFNVVEGKSSDWGTSPFYYYFVRLPWLFLNPTTLLFLLISFVYIKPARLLIYVPLFFIFVYSFLGHKEWRFIIYSIPWFNAASAIGASLCFNASKFGKKIFEILRLMFFSGIIFGFIGSSFLLYVFQYAYPGGLALTRLYEIENHPQVSVHMDVYPCMTGITRFSQLPSWYYDKTEDPKMLSNSLFISQFDYLITEDPESYNDTFDVIESVNSNTKIPILPKWLSNHIPREISIRNPAQPVYILANKKARATKPAAVDDYSSFIGHKVDEIKLWPPIYRVVSPDTLLTRDYREDRLNFFIDKDRILTHITQG
Protein: LCCL domain-containing protein (Q8I3B1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MYNFFLSIICIFFIPYFCRASFKEYLSNKKIFLKYNGTYCLYPENVIENDIIEIATDECDKVAHEYENKIVWFSFDNGRLRSNNGMCLKTYKNILVLSTCSPNKNEKSEMWKIDEETHLKNENNNCAQIAGNKLFSFTCNNLSTKEFEQSIFSSDELYLMKTRYSQQKLKNIKTEDIDTFHNNFNTLTNSYKEVDTKIVHILNRDKEMKKQKEKILHLINDMKLLVNTSSSLNEYGTGAIMKIYDNMDIEQKKYLLNVPLEKLEINEEKLDELGIEQGQIKIIIQSFLNVPENNTYTFYVKNIVGYINIKLNNEEILSNRNIEINNRTNNSAVVKLRKNKLIPIYIEISSIGNEKPSFSLYWSNNNNMPEQIINSLYLYSTIYEKVCYTPLQKKIDFTLTFENITKTNREYQFLCPLKNFNNDQNVRILKNENRPDYCYDLKSSICASAIDSYFLPNESEGIVKAVRQRIQNEKGIYEECGIILPTNTTEHIFKGITDIKLIDMDDFFINYEKNKELYKGYKGIVTDDKHSLLSKTDLDKSFISDIDINCTNNFNEKKTNYEYSSGSFIIKRIKSSDLLKQNTSIVVDVFALFEKYSDIKNMPSIYLSNWTRKTCNDIQLYIKYGKPNDIMKYPSKLLSCDDTFESLTYQSRDDNNNNNNNNNNNNNNNNNNNNNNNNNNNNDNNNIISDYYDYDDDDTIVARCLPYCFNDKEVLGSYIYMSKSPICKSAIHSGILTINGGLVEIRKLKNITQNFNSTMEITRNGIKATIGTNQNGYSYYITKPSGRFCNFPRTSYNINESINLESDIDYKNDEDKTNNNNNNNNNNNNNNNNNNYHNNNNYHNNYHNNNHPHNDNTIFPSFIQLYSKLTETPPVVLVHEKHAVLPNQLDKIQNVYNQNNYKKDFFFPQKNEALNENKKKNPTSTPSDDEEKKENKKIIQEFTTFEKNYKKDIPHYQTLIKKNENILSNLFMKKNSIKNMESQITDIRKNQKDSYDIFVKTQETVVTSLIKQFNIITKKKENHINRLEKAFSNVKTTTVKIFKEQYKSTNINDNYIIIDSIQNNSMNGSSNWKIEKYTNGNFFSSITENSFIKSEDNIYGSYILYRYTKLYKGFISLDIKLPYEGSFGIIFKYKDDKNYHNFIINRNEFYFLEVINGTVGNKINYTKTENNIYNFGMWIQIHLDFGNKYIRTFINKKFVCGYETRYHTYGFLGFGVNHCKEKIFIDKLVIGSLDQTKYYSDKMGKKNNIQNIFPPTIYLNKNMQVLQNGTKKKKQNKNFIFNKYNKEHTISIGNNNSNGCIPFEENFHTPLDNNWIIPENNNIWHIKRKETNIYLPSILKNFKNIYKNQDNSETNNISNDEENYLYSIKKTNQANNILIPSILLLNKQHLCTHMKSYTFQTNIKLNKISKAGIIFRVHSNHDFLSVILDISQKHGKIYLMKITKGIPFQLLTKTHISIQDNTWYNLKLSYNGSNIKLILNDEIILNSKINQNMPKQLGTLGLILLSGQCKYKNVVFTPSTSSQ
Protein: Large ribosomal subunit protein bL34m (39S ribosomal protein L34, mitochondrial) (L34mt) (MRP-L34) (Q9BQ48)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25278503, ECO:0000269|PubMed:25838379, ECO:0000269|PubMed:28892042}.
Interaction partners:
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein uL29m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein uL13m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS14m
- Large ribosomal subunit protein mL46
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL33m
Sequence:
MAVLAGSLLGPTSRSAALLGGRWLQPRAWLGFPDAWGLPTPQQARGKARGNEYQPSNIKRKNKHGWVRRLSTPAGVQVILRRMLKGRKSLSH
Protein: ER lumen protein-retaining receptor 3 (KDEL endoplasmic reticulum protein retention receptor 3) (KDEL receptor 3) (O43731)
Organism: Homo sapiens (Human)
Function: Receptor for the C-terminal sequence motif K-D-E-L that is present on endoplasmic reticulum resident proteins and that mediates their recycling from the Golgi back to the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18086916}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5ZKX9}. Golgi apparatus membrane {ECO:0000269|PubMed:18086916}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5ZKX9}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000269|PubMed:18086916}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5ZKX9}. Note=Localized in the Golgi in the absence of bound proteins with the sequence motif K-D-E-L. Trafficks back to the endoplasmic reticulum together with cargo proteins containing the sequence motif K-D-E-L. {ECO:0000305|PubMed:18086916}.
Interaction partners:
- ER lumen protein-retaining receptor 2
- ER lumen protein-retaining receptor 1
- X-box-binding protein 1
- ADP-ribosylation factor 4
Sequence:
MNVFRILGDLSHLLAMILLLGKIWRSKCCKGISGKSQILFALVFTTRYLDLFTNFISIYNTVMKVVFLLCAYVTVYMIYGKFRKTFDSENDTFRLEFLLVPVIGLSFLENYSFTLLEILWTFSIYLESVAILPQLFMISKTGEAETITTHYLFFLGLYRALYLANWIRRYQTENFYDQIAVVSGVVQTIFYCDFFYLYVTKVLKGKKLSLPMPI
Protein: Zinc finger and SCAN domain-containing protein 16 (Zinc finger protein 392) (Zinc finger protein 435) (Q9H4T2)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MTTALEPEDQKGLLIIKAEDHYWGQDSSSQKCSPHRRELYRQHFRKLCYQDAPGPREALTQLWELCRQWLRPECHTKEQILDLLVLEQFLSILPKDLQAWVRAHHPETGEEAVTVLEDLERELDEPGKQVPGNSERRDILMDKLAPLGRPYESLTVQLHPKKTQLEQEAGKPQRNGDKTRTKNEELFQKEDMPKDKEFLGEINDRLNKDTPQHPKSKDIIENEGRSEWQQRERRRYKCDECGKSFSHSSDLSKHRRTHTGEKPYKCDECGKAFIQRSHLIGHHRVHTGVKPYKCKECGKDFSGRTGLIQHQRIHTGEKPYECDECGRPFRVSSALIRHQRIHTANKLY
Protein: LSM domain-containing protein (Q57UJ0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDALTTSTIPSALAAAGCLQHSMVRVGLTNGMVLTGRIVEFDAVTMNMKLDAITDMAVLHPAAGEGCGDSAYETNPAALRCCNSVVVRGCHLRYMDFIDEESDNGRGLQELITAVRVVKPSVPQD
Protein: Putative uncharacterized hydrolase C1020.07 (EC 3.-.-.-) (O59760)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Uncharacterized hydrolase C25B8.12c
- Uncharacterized hydrolase C215.10
- Riboflavin kinase
Sequence:
MIPEACLFDMDGLLVDTESIYTKSTNIILKRYNKGPFSMEVKAKMMGRTSKEASRIFLDWSGIDLTCEEYIALQRETQAELWRHTKPLPGVMNLLSKLKSLNIPIALATSSDTHNFEKKSAHLSHLFDHFDGNIITGDDPRLPVGRGKPHPDIWFIALKMINDKRKAQGQAEILPENCLVFEDSITGVQSGRAAGMKVVWVPDVNILPFFSLSPEQAADKHITKVLSLENFDVTKV
Protein: Uncharacterized protein (Q38BI0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSKQERIADAMKERVTQLERELRECQQQLQEALQRGDDIQCAKEALQCEAHDIVDQWSRKTAELQTKLNECLCELSEARRLIALSEDRNTGLQNQLQQLEAHHLSQFQELEKYETQNKELSEKLAATERSLCFASQQVGAMEGRVNEMVAEIEQKSEQITSLSRKEDMLAEALLELQKSRKQAETIYNEGRERVSLLDDELSRAKRLLARTRDALLLTEQEVFCRCKIIADEANTMVGALFNQLLSAIHSNESYGEALKEAQHNSASLAEENGLLLLKLQEAEQDLSKLRVEQGQETATCREQIRLLELDVRELQDARINWSRELEAVQNELGRSETNRHTLEESKMSLNAELKIVKDCYSTLLVEHDELKISVQIMRRESEAEISRLVTEKASAMNSYEMKLQEVCMRNTTLNQILKFKEHEMLCHRESNGRQSILVENYHELVGLTQLYISKCEFIHSRMYNQVLDSREKIASLTQTISEKQLENSKLVSIARDLEEKVTSAQNDAKMFRSKVVELSTALNSNREEADNLVSENKWLSDQVFGMREELRDIDVLFNCTLNDMREQGENQQREREMLSEEVNRYEKLLQKSQQKISRCEERCSVFAAEKAAMLKTLTLAEEELLTAKSECSRAREREQFSLKEKGILEKELSQMRRDYVSSTNQVKALMEELRTHDVKQQLMNSSSRTEVEATKTKLNTYIELYENANVQVAQLTKSLQESRDAYDNLHESHQKAKVALEDAKQRCCHDAQEIQKALEERQRIASERDTLVEKYNKVHDVLKLIKKENSGTMAEEVRKLSDLCSQQEAELQELRHQNVILKRGIVKVADETHNPVERGKFVERLNLAEGPLRRPKKRPATDS
Protein: Uncharacterized protein BTRF1 (P0C734)
Organism: Epstein-Barr virus (strain GD1) (HHV-4) (Human gammaherpesvirus 4)
Interaction partners:
Sequence:
MLKCKQPGARFIHGAVHLPSGQIVFHTIHSPTLASALGLPGENVPIPALFRASGLNVRESLPMTNMRAPIISLARLILAPNPYILEGQLTVGMTQDNGIPVLFARPVIEVKSGPESNIKASSQLMIAEDSCLNQIAPFSASEHPAFSMVESVKRVRVDEGANTRRTIRDILEIPVTVLSSLQLSPTKSILKKAPEPPPPEPQATFDATPYARIFYDIGRQVPKLGNAPAAQVSNVLIANRSHNSLRLVPNPDLLPLQHLYLKHVVLKSLNLENIVQDFEAIFTSPSDTISEAETKAFEKLVEQAKNTVENIVFCLNSICSTSTLPDVVPDVNNPNISLALEKYFLMFPPSGTIMRNVRFATPIVRLLCQGAELGTMAQFLGKYIKVKKETGMYTLVKLYYLLRI
Protein: Ent-sandaracopimaradiene 3-hydroxylase (EC 1.14.14.70) (Cytochrome P450 701A8) (Ent-kaurene oxidase 4) (OsKO4) (Ent-kaurene oxidase-like 4) (OsKOL4) (OsKOS1) (Syn-pimaradiene 3-monooxygenase) (EC 1.14.14.68) (Q0DBF4)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Catalyzes the hydroxylation of ent-sandaracopimaradiene at the C3alpha position to produce ent-3beta-hydroxy-sandaracopimaradiene, an intermediates for the biosynthesis of oryzalexin D and oryzalexin E phytoalexins. Catalyzes the hydroxylation of ent-cassadiene at the C3alpha position to produce 3alpha-hydroxy-ent-cassadiene, which may be an intermediate for the biosynthesis of phytocassane phytoalexins. Catalyzes the hydroxylation of syn-pimaradiene (9-beta-pimara-7,15-diene) at the C3beta position to produce 3-beta-syn-pimaradiene. Can hydroxylate ent-kaurene in vitro, but the product is not ent-kauren-19-ol as expected for ent-kaurene oxidase activity.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- Ent-kaurenoic acid oxidase
- Oryzalexin E synthase
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Ent-kaurene oxidase 2
- Os06g0570566 protein
- Ent-kaurene oxidase-like protein 1
- Nitrate reductase
- Nitrate reductase
- Nitrate reductase 1
- 4-coumarate--CoA ligase
Sequence:
MESMLVAGAGAAAVAAVGGLVAAAALADKLVAAPPPRKNRANPPPAVPGLPIIGNLHQLKEKKPHQTFAKWSETYGPIYTIKTGASPVVVLNSTEVAKEAMIDKFSSISTRKLPKAMSVLTRKSMVAISDYGDYQKMAKRNIMIGMLGFNAQKQFRGTRERMISNVLSTLHKLVSLDPHSPLNFRDVYINELFSLSLIQSLGEDVSSVYVEEFGREISKDEIFDVLVHEMMMCAVEADWRDYFPYLSWLPNKSFDTIVSTTEFRRDAIMNALIKKQKERIARGEARASYIDFLLEAERSAQLTDDQLMLLLSESILAAADTVLVTTEWTMYEIAKNPDKQELLYQEIREACGGEAVTEDDLPRLPYLNAVFHETLRLHSPVPVLPPRFVHDDTTLAGYDIAAGTQMMINVYACHMDEKVWESPGEWSPERFLGEGFEVADRYKTMAFGAGRRTCAGSLQAMNIACVAVARLVQELEWRLREGDGDKEDTMQFTALKLDPLHVHLKPRGRM
Protein: Amidophosphoribosyltransferase (ATase) (EC 2.4.2.14) (Glutamine phosphoribosylpyrophosphate amidotransferase) (GPAT) (P35433)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional purine biosynthesis protein ATIC
- Adenylosuccinate lyase
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Bifunctional phosphoribosylaminoimidazole carboxylase/phosphoribosylaminoimidazole succinocarboxamide synthetase
- Multifunctional protein CAD
- Glutamine synthetase
- Ribose-phosphate pyrophosphokinase 2
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 1
Sequence:
MELEESGIREECGVFGCIASGDWPTQLDVPHVITLGLVGLQHRGQESAGIVTSDGSSVPKFRVHKGMGLVNHVFTEDNLKKLYVSNLGIGHTRYATTGKCELENCQPFVVETLHGKIAVAHNGELVNAARLRKKLLRHGIGLSTSSDSEMITQLLAYTPPQEQDDTPDWVARIKNLMKEAPAAYSLVIMHRDVIYAVRDPYGNRPLCIGRLMPVSDINDKEKKSSETEGWVVSSESCSFLSIGARYCHEVKPGEIVEISRHGVRTLDIIPRSNGDPVAFCIFEYVYFARPDSMFEDQMVYTVRYRCGQQLAVEAPVEADLVSTVPESATPAALGYATKCGLPYVEVLCKNRYVGRTFIQPNMRLRQLGVAKKFGVLSDNFKGKRIVLIDDSIVRGNTISPIIKLLKESGAKEVHIRVASPPIKHPCFMGINIPTKEELIANKPEFEYLAEYLGANSVVYLSVEGLVSSVQQEIKFKKQKVKKRDITIQENGNGLEYFEKTGHCTACLTGQYPVDLEW
Protein: Zinc finger BED domain-containing protein 3 (Axin-interacting protein) (Q9D0L1)
Organism: Mus musculus (Mouse)
Function: Acts as a positive regulator in the activation of the canonical Wnt/beta-catenin signaling pathway by stabilizing cytoplasmic beta-catenin. Involved in transcription activation of Wnt target gene expression. Plays a role in symmetric division of blastomeres in the early stages of embryogenesis via regulation of mitotic spindle central positioning and organization of the F-actin filament network. Plays a role in regulating the distribution of cellular organelles, via modulation of cytoskeletal dynamics and cytoplasmic lattice formation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19141611, ECO:0000269|PubMed:28992324}. Membrane {ECO:0000269|PubMed:19141611}. Secreted {ECO:0000250|UniProtKB:Q96IU2}. Note=Colocalizes with AXIN1 in the cytoplasm (PubMed:19141611). Colocalizes with NLRP5 in the oocyte subcortex (PubMed:28992324). {ECO:0000269|PubMed:19141611, ECO:0000269|PubMed:28992324}.
Interaction partners:
- Oocyte-expressed protein homolog
- Transducin-like enhancer protein 6
- Inactive protein-arginine deiminase type-6
- NACHT, LRR and PYD domains-containing protein 5
Sequence:
MKSKKPLKITMEDSRRLNDPAEQGGLCPAPVGPSYSEAWGYFHLDPAQPRHRMMSAWATCRLCGLQVGGLPNFQMWTRALCQHLSDVHLPELKKSAAPSSPTTMPCPPPPSPTMAAEGDWARLLEQMGELAMRGSQRELELERREAALMQAELELERKRQALKQEAQSVEQERHQLQVEREALSKWIKKQSPGAQVPEPPSPLPLLPKEDPDIHDNNSDNDMVTKVLL
Protein: Translation initiation factor eIF2B subunit alpha (GCD complex subunit GCN3) (Guanine nucleotide exchange factor subunit GCN3) (Translational activator GCN3) (eIF2B GDP-GTP exchange factor subunit alpha) (P14741)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Acts as a non-essential regulatory component of the translation initiation factor 2B (eIF2-B or GCD complex), which catalyzes the exchange of eukaryotic initiation factor 2 (eIF-2)-bound GDP for GTP and is regulated by phosphorylated eIF-2. It activates the translation of GCN4 in response to low amino acid, carbon, or purine availability, by suppressing the inhibitory effects of multiple uORFs present in the leader of GCN4 mRNA. It may promote either repression or activation of GCN4 expression depending on amino acid availability. Modulation of GCN3 regulatory function in response to amino acid availability occurs post-translationally.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9USP0}.
Interaction partners:
- Translation initiation factor eIF2B subunit delta
- Eukaryotic translation initiation factor 2 subunit gamma
- Translation initiation factor eIF2B subunit gamma
- Translation initiation factor eIF2B subunit epsilon
- Eukaryotic translation initiation factor 2 subunit alpha
- Eukaryotic translation initiation factor 2 subunit beta
- Translation initiation factor eIF2B subunit beta
- eIF-2-alpha kinase GCN2
- Protein DSS4
- Protein LTV1
Sequence:
MSEFNITETYLRFLEEDTEMTMPIAAIEALVTLLRIKTPETAAEMINTIKSSTEELIKSIPNSVSLRAGCDIFMRFVLRNLHLYGDWENCKQHLIENGQLFVSRAKKSRNKIAEIGVDFIADDDIILVHGYSRAVFSLLNHAANKFIRFRCVVTESRPSKQGNQLYTLLEQKGIPVTLIVDSAVGAVIDKVDKVFVGAEGVAESGGIINLVGTYSVGVLAHNARKPFYVVTESHKFVRMFPLSSDDLPMAGPPLDFTRRTDDLEDALRGPTIDYTAQEYITALITDLGVLTPSAVSEELIKMWYD
Protein: Coenzyme gamma-F420-2:alpha-L-glutamate ligase (EC 6.3.2.32) (Q58407)
Organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Function: Catalyzes the ATP-dependent addition of one alpha-linked L-glutamate molecule to coenzyme gamma-F420-2, producing alpha-F420-3, the major form of coenzyme F420 found in M.jannaschii. Thus, caps the gamma-polyglutamate tail of coenzyme F420 with a terminal alpha-linked glutamate. Prefers ATP to other purine nucleotide triphosphates; GTP gives about 25% of the activity observed with ATP. Cannot catalyze the addition of the following amino acids or analogs: D-glutamate, beta-glutamate, L-aspartate, L-glutamine, L-alpha-aminoadipate, or D,L-2-amino-4-phosphono-butyrate.
Interaction partners:
- Coenzyme F420:L-glutamate ligase
- 2-phospho-L-lactate transferase
- 2-phospho-L-lactate guanylyltransferase
Sequence:
MVKITILSPEGRSCSVWSLKNEIEKLGAKCDIFLLSSPENLMSHDFKLETDLIHSRCGIGDYFDRLTLYSWQFINALEVEGCRFINPIKTLYLTSDKFKCIKLLAKNKIKTPKTALIRDYEDAVKFIEKYNLRFPVVIKNSFSKCGLKVFMARNYDELKQLTKNAIWEGKLIQEFIDFKENDLYRDMRILVVDGEVVGGYRRVSRDFRTNLYLGNVVEKLNIDEELEELALKCADLSEAVILGVDILPTKDNYYVIELNSSPGTKGFRDIGINADKKIAEALVRYAKS
Protein: Geranylgeranyl pyrophosphate synthase (O61538)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEELNIILQKTKDKSTQKEQDEILLQPFTYIQQIPGKQFRSELALAFNHWLLIPGEKLAQIGNIVQMLHNSSLLIEDNSILRRGVPVAHSIYGVASTINAANYALFLALEKVQQLDHPEVRKVYTEQLLELHRGQGMEIYWRDSFTCPSESDYKLMTVRKTGGLFMLAIRLMQLFSSNKEDYSKLTAILGLYFQIRDDYCNLSLKEVSVNKSFAEDLTEGKFGFPVIHAVRTQKQDKQVLRKSSQRTHDIEVKKYCITLLEKLGSFQYTRKVLESLDAEARSEVSTLGSNPYMDRLLNKLLSWKTSDSASITQSNQINHNNVSRSSPNQNTFNCN
Protein: 6-phosphogluconolactonase (6PGL) (EC 3.1.1.31) (P9WQP5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase 1
- Glucose-6-phosphate 1-dehydrogenase 2
- OXPP cycle protein OpcA
- Probable 6-phosphogluconate dehydrogenase,decarboxylating Gnd2
- 6-phosphogluconate dehydrogenase, decarboxylating
- Transaldolase
- Transketolase
- ATPase
- N-acetylglucosamine-6-phosphate deacetylase
- Glyceraldehyde-3-phosphate dehydrogenase
Sequence:
MSSSIEIFPDSDILVAAAGKRLVGAIGAAVAARGQALIVLTGGGNGIALLRYLSAQAQQIEWSKVHLFWGDERYVPEDDDERNLKQARRALLNHVDIPSNQVHPMAASDGDFGGDLDAAALAYEQVLAASAAPGDPAPNFDVHLLGMGPEGHINSLFPHSPAVLESTRMVVAVDDSPKPPPRRITLTLPAIQRSREVWLLVSGPGKADAVAAAIGGADPVSVPAAGAVGRQNTLWLLDRDAAAKLPS
Protein: Flocculation protein FLO10 (Flocculin-10) (P36170)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, glucose, maltose and sucrose. Also involved in cell-substrate adhesion, haploid invasive growth and diploid pseudohyphae formation.
Subcellular location: Secreted, cell wall {ECO:0000250}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Flocculation protein FLO11
Sequence:
MPVAARYIFLTGLFLLSVANVALGTTEACLPAGEKKNGMTINFYQYSLKDSSTYSNPSYMAYGYADAEKLGSVSGQTKLSIDYSIPCNGASDTCACSDDDATEYSASQVVPVKRGVKLCSDNTTLSSKTEKRENDDCDQGAAYWSSDLFGFYTTPTNVTVEMTGYFLPPKTGTYTFGFATVDDSAILSVGGNVAFECCKQEQPPITSTDFTINGIKPWNADAPTDIKGSTYMYAGYYYPIKIVYSNAVSWGTLPVSVVLPDGTEVNDDFEGYVFSFDDNATQAHCSVPNPAEHARTCVSSATSSWSSSEVCTECTETESTSYVTPYVTSSSWSSSEVCTECTETESTSTSTPYVTSSSSSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYVTSSSWSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYVTSSSSSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYVTSSSWSSSEVCTECTETESTSYVTPYVSSSTAAANYTSSFSSSSEVCTECTETESTSTSTPYATSSTGTATSFTASTSNTMTSLVQTDTTVSFSLSSTVSEHTNAPTSSVESNASTFISSNKGSVKSYVTSSIHSITPMYPSNQTVTSSSVVSTPITSESSESSASVTILPSTITSEFKPSTMKTKVVSISSSPTNLITSYDTTSKDSTVGSSTSSVSLISSISLPSSYSASSEQIFHSSIVSSNGQALTSFSSTKVSSSESSESHRTSPTTSSESGIKSSGVEIESTSTSSFSFHETSTASTSVQISSQFVTPSSPISTVAPRSTGLNSQTESTNSSKETMSSENSASVMPSSSATSPKTGKVTSDETSSGFSRDRTTVYRMTSETPSTNEQTTLITVSSCESNSCSNTVSSAVVSTATTTINGITTEYTTWCPLSATELTTVSKLESEEKTTLITVTSCESGVCSETASPAIVSTATATVNDVVTVYSTWSPQATNKLAVSSDIENSASKASFVSEAAETKSISRNNNFVPTSGTTSIETHTTTTSNASENSDNVSASEAVSSKSVTNPVLISVSQQPRGTPASSMIGSSTASLEMSSYLGIANHLLTNSGISIFIASLLLAIV