wanglab/gogpt-training-data huggingface dataset:
Protein: Leucine-rich repeat protein kinase family protein (A0A1I9LQ53)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MLCSVTQKHTHKMTLFFFYSLLFLLLLLRISTASLPATNYFDSFLPSDAVALLSFKSTADLDNKLLYSLTEPYDYCQWRGVDCSQDRVVRLILDGVGLRGSFSPETLSRLDQLRVLSLENNSISGSIPDLSPLVNLKTLTLSKNGFSGTLSSSILSLRRLTELDLSFNNFSGEIPSGINALSRLSSLNLEFNRLNGTLPPLNLSSLISFNVSSNNLTGLVPLTKTLLRFNASSFSSNPGLCGEIINRSCGLHSSSPFFGSPKPNTTSSTSSASSSEAPVIQSEQNGEAAMIVPPVVKKVKNGWLVLGFTIGLASLIVLGLCLVVFSLFIKNRREDYDDVIITQPKREEENKEIKIQFQTTAPSSKKRIPRNGDLIFCGEGGGGGEAMYTVDQLMRASAELLGRGSVGTTYKAVMVNQMIVTVKRFAPSKTAITSDLEFENQMEIVGGLKHPNLVPVKAYFQSNGERLVIYEYQPNGSLFNLIHGSRTSKAKPLHWTSCLKIAEDVAQALHYIHQSSAKFHGNLKSTNILLGHDFEACVTDYCLSVLTDSSVPPNDPDISSYKAPEIRKSTDSRPTSKCDVYSFGVFLLELLTGKTASRQPIMEPNDMLDWVRAMRQEEERSKEENGLEMMTQTACLCRVTSPEQRPTMKEVIKMIQEIKGSVVMTEENEKFL
Protein: Loquacious, isoform F (X2J5X6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDQENFHGSSLPQQLQNLHIQPQQASPNPVQTGFAPRRHYNNLVGLGNGNAVSGSPVKGAPLGQRHVKLKKEKISAQVAQLSQPGQLQLSDVGDPALAGGSGLQGGVGLMGVILPSDEALKFVSETDANGLAMKTPVSILQELLSRRGITPGYELVQIEGAIHEPTFRFRVSFKDKDTPFTAMGAGRSKKEAKHAAARALIDKLIGAQLPESPSSSAGPSVTGLTVAGSGGDGNANATGGGDASDKTVGNPIGWLQEMCMQRRWPPPSYETETEVGLPHERLFTIACSILNYREMGKGKSKKIAKRLAAHRMWMRLQETPIDSGKISDSICGELEGEPRSSENYYGELKDISVPTLTTQHSNKVSQFHKTLKNATGKKLLKLQTCLKNNKIDYIKLLGEIATENQFEVTYVDIEEKTFSGQFQCLVQLSTLPVGVCHGSGPTAADAQRHAAQNALEYLKIMTKK
Protein: DNA/RNA-binding protein Alba-like domain-containing protein (Q583J0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA/RNA-binding protein Alba-like domain-containing protein
- DNA/RNA-binding protein Alba-like domain-containing protein
Sequence:
MPSYPSHDDRQRTKNEGAKEKGQGAENEIRVTARPGSRGYITYALALLRGEEGKPKYDSVKISAMGAAIRSAVGVAEVLKRRVAGLHQTTEISSEVIHDTYEGNDDKTEKKEVERKVSTILITLSLKPLDVNHIGYQAPLPESEVKEEEERSQISRGRGGGGGSRAGGRGAGRGGGSRGGGRGAAGSRGRGRGRGRGGTGGGAHGSQRDGSDLGEGN
Protein: Transmembrane protein 130 (Q8N3G9)
Organism: Homo sapiens (Human)
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:11256614}; Single-pass type I membrane protein {ECO:0000269|PubMed:11256614}.
Interaction partners:
Sequence:
MAQAVWSRLGRILWLACLLPWAPAGVAAGLYELNLTTDSPATTGAVVTISASLVAKDNGSLALPADAHLYRFHWIHTPLVLTGKMEKGLSSTIRVVGHVPGEFPVSVWVTAADCWMCQPVARGFVVLPITEFLVGDLVVTQNTSLPWPSSYLTKTVLKVSFLLHDPSNFLKTALFLYSWDFGDGTQMVTEDSVVYYNYSIIGTFTVKLKVVAEWEEVEPDATRAVKQKTGDFSASLKLQETLRGIQVLGPTLIQTFQKMTVTLNFLGSPPLTVCWRLKPECLPLEEGECHPVSVASTAYNLTHTFRDPGDYCFSIRAENIISKTHQYHKIQVWPSRIQPAVFAFPCATLITVMLAFIMYMTLRNATQQKDMVEVADFDFSPMSDKNPEPPSGVRCCCQMCCGPFLLETPSEYLEIVRENHGLLPPLYKSVKTYTV
Protein: Uncharacterized WD repeat-containing protein C713.05 (Q9C1X0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Spliceosome-associated protein 49
- Uncharacterized protein C20H4.06c
- Pre-mRNA-splicing factor spp42
- Pre-mRNA-splicing factor cwf18
- Pre-mRNA-splicing factor cwf19
- Pre-mRNA-splicing factor ini1
- Pre-mRNA-processing ATP-dependent RNA helicase prp11
- Splicing factor cactin
- Protein psi1
- PWI domain-containing protein C825.05c
Sequence:
MRLEAKTKLSSKAKEPINVVKYNRTGKYVLAAGNERVVRLWNVKSGACIHEYAGHGHEILDLDLVYDSTKFASCGGDKFIQVWDVNTGKVDRRLGGHLAQINTIRYNEDSSILASGSFDSKVRLWDCRSNSFSPIQVLADAKDSVSSIDIAEHLIVTGSTDGTLRTYDIRKGTLSSDYFSHPITSVKTSKSASFSLISSLNSSIHLLDQETGKILKSYIGLKNMEYRVRSSFNQSETIVFSGSEDGKVYLWDLENETQITSTSVVGTPIVTDISCHPTMDDFIIATVHGDLFIYQYN
Protein: Glutathione S-transferase (EC 2.5.1.18) (GST class-pi) (C7DJS2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368105}. Mitochondrion {ECO:0000256|RuleBase:RU368105}. Nucleus {ECO:0000256|RuleBase:RU368105}.
Interaction partners:
Sequence:
QDGDLTLYQSNTILRHLGRTLGLYGKDQQEAALVDMVNDGVEDLRCKYVSLIYTNYEAGKDDYVKALPGQLKPFETLLSQNQGGKTFIVGDQISFADYNLLDLLLIHEVLAPGCLDAFPLLSAYVGRLSARPKLKAFLASPEYVNLPINGN
Protein: Cyclin dependent kinase 19 (F6QTA4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDVFAGCQIPYPKREFLNEDDPEEKGDKNQQQQQNQHQQPTAPPQQAAAPPQAPPPQQNSTQTNGTAGGAGAGVGGTGAGLQHSQDSSLNQVPPNKKPRLGPSGANSGGPVMPSDYQHSSSRLNYQSSVQGSSQSQSTLGYSSSSQQSSQYHPSHQAHRY
Protein: UPF0654 protein C11D3.01c (Q10080)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- UPF0039 protein C11D3.02c
- Phosphoacetylglucosamine mutase 2
- Antisense-enhancing sequence 1
- Uncharacterized methyltransferase C70.08c
- UPF0591 membrane protein C15E1.02c
- UPF0300 protein C737.04
- Uncharacterized oxidoreductase C663.06c
Sequence:
MPNPGNVIGGHKAALHNPNVSEETKQREKEYLEEHEGEVGEEHQKNTGNVRGGYKAAMHNPNVSGEAKQRAQEELENLE
Protein: RNA helicase (EC 3.6.4.13) (Q9N3F4)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNTQYYANHNGQQQPPQQQQGQGWSSSYSQQSNNMPAGGVFYNGFANGTPSNNGSSGYNNFADSGNGFNNNGAESNQWGGAPAEYSESNLFHRTDSGINFDKYENIPVEVSGDSVPAAIEHFNEAGFGPAVMENVNRSGYSKPTPVQKHSIPTLLANRDLMSCAQTGSGKTAAFLLPIIQHILAGGPDMVKPPAFTNGRRTYYPCALVLSPTRELAIQIHKEATKFSYKSNIQTAILYGGRENYRDQVNRLRAGTHILIATPGRLIDIIEQGFIGLAGCRYLVLDEADRMLDMGFEPQIRKIVGQGMPPKTARTTAMFSATFPKEIQVLAKDFLKDNYIFLAVGRVGSTSENIEQRLLWVNEMEKRSNLMEILMNEHSENLVLVFVETKRGANELAYFLNRQQIRSVSIHGDLKQIERERNLELFRSGQCPILVATAVAARGLDIPNVRHVINYDLPGDSDEYVHRIGRTGRCGNLGIATSFFNDKNRGIGRDLKNLIVESNQEVPEWLHQVAAEGRIGGGQRGGNRRFGATDYRVGRGGGGSFGGNFSNYNSGGATGGFGSGPAYGGSFGGGAPRRPFTNGGFGAHSSLSSTSNSGGGGGFSGPRRGGFNSGMNRQGGGGGGFYSNPGQAPIDHWQAPQA
Protein: LAS seventeen-binding protein 5 (LAS17-binding protein 5) (P25369)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Essential for the organization of the actin cytoskeleton, fluid phase endocytosis and vesicle trafficking, together with YSC84.
Subcellular location: Cytoplasm, cell cortex {ECO:0000269|PubMed:12388763}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12388763}. Note=Localizes independently of F-actin.
Interaction partners:
- Protein YSC84
- ADP-ribosylation factor 3
- Actin cytoskeleton-regulatory complex protein SLA1
- ADP-ribosylation factor-like protein 1
- Protein GTS1
- Proline-rich protein LAS17
- LAS seventeen-binding protein 3
- Myosin tail region-interacting protein MTI1
- Altered inheritance of mitochondria protein 3
Sequence:
MGFLSDHPHTAITETIFRIVSSRDYTLEVELAPLIQLIKADHNDYNYTVNQEEAARALRKKIKYGNRLQQSRTLDLLDLFISQGVKFTVMYNDDKLLQRLRGMATNSENSGSGEKYEPRIIKKCAAYAISWLNYITQNNLENARAYSGLYQLGQTVKQRYSKSSRSRRSGGGSGGRSNFMDDSADDTLYQSNSLTSADRLYRIPQINMNKEAPRIRLIISDALASAVSLQNSLIGLPKGKFSTDDEEATSKFIQARAIRRKVLRYLQLVTEGEFLGSLIHANDELVAALTAYDDRSAQDDSSDESDHGSYDDGIYDENEQDNSRYIDSESSEEESLSSYQPSTISNPFGDHNKI
Protein: Alpha-1,3/1,6-mannosyltransferase ALG2 (EC 2.4.1.132) (EC 2.4.1.257) (Asparagine-linked glycosylation protein 2 homolog) (GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase) (GDP-Man:Man(1)GlcNAc(2)-PP-dolichol mannosyltransferase) (GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase) (Q9H553)
Organism: Homo sapiens (Human)
Function: Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:35136180}; Single-pass membrane protein {ECO:0000269|PubMed:35136180}. Note=Active on cytoplasmic side of endoplasmic reticulum membrane. {ECO:0000269|PubMed:35136180}.
Interaction partners:
- Chitobiosyldiphosphodolichol beta-mannosyltransferase
- GDP-Man:Man
- Phosphomannomutase 2
- V-type proton ATPase 116 kDa subunit a 2
- Dol-P-Man:Man
- Dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Programmed cell death 6-interacting protein
- Structure-specific endonuclease subunit MUS81
- Phosphoglucomutase-1
- Potassium-transporting ATPase alpha chain 1
Sequence:
MAEEQGRERDSVPKPSVLFLHPDLGVGGAERLVLDAALALQARGCSVKIWTAHYDPGHCFAESRELPVRCAGDWLPRGLGWGGRGAAVCAYVRMVFLALYVLFLADEEFDVVVCDQVSACIPVFRLARRRKKILFYCHFPDLLLTKRDSFLKRLYRAPIDWIEEYTTGMADCILVNSQFTAAVFKETFKSLSHIDPDVLYPSLNVTSFDSVVPEKLDDLVPKGKKFLLLSINRYERKKNLTLALEALVQLRGRLTSQDWERVHLIVAGGYDERVLENVEHYQELKKMVQQSDLGQYVTFLRSFSDKQKISLLHSCTCVLYTPSNEHFGIVPLEAMYMQCPVIAVNSGGPLESIDHSVTGFLCEPDPVHFSEAIEKFIREPSLKATMGLAGRARVKEKFSPEAFTEQLYRYVTKLLV
Protein: UTP:RNA uridylyltransferase 1 (EC 2.7.7.52) (O64642)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: UTP:RNA uridylyltransferase with a marked preference for uridine polymerization and a distributive activity for the first added nucleotides. Uridylates oligo(A)-tailed mRNAs to prevent 3' to 5' ribonucleotytic attacks. Reduces the accumulation of oligo(A)-tailed mRNAs. Prevents the accumulation of excessively deadenylated mRNAs to avoid siRNA biogenesis. Uridylation repairs deadenylated extremities to restore the size distribution observed for non-uridylated oligo(A) tails. Can prevent the 3' trimming of mRNAs still engaged on polysomes. Acts synergistically with HESO1 in unmethylated miRNA uridylation, leading to their degradation. URT1 and HESO1 prefer substrates with different 3' end nucleotides and act cooperatively to tail different forms of the same miRNAs. URT1 and HESO1 act sequentially, with URT1 mono-uridylating the miRNAs followed by their further uridylation by HESO1. URT1 and HESO1 are involved in the uridylation and clearance of RISC-generated 5' mRNA fragments. Has no effect on uridylation of heterochromatic siRNAs. Able to act on AGO1-bound miRNAs and the uridylated species stay associated with AGO1. Acts as post-transcriptional gene silencing (PTGS) suppressor.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23748567}. Cytoplasm, P-body {ECO:0000269|PubMed:23748567, ECO:0000269|PubMed:25928341}. Note=The P618L single amino acid substitutiontarget URT1 to the nucleoplasm. {ECO:0000269|PubMed:25928341}.
Interaction partners:
- Small RNA degrading nuclease 1
- Inactive exonuclease DIS3L2
- Ribonuclease II, chloroplastic/mitochondrial
- Nucleotidyltransferase
- RmlC-like jelly roll fold protein
- Small RNA degrading nuclease 2
- Nucleotidyltransferase family protein
- Small RNA degrading nuclease 5
- Small RNA 2'-O-methyltransferase
- Decapping 5-like protein
Sequence:
MADGGAEPPAPPSSINAGEFLLSILHGSPSPSSQGPQHHQSFALDPAIAAIGPTVNNPFPPSNWQSNGHRPSNHNPPSWPLAFSPPHNLSPNFLGFPQFPPSPFTTNQFDGNQRVSPEDAYRLGFPGTTNPAIQSMVQQQQQQQLPPPQSETRKLVFGSFSGDATQSLNGLHNGNLKYDSNQHEQLMRHPQSTLSNSNMDPNLSHHRNHDLHEQRGGHSGRGNWGHIGNNGRGLKSTPPPPPPGFSSNQRGWDMSLGSKDDDRGMGRNHDQAMGEHSKVWNQSVDFSAEANRLRGLSIQNESKFNLSQQIDHPGPPKGASLHSVSAADAADSFSMLNKEARRGGERREELGQLSKAKREGNANSDEIEDFGEDIVKSLLLEDETGEKDANDGKKDSKTSREKESRVDNRGQRLLGQKARMVKMYMACRNDIHRYDATFIAIYKSLIPAEEELEKQRQLMAHLENLVAKEWPHAKLYLYGSCANSFGFPKSDIDVCLAIEGDDINKSEMLLKLAEILESDNLQNVQALTRARVPIVKLMDPVTGISCDICINNVLAVVNTKLLRDYAQIDVRLRQLAFIVKHWAKSRRVNETYQGTLSSYAYVLMCIHFLQQRRPPILPCLQEMEPTYSVRVDNIRCTYFDNVDRLRNFGSNNRETIAELVWGFFNYWAYAHDYAYNVVSVRTGSILGKREKDWTRRVGNDRHLICIEDPFETSHDLGRVVDKFSIRVLREEFERAARIMHQDPNPCAKLLEPYIPEDNNGQGHN
Protein: DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) (E5KPM7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKVADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELGNFFRSLWGPYAGWAQALCQVITTFMTFLGPHRLDQMPPEELQTSSSRLGGPPWQCI
Protein: Glutaredoxin-C5, chloroplastic (AtGrxC5) (Q8GWS0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Has a glutathione-disulfide oxidoreductase activity in the presence of NADPH and glutathione reductase. Reduces low molecular weight disulfides and proteins. Can assemble a [2Fe-2S] cluster, but cannot transfer it to an apoferredoxin.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:21632542}.
Interaction partners:
- LOW PSII ACCUMULATION-like protein
- Peptide methionine sulfoxide reductase B1, chloroplastic
- Monothiol glutaredoxin-S15, mitochondrial
- Bifunctional monothiol glutaredoxin-S16, chloroplastic
- Monothiol glutaredoxin-S14, chloroplastic
- Peroxiredoxin-2E, chloroplastic
- Monothiol glutaredoxin-S17
- At5g58530
- Protein disulfide isomerase-like 1-6
- Thioredoxin-like 1-3, chloroplastic
Sequence:
MAVTAFNTLKLVSSSLDPIPSVSCSSYSFSLIYVGSPYKRCLKQSCSVRAMTSSSSAASSSSSSFGSRMEESIRKTVTENTVVIYSKTWCSYCTEVKTLFKRLGVQPLVVELDQLGPQGPQLQKVLERLTGQHTVPNVFVCGKHIGGCTDTVKLNRKGDLELMLAEANGKNGQS
Protein: D-glutamate cyclase, mitochondrial (EC 4.2.1.48) (Q7Z3D6)
Organism: Homo sapiens (Human)
Function: D-glutamate cyclase that converts D-glutamate to 5-oxo-D-proline.
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:Q8BH86}.
Interaction partners:
- Glutaminase liver isoform, mitochondrial
- Glutaminase kidney isoform, mitochondrial
Sequence:
MPFTLHLRSRLPSAIRSLILQKKPNIRNTSSMAGELRPASLVVLPRSLAPAFERFCQVNTGPLPLLGQSEPEKWMLPPQGAISETRMGHPQFWKYEFGACTGSLASLEQYSEQLKDMVAFFLGCSFSLEEALEKAGLPRRDPAGHSQTTVPCVTHAGFCCPLVVTMRPIPKDKLEGLVRACCSLGGEQGQPVHMGDPELLGIKELSKPAYGDAMVCPPGEVPVFWPSPLTSLGAVSSCETPLAFASIPGCTVMTDLKDAKAPPGCLTPERIPEVHHISQDPLHYSIASVSASQKIRELESMIGIDPGNRGIGHLLCKDELLKASLSLSHARSVLITTGFPTHFNHEPPEETDGPPGAVALVAFLQALEKEVAIIVDQRAWNLHQKIVEDAVEQGVLKTQIPILTYQGGSVEAAQAFLCKNGDPQTPRFDHLVAIERAGRAADGNYYNARKMNIKHLVDPIDDLFLAAKKIPGISSTGVGDGGNELGMGKVKEAVRRHIRHGDVIACDVEADFAVIAGVSNWGGYALACALYILYSCAVHSQYLRKAVGPSRAPGDQAWTQALPSVIKEEKMLGILVQHKVRSGVSGIVGMEVDGLPFHNTHAEMIQKLVDVTTAQV
Protein: Granulocyte-macrophage colony-stimulating factor (GM-CSF) (Colony-stimulating factor) (CSF) (Q29118)
Organism: Sus scrofa (Pig)
Function: Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes.
Subcellular location: Secreted.
Interaction partners:
- Fibronectin type-III domain-containing protein
- Colony stimulating factor 2 receptor subunit beta
- Interferon gamma
- Granulocyte colony-stimulating factor
- Interleukin-1 alpha
- Interleukin-6
- Interleukin-2
- Interleukin-4
- Interleukin-1 beta
- Multifunctional fusion protein
Sequence:
MWLQNLLLLGTVVCSISAPTRPPSPVTRPWQHVDAIKEALSLLNNSNDTAAVMNETVDVVCEMFDPQEPTCVQTRLNLYKQGLRGSLTRLKSPLTLLAKHYEQHCPLTEETSCETQSITFKSFKDSLNKFLFTIPFDCWGPVKK
Protein: Guanine nucleotide-binding protein G(T) subunit gamma-T1 (Transducin gamma chain) (P63211)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- C-C chemokine receptor type 5
- Rhodopsin
- Phosducin
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Guanine nucleotide-binding protein G
Sequence:
MPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEVRDYVEERSGEDPLVKGIPEDKNPFKELKGGCVIS
Protein: Tachykinin-related peptide 3 (TKRP-3) (P86596)
Organism: Pyrrhocoris apterus (Sap sucking bug) (Cimex apterus)
Subcellular location: Secreted {ECO:0000269|PubMed:19084564, ECO:0000305}.
Interaction partners:
Sequence:
GPSSGFFGTR
Protein: Kelch-like protein 17 (Actinfilin) (Q6TDP4)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of some cullin-RING-based BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complexes. The BCR(KLHL17) complex mediates the ubiquitination and subsequent degradation of GLUR6. May play a role in the actin-based neuronal function (By similarity).
Subcellular location: Postsynaptic density {ECO:0000250|UniProtKB:Q8K430}. Synapse {ECO:0000250|UniProtKB:Q8K430}.
Interaction partners:
- Cullin-3
Sequence:
MQPRSERPAGRTQSPEHGSPGPGPEAPPPPPPQPPAPEAERTRPRQARPAAPMEGAVQLLSREGHSVAHNSKRHYHDAFVAMSRMRQRGLLCDIVLHVAAKEIRAHKVVLASCSPYFHAMFTNEMSESRQTHVTLHDIDPQALDQLVQFAYTAEIVVGEGNVQTLLPAASLLQLNGVRDACCKFLLSQLDPSNCLGIRGFADAHSCSDLLKAAHRYVLQHFVDVAKTEEFMLLPLKQVLELVSSDSLNVPSEEEVYRAVLSWVKHDVDARRQHVPRLMKCVRLPLLSRDFLLGHVDAESLVRHHPDCKDLLIEALKFHLLPEQRGVLGTSRTRPRRCEGAGPVLFAVGGGSLFAIHGDCEAYDTRTDRWHVVASMSTRRARVGVAAVGNRLYAVGGYDGTSDLATVESYDPVTNTWQPEVSMGTRRSCLGVAALHGLLYSAGGYDGASCLNSAERYDPLTGTWTSVAAMSTRRRYVRVATLDGNLYAVGGYDSSSHLATVEKYEPQVNVWSPVASMLSRRSSAGVAVLEGALYVAGGNDGTSCLNSVERYSPKAGAWESVAPMNIRRSTHDLVAMDGWLYAVGGNDGSSSLNSIEKYNPRTNKWVAASCMFTRRSSVGVAVLELLNFPPPSSPTLSVSSTSL
Protein: Thioredoxin-like protein slr0233 (P52232)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Interaction partners:
- Putative peroxiredoxin sll0755
- OmpR subfamily
- Peroxiredoxin sll1621
- Rehydrin
- Slr0600 protein
- Slr0565 protein
- DNA-binding dual master transcriptional regulator RpaA
Sequence:
MAVKKQFANFAEMLAGSPKPVLVDFYATWCGPCQMMAPILEQVGSHLRQQIQVVKIDTDKYPAIATQYQIQSLPTLVLFKQGQPVHRMEGVQQAAQLIQQLQVFV
Protein: Ankyrin repeat- and BTB/POZ domain-containing protein 3 (BTB/POZ domain-containing protein 11) (Q6GQW0)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MARRGKKPVVRTLEDLTLDSGYGGAADSVRSSNLSLCCSDSHPASPYGGSCWPPLADSMHSRHNSFDTVNTALVEDSEGLDCAGQHCSRLLPDLDEVPWTLQELELLLLRSRDPRAGPAVPGSLPKDALAKLSMLVSRALVRIAKEAQRLSLRFAKCTKYEIQSAMEIVLSWGLAAHCTAAALAALSLYNMSSAGGDRLGRGKSARCGLTFSVGRVYRWMVDSRVALRIHEHAAIYLTACMESLFRDIYSRVLASGLPRSCSGPGPGSSSGSGPGPGSGPGAPAADKERETPGGGAASGGPCSAASSASGGSSCCAPPATAATAVPPTTATAAVAANHHHHHHTLHEAPKFTVETLEHTVNNDSEIWGLLQPYQHLICGKNASGVLSLPESLNLHRDPQRPSKPGELPMFSQSELRTIEQSLLATRVGSIAELSDLVSRAMHHLQPLNAKHHGNGTPMHHKQGALYWEPEALYTLCYFMHCPQMEWENPNVEPSKVNLQVERPFLVLPPLMEWIRVAVAHAGHRRSFSMDSDDVRQAARLLLPGVDCEPRQLKADDCFCASRKLDAVAIEAKFKQDLGFRMLNCGRTDLVKQAVSLLGPDGINTMSEQGMTPLMYACVRGDEAMVQMLLDAGADLNVEVVSTPHKYPSVHPETRHWTALTFAVLHGHIPVVQLLLDAGAKVEGSVEHGEENYSETPLQLAAAVGNFELVSLLLERGADPLIGTMYRNGISTTPQGDMNSFSQAAAHGHRNVFRKLLAQPEKEKSDILSLEEILAEGTDLAETAPPPLCASRNSKAKLRALREAMYHSAEHGYVDVTIDIRSIGVPWTLHTWLESLRIAFQQHRRPLIQCLLKEFKTIQEEEYTEELVTQGLPLMFEILKASKNEVISQQLCVIFTHCYGPYPIPKLTEIKRKQTSRLDPHFLNNKEMSDVTFLVEGRPFYAHKVLLFTASPRFKALLSSKPTNDNTCIEIGYVKYPIFQLVMQYLYYGGPESLLIKNNEIMELLSAAKFFQLEALQRHCEIICAKSINTDNCVDIYSHAKFLGVTELSAYCEGYFLKNMMVLIENEAFKQLLYDKNGEGAGQDVLQDLQRTLAIRIQSIHLSSSKGSVV
Protein: Cytochrome P450 2D1 (EC 1.14.14.1) (CYPIID1) (Cytochrome P450-CMF1A) (Cytochrome P450-DB1) (Cytochrome P450-UT-7) (Debrisoquine 4-hydroxylase) (P10633)
Organism: Rattus norvegicus (Rat)
Function: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
Sequence:
MELLNGTGLWSMAIFTVIFILLVDLMHRRHRWTSRYPPGPVPWPVLGNLLQVDLSNMPYSLYKLQHRYGDVFSLQKGWKPMVIVNRLKAVQEVLVTHGEDTADRPPVPIFKCLGVKPRSQGVILASYGPEWREQRRFSVSTLRTFGMGKKSLEEWVTKEAGHLCDAFTAQAGQSINPKAMLNKALCNVIASLIFARRFEYEDPYLIRMVKLVEESLTEVSGFIPEVLNTFPALLRIPGLADKVFQGQKTFMALLDNLLAENRTTWDPAQPPRNLTDAFLAEVEKAKGNPESSFNDENLRMVVVDLFTAGMVTTATTLTWALLLMILYPDVQRRVQQEIDEVIGQVRCPEMTDQAHMPYTNAVIHEVQRFGDIAPLNLPRFTSCDIEVQDFVIPKGTTLIINLSSVLKDETVWEKPHRFHPEHFLDAQGNFVKHEAFMPFSAGRRACLGEPLARMELFLFFTCLLQRFSFSVPVGQPRPSTHGFFAFPVAPLPYQLCAVVREQGL
Protein: L-lysine 4-chlorinase (EC 1.14.20.-) (Halogenase BesD) (G8XHD5)
Organism: Streptantibioticus cattleyicolor (strain ATCC 35852 / DSM 46488 / JCM 4925 / NBRC 14057 / NRRL 8057) (Streptomyces cattleya)
Function: Involved in the biosynthesis of terminal alkyne-containing amino acids such as L-propargylglycine (Pra) and L-beta-ethynylserine, that are produced as antibiotics by S.cattleya. Catalyzes the chlorination of L-lysine at the C4 position, leading to the production of 4-chloro-L-lysine.
Interaction partners:
Sequence:
MCAPLEKDDIRRLSQAFHRFGIVTVTELIEPHTRKLVRAEADRLLDQYAERRDLRLATTDYTRRSMSVVPSETIAANSELVTGLYAHRELLAPLEAIAGERLHPCPKADEEFLITRQEQRGDTHGWHWGDFSFALIWVLQAPPIDVGGLLQCVPHTTWDKASPQINRYLVENPIDTYHFESGDVYFLRTDTTLHRTIPLREDTTRIILNMTWAGERDLSRKLAADDRWWDNAEVSAARAIKD
Protein: D-cysteine desulfhydrase (EC 4.4.1.15) (P76316)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the alpha,beta-elimination reaction of D-cysteine and of several D-cysteine derivatives. It could be a defense mechanism against D-cysteine. Can also catalyze the degradation of 3-chloro-D-alanine.
Interaction partners:
- L-cystine transport system permease protein TcyL
- L-cystine-binding protein TcyJ
- L-cystine transport system ATP-binding protein TcyN
- Cystathionine beta-lyase MetC
- Protein MalY
- 3-mercaptopyruvate sulfurtransferase
Sequence:
MPLHNLTRFPRLEFIGAPTPLEYLPRFSDYLGREIFIKRDDVTPMAMGGNKLRKLEFLAADALREGADTLITAGAIQSNHVRQTAAVAAKLGLHCVALLENPIGTTAENYLTNGNRLLLDLFNTQIEMCDALTDPNAQLEELATRVEAQGFRPYVIPVGGSNALGALGYVESALEIAQQCEGAVNISSVVVASGSAGTHAGLAVGLEHLMPESELIGVTVSRSVADQLPKVVNLQQAIAKELELTASAEILLWDDYFAPGYGVPNDEGMEAVKLLARLEGILLDPVYTGKAMAGLIDGISQKRFKDEGPILFIHTGGAPALFAYHPHV
Protein: Uncharacterized protein C8orf48 (Q96LL4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAICPELAQTDKSALANLSDETETLKNSTDEVQTSSSFSSSGGRQSSPLTSGSKLEREKQTPSLEQGDTQSELLDYKNYEKKLSKKWINYLKLKDSNFERHQPDTKLPTEITRVSDEELNALQSYCTMKINLIHRRGDSKKKTSSRHKKLHLGLDVEASERDAFSCTVPDELLNRIYFKNMRTTPKQEAAAKQHISYQCPYCNRKRAELALSAFLKQKKTLLESFLLQERIDEHLHTKDFLTRIGEAHQDFPRLSDDPRIIWKRLTEKSHIRYSGFERSETEQKLQRDGNSACHLPFSLPFLKRLTLIKPELVIVNDNV
Protein: Chloride channel protein D (Q1ZXJ0)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Voltage-gated chloride channel. Chloride channels may have several functions including the regulation of cell volume, membrane potential stabilization and signal transduction (By similarity). Required for normal aggregation.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- RIC1 C-terminal alpha solenoid region domain-containing protein
- Calcium-binding EF-hand domain-containing protein
- EGF-like domain-containing protein
- Ubiquitin domain-containing protein
- BEACH domain-containing protein lvsD
Sequence:
MSSGNPFDNGNPNDGNKSPSIDELYSPSESLARDGDDNNNNNNNNNNNNNNNNNNNNSSVSEKKKSKKKVRIQEEERLTESYDDDGDDEERRAYIENEEGEEEETEDGIILQPIVRDHSTYRPKNLYGSSDDIREGDSFGAKVSKTFGKTNKKIKQKIGESNKKIETRVKHSNKAIEEGWKTIAQTTMKPVDNIREQHHRRAEQHEVAERAVWFKDKLQIQKYECLDYVTIYNKAHRNELYKNFSKLASDHEVLRWIVSLFMGIFIGVIAYFSHACVSNITKYKFKFVEAVLELDLFLAFLTYFLLNTLLATCSSLLAVYYEPTAAGSGIPEVKGYLNGTKIPHTLKMKTLWTKFLSMVLAVSSGLQAGSEGPMIHIGAIVGNGFSQAQSKEFGFKIPFLRSFRNDKDKRDFVTSGAGAGVAAAFSAPLGGTLFSLEEVSSFWSIALTWRAFFCCMVATYTMNVLQSNSGSLTGLIIFNTGIGDKESYNWFEIIPFLLIGVLGGLGGALFTWINVKVTEFRREKINKIKSLRVLEVFLIIGLSTCIQFFLPLFFSCQNTAPFIPSVGNSTLTDVTLTNGAFYNSTIINGTFYNSTIANGTIYNSKFYNSSIYNSTITNGTGVSYDPAETLKELSEFKRFNCKEGWYNPMATLIFASYEESITNLLKVNSNNVTNTERLGLWPMFLFCIFYLFFAAYTAGCAVATGTLVPMLVIGASYGRFVGLVVYHILGDKVSIDPGIYAVMGAAAFMGGVSRLTISLTVILIEITDRLKYLLPLMLTVMTAKWVADALIHPLFDLLMQMKYIPYLELDQSKEMKLMMCKHIMAKKPVYLAEKDTLGNLRVLKETRHNGFPVVNNDEEKLVKGLILRTQLLMILERISDVYIPNSEAIYSHIEYTTKLTWKLPSVNDFNFDPADYSQEIDLSDVMNLTVITVNVEFAVSEAFQLFRTMGLRHMPVVNENNKLKGIITKKDLLEKTCEQRYRELNHMKLGIDQLIHVGDE