wanglab/gogpt-training-data huggingface dataset:
Protein: Guanine nucleotide-binding protein G(t) subunit alpha-1 (Transducin alpha-1 chain) (P11488)
Organism: Homo sapiens (Human)
Function: Functions as signal transducer for the rod photoreceptor RHO. Required for normal RHO-mediated light perception by the retina. Guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs), such as the photoreceptor RHO. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound state. Activated RHO promotes GDP release and GTP binding. Signaling is mediated via downstream effector proteins, such as cGMP-phosphodiesterase (By similarity).
Subcellular location: Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P04695}. Membrane {ECO:0000250|UniProtKB:P04695}; Peripheral membrane protein {ECO:0000250|UniProtKB:P04695}. Photoreceptor inner segment {ECO:0000250|UniProtKB:P20612}. Note=Localizes mainly in the outer segment in the dark-adapted state, whereas is translocated to the inner part of the photoreceptors in the light-adapted state. During dark-adapted conditions, in the presence of UNC119 mislocalizes from the outer segment to the inner part of rod photoreceptors which leads to decreased photoreceptor damage caused by light. {ECO:0000250|UniProtKB:P20612}.
Interaction partners:
- Rhodopsin
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Guanine nucleotide-binding protein G
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Regulator of G-protein signaling 9
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
Sequence:
MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFERASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNKKDVFFEKIKKAHLSICFPDYDGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF
Protein: Triacylglycerol lipase 5 (TAG lipase 5) (TG lipase 5) (EC 3.1.1.3) (Lipase 5) (Q12043)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways. Also catalyzes the acylation of lysophosphatidic acid (LPA).
Subcellular location: Lipid droplet {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16135509, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:24868093, ECO:0000269|PubMed:27170177}. Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols. {ECO:0000269|PubMed:27170177}.
Interaction partners:
- Triacylglycerol lipase 4
- Sterol esterase TGL1
- Diacylglycerol O-acyltransferase 1
- Monoglyceride lipase
- Triacylglycerol lipase 2
- Phospholipid:diacylglycerol acyltransferase
- Lysophospholipid acyltransferase
- NADPH-dependent 1-acyldihydroxyacetone phosphate reductase
- Lysophosphatidic acid:oleoyl-CoA acyltransferase 1
- Phosphatidic acid phosphohydrolase 1
Sequence:
MSNTLPVTEFLLSKYYELSNTPATDSSSLFKWLYHKTLSRKQLLISDLSSQKKHAISYDQWNDIASRLDDLTGLSEWKTIDESSLYNYKLLQDLTIRMRHLRTTHDYHRLLYLIRTKWVRNLGNMNNVNLYRHSHTGTKQIIHDYLEESQAVLTALIHQSNMNDHYLLGILQQTRRNIGRTALVLSGGSTFGLFHIGVLAALFESDLMPKVISGSSAGAIVASIFCVHTTQEIPSLLTNVLNMEFNIFNDDNSKSPNENLLIKISRFCQNGTWFNNQPLINTMLSFLGNLTFREAYNKTGKILNITVSPASIYEQPKLLNNLTAPNVLIWSAVCASCSLPGVFPSTPLFEKDPHTGKIKEWGATNLHLSNMKFMDGSVDNDMPISRLSEMFNVDHIIACQVNIHVFPLLKFSNTCVGGEIEKEITARFRNQVTKIFKFFSDETIHFLDILKELEFHPYLMTKLKHLFLQQYSGNVTILPDLSMVGQFHEVLKNPSQLFLLHQTTLGARATWPKISMIQNNCGQEFALDKAITFLKEKIIISSSIKNPLQFYQPRFSEQIKSLSIMDADLPGVDLEESSSNSLSIIKSPNKTAAPGRFPLQPLPSPSSTFNKRKMDMLSPSPSPSTSPQRSKSSFTQQGTRQKANSLSFAIGASSLRLKKSPLKVPSRPQFKKRSSYYNQNMSAEMRKNRKKSGTISSYDVQTNSEDFPIPAIENGSFDNTLFNPSRFPMDAMSAATNDNFMNNSDIFQN
Protein: Uncharacterized ferredoxin-like protein YfaE (P0ABW3)
Organism: Escherichia coli (strain K12)
Interaction partners:
- Ribonucleoside-diphosphate reductase 1 subunit beta
- Ribonucleoside-diphosphate reductase 1 subunit alpha
- Iron-sulfur cluster assembly scaffold protein IscU
- 2Fe-2S ferredoxin
- NADH-quinone oxidoreductase subunit C/D
- Chaperone protein HscA
- Co-chaperone protein HscB
- Protein IscX
- Flavodoxin/ferredoxin--NADP reductase
- Thioredoxin reductase
Sequence:
MARVTLRITGTQLLCQDEHPSLLAALESHNVAVEYQCREGYCGSCRTRLVAGQVDWIAEPLAFIQPGEILPCCCRAKGDIEIEM
Protein: Serine/threonine-protein phosphatase 4 regulatory subunit 3-like central domain-containing protein (H2KYN7)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFENNETLIVWSETDVMDLALSFQEKSGCEELWQKICEVQGRDPGDPDATFDDGDDSDVGEMPSSASRLQLPPIEIGRLGELDALLHMHLTTNSAREKMTLAIENDNVVTKLCEVFRMCEDIEHTEGLRTFYSIVKNLFMLNRNTVIEMLLDDNNIKDVIGMFEFDPAYKHPRKHRDFVYKKAKFREVLNISCDELRDKIHRLYRAQYIQDACLPSLGLFEENLLSTLSSHVFFCRVDIVTLLQKDKKAMSELFGQLISEETDVIRRRDLALFLKEMISLSTSIPSNGPAATKETFFKLQLQNMFNSEILDSLEPCFKSPDHETRAVMVDVLRTMVDANAQMIRDFLLKQSKTKDKNEDVLLNMMIRHLLTDIDVHLTSGSEIVLIMKTLLDPENMTTVKSERSDFLQLFYNRCYESLLKPILENVSGGNIKKDDYMIANRQSVILRLLTFCVEHHSFSMRQRCVSNDLMNKVLVLLKSKHSFLVLSALKLLQRVVTVKDDKYIRYIVKEKVLDPVMECFRKNGNRYNIINSSVLHLFEFVRSEDVRPLIKYVVENHMEVVDSVNYVKTFKEIKIRYDQHRDREETMSVRSEDNSLASPRSFRKDRNEDQWFDEDEDLEVGTMLESIEKDSVAVSPKKEEAGQRKTGMEPMFPSLLKRKNAFDDDEAPVFGGGSAAVINNTEKKIVIKVNSDRSPSRTPSPASSPRASSSPGPSRDDEVTSSQNNKESSPTPTVKSLVDYDESDDSDDDPPSPDAVPSSSTGSPEKEGDSADGKKGDSPEYNDVSSTSNEEKFDSRNGAPVTNENGGVEAAAPTVEISRKRTSDGIDPDAKRIRTEETAPAATATVSQA
Protein: 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (HMBPP reductase) (EC 1.17.7.4) (1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase) (P62623)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the DOXP/MEP pathway for isoprenoid precursor biosynthesis. In vitro, can also hydrate acetylenes to aldehydes and ketones via anti-Markovnikov/Markovnikov addition.
Interaction partners:
- 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
- Farnesyl diphosphate synthase
- Isopentenyl-diphosphate Delta-isomerase
- 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase
- 1-deoxy-D-xylulose 5-phosphate reductoisomerase
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- 1-deoxy-D-xylulose-5-phosphate synthase
- FKBP-type 16 kDa peptidyl-prolyl cis-trans isomerase
- Small ribosomal subunit protein bS1
Sequence:
MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEVPDGAILIFSAHGVSQAVRNEAKSRDLTVFDATCPLVTKVHMEVARASRRGEESILIGHAGHPEVEGTMGQYSNPEGGMYLVESPDDVWKLTVKNEEKLSFMTQTTLSVDDTSDVIDALRKRFPKIVGPRKDDICYATTNRQEAVRALAEQAEVVLVVGSKNSSNSNRLAELAQRMGKRAFLIDDAKDIQEEWVKEVKCVGVTAGASAPDILVQNVVARLQQLGGGEAIPLEGREENIVFEVPKELRVDIREVD
Protein: CG2257 (LD13772p) (LD17992p) (Ubiquitin conjugating enzyme E2H, isoform A (EC 2.3.2.23)) (Ubiquitin conjugating enzyme E2H, isoform B) (Ubiquitin conjugating enzyme E2H, isoform C) (Q7JW03)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- WD repeat-containing protein 26 homolog
- FI21269p1
- GH10162p
- Ran-binding proteins 9/10 homolog
- lysozyme
- AT28509p
- LD28546p
- E1 ubiquitin-activating enzyme
- E3 ubiquitin-protein transferase MAEA
Sequence:
MSSPSAGKRRMDNDVIKLIESKHEVTILGGLNEFHVKFFGPTETPYEGGVWKVRVYLPDNYPFKSPSIGFVNKIYHPNIDESSGTVCLDVINQAWTALYDLSNIFESFLPQLLTYPNPVDPLNRDAAALYLHEPEEYHRKVADYVQRYATEDALRAAQQERESSDSESSMSDYSEDEARDMEL
Protein: Threonine-rich inner membrane protein GfcA (Group 4 capsule protein A homolog) (P75885)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane; Single-pass membrane protein. Note=When the protein is overexpressed.
Interaction partners:
- Uncharacterized lipoprotein GfcB
- Uncharacterized protein GfcC
- Uncharacterized lipoprotein GfcD
- Putative polysaccharide export protein GfcE
- Low molecular weight protein-tyrosine-phosphatase Etp
- Tyrosine-protein kinase etk
Sequence:
MKHKLSAILMAFMLTTPAAFAAPEATNGTEATTGTTGTTTTTTGATTTATTTGGVAAGAVGTATVVGVATAVGVATLAVVAANDSGDGGSHNTSTTTSTTR
Protein: Uncharacterized protein At2g14060 (Q9ZPT3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MKGGTGDHSYATNSHYQRSVFYEIQPLVIENVREMLLKNGFPGCIKVADLGCSTGQNTVLAMSAIAYTIMESYQQMSKNPPEIDCYLNDLPENDFNTTFKLFHSFQEKLKPEVKGKWFVSGVPGSFYSRLFPRKSLHFVHSAFSIHWLSRIPDGLESNTKSIHIKYPYPSNVYKSYLNQFKIDFSLFLKMRSEEVVHNGHMVLTFVGRKVSDTLSKDCFQVWSLLSDCLLDLASEGFVNDSMVKSFNMPFYNPNEEEVREFILKEGSFEITKIEKFDHVVPYKIDREEEDEEQSLQLEAGIKHASWARCITEPLLVAHFGDAIIEPVFNKYAHYMAKYLSVSNHRRNMTLVIVVSLTRK
Protein: Large ribosomal subunit protein P3z (60S acidic ribosomal protein P3-1) (Q9SVZ6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important role in the elongation step of protein synthesis.
Interaction partners:
- Large ribosomal subunit protein P1w
- Large ribosomal subunit protein eL38z/eL38y
- Large ribosomal subunit protein uL18z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL4y
- Large ribosomal subunit protein uL24y
- Large ribosomal subunit protein eL8z
- Large ribosomal subunit protein eL8y
- Small ribosomal subunit protein eS12y
- Large ribosomal subunit protein uL18y
Sequence:
MGVFTFVCKNGGGAWSAKQHEGELESSASSTYELQRKLVQVSLSADSSGGVQSSFSLVSPTSAVFQVIVGGGGGGGFSAGGAASSGGGAGEAAAAPKEDEKKKEESEEEEGDFGFDLFG
Protein: glucose-6-phosphate 1-epimerase (EC 5.1.3.15) (X2JAD3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Phosphoglucomutase 1
- Hexokinase type 1
- Glucose-6-phosphate isomerase
- Phosphoglucomutase 2a
- Phosphoglucomutase 2b
- Hexokinase type 2
- Phosphotransferase
- Phosphotransferase
- LD24362p
- FI19814p1
Sequence:
MATTAAAMAATSVVVLDRGNNTTCTINLHGATVVSWRVNNQEQLFVSKLASFDGKKAIRGGIPFVFPQFGAWSFGPQHGFARITRWHLERPPDRLHNGDVEAIFSLMDNDFTRSIWNYQFRITYRLILREKELHFHIGVYNPSKELSFTFNMLLHTYLKVPDVRRCQITGLQGCHFIDKTRENALYQEGREVVTVNEWTDRIYQHTPQEHVITNVVSGRKMRLHKYNFPDTVIWNPWIDRSREMSDFGDDEFPNMLCVEAGNVTSPVILLPGTAFEASQILQQFKCPYTIDPSSCRKKNYLTNFLQYD
Protein: Triacylglycerol lipase 3 (EC 3.1.1.3) (Lipase 3) (P40308)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways. Also catalyzes the acylation of lysophosphatidic acid (LPA). Important for efficient sporulation, but rather through its acyltransferase than lipase activity.
Subcellular location: Lipid droplet {ECO:0000269|PubMed:10515935, ECO:0000269|PubMed:12682047, ECO:0000269|PubMed:21820081, ECO:0000269|PubMed:23673660, ECO:0000269|PubMed:24868093}. Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols. {ECO:0000269|PubMed:23673660}.
Interaction partners:
- Putative lipase ATG15
- Diacylglycerol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase
- Monoglyceride lipase
- Triacylglycerol lipase 2
- Lipid phosphate phosphatase 1
- Triacylglycerol lipase 4
- Phosphatidic acid phosphohydrolase 1
- Diacylglycerol pyrophosphate phosphatase 1
- Triacylglycerol lipase 5
Sequence:
MKETAQEYKVSAVIPTLLKNWILRVVYATLDHIPPFVWEILHVITDIYFFWVQKLINYVRPHSRVIYYNAIKKLDECDTYQMWCQQASVVDEITGANLWRRNFFSRRYDFNSVIEQYSILENMLREEKYDVVKEKFSTTGPCMLRNFAGIGDKKLFTKSLMGTKLLIEQYLTRILEGLDILNNQTLTPTSFFQRCKLSLGTTALILQGGSLFGLFHLGVIRGLLLQDLMPNIISGSSMGACVASLFGCLSNEQLKQLLTDDNLLNIIKNDVDLLKSCGYGNLEQHLNLGTLIQNLIHHGYSQDVYLFIRFVMKYIVKEKTFEEVYQITGKVFNIVIHPTDKSCPNLLNYVTTPNVLIKSAIECSLGSGVISEDTSLLCKNLENEIEPFLNINKNKQVKFLTPENANNPSITESPYTRLTELFNVNNFIVSLARPYLAPLVVNDLKHEIKTSKYYYYKHYPNMPPINANTVRKTQRSSSQSPIKAGTVEDLEPEPLMSPVPPSSAVNDSAEYIIPELGIPQLNFTEMEPLAFKFKYHLERKLKNIATMEFRHRMEVLDNLGLLCSLIKRLIIDEKTPRSATEIAVVPRMKSLSLTRIIEGQLNNIPYWIKSGERSTWPALALIKTRCAVEFKLDDIIRARRSR
Protein: Cyclic nucleotide-gated ion channel 1 (AtCNGC1) (Cyclic nucleotide- and calmodulin-regulated ion channel 1) (O65717)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as cyclic nucleotide-gated ion channel. Can be activated by cyclic AMP which leads to an opening of the cation channel. May be responsible for cAMP-induced calcium entry in cells and thus should be involved in the calcium signal transduction. Could transport K(+), Na(+) and Pb(2+).
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Two pore calcium channel protein 1
- Calmodulin-1
- Calmodulin-6
- Calmodulin-7
- Calmodulin-2
- Calmodulin-like protein 10
- Potassium transporter 5
- Calcium-binding protein CP1
Sequence:
MNFRQEKFVRFQDWKSDKTSSDVEYSGKNEIQTGIFQRTISSISDKFYRSFESSSARIKLFKRSYKSYSFKEAVSKGIGSTHKILDPQGPFLQRWNKIFVLACIIAVSLDPLFFYVPIIDDAKKCLGIDKKMEITASVLRSFTDVFYVLHIIFQFRTGFIAPSSRVFGRGVLVEDKREIAKRYLSSHFIIDILAVLPLPQMVILIIIPHMRGSSSLNTKNMLKFIVFFQYIPRFIRIYPLYKEVTRTSGILTETAWAGAAFNLFLYMLASHVFGAFWYLFSIERETVCWKQACERNNPPCISKLLYCDPETAGGNAFLNESCPIQTPNTTLFDFGIFLDALQSGVVESQDFPQKFFYCFWWGLQNLSSLGQNLKTSTYIWEICFAVFISIAGLVLFSFLIGNMQTYLQSTTTRLEEMRVKRRDAEQWMSHRLLPENLRKRIRRYEQYKWQETRGVDEENLLSNLPKDLRRDIKRHLCLALLMRVPMFEKMDEQLLDALCDRLQPVLYTEESYIVREGDPVDEMLFIMRGKLLTITTNGGRTGFLNSEYLGAGDFCGEELLTWALDPHSSSNLPISTRTVRALMEVEAFALKADDLKFVASQFRRLHSKQLRHTFRYYSQQWKTWAACFIQAAWRRYIKKKLEESLKEEENRLQDALAKEACGSSPSLGATIYASRFAANILRTIRRSGSVRKPRMPERMPPMLLQKPAEPDFNSDD
Protein: Mitochondrial inner membrane protease subunit 2 (EC 3.4.21.-) (IMP2-like protein) (Q96T52)
Organism: Homo sapiens (Human)
Function: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space. Known to process the nuclear encoded protein DIABLO.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:15814844}; Single-pass membrane protein {ECO:0000305|PubMed:15814844}.
Interaction partners:
- SLIT and NTRK-like protein 1
- Contactin-associated protein-like 2
- Diablo IAP-binding mitochondrial protein
- Mitochondrial inner membrane protease subunit 1
- KICSTOR complex protein ITFG2
- Histidine decarboxylase
Sequence:
MAQSQGWVKRYIKAFCKGFFVAVPVAVTFLDRVACVARVEGASMQPSLNPGGSQSSDVVLLNHWKVRNFEVHRGDIVSLVSPKNPEQKIIKRVIALEGDIVRTIGHKNRYVKVPRGHIWVEGDHHGHSFDSNSFGPVSLGLLHAHATHILWPPERWQKLESVLPPERLPVQREEE
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q0WPK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM4
- DNA replication licensing factor MCM7
- Serine/threonine-protein kinase ATR
- Minichromosome maintenance 10
- Probable DNA helicase MCM8
- DNA replication licensing factor MCM6
- Probable inactive protein kinase At3g63330
- Origin of replication complex subunit 5
Sequence:
MSENSEPRQLENSTAGRELIPLSPTNSDGNDDLNYHLHAFELSRLLLSSGHPESVIDLSSKCTYFQGSPNLVKYLCSIPNSPISLAEDGFTVTLSPESPSAPASFACSLDLQENVVLEQFMDPRSLTLKHSRENAEQEELELMPLPKRSRNDGNDVNYSVIDSRPNDIRTVACGTMLGTILALESQASVFNLSASNRGIEAFVQDHQPGPQTSNASVDVNPTHRLEESKNDLPSPQEDGYYERPEIGDFQIADNQILIEEGDDKNKKDLFPKGEIQTDSVQSDPVASLMPTENELEPVQIVDDTEDLLVDDHTVDIVSTPDRELPLKPSATEANQDKSLVQKTLDQCKLPGNSKTYSCSPEIKHTRKSKVIQKRKQNFNTVRLKDQKDQAKHNTIPDFDSYTIVEEEGSGGYGIVYKATRKTDGTEFAIKCPHVGAQKYYVNNEIRMLERFGGKNCIIKHEGCLKNGDSDCIILEHLEHDRPDSLKREIDVYQLQWYGYCMFKALSSLHKQGVVHRDVKPGNFLFSRKTNKGYLIDFNLAMDLHQKYRRADKSKAASGLPTASKKHHTLVKSLDAVNRGTNKPSQKTLAPNSIKKAAGKTRARNDMTRWERLNSQGAEGSGLTSAKDVTSTRNNPSGEKRREPLPCHGRKALLDFLQETMSVPIPNHEVSSKAPTSMRKRVAALPGKAEKELLYLTPMPLCSNGRPEAGDVIEKKDGPCSGTKGFRAPEVCFRSLHQGPKIDVWSAGVTLLYLIMGRTPFTGDPEQNIKDIAQLRGSEELWEVAKLHNRESSFPKELYESRYLKGMELRKWCELNTKRREFLDVIPLSLLDLVDKCLTVNPRRRISAEDALKHDFFHPVHETLRNQMLLKQQPTVVADAVSQTLNYLQL
Protein: Metaxin glutathione S-transferase domain-containing protein (Q38CI9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MPLMSADGSGELPPVMLHRYPVTLGLPTADPYALAIECMLRIVGAHYKKRDGGLPVTLEVPVDGRNKPAMKRHEGLTSCLQLIESATHQDAEVITSALEPEALCVRLTAEVVLIPAFVYITHSDAGILRNAIQKAVEPKVASMWQRFRGSYSRHVVQQTSFCRSYKNMGEAIENVERCLRAIEAICSINTAGNGMFILGTERPCSADALIYAAASSFFHADFASRQASGDIIAMQQRLREGCPTLLTYVERLRGLYFEDYSAFYHLRAPTCGMEGEATQKAAEETFVRGRWKVLAFTGVFSITYFLVANIDVFSAVLLHYLEDDGEEEFLEDEE
Protein: CDW11/WDR57 (WD repeat domain 57 (U5 snRNP specific), isoform CRA_a) (cDNA FLJ90035 fis, clone HEMBA1001878, highly similar to WD repeat protein 57) (A0MNP2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MIEQQKRKGPELPLVPVKRQRHELLLGAGSGPGAGQQQATPGALLQAGPPRCSSLQAPIMLLSGHEGEVYCCKFHPNGSTLASAGFDRLILLWNVYGDCDNYATLKGHSGAVMELHYNTDGSMLFSASTDKTVAVWDSETGERVKRLKGHTSFVNSCYPARRGPQLVCTGSDDGTVKLWDIRKKAAIQTFQNTYQVLAVTFNDTSDQIISGGIDNDIKVWDLRQNKLTYTMRGHADSVTGLSLSSEGSYLLSNAMDNTVRVWDVRPFAPKERCVKIFQGNVHNFEKNLLRCSWSPDGSKIAAGSADRFVYVWDTTSRRILYKLPGHAGSINEVAFHPDEPIIISASSDKRLYMGEIQ
Protein: Regulator of G-protein signaling rgs-2 (P49808)
Organism: Caenorhabditis elegans
Function: Weakly inhibits G protein signaling in nervous system, interacting preferentially with the G(O) subfamily member goa-1. In vitro, it acts as a GTPase activator of goa-1. Rgs-1 and rgs-2 redundantly adjust signaling when worms are fed to allow rapid induction of egg-laying behavior. Modulates chemotaxis responses by regulating negatively the sensitivity to quinine in ASH sensory neurons.
Interaction partners:
- Regulator of G-protein signaling rgs-11
- Guanine nucleotide-binding protein subunit alpha
- Guanine nucleotide-binding protein alpha-5 subunit
- Guanine nucleotide-binding protein subunit beta-2
- Guanine nucleotide-binding protein subunit beta-1
- Guanine nucleotide-binding protein alpha-16 subunit
Sequence:
MRLLTCDCTFMGQKHSGSVSVEKKNQENDGPPTYEIVFGWSQSFENLMKHRAGQKYFAEFLKGEYSDENILFWQACEELKREKNAEKIEEKARIIYEDFISILSPKEVSLDSRVREIVNTNMGRPSASTFDEAQNQIYTLMQRDSYPRFLASNIYKTVMGTFGIKEEAV
Protein: Zinc finger protein 625 (Q96I27)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MGERLLESKKDHQHGEILTQVPDDMLKKKTPRVKSCGEVSVGHASLNRHHRADTGHKPYEYQEYGQKPYKCTYCKKAFSDLPYFRTHEWAHTGGKPYDCEECGKSFISRSSIRRHRIMHSGDGPYKCNFCGKALMCLSLYLIHKRTHTGEKPYECKQCGKAFSHSGSLRIHERTHTGEKPYECSECGKAFHSSTCLHAHKITHTGEKPYECKQCGKAFVSFNSVRYHERTHTGEKPYECKQCGKAFRSASHLRTHGRTHTGEKPYECKQCGKAFGCASSVKIHERTHTGEKPCSSNTSKGQGEKIA
Protein: TGFB-induced factor homeobox 1 (A0A8I5ZTL5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MTLLLGSATLERGTGDLGPRTRAVQLEGVVAAASGSDSEDEDSMDSPLDLSSSAASGKRRRRGNLPKESVQILRDWLYEHRYNAYPSEQEKALLSQQTHLSTLQVCNWFINARRRLLPDMLRKDGKDPNQFTISRRGAKISEASSIEAAMGIKNFMPTLEESPFHSCVVGPNPTLGRPVSPKPPSPGPILARPSVICHTTVTALKDGPFSLCQAVSVGHSTDVQQVAPSNFTDASLRYPEDTCKSGPSPNPQSGLFNTPPPTPPDLNQDFSGFQLLVDVALKQAAEMELQAKLTA
Protein: Cytochrome b5 isoform B (AtCb5-B) (Cytochrome b5 isoform 2) (Cytochrome b5 isoform E) (AtCb5-E) (O48845)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Membrane bound hemoprotein which function as an electron carrier for several membrane bound oxygenases, including fatty acid desaturases.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22773744}; Single-pass membrane protein {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22773744}; Cytoplasmic side {ECO:0000269|PubMed:19054355, ECO:0000269|PubMed:22773744}.
Interaction partners:
- NADH--cytochrome b5 reductase 1
- NADH-cytochrome b5 reductase-like protein
- Dihydroceramide fatty acyl 2-hydroxylase FAH1
- Dihydroceramide fatty acyl 2-hydroxylase FAH2
- Bax inhibitor 1
- Very-long-chain aldehyde decarbonylase CER1
- Probable lysophospholipase BODYGUARD 1
- Very-long-chain aldehyde decarbonylase CER3
- Probable steroid-binding protein 3
- Ergosterol biosynthetic protein 28
Sequence:
MGDEAKIFTLSEVSEHNQAHDCWIVINGKVYNVTKFLEDHPGGDDVLLSSTGKDATDDFEDVGHSESAREMMEQYYVGEIDPTTIPKKVKYTPPKQPHYNQDKTSEFIIKLLQFLVPLAILGLAVGIRIYTKSG
Protein: Glucose-6-phosphate 1-dehydrogenase 6, cytoplasmic (AtG6PD6) (G6PDH6) (EC 1.1.1.49) (Q9FJI5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the rate-limiting step of the oxidative pentose-phosphate pathway, which represents a route for the dissimilation of carbohydrates besides glycolysis. The main function of this enzyme is to provide reducing power (NADPH) and pentose phosphates for fatty acid and nucleic acid synthesis which are involved in membrane synthesis and cell division.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:21309870}.
Interaction partners:
- Glucose-6-phosphate isomerase 1, chloroplastic
- Glucose-6-phosphate isomerase, cytosolic
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- 6-phosphogluconate dehydrogenase, decarboxylating 1, chloroplastic
- 6-phosphogluconate dehydrogenase, decarboxylating 3, chloroplastic
- Probable 6-phosphogluconolactonase 4
- Probable 6-phosphogluconolactonase 1
- 6-phosphogluconolactonase 3, chloroplastic
- Probable 6-phosphogluconolactonase 2
- Probable 6-phosphogluconolactonase 5
Sequence:
MGSGQWHVEKRSTFRNDSFVREYGIVPETGCLSIIVLGASGDLAKKKTFPALFNLYRQGFLNPDEVHIFGYARTKISDEELRDRIRGYLVDEKNAEQAEALSKFLQLIKYVSGPYDAEEGFQRLDKAISEHEISKNSTEGSSRRLFYLALPPSVYPSVCKMIKTCCMNKSDLGGWTRIVVEKPFGKDLESAEQLSSQIGELFDESQIYRIDHYLGKELVQNMLVLRFANRFFLPLWNRDNIENVQIVFREDFGTEGRGGYFDEYGIIRDIIQNHLLQVLCLVAMEKPISLKPEHIRDEKVKVLQSVVPISDDEVVLGQYEGYRDDDTVPNDSNTPTFATTILRIHNERWEGVPFILKAGKALNSRKAEIRIQFKDVPGDIFRCQKQGRNEFVIRLQPSEAMYMKLTVKQPGLDMNTVQSELDLSYGQRYQGVAIPEAYERLILDTIKGDQQHFVRRDELKVAWEIFTPLLHRIDKGEVKSIPYKPGSRGPKEADQLLEKAGYLQTHGYIWIPPTL
Protein: Hexosyltransferase (EC 2.4.1.-) (Q389B4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323, ECO:0000256|RuleBase:RU363063}.
Interaction partners:
Sequence:
MVGQILSRRGLILVCLTFVAILLIFSTRSKRIVREASQASFSAPPPLPEFDYTEKDRESLQYVPPDVVRAWRERNFLVMLGVLSPDNAVRRRRRHLQRLTCWQYQGVARRSNNFTGDLLVTFVLARHPDHNYTHSPQLVEEGLRWQDIIALPIKEGRVSTNKVIGQDGRYWGPDAEIGMSRKMYKWFSLMLRLLPNVNYVAKSDDDMFVHTPQYLADLRALPRRRLYWGNIVNARFMPLLFATGGLYTASREVIEQFLTYEPLKKLVDVPYSKEREDEFTSLYMQHEDLLMGRVLYEMGYQPLFVGEPMCRFHNLHGKGWVGPLSHSSLMIHNVKEEEYAQLREYFGEKKQYRPSRFKVRRGRLYATCGKR
Protein: Hypoxia inducible factor 3 subunit alpha (Hypoxia inducible factor 3, alpha subunit, isoform CRA_a) (H0YDZ5)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRPAAGAARRPRCCTSWLTRCPSPAASAPTWTRPLSCASPSATCACTASAPQLELIGHSIFDFIHPCDQEELQDALTPQQTLSRRKVEAPTERCFSLRMKSTLTSRGRTLNLKAATWKVLNCSGHMRAYKPPAQTSPAGSPDSEPPLQCLVLICEAIPHPGSLEPPLGRGAFLSRHSLDMKFTYCDDRIAEVAGYSPDDLIGCSAYEYIHALDSDAVSKSIHTLLSKGQAVTGQYRFLARSGGYLWTQTQATVVSGGRGPQSESIVCVHFLISQVEETGVVLSLEQTEQHSRRPIQRGAPSQKDTPNPGDSLDTPGPRILAFLHPPSLSEAALAADPRRFCSPDLRRLLGPILDGASVAATPSTPLATRHPQSPLSADLPDELPVGTENVHRLFTSGKDTEAVETDLDIAQDPSTPLLNLNEPLGFHFVTQSGVQWHKHSSPQPRPPGLK