wanglab/gogpt-training-data huggingface dataset:
Protein: Sodium-coupled monocarboxylate transporter 2 (Electroneutral sodium monocarboxylate cotransporter) (Low-affinity sodium-lactate cotransporter) (Solute carrier family 5 member 12) (Q49B93)
Organism: Mus musculus (Mouse)
Function: Acts as an electroneutral and low-affinity sodium (Na(+))-dependent sodium-coupled solute transporter. Catalyzes the transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, nicotinate, propionate, butyrate and beta-D-hydroxybutyrate. May be responsible for the first step of reabsorption of monocarboxylates from the lumen of the proximal tubule of the kidney and the small intestine. May play also a role in monocarboxylates transport in the retina. Mediates electroneutral uptake of lactate, with a stoichiometry of 2 Na(+) for each lactate.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:16873376, ECO:0000269|PubMed:17692818}; Multi-pass membrane protein {ECO:0000269|PubMed:16873376, ECO:0000269|PubMed:17692818}. Note=Detected at the brush border membrane of the kidney. Colocalizes with vimentin in Mueller cells. {ECO:0000269|PubMed:16873376, ECO:0000269|PubMed:17692818}.
Interaction partners:
Sequence:
MRVKNFEAWDYVVFAGLFVISSGIGVFFAIKERKKTTSREFLVGGRQMSFGPVALSLTASFMSAVTVLGTPAEVYRFGASFFLFLISYVFVVFFTSELFLPVFYRSGITSTYEYLQLRFNKPVRYAATIIYIVQTILYTGVVVYAPALALNQVTGFNLWASVFATGIVCTFYCSLGGLKAVVWTDAFQMVVMIVGFLTVLIQGSNHVGGFNNVLEKAGNGSRLHIVDFDVDPLRRHTFWTITIGGTFTWLGVYGVNQSTIQRCISCKTEKHAKLALYFNLLGLWIIVACAVFSGLIMYSHFKDCDPWTSGVISAPDQLMPYFVMEIFATMPGLPGLFVACAFSGTLSTVAASINALATVTFEDFVKSCFPHLSDKLSTWISKGLCILFGIMCTSMAVVASLMGSVVQAALSIHGMCGGPMLGLFTLGLVFPFVNWKGALGGLLTGITLSFWVAIGSFIYPAPESKTLPLPLSTEHCVELNITTTVAPQISSRPVLADTWYSLSYLYFSAVGCLGCIAAGIIISFLTGKQRGKDIDPLLIRPVCNLFCFWSKKYKTLCWCGVQHDRETEQDYLDSGSAWKQGVESGLQNGLKQDTLAQIPGYNPKEKSYSNSVPEKTTYF
Protein: 1-acyl-sn-glycerol-3-phosphate acyltransferase (EC 2.3.1.51) (Q5AEL8)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Lysophospholipid acyltransferase
- Lysophosphatidic acid acyltransferase
- Bifunctional glycerol-3-phosphate/glycerone-phosphate O-acyltransferase
- Phospholipid:diacylglycerol acyltransferase
- Phospholipase
- Phosphatidate cytidylyltransferase
- Bifunctional diacylglycerol diphosphate phosphatase/phosphatidate phosphatase
- Dpp1p
- Phosphatidic acid phosphatase type 2/haloperoxidase domain-containing protein
- Phosphatidate phosphatase
Sequence:
MSAVSSFFTKLKFYLKSGLYGTLVAGCAIYGVLASIILRIVNKAEYAQYAVAKACYYVVSLFLGLKINIKNEKYLQNLPAIVVANHQSALDIYVLGKVFQPGYTVTSKKSLKYVPFLGWFMALSGTFFLDRSKSASAKKVLDGALTGLKNQGKALFIFPEGTRSATEDLTMLPFKKGAFHLARQAGIPIIPVVVSNTSTIFNSKRKIFNTGEINIEVLPPVSTSDWETHEDVTNACNNIRDDMIKTLKKLGNSKIPGSKPREDFYPSESEDTSETDVEIINEQTPLKATAVSD
Protein: Histidinol-phosphate aminotransferase (EC 2.6.1.9) (Imidazole acetol-phosphate transaminase) (P07172)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Imidazoleglycerol-phosphate dehydratase
- Histidine biosynthesis trifunctional protein
- Prephenate dehydrogenase [NADP
- Imidazole glycerol phosphate synthase hisHF
- Tryptophan synthase
- ATP phosphoribosyltransferase
- Histidinol-phosphatase
- 1-
- Probable prephenate dehydratase
- Polynucleotide 3'-phosphatase
Sequence:
MVFDLKRIVRPKIYNLEPYRCARDDFTEGILLDANENAHGPTPVELSKTNLHRYPDPHQLEFKTAMTKYRNKTSSYANDPEVKPLTADNLCLGVGSDESIDAIIRACCVPGKEKILVLPPTYSMYSVCANINDIEVVQCPLTVSDGSFQMDTEAVLTILKNDSLIKLMFVTSPGNPTGAKIKTSLIEKVLQNWDNGLVVVDEAYVDFCGGSTAPLVTKYPNLVTLQTLSKSFGLAGIRLGMTYATAELARILNAMKAPYNISSLASEYALKAVQDSNLKKMEATSKIINEEKMRLLKELTALDYVDDQYVGGLDANFLLIRINGGDNVLAKKLYYQLATQSGVVVRFRGNELGCSGCLRITVGTHEENTHLIKYFKETLYKLANE
Protein: Deformed epidermal autoregulatory factor 1 homolog (Nuclear DEAF-1-related transcriptional regulator) (NUDR) (Q9Z1T5)
Organism: Mus musculus (Mouse)
Function: Transcription factor that binds to sequence with multiple copies of 5'-TTC[CG]G-3' present in its own promoter and that of the HNRPA2B1 gene. Down-regulates transcription of these genes. Binds to the retinoic acid response element (RARE) 5'-AGGGTTCACCGAAAGTTCA-3'. Activates the proenkephalin gene independently of promoter binding, probably through protein-protein interaction (By similarity). Regulates epithelial cell proliferation and side-branching in the mammary gland. Required for neural tube closure and skeletal patterning. Controls the expression of peripheral tissue antigens in pancreatic lymph nodes. Isoform 1 displays greater transcriptional activity than isoform 2. Isoform 2 may inhibit transcriptional activity of isoform 1 by interacting with it and retaining it in the cytoplasm. Transcriptional activator of EIF4G3 (By similarity). May also involved in behavior.
Subcellular location: [Isoform 1]: Nucleus. Cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus. Note=Displays some nuclear localization when expressed with isoform 1, suggesting that it may heterodimerize with isoform 1 and shuttle to the nucleus using the nuclear localization signal of isoform 1.
Interaction partners:
- Coiled-coil and C2 domain-containing protein 1A
Sequence:
MEDSDSAAKQLGLAEAAAVAAAAAVAAAAAAAAESEAEEPVLSRDEDSEEDADSEAERETRRVTAVAVMAAESGHMDMGTEALPSPDEAAAAAAAFAEVTTVTVANVGSSADNVFTTSVANAASISGHVLSGRTALQIGDSLNTEKATLIVVHTDGSIVETTGLKGPAAPLTPGPQSPPTPLAPGQEKGGTKYNWDPSVYDSELPVRCRNISGTLYKSRLGSGGRGRCIKQGENWYSPTEFEAMAGRASSKDWKRSIRYAGRPLQCLIQDGILNPHAASCTCAACCDDMTLSGPVRLFVPYKRRKKENELPTTPVKKDSPKNITLLPATAATTFTVTPSGQITTSGALTFDRASTVEATAVISESPAQGDVFAGATVQEAGVQPPCRVGHPEPHYPGYQDSCQIAPFPEAALPTSHPKIVLTSLPALAVPPSTPTKAVSPTVVSGLEMSEHRSWLYLEEMVNSLLNTAQQLKTLFEQAKQASSCREAAVTQARMQVDTERKEQSCVNCGREAMSECTGCHKVNYCSTFCQRKDWKDHQHVCGQSASVTVQADDVHVEESVIEKVAV
Protein: Cysteine protease XCP1 (EC 3.4.22.-) (Xylem cysteine peptidase 1) (AtXCP1) (O65493)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Cysteine protease involved in xylem tracheary element (TE) autolysis during xylogenesis in roots. Participates in micro autolysis within the intact central vacuole before mega autolysis is initiated by tonoplast implosion.
Subcellular location: Vacuole {ECO:0000269|PubMed:11788755}. Cell membrane {ECO:0000269|PubMed:11788755}. Note=Predominantly vacuolar. May be associated to plasma membrane.
Interaction partners:
- NAC domain-containing protein 30
- UPF0235 protein At5g63440
- Protein TRACHEARY ELEMENT DIFFERENTIATION-RELATED 6
- Cellulose synthase A catalytic subunit 7
- Metacaspase-9
- Cellulose synthase A catalytic subunit 4
- Cellulose synthase A catalytic subunit 8
- Transcription factor MYB46
- Transcription factor MYB83
- NAC domain-containing protein 37
Sequence:
MAFSAPSLSKFSLLVAISASALLCCAFARDFSIVGYTPEHLTNTDKLLELFESWMSEHSKAYKSVEEKVHRFEVFRENLMHIDQRNNEINSYWLGLNEFADLTHEEFKGRYLGLAKPQFSRKRQPSANFRYRDITDLPKSVDWRKKGAVAPVKDQGQCGSCWAFSTVAAVEGINQITTGNLSSLSEQELIDCDTTFNSGCNGGLMDYAFQYIISTGGLHKEDDYPYLMEEGICQEQKEDVERVTISGYEDVPENDDESLVKALAHQPVSVAIEASGRDFQFYKGGVFNGKCGTDLDHGVAAVGYGSSKGSDYVIVKNSWGPRWGEKGFIRMKRNTGKPEGLCGINKMASYPTKTK
Protein: Small proline-rich protein 2B (O70554)
Organism: Mus musculus (Mouse)
Function: Cross-linked envelope protein of keratinocytes. It is a keratinocyte protein that first appears in the cell cytosol, but ultimately becomes cross-linked to membrane proteins by transglutaminase. All that results in the formation of an insoluble envelope beneath the plasma membrane (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MSYYQQQCKQPCQPPPVCPPPKCPEPCPPPKCPEPCPPPVCCEPCPPPKCPEPCPPPVCCEPCPPPVCCEPCPPQPWQPKCPPVQFPPCQQKCPPKNK
Protein: Claudin (Q93198)
Organism: Caenorhabditis elegans
Interaction partners:
- Chondroitin proteoglycan 3
- Lens fiber membrane intrinsic protein
- Serpentine Receptor, class H
- Probable trafficking protein particle complex subunit 2
Sequence:
MCLSGLTQILYGLIMAGSAILTAVALFTPSWNTVENNVKDITHINTSEWNGLMPWSCIGHSQGTQCQDWWANLPGWMKCVVVCMILSLIVQIFAVVYNFLTCLACCCKKYIIHPLTLFAVISTILLLIAVIVYAAEWNQFTNGINTNSQLGYSFWLAVGALILSAADVILGALTVCLGEHCC
Protein: Myelin expression factor 2 (Q32PS6)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MADTEQVADLTEIKDEETGDSPADECEQEPEQNQDDTNGDKTDTEDKSESKEKNSGGRKSHRYHPYKERSGGADKKTTHRNRVFISNIPYDKKWQAIKDLMREKVGEVTYVELFKDGEGKSRGCGVVEFKDEEFVKKAIEVMSKHDLNGRPLNIKEDPDGEHARRVLQRSGRMYGGGRGQDSSGINIPPSIANNPNIPHEIISALQAGRLGATIFVANLDFKVGWKKLKEVFGMAGTVRRADVKEDKDGKSRGMGTVTFEQPLEAVQAISMFNGQMLFDRQMHVKMDDKSLPPDDFRPVEKSPQLPRGLGGIGMGLGPGGQPINANCLSGSSMGPGGMDGGCSNMNRMSGMGGGMGGGFSGMDCMAGMGGFSGRDMSMGRMGDMYRSGMGGMDRDFGRNDLGMSRSFGDSFSSLGGGFGGMGNSGMGPMGSGLGMGNMGMDRMNSGFDRMSSSMDMSRGFGQFGGSGYMGGMSDRSKGGCQIFVRNLSYDLSWQKLKEKFSHCGQVMYAEIKMENGKSKGCGTVRFDSPESAEKACRLMNGTKINGREVDVRLDRNA
Protein: Methyltransferase 22, Kin17 lysine (H3BTF5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVQLAPAAAMDEVTFRSDTVLSDVHLYTPNHRHLMVRLNSVGQPVFLSQFKLLWSQDSWTDSGAKGGSHRDVHTKEPPSAETGSTGSPPGSGHAQEEDDVLGEEAQGSPHDIIRIEHTMATPLEDVGKQVWRGALLLADYILFRQDLFRGCTALELGAGTGLASIIAATMARTVYCTDVGADLLSMCQRNIALNSHLAATGGGIVRVKELDWLKDDLCTDPKVPFSWSQEEISDLYDHTTILFAAEVFYDDDLTDAVFKTLSRLAHRLKNACTAILSVEKRLNFTLRHLDVTCEAYDHFRSCLHALEQLADGKLRFVVEPVEASFPQLLVYERLQQLELWKIIAEPVT
Protein: Solute carrier family 22 member 21 (Organic cation/carnitine transporter 3) (Solute carrier family 22 member 9) (Q9WTN6)
Organism: Mus musculus (Mouse)
Function: Sodium-ion independent, medium affinity carnitine transporter. Also transports organic cations such as tetraethylammonium (TEA) without the involvement of sodium. Relative uptake activity ratio of carnitine to TEA is 746.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:11010964, ECO:0000269|PubMed:12535646, ECO:0000269|PubMed:16288981}; Multi-pass membrane protein {ECO:0000269|PubMed:11010964, ECO:0000269|PubMed:12535646, ECO:0000269|PubMed:16288981}.
Interaction partners:
Sequence:
MLDYDEVTAFLGEWGTFQRLIFFLLSASIIPNGFTGLSAVFLTAIPEHRCRIPDTVNLSSAWRNHSIPMETKDGPEVPQKCRRYRLATIANFSELGLEPGRDVDLEQLEQENCLDGWEYDKDIFLSTIVTEWDLVCKDDWKAPLTTSFFYVGVLLGSFISGQLSDRFGRKNILFLTMAMHTGFSFIQVFSVNFEMFTLLYTLVGMGHISNYVAAFVLGTEMLSKSVRIIFATLGVCIFFAFGFMVLPLFAYFIREWRRLLLAITLPGVLCGALWWFIPESPRWLISQGRIKEAEVIIRKAAKINGIVAPSTIFDPSETNKLQDDSSKKPQSHHIYDLVRTPNIRILTIMSIILWLTISVGYFGLSLDTPNLNGNIYVNCFLLAAVEVPAYVLAWLLLQHVSRRYSMAGSLFLGGSVLLLVQLVPSDLHYLSTTLVMVGKFGITSAYSMVYVYTAELYPTVVRNMGVGVSSTASRLGSILSPYFVYLGAYDRRLPYILMGSLTILTAIITLFFPESSGVSLPETIDEMQKVKKLKQRQSLSKKGSPKESKGNVSRTSRTSEPKGF
Protein: DNA-directed RNA polymerase (EC 2.7.7.6) (Q8IIB0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- rRNA adenine N
- rRNA adenine N
- DNA-directed RNA polymerase subunit beta
- High mobility group protein B1
Sequence:
MFVCKKCSRYVIKKIFYTFICESKYQLLFLRKGNDYKNIFFLEKGYISTHVRGDKKERTQKKKNDLDIKRLFLDKPSTPNIKDEYEKKTNDNNNMEEYNICNNNIITNNNKIKNSSHMNTFNSNRKKVCVKDNINNNTINNNYEEQKENKEEYINTPKAKNNLYNLPYKNKDTHIIDKKKLDEQVVKELHNLIISIKKIDKDKKENIIKYINTLNKKYVKNINKNIIVFFENLDIYMSVNGLLICDIGGEEIFNYINKIKLTNNIDIKKETYNDDIEKHNVNTNERFLHMDDVTKEDNININNMFDINYIKEKKKRIYGDNIYPIVVKSEEKEEVVPKKKKKNSNNIIVHNNNIINNKCGDYNIINCTNDLGEKTKNHQTNYSNNPKFDYQYNEEKEKEEEKESNIINVRRQMLIERSSYKKAIEEAEEFVSNLHDLKKITEIQGLCKIYLNWISELEKRIILYKEKNKNKKKKKIFPDFIDDKLLATITVKWTIQYTFNPLKKKYSNNVSTQSKYFEHEYSYQSLFTHIAIKIGEEINNELNFQLLEKKNHLYNYMKKNKNNSSFSHFQKYRIIKQMKQQIGKGNHMKQHAMLGGDNQTSHLNSCANNNFDINSCANNNFDINSCANNNFGINSCGNNNFGINSCGNNNFGINSCDEYYGHTNNHVHIKHDDDNIIEWNSVKKATIGGLLLNMLIENAKMDVDINVAKNEFKNEYKYYLFLHKTAKNNAEDLYEECKYKKELNYQKFYEEESNTLKFIILDKYKKNNSYDNNFKKNYMEKKICTYNYGTHDKNVVKQNNGDKQNNGDKQNNGDKQNNGDKQNNGDKHNCANRQELQLSDNKKESNFCQKQREKLMRKEIILYRSKRDRNKIELPVFIHSYVWKNNNWYGVIHMRECCANYLLNNAINSHIPLNYLPMICKPKRWENFEGGMLLLKNSFIRCNIKPLFNLNVCNLNRIKNIVSEIGNVGWKINKEILHYIEYAYIHGITIGKIPLYKNYTLPKYINLKEQNNEEIKKYLLLKEEINRLNKCLISERPTFLQKLAVAKTFKDNDIIYFPHNIDFRGRMYPLSPHLHHMSDDICRSLITFAEQKEIGNKGLFWLKIHLANTFGKDKLSFQKRIQWVDQNINNIKKLTQQPFDNIEFWNMAEKPWQALAVAIDLKNALESPNASKYKSSIPIQQDGTCNGLQHYAALGKDKYGGKAVNIIPSDEPQDIYSVVLDIVISKIKNDLMNISNGHHNNIISFSINENIKTNKKYNNNINNNINNYNNNNHNRNSNSNVNKNELASYCFKFDLLKRKVVKQTIMTICYGVTSIGAKNQVKGKIQTMIGKELDKNIINKLSQYIANYIFESISEIFKRAMIIKKWFNNLSKVTNELNIPITWISPIGLPCEQPYRLGNRILVNTPLQSISVISYKNSQLHKNKQRLGFPPNFVHSLDASHLMMTAEKMVIQNNFSFAAVHDSYWAHACNVDIMNQFIRESFITLYNEPILENIYNNFRIRLGKFATKIPSSPEQGELDISMVKDSLYFFS
Protein: COP9 signalosome complex subunit 2 (CSN complex subunit 2) (SGN2) (Q9HFR0)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the COP9 signalosome (CSN) complex that acts as an regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunit of SCF-type E3 ubiquitin-protein ligase complexes (By similarity). Required, indirectly, for activation of ribonucleotide reductase through the degradation of the protein spd1, thereby supplying deoxyribonucleotides for DNA replication and repair.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11854407}. Nucleus {ECO:0000269|PubMed:11854407}.
Interaction partners:
- COP9 signalosome complex subunit 1
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 3
- COP9 signalosome complex subunit 7
- Endoplasmic reticulum chaperone BiP
- DNA damage-binding protein 1
- Eukaryotic translation initiation factor 3 subunit H
- Tryptophan synthase
- Cullin-4
Sequence:
MSNDFMLEDDENYDFEFEDDDDDMIEPYVDVENCYYNSKSLKEENPESALTSFYSIVEKCEGEQNEWAFKALKQITKINFQLKKYDDMLQSYQRLLGYTNWLSITKNYSEKSIYNIVEYASSCENTEFLEKFYDVTTKALQNLNNERLMLKVLMHVARFLLTQKNYHKFKYLLRQMHELLSDENNSVADQNRGTHLLELYSLEIQMYSDIEDNKRLKELYQSSLRVKTAIPHPRIMGIIRECGGKMHMQENQWSEAQTNFFESFKSYDEAGSSDRIRVLKYLVLANMLSESEINPFDSPETQPYKDNPHIIAMTKLVEAYQIRDITAVERILQTYQHDILDDDFIRQYVDKILYSIRSQVLIELVKPYTSVKLSLLAKKLGVSISIIEQALVGLIIDERVNGKIDMVNEVFTISQPKNTIHNQLVEDVQKLWNTATK
Protein: Treacle protein (Treacher Collins syndrome protein) (Q13428)
Organism: Homo sapiens (Human)
Function: Nucleolar protein that acts as a regulator of RNA polymerase I by connecting RNA polymerase I with enzymes responsible for ribosomal processing and modification. Required for neural crest specification: following monoubiquitination by the BCR(KBTBD8) complex, associates with NOLC1 and acts as a platform to connect RNA polymerase I with enzymes responsible for ribosomal processing and modification, leading to remodel the translational program of differentiating cells in favor of neural crest specification.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12777385}.
Interaction partners:
- Nucleolar protein 56
- DNA-directed RNA polymerases I and III subunit RPAC2
- Nucleolar transcription factor 1
- Nucleolar and coiled-body phosphoprotein 1
- Centriole and centriolar satellite protein OFD1
- Kelch repeat and BTB domain-containing protein 8
- DNA-directed RNA polymerase I subunit RPA1
- Ligand of Numb protein X 2
- Muskelin
- Nibrin
Sequence:
MAEARKRRELLPLIYHHLLRAGYVRAAREVKEQSGQKCFLAQPVTLLDIYTHWQQTSELGRKRKAEEDAALQAKKTRVSDPISTSESSEEEEEAEAETAKATPRLASTNSSVLGADLPSSMKEKAKAETEKAGKTGNSMPHPATGKTVANLLSGKSPRKSAEPSANTTLVSETEEEGSVPAFGAAAKPGMVSAGQADSSSEDTSSSSDETDVEGKPSVKPAQVKASSVSTKESPARKAAPAPGKVGDVTPQVKGGALPPAKRAKKPEEESESSEEGSESEEEAPAGTRSQVKASEKILQVRAASAPAKGTPGKGATPAPPGKAGAVASQTKAGKPEEDSESSSEESSDSEEETPAAKALLQAKASGKTSQVGAASAPAKESPRKGAAPAPPGKTGPAVAKAQAGKREEDSQSSSEESDSEEEAPAQAKPSGKAPQVRAASAPAKESPRKGAAPAPPRKTGPAAAQVQVGKQEEDSRSSSEESDSDREALAAMNAAQVKPLGKSPQVKPASTMGMGPLGKGAGPVPPGKVGPATPSAQVGKWEEDSESSSEESSDSSDGEVPTAVAPAQEKSLGNILQAKPTSSPAKGPPQKAGPVAVQVKAEKPMDNSESSEESSDSADSEEAPAAMTAAQAKPALKIPQTKACPKKTNTTASAKVAPVRVGTQAPRKAGTATSPAGSSPAVAGGTQRPAEDSSSSEESDSEEEKTGLAVTVGQAKSVGKGLQVKAASVPVKGSLGQGTAPVLPGKTGPTVTQVKAEKQEDSESSEEESDSEEAAASPAQVKTSVKKTQAKANPAAARAPSAKGTISAPGKVVTAAAQAKQRSPSKVKPPVRNPQNSTVLARGPASVPSVGKAVATAAQAQTGPEEDSGSSEEESDSEEEAETLAQVKPSGKTHQIRAALAPAKESPRKGAAPTPPGKTGPSAAQAGKQDDSGSSSEESDSDGEAPAAVTSAQVIKPPLIFVDPNRSPAGPAATPAQAQAASTPRKARASESTARSSSSESEDEDVIPATQCLTPGIRTNVVTMPTAHPRIAPKASMAGASSSKESSRISDGKKQEGPATQVSKKNPASLPLTQAALKVLAQKASEAQPPVARTQPSSGVDSAVGTLPATSPQSTSVQAKGTNKLRKPKLPEVQQATKAPESSDDSEDSSDSSSGSEEDGEGPQGAKSAHTLGPTPSRTETLVEETAAESSEDDVVAPSQSLLSGYMTPGLTPANSQASKATPKLDSSPSVSSTLAAKDDPDGKQEAKPQQAAGMLSPKTGGKEAASGTTPQKSRKPKKGAGNPQASTLALQSNITQCLLGQPWPLNEAQVQASVVKVLTELLEQERKKVVDTTKESSRKGWESRKRKLSGDQPAARTPRSKKKKKLGAGEGGEASVSPEKTSTTSKGKAKRDKASGDVKEKKGKGSLGSQGAKDEPEEELQKGMGTVEGGDQSNPKSKKEKKKSDKRKKDKEKKEKKKKAKKASTKDSESPSQKKKKKKKKTAEQTV
Protein: RPE-retinal G protein-coupled receptor (P47804)
Organism: Homo sapiens (Human)
Function: Receptor for all-trans- and 11-cis-retinal. Binds preferentially to the former and may catalyze the isomerization of the chromophore by a retinochrome-like mechanism.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Retinol dehydrogenase 10
- Retinol dehydrogenase 5
- Guanine nucleotide-binding protein G
- Retinaldehyde-binding protein 1
Sequence:
MAETSALPTGFGELEVLAVGMVLLVEALSGLSLNTLTIFSFCKTPELRTPCHLLVLSLALADSGISLNALVAATSSLLRRWPYGSDGCQAHGFQGFVTALASICSSAAIAWGRYHHYCTRSQLAWNSAVSLVLFVWLSSAFWAALPLLGWGHYDYEPLGTCCTLDYSKGDRNFTSFLFTMSFFNFAMPLFITITSYSLMEQKLGKSGHLQVNTTLPARTLLLGWGPYAILYLYAVIADVTSISPKLQMVPALIAKMVPTINAINYALGNEMVCRGIWQCLSPQKREKDRTK
Protein: Two-component response regulator ARR6 (Q9ZWS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as response regulator involved in His-to-Asp phosphorelay signal transduction system. Phosphorylation of the Asp residue in the receiver domain activates the ability of the protein to promote the transcription of target genes. Type-A response regulators seem to act as negative regulators of the cytokinin signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:11574878}.
Interaction partners:
- Histidine kinase 4
- Histidine kinase 3
- Histidine kinase 2
- Histidine-containing phosphotransfer protein 5
- Histidine-containing phosphotransfer protein 3
- Two-component response regulator ARR22
- Ethylene-responsive transcription factor CRF5
- Adenylate isopentenyltransferase 7, mitochondrial
- Putative two-component response regulator ARR20
- Adenylate isopentenyltransferase 8, chloroplastic
Sequence:
MAEVMLPRKMEILNHSSKFGSPDPLHVLAVDDSHVDRKFIERLLRVSSCKVTVVDSATRALQYLGLDVEEKSVGFEDLKVNLIMTDYSMPGMTGYELLKKIKESSAFREVPVVIMSSENILPRIDRCLEEGAEDFLLKPVKLSDVKRLRDSLMKVEDLSFTKSIQKRELETENVYPVHSQLKRAKI
Protein: 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase (SEPHCHC synthase) (EC 2.2.1.9) (Menaquinone biosynthesis protein MenD) (P9WK11)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the thiamine diphosphate-dependent decarboxylation of 2-oxoglutarate and the subsequent addition of the resulting succinic semialdehyde-thiamine pyrophosphate anion to isochorismate to yield 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC).
Interaction partners:
- o-succinylbenzoate synthase
- Putative isochorismate synthase MenF
- 1,4-dihydroxy-2-naphthoyl-CoA synthase
- Demethylmenaquinone methyltransferase
- GDP-mannose-dependent alpha-mannosyltransferase
- Probable conserved transmembrane protein
- Putative non-heme bromoperoxidase BpoC
- 1,4-dihydroxy-2-naphthoate octaprenyltransferase
- Probable 2-succinylbenzoate--CoA ligase
Sequence:
MNPSTTQARVVVDELIRGGVRDVVLCPGSRNAPLAFALQDADRSGRIRLHVRIDERTAGYLAIGLAIGAGAPVCVAMTSGTAVANLGPAVVEANYARVPLIVLSANRPYELLGTGANQTMEQLGYFGTQVRASISLGLAEDAPERTSALNATWRSATCRVLAAATGARTANAGPVHFDIPLREPLVPDPEPLGAVTPPGRPAGKPWTYTPPVTFDQPLDIDLSVDTVVISGHGAGVHPNLAALPTVAEPTAPRSGDNPLHPLALPLLRPQQVIMLGRPTLHRPVSVLLADAEVPVFALTTGPRWPDVSGNSQATGTRAVTTGAPRPAWLDRCAAMNRHAIAAVREQLAAHPLTTGLHVAAAVSHALRPGDQLVLGASNPVRDVALAGLDTRGIRVRSNRGVAGIDGTVSTAIGAALAYEGAHERTGSPDSPPRTIALIGDLTFVHDSSGLLIGPTEPIPRSLTIVVSNDNGGGIFELLEQGDPRFSDVSSRIFGTPHDVDVGALCRAYHVESRQIEVDELGPTLDQPGAGMRVLEVKADRSSLRQLHAAIKAAL
Protein: Putative NAD(P)H nitroreductase Rv3131 (P9WIZ7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Stimulates pro-inflammatory cytokine expression via TLR2 signaling pathway. Activation of TLR2 results in the phosphorylation and activation of NF-kappa-B. Also induces TLR2 expression. May influence the innate immune responses to facilitate the survival of M.tuberculosis in the granulomatous microenvironment.
Interaction partners:
- Probable diacyglycerol O-acyltransferase tgs1
- Universal stress protein Rv3134c
- Ferredoxin
- Uncharacterized protein Rv1738
- Uncharacterized protein Rv2030c
- Alpha-crystallin
- Universal stress protein Rv1996
- Uncharacterized protein Rv0080
- Uncharacterized protein Rv3127
- Dormancy associated translation inhibitor
Sequence:
MTAAVDGKGPAAMNTHFPDAETVRTVLTLAVRAPSIHNTQPWRWRVCPTSLELFSRPDMQLRSTDPDGRELILSCGVALHHCVVALASLGWQAKVNRFPDPKDRCHLATIGVQPLVPDQADVALAAAIPRRRTDRRAYSCWPVPGGDIALMAARAARGGVMLRQVSALDRMKAIVAQAVLDHVTDEEYLRELTIWSGRYGSVAGVPARNEPPSDPSAPIPGRLFAGPGLSQPSDVLPADDGAAILALGTETDDRLARLRAGEAASIVLLTATAMGLACCPITEPLEIAKTRDAVRAEVFGAGGYPQMLLRVGWAPINADPLPPTPRRELSQVVEWPEELLRQRC
Protein: ATP-dependent DNA helicase ku70 (EC 3.6.4.12) (Q54MA9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in non-homologous end joining (NHEJ) DNA double strand break repair.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- DNA 3'-5' helicase
- X-ray repair cross-complementing protein 5
- DNA ligase 4
- DNA-dependent protein kinase catalytic subunit
- BRCT domain-containing protein
- Double-strand break repair protein
- Exonuclease 1
- DNA ligase 3
- Telomerase reverse transcriptase
- DNA cross-link repair 1 protein
Sequence:
MSGTNSWLNNNNNNSNTTLTNTNTIGGTNFGINQFDGDDWDNIFDGNNGDGDGDLDGDSYKSYQNPYSYRDCIIFLIDASKAMFEPNENNEIPFHNAVKCLIQTITDKIITSDSDLIGVCFYNTNKKKNINDFENIYVLSDLDIPDPKIILTLEEMLENSNFTTNGLGNCQGEMPFCDALWTCSTMFSNIKQSGSSSGENSNNNNFKRIFLFTNEDNPNAYNDSIRNSSIQRSKDLSDLNIQIELFSMNKSVNDKFDFSLFYQHILIFADEENYLDPTQFDASSKFSDLRFKLKRKEFKKRSLGKLPLYIGNLNNNNNNSNSLDSQVIISTQLYNLFSHAHKSSPTLLDPKTNLPVKQLIKNVCANTQATLLPSQIKLCYHYGGEPVIFTKDEMQTIKSIDRIGFTLLGFKPLENIKPYHSIKHSQFIFPDDQSIKGSVLAFNALVEQMLKSGKAAICRFTPRSSSSPRMVALIPQEEILQSESEFNNQQLLNSLSSQQQQQQSSQQSSSSQQQQQQQQQQQQQQQQQQQQQLPSSSQQSNNNRKIQIRPRGMHVIYLPFADDIRYPNNIGVKSDGLEIKQENIDKAKNIIKMMKIKFDEKKFVNPGLQKHYASLQAIALERDKVEETVDNIQPDRKLIEKVIDTTQDFSDGIFPVGYASTVSSATSSTSSSSAKRLRDGKDLSTMDWPDMVKSGEIIKLTVDDLKSFLSNQNIKPSSKAKKADLIDLISNLISGGNFKPDKLHLLKKDSPPLSDNTITTNGGDDDDNNRPSKKVKSTSTSTTASKNTSSSSPPLVSAATMNKKAPPKKSFSVKDKNSSNNSSGGSSKANVNDEFDIDFKNSDQDDDTDNESDVNNKATTSTTTITTTTAAPKKNNFVNNGMFDTRELCKYGKNCYRTNKQHLDEYRHQ
Protein: ATP synthase F(0) complex subunit j, mitochondrial (6.8 kDa mitochondrial proteolipid protein) (MLQ) (ATP synthase membrane subunit 6.8PL) (ATP synthase subunit ATP5MPL, mitochondrial) (P56379)
Organism: Mus musculus (Mouse)
Function: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Minor subunit required to maintain the ATP synthase population in the mitochondria.
Subcellular location: Mitochondrion membrane {ECO:0000250|UniProtKB:P56378}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATP synthase peripheral stalk subunit d, mitochondrial
- ATP synthase peripheral stalk subunit b, mitochondrial
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase F
- ATP synthase peripheral stalk subunit OSCP, mitochondrial
- ATP synthase F
Sequence:
MFQTLIQKVWVPMKPYYTQVYQEIWVGVGLMSLIVYKIRSADKRSKALKGPAPAHGHH