wanglab/gogpt-training-data huggingface dataset:
Protein: Ubiquitin carboxyl-terminal hydrolase 11 (EC 3.4.19.12) (Deubiquitinating enzyme 11) (Ubiquitin thioesterase 11) (Ubiquitin-specific-processing protease 11) (P51784)
Organism: Homo sapiens (Human)
Function: Protease that can remove conjugated ubiquitin from target proteins and polyubiquitin chains. Inhibits the degradation of target proteins by the proteasome. Cleaves preferentially 'Lys-6' and 'Lys-63'-linked ubiquitin chains. Has lower activity with 'Lys-11' and 'Lys-33'-linked ubiquitin chains, and extremely low activity with 'Lys-27', 'Lys-29' and 'Lys-48'-linked ubiquitin chains (in vitro). Plays a role in the regulation of pathways leading to NF-kappa-B activation. Plays a role in the regulation of DNA repair after double-stranded DNA breaks. Acts as a chromatin regulator via its association with the Polycomb group (PcG) multiprotein PRC1-like complex; may act by deubiquitinating components of the PRC1-like complex. Promotes cell proliferation by deubiquitinating phosphorylated E2F1.
Subcellular location: Nucleus {ECO:0000269|PubMed:12084015, ECO:0000269|PubMed:15314155, ECO:0000269|PubMed:20233726, ECO:0000269|PubMed:28992046}. Cytoplasm {ECO:0000269|PubMed:15314155, ECO:0000269|PubMed:28992046}. Chromosome {ECO:0000269|PubMed:20233726, ECO:0000269|PubMed:20601937}. Note=Predominantly nuclear (PubMed:12084015, PubMed:15314155). Associates with chromatin (PubMed:20233726, PubMed:20601937). {ECO:0000269|PubMed:12084015, ECO:0000269|PubMed:15314155, ECO:0000269|PubMed:20233726, ECO:0000269|PubMed:20601937}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 7
- Breast cancer type 2 susceptibility protein
- NF-kappa-B inhibitor alpha
- Cellular tumor antigen p53
- Zinc finger-containing ubiquitin peptidase 1
- Ubiquitin carboxyl-terminal hydrolase 4
- Eukaryotic translation initiation factor 4B
- Transcription elongation factor A protein-like 1
- Telomerase Cajal body protein 1
- TP53-binding protein 1
Sequence:
MAVAPRLFGGLCFRFRDQNPEVAVEGRLPISHSCVGCRRERTAMATVAANPAAAAAAVAAAAAVTEDREPQHEELPGLDSQWRQIENGESGRERPLRAGESWFLVEKHWYKQWEAYVQGGDQDSSTFPGCINNATLFQDEINWRLKEGLVEGEDYVLLPAAAWHYLVSWYGLEHGQPPIERKVIELPNIQKVEVYPVELLLVRHNDLGKSHTVQFSHTDSIGLVLRTARERFLVEPQEDTRLWAKNSEGSLDRLYDTHITVLDAALETGQLIIMETRKKDGTWPSAQLHVMNNNMSEEDEDFKGQPGICGLTNLGNTCFMNSALQCLSNVPQLTEYFLNNCYLEELNFRNPLGMKGEIAEAYADLVKQAWSGHHRSIVPHVFKNKVGHFASQFLGYQQHDSQELLSFLLDGLHEDLNRVKKKEYVELCDAAGRPDQEVAQEAWQNHKRRNDSVIVDTFHGLFKSTLVCPDCGNVSVTFDPFCYLSVPLPISHKRVLEVFFIPMDPRRKPEQHRLVVPKKGKISDLCVALSKHTGISPERMMVADVFSHRFYKLYQLEEPLSSILDRDDIFVYEVSGRIEAIEGSREDIVVPVYLRERTPARDYNNSYYGLMLFGHPLLVSVPRDRFTWEGLYNVLMYRLSRYVTKPNSDDEDDGDEKEDDEEDKDDVPGPSTGGSLRDPEPEQAGPSSGVTNRCPFLLDNCLGTSQWPPRRRRKQLFTLQTVNSNGTSDRTTSPEEVHAQPYIAIDWEPEMKKRYYDEVEAEGYVKHDCVGYVMKKAPVRLQECIELFTTVETLEKENPWYCPSCKQHQLATKKLDLWMLPEILIIHLKRFSYTKFSREKLDTLVEFPIRDLDFSEFVIQPQNESNPELYKYDLIAVSNHYGGMRDGHYTTFACNKDSGQWHYFDDNSVSPVNENQIESKAAYVLFYQRQDVARRLLSPAGSSGAPASPACSSPPSSEFMDVN
Protein: GEO07442p1 (Programmed cell death 5) (Programmed cell death gene-5 protein) (RE17056p) (Q9VUZ8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein uL14
- Small ribosomal subunit protein uS17
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL29
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS4
- FI01658p
- Probable small nuclear ribonucleoprotein E
- 40S ribosomal protein S24
- Small ribosomal subunit protein eS6
Sequence:
MSDSDLDALRAQRMSQMQSQFGGGNDAEKQQAQQEQMRAQEEMKHSILSQVLDQQARARLNTLKVSKPEKAQMFENMVIRMAQMGQVRGKLDDAQFVSILESVNAQMPQSKSSVKYDRRRAAIDSDDDEDYGC
Protein: Mesencephalic astrocyte-derived neurotrophic factor (Arginine-rich protein) (Protein ARMET) (Q9CXI5)
Organism: Mus musculus (Mouse)
Function: Selectively promotes the survival of dopaminergic neurons of the ventral mid-brain. Modulates GABAergic transmission to the dopaminergic neurons of the substantia nigra. Enhances spontaneous, as well as evoked, GABAergic inhibitory postsynaptic currents in dopaminergic neurons. Inhibits cell proliferation and endoplasmic reticulum (ER) stress-induced cell death. Retained in the ER/sarcoplasmic reticulum (SR) through association with the endoplasmic reticulum chaperone protein HSPA5 under normal conditions. Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia. Following secretion by the ER/SR, directly binds to 3-O-sulfogalactosylceramide, a lipid sulfatide in the outer cell membrane of target cells. Sulfatide binding promotes its cellular uptake by endocytosis, and is required for its role in alleviating ER stress and cell toxicity under hypoxic and ER stress conditions.
Subcellular location: Secreted {ECO:0000269|PubMed:17507765, ECO:0000269|PubMed:23956175}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:23956175}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P55145}. Note=Retained in the endoplasmic reticulum (ER), and sarcoplasmic reticulum (SR) under normal conditions. Up-regulated and secreted by the ER/SR in response to ER stress and hypoxia. {ECO:0000250|UniProtKB:P55145}.
Interaction partners:
- Endoplasmic reticulum chaperone BiP
- Protein disulfide isomerase Creld2
- DnaJ homolog subfamily B member 11
- Stromal cell-derived factor 2-like protein 1
- X-box-binding protein 1
- Ubiquitin-conjugating enzyme E2 N
- Endoplasmin
- Protein disulfide-isomerase A4
- Proactivator polypeptide-like 1
- Protein disulfide-isomerase A6
Sequence:
MWATRGLAVALALSVLPDSRALRPGDCEVCISYLGRFYQDLKDRDVTFSPATIEEELIKFCREARGKENRLCYYIGATDDAATKIINEVSKPLAHHIPVEKICEKLKKKDSQICELKYDKQIDLSTVDLKKLRVKELKKILDDWGEMCKGCAEKSDYIRKINELMPKYAPKAASARTDL
Protein: Candida glabrata strain CBS138 chromosome E complete sequence (Q6FVL9)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- L21
- Small ribosomal subunit protein eS6
- Large ribosomal subunit protein uL23
- RP41
- Candida glabrata strain CBS138 chromosome M complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
- YL17
- L17A
- 60S ribosomal protein L13
- L2
Sequence:
MSNPFDLLGNDVEDPQAAIPLATKEVVKKSTSSKKADVPPPSADPAKARKNKGKLSGNEGAIRDKKAGRDNNRARDVGSSATARRNNDRKMTDRHSRTGKTDSQKKINQAWGDNDRELTVEEQAKRDAESELAEDAEAPETQPAGPQKMSLADYMNQVDNNDLNKVPEARKVEETLQAEAKSDVPDYAPATKTKAVKSKQLKTKEFLQFDATFSDNNRDNRDSNRRGGFRGNSRGGRGGNRGGNRGGKSNSSRGGKNTAEVNKKIDTSSLPSLI
Protein: Diphthine--ammonia ligase (EC 6.3.1.14) (ATP-binding domain-containing protein 4) (Diphthamide synthase) (Diphthamide synthetase) (Protein DPH6 homolog) (Q7L8W6)
Organism: Homo sapiens (Human)
Function: Amidase that may catalyze the last step of diphthamide biosynthesis using ammonium and ATP. Diphthamide biosynthesis consists in the conversion of an L-histidine residue in the translation elongation factor (EEF2) to diphthamide (By similarity).
Interaction partners:
- Diphthine methyl ester synthase
- Elongation factor 2
- Diphthine methyltransferase
- 2-
- Diphthamide biosynthesis protein 3
- 2-
- DnaJ homolog subfamily C member 24
Sequence:
MRVAALISGGKDSCYNMMQCIAAGHQIVALANLRPAENQVGSDELDSYMYQTVGHHAIDLYAEAMALPLYRRTIRGRSLDTRQVYTKCEGDEVEDLYELLKLVKEKEEVEGISVGAILSDYQRIRVENVCKRLNLQPLAYLWQRNQEDLLREMISSNIQAMIIKVAALGLDPDKHLGKTLDQMEPYLIELSKKYGVHVCGEGGEYETFTLDCPLFKKKIIVDSSEVVIHSADAFAPVAYLRFLELHLEDKVSSVPDNYRTSNYIYNF
Protein: Serine/threonine-protein kinase CDG1 (EC 2.7.11.1) (Protein CONSTITUTIVE DIFFERENTIAL GROWTH 1) (Q9LSE1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein kinase involved in the positive regulation of brassinosteroid (BR) signaling and plant growth. Mediates BR signal transduction from BRI1 receptor kinase to BSU1 phosphatase. After activation by phosphorylation at Ser-234 by BRI1, CDG1 phosphorylates BSU1 at 'Ser-764' in the phosphatase domain, increasing the ability of BSU1 to inactivate the negative regulator of BR signaling ASK7/BIN2 by dephosphorylation at 'Tyr-200'. The full kinase activity of CDG1 is required for its biological function.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21855796}; Lipid-anchor {ECO:0000303|PubMed:21855796}. Note=Plasma membrane localization is required for CDG1 to function in BR signaling. {ECO:0000269|PubMed:21855796}.
Interaction partners:
Sequence:
MVSCLCFRPSRKTKLKDKSHKRSIRNQTSSSSAQPAGTAKEVDSSSSQTVVQDSSRYRCQIFSYRELAIATNSFRNESLIGRGGFGTVYKGRLSTGQNIAVKMLDQSGIQGDKEFLVEVLMLSLLHHRNLVHLFGYCAEGDQRLVVYEYMPLGSVEDHLYDLSEGQEALDWKTRMKIALGAAKGLAFLHNEAQPPVIYRDLKTSNILLDHDYKPKLSDFGLAKFGPSDDMSHVSTRVMGTHGYCAPEYANTGKLTLKSDIYSFGVVLLELISGRKALMPSSECVGNQSRYLVHWARPLFLNGRIRQIVDPRLARKGGFSNILLYRGIEVAFLCLAEEANARPSISQVVECLKYIIDHTIRKERRTRRRLLGGNKDGAGTSRSPDETMMRMLEEEEEYVTSEEAIERRRVIVDDARTWAGMNRRGATPPTPTP
Protein: Serine acetyltransferase (SAT) (EC 2.3.1.30) (Q06750)
Organism: Bacillus subtilis (strain 168)
Function: Catalyzes the acetylation of serine by acetyl-CoA to produce O-acetylserine (OAS).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Cysteine synthase
- Cysteine--tRNA ligase
- Probable cysteine synthase
- O-acetylserine dependent cystathionine beta-synthase
- Cystathionine gamma-lyase
- Mini-ribonuclease 3
- Uncharacterized protein YacP
- Probable L-serine dehydratase, beta chain
- Probable L-serine dehydratase, alpha chain
- Putative TrmH family tRNA/rRNA methyltransferase YacO
Sequence:
MFFRMLKEDIDTVFDQDPAARSYFEVILTYSGLHAIWAHRIAHALYKRKFYFLARLISQVSRFFTGIEIHPGATIGRRFFIDHGMGVVIGETCEIGNNVTVFQGVTLGGTGKEKGKRHPTIKDDALIATGAKVLGSITVGEGSKIGAGSVVLHDVPDFSTVVGIPGRVVVQNGKKVRRDLNHQDLPDPVADRFKSLEQQILELKAELEDRKERINQK
Protein: Protein UL96 (F5H8R6)
Organism: Human cytomegalovirus (strain Merlin) (HHV-5) (Human herpesvirus 5)
Subcellular location: Virion {ECO:0000250}.
Interaction partners:
Sequence:
MTSVNKQLLKDVMRVDLERQQHQFLRRTYGPQHRLTTQQALTVMRVAAREQTRYSQRTTQCVAAHLLEQRAAVQQELQRARQLQSGNVDDALDSLTELKDTVDDVRATLVDSVSATCDLDLEVDDAV
Protein: NAD(P)-binding Rossmann-fold superfamily protein (Oxidoreductase, putative) (Q9C8D3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSDTKTVRFGLLGCIRFASKFVRTVTESSNAVIIAISDPSLETAKTFATGNNLSPETVTIYGSYEELLNDANVDAVYLTMPVTQRARWAVTAAEKKKHVLVEKPPAQDATELEKIVEACEYNGVQFMDGTIWLHHQRTVKIRDTMFDSGLLGDVRHMYSTMTTPVPEQVLERLTKEAMGLAGAIGELGWYPIGAALWAMSYQMPISVRALPSSVSTNSVGTILSCTASLQFGSTATTTAIVHCSFLSQLSTDLAISGSKGSIQMNDYVIPYKEDKAWFEYTSGAKFVDMHIGWNVTPERVTVDCSGTPETQEAMMLREFTRLVEGIKRGDLEADRRWPDISKKTQLIVDAVKKSVDIGCEVVHL
Protein: ABC-type glycine betaine transport system substrate-binding domain-containing protein (Q9HTH6)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Probable permease of ABC transporter
- Probable ATP-binding component of ABC transporter
- Quaternary amine transport ATP-binding protein
- Probable permease of ABC transporter
- HTH-type transcriptional regulator CdhR
- 3-dehydrocarnitine:acetyl-CoA trimethylamine transferase
- Betainyl-CoA thioesterase
- Probable lipolytic enzyme
- L-carnitine dehydrogenase
- 3-oxoadipate CoA-transferase
Sequence:
MKTTIRQLGCALLILASGAALAAEPEQCRTVRLGTVNWTDVVASSAVAEALLDGLGYQVKQTSASQQIVLAGLADKQLDLFLGYWQPTMQPVARPYLDKGRIEVIEPPTLADAQSTYAVPSYVAEGGLKTFADIARFKDKLGGRIYAIEPGSGSNRITRKMIDDNRFGLKGFQLVESSEAGMLTAVKRAIKRKQWVVFFGWKPHPMNLQIDMTYLTGSEDVFGPDEGAATVSTMTAAGYQAQCGNVARLLHNLRFSSAQVSQVMAPILDRTQPLDAARQWLKANPEPLKAWLDGVSTFDGKDGLAALQASLK
Protein: Glycoprotein 24A (gp24A) (Contact site B protein A) (P16642)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Cell-cell adhesion during early development.
Subcellular location: Cell surface.
Interaction partners:
Sequence:
MVDLKITLVNEDGESTISGKGHPLPAPLIFPPIYIFRFTQYQTEGKLWDKNEFQIKSGKIEFDGEEYDIPESKGTWSKDDEENAIDVNLHLFRPPEKFFPKN
Protein: Large ribosomal subunit protein uL5 (60S ribosomal protein L11) (Q9CXW4)
Organism: Mus musculus (Mouse)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel. As part of the 5S RNP/5S ribonucleoprotein particle it is an essential component of the LSU, required for its formation and the maturation of rRNAs. It also couples ribosome biogenesis to p53/TP53 activation. As part of the 5S RNP it accumulates in the nucleoplasm and inhibits MDM2, when ribosome biogenesis is perturbed, mediating the stabilization and the activation of TP53. Promotes nucleolar location of PML.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:15195100, ECO:0000269|PubMed:21804542}. Cytoplasm {ECO:0000269|PubMed:21804542, ECO:0000269|PubMed:36517592}.
Interaction partners:
- Large ribosomal subunit protein bL12m
- Large ribosomal subunit protein uL22
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein uS10
- Large ribosomal subunit protein uL24
- Elongation factor 2
- Small ribosomal subunit protein uS7
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein eS10
Sequence:
MAQDQGEKENPMRELRIRKLCLNICVGESGDRLTRAAKVLEQLTGQTPVFSKARYTVRSFGIRRNEKIAVHCTVRGAKAEEILEKGLKVREYELRKNNFSDTGNFGFGIQEHIDLGIKYDPSIGIYGLDFYVVLGRPGFSIADKKRRTGCIGAKHRISKEEAMRWFQQKYDGIILPGK
Protein: MKIAA0629 protein (Q6ZQ80)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
NTVARFAADLAEELVFEGIMEVCQFSCPQTPASSQCQSFDFEDKVVKSYAKDLSESVIQEAFIELSQTNVTFTTKAAVNVSMGNVKYVSAESVSPTQTFTFSSSFSGQAVMMTKPMQEHKKEYTVQQALFCTSGIVTSIPVPLAGSALLPYHMSSTLYPSKCLSSEPSKASGGSTQEHIAIERSAEEVDCLRSTCLPSELNPCNQNDFKPTNGDIDRQSPSKLMSGPVIISNFSAAMVHTIVNETLESMTSFKATKTIDTNADYLTKTIKGKACSPSLCDQAAPQENKASSKDMFAEQLSKSIIKHSLDKSKSMLPNRDKKPGSKEHVLVLGEESQMTLGETPKFLDFSDNSPHRSLLVGNYCVAECKDSVGFGFSLEALPPCSMMTNQKSDLKEVVKDKEVTRHNLNNTALEPMPFGQESSFRHSQTFSSAVLTCVDGLHEEDKQKIRDRNVIPDTPPSTPLVPSQTSSEWDIKTLSKQLKGELAKEFAPATPPSTPHNSSVGSLSENEQTTIEKEEFMLKLMRSLSEEVESSEGEEHPGMHVKAEHPGKKVQFAEAFATHIISLATEAAASHLDHETTQEFKVQNPHLNVPSQRNVLPALSHSDESIQTCTFASDMAADVIAEAEKIANARSCMLFRHERNICHVEGGRGKAEEKLDVEDVAHPREVDTCVLSLPSGMPGLTYKYPSCESVTDEYAGHVIQVLQQQGGSGELIMEQYASRLAYRSVTAAAREAAKTVKMKCGSKLFPLHGCHGKTNKELLVFSSKERHQEVDRQRKRNGSHLCKYQTCERTQDPCRNELSELYSFSASLASSITRDAKKQLTAPKVDLPKSSTDGCFFEKSECVDSSENVTGPERSKSCQPLQSHGFCQNTGYLSGYSCAENAQAIEQYARKVVGDTLELSLGPTVFHNSETTASADRITYAEKLSPLINEACRYCDLKEFHGCTRNSAQLFSKQSPCASAKPSSRSKLSSIRQKSRIFHLDVPQIHVNLDKRAVLAEKIVAEAIEKAERMCVCVCACVRG
Protein: Oxysterol-binding protein-related protein 7 (ORP-7) (OSBP-related protein 7) (Q9BZF2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:14593528}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:14593528}. Cell membrane {ECO:0000269|PubMed:14593528}.
Interaction partners:
- Vesicle-associated membrane protein-associated protein A
Sequence:
MDFQERDPPFLPESAQSSKPSSAQQASELWEVVEEPRVRLGTEGVMPERQEGHLLKKRKWPLKGWHKRYFVLEDGILHYATTRQDITKGKLHGSIDVRLSVMSINKKAQRIDLDTEDNIYHLKIKSQDLFQSWVAQLRAHRLAHRLDMPRGSLPSTAHRKVPGAQLPTAATASALPGLGPREKVSSWLRDSDGLDRCSHELSECQGKLQELHRLLQSLESLHRIPSAPVIPTHQASVTTERPKKGKRTSRMWCTQSFAKDDTIGRVGRLHGSVPNLSRYLESRDSSGTRGLPPTDYAHLQRSFWALAQKVHSSLSSVLAALTMERDQLRDMHQGSELSRMGVSEASTGQRRLHSLSTSSDTTADSFSSLNPEEQEALYMKGRELTPQLSQTSILSLADSHTEFFDACEVLLSASSSENEGSEEEESCTSEITTSLSEEMLDLRGAERCQKGGCVPGRPMGPPRRRCLPAASGPGADVSLWNILRNNIGKDLSKVSMPVQLNEPLNTLQRLCEELEYSSLLDQASRIADPCERMVYIAAFAVSAYSSTYHRAGCKPFNPVLGETYECERPDRGFRFISEQVSHHPPISACHAESENFAFWQDMKWKNKFWGKSLEIVPVGTVNVSLPRFGDHFEWNKVTSCIHNVLSGQRWIEHYGEVLIRNTQDSSCHCKITFCKAKYWSSNVHEVQGAVLSRSGRVLHRLFGKWHEGLYRGPTPGGQCIWKPNSMPPDHERNFGFTQFALELNELTAELKRSLPSTDTRLRPDQRYLEEGNIQAAEAQKRRIEQLQRDRRKVMEENNIVHQARFFRRQTDSSGKEWWVTNNTYWRLRAEPGYGNMDGAVLW
Protein: Plasmalemma vesicle-associated protein (Plasmalemma vesicle protein 1) (PV-1) (gp68) (Q9WV78)
Organism: Rattus norvegicus (Rat)
Function: Endothelial cell-specific membrane protein involved in the formation of the diaphragms that bridge endothelial fenestrae. It is also required for the formation of stomata of caveolae and transendothelial channels. Functions in microvascular permeability, endothelial fenestrae contributing to the passage of water and solutes and regulating transcellular versus paracellular flow in different organs. Plays a specific role in embryonic development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10366592, ECO:0000269|PubMed:10557298}; Single-pass type II membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000269|PubMed:10366592, ECO:0000269|PubMed:10557298}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:15640522}. Note=Membrane-associated protein of caveolae (PubMed:10366592). Found in fenestral and stomatal diaphragms in fenestrated endothelia and transendothelial channels (PubMed:10557298). Also colocalized with CAV1 in perinuclear region (PubMed:15640522). {ECO:0000269|PubMed:10366592, ECO:0000269|PubMed:10557298, ECO:0000269|PubMed:15640522}.
Interaction partners:
Sequence:
MGLSMDRSPYSRTGDRDRGCWYYLRYFFLFVSLIQFLIILGLVLFMIYGNVHATTESSLRATEIRADNLYSQVVGLSAAQANLSKQLNISTLVKDTVMQQLLTTRREVERINASFRQCQGDLITYINYNRFIAAIILSEKQCQEQLKEGNKTCEALLFKLGEKVKTLEMEVVKEKAVCSKDKDSLLAGKRQAEMQQEACGKAREQQKQDQQVTEEQLRKVQSLCLPLDQEKFQADVLNVWRDSLVYRSLDNIGYHYSLMPEFSSLRRTCESLPGIMTTKVEELARGLRAGIERVTRENGELRRQKLELERAIQGEREARTRAGTEAQARETQLRTECARQTQLALEEKAALRTQRDDLERQLEARKRELEQLRTEVDVRISALDTCVKAKSLPAIQPRLPGPPPNPPPIDPASLEEFKKRILESQRPPLVNPAVPPSG
Protein: Guanine/hypoxanthine permease GhxQ (Q46817)
Organism: Escherichia coli (strain K12)
Function: High-affinity transporter for guanine and hypoxanthine.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24214977}; Multi-pass membrane protein {ECO:0000269|PubMed:24214977}.
Interaction partners:
- Xanthine permease XanQ
- Uric acid transporter UacT
- Putative purine permease YbbY
- Putative pyrimidine permease RutG
- Xanthine permease XanP
- Uracil permease
- Guanine deaminase
Sequence:
MSGDILQTPDAPKPQGALDNYFKITARGSTVRQEVLAGLTTFLAMVYSVIVVPGMLGKAGFPPAAVFVATCLVAGFGSLLMGLWANLPMAIGCAISLTAFTAFSLVLGQQISVPVALGAVFLMGVIFTAISVTGVRTWILRNLPMGIAHGTGIGIGLFLLLIAANGVGMVIKNPIEGLPVALGAFTSFPVMMSLLGLAVIFGLEKCRVPGGILLVIIAISIIGLIFDPAVKYHGLVAMPSLTGEDGKSLIFSLDIMGALQPTVLPSVLALVMTAVFDATGTIRAVAGQANLLDKDNQIINGGKALTSDSVSSIFSGLVGAAPAAVYIESAAGTAAGGKTGLTATVVGALFLLILFLSPLSFLIPGYATAPALMYVGLLMLSNVSKLDFNDFIDAMAGLVCAVFIVLTCNIVTGIMLGFVTLVVGRVFAREWQKLNIGTVIITAALVAFYAGGWAI
Protein: UDP-glucose:glycoprotein glucosyltransferase (EC 2.4.1.-) (EMS-mutagenized BRI1 suppressor 1) (Protein PRIORITY IN SWEET LIFE 2) (Q0WL80)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Required for elongation factor Tu receptor (EFR), but not flagellin-sensing 2 (FLS2) signaling.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000305}.
Interaction partners:
- Calnexin homolog 2
- Calnexin homolog 1
- Calreticulin-3
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Calreticulin-2
- Calreticulin-1
- Protein IMPAIRED IN BABA-INDUCED STERILITY 1
- Protein OS-9 homolog
- Probable glucan 1,3-alpha-glucosidase
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
Sequence:
MGTTTNLRSWLYLILLFIVVVGVNAQNRRPKNVQVAVKAKWQGTPLLLEAGELISKESKQLFWEFTDAWLGSDGDDSDCKSARDCLLKISKQASTLLAQPVASLFHFSLTLRSASPRLVLYRQLADESLSSFPHGDDPSATGCCWVDTGSSLFYDVADLQSWLASAPAVGDAVQGPELFDFDHVHFDSRAGSPVAVLYGAVGTDCFRKFHLSLAKAAKEGKVTYVVRPVLPLGCEGKTRPCGAIGARDNVSLAGYGVELALKNMEYKAMDDSAIKKGITLEDPRTEDLSQDVRGFIFSKILDRKPELRSEVMAFRDYLLSSTVSDTLDVWELKDLGHQTAQRIVHASDPLQSMQEINQNFPSVVSSLSRMKLNESIKDEILSNQRMVPPGKALLALNGALLNIEDIDLYMLMDLAHQELSLANHFSKLKIPDGAIRKLLLTTPLPEPDSYRVDFRSVHVTYLNNLEEDDMYKRWRSNINEILMPAFPGQLRYIRKNLFHAVYVIDPATACGLESIETLRSLYENQLPVRFGVILYSTQLIKTIENNGGQIPSSDAVTNAQVKEDLSTMVIRLFLYIKEHHGIQTAFQFLGNLNTLRTESADSSEADIEQEHVDGAFVETILPKVKTLPQDILLKLRQEHTLKEASEASSMFVFKLGLAKLKCSFLMNGLVFDSVEEETLLNAMNEELPKIQEQVYYGQIESHTKVLDKLLSESGLSRYNPQIISGGKNKPRFVSLASSTRKGESMLNDVNYLHSPETSEDVKYVTHLLAADVATKKGMKLLHEGVRYLIGGSKSARLGVLFSSSQNADPHSLLFIKFFEKTASSFSHKEKVLYFLDKLCLFYEREYLLKTSVESASSQMFIDKVLELADEYGLSSKAYRSCLVESVDEELLKRLTKVAQFLSWELGLESDANAIISNGRVIFPVDERTFLGQDLHLLESMEFNQRVKPVQEIIEGIEWQDVDPDLLTSKYFSDVFMFVSSAMATRDRSSESARFEVLNSEYSAVLLGNENATIHIDAVIDPLSPTGQKLASLLQVLQKHVQTSMRIVLNPMSSLVDIPLKNYYRYVLPNTDDYSSTGFDVDGPKAFFANMPLSKTLTMNLDVPEPWLVEPVIAIHDLDNILLENLGDTTTLQAVFEVESLVLTGHCAEKDHEAPRGLQLILGTKNRPHLVDTLVMANLGYWQMKVSPGVWYLQLAPGRSSELYALKGGNDGSQDQSSLKRITIDDLRGKVVHLEVVKRKGKEHEKLLVPSDGDDAVQQNKEGSWNSNFLKWASGFVGGRQQSMKGGPDKEHEKGGRQGKTINIFSIASGHLYERFLKIMILSVLKNTNRPVKFWFIKNYLSPQFKDVIPHMAQEYNFEYELITYKWPSWLHKQKEKQRIIWAYKILFLDVIFPLSLEKVIFVDADQIIRTDMGELYDMDIKGRPLAYTPFCDNNREMDGYKFWKQGFWKEHLRGRPYHISALYVVDLVKFRETAAGDNLRVFYETLSKDPNSLSNLDQDLPNYAQHTVPIFSLPQEWLWCESWCGNATKAKARTIDLCNNPMTKEPKLQGARRIVTEWPDLDLEARKFTAKILGEDVELNEPVAAPATDKPNPLPSNDISEDTEQDLESKAEL
Protein: Leucine--tRNA ligase, cytoplasmic (EC 6.1.1.4) (Leucyl-tRNA synthetase) (LeuRS) (cLRS) (Q9P2J5)
Organism: Homo sapiens (Human)
Function: Catalyzes the specific attachment of an amino acid to its cognate tRNA in a two step reaction: the amino acid (AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA. Exhibits a post-transfer editing activity to hydrolyze mischarged tRNAs.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Arginine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Lysine--tRNA ligase
- Glutamine--tRNA ligase
- Methionine--tRNA ligase, cytoplasmic
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Eukaryotic translation elongation factor 1 epsilon-1
- Aspartate--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, mitochondrial
Sequence:
MAERKGTAKVDFLKKIEKEIQQKWDTERVFEVNASNLEKQTSKGKYFVTFPYPYMNGRLHLGHTFSLSKCEFAVGYQRLKGKCCLFPFGLHCTGMPIKACADKLKREIELYGCPPDFPDEEEEEEETSVKTEDIIIKDKAKGKKSKAAAKAGSSKYQWGIMKSLGLSDEEIVKFSEAEHWLDYFPPLAIQDLKRMGLKVDWRRSFITTDVNPYYDSFVRWQFLTLRERNKIKFGKRYTIYSPKDGQPCMDHDRQTGEGVGPQEYTLLKLKVLEPYPSKLSGLKGKNIFLVAATLRPETMFGQTNCWVRPDMKYIGFETVNGDIFICTQKAARNMSYQGFTKDNGVVPVVKELMGEEILGASLSAPLTSYKVIYVLPMLTIKEDKGTGVVTSVPSDSPDDIAALRDLKKKQALRAKYGIRDDMVLPFEPVPVIEIPGFGNLSAVTICDELKIQSQNDREKLAEAKEKIYLKGFYEGIMLVDGFKGQKVQDVKKTIQKKMIDAGDALIYMEPEKQVMSRSSDECVVALCDQWYLDYGEENWKKQTSQCLKNLETFCEETRRNFEATLGWLQEHACSRTYGLGTHLPWDEQWLIESLSDSTIYMAFYTVAHLLQGGNLHGQAESPLGIRPQQMTKEVWDYVFFKEAPFPKTQIAKEKLDQLKQEFEFWYPVDLRVSGKDLVPNHLSYYLYNHVAMWPEQSDKWPTAVRANGHLLLNSEKMSKSTGNFLTLTQAIDKFSADGMRLALADAGDTVEDANFVEAMADAGILRLYTWVEWVKEMVANWDSLRSGPASTFNDRVFASELNAGIIKTDQNYEKMMFKEALKTGFFEFQAAKDKYRELAVEGMHRELVFRFIEVQTLLLAPFCPHLCEHIWTLLGKPDSIMNASWPVAGPVNEVLIHSSQYLMEVTHDLRLRLKNYMMPAKGKKTDKQPLQKPSHCTIYVAKNYPPWQHTTLSVLRKHFEANNGKLPDNKVIASELGSMPELKKYMKKVMPFVAMIKENLEKMGPRILDLQLEFDEKAVLMENIVYLTNSLELEHIEVKFASEAEDKIREDCCPGKPLNVFRIEPGVSVSLVNPQPSNGHFSTKIEIRQGDNCDSIIRRLMKMNRGIKDLSKVKLMRFDDPLLGPRRVPVLGKEYTEKTPISEHAVFNVDLMSKKIHLTENGIRVDIGDTIIYLVH