lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates. Plays a role in sustaining courtship behavior in males, possibly through the reception of a stimulating arrestant pheromone.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MKRNAFEELRVQLRTLKWLGVLRFTIDFNKCLVRENASEERSAWLYLIGVVGITCSLIVYSTYFPSHFIMGKHNTTGNCYALINIRSCSIVTMLIYTQLYIQRFRFVALLQSILRFNQISGSHREEGRFAFYYYTHLSLLIICMLNYAYGYWTAGVRLTTIPIYLLQYGFSYLFLGQVVVLFACIQQILLSILKYYNQVVLKNIKSSKESREFYYNFCKYNQVIWLSYTEINHCFGLLLLLVTGLILLITPSGPFYLVSTIFEGRFRQNWQFSLMSFTAILWSLPWIVLLVLAMGRNDVQKEANKTAKMLTKVPRTGTGLDRMIEKFLLKNLRQKPILTAYGFFALDKSTLFKLFTAIFTYMVILVQFKEMENSTKSINKF
The following text describes a protein:
Function:
Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Sequence:
MLNREHFDTLNYSSFAGLLQFAEPSPLHTTTIVEKCTLKLVDEFNHMLCQATEPLSSFLEYIRYGHMIDNVVLIVTGTLHERDVQELLEKCHPLGMFDSIASLAVAQNMRELYRLVLVDTPLAPYFSECITSEGPSILSLIACSFEDDSYLIRFCAFQVELDLDDMNIEIMRNTLYKAYLEDFYRFCQKLGGATAEIMSDLLAFEADRRAVNITINSIGTELTRDDRRKLYSNFGLLYPYGHEELAICEDIDQVRGVMEKYPPYQSIFAKLAYGESQMLDKAFYEEEVKRLCLAFEQQFHYGVFFAYVRLREQEIRNLMWISECVSQNQKSRVHDSVVLIFW
The following text describes a protein:
Function:
Component of the origin recognition complex (ORC) that binds origins of replication. It has a role in both chromosomal replication and mating type transcriptional silencing. Binds to the ARS consensus sequence (ACS) of origins of replication.
Subcellular Localization:
Nucleus.
Sequence:
MSDLNQSKKMNVSEFADAQRSHYTVYPSLPQSNKNDKHIPFVKLLSGKESEVNVEKRWELYHQLHSHFHDQVDHIIDNIEADLKAEISDLLYSETTQKRRCFNTIFLLGSDSTTKIELKDESSRYNVLIELTPKESPNVRMMLRRSMYKLYSAADAEEHPTIKYEDINDEDGDFTEQNNDVSYDLSLVENFKRLFGKDLAMVFNFKDVDSINFNTLDNFIILLKSAFKYDHVKISLIFNINTNLSNIEKNLRQSTIRLLKRNYHKLDVSSNKGFKYGNQIFQSFLDTVDGKLNLSDRFVEFILSKMANNTNHNLQLLTKMLDYSLMSYFFQNAFSVFIDPVNVDFLNDDYLKILSRCPTFMFFVEGLIKQHAPADEILSLLTNKNRGLEEFFVEFLVRENPINGHAKFVARFLEEELNITNFNLIELYHNLLIGKLDSYLDRWSACKEYKDRLHFEPIDTIFQELFTLDNRSGLLTQSIFPSYKSNIEDNLLSWEQVLPSLDKENYDTLSGDLDKIMAPVLGQLFKLYREANMTINIYDFYIAFRETLPKEEILNFIRKDPSNTKLLELAETPDAFDKVALILFMQAIFAFENMGLIKFQSTKSYDLVEKCVWRGI
The following text describes a protein:
Function:
Acts as a negative regulator of abscisic acid (ABA) response.
Subcellular Localization:
Nucleus.
Sequence:
MERFYGEKEQHSKEIDLTLKLSTCGENLEEKRLIRSSSMAGEMENWCSFVPSLERSCSLPIDSGKIMLLERQRSVADSELHGPRHSAEVVVDSKFQISTKRENVSMIFKKPIGKEIPLPPKSADTKHENRAKKTTLPDYCSLKGDVMEILRQMPTVTTTGDGPNGKRIEGFLYKYRSGEVCIVCVCHGSFLTPKEFVMHAGGKEVANPMKHITVYPVSF
The following text describes a protein:
Function:
After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane.
Subcellular Localization:
Postsynaptic cell membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MMVQSIQIVLPVALFFLIVFNGFTVEGSKKEAQLYRDLLTNYSYLVRPVRNPKKALTVTMKVFIQQVLLVDAKHQMIEVNAWLKYIWTDFRLRWNPLDYENITSVRFQGEDQIWQPDILLYNRYIEDEQESFDITYKTNAVAYSDGVINWIPPGIFKLSCKMDITLFPFDEQICFMKFGSWTYHGFALDLRLDVVKGQEPSADLSTYITNGEWHLLSAPARREEKFYKCCKEPYPTVKFYLHLRRRTFYYVFNVVLPTLLVSFMSLLAFCLPATDLSEKIGLQTTILLSVCFFLTILSEMTPTTSEAVPLLGVFFSALTFIVAMSTTFTILVLNIRYRQITNHYLSPMFRSIFLECLPWLMMMKRPDHKFRRGSSYRDSSADQCVQCAKNAELKSILRGTDNQQQIETNTFYPFPTETLSLNRKVGDGLFIQRRCQIHEEARSEKFTHGMLACEKSLRENGSELANILVTILKMYEVMVSQVERIRKRIALKRKRKDIQDEWKFAAQAVDRFCLIIFTIVFIICCFIFVAIPPIKILD
The following text describes a protein:
Function:
Component of the SET1 complex that specifically di- and trimethylates 'Lys-4' of histone H3 and of the MLL3/4 complex which also methylates histone H3 'Lys-4'.
Subcellular Localization:
Nucleus.
Sequence:
MNLELLESFGQNYPEEFDGSLDCISLAVTCAFNKYGTLLAVGCNDGRIVIWDFLTRGIAKIISAHVHPVCSLSWTRNGHKLLSASTDNNVCIWDVLTGELEHKYRFPSPVLKVQFDPRNDNRLLVCPMRYAAVLVEVGGTHRCLPLDSDGDLNIVASFDRRGKHIYTGNAKGKILVLDVETFEVVASFRIIVGTSSATAVKSIEFARRGDAFLINTSDRVIRVYDSKEIITLGKDGEPEPIQKLQDLVNKTTWKKCCFSGDGEYICAGSARQHALYIWEKSIGNLVKILHGTKGELLLDVVWHPVRPIIASISSGLVSIWAQNQVENWSAFAPDFKELDENVEYEERESEFDIADEDKSVDLNADAQQDEEIEVDVQKVEPVAAFCSSDEEGEDENALQFLPMAPEVEDPEDGWTGQDGLEPSAVMLGHMEPHDYEDDIMASKRRRMQLYDVSLPDAPTDETHPLISSKASKDKQQPVGGKKAAGRTKK
The following text describes a protein:
Function:
Atypical Ras-like protein that acts as a potent regulator of NF-kappa-B activity by preventing the degradation of NF-kappa-B inhibitor beta (NFKBIB) by most signals, explaining why NFKBIB is more resistant to degradation. May act by blocking phosphorylation of NFKBIB and mediating cytoplasmic retention of p65/RELA NF-kappa-B subunit. It is unclear whether it acts as a GTPase. Both GTP- and GDP-bound forms block phosphorylation of NFKBIB (By similarity).
Subcellular Localization:
Cytoplasm.
Domain:
In contrast to other members of the Ras family, the members of the KappaB-Ras subfamily do not contain the conserved Gly and Gln residues in positions 13 and 65, which are replaced by Leu residues, and are therefore similar to the constitutively active forms of oncogenic forms of Ras. This suggests that members of this family are clearly different from other small GTPases proteins.
Sequence:
MGKGCKVVICGLLSVGKTAILEQLLYGNHTIGMEDCETLEDVYMASVETDRGVKEQLHLYDTRGLQKGVELPKHYFSFADGFVLVYSVNNLESFQRVELLKKEIDKFKDKKEVAIVVLGNKLDLSEQRQVDADVAQQWARSEKVKLWEVTVTDRRTLIEPFTLLASKLSQPQSKSSFPLPGRKNKGNSNPEN
The following text describes a protein:
Function:
Glyoxylate reductase that reversibly reduces glyoxylate to glycolate, or alternatively hydroxypyruvate to D-glycerate, using either NADPH or NADH as a cosubstrate. Does not act as a hydroxyisocaproate dehydrogenase even though it also has minor activity on alpha-ketoisocaproate.
Miscellaneous:
MISCELLANEOUS: Present with 3280 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus. Mitochondrion.
Sequence:
MSKKPIVLKLGKDAFGDQAWGELEKIADVITIPESTTREQFLREVKDPQNKLSQVQVITRTARSVKNTGRFDEELALALPSSVVAVCHTGAGYDQIDVEPFKKRHIQVANVPDLVSNATADTHVFLLLGALRNFGIGNRRLIEGNWPEAGPACGSPFGYDPEGKTVGILGLGRIGRCILERLKPFGFENFIYHNRHQLPSEEEHGCEYVGFEEFLKRSDIVSVNVPLNHNTHHLINAETIEKMKDGVVIVNTARGAVIDEQAMTDALRSGKIRSAGLDVFEYEPKISKELLSMSQVLGLPHMGTHSVETRKKMEELVVENAKNVILTGKVLTIVPELQNEDWPNESKPLV
The following text describes a protein:
Function:
Transcription factor that regulates the expression of the CLB2 cluster of genes during the G2/M phase of the mitotic cell cycle. The CLB2 cluster of genes includes mitotic regulators such as CLB1, CLB2, CDC5 and CDC20 as well as SWI5 and ACE2, transcription factors required for the subsequent temporal wave of cell cycle regulated gene expression in the M/G1 phase interval. Involved in HMRa silencing. FKH1 and FKH2 associate with the coding regions of active genes and influence, in opposing ways, transcriptional elongation and termination, and coordinate early transcription elongation and pre-mRNA processing. Both FKH1 and FKH2 play a role as regulators of lifespan in collaboration with the anaphase-promoting complex (APC), likely through combined regulation of stress response, genomic stability, and cell cycle regulation. FKH1 and FKH2 function also in controlling yeast cell morphology by preventing preudohyphal growth. Acts as a rate-limiting replication origin activator via its interaction with the origin recognition complex (ORC).
Miscellaneous:
MISCELLANEOUS: Present with 656 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus. Cytoplasm, cytosol. Note=Relocalizes to the cytosol in response to hypoxia.
Domain:
The FHA domain is necessary for the interaction with NDD1.
Sequence:
MSSSNFNEMNELNMTQTNYGSTKYTAQHHQGVINAIISSLTAPDQPTTVSLQYSNDKNMATEIQAYAKLSGPNWTYYVKDLEVSIGRNTDPLNSALQENSDGVKNSYRVNIDLGPAKVVSRKHAIIKYNMNIGGWELHILGRNGAKVNFQRTHNGPNNPPIRLSSGTLLDIGGTQMMFILPDSDPVVAPICIEHLMPNLINMFGLEGNNNPLLRDIIKQSNYAKQRQLTSNQQIKGFKLYGSGGNAPFGSGANLGPSEQGIFNNNNNSKNKNGYFTSINPNYTASTTTSNTINPQAASPQGPPNTIIAANFVDSYKSSNAYPQALDFTSDLSHDENRNVKPPHSYATMITQAILSSPEGVISLADIYKYISSNYAYYRFAKSGWQNSIRHNLSLNKAFEKVPRRPNEPGKGMKWRISESYQQEFLNKWNTGKVGKIRRGSSVARQLQLHMAKFNSLPMEMDYRLSLNMAQPPKRQLQSHNVLEPSNNNIIEGFVQHVPSKGNLPASQQSQPPVSHQNQSQQPPPQEQRQEIQFTFADTQNRNIALARPIKTPQLQAPNSNANLNQNNMKEYKESLHPPAISISQMNRQSPNNALVSFTNACANSKIINNISDSADKSTNNNGGTKMNLPAISTSSLDENGNLEPTTTTSSGNSNSVPQTGTTTSSLAANSLRLSQPYDTLLRSPTKAFHITAMEAYTPERGSANRARSPLHSNSNNTNNNGANNSNLQTSGMENKQTGLVLDSNVLKSMESNNDNRRLTPSTSKSQNVKSSPGVWNLLQFSSTNNTPAADSGGNKRGFSINPDIKAKENENATSEKDSDSNSNDLETKDINSSPLKNQGGSTANAKELILDTDGAKISIINN
The following text describes a protein:
Function:
Catalyzes the condensation of L-2,3-diaminopropionic acid (L-Dap) and citryl-diaminoethane to form L-2,3-diaminopropionyl-citryl-diaminoethane, the third step in staphyloferrin B biosynthesis.
Sequence:
MIVVQTLFIHIYQIQFVITRRYRIVNQTILNRVKTRVMHQLVSSLIYENIVVYKASYQDGVGHFTIEGHDSEYRFTAEKTHSFDRIRITSPIERVVGDEADTTTDYTQLLREVVFTFPKNDEKLEQFIVELLQTELKDTQSMQYRESNPPATPETFNDYEFYAMEGHQYHPSYKSRLGFTLSDNLKFGPDFVPNVKLQWLAIDKDKVETTVSRNVVVNEMLRQQVGDKTYEHFVQQIEASGKHVNDVEMIPVHPWQFEHVIQVDLAEERLNGTVLWLGESDELYHPQQSIRTMSPIDTTKYYLKVPISITNTSTKRVLAPHTIENAAQITDWLKQIQQQDMYLKDELKTVFLGEVLGQSYLNTQLSPYKQTQVYGALGVIWRENIYHMLIDEEDAIPFNALYASDKDGVPFIENWIKQYGSEAWTKQFLAVAIRPMIHMLYYHGIAFESHAQNMMLIHENGWPTRIALKDFHDGVRFKREHLSEAASHLTLKPMPEAHKKVNSNSFIETDDERLVRDFLHDAFFFINIAEIILFIEKQYGIDEELQWQWVKGIIEAYQEAFPELNNYQHFDLFEPTIQVEKLTTRRLLSDSELRIHHVTNPLGVGGINDATTISET
The following text describes a protein:
Function:
Voltage-gated proton-selective channel that conducts outward proton currents in response to intracellular acidification. Lacks a canonical ion-channel pore domain and mediates proton permeability via its voltage sensor domain. Appears to play a dominant role in regulation of CO2/HCO3(-)/H(+) equilibrium in sperm flagellum. Prevents the acidification resulting from HCO3(-) synthesis and thus sustains high HCO3(-) levels inside sperm for capacitation. Provides for proton efflux that compensates for electron charge generated by NADPH oxidase activity either in the extracellular or phagosomal compartments, thus enabling the production of high levels of bactericidal reactive oxygen species during the respiratory burst. Opens when the pH of airway surface liquid exceeds 7 and contributes to respiratory epithelial acid secretion to maintain pH in the mucosa.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Apical cell membrane; Multi-pass membrane protein. Cytoplasmic vesicle, phagosome membrane; Multi-pass membrane protein. Cell projection, cilium, flagellum membrane; Multi-pass membrane protein. Note=Detected within the principal piece of the sperm flagellum. Detected mainly at intracellular membranes upon overexpression in HeLa cells.
Domain:
The voltage sensor domain (VSD, segments S1-S4) conducts both gating and ion permeation. The segment S4 is probably the voltage-sensor and is characterized by a series of positively charged amino acids at every third position. Unlike other voltage-gated ion channels it lacks the pore domain; The C-terminal coiled coil region mediates homodimerization and cooperative channel gating. It is essential for normal subcellular localization.
Sequence:
MATWDEKAVTRRAKVAPAERMSKFLRHFTVVGDDYHAWNINYKKWENEEEEEEEEQPPPTPVSGEEGRAAAPDVAPAPGPAPRAPLDFRGMLRKLFSSHRFQVIIICLVVLDALLVLAELILDLKIIQPDKNNYAAMVFHYMSITILVFFMMEIIFKLFVFRLEFFHHKFEILDAVVVVVSFILDIVLLFQEHQFEALGLLILLRLWRVARIINGIIISVKTRSERQLLRLKQMNVQLAAKIQHLEFSCSEKEQEIERLNKLLRQHGLLGEVN
The following text describes a protein:
Function:
Plant lipoxygenase may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. It catalyzes the hydroperoxidation of lipids containing a cis,cis-1,4-pentadiene structure (By similarity).
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MLRPQLNPSSSHHHTTTTSSSSSTQLYFASSSCIASLRRPSPPSLIAGAGCRTTRRRQQGRQRVVVRCASSSAASSASEAARRGTGSSDMAPAAVVKVKAVATIKVTVEGLLNSLRPSKAIDNIRDLIGRSLFLELVSSELEAKTGKKKATVHSYAHKVDDDDHGVVTYEADFDVPTGFGPIGAVVVTNELGQEMFLEDLNLTAGDGAGNSTVLPIRCNSWVQPKSSIDEGTPGKRIFFAKAYLPGQTPAGLRSYREEDLKQKRGNGAGQREADDRVYDYDVYNDLGNPDSNGDLARPVLGGSKQFPYPRRCRTGRPPSKKDPKSETRKGNVYVPRDEEFSEVKNAQFLLKTLQSVLHAAVPAAQSALIDNLSLNLPFPSFFVIDKLFEDGVELPGVEKLGFLHSIVPRLLELLRDSPGDKILLFDTPANVQKDKFAWLRDEEFARETLAGINPYAIELVREFPLKSKLDPAVYGPAESAITADLLEEQMRRVMTVEEAISQKRLFMLDFHDLFLPYVHKIRSLKHTTMYGSRTIFFLTDDGTLRLLAIELTRPASPSQPQWRQVFTPSTDTTKSWLWRMAKAHVRAHDAGHHELITHWLRTHCAVEPYIIAANRQLSEMHPIYQLLHPHFRYTMRINALARSRLISAAGIIELSFSPQKYSMELSSVAYDKLWRFDMEALPADLVRRGMAEEDPTAEHGLRLAIEDYPFANDGLLIWDAIKTWVQAYVARFYPDADSVAGDEELQAFWTEVRTKGHGDKKDAPWWPKLDSPESLAHTLTTIVWVAAAHHAAVNFGQYDFGGYFPNRPSIARTVMPVEEPVDGAAMERFLDNPDQALRECFPSQVQATVVMAVLDVLSTHSTDEEYLGGEQTRPWNSDAAVQAAYAGFTARLKEIEGVIDGRNKDRKLKNRCGAGILPYQLMKPFSDAGVTGMGIPNSTSI
The following text describes a protein:
Function:
Involved in sporulation.
Subcellular Localization:
Forespore outer membrane; Peripheral membrane protein. Spore coat. Note=Initially localizes to a focus at one end of the forespore, which then undergoes transformation into a ring adjacent to the forespore. Next, the ring becomes a cap at the mother cell pole of the forespore that eventually spreads around the entire developing spore.
Sequence:
MVKGTIKEKYGIHIRQLSMYQHTYQCFQTPNSYFLIVPVSQFSETELAELYYMSQYLQEQSDPYVSVFIFTKEGELTFEHEGKTYALLKAAPPYSNRAFSIGAELAEFHRKGRGYPYEVKAAGRIGQWKDLWGKRIDQLEAFWQRKVQTPPHEPFDKKMIESFPYYLGLSENAIQYLVDTELDDKPQAADSGTICHQRMERHTWSPESLIRIPADWVFDHASRDLAEYMRHTFLHHRQDFNQQGFLFLQEYEQVTPLSSFSKRLLYSRLLFPLHYFEIVESYYMSSESEKHYFEEQLDFILNDCGRYEQFLNTAQEFMNMRAQKLFVPRVSWLGKGSSR
The following text describes a protein:
Function:
Catalyzes the first and rate-limiting reaction of the four reactions that constitute the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process allows the addition of 2 carbons to the chain of long- and very long-chain fatty acids (VLCFAs) per cycle. Condensing enzyme that exhibits activity toward saturated C18 to C26 acyl-CoA substrates, with the highest activity towards C22:0 acyl-CoA. May participate to the production of both saturated and monounsaturated VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Domain:
The C-terminal di-lysine motif may confer endoplasmic reticulum localization.
Sequence:
MLVYNQLEAVITRHTATTMEGIVTMYQDFMKKADPRIADYPLMQSPFLVLGILLAYVYFVLSLGPRLMANRKPLNLKKFMVLYNFFLVGLSLYIVYEFLMAGWLTGYTWRCDPVDFSQDPKALRMVSVAWLFVFSKFIELTDTVIFVLRKKNEQVTFLHLFHHSVLPWSWWWGAKFGPGGMGSFHAMINSMVHVVMYFYYGLSAAGPAFQKYLWWKKHITAIQLAQFVIVSVHISQYYFMPSCQYQFPIFIHLIWIYGTIFFILFSNFWYQSYTKGKRLPRVAQQAAQHNGSSIHENGTVTNGKVKSN
The following text describes a protein:
Function:
mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria.
Subcellular Localization:
Cytoplasm.
Sequence:
MSTIDLPTSSLPGSSGDPSGTEMSHSDVDVSVDIDVIFPDHTQTLSFSLLLSNTIHDVRQVILELMLAPPHTCFHLEYKREKLHSFLEIGQIPHLKLSKTRKIVLEVVLDPYTERESKYHIYTLLEFLSRKLPSSSTSPGIRAGFCIFPSLNIPSGENLQIKSSSSLEEINKIPENIVTQSLSYTNLLKKFETSPNPSNNGCFRSLALSGWNPVPAEFVIQGHLLYLTVLTIEGKTYNITSHVSGFYVNNCTSTKFDPSPCDDLQSHSLVLLLEQLSPLFKERLHLSLNDYKSGDAIAQASITGTLPQAPWITFPVPHRADLSRTQKSELFPYIENQGNLRDWNEEIQSTREMDHEDVQDRVLRERLTVKTLQDFTDMAVEGAIDMVNGNIPSLNPLEPTASQMFVHNNIFFSYGRDSVGIFSTKGGDSAAYSAVGKDILAIRLLNQFDLSNPSLLGTCVVDYAGHRVVAQTIVPGIFKQLENGSSHLIYGKVEGESDFRFDESFEGELSRISDLLHIKKHFFVDGKEKSFPLYTSMDAKALKGSDGRTYLMDLYSLFPLDAQFLEVISDEKNEEFPAYPHKLVHVRPELVQLFYEMKLQAFVNANHNAPKKKNLNDSLKSVELEGNGIKLSSEKGKNNVNKVRNDNARFDCGFNPDCFRSDYIFPPDNKELYDKDIENSYALSQYLHAEVIPNFVKSLSEPSSFLPIDGVALCRAMHRSGINIRYLGEIANIILQKSPNNVILLKLVTSEIFIRSIKHVFRNFLAVVPQVLRSHLLSHLLNNLFTVYGYVEPTKPLINENIANLFFQATQVIYSINSTSLYSSIKKEASSRFRFNLTDDLLHSLNPICILRGTCLRLGIQISCKDYFSNKSDDKICEEHAVPNGSTKFTGKKGNKKKRNLGKSQNTTNRQVESEQINIFRPKDILNLMPVIKTCIPYSGLAQESLEACKACLLQGNKELCYNLLNESLSLHEQIYGVLHTEVARAYCQLAMIYHQLEKKEEAVELARKAVIVCERFLGFDSSETSLAYMNLSLYEFSQKNEMQAVMHMQHALKLWYLVFGPDHPNTINSFTNLSLMLHGSEKFIQSQKCLQIAVDLSDKIFGKTTPTASLYLQLAQLMVLNKDSRSALHAVRVAYDILKETLGPDHQNTKEAEHWLSEFTALAVNQERQSRT
The following text describes a protein:
Function:
Component of the commander complex that is essential for endosomal recycling of transmembrane cargos; the Commander complex is composed of composed of the CCC subcomplex and the retriever subcomplex (By similarity). Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels (By similarity). Involved in regulation of NF-kappa-B signaling (By similarity). Promotes ubiquitination of I-kappa-B-kinase subunit IKBKB and its subsequent proteasomal degradation leading to NF-kappa-B activation; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex (By similarity). May down-regulate NF-kappa-B activity via association with COMMD1 and involving a CUL2-dependent E3 ubiquitin ligase complex. Regulates the cellular localization of COMM domain-containing proteins, such as COMMD1 and COMMD10 (By similarity). Component of the CCC complex, which is involved in the regulation of endosomal recycling of surface proteins, including integrins, signaling receptor and channels. The CCC complex associates with SNX17, retriever and WASH complexes to prevent lysosomal degradation and promote cell surface recycling of numerous cargos such as integrins ITGA5:ITGB1 (By similarity). Plays a role in copper ion homeostasis (By similarity). Involved in copper-dependent ATP7A trafficking between the trans-Golgi network and vesicles in the cell periphery; the function is proposed to depend on its association within the CCC complex and cooperation with the WASH complex on early endosomes (By similarity).
Subcellular Localization:
Endosome. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome.
Sequence:
MEEADRILIHSLRQAGTAVPPEVQTLRAFTTELVVEAVVRCLRVINPDVGSGLSHLLPPAMSARFRLAMSLAQACMDLGYPLELGYQNFLYPSEPDLRDLLLFLAERLPTDASEDADQPAGDSAIFLRAIGSQIRDQLALPWVPPLLRTPKVQRLQGSALQQAFHSSRLVLPELNCRGEPREFQASPLLLPAPSQVPQLLGRAASLLEHHAIQLCQHVNRDCPGDEDRVRWASRLPSQEDPRAPQQRLHKQLIEHLRQSWGPLGAPTQVRDLGEMLQAWGAKAMTGVPKGSRFTHSEKFTFHLEPQVQAAQVADIPAASQRPEQDTRAAQEEELESLREQLASVNHNIEEVEANMKSLGMNLVQVETECRQSELSVAEQEQALRLKSRTVELLPDGAANLTKLQLVVESSAQRLIHLASQWEKHRVPLLAEYRHLRKLQDCRELESSRRLVEIQELHQSVRAAAEEARRKEEVYKQLVSELETLPKDVSRLAYTQRILEIVGNIRKQKEEITKILSDTKELQKEINSLSGKLDRTFAVTDELVFKDAKKDDAVRKAYKYLAALHENCSQLIQTIEDTGTIMREVRDLEEQIETEMGKKTLSNLEKICEDYRALRQENAGLLGRVREV
The following text describes a protein:
Function:
May modulate chromatin structure by regulation of histone octamer formation.
Subcellular Localization:
Nucleus.
Domain:
The acidic domain may be involved in the interaction with histones.
Sequence:
MSENNEIEMELPFDSSAITSTEVLDRVNALLTLQDTQNELTEQMEKEILEIEKKYLKKFQPLAEKRFEIVSGKVEPTKEDQQCKAPIQVENLKSVPTDKGIPKFWLHVLQNTEVKDIIEECDIEALEYLVDIKIVQVGDAQDYSLDFHFSENPFFTNTVISKTVKLEEDNELNEIVSTPINWKDGKNFTVQSKKKTVKSKPTKGKAATTTSTTVQEVVPCFFSTFVSPNQDPTSDEEADEIMYIQYQIIAKLKDIVIPEAVNFFLGRASDAEENDYDFGEDFEDEEGEDDDEEDDEEEQTIKKPSGKGKAQPQQPQDCKQQ
The following text describes a protein:
Function:
Converts glutamate to gamma-aminobutyrate (GABA), consuming one intracellular proton in the reaction. The gad system helps to maintain a near-neutral intracellular pH when cells are exposed to extremely acidic conditions. The ability to survive transit through the acidic conditions of the stomach is essential for successful colonization of the mammalian host by commensal and pathogenic bacteria.
Miscellaneous:
MISCELLANEOUS: Changing Lys-276 to Ala increases thermal stability and protease resistance. The unfolding temperature is increased by 11 degrees Celsius.
Subcellular Localization:
Cytoplasm. Membrane. Note=Localized exclusively in the cytoplasm at neutral pH, but is recruited to the membrane when the pH falls.
Sequence:
MDKKQVTDLRSELLDSRFGAKSISTIAESKRFPLHEMRDDVAFQIINDELYLDGNARQNLATFCQTWDDENVHKLMDLSINKNWIDKEEYPQSAAIDLRCVNMVADLWHAPAPKNGQAVGTNTIGSSEACMLGGMAMKWRWRKRMEAAGKPTDKPNLVCGPVQICWHKFARYWDVELREIPMRPGQLFMDPKRMIEACDENTIGVVPTFGVTYTGNYEFPQPLHDALDKFQADTGIDIDMHIDAASGGFLAPFVAPDIVWDFRLPRVKSISASGHKFGLAPLGCGWVIWRDEEALPQELVFNVDYLGGQIGTFAINFSRPAGQVIAQYYEFLRLGREGYTKVQNASYQVAAYLADEIAKLGPYEFICTGRPDEGIPAVCFKLKDGEDPGYTLYDLSERLRLRGWQVPAFTLGGEATDIVVMRIMCRRGFEMDFAELLLEDYKASLKYLSDHPKLQGIAQQNSFKHT
The following text describes a protein:
Function:
Component of the KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Bud32 has ATPase activity in the context of the KEOPS complex and likely plays a supporting role to the catalytic subunit Kae1.
Subcellular Localization:
Cytoplasm.
Domain:
This protein is considered an atypical serine/threonine kinase, because it lacks the conventional structural elements necessary for the substrate recognition as well as a lysine residue that in all other serine/threonine kinases participates in the catalytic event (By similarity). Bud32 has protein kinase activity in vitro, but in the context of the KEOPS complex, the catalytic subunit Kae1 switches the activity of Bud32 from kinase into ATPase.
Sequence:
MKLIKQGAEAKIYLAEFSELYFDYPIKVIVKERIKKRYRIPEIDLKLRKERTIREARILRRAKEFGVNVPYVFEVDTKNMIIVMEYIEGERLKELLEKLPMEERLKVCREVGRQIGKLHEAGIVHGDLTTSNMILREGKVYFIDFGLAEFDDTIEAQGVDLHLLKRAMESTHYKWFERGFEEVLKGYIEIRGEDKGREIREKIREIELRGRYRERSWITQ
The following text describes a protein:
Function:
Regulatory subunit of the condensin complex, a complex required for conversion of interphase chromatin into mitotic-like condense chromosomes. The condensin complex probably introduces positive supercoils into relaxed DNA in the presence of type I topoisomerases and converts nicked DNA into positive knotted forms in the presence of type II topoisomerases.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MLEFQIPIHFEDISLVSNDKYTCLLYRNSIKMYMYFIEHYISYQIANHSNSGTTAPTITNAIENSEEDEIIKSKKPSRSKKSTSTVTSKSKKSTTIELFEKDEDKILILTSIINLLELNLSQIWRLEYPEEEFINLISKIAYGMFEQIHNLRNKGIKNLIFQILAILILKYNHSFNFTGKIINLLHTNEALSIHCADLYKFIQQFHRRQQRNEKLQRIQNGQPSQMTIEKNKSTFLISDVIREIGKQKDQRDTSGFKNLAKFLSELTERLPKSVLPFISLLVVHLDSESYLMRNAVTESIGFLIGKALGEDEGNGTNSDNEEKKIKKEEDRKKKENDKQDLLNILFDRVRDVNGYCRSSVLKTLSLLVVNNWVSSKDLLNQYLEITKVAIERLSDKNVQVRKRAILLLLNLLDSNPYNDNLSMELFKEKKDRLDSLINVSVQILRKQKEKDRQQQNGSIVNAGDVVLSQQVPEDDELPNYEEGQAKQEYPTEEDEKLEDDFVYRNIKINGEQFFNIISKLRPFEGIKIFKPDRLPSYVSHLTTYLSQSIKFIKMINQAMDTIYQLMGSTSSFDVIESIHFIEVSHKFKIDKSKEATNKMLSLIWNKEPSIKEESIKAFNELLINEPKISEPNSHSRACWLIAKNLIGQTLSATLGETTSLEELIIEFMKKKLIDQDVIRVLWDIFLNKSPPKNIQISKYDRRGALIILSMAANVDSTIVKDKIDALIHLGLENKTDDYLPRYACITLQKLRSKQQHSSSANPTSKSNEPTIQPRFKNNQHLFERLVYYITQPLNKITDDSNENINNNKWYMFTEQAINTIYILSEQPDIIASDIIKTISKQINLTLTNGALSEIDSLTLSRFIFVLGHIAVKQLVYVEEIESEKKRAKYQQSLNEKQKATTSKKSSLEKELGTDQAEAETEAEQIQQQAEADILSDNNLIGLYKPLVIAICSNVNNLFDQESLQTSAVLTLSKFMSVDPNFCEQNLQLLFTLLETCETEVIRSNIIIGLGDLAFRFPNLVEPWTSKIYSRLRDPDPKARKNSLMVLTHLILNDMIKVKGQISEMAICLEDPDSRISDIAKLFFTTLSSKGNNLYNSLPDIIGKITSSSNITSSSSTPLPQSPPINPTSSPTLSNISSTQSNSNILPIQKESIKNILKYLFSFIEKDKQNETLIEKLILRFKVSKTIFESQNISYCLQLLNFNEKSLKKLLEHFKLYQDKLFDNEVYNNLLLVISKTKKHQTFSKSNEIKQILDELENKIESTRNQTNNPGEDSMEQDIAKPTPSKPSKKAPAKKKVSAKASSKTPTKKTINKKNDSSEEHSESGQSESDKMDISSDEGISTKKTITTPRMPTRQVKTPIRKQIKKIESSSEDDNSESESESESDNRESINSESDSDSTSETIKKSIKKPVSKKPPASKKPPAPKKPAAKRLRKIQQSESDSDSESNESDSFETDD
The following text describes a protein:
Function:
Catalyzes the decarboxylation of 3-oxo-tetronate 4-phosphate to dihydroxyacetone phosphate (DHAP) and CO(2).
Sequence:
MNSEIEKVKRELVKIGKRIAQENLIVGPGGNISAKVGNRVYIKASGISFEDATEDDYIGVDFNSGEVIEGDKKPSSEIWMHLECYKVREDVKAVVHTHPIYSIAYAFQDEPLKLFTPDMVALLGGEIPVVEYVVPGGKEFAGVVGGVIKNHNGVLVKNHGLVTVGSNLKEALYRTLLIENSIKTIFVAKLFGKMGFFTKEQIEEIDSLEVEKYRRKLLKEKG