lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Essential for the generation of mature 18S rRNA, specifically necessary for cleavages at sites A0, 1 and 2 of the 47S precursor. Directly interacts with U3 snoRNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
TAAMEESFPRGGTRKTHKLEKAFQQSVEQDNLFDISIEEESTKRKKSQKGPAKTKKLKIEKRESSKSVREKFEVLSVESLREGMRILGCVKEVHELELVISLPNGLQGFVQATEICDAYTEQLNEQVAQEEPLKDLVCLSELFSPGMLVRCVVSSVGITESGKKSVKLSLNPKNVNEVLSAEALKPGMLLTGTVSSLEDHGYLVDIGVSGARAFLPLQKAQEYIRQKNKGAKLKVGQYLNCIIEEVKGNGGVVGLSIGPSEVSAAIATEEQNWTLNNLLPGLVVKAQVQKVTPVGLTLNFLTFFSGLVDFMHLDPKKAGTYFSNQAVRACVLCVHPRTRAVRLSLRPIFLQPGRSLTRLSCQHLGAVLDDVPVQSFFSKAGATFRLKDGALAYARLSHLSDSKNIFNAEAYKPGNIHKCRIIDYSQMDEMVLLSLRPSIIESQYFRYHDIKPGALVKGTVLTIEPYGMLVKVGEQIRGLIPPMHLADILIKNPEKKYHIGDEVKCRVLLCDPEAKKLMMTLKKTLIESKLPAITCYADAKPGLQTHGFILRVKDYGCIVKFYNDVQGLVPKHELSAEYVPDPERVFYTGQVVKVVVLNCEPSKERMLLSFKLLGDPKKEHTGHSQKKRRAISVGQLVDVKVLEKTKDGLEVSVLPHNIPAFLPTPHLSDHVANGPLLYHWLQAGDTLHRVLCLSQSEGRVLLCRKPALVSTVEGGQDPKNFAEIHPGMLLIGFVKSIKDYGVFVQFPSGLSGLAPKAIMSDKFVTSTSDHFVEGQTVVAKVTNVDEEKQRMLLSLRLSDCGLGDLATTSLLLLSQCLEERQGVRSLMSNRDSVLIQTLAEMTPGMVLDLEVQEVLEDGSVVFSEGPVSGLVLRASKYHRAGQEVEPGQKKKVVILNVDMLKLEVHVSLCHDLVNRKPKKLKKGSEHQAIVQHLEESFAVASLVETGHLAAFSLTSHLNDTFRFDSEKLQVGQGVSLTLKTTEPGMTGFLLAVEGPAAKRTVRQTRKDSETVDEDEEADPALVVGAVKKHTLSIGDMVTGTVKSIKPTHVVVTLEDGIIGCIHASHILDDVPVGTSPTAKLKVGRTVTARVIGGRDMKTFKFLPISHPRFIRTIPELSVRPSELEKDGCTALNTHSSSHLEKIKQYQAGQTLICFLKKYNVVKKWLEVEIAPDIRGRIPLLLTSLSFKVLKHPDKKFRIGQALKATVVGPDSSKAFLCLSLIGPHKLEKGEVAMGRVVKVTPKEGLTVSFPFGKIGKVSVFHVSDSYSETPLEDFVPQKIVRCYVLSATGHVLTLSLRSSRTNPETKSKITDPEINSIQDIQEGQLLRGYVKSVQPHGVLFGLGPSVVGLVQYPHVSQYSPSKKTLYNRYLPEGKLLTAKVLSLKCQKNLVELSFLPNDTGKPDVFPASLGLPLLKQEERTEEAEENKHKEEEKEEKNQKRKGKRNQEGQEGVQLPGEEKKEPQKLQAKKQGKRRRRESAGEQERVNKKQKKAAPSEEDDSGVEVYYREGEEEVEEMSVLPKEKPRRPAEVPRLQLSSGFIWDVGLDSLTPALPPRGESSDSEEDNKPQQSTQKKSKKERMLEKQKAEKELSRIEEALMDPGRQPESADDFDRLLLSSPNSSILWLQYMAFHLQATEIEKARAVAERALKTISFREEQEKLNVWVALLNLENMYGSQESLTKVFERAVQYNEPLKVFLHLADIYNKSEKFQEAGELYNRMLKRFRQEKAVWIKYGAFLLRRGQAGASHRVMQRALECLPNKEHVDVIAKFAQLEFQLGDAERAKAIFENTLSTYPKRTDVWSVYIDMTIKHGSQKEVRDIFERVIHLSLAPKRMKFFFKRYLDYEKQHGTEKDVQAVKAKALEYVEAKSSVLED
The following text describes a protein:
Function:
Catalyzes the synthesis of dihydrouridine, a modified base found in the D-loop of most tRNAs. Specifically modifies U16 and U17 in cytoplasmic tRNAs. Affects the level of some mature tRNA and thereby the total cellular translation.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Predominantly cytoplasmic localization with a minor population localized to the nucleus.
Sequence:
MPKLQGFEFWSRTLGGARHVVAPMVDQSELAWRLLSRRHGAQLCYTPMLHAQVFVRDANYRKENLYCDVCPEDRPLIVQFCANDPEVFVQAALLAQDYCDAIDLNLGCPQMIAKRGHYGAFLQEEWDLLQRMILLAHERLSVPVTCKIRVFPEIDKTVRYAQMLEKAGCQLLTVHGRTKEQKGPMAGTASWEHIKAVRKAVGIPVFANGNIQCLQDVERCIQDTGVQGVMSAEGNLHNPALFEGRSPAVWELAEEYLDIVRQHPCPLSYVRAHLFKLWHHTLQVHQQLREELAKVKTLEGVAAVSQALKLRCQEDMSRQQEGVRPADNLPAFHWICQPYIRPGPREGSKENSGGRSKRALEEEEGSMEGLSKNKLKKQLRNPHKTFDPSLKPKYAKCDQCGNPKGNRCVFNLCRGCCKKRAFRETADCPGHGLLFKTKLEKSLAWKGTQPGLQEAQQVRPVTPSGFSEVVGSALA
The following text describes a protein:
Function:
Restriction factor required to restrict infectivity of lentiviruses, such as HIV-1: acts by inhibiting an early step of viral infection. Impairs the penetration of the viral particle into the cytoplasm. Non-ATP-dependent, non-specific lipid transporter for phosphatidylserine, phosphatidylcholine, and phosphatidylethanolamine. Functions as a scramblase that flips lipids in both directions across the membrane. Phospholipid scrambling results in HIV-1 surface exposure of phosphatidylserine and loss of membrane asymmetry, which leads to changes in HIV-1 Env conformation and loss of infectivity.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein; Cytoplasm, perinuclear region. Note=(Microbial infection) Upon HIV-1 infection, it is redirected to perinuclear region following interaction with HIV-1 Nef, excluding it from virions particles, thereby preventing subsequent antiviral defense activity (Probable).
Sequence:
MGAVLGVFSLASWVPCLCSGASCLLCSCCPNSKNSTVTRLIYAFILLLSTVVSYIMQRKEMETYLKKIPGFCEGGFKIHEADINADKDCDVLVGYKAVYRISFAMAIFFFVFSLLMFKVKTSKDLRAAVHNGFWFFKIAALIGIMVGSFYIPGGYFSSVWFVVGMIGAALFILIQLVLLVDFAHSWNESWVNRMEEGNPRLWYAALLSFTSAFYILSIICVGLLYTYYTKPDGCTENKFFISINLILCVVASIISIHPKIQEHQPRSGLLQSSLITLYTMYLTWSAMSNEPDRSCNPNLMSFITRITAPTLAPGNSTAVVPTPTPPSKSGSLLDSDNFIGLFVFVLCLLYSSIRTSTNSQVDKLTLSGSDSVILGDTTTSGASDEEDGQPRRAVDNEKEGVQYSYSLFHLMLCLASLYIMMTLTSWYSPDAKFQSMTSKWPAVWVKISSSWVCLLLYVWTLVAPLVLTSRDFS
The following text describes a protein:
Function:
Disease resistance (R) protein that specifically recognizes the AVR-Pik effector avirulence protein from M.oryzae. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via an indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth. Contribution of Pik-2 is required to recognize the effector avirulence protein AVR-Pik.
Domain:
The HMA-like (RATX1) domain is responsible for the specific recognition of AVR effectors.
Sequence:
MEAAAMAVTAATGALAPVLVKLAALLDDGECNLLEGSRSDAEFIRSELEAVHSLLTPNILGRMGDDDAACKDGLIAEVRELSYDLDDAVDDFLELNFEQRRSASPFGELKARVEERVSNRFSDWKLPAASLPPSSVHRRAGLPPPDAGLVGMHKRKEELIELLEQGSSDASRWRKRKPHVPLRIMGGEMQKIVFKIPMVDDKSRTKAMSLVASTVGVHSVAIAGDLRDEVVVVGDGIDSINLVSALRKKVGHAELLQVSQVKEDVKEITAMLAPVKSICEFHEVKTICILGLPGGGKTTIARVLYHALGTQFQCRVFASISPSSSPSPNLTETLADIFAQAQLGVTDTLSTPYGGSGTGRALQQHLIDNISAFLLNKKYLIVIDDIWHWEEWEVIRKSIPKNDLGGRIIMTTRLNSIAEKCHTDDNDVFVYEVGDLDNNDALSLSWGIATKSGAGNRIGTGEDNSCYDIVNMCYGMPLALIWLSSALVGEIEELGGAEVKKCRDLRHIEDGILDIPSLQPLAESLCLGYNHLPLYLRTLLLYCSAYHWSNRIERGRLVRRWIAEGFVSEEKEAEGYFGELINRGWITQHGDNNSYNYYEIHPVMLAFLRCKSKEYNFLTCLGLGSDTSTSASSPRLIRRLSLQGGYPVDCLSSMSMDVSHTCSLVVLGDVARPKGIPFYMFKRLRVLDLEDNKDIQDSHLQGICEQLSLRVRYLGLKGTRIRKLPQEMRKLKHLEILYVGSTRISELPQEIGELKHLRILDVRNTDITELPLQIRELQHLHTLDVRNTPISELPPQVGKLQNLKIMCVRSTGVRELPKEIGELNHLQTLDVRNTRVRELPWQAGQISQSLRVLAGDSGDGVRLPEGVCEALINGIPGATRAKCREVLSIAIIDRFGPPLVGIFKVPGSHMRIPKMIKDHFRVLSCLDIRLCHKLEDDDQKFLAEMPNLQTLVLRFEALPRQPITINGTGFQMLESFRVDSRLPRIAFHEDAMPNLKLLEFKFYAGPASNDAIGITNLKSLQKVVFRCSPWYKSDAPGISATIDVVKKEAEEHPNRPITLLINAGYKEISTESHGSSENIAGSSGIDTEPAQAQHDNLPAVRDDYKGKGILLDGRCPTCGRATKIEEETQDRVADIEIQTETTS
The following text describes a protein:
Function:
Plays a role in the maintenance of the appropriate processing of 47S/45S pre-rRNA to 32S/30S pre-rRNAs and their subsequent processing to produce 18S and 28S rRNAs (By similarity). Also acts at the level of transcription regulation. Along with PRMT5, binds embryonic globin promoter (By similarity). Represses the expression of embryonic globin Hbb-y gene. In neuroblastoma cells, may also repress the expression of oxidative stress genes, including CHAC1, HMOX1, SLC7A11, ULBP1 and that encoding the small nucleolar RNA SNORD41 (By similarity). Preferentially binds to a DNA motif containing 5'-GGTTAT-3' (By similarity). Negatively regulates the antiviral innate immune response by targeting IRF3 and impairing its DNA-binding activity (By similarity). In addition, inhibits NF-kappa-B-mediated expression of pro-inflammatory cytokines (By similarity). Stimulates phagocytosis of photoreceptor outer segments by retinal pigment epithelial cells. Prevents NCL self-cleavage, maintaining a normal steady-state level of NCL protein in undifferentiated embryonic stem cells (ESCs), which in turn is essential for ESC self-renewal.
Subcellular Localization:
Nucleus, nucleolus. Cytoplasm. Cell projection, cilium, photoreceptor outer segment. Note=Component of pre-ribosomal particles, including pre-40S, pre-60S and pre-90S (By similarity). Associated with cytoplasmic ribosomes, but not polysomes, as a component of the 60S subunit. In the retina, predominantly expressed in photoreceptor outer segments. In the nucleolus, colocalizes with nucleolin/NCL, therefore may reside in the dense fibrillar component (DFC).
Domain:
The N-terminal zinc-finger domains are required for the appropriate production of 28S rRNA and the formation of pre-60S particles.
Sequence:
MVFFTCNACGESVKKIQVEKHVSNCRNCECLSCIDCGKDFWGDDYKSHVKCISEGQKYGGKGYEAKTHKGDAKQQAWIQKINELIKKPNVSPKVRELLQQISAFDNVPRKKAKFQNWMKNSLKVHSDSVLEQVWDIFSEASSSEQDQQQPPSHTAKPHAEMPITKVPSAKTNGTTEEQTEAKKNKRERKEERQKNRKKEKKELKLENHQENLRGQKPKKRKKNQEAGHEAAGEEAAEASGPPEKKKAQGGQASEEGADRNGGPGEDAAEGQTKTAAGKRKRPKHSGAESGYKKKKMKLPEQPEEGEAKDHEAPSKGKFNWKGTIKAVLKQAPDNEISVKKLKKKVIAQYHAVMNDHHTSEEELLAIFNRKISRNPTFKVLKDRVKLLK
The following text describes a protein:
Function:
Seems to play a role in mitotic chromosome segregation and maintenance of chromatin structure. Has ATPase activity.
Subcellular Localization:
Nucleus.
Sequence:
MEPEHSNYDLKNHPTSVQESTLNGSAVTDPQFGNTTNSLPSMNGLLNHENSFASQQSLSSSAFDDSEIVTSTANSTVVSSALSTPKIDDAQNSDDVRVDGTRRSSRAKRPVYRDFSYTEIDEHEIPIPKKRKSKPAPKQKKSVASDDEDAYDKRHRFSINSASGTEIRTSLRSSKGKSVNYNEQEFYDDFEDEEEEVEEQVEEEYEPIIDFVLNHRKRADAQDDDPKSSYQYLIKWQEVSHLHNTWEDYSTLSSVRGYKKVDNYIKQNIIYDREIREDPTTTFEDIEALDIERERKNMLFEEYKIVERIVASETNEEGKTEYFVKWRQLPYDNCTWEDADVIYSMAPNEVYQFLQRENSPYLPYKGVFYNTRPPYRKLEKQPSYIKGGEIRDFQLTGINWMAYLWHRNENGILADEMGLGKTVQTVCFLSYLVHSLKQHGPFLIVVPLSTVPAWQETLANWTPDLNSICYTGNTESRANIREYEFYLSTNSRKLKFNILLTTYEYILKDKQELNNIRWQYLAIDEAHRLKNSESSLYETLSQFRTANRLLITGTPLQNNLKELASLVNFLMPGKFYIRDELNFDQPNAEQERDIRDLQERLQPFILRRLKKDVEKSLPSKSERILRVELSDMQTEWYKNILTKNYRALTGHTDGRGQLSLLNIVVELKKVSNHPYLFPGAAEKWMMGRKMTREDTLRGIIMNSGKMVLLDKLLQRLKHDGHRVLIFSQMVRMLNILGEYMSLRGYNYQRLDGTIPASVRRVSIDHFNAPDSPDFVFLLSTRAGGLGINLNTADTVIIFDSDWNPQADLQAMARAHRIGQKNHVNVYRFLSKDTVEEDILERARRKMILEYAIISLGVTEKSKNSKNDKYDAQELSAILKFGASNMFKATENQKKLENMNLDDILSHAEDRDSSNDVGGASMGGEEFLKQFEVTDYKAEDLNWDDIIPEEEMERIEEEERMLAAQRAKEEERERREEEERENDEDHPSRTYKRTTKSITKRQQRREEMVREKEIRLLYRAMIKFGLVDERFDTIVKEAELQATDPKRIYSLSADMVKACDEAVERLGADDTKNKQPRKAILIEFKGVKNINAETVTLRVKDLTHLHRAYKGLDPLKQIIGYPIRSVHSWNCSWGIKEDSMLLAGINKHGFGCWQAIKNDPDLGLHDKIFLDEAKNDKESRYVPSAVHLVRRGEYLLSVVREHPDLFVVKTDQPTKRKYNRKAPTKSSTRQTTLDGSISNTKKSSRTKKKKEEETNRGDETSPEGTVGEDEVEEEPRQAEPPKRALRSNSGKAASNKRTTRNSMKTHSAMDTLTAVAALDAELDNMSNEKAKEEVDHVKSENGESVNEPNTEDLSLETEENTTVSDISPLVKNEA
The following text describes a protein:
Function:
Part of the tripartite ATP-independent periplasmic (TRAP) transport system.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MITSAAFVAIMLVGVPIGLCLCLAGLVYIAASGNPVLFQSYPLQLFGGVDSYGLIAIPLFILIGEIMNGGGITRRIVDMAMAFVGSLKGGLAYVNILANMFISSILGSATAQVAIMAQIMVPEMEKKGYDKTFAAGLTAYGGMLGPIIPPSVMFVVYSVLAQVSVSDMLIAGIVPGVILTVMFCLVIALMGYIYNYPRADYQTPRQRVMTILRTSPTLLIPIVIVGTILGGLANATESAAVGAVAAALVGKYWTKEFEFSQLPQMMLRSAIYSAIVLFLVAAAAVFSWVLIFGKVPQETAGWIQSAAKDPISFMLICNVILLVIGTVIDGIPGLIMTVPILLPVATDVYHIDPRHFGVVVVINLVLGLLSPPVGLCFFVAAAVTGAKPGKMFMVTLPFFVISCVLLVLLSLFPSLSLILVK
The following text describes a protein:
Function:
Involved in protein export. Acts as a chaperone by maintaining the newly synthesized protein in an open conformation. Functions as a peptidyl-prolyl cis-trans isomerase (By similarity).
Subcellular Localization:
Cytoplasm. Note=About half TF is bound to the ribosome near the polypeptide exit tunnel while the other half is free in the cytoplasm.
Domain:
Consists of 3 domains; the N-terminus binds the ribosome, the middle domain has PPIase activity, while the C-terminus has intrinsic chaperone activity on its own.
Sequence:
MSLNIETTQGLERRVAITVPTEIVSKAVREEFKRAAKNVRVDGFRKGHVPAHIIEQRFGASIRQDVLNDLLPRHFFNAVIAEKINIAGRPTFAIETFEEGKDLVFTATFEVYPEVKLQGLENIKVEKPTVEITEADIDKMIDVLRKQQATWAESQDVVKADDRVTIDFVGSVDGEEFEGGKATDFVLFMGQGRMIPGFEEGIVGHKAGEQFDIDVTFPAEYHAENLKGKAAKFAITLKKIENMVLPELTDEFVAKFGPNTKSVADLRAEIRKNMERELKNALVSRVKQQVINGLIEQNPIDVPVSAVEEEINVLRNQAAQRFGGNAQQTAQLPRELFEAEATRRVQVGLLFSEVIKSNELKADEERAKAMIADIASAYEQPAEVVEYYSKNEELMNNIRNVVLEEQAVDAVLAKAQVTEKVSSFDEIMNPQA
The following text describes a protein:
Function:
Channel that opens in response to stretch forces in the membrane lipid bilayer. Forms a nonselective ion channel with a conductance of about 4 nanosiemens. May participate in the regulation of osmotic pressure changes within the cell.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MNFIKEFREFAMRGNVVDMAVGVIIGSAFGKIVSSLVSDIFTPVLGILTGGIDFKDMKFVLAQAQGDVPAVTLNYGLFIQNVIDFIIIAFAIFMMIKVINKVRKPEEKKTAPKAETLLTEIRDLLKNK
The following text describes a protein:
Function:
Efflux system for nickel and cobalt.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPLTGSLHSPLARGLLAGAAVVLVLGVADAALHDLLAQNPFGAPKPAPAAEPEASGLIGWLLAKQSEFYRQMSATIRAAKSDGSAVWTLLFISFAYGIFHAAGPGHGKAVIASYLVANRETARRGIALSFASALMQSVVAILIVGISAWILNATAKTMCKAEGMIEIASYGLIALFGLRLVWVKGGAFIRALQATQPVPAIAGVPQHHDHGHHHHREAHDHHDHDHHDHGHAHHDHGHDHVHDEHCGHSHGPAPSELAGPGGWRRGFAAILTVGIRPCSGAILVLVFALAQGLFWAGIAATFLMGLGTAITVAAIAVVAVSAKDIAARLSAGRDGGGALFMRGIEFGAAGLVLLFGVGLLFGYIAAERTTCF
The following text describes a protein:
Function:
Sorting nexin, involved in the separation or division of vacuoles throughout the entire life cycle of the cells. Involved in retrieval of late-Golgi SNAREs from post-Golgi endosomes to the trans-Golgi network, for cytoplasm to vacuole transport (Cvt), and autophagy of large cargos including mitophagy, pexophagy and glycophagy.
Subcellular Localization:
Cytoplasm, cytosol. Preautophagosomal structure membrane; Peripheral membrane protein. Endosome membrane; Peripheral membrane protein. Note=Endosome and other perivacuolar punctate structures. Associates to phosphatidylinositol 3-phosphate, necessary for peripheral membrane localization to the perivacuolar punctate structures.
Domain:
The PX domain binds phosphatidylinositol 3-phosphate which is necessary for peripheral membrane localization to the perivacuolar punctate structures.
Sequence:
MSSEDQFTSIQWDRDDGENTNNTPTDTTIKSKSSKSKKSKKSSSKKKNGNKISPSSTTETSDADDTMKEVTDQLESTQINDDNHEVDDGNKEQNVDANQIGNSDEDPTNSLLLPVNPQPKEPQEEKEDLQQQLQQPQQQLASIQQEPAPIQPPFNAVVNDESLSIQQQQQQQQPTGYVDISYYEKYSIKTTVTHPNRDLDTASKPFISYLVTTTTDNPSILKLTKEKKPKQGEEYLTFSVRRRYGDFRYLYESLSNDFPTVMIPPLPSKSNFKYLTGDTFSSEFVHKRLHSLDRFIRFILQHKILSQSSIFHLFISNSNDWATFTTSLKLKDSSSDESGIVGRVVNEDLITETVMNFLTPSKHKKETNKDILEINDKLKKLYENLIKLDKIFTKLKKKNHELGNDYDQFSNQILKLSSVQKGEDSIMTTNFKIFSDSLNYFSKSYNEMYRYIDENFLISLQDLAKFCLRFIQLIKLKNDKSTDLAVLQDFLNKELANNSGGSGSGSGSGGSGLHQPPNPVISSYQGGIVNNTTQLIKDTLSTSNTTISNTIKSDKIKNLEQEIAKETKILTDLTNKIINEEYPNWEKFNKIEIKNSMLGLCDQNIKFYNDLLEKFGEVEMKLIKRLDEDM
The following text describes a protein:
Function:
Catalyzes the sodium-dependent uptake of extracellular L-proline.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MENSFAITTTFIVYLILMLAIGVYAYQRTKNSADYFLGGRSLGPWPAALSAGASDMSGWLLLGLPGYAYAAGIESFWLAGGLLVGTWANWLVNAKRLRTYSITTDSLTLPEFLSRRFNDNSKLIQTISAFFILLFFLFYTSSGLVAGGKLFETVFGLDYSTAVIIGTVCVVSYTLFGGFLAVSWTDLVQGLLMAAALMIVPIAAMNGGFTQLNHDLAAINPELLTLWNDAKGEPLSAIAIISLVAWGLGYFGQPHILARFKASRSNKDLITARRIAVVWTGLSMAGAILVGLTGLIFVTQSGTIGLDDGEKIFMLLVNSLFHPVIAGILLAAILAAIMSTADSQLLVSSSALAEDFYKQVFKTDASSEDIVRVGRIAVILISLIALFLAMTPDSSVLGLVSYAWAGFGAAFGPALVLSLYWPRMNRHGALSGIIVGGVTIVVWKQLSGGWFDVYEIVPGIILSTLSIVVVSLLTGEPDEKVKAQHATFKKQLIELE
The following text describes a protein:
Function:
Probably acts as a transcriptional activator. Binds to the GCC-box pathogenesis-related promoter element. May be involved in the regulation of gene expression by stress factors and by components of stress signal transduction pathways (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MEESNDIFQNNFSPKISEIRASLSQIILAGGPNTLDSIFSLLTPSSVESATTSFNTHNPPPPPQLGSSVYLRQRDIIEKFHLQNRAISTPHPPLFSSTYDHHQTSELMLQAAAGSPAAAFAAALAAGRVTKKKKLYRGVRQRHWGKWVAEIRLPQNRMRVWLGTYDTAEAAAYAYDRAAYKLRGEYARLNFPNLKDPSELLGLGDSSKLIALKNAVDGKIQSICQRVRKERAKKSVKVSKNSSATADSSCLSSPEILSSSPVTTTTTAVTSEDSYWVSPMGLCNSENSSPVSVSVPSEVPATAEEEAMMGVDTDGFLLARMPSFDPELIWEVLAN
The following text describes a protein:
Function:
Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKLLLLLLLSILISINYSAPTFTNRGISSVYSKNDINNLNRFISTQKQGKLYGTDNQQLKDTFYAVGALTRLGESVSDAKTICSTVKEQLETNKFSDIELLYNGVTILSELKCIEEISSASKKIQETLKSKLQNGDLLETTQAVNIVFTLQSAKLVTNDDFDLTSSVKRIVSLMVEDEGTFKSTESDSEGTLLNTAAAYFALARLSHRLDNQEVDKQVAKVVHKMDTVIANAEETTDTLYFTDLQTTASLFHSMLSLASINEKVADFVSAKQVNQIAEYLLKQKNVESLSNAYYLIVGLKKCQKNSVSQPLSLTLEKSIFSPSNLATVDAFVTDIFGQNIPATVNVNKIVSSKAPRSTPVLSDKKMTTTGNKHSIDVSNENLKLGLYNIEFKVVPTDNEDYAEITSTQVITITGSITVDDMKFSFAPKADQLGSPKNSQDVVFGKKLSLVDIPANNLARVFFRINSDKQVFVPQQVGIRFYSPSREIVVPVTHSAESFSYTLTNKEMGKLLGYQSGNYQMDLIVGDQSITPLQWNFGEINLKFSQKTQPTSRYTENQPIVHAFRQPEKRPPQSVSNLFTLLVLSPAAIFLLGIFVVGFNLGKFPTGMGFIWTMGFIASVSSIALLIINYWIHSTMDVTLKRLALLLIPTIFFGHRSMSYYYNKYNTEKEIKKD
The following text describes a protein:
Function:
The natural substrate for this enzyme may be peptidyl-tRNAs which drop off the ribosome during protein synthesis.
Sequence:
MGDKLLDPTQIINGLAVMLSFFVGYRYALKRGDAKDSVTEGAATPFSQESSVSSGSEASVSDKGYGGLNDNFKMVLVVRNDLKMGKGKIAAQCGHGAVGAYQRAVVRTPRLLRSWENCGCAKIAVRVESEAELMAIKKEAERQQLNTCLIRDAGRTQIEANSKTVLAVGPAAAADIDRVTGHLKLL
The following text describes a protein:
Function:
Regulator of the Hippo/SWH (Sav/Wts/Hpo) signaling pathway, a signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. Mer acts synergistically along with Ex and Kibra to regulate the Hippo signaling pathway.
Subcellular Localization:
Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytoskeleton. Apical cell membrane. Cell projection, rhabdomere. Note=Membrane-associated, adherens junctions and endocytic compartments. Cytoplasmic, punctate.
Sequence:
MSPFGSKKNRSLSVRVSTFDSELEFKLEPRASGQDLFDLVCRTIGLRESWYFGLQYVDTRSNVSWLKMEKRVRDQRVELHASNNVYVFSFYAKFFPENVSEELIQEITQHLFFLQVKQSILSMDIYCRPEASVLLASYAVHVQYGPYDYETYKDGMLAGGELLPKGVTDQYQMTPEMWEERIKTWYMDHEPMTRDEVEMEYLKIAQDLDMYGVNYFPITNKNKTKLWLGVTSVGLNIYDERDKLTPKTTFQWNEIRHVSFDDKKFTIRLVDAKVSNFIFYSQDLHINKMILDLCKGNHDLYMRRRKPDTMEIQQMKAQAKEEKQRRQIERKKFIREKKLREKAEHERYELEKSMEHLQNEMRMANDALRRSEETKELYFEKSRVNEEQMQLTECKANHFKTEMDRLRERQMKIEREKHDLEKKIRDADFYVHQLTVENDKREAETEKLRKELICAKMAEREATARLLEFLNSGRKSSTDSLLTASSVSHAANTASSMAAISTPSLITSSSTNDLETAGGAELTTHSSHYLVQGDNSSGISDDFEPKEFILTDNEMEQITNEMERNHLDYLRNSKQVQSQLQTLRSEIAPHKIEENQSNLDILSEAQIKAGENKYSTLKKLKSGSTKARVAFFEEL
The following text describes a protein:
Function:
Catalyzes the formation of the signaling molecule cAMP in response to G-protein signaling.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MLGEVVNPEANVYTAEECDICRPDSNADQSHDTEGDYIALKKWELGFLRRECVNLGLETFYLKYMERVQRSYLSIFVVLQTFVSISHVIVIVTGKPHPTAAIHPDLICYLFGILIVWISLFAAFKEGLVKAYPWVPYVSSSIAVITMIITDLTIPLYHAVVTFINPPLRPSYASHTILAIYIFLPLTENIHGIILGSATSLCYLIVMTLITYRLEENTALKVITELIYFICLNLFGLYFRLINEVAIRRTFLDRRELVEGNLLLKFARNQEKELLLSILPEHTAELMEKDIRAMIEKMRNDQHNANQTINTQNFFRTGTQWRSINKLYVQKHTNVTILYADVVNYTHMTTQLPVRTLVDVLHELFVKFDEASKEFNVLRIKFLGDCYYCVSGVPVRNKYHAKSCVNLGLRMIKDIRDVRMSRDLNIDMRIGIHSGSIISGVIGACKWQYDIWSKDVIIANKMESTGEAGKVHVTMQTLELLDGEYIFEEGTPQAKEDPILVKHNIQTFLIVPQPGYDDGSFFTVQEPGPSSRMSSGVKRKTIKKERSLVTRNFMQNSMEQFREIMKLTNVEMAYELERMPIGRFQFNKLFSSYKTYMQEPSHTSAPARTVENGPRCSEEDTNRLDNMSPFFMCFENKRWELSYLQEPDLMLKYSVLMSFIVFVCILLIQILNDASGIYFWLLNGLSGALLLAFIPITWFKKVWDVYTPYSIDDLLRVRKPQSRVMRIFYDFSNDIMSNFVIRTVIYLITIALLVVCSLMYLIECNYDLLEQTSTTSVPVSDNLTSLFQENQTSPDPMAKNFCTNPWSVTQCLTLAIGMAFLFLRIHFLLKAAVGLLIFFFYCWAIFDDLYYYFDSSASMNPGLDPKVSHLMLILFIVIIFHWIDRQSEYIARTDYNWKQQLLKQKEEAEVTKQTNKILVENILPTHVAEIYINRQLKNEFYNEEYENVAVMFATITNMEVNTDISVENEKSVLKVLNEIICDFDERLQYFDGYLKVEKIKVAGWTYMAACGLDPGRCDSSSSLSGYRSVSGMTRTSLMTNGRRSLNPRTSLEVAHKASTSTRSNSSNSRHSNNVTIVMAEFALELMRVLRDFSNENFKQTSPGLLRVGISHGKVMAGVVGSSKPLYDIWGNAVNMASRMDSTGRPGRIQVTKESAEVLQSYGYQCDYRGEIFVKGRGKIPTYFLKIGSDLKFLKKASCDKAGNGHVPTEHITTKL
The following text describes a protein:
Function:
Cell surface proteoglycan.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MKSLLVLCVVCPLAVLCVSGTAEQKSKNCNEVRAAFSSKGFNINDVPNKGISGASLKVCPQGFSCCTVEMEEKLSQQSHTEIKAPVSRLSTNLQTIFKERHNHFDNFFRELLKNAEASLHNMFLRTYGKMYEQNSELFGNFFASLTRYYIDGSAKVDLDAMLTDFWADLLERMFRLVNVQFEFSDAYMECVSRNTDELQPFGDVPRKLRIQLKRAFIAARTFVRGLKLMPEVFNKVSTVSATPSCVRAATKMLYCPYCSGQVALKPCQNYCLNVMRGCLANQADLDTEWNNFLDAMLNLADRLEGPFNFESVMDPIDVKISEAIMNMQENSMQVSQKVFQGCGTPKLSQSFRSKRSLKETGFTGRFRPYTPEARPTTAAGTSLDRLVRRKNLLLLWSNPFPSFFCVRPARVCMHSGLGAWRGSFTADSLSHRYELHVIGNGLANQGTNPDVEVDITKPHTVIRSQIAALKEMTIWLKTAHSGNEIIESIDDDSSGESGSGCDSASCEPDIYFFTTTTPIPKGPRVNLVHSNNSAGVPIRAGVTLALCGLIAALLAPRLR
The following text describes a protein:
Function:
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MASSSAPVHPARYLSVFLVMLIGIYLLVFFTGDKHTAPKLGIDLQGGTRVTLTARTPDGSAPSREALAQAQQIISARVNGLGVSGSEVVVDGDNLVITVPGNDGSEARNLGQTARLYIRPVLNSMPAQPAAEEPQPAPSAEPQPPGQPAAPPPAQSGAPASPQPGAQPRPYPQDPAPSPNPTSPASPPPAPPAEAPATDPRKDLAERIAQEKKLRQSTNQYMQMVALQFQATRCESDDILAGNDDPKLPLVTCSTDHKTAYLLAPSIISGDQIQNATSGMDQRGIGYVVDLQFKGPAANIWADYTAAHIGTQTAFTLDSQVVSAPQIQEAIPGGRTQISGGDPPFTAATARQLANVLKYGSLPLSFEPSEAQTVSATLGLSSLRAGMIAGAIGLLLVLVYSLLYYRVLGLLTALSLVASGSMVFAILVLLGRYINYTLDLAGIAGLIIGIGTTADSFVVFFERIKDEIREGRSFRSAVPRGWARARKTIVSGNAVTFLAAAVLYFLAIGQVKGFAFTLGLTTILDLVVVFLVTWPLVYLASKSSLLAKPAYNGLGAVQQVARERRAMARTGRG
The following text describes a protein:
Function:
Mitochondrial antiporter which catalyzes the transport of citrate and oxoglutarate across the membrane. Also shows specificity for oxaloacetate, and to a lesser extent succinate and fumarate. Transports isocitrate, cis-aconitate and L-malate with very low efficiency. Does not show uniporter activity. Helps to maintain normal citrate levels and NADPH/NADP(+) ratios under conditions of oxidative stress. In addition, associates with the mitochondrial nucleoid and binds DNA in vitro, although the relevance of these data in vivo is unclear.
Miscellaneous:
MISCELLANEOUS: Present with 2930 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane; Multi-pass membrane protein. Mitochondrion matrix, mitochondrion nucleoid.
Sequence:
MPSTTNTAAANVIEKKPVSFSNILLGACLNLSEVTTLGQPLEVVKTTMAANRNFTFLESVKHVWSRGGILGYYQGLIPWAWIEASTKGAVLLFVSAEAEYRFKSLGLNNFASGILGGVTGGVTQAYLTMGFCTCMKTVEITRHKSASAGGVPQSSWSVFKNIYKKEGIRGINKGVNAVAIRQMTNWGSRFGLSRLVEDGIRKITGKTNKDDKLNPFEKIGASALGGGLSAWNQPIEVIRVEMQSKKEDPNRPKNLTVGKTFKYIYQSNGLKGLYRGVTPRIGLGIWQTVFMVGFGDMAKEFVARMTGETPVAKH