lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Serine/threonine-protein kinase and endoribonuclease that acts as a key sensor for the endoplasmic reticulum unfolded protein response (UPR). In unstressed cells, the endoplasmic reticulum luminal domain is maintained in its inactive monomeric state by binding to the endoplasmic reticulum chaperone HSPA5/BiP. Accumulation of misfolded proteins in the endoplasmic reticulum causes release of HSPA5/BiP, allowing the luminal domain to homodimerize, promoting autophosphorylation of the kinase domain and subsequent activation of the endoribonuclease activity. The endoribonuclease activity is specific for XBP1 mRNA and excises 26 nucleotides from XBP1 mRNA. The resulting spliced transcript of XBP1 encodes a transcriptional activator protein that up-regulates expression of UPR target genes. Acts as an upstream signal for ER stress-induced GORASP2-mediated unconventional (ER/Golgi-independent) trafficking of CFTR to cell membrane by modulating the expression and localization of SEC16A.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MPARRLLLLLTLLLPGLGIFGSTSTVTLPETLLFVSTLDGSLHAVSKRTGSIKWTLKEDPVLQVPTHVEEPAFLPDPNDGSLYTLGSKNNEGLTKLPFTIPELVQASPCRSSDGILYMGKKQDIWYVIDLLTGEKQQTLSSAFADSLCPSTSLLYLGRTEYTITMYDTKTRELRWNATYFDYAASLPEDDVDYKMSHFVSNGDGLVVTVDSESGDVLWIQNYASPVVAFYVWQREGLRKVMHINVAVETLRYLTFMSGEVGRITKWKYPFPKETEAKSKLTPTLYVGKYSTSLYASPSMVHEGVAVVPRGSTLPLLEGPQTDGVTIGDKGECVITPSTDVKFDPGLKSKNKLNYLRNYWLLIGHHETPLSASTKMLERFPNNLPKHRENVIPADSEKKSFEEVINLVDQTSENAPTTVSRDVEEKPAHAPARPEAPVDSMLKDMATIILSTFLLIGWVAFIITYPLSMHQQQQLQHQQFQKELEKIQLLQQQQQQLPFHPPGDTAQDGELLDTSGPYSESSGTSSPSTSPRASNHSLCSGSSASKAGSSPSLEQDDGDEETSVVIVGKISFCPKDVLGHGAEGTIVYRGMFDNRDVAVKRILPECFSFADREVQLLRESDEHPNVIRYFCTEKDRQFQYIAIELCAATLQEYVEQKDFAHLGLEPITLLQQTTSGLAHLHSLNIVHRDLKPHNILISMPNAHGKIKAMISDFGLCKKLAVGRHSFSRRSGVPGTEGWIAPEMLSEDCKENPTYTVDIFSAGCVFYYVISEGSHPFGKSLQRQANILLGACSLDCLHPEKHEDVIARELIEKMIAMDPQKRPSAKHVLKHPFFWSLEKQLQFFQDVSDRIEKESLDGPIVKQLERGGRAVVKMDWRENITVPLQTDLRKFRTYKGGSVRDLLRAMRNKKHHYRELPAEVRETLGSLPDDFVCYFTSRFPHLLAHTYRAMELCSHERLFQPYYFHEPPEPQPPVTPDAL
The following text describes a protein:
Function:
Secreted effector that interacts with and inhibits host apoplastic pathogenesis-related papain-like cysteine proteases (Probable). Inhibition of host proteases by a pathogen extracellular protease inhibitor forms a specific type of defense-counterdefense mechanism between plants and microbial pathogens (Probable).
Subcellular Localization:
Secreted. Note=Localizes to host apoplast where it targets defense proteases for inhibition.
Sequence:
MRASLSILVAFPALAAARDVVTIGMTGSWHPADVTEDNTKLLGTALSGSSFSKSVGDKRVCYSEVTSLETQVVAGTNYRFHISGCDVTDSDGECSTSALSSCELSGFVVQIFEQSWTNTLKVTNIKAEEAATASSSSTPAPTPASTSTSASSSEETMLQSSVQQRAMFSDFV
The following text describes a protein:
Function:
Required for seed viability.
Subcellular Localization:
Nucleus envelope. Nucleus, nuclear pore complex.
Sequence:
MGIVLEPPCPKSVDGISIDPEPNWNFESLVAEIASVEKKLNGFSMYPQPITNTTLRMGRRGGGFVMHVSEDEMESDEGEESDDEEEEEDHSQICTAGKRFACDELYLSDESDEEFDHEPEYMMNKLGLAESALYEVINDHQTEIKDDIRNQVSVVETEIMNEIETSLSAIARVEKYSETRKEVERKLDLQYQRKVAEALDTHLTAVQREHKIKSQIEERKIRSEEAQEEARRKERAHQEEKIRQEKARAEAQMLAKIRAEEEKKEVERKAAREVAEKEVADRKAAEQKLAEQKAVIESVTGSSATSNAQAGGNSIRAAESALILENHRLKKLEELETTNQSLKSRSNENFSSFEKHIGRVIRQISGTKDSVSGKINDIVKIFKDPRCPVSISIAAFAKKMVTTKEKPNPFACSYVIVYINSQFPQVMDILLAEFHKACIYTVPKHIVNSQSAWDSDAYERLDSIMRLYGALVQTDIRVGNATNVHGIEHGWAWLARFLNKIPANRATATALNSFLQTAGFGLHQRYKSQFLKVVNVVREHFLQKLRAKKDTSDLLVIIAEITAYLDDRMYLKEPEGRAMKTTSTLSSELTAELNQPNYNQNYQRNDYRNYY
The following text describes a protein:
Function:
Insect-immune protein with antimicrobial activity. Forms a protein complex at the bacterial surface. Can inhibit hemocyte aggregation.
Subcellular Localization:
Secreted.
Sequence:
MVSKSIVALAACVAMCVAQPVEKMPVLKDQPAEVLFRESQATVLECVTENGDKDVKYSWQKDGKEFKWQEHNIAQRKDEGSLVFLKPEAKDEGQYRCFAESAAGVATSHIISFRRTYMVVPTTFKTVEKKPVEGSWLKLECSIPEGYPKPTIVWRKQLGEDESIADSILARRITQSPEGDLYFTSVEKEDVSESYKYVCAAKSPAIDGDVPLVGYTIKSLEKNTNQKNGELVPMYVSNDMIAKAGDVTMIYCMYGGVPMAYPNWFKDGKDVNGKPSDRITRHNRTSGKRLFIKETLLEDQGTFTCDVNNEVGKPQKHSVKLTVVSGPRFTKKPEKQVIAKQGQDFVIPCEVSALPAAPVSWTFNAKPISGSRVVASPSGLTIKGIQKSDKGYYGCQAHNEHGDAYAETLVIVA
The following text describes a protein:
Function:
Mannosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the eighth mannose residue in an alpha-1,6 linkage onto Man(7)GlcNAc(2)-PP-dolichol to produce Man(8)GlcNAc(2)-PP-dolichol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MQLDHFDYMVIVMVGFYLTLAPFTKVEESFNMQAIHDIVYFGVSDLSKYDHVDFPGVVPRTFVGAGVLGIIARGLKGAVFKGAMKFDIQLLTRGALGIINAVCFMFLRHSIADFFTLSRYPNLGNIIASFFAAFQFSQFHMIYYASRTLPNMMAMPLVTFALSKAVAGEFESTITLLAVAGSIFRVEILLLTAIFTVLCLVQRRVYLSKAVVAGLKGALIGSTISIGVDSYFWQNGTPSFNPLEQFKLVFPELQGFIFNVIEGNSSEWGVSPYSQYFLVDLPKLILNPVVLLLIPYGYIKDPSGKRGHLRLLGLTATIYVAIYSLQPHKEWRFIIYTVPIFTLLAAVGATSIWEKRNTNKIYMVGSVIIILTTFLTFVLSCFMGSISSFNYPGGFALEAFHDLPEVAKHTFHFGERGQAYVDPIMVHVDVPTCMTGAIRFGESEDFTESGAIIYDKTEDKETLEDLWDGFDYVITAEKRPDMDLADTITALTRVDAKEALRTFSAAVKDPSGTANEFVRVLKLAFGEDVNDAYLELEKVWDRIVVTEPALFIYKRKESQEV
The following text describes a protein:
Function:
Catalyzes the reduction of N-oxygenated molecules, acting as a counterpart of cytochrome P450 and flavin-containing monooxygenases in metabolic cycles. As a component of prodrug-converting system, reduces a multitude of N-hydroxylated prodrugs particularly amidoximes, leading to increased drug bioavailability. May be involved in mitochondrial N(omega)-hydroxy-L-arginine (NOHA) reduction, regulating endogenous nitric oxide levels and biosynthesis. Postulated to cleave the N-OH bond of N-hydroxylated substrates in concert with electron transfer from NADH to cytochrome b5 reductase then to cytochrome b5, the ultimate electron donor that primes the active site for substrate reduction.
Subcellular Localization:
Mitochondrion outer membrane; Peripheral membrane protein. Peroxisome.
Sequence:
MGASSSSALARLGLPAQARPRWLGVAVLGLAAVALGAVAWRRAWPRRRRRLQQVGTVAKLWIYPVKSCKGVPVSEAECTAMGLRSGNLRDRFLLVIKEDGHIVTARQEPRLVLVSITYENNCLIFKAPDMDQLVLPSKQPSSNKLHNCRIFGLDIKGRDCGNEAAQWFTNFLKTEVYRLVQFETNMKGRTSRKLLPTLDQNYQVAYPDCSPLLIMTDASLVDLNTRIEKKMKMENFRPNIVVTGCDAFEEDTWDELLIGSVEVKKIMACPRCILTTVDPDTGVIDRKEPLDTLKSYRLCDPSERELYKLSPLFGIYYSVEKIGSLRVGDPVYRMV
The following text describes a protein:
Function:
Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (By similarity).
Sequence:
MKLVTSEEIKRLEERLEREYSIPPILLMENAASFLFSFLKEKFEDIENRKIAILCGPGNNGGDGVALARYLYSNGIRKITIFSYLWGKKISDLLKIQLGLLKNLVEIKDILQDYTELKEYELIVDGIFGIGLKREIDDDLKKIFRYINNLGKKIISIDIPSGINSDTGEIMGEALRADYVLTMFLPKVGLFETGAVDYVGEVIVGRLGIPIEIVNDIVESNIHLVDWELLKDIVRIPSKGVHKGKKGKVLIIGGSFRYTGAPILSALSALRTGAGMVYLAVPEKISMVYRGNYPEIIYIPLKDKDGYISYDNLGYILEIIETYGIEAVAIGPGIGINEDVRRLVQDFLRKVDKKVVVDADALSFVKDILGDISGKDVVFTPHYGEMSRIVEESVETISKKRVEIGRNFVERYKLNLIIKGPNSLFFDPKNHVYVNPFADFLLATAGSGDVLTGIIAGFSAQGYSLKEACILGNFVHGYSSVIWKKYKGSVGLTASDIIKILPLAIDEVIRRRNV
The following text describes a protein:
Function:
Plays a role in promoting the proliferation of synovial fibroblasts in response to pro-inflammatory stimuli.
Subcellular Localization:
Nucleus.
Sequence:
MAILEPAGRAPDPGRAGGGQGGQGLCAAELRAPSTAGSGRQGALWREPRRARGALWRLEADRLLPPLPARLLRAGGGRGMDRNPSPPPPRRDEDADEDVAGGDCIGSTVYSRHWLFGVLSGLIQIVSPENTKSSSDDEEQQMELDEEMENEICRVWDMSMDEDVALFLQEFNAPDIFMGVLAKSKCPRLREICVGILGNMACFQEICVSISNDNNLGQVLLHCLYDSDPPTLLETSRLLLTCLSQTEVASVWVERIREYPAIYDSICFIMSSSTNVDLLVKVGEVVDKLFDLDEKLMLEWIRNGAVQPQDPPQEDSEEQPVFRIVPCVLEAAKQVRSENPEGLDVYMHILQLLTTVDDGIQAIVQCPDTGKDTWNLLFDLVCHEFCQSDDPPIILQEQKTVLASVYSVLSSIYASQAQQEYLKIEEDLPLIDSLIRVLQNMEHCQKKPENSADSNTEETKKSDLTQDDFHLKILKDISCEFLSNIFQVLTKETVARGLKEGQLSKQKCSCAFQNLLPFYSPVIEDFLKILHEVDKTLADDLEESFPNLKVQT
The following text describes a protein:
Function:
Regulator of sister chromatid cohesion in mitosis stabilizing cohesin complex association with chromatin. May antagonize the action of WAPL which stimulates cohesin dissociation from chromatin. Cohesion ensures that chromosome partitioning is accurate in both meiotic and mitotic cells and plays an important role in DNA repair. Required for efficient DNA double-stranded break repair.
Miscellaneous:
MISCELLANEOUS: Named sororin after the Latin word 'soror', which means 'sister', because of its critical role in sister chromatid cohesion.
Subcellular Localization:
Nucleus. Chromosome. Cytoplasm. Note=Associates with nuclear chromatin from S phase until metaphase and is released in the cytoplasm upon nuclear envelope breakdown.
Domain:
The KEN box is required for the association with the APC/C complex.
Sequence:
MSGRRTRSGGAAQRSGPRAPSPTKPLRRSQRKSGSELPSILPEIWPKTPSAAAVRKPIVLKRIVAHAVEVPAVQSPRRSPRISFFLEKENEPPGRELTKEDLFKTHSVPATPTSTPVPNPEAESSSKEGELDARDLEMSKKVRRSYSRLETLGSASTSTPGRRSCFGFEGLLGAEDLSGVSPVVCSKLTEVPRVCAKPWAPDMTLPGISPPPEKQKRKKKKMPEILKTELDEWAAAMNAEFEAAEQFDLLVE
The following text describes a protein:
Function:
Calcium-dependent NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor. May play a role in cell growth and apoptosis; [Isoform v2]: Calcium-dependent NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor. Involved in endothelial generation of reactive oxygen species (ROS), proliferation and angiogenesis and contributes to endothelial response to thrombin. Regulates redox-dependent processes in lymphocytes and spermatozoa; [Isoform v1]: Calcium-dependent NADPH oxidase that catalyzes the generation of superoxide from molecular oxygen utilizing NADPH as an electron donor; [Isoform v5]: This isoform lacks calcium-binding domains and was showed to present a NADPH oxidase activity in a calcium-independent manner. May be involved in endothelial generation of reactive oxygen species (ROS), proliferation and angiogenesis and contribute to endothelial response to thrombin. However another study showed an absence of oxidase activity. Subject to rapid degradation; [Isoform v3]: Lacks calcium-dependent NADPH oxidase activity; [Isoform v4]: Lacks calcium-dependent NADPH oxidase activity.
Subcellular Localization:
[Isoform v2]: Endoplasmic reticulum. Cell membrane; Multi-pass membrane protein. Note=Calcium-sensitive association and dissociation between the N- and C-terminal domains appears to facilitate its localization to the cell membrane; [Isoform v5]: Endoplasmic reticulum.
Domain:
[Isoform v2]: The C-lobe of the N-terminal calmodulin-like regulatory EF-domain acquires a folded and ordered structure upon calcium binding, and as a consequence, it is able to bind the C-terminal catalytic dehydrogenase domain, triggering enzyme activation; [Isoform v1]: The C-terminal catalytic dehydrogenase domain mediates its homooligomerization; [Isoform v3]: Absence of enzyme activity may be because the third EF-hand domain is interrupted by an insert; [Isoform v4]: Absence of enzyme activity may be because the third EF-hand domain is interrupted by an insert; [Isoform v5]: Absence of enzyme activity may be due to absence of EF-hand domains.
Sequence:
MNTSGDPAQTGPEGCRGTMSAEEDARWLRWVTQQFKTIAGEDGEISLQEFKAALHVKESFFAERFFALFDSDRSGTITLQELQEALTLLIHGSPMDKLKFLFQVYDIDVCARQGASAGTEWGAGAGPHWASSPLGTGSGSIDPDELRTVLQSCLRESAISLPDEKLDQLTLALFESADADGNGAITFEELRDELQRFPGVMENLTISAAHWLTAPAPRPRPRRPRQLTRAYWHNHRSQLFCLATYAGLHVLLFGLAASAHRDLGASVMVAKGCGQCLNFDCSFIAVLMLRRCLTWLRATWLAQVLPLDQNIQFHQLMGYVVVGLSLVHTVAHTVNFVLQAQAEASPFQFWELLLTTRPGIGWVHGSASPTGVALLLLLLLMFICSSSCIRRSGHFEVFYWTHLSYLLVWLLLIFHGPNFWKWLLVPGILFFLEKAIGLAVSRMAAVCIMEVNLLPSKVTHLLIKRPPFFHYRPGDYLYLNIPTIARYEWHPFTISSAPEQKDTIWLHIRSQGQWTNRLYESFKASDPLGRGSKRLSRSVTMRKSQRSSKGSEILLEKHKFCNIKCYIDGPYGTPTRRIFASEHAVLIGAGIGITPFASILQSIMYRHQKRKHTCPSCQHSWIEGVQDNMKLHKVDFIWINRDQRSFEWFVSLLTKLEMDQAEEAQYGRFLELHMYMTSALGKNDMKAIGLQMALDLLANKEKKDSITGLQTRTQPGRPDWSKVFQKVAAEKKGKVQVFFCGSPALAKVLKGHCEKFGFRFFQENF
The following text describes a protein:
Function:
Catalyzes the NADPH dependent reduction of L-gamma-glutamyl 5-phosphate into L-glutamate 5-semialdehyde and phosphate. The product spontaneously undergoes cyclization to form 1-pyrroline-5-carboxylate.
Miscellaneous:
MISCELLANEOUS: Present with 6920 molecules/cell in log phase SD medium.
Sequence:
MSSSQQIAKNARKAGNILKTISNEGRSDILYKIHDALKANAHAIEEANKIDLAVAKETGLADSLLKRLDLFKGDKFEVMLQGIKDVAELEDPVGKVKMARELDDGLTLYQVTAPVGVLLVIFESRPEVIANITALSIKSGNAAILKGGKESVNTFREMAKIVNDTIAQFQSETGVPVGSVQLIETRQDVSDLLDQDEYIDLVVPRGSNALVRKIKDTTKIPVLGHADGICSIYLDEDADLIKAKRISLDAKTNYPAGCNAMETLLINPKFSKWWEVLENLTLEGGVTIHATKDLKTAYFDKLNELGKLTEAIQCKTVDADEEQDFDKEFLSLDLAAKFVTSTESAIQHINTHSSRHTDAIVTENKANAEKFMKGVDSSGVYWNASTRFADGFRYGFGAEVGISTSKIHARGPVGLDGLVSYQYQIRGDGQVASDYLGAGGNKAFVHKDLDIKTVTL
The following text describes a protein:
Function:
Pectinolytic enzymes consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MKKYLLSLLAAVTYTTAQSVSGSAEGFASGVTGGGGATPVYPADTAELESLLSSEGEQVIVLTKTYDFTGTSATGTACYSWGTGEGCQLILQDDCGDTPSTTVTYDAAGKTPIPVASDKTLLGVGSEGVIKGKGLSFTDNVSNIIVQNIKITELNPEYVWGGDALTFDGSSNICIDHVETSLIGRVHYVFGYNPNSGITLSNNFINGETTYSTSCDGYQYWGLELVGKNDSITFKGNYLYKTSGRSPALSGSTKFHACNNVWSDNNGHAIEGNEKGQGLFEGNVFQEVATVVSSTFWEAGDLFLSSADGTGNDACASYIGRNCASSIYMNDGGDYTSYTDVSWLGDWSGLTIAECAEAREIEGTVPTSAGNTL
The following text describes a protein:
Function:
Involved in the catabolism of monoamine ethanolamine. Catalyzes the ATP-dependent gamma-glutamylation of ethanolamine. No activity with polyamines. No complementation of the L-glutamine auxotrophy of an E.coli glnA mutant. Enables survival of S.coelicolor under high local environmental ethanolamine conditions. May play a role during starvation conditions to limit intracellular ethanolamine concentration, which in excess is toxic to the cells.
Sequence:
MSPGQKEALPVADRTPPLGVEELHALVAAGDIDTVVLAFPDMQGRLQGKRFAARFFLDEVLEHGTEGCNYLLAVDADMNTVDGYAMSSWDRGYGDFAMRADPATLRRLPWNEGTAMAVADLAWEDGSPVLAAPRQILRRQLERLAGHGYTAQVGTELEFIVFRDTYEHAWDANYRGLTPANQYNVDYSVLGTGRVEPLLRRIRNEMAGAGLTVESAKGECNPGQHEIAFRYDEALVTCDQHAVYKTGAKEIAAQEGMSLTFMAKYNELEGNSCHIHLSLADADGRNAMAEGGGMSDVMRHFLAGQLVALREFSLLYAPHINSYKRFQPGSFAPTAVAWGHDNRTCALRVVGHGRSLRFENRLPGGDVNPYLAVAGLVAAGLHGIEQRLELPEPCPGNAYTADFAHVPTTLREAAELWENSTLAKAAFGDEVVAHYRNMARVELDAFDAAVTDWELRRSFERM
The following text describes a protein:
Function:
Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(FEM1B) complex specifically recognizes proteins ending with -Gly-Leu-Asp-Arg, leading to their ubiquitination and degradation.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MALDGLAGYVYKAAAEGRVLTLAALLLHRTEPEIRTLLSTVTQHGGQRSTPLIIAARNGHSKVVRLLLEHYKVDVQQTGTVRFDGYIIDGATALWCAAGAGHYEVVKLLVSHEANVNHTTVTNSTPLRAACFDGRLDIVRFLVENNANISIANKYDNTCLMIAAYKGHSDVVHYLLRQHADPNARAHCGATALHFAAEAGHLDIVRELVKWKAAMVVNGHGMTPLKVAAESCKADVVELLLAHSDCDAKSRIEALELLGASFANDRENYNITKTYQYLYLAMLERFRDPSNILHKEVLPPIEAYGMRTECRNPQELGAILHNTDDLHLEGLIVRERILGSDNIDVSHPIIYRGAVYADNMQFEQCIKLWLHALQLRQKGNRNTHKDLLRFAQVFSQMIHLNEPVKSRDVERVLECSVLEIERGIARIQNPQEPDAHSTLENHECNLYTFLYLVCISTKTCCSEEEQPCINKQIYRLVHLDPRTREGGSLLHLAVDSGTPVDDFHTNDVCSFPSAPVAKLLIDCGANVNAVDQMGNSPLHVIVQYNRPISDFLTLHAIIISLVEAGAHTDMTNKEKKTPLDRSTTGVSEILLKTQMKLSLKCLAARAVRLHNIKYQNQIPRTLEEFVEFH
The following text describes a protein:
Function:
Plays an important role in the functional organization of mitotic chromosomes. Exhibits low basal ATPase activity, and unable to polymerize.
Subcellular Localization:
Nucleus.
Sequence:
MGSALTTKKLVIIHPGSKHLRIGRASDVNPHTILHAIARPRRKNGPLHRDPVLIPTVVLSKENKVLVDETYQSMRGTLQSCLRSDGTPRPATSVQQVATSNKQCTPIQGSISKLQLVTKSEVEDYIIGDQVLYVHPMDQFNVHFPFRHGDLNIHSGVGGSLSSVLADLETIWGHCIVNLLEIPKSELKHYRAVLVIPDIYNRLFLKELVSLLLTHLGFGGCFLLQDHVAATFGAGLGAACVVDLGDQKTSVSCVEDALSQRATRIRLDYGGSDITQSFHYLLQRAGFPYKECQPQHPLDGALLTRIKEGYCHLNLDFCGLRDVNFVVERPGVSTLRYHVKVGDELLLAPLGLFNTEVFALTGQDKRGQGQANASGDPEDPHDANYLRETSRRAHKEALENQSASAASMDTAENSTNTGGQGEEDLVVDSLAADAAPDDQPQQQLLYSLDQAILHSIERCSSDEMKRRMYSCILLVGGGAKFEGLSTWLHNRLLLQIPFQFRPEQTEIIVGPKEMDPSMVAWKGAAIMSCLESAQELWIRPAEWKKIGVRLLRERAPFYW
The following text describes a protein:
Function:
Uptake of Fe(2+) ions across the membrane.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MFVPFLIMFREGLEAALIVSLIASYLKRTQRGQWMGAVWVGVVVAAVLCLAIGIFINETTGEFPQKQQELFEGIIAVVAVCILTYMVFWMRKVSKSVKVHLEGAIDNALNSGRGQGWALVAMVFFAVAREGLESVFFLLAAFQQDVGIGAPIGAILGLVCAILVGMAIYWGGVKLHLAKFFKWTSLFILFVAAGLAAGAIRAFHEAGLWNHFQDIAFDLTDVLSTHSLLGTFLEGMFGYQEAPTVSEVSVYFIYLIPALILFFLPPRSTAGSAIAAARKINP
The following text describes a protein:
Function:
Bifunctional DNA N-glycosylase with associated apurinic/apyrimidinic (AP) lyase function that catalyzes the first step in base excision repair (BER), the primary repair pathway for the repair of oxidative DNA damage. The DNA N-glycosylase activity releases the damaged DNA base from DNA by cleaving the N-glycosidic bond, leaving an AP site. The AP lyase activity cleaves the phosphodiester bond 3' to the AP site by a beta-elimination. Primarily recognizes and repairs oxidative base damage of pyrimidines.
Subcellular Localization:
Nucleus. Mitochondrion.
Sequence:
MIKTRLRSGAAAAKRISTLTPDVSAVKTKKKSNQSQANGGEDKPRVKEDILEQATSSKKVSQRKARSVPVKIEYSDGALKEEHSAGASPYFTWKPDNWEQVLSNIRQMRQEREAPVDTMGCDKCPDQTLPEKLVRYQLLVSLMLSSQTKDEVTHAAVGRLRDFGLTPEVVSAAEEKQLEELIYPVSFYKNKAKHLKRTSQVLLDEYDGDIPDSIEGLCKLPGVGPKMSYLAMSCGWKRTVGIGVDTHVHRISNWLGWLPQATKTPEQTRKALEAWLPRDLWDEVNLLLVGFGQTVCKPVAPKCSSCLNLQLCPYGRKQVNSKKEAT
The following text describes a protein:
Function:
Essential for the assembly of the mitochondrial F1-F0 complex. May interact with the alpha and/or beta subunits of F1-ATPase.
Miscellaneous:
MISCELLANEOUS: Present with 2840 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion.
Sequence:
MWRLTRKIGTRIHISNQLSPIFNKAIGTVPVFRFYSSSPEQKYRKKLLEEAQKQGFNSIEELKNHLKETIESKKREFNKIDPLKELEDYQQKTQMENNNSKHLMTKSRSPLDPSAPKVPFKTLDSFLDVGKLKDLSKQEVEFLWRARWAQKDNTLCAVIPVSVYDKMMANARNNPIFVLPLPRQVQSEDAKPNEEQGMELHYIQWQFVGPQTTHCMMTSLAEYKLHQEFARPHTTLQFHSDLVKDKGIVFMNGHVEPDTNVNVQDAQLLLLNVQRFYGAMGEETPVAKQRVQLLRDFSKASPGFTVEKLISLSQSMEN
The following text describes a protein:
Function:
Required for efficient assembly of cytochrome c oxidase in the mitochondrial inner membrane. Seems to be involved in the SHY1-mediated step of cytochrome c oxidase maturation. May aid in stabilizing an early COX1 intermediate containing the nuclear subunits COX5A and COX6.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Note=Mitochondrial matrix soluble protein partially associated with the inner membrane.
Sequence:
MRAVTRNKIVNNLYFSTFLIAFASVAIGSVLPCPAHSVDSDSPAVQQHKLQLAHEQELKRKDALSKKI
The following text describes a protein:
Function:
Converts guanine to guanosine monophosphate, and hypoxanthine to inosine monophosphate. Transfers the 5-phosphoribosyl group from 5-phosphoribosylpyrophosphate onto the purine. Plays a central role in the generation of purine nucleotides through the purine salvage pathway (By similarity).
Subcellular Localization:
Endoplasmic reticulum.
Sequence:
MDPVRLYYSYNDIHKMCAQQAEKILETFRPDVIIAIGGGGFIPARILRTFLKKKGSKNIPIQAIGLSLYEELVSDSPEEVPGLEVKRTQWLDFSTLGMVDLVGKNILIVDEVDDTRTTLHYALRELQRDVAEQAKKLNREGEKTTFGIFVVHNKVKPKNAQLDKEILDKYYFTGCNTPDCWIMYPWEAQDIEEHDSHVAKMGDLKP
The following text describes a protein:
Function:
DNA-binding component of the Fanconi anemia (FA) core complex. Required for the normal activation of the FA pathway, leading to monoubiquitination of the FANCI-FANCD2 complex in response to DNA damage, cellular resistance to DNA cross-linking drugs, and prevention of chromosomal breakage. In complex with CENPS (MHF heterodimer), crucial cofactor for FANCM in both binding and ATP-dependent remodeling of DNA. Stabilizes FANCM. In complex with CENPS and FANCM (but not other FANC proteins), rapidly recruited to blocked forks and promotes gene conversion at blocked replication forks. In complex with CENPS, CENPT and CENPW (CENP-T-W-S-X heterotetramer), involved in the formation of a functional kinetochore outer plate, which is essential for kinetochore-microtubule attachment and faithful mitotic progression. As a component of MHF and CENP-T-W-S-X complexes, binds DNA and bends it to form a nucleosome-like structure. DNA-binding function is fulfilled in the presence of CENPS, with the following preference for DNA substates: Holliday junction > double-stranded > splay arm > single-stranded. Does not bind DNA on its own.
Subcellular Localization:
Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore. Note=Assembly of CENPS and CENPX and its partner subunits CENPT and CENPW at centromeres occurs through a dynamic exchange mechanism. Although exchange is continuous in the cell cycle, de novo assembly starts principally during mid-late S phase and is complete by G2. CENPX being less stably bound at the kinetochore than CENPS.
Sequence:
MEETGAVFRKELVSKLLHLHFKDKKTKVSGDALQLVAELLKIFVVEAAIRSVRQAQAEGLAHVDVEQLEKVLPQLLLDF
The following text describes a protein:
Function:
The phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS), a major carbohydrate active transport system, catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The enzyme II LacEF PTS system is involved in lactose transport.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The EIIC type-3 domain forms the PTS system translocation channel and contains the specific substrate-binding site; The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on a cysteinyl residue. Then, it transfers the phosphoryl group to the sugar substrate concomitantly with the sugar uptake processed by the PTS EIIC type-3 domain.
Sequence:
MNKVFDKLKPVFEAIAANKYISAIRDGFIACMPIIIFSSIFMMVAYVPNAWGFYWPDNVTNTLMVAYNYSMGLLALFVAGTTAKNLTDSKNLELPKTNQINPVAVIVASEISFVILSILPLKTGVDLTYMGTQGLICAYIVGLIVPNIYYVCIKNNVTIKLPEQVPGNIAQSFKDLIPMGLSVTAFWLFGVGFKAATGTVLPRWIIQVLSPLFQASDSYLGLALIAGAMAFFWFCGVQGPSIVQPAVVPIMIANTAANLQQYQAGQHVSHVLAMNTMDYVMNFGGTGATLVVPFIMLFAARSAQLKAVGKAAFVPCTFGVNEPVLFGMPIIMNPMLFIPFLATPIVNVCLFKFFVSVLGMNSMMYTMPWTVPGPIGILISTGFAPLAFVFVLLTLVLDVAIYFPFIRVYDSTLLAEEKAKEEVIEDDGMAVLASDTVSPSIPTGLTVATATDDDATHVLPETAPSAHGEAYFKQNEVDVLVLCAGGGTSGILANALNKLSKERGLKLSAAARAYGQDMDLIKDMNMVILAPQMESMKGNLKKITDKYGVKLVTTTGRQYIELTNNGDMALDFVESNL
The following text describes a protein:
Function:
Component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation.
Subcellular Localization:
Cytoplasm.
Sequence:
MTVSQIPTHGEIQALLSTSAYDPAIVSKLEAYVRAQVSSVASSLESDAQYSFEANRTLVKLYQFFPHLEGELGMTVTALAAFLALLQFPETDFMALGCLIPERVQSMEPCATLVRCAELLESCQFSEFWPEFRKLGIPEYGARDNETVVSDDRKLLSNAVNGSSASNQIRINMIQMLARTYRSAPLSSVLGALDLKDVESLKGFSSKVMLVAGGGEGEVTGTENEIPIVEKIEGDLLLLPRRLRIARGLGQLSRRG