lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Involved in the metabolism of aliphatic and aromatic oximes. Involved in the biosynthesis of both short-chain and long-chain aliphatic glucosinolates.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MEDIIIGVVALAAVLLFFLYQKPKTKRYKLPPGPSPLPVIGNLLQLQKLNPQRFFAGWAKKYGPILSYRIGSRTMVVISSAELAKELLKTQDVNFADRPPHRGHEFISYGRRDMALNHYTPYYREIRKMGMNHLFSPTRVATFKHVREEEARRMMDKINKAADKSEVVDISELMLTFTNSVVCRQAFGKKYNEDGEEMKRFIKILYGTQSVLGKIFFSDFFPYCGFLDDLSGLTAYMKECFERQDTYIQEVVNETLDPKRVKPETESMIDLLMGIYKEQPFASEFTVDNVKAVILDIVVAGTDTAAAAVVWGMTYLMKYPQVLKKAQAEVREYMKEKGSTFVTEDDVKNLPYFRALVKETLRIEPVIPLLIPRACIQDTKIAGYDIPAGTTVNVNAWAVSRDEKEWGPNPDEFRPERFLEKEVDFKGTDYEFIPFGSGRRMCPGMRLGAAMLEVPYANLLLSFNFKLPNGMKPDDINMDVMTGLAMHKSQHLKLVPEKVNKY
The following text describes a protein:
Function:
Reversibly inhibits the activity of ATP2A2/SERCA2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Binds preferentially to the ATP-bound E1 conformational form of ATP2A2 which predominates at low Ca(2+) concentrations during the diastolic phase of the cardiac cycle (By similarity). Inhibits ATP2A2 Ca(2+) affinity by disrupting its allosteric activation by ATP (By similarity). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN. ATP2A2 inhibition is alleviated by PLN phosphorylation (By similarity). Also inhibits the activity of ATP2A3/SERCA3 (By similarity). Controls intracellular Ca(2+) levels in elongated spermatids and may play a role in germ cell differentiation (By similarity). In the thalamic reticular nucleus of the brain, plays a role in the regulation of sleep patterns and executive functioning (By similarity).
Miscellaneous:
MISCELLANEOUS: For practical reasons, PLN activity is most often studied with ATP2A1 instead of ATP2A2.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Sarcoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. Membrane; Single-pass membrane protein. Note=Colocalizes with HAX1 at the endoplasmic reticulum. Colocalizes with DMPK at the sarcoplasmic reticulum.
Sequence:
MEKVQYLTRSAIRRASTIEMPQQARQKLQNLFINFCLILICLLLICIIVMLL
The following text describes a protein:
Function:
Catalyzes the removal of a penultimate prolyl residue from the N-termini of peptides. In the food vacuole, involved in the final step of host hemoglobin catabolism, by cleaving hemoglobin-derived oligopeptides. In the cytoplasm, may be involved in the last steps of the turnover of ubiquitinated proteins (Probable).
Subcellular Localization:
Vacuole lumen. Cytoplasm. Note=Localizes to the digestive (or food) vacuole, an acidic vacuole where host hemoglobin is digested.
Sequence:
MQLNFLLFVFIFLMVFHLNIFNKGKRQNLVSAYLNHFKKSYFSGVTSGSDCVNKSEVSSDNNNNNNNNNNKIAHNFFSKKYQRNFENNNLSENQENNKNIIYSGSNIFKNIYNTEMMSNNNTVDVNMMDNNPAARLEELRTIMKKNKIDVYILINSDEHNSEIINEKDKKIVKITNYSGADGILIVTKDKPILYVNALYELQAMNELDQNLFTLRISRIDNRDEIFETISSLEFNTIAFDGKNTSVVFYEKLRKALLNAYPKKKIVEKIIYNNNFDDVNKKDDENVLNFLVLEKSLVEIKDYPVNNKTLYIHDRKYNGACAGEKIDKLKQSLMYDIKNVDNLLLSELDEIAYLLNLRGYDYQYSPLFYSYLLFQFDREEQDFSKIVFFTTVKNLPADVKNLLEINKVIVKEYEEIVPYLRDVVIPSIPKHNDDNPDFKKYDISLSPYINLMIYKLFDRKNVLLQNSPVVKMKAVKNDVEIDNMKQAHILDGLALLQFFHWCEQKRKTKELFNETEMSLRHKVDYFRSTKKNFIFPSFSTISASGPNAAVIHYECTDKTNATIKPAIYLLDSGGQYLHGTTDVTRTTHFGEPTAEEKRIYTLVLKGHLRLRKVIFASYTNSSALDFIARENLFNNFMDYNHGTGHGVGLTLNVHEGGCSIGPVGGAPLKKNMVLSNEPGYYMKDKFGVRIENMQYVISKEITDTTEYLSFDDLTMYPYEKKLLDFSLLTNQEIKELNEYHTTIRNTLLPLVKQSPQEYGESVEKYLIEITEPIAIHNN
The following text describes a protein:
Function:
Zinc metalloprotease that mediates intramembrane proteolysis of proteins such as ATF6, ATF6B, SREBF1/SREBP1 and SREBF2/SREBP2. Catalyzes the second step in the proteolytic activation of the sterol regulatory element-binding proteins (SREBPs) SREBF1/SREBP1 and SREBF2/SREBP2: cleaves SREBPs within the first transmembrane segment, thereby releasing the N-terminal segment with a portion of the transmembrane segment attached. Mature N-terminal SREBP fragments shuttle to the nucleus and activate gene transcription. Also mediates the second step in the proteolytic activation of the cyclic AMP-dependent transcription factor ATF-6 (ATF6 and ATF6B). Involved in intramembrane proteolysis during bone formation. In astrocytes and osteoblasts, upon DNA damage and ER stress, mediates the second step of the regulated intramembrane proteolytic activation of the transcription factor CREB3L1, leading to the inhibition of cell-cycle progression.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MDLIFGLMTIAAIYLWVLFMDRFFKSCSHYGYIQFLKGTGLEIKLFQFSWTTTAFNKLLLKWGSHNTKFLNLWFNLGLCVSLVLLPASIYLLLVAFFQNFLSSASGEESIIQPVVPGINLPASEMGYYSLTLLISSVLHELGHALGAVQEDVNVINVGANVIFILPVAYVNLNSDKLFSLNPWKRLKILCAGVWHNLLIALVAYLLYTSLPSVFSPFFNFGKGVVVTEFEAKSPIFGNRGLNVGDLILKINDCEVDDENAWYKCLVALRTKKPAFCIEGDVVRDLDESVHLKHSESGIVSCCHSENKGKLCFEYLDSKDSILELPPYACLPGRPAIEASTNFCISDPHVCPKDTYCFRPILTNNTNLFKIKRVNKNDVIYIGPVSDLVRTVTVSSYVPKYSFLGTRIPDVTTKFLGYLAMFSMGLALVNILPCLFMDGQHITNTLFHIIFASHLRTTHIKIISGVVTASFTLLLVIHCVIVIWTRLN
The following text describes a protein:
Function:
Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MERKQSSKLNIAFIHPDLGIGGAERLIVDAAVELASHGHSVHIFTAHHDKNRCFEETRAGIFPVTVYGDFLPRHIFYRLHAVCAYLRCMFVALCVLFMWPSYDVIVADLVSVVIPLVKLKKSTKVVFYCHFPDLLLARHTTFLRRMYRKPIDFIEELTTGMADMILVNSRFTASIFAKTFKHLHARGIRPAVLHPAVNVDQFEKPHSYKLNFLSINRFERKKNIDLAVSAFAMLHTLEGNIHQTSNLADANLTIAASNTVVLQCQYKQVRKSVTGRTLVIIVGCTPGIPLKRIIVIQGFHLTSQHVLCGYDRRLRENVEYLEELKSLAEREGVADRVNFVTSCSTAERNSLLSQCLCVLYTPTDEHFGIVPLEAMAAQKPVIACNSGGPVETIKNGETGFLCDPTPKDFALAMAKLIQDPEMAKRLGEQARQHVNESFSTRIFGQRLNQFLLDVAGNKQD
The following text describes a protein:
Function:
Unmethylated CpG islands (CGIs)-binding protein which localizes to H3K4me3-decorated CGIs, where it acts as a transcriptional repressor. Tethers L3MBTL3 to chromatin and interacts with the KDM1A histone demethylase complex to modulate H3K4me2 and H3K4me3 levels at CGIs. Plays a role in atherogenesis by binding with LDL on cell surface and promoting LDL oxidation which leads to the formation of foam cell.
Subcellular Localization:
Nucleus. Chromosome. Secreted. Note=In atherosclerotic lesions, it is found in the extracellular compartment and in foam cells cytoplasm.
Domain:
Winged-helix (WH) domain directly recognizes and binds unmethylated CpG-containing DNA via simultaneous interactions with both the major and the minor groove of DNA.
Sequence:
MAGPPALPPPETAAAATTAAAASSSAASPHYQEWILDTIDSLRSRKARPDLERICRMVRRRHGPEPERTRAELEKLIQQRAVLRVSYKGSISYRNAARVQPPRRGATPPAPPRAPRGAPAAAAAAAPPPTPAPPPPPAPVAAAAPARAPRAAAAAATAPPSPGPAQPGPRAQRAAPLAAPPPAPAAPPAVAPPAGPRRAPPPAVAAREPPLPPPPQPPAPPQQQQPPPPQPQPPPEGGAVRAGGAARPVSLREVVRYLGGSGGAGGRLTRGRVQGLLEEEAAARGRLERTRLGALALPRGDRPGRAPPAASARPSRSKRGGEERVLEKEEEEDDDEDEDEEDDVSEGSEVPESDRPAGAQHHQLNGERGPQSAKERVKEWTPCGPHQGQDEGRGPAPGSGTRQVFSMAAMNKEGGTASVATGPDSPSPVPLPPGKPALPGADGTPFGCPPGRKEKPSDPVEWTVMDVVEYFTEAGFPEQATAFQEQEIDGKSLLLMQRTDVLTGLSIRLGPALKIYEHHIKVLQQGHFEDDDPDGFLG
The following text describes a protein:
Function:
Negative regulator of sigma-B activity. Dephosphorylates RsbS. Plays a role both in maintaining low sigma-B activity during growth and in reestablishing prestress sigma-B activity after induction. Could have a negative feedback role by indirectly communicating sigma-B protein levels.
Sequence:
MIQVEENEHIQTLVYQLNKEGKSICGDSFFMKADDKELICAVADGLGSGSLANESSAAIKDLVENYASEDVESIIERCNQAMKNKRGATASILKINFEQRQFTYCSVGNVRFILHSPSGESFYPLPISGYLSGKPQKYKTHTATYEKGSKFIIHTDGLNVPDIRSHLKKGQSVEEISNSLKMYTTSRKDDLTYILGQLS
The following text describes a protein:
Function:
DNA-dependent RNA polymerase which catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular Localization:
Nucleus.
Sequence:
MEALRIAEAELTVYVHPSNAKRVRHAVNRQLSSLLFTYDDRFNGVVLMHEVAFHLGQGNEGEPNKDESGGPKDESGEPKSCAKGKIKDGRGEPKSCVKGKTKDKSSEPKDESGKPKICIKGKIMNGLVPYFGVQVQAQLLLFSPQPDMILEGKVEMLGKESIHAIVLGLFSVAIMSEDIHEKFRFKRKSDRGKYVSRTDKHHVIKRGTMIRFSVKRVDTEMNCHITGSLIPPHTGCMRWLSVHDTEYASELKSGESRPRDTSIKFEQNEQEHRILKNEDGMVKSERPHKSRKRRHTEE
The following text describes a protein:
Function:
Binds to human plasminogen (and plasmin) via its kringle repeats. Also binds to albumin, immunoglobulin G and fibrinogen. Could provide the bacteria with a mechanism for invasion, as streptococcal-bound plasmin could permit tissue penetration.
Miscellaneous:
MISCELLANEOUS: PAM has more than one binding site for plasminogen; it is thought that each of the a-repeats can bind one plasminogen molecule.
Subcellular Localization:
Secreted, cell wall; Peptidoglycan-anchor.
Sequence:
RKLKTGTASVAVALTVVGAGLASQTEVKANRADDARNEVLRGNLVRAELWYRQIQENDQLKLENKGLKTDLREKEEELQGLKDDVEKLTADAELQRLKNERHEEAELERLKSERHDHDKKEAERKALEDKLADKQEHLNGALRYINEKEAEAKEKEAEQKKLKEEKQISDASRQGLRRDLDASREAKKQVEKDLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKGLANLTAELDKVKEEKQISDASRQGLRRDLDASREAKKQVEKALEEANSKLAALEKLNKELEESKKLTEKEKAELQAKLEAEAKALKEQLAKQAEELAKLRAEKASDSQTPDAKPGNKAVPGKGQAPQAGTKPNQNKAPMKETKRQLPSTGETT
The following text describes a protein:
Function:
Glycosyltransferase that specifically catalyzes mannosylation of cytoplasmic tRNA(Asp) modified with queuosine at position 34 (queuosine(34)). Mannosylates the cyclopentene moiety of queuosine(34) in tRNA(Asp) to form mannosyl-queuosine(34).
Sequence:
MSCAKPHILIIEPFYGGSHKQLIGALIEGLNHGDSEIFSLPAKKWHWRARTSALHFAQLIPRDHAFRVLFASSVLSLAELIGLRPDLAACRKIVYFHENQLIYPVREVKQRDCQYGFNEILSCLAADMVLFNSQFNCNSFLDNVQPFLNMQPDFKIKHIREQIEKKCQVLYFPVNFERFPIRKECVKGETAEDLDEKCIHLIWPHRWEHDKNPKLLVDTLCQLHERQVDFKVTICGESYQEIPEEFEHIQEKLGSKLVNFGHLEREEYLKTLLTGDIVISTADHEFFGVAMLEAAFCGCYPIAPNKLVYPEIYPKENLYNTSNALTKKLYNFCRMPRVFRKQRDQFFENFNFDRFSAKELVPKYLDIFNKHIADEQS
The following text describes a protein:
Function:
Participates in the formation of new permeability pathways in Plasmodium-infected erythrocytes enabling the uptake of nutrients from the blood plasma.
Subcellular Localization:
Host cell membrane; Single-pass membrane protein. Host cell membrane; Peripheral membrane protein; Cytoplasmic side. Host cytoplasm. Cytoplasmic vesicle, secretory vesicle, rhoptry.
Sequence:
MVSFFKTPIFILIIFLYLNEKVICSINENQNENDTISQNVNQHENINQNVNDNDNIEQLKSMIGNDELHKNLTILEKLILESLEKDKLKYPLLKQGTEQLIDISKFNKKNITDADDETYIIPTVQSTFHDIVKYEHLIKEQSIEIYNSDISDKIKKKIFIVRTLKTIKLMLIPLNSYKQNNDLKSALEELNNVFTNKEAQEESSPIGDHGTFFRKLLTHVRTIKENEDIENKGETLILGDNKIDVMNSNDFFFTTNSNVKFMENLDDITNQYGLGLINHLGPHLIALGHFTVLKLALKNYKNYFEAKSIKFFSWQKILEFSMSDRFKVLDMMCDHESVYYSEKKRRKTYLKVDRSNTSMECNILEYLLHYFNKYQLEIIKTTQDTDFDLHGMMEHKYIKDYFFSFMCNDPKECIIYHTNQFKKEANEENTFPEQEEPNRQISAFNLYLNYYYFMKRYSSYGVKKTLYVHLLNLTGLLNYDTRAYVTSLYLPGYYNAVEMSFTEEKEFSKLFESLIQCIEKCHSDQARQISKDSNLLNNITKCDLCKGAFLYANMKFDEVPSMLQKFYVYLTKGLKIQKVSSLIKTLDIYQDYSNYLSHDINWYTFLFLFRLTSFKEIAKKNVAEAMYLNIKDEDTFNKTVVTNYWYPSPIKKYYTLYVRKHIPNNLVDELEKLMKSGTLEKMKKSLTFLVHVNSFLQLDFFHQLNEPPLGLPRSYPLSLVLEHKFKEWMNSSPAGFYFSNYQNPYIRKDLHDKVLSQKFEPPKMNQWNKVLKSLIECAYDMYFEQRHVKNLYKYHNIYNINNKLMLMRDSIDLYKNNFDDVLFFADIFNMRKYMTATPVYKKVKDRVYHTLHSITGNSVNFYKYGIIYGFKVNKEILKEVVDELYSIYNFNTDIFTDTSFLQTVYLLFRRIEETYRTQRRDDKISVNNVFFMNVANNYSKLNKEEREIEIHNSMASRYYAKTMFAAFQMLFSTMLSNNVDNLDKAYGLSENIQVATSTSAFLTFAYVYNGSIMDSVTNSLLPPYAKKPITQLKYGKTFVFSNYFMLASKMYDMLNYKNLSLLCEYQAVASANFYSAKKVGQFLGRKFLPITTYFLVMRISWTHAFTTGQHLISAFGSPSSTANGKSNASGYKSPESFFFTHGLAAEASKYLFFYFFTNLYLDAYKSFPGGFGPAIKEQTQHVQEQTYERKPSVHSFNRNFFMELVNGFMYAFCFFAISQMYAYFENINFYITSNFRFLDRYYGVFNKYFINYAIIKLKEITSDLLIKYEREAYLSMKKYGYLGEVIAARLSPKDKIMNYVHETNEDIMSNLRRYDMENAFKNKMSTYVDDFAFFDDCGKNEQFLNERCDYCPVIEEVEETQLFTTTGDKNTNKTTEIKKQTSTYIDTEKMNEADSADSDDEKDSDTPDDELMISRFH
The following text describes a protein:
Function:
Methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues in some proteins.
Sequence:
MASLPNGAAAASSAAGGAPPVDKEVDFANYFCTYAYLYHQKEMLCDRVRMDAYHSAVFRNPHHFRGKVVLDVGTGSGILAIWSAQAGARKVYAVEATNVAEHARELVRANGVADIVEVIQGTMEDIVLPEKVDVIISEWMGYYLLRESMFDSVICARDRWLNPGGVMYPSHARMWLAPIRSGLGDKKMEDFEIAMNDWNHFVEDTQAYYGVNMNALTKAYRAEHEKFYLKSSIWNNLHPNQLIGQPAVVKEMDCLTATVEEIREVRAQVTLPINQDRTRLAALAGWFDVHFRGSKQNPAVEEVELNTAPDENGGTHWGQQVFLMTPSPRVNEGDSVNVSFSMVRSKENHRLMDMDITYELHEASGRKLPAVATKIFLE
The following text describes a protein:
Function:
Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAPRLQLEKAAWRWTETVPPEAVTQEHIEAAYRVGLEPCQRGTCRRNCRGNPNCLVGIGEHVWLGEIDENSFHNIDDPNCERRKKNAFVGLTNLGATCYVNTFLQMWFLNLELRQALYLCSSNEHAAGESIPKDKDYEPQTICEHLQYLFALLQNSKRRYIDPSGFVKALGLDTGQQQDAQEFSKLFMSLLEDTLSKQKNPDVRNIVQKQFCGEYAYVTVCNQCGRESKLVSKFYELELNIQGHKQLTDCITEFLKEEKLEGDNRYFCETCQSKQNATRKIRLLSLPCTLNLQLMRFVFDRQTGHKKKLNTYIGFSELLDMEPFMEQKNGVYVYELSAVLIHRGVSAYSGHYIAHVKDPQTGEWYKFNDEDIEKMEGKKLQLGIEEDLAEPSKSQTRKPKCGKGTHCSRNAYMLVYRLQTREKSLTVEVPAFLQELVERDNCKFEEWCNEMAEMRKQSVARGKIKHEEVKELYQRLPAEAGSPYDFISLEWLQKWLDESTPPKPIDNTACLCSHGKLHPDKICIMKRISEYVADFFYRRYGGGPRLNVKALCKDCVVERCRILRLKNQLNEDYKTVTNLLKITVKGSEGFWVGKASLRSWRQLALEQLNEQDEDAEHSNGKLNGNAPNKDEVNEEKREEEEELNFNEDIVCPHGDLCISENERRVVSKEAWKKLKQYFPKAPEFPSNKECCSQCKILEREGEENEALHKMMASEQKTSLQNLFHDKCRPCLGSWPQETDELYIVSQFFVEEWRKFVRRPTRCSPVSSLGNSALLCPHGGLMFTYASMTKEDSKLIALIWPSEWERIQKLFVVDHVIKITRTRAAGEPESALYSSEPQLCPECRGGLLCQQQRDLREYTQATIYIHKVVDNKKVMKDAAPELNVSSSEAEEEREENKPEGEQDPDFNQSNGGAKRQKLSHQSYISYQKQGIRRSTRHRKVRGEKALLVSANQTLKELKIQIMHAFSVAPFDQNLLIDGKILSDDTATLGSLGIIPESVILLKADEPIADYAAMDDVMQVCMPEEGFKGTGLLGH
The following text describes a protein:
Function:
Ubiquitin-like modifier involved in autophagosomes formation. May mediate the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton.
Subcellular Localization:
Cytoplasm, cytoskeleton. Membrane.
Sequence:
MYVFAHVTCLCTNQDLNRYPIIEEKEKGCVCEFFVENQDHLLLLKEFDPCPYHINPSFHKGGSSLKLDNDLEKRQAESLRIMEKYPDRIHVIVDKAEKFEIPNIDKKKYLSDLINREILSSVYEEEKDEDGFLYITYSGLLLTFNLIFFTFVTSTKCPPTTPKHPKPPKKDTAVKPTCPTDTLKLGVCADLWAAVCLCTALKANVLGINLNVSVDLSLLLNYCGKKLRYGLQCA
The following text describes a protein:
Function:
Catalyzes conversion of folates to polyglutamate derivatives allowing concentration of folate compounds in the cell and the intracellular retention of these cofactors, which are important substrates for most of the folate-dependent enzymes that are involved in one-carbon transfer reactions involved in purine, pyrimidine and amino acid synthesis.
Sequence:
MSAEGGDGLANPKPSPYEEAMSALSSLITTRTRAEKSNSGDRFDLLFDYVKILELEEPISKLKVIHVAGTKGKGSTCVFTESILRNCGFHTGLFTSPHLMDVRERFLLDGADICQEKFLAYFWWCYDRLKEKTTDDIPMPTYFRFLALLAFKIFSAEQVDVAIMEVGLGGKFDATNVVQAPIVCGISSLGYDHMEILGNTLGLIAGEKAGIFKQGIPAFTVPQPEEAMPVLEENASKLNVNLQVASPLDPNMLNGAHLGLDGEHQFVNAGLAVALCSTWLQRTGHVDVPYHINTSSLPEQFIKGLTTASLQGRAQIVPDQYISSEGPEDLVFYMDGAHSPESMEVCGRWFSHVIKEDEKLVSYAEHQPSDNSSMSFEMARGFHNSTTRKSSTQILLFNCMSVRDPQLLLPRLVKACASHGVQFKQALFVPNVSVYNKVISNVPQPSTRVDLSWQLTLQRVWESLVNADKGGYTKDSGLSPDEAQDETEKGIISSTNSKVFPTLPLAIKWLRDNARQNQSVRVQVLVTGSLHLIGDVLRLIRK
The following text describes a protein:
Function:
GTPase-activating protein for RAC1 and perhaps CDC42, but not for RhoA small GTPase. May attenuate RAC1 signaling in neurons (By similarity).
Domain:
The F-BAR domain mediates oligomerization, binds membranes, and induces plasma membrane protrusions.
Sequence:
MSSQTKFKKDKEIIAEYEAQIKEIRTQLVEQFKCLEQQSESRLQLLQDLQEFFRRKAEIELEYSRSLEKLAERFSSKIRSSREHQFKKDQYLLSPVNCWYLVLHQTRRESRDHATLNDIFMNNVIVRLSQISEDVIRLFKKSKEIGLQMHEELLKVTNELYTVMKTYHMYHAESISAESKLKEAEKQEEKQFNKSGELSMNLLRHEDRPQRRSSVKKIEKMKEKRQAKYSENKLKCTKARNDYLLNLAATNAAISKYYIHDVSDLIDCCDLGFHASLARTFRTYLSAEYNLETSRHEGLDVIENAVDNLDSRSDKHTVMDMCSQVFCPPLKFEFQPHMGDEVCQVSAQQPVQTELLMRYHQLQSRLATLKIENEEVRKTLDATMQTLQDMLTVEDFDVSDAFQHSRSTESIKSAASETYMSKINIAKRRANQQETEMFYFTKFKEYVNGSNLITKLQAKHDLLKQTLGEGERAECGTTRPPCLPPKPQKMRRPRPLSVYSHKLFNGSMEAFIKDSGQAIPLVAESCIRFINLYGLQQQGIFRVPGSQVEVNDIKNSFERGEDPLVDDQNERDINSVAGVLKLYFRGLENPLFPKERFQDLISTIKLENPADRVHPIQQILITLPRVVIVVMRYLFAFLNHLSQYSDENMMDPYNLAICFGPTLMHIPDGQDPVSCQAHVNEVIKTIIIHHEAIFPSPRELEGPVYEKCMAGGEEYCDSPHSEPGTIDEVDHDNGTEPHTSDEEVEQIEAIAKFDYVGRSPRELSFKKGASLLLYHRASEDWWEGRHNGVDGLIPHQYIVVQDMDDAFSDSLSQKADSEASSGPLLDDKASSKNDLQSPTEHISDYGFGGVMGRVRLRSDGAAIPRRRSGGDTHSPPRGLGPSIDTPPRAAACPSSPHKIPLSRGRIESPEKRRMATFGSAGSINYPDKKALTEGLSMRSTCGSTRHSSLGDHKSLEAEALAEDIEKTMSTALHELRELERQNTVKQAPDVVLDTLEPLKNPPGPISSEPASPLHTIVIRDPDAAMRRSSSSSTEMMTTFKPALSARLAGAQLRPPPMRPVRPVVQHRSSSSSSSGVGSPAVTPTEKMFPNSSSDKSGTM
The following text describes a protein:
Function:
Part of the NCT transcriptional regulatory complex that acts as a key regulator of ergosterol biosynthesis and the azole exporter cdr1B. The NCT complex binds the promoters of genes linked to azole susceptibility, and especially represses the expression of cdr1B transporter.
Subcellular Localization:
Nucleus.
Sequence:
MTEQDNSYRPRSPDLSTFQPAIPSPVYQFGNPLAHRTSYDASPFFTPHYQQPPVASARALQQYIPPYPDHSFDADMARRSSRLSRAVEVAPAPAPEMKYEEPKYEEPLYQEPVKPEQPSEPVEHPKLDPAAGIEVKTKFPVARIKRIMQADEDVGKVAQVTPIAVSKALELFMISLVTKAAKEAKDRNSKRVTASHLKQAVAKDEVLDFLADIIAKVPDQPTGRKHEDDGSDQNEQPKRKRGGRRPKDDSD
The following text describes a protein:
Function:
Acts as a component of the essential kinetochore-associated NDC80 complex, which is required for chromosome segregation and spindle checkpoint activity. Required for kinetochore integrity and the organization of stable microtubule binding sites in the outer plate of the kinetochore. The NDC80 complex synergistically enhances the affinity of the SKA1 complex for microtubules and may allow the NDC80 complex to track depolymerizing microtubules.
Subcellular Localization:
Nucleus. Chromosome, centromere, kinetochore.
Sequence:
MTDGGSSQWKRGSPGRGRDPRAVEFARDWPRVVMAAFRDMEEVSQGLLSLLGANRAEAQHRRLLGRHEQVVERLLETQDGAEQRLREILATEKEVAQGLLDAKEQAHRGGTELQQLEAELQKASEEDSRLKASLLRELEELRDIEADLERQERDVDEDTTVTIPSAVYVAQLYHRISKIEWDYECEPGMVKGIHHGPSVAQPLHLDGTQLSKKFVSDYLWSLVDTEW
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:
MIKRAGDVLGALERALTVIAVVFLFVIMLLVVTDVFMRYALNRPFAFTYDLIGLYLLAGVFFFTLSDGLREHAHVGVDILLSRFSPAGRRLSEIITALAGLFVFVLICKVGFERALENYEQHDVLAGAIAWPTWISAALVPFGCGVLVLRLALQLVGNVLSLVSGRDLYPLPPVTGVGETRSFE
The following text describes a protein:
Function:
A acetyltransferase, which acetylates the inositol ring of phosphatidylinositol during biosynthesis of GPI-anchor.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MSQADVGATTEHSSFVGTLTGCAQRELFLTFLITMLGLFIRNLTLPWIFLGRRYDTGRFTYWLKFVADVIFLCVPSLLAMTVLNEHLILLSTIMIIISAVLLIFVLFEAAEQHHNHHQLSVILRQSWSRFVEEQHKPTQFVTYFRSLTMILVTLAILAVDFPIFPRKYAKTEKFGHSMMDVGVAAFLFQAALGSRMAKSPSSGRQLSHHSPRPWYLSSTFLLFALGAGRAVLLEVIGYPQHVTEYGVHWNFFFTMAAIRILSSSILPRCYPLVLSVIFGICHQTMLKSTGLQAWILDESANRRENLITANAEGLTSLMGYLTIFYASLAIGEFMAKTSIRIKSWIRRCFQLFALSLILFFIQIAAEKCVDPPCRRVVNATYIFSQLTLMTFATGVCLSIQMFNTVAWCSSFPQFSNGEDPYSVVSPCLSDSINRHSLLFFLVSNVLTGLVNLSVDAHRQPPHIAFPILLAYVTVCTGLMHFLEYRKIKFATRPHAE
The following text describes a protein:
Function:
Catalyzes the transfer of the gamma-phospho group of ATP to thymidine to generate dTMP in the salvage pathway of pyrimidine synthesis. The dTMP serves as a substrate for DNA polymerase during viral DNA replication. Allows the virus to be reactivated and to grow in non-proliferative cells lacking a high concentration of phosphorylated nucleic acid precursors.
Sequence:
MAEGGFGADSVGRGGEKASVTRGGRWDLGSSDDESSTSTTSTDMDDLPEERKPLTGKSVKTSYIYDVPTVPTSKPWHLMHDNSLYATPRFPPRPLIRHPSEKGSIFASRLSATDDDSGDYAPMDRFAFQSPRVCGRPPLPPPNHPPPATRPADASMGDVGWADLQGLKRTPKGFLKTSTKGGSLKARGRDVGDRLRDGGFAFSPRGVKSAIGQNIKSWLGIGESSATAVPVTTQLMVPVHLIRTPVTVDYRNVYLLYLEGVMGVGKSTLVNAVCGILPQERVTSFPEPMVYWTRAFTDCYKEISHLMKSGKAGDPLTSAKIYSCQNKFSLPFRTNATAILRMMQPWNVGGGSGRGTHWCVFDRHLLSPAVVFPLMHLKHGRLSFDHFFQLLSIFRATEGDVVAILTLSSAESLRRVRARGRKNDGTVEQNYIRELAWAYHAVYCSWIMLQYITVEQMVQLCVQTTNIPEICFRSVRLAHKEETLKNLHEQSMLPMITGVLDPVRHHPVVIELCFCFFTELRKLQFIVADADKFHDDVCGLWTEIYRQILSNPAIKPRAINWPALESQSKAVNHLEETCRV
The following text describes a protein:
Function:
Allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln).
Sequence:
MSVSKKDVEYVAELARLEFKEEEKDSFVNDLNKILNYMEKLDELNTDDVDIVVNPYYIENKYREDNVEKSMELKEVIDNAPESLEEYVIVPKVID
The following text describes a protein:
Function:
Involved in prephenate-dependent formation of 5-hydroxyuridine (ho5U) modification at position 34 in tRNAs, the first step in 5-methoxyuridine (mo5U) biosynthesis.
Sequence:
MKKPELLVTPTSTADILPLIQAGATAFLVGEQRYGLRLAGEFSREDVTKAVEIAHKEGAKVYVAVNAIFHNDKVGELGEYLAFLAEAGVDAAVFGDPAVLMAARESAPDLKLHWSTETTGTNYYTCNYWGRKGAARSVLARELNMDSIVEIKENAEVEIEIQVHGMTCMFQSKRSLIGNYFEYQGKVMDIERKKKESGMFLHDKERDNKYPIFEDENGTHIMSPNDVCIIDELEELIDAGIDSFKIDGVLKMPEYLIEVTKMYREAIDLCVENRDEYEAKKEDWIERIESIQPVNRKIDTGFFFKETVY
The following text describes a protein:
Function:
Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NCOR2 to the androgen response elements/ARE on target genes, negatively regulating androgen receptor signaling and androgen-induced cell proliferation. Transcription activation is also down-regulated by NR0B2. Activated, but not phosphorylated, by HIPK3 and ZIPK/DAPK3.
Miscellaneous:
MISCELLANEOUS: In the absence of ligand, steroid hormone receptors are thought to be weakly associated with nuclear components; hormone binding greatly increases receptor affinity. The hormone-receptor complex appears to recognize discrete DNA sequences upstream of transcriptional start sites; MISCELLANEOUS: Transcriptional activity is enhanced by binding to RANBP9.
Subcellular Localization:
Nucleus. Cytoplasm. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of RACK1.
Domain:
Composed of three domains: a modulating N-terminal domain, a DNA-binding domain and a C-terminal ligand-binding domain. In the presence of bound steroid the ligand-binding domain interacts with the N-terminal modulating domain, and thereby activates AR transcription factor activity. Agonist binding is required for dimerization and binding to target DNA. The transcription factor activity of the complex formed by ligand-activated AR and DNA is modulated by interactions with coactivator and corepressor proteins. Interaction with RANBP9 is mediated by both the N-terminal domain and the DNA-binding domain. Interaction with EFCAB6/DJBP is mediated by the DNA-binding domain (By similarity).
Sequence:
HHQQQQDAATEGSSSGRARRPSGASTSSKDSYLGSTSVISDSAKELCKAVSVSLGLGVEALEHLSSGEQLRGDCMYAPLLGGPPVVRPTPCLPLVECKGSLLDDGPGKGTEETAEYTPFKGGYNKGLEAESLGCSGSGEAGSSGTLELPSTLSLYKSGTLDEAAAYQTRDYYNFPLALAGQPPPPHPRRIKLENPLDYGSAWAAAAAQCRYGDLASLHGGGAAGPGSGSPSTAASSSWHTLFTTEEGQLYGLCGGGGGSGPGEAGAVAPYGYTRPPQGLTGQEGDFPAPEVWYPGGVVSRVPYPNPSCVKSEMGPWMESYSGPYGDMRLETARDHVLPIDYYFPPQKTCLICGDEASGCHYGALTCGSCKVFFKRAAEGKQKYLCASRNDCTIDKFRRKNCPSCRLRKCYEAGMTLGARKLKKLGNLKLQEEGESSSASSPTEDTTQKLTVSHIEGYECQPIFLNVLEAIEPGVVCAGHDNNQPDSFAALLSSLNELGERQLVHVVKWAKALPGFRNLHVDDQMAVIQYSWMGLMVFAMGWRSFTNVNSRMLYFAPDLVFNEYRMHKSRMYSQCVRMRHLSQEFGWLQITPQEFLCMKALLLFSIIPVDGLKNQKFFDELRMNYIKELDRIIACKRKNPTSCSRRFYQLTKLLDSVQPIARELHQFTFDLLIKSHMVSVDFPEMMAEIISVQVPKILSGKVKPIYFHTQ