lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Component of the RPD3C(L) histone deacetylase complex (HDAC) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSQQTPQESEQTTAKEQDLDQESVLSNIDFNTDLNHNLNLSEYCISSDAGTEKMDSDEEKSLANLPELKYAPKLSSLVKQETLTESLKRPHEDEKEAIDEAKKMKVPGENEDESKEEEKSQELEEAIDSKEKSTDARDEQGDEGDNEEENNEEDNENENEHTAPPALVMPSPIEMEEQRMTALKEITDIEYKFAQLRQKLYDNQLVRLQTELQMCLEGSHPELQVYYSKIAAIRDYKLHRAYQRQKYELSCINTETIATRTFIHQDFHKKVTDLRARLLNRTTQTWYDINKERRDMDIVIPDVNYHVPIKLDNKTLSCITGYASAAQLCYPGEPVAEDLACESIEYRYRANPVDKLEVIVDRMRLNNEISDLEGLRKYFHSFPGAPELNPLRDSEINDDFHQWAQ
The following text describes a protein:
Function:
Copper metallochaperone essential for the assembly of the mitochondrial respiratory chain complex IV (CIV), also known as cytochrome c oxidase. Binds two copper ions and delivers them to the metallochaperone SCO1 which transports the copper ions to the Cu(A) site on the cytochrome c oxidase subunit II (MT-CO2/COX2).
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Sequence:
MTYVCTTKHATLGSHHFYRDMSSLAAASCESQSSESQEKKPLKPCCACPETKKARDACIIEKGEENCQHLIEAHKECMRSLGFKV
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Sequence:
MQPILEIRNGTKLFGRIPAFQEVDFAVSPGEVHAILGENGAGKSTLTKVLAGVYKLTSGEMLLNGTPVHLSTPAEGLKQGVVMVYQETNLVPSMTVAQNIYLGEEKVFNRLRGLYIQARQFLAGMGFQVDPTAQVSQLGAAQKQMVEIARAVHHKAKVIIFDEPTATLTPEEKRHFFNLIRRLVADKVAIIFISHALEEAMQLADRITILRDGRLVASDVKETFTRDTVIQAMVGRNLTETLHGDHGRPPRPYGERVLSVENLSSGTMVRNTSFSIFAGQVTGVFGLIGAGRTEMMKVVAGVLKRDIFHGGEIKYRGKSVRYRVPRMAVREGIVYVTEDRKFDGFFETMTVAENLHLGELSRFSNPLSVISMTQAKELARQWAGRLQLRSINEKARVIELSGGNQQKVVIARSLIQKPRLIIFDEPTRGVDVGAIVEIHQFINSLADDGLAVVVISSYLPEVLALSDRILVAKRGKIVEEIKTAEATEQQIMYAAVH
The following text describes a protein:
Function:
May act as a substrate-specific adapter of an E3 ubiquitin-protein ligase complex (CUL3-RBX1-BTB) which mediates the ubiquitination and subsequent proteasomal degradation of target proteins.
Domain:
The BTB/POZ domain mediates the interaction with some component of ubiquitin ligase complexes.
Sequence:
MGLVTVGELKPAFTGKRGFRLNSTIRHASEWPISDVSSDLTVQVGSSSFCLHKFPLVSRSGKIRKLLADPKISNVCLSNAPGGSEAFELAAKFCYGINIEINLLNIAKLRCASHYLEMTEDFSEENLASKTEHFLKETIFPSILNSIIVLHHCETLIPVSEDLNLVNRLIIAVANNACKEQLTSGLLKLDYSFSGTNIEPQTPLDWWGKSLAVLNLDFFQRVISAVKSKGLIQDVISKILISYTNKSLQGLIVRDPKLEKERVLDSEGKKKQRLIVETIVRLLPTQGRRSSVPMAFLSSLLKMVIATSSSASTGSCRSDLERRIGLQLDQAILEDVLIPINLNGTNNTMYDIDSILRIFSIFLNLDEDDEEEEHHHLQFRDETEMIYDFDSPGSPKQSSILKVSKLMDNYLAEIAMDPNLTTSKFIALAELLPDHARIISDGLYRAVDIYLKVHPNIKDSERYRLCKTIDSQKLSQEACSHAAQNERLPVQMAVQVLYFEQIRLRNAMSSSIGPTQFLFNSNCHQFPQRSGSGAGSGAISPRDNYASVRRENRELKLEVARMRMRLTDLEKDHISIKQELVKSNPGTKLFKSFAKKISKLNSLFSFSSLKPSLSGKASSESRFLFQRKRRHSVS
The following text describes a protein:
Function:
Gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLPKQFLKLFKDPCDVYTAIHPLFYVCTFFGLAPYSLVRVENGKKVFKFAWWPLTRNALLVLILLGALTYHAIFDLISFKDSDLQQKLRYFEEVFSSLLSCCSVIFGCIFALKVIEVFKNIEEVDVAFRSLAVWVPYKHLYVNILIHLSGLVTIVATLTVTIIFFASYQYGTKTYSLFIVFMTVILPYFINLLMELQYCHYLNILRVRYQLLNEYLETLVQETNRTSVEGWTDVSNVKRKSKEISKLPKSMLAISDPVFIVDQVAALHIKLTDTAHMINYAFCVQQLLRITVAFISIVTALFLVAINFNKSSSEENEGKTTQLDYFFTFWAFSNACEVMAIVWITSETCEEANTCPRILHKIRNNTTNTNLQDTIEIYSLQMYHNRLYFTVCGLFPLDYTLLYTIVAGVTTYLVILIQFNNSDFVQRNSTEFDNATESY
The following text describes a protein:
Function:
Catalyzes the ring-opening hydrolysis of 3-dehydro-scyllo-inosose (diketo-inositol) to 5-dehydro-L-gluconate, and thus probably functions in a myo-inositol degradation pathway together with IolG, IolM and IolO.
Miscellaneous:
MISCELLANEOUS: The proposed catalytic mechanism involves two water molecules. The first molecule is bound as a bridge between the two metal ions and attacks the carbonyl carbon of the substrate. The second water molecule, that is bound to metal 1, likely functions as a proton donor in catalysis.
Sequence:
MERPTGVYFQTMTMKQIRERLKQCDLIIIPVGSTENHGPNAPTGEDTFLVTRMAEQVALKTGCTVAEPIWYGYHPYHHIGMPGTVPVKDEAFIDYLVSVIAGFWNTGFRKQILLNGHGQEFVIPIAIHKFAKIFQVPAIIINLNWYHAIQDKFKTKEEGGPYETPFIHADEVETSWSLALFPEFMHQEWAVDTEPKGFLPEGHIDKAGNLLHRPIAWYGHVGGGPIEVVAYPEGVVGKATLASAEKAKEGVEALLDYLEKLVRDIMERFPAGKLPPAEMLSQRPKEELEALTKEPLTEGWRNLYTAGNLWG
The following text describes a protein:
Function:
RNA-binding 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. This subunit can bind 18S rRNA.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MASMMQRTSNFQWGDIEEDDDDLDILLPQVIGPDENGVKKVIEYRLNDEGRRIKVTTTTRVQKRLLSQRAAERRSWPKFGDAAREEPGLYLTVRSTEDIHLERGSQAEEATTSGDSMPQAGGVLMVCRVCRMRGDHWTARCPQRDLLSLMETPLTTTEASTSTEVYVPPSMRAGADMRRRNDENSVRVTNLSEDTREQDLMELFHPFGAVTRAYVAVDKNTNMSRGFGFVNFVSREDAERDINTLNGYGYDNLILRVEWATPRPRGNLLRSSSFFKISIFVLISVACFFLGKHWSDDGFRRLVFFSSEPSRSPIVALSPDLGKTYNISDLIHKSHPIPPVPLTPPPPPSTVDLHVFGIVDENGTMSDEFQVGDYDAESLGNQTESESGDGEAELTTVRASVGRIEICPEVMTDYIPCLDNEEAIKRLDSTVRGERFERHCPEEGTGLNCTVPVPNGYRPPIPWPKSREEVWFNNVPHTRLVEDKGGQNWISKENDKFKFPGGGTQFIHGADQYLDQISQMVSDISFGNHTRVVLDIGCGVASFGAYLMSRDVLTLSIAPKDVHENQIQFALERGVPAMVAAFTTRRLLYPSQAFDLVHCSRCRINWTRDDFMYCHVMLNEDGILLLEVNRMLRAGGYFVWAAQPVYKHEKALEEQWEEMLNVTTRLCWVLVKKEGYIAIWQKPTNNTCYLSRDAGIMPPLCNPEDDPDSVWYVDLKACITRIEDNGYGANLAPWPSRLQTPPDRLQTIQIDSYIARKELFMAEYKYWKEIISNYVNALHWKQIGLRNVMDMRAGFGGFAAALAELKVDCWVLNVVPVSGPNTLPVIYDRGLLGVMHDWCEPFDTYPRTYDLLHAAGLFSIERKRCNMTTIMLEMDRILRPGGRVYIRDTINVMSELQEIGNAMRWHTTLRETAEGPHASYRVLLCEKKFENKVESSVDKHPAKKKRRKSKGKRH
The following text describes a protein:
Function:
DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with RO60. Binds to poly(U) RNA (By similarity).
Subcellular Localization:
Nucleus. Note=Colocalizes partially with RO60.
Domain:
The third RNA recognition motif, called PUMP domain, is atypical and may rather mediate homodimerization and/or protein-protein interactions.
Sequence:
MATATIALQVNGQQGGGSEPAAAAAAAAAAVVAAGDKWKPPQGTESIKMENGQSTGTKLGLPPLTPEQQEALQKAKKYAMEQSIKSVLVKQTIAHQQQQLTNLQMAAVTMGFGDPLSPLQSMAAQRQRALAIMCRVYVGSIYYELGEDTIRQAFAPFGPIKSIDMSWDSVTMKHKGFAFVEYEVPEAAQLALEQMNSVMLGGRNIKVGRPSNIGQAQPIIDQLAEEARAFNRIYVASVHQDLSDDDIKSVFEAFGKIKSCTLARDPTTGKHKGYGFIEYEKAQSSQDAVSSMNLFDLGGQYLRVGKAVTPPMPLLTPATPGGLPPAAAVAAAAATAKITAQEAVAGAAVLGTLATPGLVSPALTLAQPLGALPQAVMAAQAPGVITGVTPARPPIPVTIPSVGVVNPILASPPTLGLLEPKKEKEEEELFPESERPEMLSEQEHMSISGSSARHMVMQKLLRKQESTVMVLRNMVDPKDIDDDLEGEVTEECGKFGAVNRVIIYQEKQGEEEDAEIIVKIFVEFSMASETHKAIQALNGRWFGGRKVVAEVYDQERFDNSDLSA
The following text describes a protein:
Function:
Required for proper chemotaxis and phagocytosis; proper spatiotemporal control of F-actin levels in chemotaxing cells. Negative regulator of the PI3K (phosphatidylinositol 3 kinase) pathway. Predominantly phosphorylates serines and threonines and tyrosines at a lower level (By similarity).
Subcellular Localization:
Membrane.
Sequence:
MKRFFSNLFKRKQDQNSHIKQINGPTTSTPTTTPTTPTTPTTTQTPTPQNNNTNNNTNNNNNTNSNNSNQQKKEQAQASPSTNQTQTPSNNTISTSPTVTTQPSFTPGVISTSKLTTSPPESPRPPTSTTNTTQPSTTTTTATNSTNTNTASAPTKTASPSSPSATASPNNNSNNTTTTAATTTTTTTTTTTTNANQTASVNHTSSDQSLNAQNVTQTNNNNNNNNNNNNNNNANNTKPINPNDYIPLDFVDSTPKVDNNQPKRKASGPPEILPEEIDRTDFLGQGSFGSVYKGKCRGQEVAVKIPRKQKLSLYELTSFRHEVKIMSKIFHPNVVLFLGACTQSGKMQIVTELCQTDLEKLLHNDRTKKEFSLFRRMQMAKDAALGMNWLHGITRIVHNDLKTANLLVDINLRVKVTDFGFSQIKEGEEFQDKAAKGTPLWMAPEVMMGNPYNEKADVYSFGIILWEILTKEAPYSHHKDYDIFFNAICNEKERPPIPADTLPSLRHLIQTCWDHNPQNRPSFSEILFRLNEILIDCAIDFDDGRKYWKEHFLVPKQELQEEVEWSDFEKTLKATHKQLNLDYAPLKELLVQQSHQTVQKTKQVVTMERFDKVSKWFGSFFEPNTGIETIDNINKLSAKIWFHGDIVREQATSRLSKAAEGAFLIRLSSTEPKTCPFTLSMKNNQHRRIQLIDENNFTGFKIQGKTAVYNSLIELVEKCNDYPLLVPCPKFTQETFNPYDPYTN
The following text describes a protein:
Function:
Probable acyltransferase which may mediate the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). May also catalyze the conversion of lysophosphatidylethanolamine (1-acyl-2-hydroxy-sn-glycero-3-phosphoethanolamine or LPE) into phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity), as well as the conversion of lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) into phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity). Required for incorporation of arachidonic acid into PC, PE, and PS.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The di-lysine motif may confer endoplasmic reticulum localization.
Sequence:
MGVVGALSEVTSASEDALRLLISVLAGYPLAVVHRTFFYNKPAQHQHLFFVIVGLSLWMFNCGSSVIHPILSIFGAFFITNFMAGTDASIYAAHIVFLGHLLIGYWFHETDTYDITWTTPFCIMTLRFIGLVMDVYDGAQKPEHLKPDQKLTAISDKPGLLEIAAFGLFFQGTLVGPQFTLSKFRSFVNGDWLDSDGQPPKSAFLPSIGRFLAGCTYMVLHQWGQFWIPDQYFNSDAYNNLSFFWRWSWVTLWFRLTMYKYCAMWLITEGASILSGLGHNGKDAEGNDRWDGVRDLHIIKWETGHDYNSVVESFNCGTNTFAKNHIHRRLRWVNNKLASHVITLSYLAIWHGYHLGYFLLFGVELGCVQAQNQLYALIKRTPGWSEAISKPISRPFIWIFGKLTISYSMGFAFLMFGLIKTKYWIGPVKSLYFIGFIIYFIVWPILHMVLLRVLPRHPKKAAAEKPEEVKKEL
The following text describes a protein:
Function:
Multidrug efflux protein that confers resistance to a wide range of toxic compounds, including ethidium, methyl viologen, acriflavine, tetraphenylphosphonium (TPP(+)), benzalkonium, propidium, dequalinium and the aminoglycoside antibiotics streptomycin and tobramycin. Can also transport the osmoprotectants betaine and choline. The drug efflux is coupled to an influx of protons. Can couple antiport of a drug to either one or two protons, performing both electrogenic and electroneutral transport of a single substrate. Simultaneously binds and cotransports proton and drug.
Miscellaneous:
MISCELLANEOUS: Mutants designed to insert with biased topology are functional regardless of the topology; MISCELLANEOUS: Encoded by the cryptic lambdoid prophage DLP12.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Note=Forms antiparallel homodimers. The topology could be controlled by a single positively charged residue placed in different locations throughout the protein, including the very C terminus.
Domain:
Binds different substrates in the same active site. Binding of the substrate induces conformational changes of EmrE. The asymmetric antiparallel homodimer exchanges between inward- and outward-facing states that are identical except that they have opposite orientation in the membrane. The conserved C-terminal tail is strongly coupled to EmrE's drug-binding domain and participates in secondary gating of EmrE-mediated proton/drug transport, occluding the binding pocket of fully protonated EmrE in the absence of drug to prevent dissipative proton transport.
Sequence:
MNPYIYLGGAILAEVIGTTLMKFSEGFTRLWPSVGTIICYCASFWLLAQTLAYIPTGIAYAIWSGVGIVLISLLSWGFFGQRLDLPAIIGMMLICAGVLIINLLSRSTPH
The following text describes a protein:
Function:
Plays a role as an inducible effector molecule that mediates Fas resistance produced by surface Ig engagement in B cells.
Subcellular Localization:
Cytoplasm.
Sequence:
MASGDDSPIFEDDESPPYSLEKMTDLVAVWDVALSDGVHKIEFEHGTTSGKRVVYVDGKEEIRKDWMFKLVGRETFCVGAAKTKATINIDAISGFAYEYTLEINGKSLKKYMENRSKTTNTWVLHMDGENFRIVLEKDTMDVWCNGKKLETAGEFVDDGTETHFSLGNHDCYIKAVSSGKRKEGIIHTLIVDNREIPEIAS
The following text describes a protein:
Function:
Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular Localization:
Mitochondrion inner membrane. Mitochondrion membrane.
Sequence:
MAAKILKYAAIPAAAVVGLGSFRIYSLNEKTNEELISPRELSIYSPDGRAVQFVEEQPGLVQTGLGSVRVGLQPYVRAVQNGLTSVKVGVISLYQSGQDTYHFLRDPPPGFLPRVTVIGVSGLGGLILARKGSRLKRIVVPLGLASAGTAVCYPTQTVGALKITGKKVYSVSSSVASMFKSKPKEDVVKSVVNVESAAAVQSPDTESPTKALSELPPESDVASATPEQDVTPVPDVVPSVELSPTADVADPPPVDVASGTSAPPSEPEPNPAPALEAAPVTEAAPVEDTVPDAESTPEPSPEPIAETVKESTIEPLEAPAAGAVIDTAPEPTPSSETEVTSVVESDQEIVPELEVPVLTAVIEEITPTVEEATSPAPVLPNDFTPTISDEGPAFVAPPPAKEAIPLTPPPVEASQPIADEAPPSEPVTAKSRFVPDPSLLDHGQSNPEDADMYSTRS
The following text describes a protein:
Function:
Catalyzes the intermembrane transfer of phosphatidylglycerol and phosphatidylinositol.
Sequence:
MASMVGGCLLLVALLTVVSPSLAHVTWESCGEGDVEVLNVTMTPDPAVRGGVFTFNLPAKTPRVIEGGHVSVFVFYKGIPVYFENDDLCVKTKCPITSDVFTFTNTQQLPSITPPGPYQLRIKASDLDGKPLFCAKMKFQIVSGAESKSAPLLVASR
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of beta-ketoacyl-ACP substrates to beta-hydroxyacyl-ACP products, the first reductive step in the elongation cycle of fatty acid biosynthesis.
Sequence:
MIDFTGKTSLITGASGGIGSAIARLLHKLGSKVIISGSNEKKLKLLGNTLKDNYIIEVCNLANKEECNNLISKISNLDILVCNAGITSDTLAIRMKDQDFDKVIDINLKANFILNREAIKKMIQKRYGRIINISSIVGIAGNPGQANYCASKAGLIGMTKSLSYEVATRGITVNAVAPGFIKSDMTDKLNEKQREAIVQKIPLGTYGIPEDVAYAVAFLASNHASYITGQTLHVNGGMLMV
The following text describes a protein:
Function:
Involved in the regulation of the sulfoquinovose operon. Represses the expression of the yihUTS operon and of the yihV and csqR genes. Binds DNA inside the spacer between the bidirectional transcription units comprising the yihUTS operon and the yihV gene, and upstream the csqR gene itself.
Sequence:
MSLTELTGNPRHDQLLMLIAERGYMNIDELANLLDVSTQTVRRDIRKLSEQGLITRHHGGAGRASSVVNTAFEQREVSQTEEKKAIAEAVADYIPDGSTIFITIGTTVEHVARALLNHNHLRIITNSLRVAHILYHNPRFEVMVPGGTLRSHNSGIIGPSAASFVADFRADYLVTSVGAIESDGALMEFDVNEANVVKTMMAHARNILLVADHTKYHASAAVEIGNVAQVTALFTDELPPAALKSRLQDSQIEIILPQEDA
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA. Required for optimal pre-ribosomal RNA transcription by RNA polymerase I together with a subset of U3 proteins required for transcription (t-UTPs).
Miscellaneous:
MISCELLANEOUS: Present with 6560 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus, nucleolus. Note=Associated with ribosomal chromatin, even in the absence of transcription.
Sequence:
MTQSLGIEQYKLSVVSGGKPALNNLSSVTGNKNIARLSQDQRNYIIPFNNQIKVYSVETRQCVKTLKFANNSLLSGIFLQEEENNESIVKILLGDITVPQQEDAHLITVFTNNGHVIVLNYKGKLVESPKHFKISLADEKLANVFHSEGNYRILTTFKDPSQKAHNSLQSYRLYALTFDDAKKQFEVAHQAEWHNVILSNISSNGKLLAHMCKDVSTKDHEHKSISVVSLFDDSVNLSFPLGSILSSQTQSLSYNTRYVSSMAIDNMGQQLAVGFASGVISIVSLADLQIRLLKWHIDSVLSLSFSHDGSYLLSGGWEKVMSLWQLETNSQQFLPRLNGIIIDCQVLGPQGNYYSLILQMTENNSNSDYQFLLLNASDLTSKLSINGPLPVFNSTIKHIQQPISAMNTKNSNSITSLNHSKKKQSRKLIKSRRQDFTTNVEINPINKNLYFPHISAVQIFDFYKNEQVNYQYLTSGVNNSMGKVRFELNLQDPIITDLKFTKDGQWMITYEIEYPPNDLLSSKDLTHILKFWTKNDNETNWNLKTKVINPHGISVPITKILPSPRSVNNSQGCLTADNNGGLKFWSFDSHESNWCLKKISLPNFNHFSNSVSLAWSQDGSLIFHGFDDKLQILDFDTFKKFESLENTKTVSEFTLDSEIQTVKLINDTNLIVATRTTLNAINLLRGQVINSFDLYPFVNGVYKNGHMDRLITCDERTGNIALVINQQLTDLDGVPTINYKSRIIIFDSDLSTKLGNFTHHEYISWIGWNYDTDFIFLDIESTLGVVGTTVNTQLSDEVNNEGILDGLVSNTITTSASNSDIFAEQLHKLSSRGKKSDTRDKNTNDNDEDEEDIALEFINGEKKDKLVNMNSFTSMFDNIQNVQMDTFFDRVMKVLT
The following text describes a protein:
Function:
A cytochrome P450 monooxygenase involved in the biosynthesis of adrenal corticoids. Catalyzes a variety of reactions that are essential for many species, including detoxification, defense, and the formation of endogenous chemicals like steroid hormones (By similarity). Steroid 11beta, 18- and 19-hydroxylase with preferred regioselectivity at 11beta, then 18, and lastly 19. Catalyzes the hydroxylation of 11-deoxycortisol and 11-deoxycorticosterone (21-hydroxyprogesterone) at 11beta position, yielding cortisol or corticosterone, respectively, but cannot produce aldosterone. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate for hydroxylation and reducing the second into a water molecule. Two electrons are provided by NADPH via a two-protein mitochondrial transfer system comprising flavoprotein FDXR (adrenodoxin/ferredoxin reductase) and nonheme iron-sulfur protein FDX1 or FDX2 (adrenodoxin/ferredoxin). Due to its lack of 18-oxidation activity, it is incapable of generating aldosterone. Could also be involved in the androgen metabolic pathway (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein.
Sequence:
MALRVTADVWLARPWQCLHRTRALGTTAKVAPKTLKPFEAIPQYSRNKWLKMIQILREQGQENLHLEMHQAFQELGPIFRHSAGGAQIVSVMLPEDAEKLHQVESILPHRMPLEPWVAHRELRGLRRGVFLLNGADWRFNRLQLNPNMLSPKAIQSFVPFVDVVARDFVENLKKRMLENVHGSMSINIQSNMFNYTMEASHFVISGERLGLTGHDLKPESVTFTHALHSMFKSTTQLMFLPKSLTRWTSTRVWKEHFDSWDIISEYVTKCIKNVYRELAEGRQQSWSVISEMVAQSTLSMDAIHANSMELIAGSVDTTAISLVMTLFELARNPDVQQALRQESLAAEASIVANPQKAMSDLPLLRAALKETLRLYPVGSFVERIVHSDLVLQNYHVPAGTFVIIYLYSMGRNPAVFPRPERYMPQRWLERKRSFQHLAFGFGVRQCLGRRLAEVEMLLLLHHMLKTFQVETLRQEDMQMVFRFLLMPSSSPFLTFRPVS
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.
Sequence:
MAEYVQVVKRAFKHLGGHGGVRGAILQLLRVNDLKTGTLVGVDKYGNKYYEDKRNFFGRHRWVVYTSEMNGKNTFWEVDGSMVPPEWQKFGGFTCLSIGSAALCLRKLLQPLPSCCCPPLLCISRLLLFRHRWLHSMTDDPPTTHPPVARKFIWENHKFNLSGTPGQYVPYSTTRKKIQEWIPPTTASK
The following text describes a protein:
Function:
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and in RNA transcription by RNA polymerase II (By similarity). In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment (By similarity). In transcription, TFIIH has an essential role in transcription initiation (By similarity). When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape (By similarity). Necessary for the stability of the TFIIH complex and for the presence of normal levels of TFIIH in the cell. Required for efficient binding of TFIIH to damaged DNA. Dispensable for normal development, but required when transcription is challenged.
Subcellular Localization:
Nucleus. Chromosome. Note=Localized to paired homologous chromosomes (bivalents) about 10 minutes after UV irradiation, but localization is lost after 35 minutes, probably as a result of successful DNA damage repair as part of the TFIIH complex.
Sequence:
MVNVKKGVLVTSDPAFRQLLIHLDDSRQLGSKFIVRELDDTHLFIEKEIVPMLENKVEQIMENMNPEAVDK
The following text describes a protein:
Function:
Directs RNA polymerase II nuclear import.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAAASVDSRSSDAGKRVILRVKRKRTDDPVEALVVSHILPSKKNKTEEKEAKDKSSAVDQVFTLLGTTADGDRSAAQKILKNIKSKPLSHANIKTQKALPEKLQTKLRKEKKKSHQDARFKLVSSNRPSQADALHSTDEPCSTAPLAVDEDSSEFQSDEVQNFFKVYDVIRDEDIASKDKLTPESKQEDTSAIVCNSVKMVREKLAVSNDKNQEYSIADKGYVYDFYYADDIINKDLGDVLEITGVNDDFMLEKMDQEFDEMFDDDDDSNDENNWRNDYPDEGEWSSEDENRVTRLPDPDFGFDMDDRKYHRQAFGEDISSDDELDFYGKPCKLDESETYNEELNDLDEGF
The following text describes a protein:
Function:
Cell surface receptor that may play a role in the innate and adaptive immune response. Acts as a counter-receptor for CD276 and interaction with CD276 on T-cells enhances T-cell activation.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MKASPGRPPRIAAVEAQGGQWPGVIWAARKRMEPGVRCPQSLLLLLLLLLMLWVSALQDEEVYTKVSRREGETLTVSCPYLVRPNRREGKVWCKVRRRKCDPNFSRAWTTGPRYLLQDDPLAGLITVAMNGLRLQDSGKYWCMRNSSHTLYPIKGIQLVVSHAPSKESRPETTESSHWNLVASITARSPTTVTATAIEPPGARSSTILSGSTIRSAPAALPTTAKITSPTIRSLTVARHRTIKTLAVTRHPTTGSPSEATPSTTRSSALARSSPTRSLTTVRSTPTAVAKSFSTGPPSVTWSFSISLPTGAKSSSTKSPTMARSASTRSPAMARGLSTRSSTMAVVLITGASTKARVLPATPPSKARCPSSLGMDDVISSFRDASLTVPVVLVGCLWFLMLAAVFYGFWKKSRMRSERWPPGRPGMGWTGIDPASTGLQELWG
The following text describes a protein:
Function:
Transcriptional activator that binds the same DNA consensus sequence as p53. Has a role in normal development to ensure proper meiotic chromosome segregation. Promotes apoptosis under conditions of cellular and genotoxic stress in response to DNA damage, hypoxia, or starvation. Regulates germline apoptosis in response to DNA damage. Its pro-apoptotic activity is inhibited when bound to ape-1 in vitro. Plays a role in cell cycle arrest in the germline in response to DNA damage by UV-C light. However, not required for survival in response to DNA damage induced by UV-C light, indicating that it is unlikely to be involved in DNA repair. Required for induction of ced-13 in response to DNA damage. Regulates DNA damage-induced apoptosis by inducing transcription of the programmed cell death activator egl-1. Regulates germline proliferation by activating phg-1. Modulates lifespan.
Subcellular Localization:
Nucleus.
Sequence:
MEPDDSQLSDILKDARIPDSQDIGVNLTQNLSFDTVQKMIDGVFTPIFSQGTEDSLEKDILKTPGISTIYNGILGNGEETKKRTPKISDAFEPDLNTSGDVFDSDKSEDGLMNDESYLSNTTLSQVVLDSQKYEYLRVRTEEEQQLVIEKRARERFIRKSMKIAEETALSYENDGSRELSETMTQKVTQMDFTETNVPFDGNDESSNLAVRVQSDMNLNEDCEKWMEIDVLKQKVAKSSDMAFAISSEHEKYLWTKMGCLVPIQVKWKLDKRHFNSNLSLRIRFVKYDKKENVEYAIRNPRSDVMKCRSHTEREQHFPFDSFFYIRNSEHEFSYSAEKGSTFTLIMYPGAVQANFDIIFMCQEKCLDLDDRRKTMCLAVFLDDENGNEILHAYIKQVRIVAYPRRDWKNFCEREDAKQKDFRFPELPAYKKASLESINIKQEVNLENMFNVTNTTAQMEPSTSYSSPSNSNNRKRFLNECDSPNNDYTMMHRTPPVTGYASRLHGCVPPIETEHENCQSPSMKRSRCTNYSFRTLTLSTAEYTKVVEFLAREAKVPRYTWVPTQVVSHILPTEGLERFLTAIKAGHDSVLFNANGIYTMGDMIREFEKHNDIFERIGIDSSKLSKYYEAFLSFYRIQEAMKLPK