lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Generates hydrogen peroxide which is required for the activity of thyroid peroxidase/TPO and lactoperoxidase/LPO. Plays a role in thyroid hormones synthesis and lactoperoxidase-mediated antimicrobial defense at the surface of mucosa. May have its own peroxidase activity through its N-terminal peroxidase-like domain.
Subcellular Localization:
Apical cell membrane; Multi-pass membrane protein.
Sequence:
GPLFRTIVLDQFVRLRDGDRYWFENTRNGLFSKEEIAEIRNTSLRDILVAVTNVDPSALQPNVFFWLAGDPCPQPSQLSAKGLPACAPLFIRDYFEGSGFGFGLTIGTLCCFPLVSLLSAWIVARLRKRNFKRLQRQDRQSIMSEKLVGGVEALEWQGRNEPCRPVLVHLQPGQIRVVDGRLTVLRTIQLRPPQQVNLILSSNRGRRTLLLKIPKEYDLVLLFNMEEERQALVENVRGALKENGLSFQEWELREQELMRAAVTRQQRGHLLETFFRHLFSQVLDINQADAGTLPLDSSTKVREALTCELSRAEFADSLGLKPQDMFVESMFSLADKDGNGYLSFREFLDILVVFMKGSPEEKSRLMFRMYDFDGNGLISKDEFIRMLRSFIEISNNCLSKAQLAEVVESMFRESGFQDKEELTWEDFHFMLRDHDSDLRFTQLCVKGVEVPEVIKNLCRRASYISQEKICPSPRMSAHCARNNMKTASSPQRLQCPMDTDPPQEIRRRFGKKVTSFQPLLFTEAHREKFQRSRRHQTVQQFKRFIENYRRHIGCVAVFYTITGALFLERAYYYAFAAHHSGITDTTRVGIILSRGTAASISFMFSYILLTMCRNLITFLRETFLNRYIPFDAAVDFHRLIASTAIILTVLHSAGHVVNVYLFSISPLSVLSCLFPGLFHDDGSEFPQKYYWWFFQTVPGLTGVLLLLALAIMYVFASHHFRRRSFRGFWLTHHLYIFLYILLIIHGSFALIQMPRFHIFFLVPAIIYVGDKLVSLSRKKVEISVVKAELLPSGVTHLRFQRPQGFEYKSGQWVRIACLALGTTEYHPFTLTSAPHEDTLSLHIRAAGPWTTRLREIYSPPTGDTCARYPKLYLDGPFGEGHQEWHKFEVSVLVGGGIGVTPFASILKDLVFKSSVSCQVFCKKIYFIWVTRTQRQFEWLADIIREVEENDRQDLVSVHIYITQLAEKFDLRTTMLYICERHFQKVLNRSLFTGLRSITHFGRPPFEPFFNSLQEVHPQVRKIGVFSCGPPGMTKNVEKACQLINRQDRTHFSHHYENF
The following text describes a protein:
Function:
VSG forms a coat on the surface of the parasite. The trypanosome evades the immune response of the host by expressing a series of antigenically distinct VSGs from an estimated 1000 VSG genes.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MMFGKATGEKIELASTSAAITLLICMLGTPSEVDATAGHAIKRQHWVAIFELGQDAEKIPALALTNLRSAASVAEDAFTKLLRALIYAQANLTRRTLPKEKAAWFFLGEEVAAGLAYFKGGKAAADITAARNAGRLQGAITEFIELHAEGSDGTNGCLSADDDGGNPISGKATFSGATTACKANWDDVKAASTRPTVIAANGLVGKLQNGVDHDNLVNGAKQCDINSAKTTFKLSDGASDGTNVGTHIPKMAAGIITVGTTGLEIPSMASVGPTTGHHDFLKSIVQAAKCDQHRLQKAAVDTLAEAQKEPRFKKATKIHLQNKKSDDPDDEDSRERAIKTAYGDDDGMRKVLYAHPDGQPIPKAALGTDADTTLGQITDVGELMRLYFYYSDLNKQKLLEAEKKLQEVETKTATKSAEDKEKECNTKGKDKKEECEKLAKEGCVFNTEAKKCELKKEVKPELEKANQETGKTTTDKCGIEKPPEDCEKVQGTKPKGKNVVCGWIDYIDGKGKVEPACRSSSFLVDKKLALISAAFVSLLF
The following text describes a protein:
Function:
Mediates the side-chain deamidation of N-terminal glutamine residues to glutamate, an important step in N-end rule pathway of protein degradation. Conversion of the resulting N-terminal glutamine to glutamate renders the protein susceptible to arginylation, polyubiquitination and degradation as specified by the N-end rule. Does not act on substrates with internal or C-terminal glutamine and does not act on non-glutamine residues in any position.
Sequence:
MAAAAATSEQVGQRENKGVLTSLTGLGASERWLERQSLLYTSHYCEENVYKLLERVQQHHPEQLDRWYALFLSNQARHMAIFAQSLGDPVRGSVVVWDYHVIALRLGAAHPSAAEDLVFDFDSVLPFPCDAETYLNATFPYSFLDLAHNMRAQVHMVPAKQFLSTFASDRSHMRRHDGSYTKPPPPYPCIHSPDAPSTNNLSAFLAIRGAQDVGPVPASLPHAPDATQHAAQRGDEHGHDHQSRPSTRSKSARPSGIAPPMHGPGSHGISPVHADENLWLTISELRQHLQ
The following text describes a protein:
Function:
Small polypeptide acting as a regulatory molecule which coordinates cellular responses required for differentiation, growth and development, including leaves shape, pedicule elongation, inflorescence organization and fruit maturation, probably by restricting polar cell proliferation in lateral organs and coordinating socket cell recruitment and differentiation at trichome sites.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MESIMSLKRKEKKSQSRRLGKYLKEQKGRIYIIRRCVMMLLCSHD
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MGGDRGKKPVDTPADMLLPSRKRWLGDGGSDRAHGGCLFYETTPSSFTHGSSSSSPNRPLHDRMEVDTKESEIPRQRTENDRKISARIKRSHQARRRQRYEDQEDRVHGNVHFASICPPPVSWLELKHNMEVKLDLNLDDIEKSIVIPRCQEMDTSGNPDKVDKYLVAAKNLTRILNLEHPVLTETGHLRDRARSLHGTTISSIITEFCYLKVWRVSPLRRLGYLPGPIWESSVRSTFNESISATVSSSSSSSFTCSGSTNGSSDNNQASLEDGPDKRLACTGFINIQSVSVLDDIASIITEGGYQQLLRGAFDRHYSELARYFEILDIENILGSHMKDSVEILVNAWVRAMRITLNVLTEMRRQLHKQNFGAFNSFKHDYFMVIATQSIKKLVACGSSMCSWQQNSQDDPSTQSCAARESTKHTTQMILNLVMMYRALNYAMPELLALFSGRTEQIVLAEFRGLIDRSSSTVLQLFMELNNLIKSQRLVMVDIGVHHITRHITEYMRVLFEKKSTIYQMLDSKPNAFGELVMGLVSSLESMLEMNSRSLVLQGQKQVFLLNNLHFMIEQVKRCIDSGLILGESCLVQREDQLDQLITAYIEASWDPVISSFEKRTQVAIILWPHQLFDKFNSSFERIYSVQKTWKVTNPNVRLKLREAIIQKLIPVYQMQMGNQSEKKQMSARYSVEQLESQLLEMFEG
The following text describes a protein:
Function:
Pore-forming (alpha) subunit of a voltage-gated inwardly rectifying potassium channel. Charactherized by a fast rate of activation during depolarization followed by a rapid inactivation at much more depolarized value causing inward rectification due to a C-type inactivation mechanism. Exhibits a rapid recovery from inactivation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MPAMRGLLAPQNTFLDTIATRFDGTHSNFVLGNAQVAGLFPVVYCSDGFCDLTGFSRAEVMQRGCACSFLYGPDTSELVRQQIRKALDEHKEFKAELILYRKSGLPFWCLLDVIPIKNEKGEVALFLVSHKDISDTKNRGGPDNWKERGGGRRRYGRAGAKGFNANRRRSRAVLYHLSGHLQKQPKGKHKLNKGVFGEKPNLPEYKVAAIRKSPFILLHCGALRATWDGFILLATLYVAVTVPYSVCVSTAREPSAARGPPSVCDLAVEVLFILDIVLNFRTTFVSKSGQVVFAPKSICLHYVTTWFLLDVIAALPFDLLHAFKVNVYFGAHLLKTVRLLRLLRLLPRLDRYSQYSAVVLTLLMAVFALLAHWVACVWFYIGQREIESSASELPEIGWLQELARRLETPYYLVGRSPAVGNSSGQSDNCSSGSSEANRTGLELLGGPSLRSAYITSLYFALSSLTSVGFGNVSANTDTEKIFSICTMLIGALMHAVVFGNVTAIIQRMYARRFLYHSRTRDLRDYIRIHRIPKPLKQRMLEYFQATWAVNNGIDTTELLQSLPDELRADIAMHLHKEVLQLPLFEAASRGCLRALSLALRPAFCTPGEYLIHQGDALQALYFVCSGSMEVLKGGTVLAILGKGDLIGCELPRREQVVKANADVKGLTYCVLQCLQLAGLHESLALYPEFAPRFSRGLRGELSYNLGAGGGTAEADTSSLSGDNTLMSTLEEKETDGEQGPTVSPAPADEPSSPLLSPGCTSSSSAAKLLSPRRTAPRPRLGGRGRLGRAGASQAEAGPSAHPRSLEGLRLPPVPWNVPPDLSPRVVDGIEDGCGSDQPKFSFRVQSGPECSSSPSPGPENGLLTVPLGPSEARNMDTLDKLQQAVMELSEQVLQMREGLQSLRQAVQLVLAPHGEGPCPRVSGEGPRPASTSGLLQPLCVDTGASSYCLQPPAGSVLSGTWPHPRPGPPPLMAPWPWGPPASQSSPWPRATAFWTSTSDSEPPGSGELCPEPSTPGSPPPEEGARTGPPEPVNQAEAASTGEPPPGSGGLALPWEPHSLEMVLIGCHGSGTVQWTQEEGTGV
The following text describes a protein:
Function:
Prolyl cis/trans isomerase with specificity for phospho-Ser-Pro bonds.
Sequence:
GARLSSLKREPRNPNPRPKRPLRFRDRRDAKIGTESPAAAAAASGEGDAGRKRPSGDDAPADSKRRRPEAASSGSRDRNHHRHHHQKPREGDGGKEKKEKLRASHILIKHEGSRRKASWRDPEGVAISATTRDDAADLARALREQIAAGELKFEVAATDNSDCNSAKRGGDLGPFERGKMQKAFEKAVVALKVGEMSDVVDTDSGVHIILRTG
The following text describes a protein:
Function:
May play a role in anterograde transport of membrane proteins from the endoplasmic reticulum to the Golgi.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Membrane; Multi-pass membrane protein.
Sequence:
MALQWMILACVVAAEAAVAALLTLPAPRAVRGQIVGLTSMFLQPFAGVLPFAGFQLLDIYWKKEHRLMCTTEVCTAEERVHFEKAIFKAQRNVILCVSVFLLYWSIYRICKINKDIKALEEIEKRIKEE
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that participates in multiple biological processes including cell survival, differentiation, apoptosis, and in particular, the innate immune response. Participates in the activation of interferon-gamma signaling by promoting proteasomal degradation of the repressor SOCS1. Plays a positive role in the TNFalpha and IL-1beta signaling pathways. Mechanistically, induces the 'Lys-63'-linked polyubiquitination of MAP3K7/TAK1 component leading to the activation of NF-kappa-B. Also modulates STAT3 activity through negative regulation of PIAS3, either by degradation of PIAS3 through the ubiquitin-proteasome pathway or exclusion of PIAS3 from the nucleus. Negatively regulates TLR3/4-mediated innate immune response by catalyzing 'Lys-6'- and 'Lys-33'-linked polyubiquitination of TICAM1 and thereby disrupting the TICAM1-TBK1 interaction.
Subcellular Localization:
Cytoplasm. Nucleus. Nucleus, nuclear body. Note=Nucleo-cytoplasmic translocation is involved in regulation of NF-kappa-B.
Domain:
The coiled coil domain is required for homodimerization; The region immediately C-terminal to the RING motif is sufficient to mediate the interaction with SOCS1.
Sequence:
MAENWKNCFEEELICPICLHVFVEPVQLPCKHNFCRGCIGEAWAKDSGLVRCPECNQAYNQKPGLEKNLKLTNIVEKFNALHVEKPPAALHCVFCRRGPPLPAQKVCLRCEAPCCQSHVQTHLQQPSTARGHLLVEADDVRAWSCPQHNAYRLYHCEAEQVAVCQYCCYYSGAHQGHSVCDVEIRRNEIRKMLMKQQDRLEEREQDIEDQLYKLESDKRLVEEKVNQLKEEVRLQYEKLHQLLDEDLRQTVEVLDKAQAKFCSENAAQALHLGERMQEAKKLLGSLQLLFDKTEDVSFMKNTKSVKILMDRTQTCTSSSLSPTKIGHLNSKLFLNEVAKKEKQLRKMLEGPFSTPVPFLQSVPLYPCGVSSSGAEKRKHSTAFPEASFLETSSGPVGGQYGAAGTASGEGQSGQPLGPCSSTQHLVALPGGAQPVHSSPVFPPSQYPNGSAAQQPMLPQYGGRKILVCSVDNCYCSSVANHGGHQPYPRSGHFPWTVPSQEYSHPLPPTPSVPQSLPSLAVRDWLDASQQPGHQDFYRVYGQPSTKHYVTS
The following text describes a protein:
Function:
Necessary for protein translocation in the endoplasmic reticulum.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MNKDFEFSSRVTPKRLLTGTRKLQSRGVTVSMYKNPCFLPNQLLTQILVRVLLSEARTKTKIKSWEFVGSKKKKMDAIDSVFDPLREFSKDSVRLVKRCHKPDRKEFTKVAVRTAIGFVVMGFVGFFVKLIFIPINNIIVGSG
The following text describes a protein:
Function:
Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels.
Subcellular Localization:
Secreted.
Sequence:
MNFLLTWIHWGLAALLYFHNAKVLQAAPAHGDGDRQQSEVIPFMTVYERSVCRPIETMVDIFQEYPDEVEYILKPPCVALMRCGGCCNDEALECVPTELYNVTMEIMKLKPYQSQHIHPMSFQQHSKCECRPKKETRIIQENHCEPCSERRKHLYKQDPLTCKCSCKFTDSRCKSKQLELNERTCRCEKPRR
The following text describes a protein:
Function:
NAD(+) hydrolase (NADase) that catalyzes cleavage of NAD(+) into ADP-D-ribose (ADPR) and nicotinamide.
Domain:
The TIR domain mediates NAD(+) hydrolase (NADase) activity. Self-association of TIR domains is required for NADase activity.
Sequence:
MAKSVSISYLALEQIFNDTIGAGEIKVAGLLVGHPVNGGVHIARTIPTSRGTVTYVRISAEEISRAVEELNPGEKIVGWYHSRPGQGVFFSQDDIETHEKCLDFNPYFQALVIDPHQAKYGTPMADCVRFYTVRNHKEVPIHGYKLTGSSMQSYYDPKEFVFDKYGFPHHYTLTHAGKTKISHRKSNMDASFEYDVFICHAHEDKEFFVRELAEKLHSKGLRVWYDEFTLSLGDNLRRSIENGLAKSRYGIVVLSKRFFEKEWPQKELDGLVAKEVEGKKVILPVWHGITREEVQSFSSILANRLAASSEKGIDYVVNEILRVLRKKSV
The following text describes a protein:
Function:
Catalytic subunit of the peripheral V1 complex of vacuolar ATPase (V-ATPase). V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells; Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment.
Sequence:
MPTAQGARGHNDDKAGIQMLMAAEQEAQQIVNSARNSRASRLREAKGEADREVSQYRASRESDFRRKLSEATGDSGAITKRIEADTLQRLQALTAIANQSTERVSALLVSWVTSVKNDFGDDADFEDDAE
The following text describes a protein:
Function:
Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP).
Subcellular Localization:
Cytoplasm.
Sequence:
MRDSMSEADRSSPGSGKTDREDETAENATQDVIAVTPDDERTGLANRLDAHTGDGVRHRAFTCLLFDEDGRVLLAQRADRKRLWDTHWDGTVASHPIEGQSQVDATRQRLAEELGIEPHQYDKLEITDRFEYKRRYLDEGLEWEVCAVLQATLHDTSFDRDPEEVGGAMWVDYEDLYENPRYYRQLRLCPWFEIAMRRDFEGDADPVPDGTRA
The following text describes a protein:
Function:
Vesicle-associated membrane protein-associated protein (VAP) implicated in maintaining the cortical endoplasmic reticulum (ER)-plasma membrane (PM) attachment. ER-PM contacts function to modulate the distribution of contractile ring components to ensure robust ring assembly. ER-PM contacts function also in controlling exocytosis and maintenance of cell polarity regulating cell shape. VAPs play an important role in regulating eisosome assembly. VAPs also contribute to ER-phagy by tethering atg8 to the ER membrane, but also by maintaining the ER-plasma membrane contact (Ref.7).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type IV membrane protein. Note=Localizes at the cortical endoplasmic reticulum-plasma membrane contact sites.
Domain:
The MSP domain is required for binding to the FFAT motif of target proteins.
Sequence:
MALECDSTIVFPRPLTRLVKCDLELRNTAPYPIGFKVKTTAPKQYCVRPNGGRIEANSAVSVEVILQPLDHEPAPGTKCRDKFLVQSTELKPELQGMDIADIWTQVSKANISERKIRCVYSEGPSTANAHANAHHQPAQTTTTSIPTSATDNYTTVNGNVNQSYSKGIDGTALPSTHANPVAAPSTATTQHTQLPKTSAVSHQKPHEAPSTAVKAPTATVAENEPYPKPQSVPTTTSPNNENNALRSTANVINNTRQSTATSPSMFAGNSGNQIGLARVSSSFGRPTSGAKVVPQIHNTVTVQTAFLLAIICFLIGLLF
The following text describes a protein:
Function:
May bind DNA.
Subcellular Localization:
Nucleus.
Sequence:
MAKTALTPPASGSEVPRSGTPGDASGNKPQTDATGVSATDTASQKRGRGRPPKAKSDSSQIGAVSAKASTKPSGRPKRNVAQAVPSTSVAAAVKKRGRAKRSTVTAAVVTTATGEGSRKRGRPKKDDVAAATVPAETVVAPAKRRGRKPTVEVAAQPVRRTRKSTSVAPVAANVGDLKKRTALLQKKVKEAAAKLKQAVTAIDEVQKLADGM
The following text describes a protein:
Function:
Transcription factor which regulates nonfermentable carbon utilization. Activator of gluconeogenetic genes (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MMTVHRDKAAKRKKTNVACVNCSRSHVTCESQRPCTRCVKKGLEMSCVNAPRKRRKYLADVPEDQLPIPLKPADADAGPGMSERDGAAESGSKGPEHQFQDQGKIVHKPKFLSNAANLEYSTLSDIIHQDTLLNKIPVSLLYNGTDSPTPPSEALSGTHSASHGADVAGSRLSERPVHNVLNSMSSSRFVLRGLLGPQTDSILSSNVDLFKVHFPLVPQAVADGTLDFKRHSQGSMVAKKLRYDKSINQYYLSPACALPEVPNPNKHLCNGTVSFSLESRAPDEHQVLYRSDWPHSLRYGTPMEIYTLISEPFCHTSGFHSLLKYLHSRFHRHDLVEMCRSIAEFRPIFIASAVDLTEEDMIFMEQSYQRTLLEYDRFITQIGTPTCVWRRNGQISYLNDEFCLLTGWTREELLSKMTFIVELLDDNSVREYFKTFSKVAYKDFKGFEQMETCVLLSPIEGRTIECSCMWTWKRDVFGMPMMIVGHFLPVIAHPEPRDTDRLADSDFCISAGEGNPI
The following text describes a protein:
Function:
Could be part of the type IV piliation system (T4P). May contribute at the cohesion between the S-layer and the outer membrane by forming oligomers. Could also be the main channel through which trafficking is managed.
Subcellular Localization:
Cell envelope.
Sequence:
MNKRHALLLTAVLGMATAYAQTAPTTTTVNTLQTVYRDPSLTSAPITANVGKYVGPLSTFLASIAKSAGYEVVFNFNIDALALINGEIVFGNSTASVTTSYATPLGRPQELPAKPVVHNFSNAPFNEAWPLLMDVYELDYQLVKVGSANVIRIGQRPKQLALPLKFISAESALTAIEKFFGEEKFETVISLDSNNKPFQTTRPTGKFGLPNSIKVIPDSSNKRLIIGSNSEDGIRIRSFVETIDVQSSGKVISTDSISEIYIVRGQKESVLQFLRDSFPELIVTDYASGGLAIEGPRTSVNRAIILLGQVDRAPEIPIVQRIYTVRGQAADITALLAAQYPTLRVTPVGQTGQLVLNGAQAQLDTALALLEQVDRPAPVAESRTVQRVFQLVNASAEEVKATLEGTLARDLTADSNNDVLPNVPVTATDANGNTTVVSVPNALGKTANQGTANAQAQTAQTPANTQQATLIADKRTNSLIVRGTPEQVAQVAELVPQLDQVVPQINVQVRIQEVNERALQSLGLNWRATFGGFNVAVSGGTGLAATFNPTQSFLGFNIFPTLTALETQGLTRRVYDGNVTMQSGQRSLSATGGAQNASSGAAASVKSGGRLEINIPSAAGNIVRQIDYGLNLDFFSPQVAPDGTITLRIRGQVNQPATAITADSLPNLIDFTNSEAQSTITFKNGQTILMSGLLGSTETTNRSGVPFLSSLPGVGAAFGEKRTEKTQSQLLVIITGTVVK
The following text describes a protein:
Function:
Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has replication fork regression activity, unwinds stalled or blocked replication forks to make a HJ that can be resolved. Has a DNA unwinding activity characteristic of a DNA helicase with 3'-5' polarity.
Sequence:
MKNSVSKTETQSNGLLLPVTVIKGVGPSKAAALASIGIDTLQDLLNFFPRRYLDRNLTDNVLLKTGETVTLIVEVIDAYLAHGKKSRLVVGTKTRNNERISIVFFRGVNFFQKIFQPGTTLVATGKLEYFRGFQLIHPDYEILTSAIKTTYPISSTGSKKKKQEQEPEEELSELPEMIHAGRIIPLYPSGEVLKSEGLDSRGFRKILYSALEKLKGKIPEILPNEIVKRRGLILREESYREIHFPTDENSLDTAKYRLKYEELFYFNLLIEHKKKEREKIKRVLWPLPESETANKVRKNLPFQLTEDQNSALQKIKELTNKEQPIAVLLQGDVGSGKTLVALLTALRYIDNQIQVCMVAPTEILARQHYQTILSFLGNMPFLGIELLVGKEPKKNRYEKLYRIKKGDTLFVIGTHSVFQEDVYFSELGLVIIDEQHKFGVDQRETLRSKGKNPDILAMTATPIPRTLCLTLYGDLDLLTIKSKPKGRMPIQTKWFQEDRREGIYKSIRKYVSSGRQCYIVYPLVEESEKVDLKSCIEAYEYLKHEIFPDFEVGLVHGKMEVEEKDRVMREFSKNRIQILVSTTVIEVGIDVPNSTVMVIEHADRFGISQLHQLRGRVGRGDQESFCILMTDSKVTEDAKVRLEAMVNFSDGFALSEIDLQLRGPGELMGVRQSGLPDFKIADLRKDSNLIELTREDATLFGNPGDLEKEEIRGRFSEGRLLFSN
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:
MSQNNRKGGNKNFQKNNQNNNNNQQGGQQQQQQGGHQKHHNKHNQQNNQQQGGQQQGKGRGKAPTNVESFPINLTPQQIQQFQTYQQQIQSNPSPQFQSNYLPPATALFTPVINYFINLYSNFKSQSHQDILVSYDSFFKACETYYPHCSLPTIENLLPVLGDKFEDSFTDRFFVLLYKEIYYRYYYALVFQPNITTCVESWQNYYQIFHTLLSANSPNDVEIDLPNAWLWDLVDEFVYQYHTFAKFKLKKQDVDFLSENPEIWDTTNVIRYLYYIIKKSQIFSATTNRFENSSEDFCSHPVYKMLGYYSVISLVRVQCLLGDYTLALKTLELIDMGKKAMYTYVTACHITLYYYLGFAYIMSRKYNEATKALNTILVSVASKSKSSSFQSDHNEKKIDKMYALLTICQALYPNKIDENVNNNLKEKFGDKLLRLQKGDLSVYEELYTFAAPRCIGPVPPYISGYNVTALDSHRLQLSLFLEEVKQQSLLTTIRSYITLYSTISIQKLATLLQMDPEDLRVKLTCYKHKLFNVLGKGENKWNNQLDIDFYIDQDMIHIDNRLYAKETDSFINSILKFEGSLTPSYNWM
The following text describes a protein:
Function:
Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at the specific target site 5'-[CT]CCTTp site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.
Sequence:
MSSGSEDDKPLAKVNGHASAPTISKADDRAMDAADSKVHMAPVGVSIRNGPVDQDRMDVDSSVSGQAKRKSRTSIDQSINYKDDSSDDEAPLAKRSKTQHKQPDSDSDDEPIAKKNGARLPPSAKNTDMDVDSDDDEPLGKIAAKKANIEKEAAKEAKSIRAGTKAKKPAAKKAVKDESSDDEPLAKPTKRQVNGTAAKKTNGVKKEESDSDVPIAKRAKKAPAAKPAAKPAAKPAAKAATKAAPKGKVAAVKKSVKEESKDITDEDDEEEEYKWWEESAKKEDDSIKWTTLEHNGVIFPEDYQRLPKDVKLLYDGTPVELDIEAEEAATFFGFMLNSTVNVENPTFQKNFFRDFKEILDRTGGAKDKNGKKVDIKEFEKLDFSQLWAYKDAQTKAKNARSSAEKKAEKAERDKRDAPYLYCKWDGRKEKVGNPRVEIPGLFRGRGDHPKTGCIKKRVLPEQITINIGKEAKVPEPPAGHKWKAVQHDNKATWLAMWQENINGHYKYVMLAANSTVKGKADFKKFEKARELKKYIDRIRADYTKDLKSEVMADRQRATAMYLIDKFALRAGNEKDTENEAETVGCCSLKYEHVTLREPNTVIFDFLGKDSIRFYNEFTVDRQVFKNLKMFKKPPKEDGDDIFDRLTTTQLNKHLSSYMPGLTAKVFRTYNASYTMSKLLQELKVTNATVHEKVKLYNDCNRQVAILCNHKRTVGASHEQQMKKLVEQIKGLRYQKWRTKMMMLDLDPKLKKKKGAAYFELDEDLTEEWVKSHQEFLVEDQKAKINKKFEKDNEKRIADGEKPLPASELKERLKAASELEAKFKKENKTKKVEAEGKGPSVEKLEAALEKLDQRIKNLELQSADREGNKEVALGTSKINYIDPRLTVVFSAKFNVPIEKFFSKTLREKFKWAIESVGNDSTWEF
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Subcellular Localization:
Cytoplasm.
Sequence:
MPEPKLSNFFELEEHRFYSESIPCGIDEAGRGPYAGPLSVALVSFSQNSLTQILEGKILKGLTDSKKLSEKKRESLYPEIIKAAQFSYQTFISPNYIDRKGINRAVLEGILKCTKLINRFTQSKFPLKLLIDGNYNFNRYPEWMNLKDCSTFYIKGDLRIVSIAAASILAKVSRDRYMISVSKKYPIYRFDQHKGYGTKLHEELILLHGLSDIHRRSFTGKFLEQISESNL
The following text describes a protein:
Function:
RNA-binding protein that acts as a regulator of mRNA splicing of a subset of genes encoding key structural proteins involved in cardiac development, such as TTN (Titin), CACNA1C, CAMK2D or PDLIM5/ENH. Acts as a repressor of mRNA splicing: specifically binds the 5'UCUU-3' motif that is predominantly found within intronic sequences of pre-mRNAs, leading to the exclusion of specific exons in target transcripts (By similarity). RBM20-mediated exon skipping is hormone-dependent and is essential for TTN isoform transition in both cardiac and skeletal muscles (By similarity). RBM20-mediated exon skipping of TTN provides substrates for the formation of circular RNA (circRNAs) from the TTN transcripts (By similarity). Together with RBM24, promotes the expression of short isoforms of PDLIM5/ENH in cardiomyocytes (By similarity).
Subcellular Localization:
Nucleus. Cytoplasm, Cytoplasmic ribonucleoprotein granule. Note=The active form that regulates alternative splicing localizes to the nucleus. Also localizes to cytoplasmic ribonucleoprotein granules; localization to cytoplasmic ribonucleoprotein granules plays an important regulatory role. Subcellular localization is regulated by phosphorylation of different parts of the protein: while phosphorylation of the RS (arginine/serine-rich) region promotes nuclear localization, phosphorylation of the C-terminal disordered region promotes localization to cytoplasmic ribonucleoprotein granules (By similarity).
Sequence:
MVLAAAMSQDAEPSGPEQPDRDARSVPGAPAPPAPPGPRGMQPPPPPPPPPPPPPQAGLPQIIQNAAKLLDKTPFSVSNPNPLLPSPASLQLAQLQAQLTLHRLKLAQTAVTNNTAAATVLNQVLSKVAMSQPLFNQLRHPSMISAPHGHTGVPPHATTVPSTRFPSNAITFSAGQTRGPGPSVNLPSQPPNTMVMHPFSGVMPQTPAQPAVILGIGKTGPAPAAAGFYEYGKATSGQAYGSETDSQPSFLPASASTSGSVTYEGHYSHSGQDSQAAFPKDFYGPTSQGSQVAGTFAADTAGGLKGEVGPLLQGPNSQWESPHGFSGQSKPDLTAAPNLWPPHPSQPYELYDPEEPTPDRTPPSLGGRLNHSKQGFSGARRRAKEEQAVLSMRPLQVQELNDFHGVAPLHLPHICSICDKKVFDLKDWELHVKGKLHAQKCLLFSENTGVRCVLGPAEGTLCASPNSTAVYNPAGNEDYASNLGTSYAALPARTFTQSNPAFPSASPGMNFVQRKLGAGRVVHICNLPEGSCTENDVINLGLPFGKVTNYILMKSTNQAFLEMAYTEAAQAMVQYYQEKSAMINGEKLLIRMSKRYKELQLKKPGKTVAAIIQDIHSQRERDMFREADRYGPERPRSRSPVSRSLSPRSHTPSFTSCSSSHSPPGPSRADWGNGRDSWEHSPYARREEERGPAPWRENGEDKRDRTDMWAHDRKHYPRQVDKTELDERLEGGRGYREKHPRSGSPSSLHSVSGYKSREDGYYRKEPKGKSDKYLKQQQEAPGRSRRKDEARLRDGRHPYPDDSGKEDGLEAKGTKSKQSEKNRTKRPDRDQEGADDRKESRMAESEAGKEEQDSMEESPSSVGRQEKETESSDAENTRTRKEQDSESGSEAEGESWYPTNMEELVTVDEVGEEEDFIMEPDIPELEEIVPIDQKDKICPEICPCVTTTLELDLAQDFTKEGVKTIGNGATEISLKSPKEPPSASTSCPSDMDVEMPGLNLDAERKPAECETGLSLEGSGCYEQQAKGAESSDVCLAPMLEQMSSPKPAEERAWQPGPFLDDGKVGGTPEDGAAEGRPLEEKASTPTETDLQSQACQGVSTQENSGYVEMKSLDARSPEYTEVELKQPLSLPSWEPEDVFSELSIPLGVEFVVPRTGFYCKLCGLFYTSEEMAKMSHCRSAVHYRNLQKYLSQLAEEGLKETEGAGSPRPEDSGIVPHFERKKL
The following text describes a protein:
Function:
May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process.
Sequence:
MEGKIGKVLVVDDDENIAEVIKMYLENSGYDTRVCYNGKEAQEGFLEYKPDLVLLDIMLPHIDGVDVLKWIRKDSTIPIIMLTAKGDTFDKVLALELGADDYIVKPFEPKELLARVKAVLRRYNVDNENKEALNFEQLTIDVNSYTVVYKNKEIKMPPKEFELLYYLARNKNRVFTREQLLCEVWGYDYPGDSRTVDVHIKRLREKLEGGPNWEIETVWGVGYKFEVK
The following text describes a protein:
Function:
HflC and HflK could regulate a protease.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MSLGHSHSHSHHEHHHDHDHDHDHGHGAQAASPWRRLLVAALLVLFAVAAACLVQVRSGEAMVITRFGNPARVLLEPGLAWRLPLPFESAIPVDLRLRTTSSGLQDVGTRDGLRIIVQAYVAWQVQGDADNVQRFMRAVRNQPDEAARQLRTFVGSALETTASAYDLADLVNTEASRVRIGDFEARLREQIDHQLLATYGVKVVQVGIERLTLPKVTLGATVDRMRAERETIATERTAEGRRQAAEIRSAAERDARVIQAEASVKAAEIEAQARVEAARIYGKAYAGSPQLYNLLRSLDTLGTIVNGDTRLVLRTDAAPFRVLVDGPPALPAEAPANGRRP
The following text describes a protein:
Function:
Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism.
Subcellular Localization:
Cytoplasm.
Domain:
Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.
Sequence:
MKNIIFMGPPGAGKGTQAKILCERLSIPQISTGDILREAVKNQTAMGIEAKRYMDAGDLVPDSVVIGIIKDRIREADCKNGFLLDGFPRTVEQAEALDTLLKNEGKSIDKAINLQVPDAELLKRLLGRAEIEGRADDNEVTIKNRLDNYNKKTLPLLDFYATRKKLSQVNGVGSLEEVTSLIQKELA
The following text describes a protein:
Function:
Nucleoside triphosphate pyrophosphatase that hydrolyzes dTTP and UTP. May have a dual role in cell division arrest and in preventing the incorporation of modified nucleotides into cellular nucleic acids.
Subcellular Localization:
Cytoplasm.
Sequence:
MVSATTHPFILASASPRRRELLARLGVSYHRVASQAEEQPLPPPAELLSHLPSLPIPLPIESHPTLVAWRKASDISYQHPDAIVLAADTEVAIDGMVLGKPRDEAHAHEMLRRLVGRAHTVLTGLCLVTPPSVHTSGFLYDGKRVLFDLVASQVHMRPLSDEQIAAYVAQGESLDKAGGYGLQSGGGALITRIEGSYTNVVGLPLPAVARLLRAVGIEPPVDPMKAYDEWLRSQGKEPAPWPTQP