lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the hydroxylation of the 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzoquinone at the C6 position and participates in the biosynthesis of ubiquinone (Probable). Catalyzes the reaction through a substrate-mediated reduction pathway, whereby NADH shuttles electrons to 5-methoxy-2-methyl-3-(all-trans-decaprenyl)benzoquinone, which then transfers the electrons to the two Fe(3+) centers. The binding of 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzoquinone (DMQn) mediates reduction of the diiron center by nicotinamide adenine dinucleotide (NADH) and initiates oxygen activation for subsequent DMQ hydroxylation. The physiological substrates are 5-methoxy-2-methyl-3-(all-trans-nonaprenyl)benzoquinone (DMQ(9)) and 5-methoxy-2-methyl-3-(all-trans-decaprenyl)benzoquinone (DMQ(10)), however in vitro the enzyme does not have any specificity concerning the length of the polyprenyl tail, and accepts tails of various lengths with similar efficiency. Also has a structural role in the COQ enzyme complex, stabilizing other COQ polypeptides. Involved in lifespan determination in a ubiquinone-independent manner (By similarity). Plays a role in modulating mitochondrial stress responses, acting in the nucleus, perhaps via regulating gene expression, independent of its characterized mitochondrial function in ubiquinone biosynthesis.
Subcellular Localization:
Mitochondrion inner membrane; Peripheral membrane protein; Matrix side. Mitochondrion. Nucleus. Chromosome.
Sequence:
MSCAGAAAAPRLWRLRPGARRSLSAYGRRTSVRFRSSGMTLDNISRAAVDRIIRVDHAGEYGANRIYAGQMAVLGRTSVGPVIQKMWDQEKDHLKKFNELMVTFRVRPTVLMPLWNVLGFALGAGTALLGKEGAMACTVAVEESIAHHYNNQIRTLMEEDPEKYEELLQLIKKFRDEELEHHDIGLDHDAELAPAYAVLKSIIQAGCRVAIYLSERL
The following text describes a protein:
Function:
Works in parallel with pry-1 in negatively regulating bar-1 signaling in vulval precursor cells and Q neuroblasts. Shown to have a role in excretory cell development.
Miscellaneous:
MISCELLANEOUS: Reporter transgenes fail to show detectable expression indicating that axl-1 may be expressed at low levels.
Sequence:
MTMRSKFSIDRVLHDTAFAKWCQKEESRNADSITLYTSILDFESKLKTGSPSLSLLKLARHIHRKYVSLNTGTCHVIGDSIRTKISTRVHEVLDGKPPYIDLFDPLKQPLFQHLRSMHTEFSTTTADVNTTWEDASSTSSSNKGATIWFNEDAIDKSSRHEIGQSTVTHESEDDRFSFFNAVCTRLNSLQETKNSSETEEHAESPRKEKSSTPYGTDGFAPPPRSTQTNTLKVSNLPKRFESLYKKKRQQVATSDSSGFGSNASDFWSFERYGKSNQGTLERPNRLFTGTNNGFSTLQPKRRGSEAPKMTVELRYENDVPMVAKISANHAQSVTLRYFRHLFGLHYTDNCRFFFKSTCEDGSAQYQWTLLFHDDDILPVFQNRITAICRMCPPPEDHDLI
The following text describes a protein:
Function:
Probable gustatory receptor which mediates acceptance or avoidance behavior, depending on its substrates.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MRFLRRQTRRLRSIWQRSLPVRFRRGKLHTQLVTICLYATVFLNILYGVYLGRFSFRRKKFVFSKGLTIYSLFVATFFALFYIWNIYNEISTGQINLRDTIGIYCYMNVCVCLFNYVTQWEKTLQIIRFQNSVPLFKVLDSLDISAMIVWRAFIYGLLKIVFCPLITYITLILYHRRSISESQWTSVTTTKTMLPLIVSNQINNCFFGGLVLANLIFAAVNRKLHGIVKEANMLQSPVQMNLHKPYYRMRRFCELADLLDELARKYGFTASRSKNYLRFTDWSMVLSMLMNLLGITMGCYNQYLAIADHYINEEPFDLFLAIVLVVFLAVPFLELVMVARISNQTLTRRTGELLQRFDLQHADARFKQVVNAFWLQVVTINYKLMPLGLLELNTSLVNKVFSSAIGSLLILIQSDLTLRFSLK
The following text describes a protein:
Function:
Is involved in the conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MAQNDTVKLIGSWASPFSIRARAALHLKSVKYEYLDEPDSLNIVQYIDEAWSSGPSILPSHPVERANARFWAIFIDEKIFGSLEAVGGAKDDEGRMAAAGKLMENLAILEEAFQKSSKGLGFFGGENIGFLDLACGTLLGPVSVIEAFSGVKFLRQETTPGLIQWAQKFRAHEAVKPYMPTPEEFVAFAKKKFNVE
The following text describes a protein:
Function:
Forms the portal vertex of the capsid. This portal plays critical roles in head assembly, genome packaging, neck/tail attachment, and genome ejection. Procapsid assembly may initiate with a nucleation complex composed of portal and scaffolding proteins. The portal protein multimerizes as a single ring-shaped homododecamer arranged around a central channel. Switches upon genome packaging from an asymmetrical conformation in the procapsid (PC-portal) to a symmetrical ring in the mature capsid (MV-portal). This change of conformation may serve as a signal for headful packaging.
Subcellular Localization:
Virion.
Sequence:
MADNENRLESILSRFDADWTASDEARREAKNDLFFSRVSQWDDWLSQYTTLQYRGQFDVVRPVVRKLVSEMRQNPIDVLYRPKDGARPDAADVLMGMYRTDMRHNTAKIAVNIAVREQIEAGVGAWRLVTDYEDQSPTSNNQVIRREPIHSACSHVIWDSNSKLMDKSDARHCTVIHSMSQNGWEDFAEKYDLDADDIPSFQNPNDWVFPWLTQDTIQIAEFYEVVEKKETAFIYQDPVTGEPVSYFKRDIKDVIDDLADSGFIKIAERQIKRRRVYKSIITCTAVLKDKQLIAGEHIPIVPVFGEWGFVEDKEVYEGVVRLTKDGQRLRNMIMSFNADIVARTPKKKPFFWPEQIAGFEHMYDGNDDYPYYLLNRTDENSGDLPTQPLAYYENPEVPQANAYMLEAATSAVKEVATLGVDTEAVNGGQVAFDTVNQLNMRADLETYVFQDNLATAMRRDGEIYQSIVNDIYDVPRNVTITLEDGSEKDVQLMAEVVDLATGEKQVLNDIRGRYECYTDVGPSFQSMKQQNRAEILELLGKTPQGTPEYQLLLLQYFTLLDGKGVEMMRDYANKQLIQMGVKKPETPEEQQWLVEAQQAKQGQQDPAMVQAQGVLLQGQAELAKAQNQTLSLQIDAAKVEAQNQLNAARIAEIFNNMDLSKQSEFREFLKTVASFQQDRSEDARANAELLLKGDEQTHKQRMDIANILQSQRQNQPSGSVAETPQ
The following text describes a protein:
Function:
Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate.
Domain:
Modular enzyme with four functionally distinct domains. The isolated Hcy-binding domain catalyzes methyl transfer from free methylcobalamin to homocysteine. The Hcy-binding domain in association with the pterin-binding domain catalyzes the methylation of cob(I)alamin by methyltetrahydrofolate and the methylation of homocysteine. The B12-binding domain binds the cofactor. The AdoMet activation domain binds S-adenosyl-L-methionine. Under aerobic conditions cob(I)alamin can be converted to inactive cob(II)alamin. Reductive methylation by S-adenosyl-L-methionine and flavodoxin regenerates methylcobalamin.
Sequence:
MASSPSTPPADTRTRVSALREALATRVVVADGAMGTMLQAQNPTLDDFQQLEGCNEVLNLTRPDIVRSVHEEYFAAGVDCVETNTFGANHSALGEYDIPERVHELSEAGARVAREVADEFGARDGRQRWVLGSMGPGTKLPTLGHAPYTVLRDAYQRNAEGLVAGGADALLVETTQDLLQTKASVLGARRALDVLGLDLPLIVSVTVETTGTMLLGSEIGAALTALEPLGIDMIGLNCATGPAEMSEHLRYLARHSRIPLTCMPNAGLPVLGKDGAHYPLTAPELADAHETFVREYGLSLVGGCCGTTPEHLRQVVERVRDTAPTARDPRPEPGAASLYQTVPFRQDTSYLAIGERTNANGSKKFREAMLDGRWDDCVEMARDQIREGAHMLDLCVDYVGRDGVADMEELAGRFATASTLPIVLDSTEVDVIRAGLEKLGGRAVINSVNYEDGAGPESRFARVTKLAREHGAALIALTIDEVGQARTAEKKVEIAERLIDDLTGNWGIHESDILVDCLTFTICTGQEESRKDGLATIEGIRELKRRHPDVQTTLGLSNISFGLNPAARILLNSVFLDECVKAGLDSAIVHASKILPIARFDEEQVTTALDLIYDRRREGYDPLQKLMQLFEGATAKSLKASKAEELAALPLEERLKRRIIDGEKNGLEQDLDEALRERPALEIVNDTLLDGMKVVGELFGSGQMQLPFVLQSAEVMKTAVAHLEPHMEKTDDDGKGTIVLATVRGDVHDIGKNLVDIILSNNGYNVVNLGIKQPVSAILEAADEHRADVIGMSGLLVKSTVIMKENLEELNQRKLAADYPVILGGAALTRAYVEQDLHEIYDGEVRYARDAFEGLRLMDALIGIKRGVPGAKLPELKQRRVRAATVEIDERPEEGHVRSDVATDNPVPTPPFRGTRVVKGIQLKEYASWLDEGALFKGQWGLKQARTGEGPSYEELVESEGRPRLRGLLDRLQTDNLLEAAVVYGYFPCVSKDDDLIVLDDDGNERTRFTFPRQRRGRRLCLADFFRPEESGETDVVGFQVVTVGSRIGEETARMFEANAYRDYLELHGLSVQLAEALAEYWHARVRSELGFAGEDPAEMEDMFALKYRGARFSLGYGACPDLEDRAKIAALLEPERIGVHLSEEFQLHPEQSTDAIVIHHPEAKYFNAR
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:
MAQTTKFTSLVQVLTRPTGWYWGISKMFRECVIKFGALVGEDKYGNKYYENKNYFVARHRWVDYKDWWKYDASDIPAEWHRWIHFMTDDPPTIDPPVERKFLSGHKSNMTGSYREYVPYSTTRRKIDSWSPPQKE
The following text describes a protein:
Function:
Binds to DNA and alters its conformation. May be involved in regulation of gene expression, nucleoid organization and DNA protection.
Subcellular Localization:
Cytoplasm, nucleoid.
Sequence:
MMNMQNMMRQAQKLQKQMEQSQAELAAMQFVGKSAQDLVQATLTGDKKVVSIDFNPAVVDPEDLETLSDMTVQAINSALEQIDETTKKKLGAFAGKLPF
The following text describes a protein:
Function:
Putative oxidoreductase. Acts as a tumor suppressor and plays a role in apoptosis. Required for normal bone development (By similarity). May function synergistically with p53/TP53 to control genotoxic stress-induced cell death. Plays a role in TGFB1 signaling and TGFB1-mediated cell death. May also play a role in tumor necrosis factor (TNF)-mediated cell death. Inhibits Wnt signaling, probably by sequestering DVL2 in the cytoplasm.
Subcellular Localization:
Cytoplasm. Nucleus. Mitochondrion. Golgi apparatus. Lysosome. Note=Partially localizes to the mitochondria. Translocates to the nucleus upon genotoxic stress or TNF stimulation (By similarity). Translocates to the nucleus in response to TGFB1. Isoform 5 and isoform 6 may localize in the nucleus. Localized to the lysosome probably upon binding to VOPP1.
Domain:
The WW 1 domain mediates interaction with TP53, and probably TP73, TFAP2C, LITAF and WBP1.
Sequence:
MAALRYAGLDDTDSEDELPPGWEERTTKDGWVYYANHTEEKTQWEHPKTGKRKRVAGDLPYGWEQETDENGQVFFVDHINKRTTYLDPRLAFTVDDNPTKPTTRQRYDGSTTAMEILQGRDFTGKVVVVTGANSGIGFETAKSFALHGAHVILACRNMARASEAVSRILEEWHKAKVEAMTLDLALLRSVQHFAEAFKAKNVPLHVLVCNAATFALPWSLTKDGLETTFQVNHLGHFYLVQLLQDVLCRSAPARVIVVSSESHRFTDINDSLGKLDFSRLSPTKNDYWAMLAYNRSKLCNILFSNELHRRLSPRGVTSNAVHPGNMMYSNIHRSWWVYTLLFTLARPFTKSMQQGAATTVYCAAVPELEGLGGMYFNNCCRCMPSPEAQSEETARTLWALSERLIQERLGSQSG
The following text describes a protein:
Function:
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:
MYPTPNPPNHTTHLTPQDRTKRVKDARNEAQKEIEDYKTEKENEYQKFEKEHSSGNQKAEEDAKKATDVKVKEIDDIGKKSGSKVVDQLITAVTNAKPEPPRK
The following text describes a protein:
Function:
Transcription factor (By similarity). Binds to DNA sequence motif 5'-CTGTTTCA-3'. Regulates expression of a class of small RNAs, known as 21U-RNAs, perhaps acting redundantly with fkh-4 and fkh-3.
Subcellular Localization:
Nucleus.
Sequence:
MQYALTVIFQSILFVQCQVGEAAFVISQEHEVSKSISINMTLFPSIKWIIHKSFYLYLTYFVMSQQTLPCFQAADSYNYSHSLPKVQFARFSKYTPQSISYSSTQMYQQKEYSDHITEMTNVHKSRKRKLMVTEDQWGSQITIPKVIQNRPLIEKWFVQKRFKMVKVRNIQRPQLSYQLLSALTCLNSPDGMISTTEIYSFILHHWRYYRYANENWKNSVRHVLCKCQLFDVLQVEGLSRKGNVYKLKRPDNVEKEMIDVKTLGCMQKDSRGIDFYIKMLAGQIGLPRHLFYSIVGNEMPEYAGPENSAIFYHLLSMRKIIPKLETRYFLEHWQMEHKATEPMFFEEFVPYSTSLVSCVENISSYGEGVGPGNDELYDLSDRQIICFHKNIRAYHSLQKRCHKMNYSNWMTPSLIYVQEAVMDKEIVEDDIRNGTIECEGVARKEEAKKNFQDPALISIYN
The following text describes a protein:
Function:
Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane.
Subcellular Localization:
Cell outer membrane; Lipid-anchor.
Sequence:
MKRILTSAALIGMTTLLAACGFQLRGLGDAQFALKEIDVSARNAYGPTVRELKETLENSGVKVTSNAPYHLVLVREDNQQRTVSYTGSARGAEFELTNTINYEIVGANDLVLMSNQVQVQKVYVHDENNLIGSDQEAAQLRSEMRRDLIQQLSMRLQALTPAQLDEAQRQAEAKAKAEAEALRAADEAERQRRAAEPQQSPIEFPTP
The following text describes a protein:
Function:
Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope.
Subcellular Localization:
Cytoplasm. Nucleus. Note=Nuclear rim.
Sequence:
MNAENTFSILNTNEPNAGGSQVTESEIEEEDIEFLSFAALKIGATSSLSNSSLGLPEYSNLFAINNLKSLFVAGVPNYLIIGSTLDLQKSLIDADENVDANVLKDSASIRHVSLPDAKFSMVSFSSNGEFVIAYDFVSFELSVYETDALLKNSATSIYKAVFPDLVQVLPNPEINNLVILRNLKLEVFLLSLSKFQVESPLAKDATCAAWSRRGKQCVIGFNNGTMSQYTPAGEIKLRIPRPPSLENYFVECISWIENREFVVFYSPLTSLSNESDEPPHESECFVISVGMNGHFNFGKAGDPTPPFGAVNRRDHHYIASLHAWKPDLRSLVVVANTASADLGVLALSMEKNQWSILNIVDETKRASLPYSNKKDSDSSPTALVMDFTATDRISKPLDPTEAPADCSPLPIVWVFNDEFQLVAYRIFYADAISKSIDYPEMNVIKDKNKDSTVRASNNENIPTPDKQASPFVKNLSSTSSPFSQSSAFGNFKFGQATSFDKGLSTDASSGAKSNTPVFGQPSTFGQAPVFGQPSAFGQAPVFGQPSAFGQSSFSFGTSNMNQKLDFGTFKSPLSGAATGEAKTNLEKAVTSASGKASFTGFAPSQSTTSGLNFDSIPKDNEAASIFGSSQVSTKNTSGFQFSNNTLLADNVDEDIESDHDTKIEELANSDVEPSTEQNIGGDVSWGASTFQSKPQPSFSFGLTLDDKSNTPGKNFSIFGKTAETQVEQKKPENNVLTKPFSFAPSDKSMFAANIPSAGEGLDQQKTSKALPSTGITKLSENDNEKAEESNETKGFNTTIAKQNDKSSKSEGKASVANMSALNKSTNNETSDSKPSLKSPLFNFSADAPTFTFNKPSETPPFSFNKPLVEKESKQDVSDTSDRSPFSFKAFGIDSKKSPTPEPTEMAESNISEESEGWKLIEQPNVESEIEDQDEESSDLNGKRRSTPPKIHEVGVNKMLDVVPKEKRDLNSFFPKQPLVVQSTDKNKKEPQESLEDEILSAEGFSEVEAANKISRFEPFSSPKLKLATSDNAPEKYVFEESESSDLEEGPVPLRNLESLADLPEAESNEKLPMVNTFERLYLQFKNELDLVWQNINIIAEYIEGQTSTPSAVSEQATMAMLSQNTEELEDLLDTVTSFSAFCSDYSKQIDYLEACLVRINAKRIQVTRLLKALTNPAFEKQMELRQLGPEALRRQKELRLKMEKVLKSLSTLEQQAVDARMSDTRRFKKPTLGSIEVAYSRIATLLGQRLKQLYKLEKDIKRMATKKKMITKKSMSSDMMTQFRALGISQSSTKQVSAHYLREFERQDAFRNGVFKRLTSLKKAD
The following text describes a protein:
Function:
Choline-specific glycerophosphodiesterase that hydrolyzes glycerophosphocholine (GPC) and lysophosphatidylcholine (LPC) and contributes to supplying choline to the cells. Has a preference for LPC with short (12:0 and 14:0) or polyunsaturated (18:2 and 20:4) fatty acids. In vitro, hydrolyzes only choline-containing lysophospholipids, such as sphingosylphosphorylcholine (SPC), platelet-activating factor (PAF) and lysoPAF, but not other lysophospholipids.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MRTEQAGITIMALQTLLLVTSVLLNVCPSFAVNKLLVVLVDGLREDYPARDLHLLQFQAIAREGVKAQYVTPVFPAKSYPNYYSIMTGLYSESHGMTGNYMHDAERNVSFLVGFNQESFEPFWWENAEPLWITATKAGKAVNMYYWPGCQVPIRNYVPNKCIELTDLPSFENMLNSIDEIVQLFGDDVIDMAGLYYQKVDIWGHRYGPESELVRDKVLEVDTMLGYLRQKLTDTGLDQSVNVIILSDHGMASLPDYSATSGYISLKDYVDVNDLKKPTLYSDMLVHIWPKDGLLEKVHSDLLNVPHSIVLKKEEIPEDWHYKRGKYVPPLLLVMQYPWLVFEDAAIPWTWDNATQFPRGSHGFSNSRMDMKGVFMAFGPDFRKGYEAGAIDIVDEYQLMCRLLDIIPLPNNGTWSRVEGMLLDGAISGTVSQHACVVSTFVIVQFMSIYFSVYCLLY
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MATPPLSGPGPGLPPPPPAPAPAPAPPAGAGAGAAAAAAAFPGPPPPPPPPPPPQAAREVNTASLCRIGQETVQDIVFRTMEIFQLLRNMQLPNGVTYHTGTYQDRLGKLQDHLRQLSILFRKLRLVYDKCNENCAGLDPVPIEQLVPYVEDDGSKNDDRGSTSQLRFASEERREIAEVNKKLKQKNQQLKQIMDQLRTLIWDINAMLAMRN
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MFRSTFFGLSRAIVQPATPLTVRAAFQSRFYSAAAAASQPTTTATTTTPLQQQQQQQPTTQPTTPIQTQTGAAPTESTKPVAKPYLVGRAWTQRLPVYHLAKRGGNKKLTQIKKVQGDGQALRRDLAQFLGLEVKEVRVKVPTGHLEVDGHRREEIVKFLDGLGF
The following text describes a protein:
Function:
Plays a role in weight homeostasis. Involved in the control of feeding behavior through the central melanocortin system. Acts as alpha melanocyte-stimulating hormone antagonist by inhibiting cAMP production mediated by stimulation of melanocortin receptors within the hypothalamus and adrenal gland. Has very low activity with MC5R. Is an inverse agonist for MC3R and MC4R being able to suppress their constitutive activity. It promotes MC3R and MC4R endocytosis in an arrestin-dependent manner.
Subcellular Localization:
Golgi apparatus lumen. Secreted.
Sequence:
RMLLLLLCCWSFSLLRLSSSLIHGHMPVDQGPISSHRSDAPYLPDIERSRVPDSVLDPDLLSADAVEDHFVMEPGSYEEDSSAGLQLQGRAMRSSRRCIPHQQSCLGYPLPCCDPCDTCYCRFFNAICYCRQIGHTCAPRRT
The following text describes a protein:
Function:
Probable E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins.
Sequence:
MFFSGDPSNRKRVDLGGRSSKERDRKKLLEQAKLERNKRSWMRQQNSAAVIIQKCFRGRKVVKAERGKAREQFYTTYGKHCERVDSQCFGPDSDFLRQLQFFYSPQNISDFSTLVEACRSLLQFAKDSGGILKLVGGSDYLSKRALVDYRVKSLAYACIGAVHHNRYQFKDELLSTSLDSGSSINILLKAAAMLIDPKLPWSCKIVSYLLQQNVYRIFREVVITGKECLNSEGRVGKVSLMETLLVLVIAHTGQGHCVCPNIDLQWSFTSQVLSIPFVWHIFPYLKEIYVSRGLCQHYLHNMATCTHSYEKVLPADISVEFPGYACLLGNLLEAVGVALARPACPYDLAIDFANVATLLLEILPPIQTSKTGGREENSIAGDDDMIIDDAPAVLPLSKELEKQISNAIDPRFLLQLINVLFGSSSLVADSSKDKISDKEAAAVAAACSFLHVTFTILPLERIMTVLAYRTELVSVLWNFMKRCHKNQNWSCLSAVSPYLPADAFGWLLPLAVFCPVYKHMLMIVDNEEFYEQEKPLSLNDIRLLIVILKQDLWQILWLNPVAPMKFNTNTLSLKKHRVEFVQYRVIVVASELLSQLQDWNNRRQFAHPSNFHADGVNDHFISQAMTENTRAYDILKQAPFLVPFTSRVKLFTSQLAAIKERHGSHSLFNRSSFKIRRDHILEDAFSQLSTLAEEDLRGVIRVTFVNEFGVEEAGIDGGGIFKDFMENITRAAFDMQYGLFKETIDHLLYPNPGSGMIHEQHLQFFHFLGIILGKAMFEGILVDIPFATFFLSKLKQKHNYLNDLPSLDPELYRHLIFLKRYEGDLAELELYFVIFNNEFGEQTAEELIPGGKNIRVVNDNVITFIHLVANHRLNTQIRQQSSHFLRGFQQLIQKDWIDMFNEHELQLLISGSVDNFDVDDLRSNTNYAGGYHREHYVIDMFWEILKNFSLENQHKFLKFVTGCSRGPLLGFKYLEPLFCIQRAGGSATEDALERLPTSATCMNLLKLPPYRSKEQMEQKLLYAINAEAGFDLS
The following text describes a protein:
Function:
Catalyzes the glycosylation of anthocyanins from UDP-glucose.
Sequence:
MATSVNGSHRRPHYLLVTFPAQGHINPALQLANRLIHHGATVTYSTAVSAHRRMGEPPSTKGLSFAWFTDGFDDGLKSFEDQKIYMSELKRCGSNALRDIIKANLDATTETEPITGVIYSVLVPWVSTVAREFHLPTTLLWIEPATVLDIYYYYFNTSYKHLFDVEPIKLPKLPLITTGDLPSFLQPSKALPSALVTLREHIEALETESNPKILVNTFSALEHDALTSVEKLKMIPIGPLVSSSEGKTDLFKSSDEDYTKWLDSKLERSVIYISLGTHADDLPEKHMEALTHGVLATNRPFLWIVREKNPEEKKKNRFLELIRGSDRGLVVGWCSQTAVLAHCAVGCFVTHCGWNSTLESLESGVPVVAFPQFADQCTTAKLVEDTWRIGVKVKVGEEGDVDGEEIRRCLEKVMSGGEEAEEMRENAEKWKAMAVDAAAEGGPSDLNLKGFVDEDE
The following text describes a protein:
Function:
Specifically methylates the N1 position of guanosine-37 in various cytoplasmic and mitochondrial tRNAs. Methylation is not dependent on the nature of the nucleoside 5' of the target nucleoside. This is the first step in the biosynthesis of wybutosine (yW), a modified base adjacent to the anticodon of tRNAs and required for accurate decoding.
Subcellular Localization:
Mitochondrion matrix. Nucleus. Cytoplasm. Note=Predominantly in the mitochondria and in the nucleus.
Sequence:
MLKSLCFVIRPAIVSRPQFRLPTIARLSLRQFQNQPQSVGFFTMAPLETRALALSPSATICPPSRIGTTELDRSAFDLDVQILSAVVEPGMIGKLRSHPSLKDLVLDLPKTKPIVECPAGLAPVAARDVKGLKLLRFHLSKESELPEEAKEVLKGAKALVKEVVRLGYDNWNASEILGACLPTTKSEDIPSSFTTTGHIGHMNLREEWLPFRYLIGQVVLDKNPGLRTIVNKLDTIHAQFRYFDMEVIAGDNDYIATVNESGCSFTFNFSNVYWNSRLHHEHERLISLFPPGCVIADVMAGVGPFAIPAAKKGCYVLGNDLNPESVKWMRENRLRNKVEPTLRVSEIDGFEFIRIAPLEVWTRPFDPAPPPKVSNRQRDREAKEARRKREQAKAAGQPVTETAPMSIPSQEVAIKPHPPQPPKLISHFIMNLPDSAITFLPSYVSCYTPLLAERSFIDEYGGEEEAKRKVEMPMVHCYCFTKEIEIGKAEIDILQRASTNLSFNLTPQVENYNLHHVRSVAPNKDMYCLSFRLPREVAFRHNG
The following text describes a protein:
Function:
Involved in cardiomyocyte differentiation.
Subcellular Localization:
Nucleus.
Sequence:
MGSRRAAGRGWGLGGRAGAGGDSEDDGPVWTPGPASRSYLLSVRPEASLSSNRLSHPSSGRSTFCSIIAQLTEETQPLFETTLKSRAVSEDSDVRFTCIVTGYPEPEVTWYKDDIELDRYCGLPKYEITHQGNRHTLQLYRCQEEDAAIYQASARNTKGIVSCSGVLEVGTMTEYKIHQRWFAKLKRKAAAKMREIEQSWKHGKEASGEADTLLRKISPDRFQRKRRLSGVEEAVLSTPVREMEEGSSAAWQEGETESAQHPGLGLINSFAPGEAPTNGEPAPENGEDEERGLLTYICEVMELGPQNSPPKESGAKKKRKDEESKPGEQKLELEKAEGSQCSSENVVPSTDKPNSSRREKSTDTQPAQTQPRGRVARGPGIESTRKTASVLGIQDKVQDVPAPAPAPVPAPALAPAPVPVPAPTPVPSRSSEQVYFSLKDMFMETTRAGRSQEEEKPPPPSTRVAGESPPGKTPVKSRLEKVPMVSSQPTSSMVPPPIKPLNRKRFAPPKSKVESTTTSLSSQTSESMAQSLGKALPSASTQVPTPPARRRHGTRDSPLQGQTSHKTPGEALESPATVAPTKSANSSSDTVSVDHDSSGNQGATEPMDTETQEDGRTLVDGRTGSRKKTHTDGKLQVDGRTQGDGAQDRAHASPRTQAGEKAPTDVVTQGSERPQSDRSSWKNLVTQRRVDMQVGQMQAGERWQQDPGDARIQEEEKETQSAAGSIPVAFETQSEQLSMASLSSLPGALKGSPSGCPRESQAIECFEKSTEAPCVQERSDLMLRSEEAAFRSHEDGLLGPPSGNRTYPTQLPPEGHSEHLGGQTHQRSEQEDSLSQCPKKEQPQEPLHVGLSGGHSTGLSQEVPAMPSLPGTGLTSSLQEELPGTAASLHTNTDVPLPSRDQDFPSSAPTLQLGPGSPTQSHPPEAMATSSEGACAKEPNVDGRSSGTRSCDPGLIDSLKNYLLLLLKLSSPETSEARAESQEVADTGGLTSSSTLVPTMEVAGLSPRTSRRILERVENNHLVQSAQTLLLSPCTSRRLTGLLDREVQAGQQALAAAQCSRGPCPTPLTIPAIVVGEEGSAGEDSEERTSQESDKKGLLGEVEGHTVESRTQEPCQEEAMPGEALTGLPAATPEELALGARRKRFLPKVRAGSDGEANKAEERESPTVSPRGPRKGLTPGSPGTPGRERRSPTQARKASMLEVPGAEEEPATGDLVSRSKDSGLDSEPAVDEGKQEALAKQRKAKDLLKAPQVIRKIRVEQFPDSSGSLKLWCQFFNIVSDSVLTWAKDQHPVGEVNRSAGDEGPAALAIVQASPTDCGVYRCTIQNEHGSASTDFCLSPEVLSGFISREEGEVGEEIEMTPMVFAKGLADSGCWGDKLFGRLVSEELRGGGHGLQKASRAKVIYGLEPIFESGRTCIIKVSSLLVFGPSSETSLLGRNYDVTIQGCKIQNMSREYCKIFAAEARAASGFGEVPEIIPLYLIYRPANNIPYATLEEDLGKPLQTYCSRQWGCAGAPAAASSSEALQKCQTFQHWLYQWTNGSFLVTDLTGADWKMTDVQIATKLRGYQGLKESCFPALLDQFASSHQCNTYCDMLGLKPLKGPEAAHPQAKAKGSKSPSAGRKGSQLSPQPQKKGLPSPQGSRKSAPSSRATLQASQAATVQLLGQPPVQDGSSKAQSMR
The following text describes a protein:
Function:
Has NAD(+) glycohydrolase activity and extremely low ADP-ribosyltransferase activity.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MPSNICKFFLTWWLIQQVTGLTGPLMLDTAPNAFDDQYEGCVNKMEEKAPLLLKEDFNKSEKLKVAWEEAKKRWNNIKPSMSYPKGFNDFHGTALVAYTGSIGVDFNRAVREFKENPGQFHYKAFHYYLTRALQLLSNGDCHSVYRGTKTRFHYTGAGSVRFGQFTSSSLSKTVAQSPEFFSDDGTLFIIKTCLGVYIKEFSFYPDQEEVLIPGYEVYQKVRTQGYNEIFLDSPKRKKSNYNCLYSSAGTRESCVSLFLVVLTSLLVQLLCLAEP
The following text describes a protein:
Function:
Involved in the N-terminal endoproteolytic cleavage of the P2 precursor of the a-factor mating pheromone. Capable of proteolysing the established mammalian insulin-degrading enzymes (IDEs) substrates amyloid-beta peptide and insulin B-chain.
Subcellular Localization:
Membrane; Peripheral membrane protein.
Sequence:
MGVSLLASSSAFVTKPLLTQLVHLSPISLNFTVRRFKPFTCLSRYYTTNPYNMTSNFKTFNLDFLKPDLDERSYRFIELPNKLKALLIQDPKADKAAASLDVNIGAFEDPKNLPGLAHFCEHLLFMGSEKFPDENEYSSYLSKHGGSSNAYTASQNTNYFFEVNHQHLFGALDRFSGFFSCPLFNKDSTDKEINAVNSENKKNLQNDIWRIYQLDKSLTNTKHPYHKFSTGNIETLGTLPKENGLNVRDELLKFHKNFYSANLMKLCILGREDLDTLSDWTYDLFKDVANNGREVPLYAEPIMQPEHLQKIIQVRPVKDLKKLEISFTVPDMEEHWESKPPRILSHLIGHEGSGSLLAHLKKLGWANELSAGGHTVSKGNAFFAVDIDLTDNGLTHYRDVIVLIFQYIEMLKNSLPQKWIFNELQDISNATFKFKQAGSPSSTVSSLAKCLEKDYIPVSRILAMGLLTKYEPDLLTQYTDALVPENSRVTLISRSLETDSAEKWYGTAYKVVDYPADLIKNMKSPGLNPALTLPRPNEFVSTNFKVDKIDGIKPLDEPVLLLSDDVSKLWYKKDDRFWQPRGYIYLSFKLPHTHASIINSMLSTLYTQLANDALKDVQYDAACADLRISFNKTNQGLAITASGFNEKLIILLTRFLQGVNSFEPKKDRFEILKDKTIRHLKNLLYEVPYSQMSNYYNAIINERSWSTAEKLQVFEKLTFEQLINFIPTIYEGVYFETLIHGNIKHEEALEVDSLIKSLIPNNIHNLQVSNNRLRSYLLPKGKTFRYETALKDSQNVNSCIQHVTQLDVYSEDLSALSGLFAQLIHEPCFDTLRTKEQLGYVVFSSSLNNHGTANIRILIQSEHTTPYLEWRINNFYETFGQVLRDMPEEDFEKHKEALCNSLLQKFKNMAEESARYTAAIYLGDYNFTHRQKKAKLVANITKQQMIDFYENYIMSENASKLILHLKSQVENKELNENELDTAKYPTGQLIEDVGAFKSTLFVAPVRQPMKDFEISAPPKLNNSSESE
The following text describes a protein:
Function:
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB).
Subcellular Localization:
Endosome membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MFRAQSNIFDDVVVKATDENLTSENWEYILDVCDKVGSSDTGAKDAVAAMIKRLAHRNANVQLYTLELANALSQNCGIQMHKELASRSFTDAMLRLANDRNTHQAVKAKILERMGEWSEMFSRDPDLGIMEGAYMKLKTQNPNLRAPSKPQKTQISDSDRQKEEEELQMALAMSIKESKGATPSAAKANAPQESNAGSSSQAAPAPQPVQPGTTAATVSRVRALFDFQPSEPGELQFKKGDIIAVLESVYKDWWKGSLRGNTGIFPLNYVEKLQDPTREELEKEAQTEAEVFAQIRNVEKLLALLSTNTQAGGGDGRDNEEITELYHSTLAIRPKLIELIGKYSQKKDDFTQLNEKFIKARRDYESLLEASMSQPPQPSYGSRPPYGYNAPPPSNYTGYPPSSPPPQQYGYGAGAPPQGSAPQYPPVGANPAFFMVPPAGEQRPQQQTPQPGPPSDPYSLPQGRVPIGGRPQSYAPQELATAHYDSPVDNRHSFAGPSQPQGAPSAPQGYEYPPSQAPPGYPPQQGAPLQGPPPGQQNPYEQISSPPTHQQPPSDPYSQPPPQVGHGYPPQQPAHAPPAPPGASSSPAPAQGYLPYRPPGQAPSAPPVGGGGDEGFYR