lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Critical mediator, in cooperation with CASP4, of endoplasmic reticulum-stress induced apoptosis. Required or the activation of CASP4 following endoplasmic reticulum stress.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MAPAAAVDSSPLQDWSDEMESNGDFELASSSGNGSGAPGAPDHGWHKVTNPKKQRLRERKLKAEGGGGGEGGAGLGQDGKNSSKAFEALEKEAEARTERRKSRKAAWSASVAAAATPAANGVHDPHGSDDEEQGSDVESKNAAVANGGGGSANGGEKKKKAKKPKVSIADAAAAIDPVDLADYLATLSASYDDIQLIRCVDYFVKIFSPVNTVEIAWDKMSRDPLLKSVQVPIGDLPDKVCRATANWLGQKSVDALSQFVSWALNDVLFEAQPQQKGGKSGPTVSNSTKIAVLVVVAILLRRRSEVLLGMMETLRQPKFQAPPKLYVLAWMYGQVAREDLLAGLYLWSHNLLPFAVGSSSTPVTRDIALQFFEGFVMKDLAKNRPSLLTGATRKERLISPHALIACLHMAYPPESSRTKATQRYLAIYPTVKEISLGGSTRTRALKTVAQQLLPMSLTVAEEDDAELSLEGCDLFRWCLFQSPDSYKQWEKLYPERLKGSVRVLKFLRGTWRESQSMLSPLKELQSTVTSLKLQSLKMKQDPKLEAESIKALDHCKFLQKKMSLWNACLSASVALACTAAAGYAFYLLSPDKNPWNWDGKILLSNL
The following text describes a protein:
Function:
The phosphorylation of phosphatidylinositol (PI) to PI4P is the first committed step in the generation of phosphatidylinositol 4,5-bisphosphate (PIP2), a precursor of the second messenger inositol 1,4,5-trisphosphate (InsP3) (By similarity). Undergoes autophosphorylation and phosphorylates serine/threonine residues of protein substrates. Phosphorylates RPN10 and UFD1 in vitro.
Subcellular Localization:
Membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MSSAGVALSPVRSEPLIMPLVRANSCLDSYPDDTIMIYLTLPGSVIPMRVLESDSIESVKLRIQSYRGFVVRNQKLVFGGRELARSNSNMRDYGVSEGNILHLVLKLSDLQVLDVKTTCGKHCRFHVERGRNIGYVKKQISKKRGDFVDPDEQEILYEGEKLEDQSLINDICRNDDSVLHLLVRRSAKVRVKPVEKNFELSIVAPQAKDKKGREAKSIVPPKKLSLEPVVVNSKAKVPLVVKDMIQSASDGLKSGNSPVRSSEGTGGAYFMQGPSGNKFVGVFKPIDEEPMAENNPQGLPLSPNGEGLKKGTKVGEGALREVAAYILDHPKSGNKSMFGEEIGFAGVPPTAMIECLHPGFNHPKGIKTKIGSLQMFTENDGSCEDMGPLSFPVEEVHKISVLDIRLANADRHGGNILMTKDESGKLVLVPIDHGYCLPESFEDCTFEWLYWPQARKPYSAETQEYIRSLDAEEDIDLLKFHGWKMPAETAQTLRISTMLLKKGVERGLTAFEIGTIMCRETLSKKSLVEEMVEEAQEAVLPGTSEAAFLEALSDVMDYHLDHSQEH
The following text describes a protein:
Function:
Catalyzes the activation of phenylacetic acid (PA) to phenylacetyl-CoA (PA-CoA).
Sequence:
MSSEPTTGTAPAPRRGEPLPHDLLDDAERLSREQLRELQLDRLRATLRHAYDNVELYRKKFDAAGVTPDDCRSLADLSRFPFTTKADLRDTYPFGMFAVPMADVRRVHASSGTTGRATVVGYTENDLSMWADVVARSIRAAGGRPGHKVHISYGYGLFTGGLGAHYGAERAGCTVIPASGGMTARQVQIIQDFRPEIIMVTPSYMLTLLDEFERQGVDPRTSSLQVGIFGAEPWTEEMRREIEERMDIHAVDIYGLSEVIGPGVAQECVETKDGLHIWEDHFYPEVVDPLTDAVLPGGEEGEIVFTSLTKEALPVIRYRTRDLTRLLPGTARPAFRRMRKVTGRCDDMIILRGVNVFPTQVEEIVLRTPGVAPHFQMRLTERGRMDHMTVRVEARPDAAPEQRDAAARAIAQGVKDGVGVTVEVEVVEPETLERSLGKIRRVWDQRGA
The following text describes a protein:
Function:
Required for protein transport between the Golgi and the endoplasmic reticulum. May tether coatomer-coated retrograde transport vesicles to the ER membrane through interaction with coatomer as well as the SNARE complex. May contribute to the stabilization of the SNARE complex.
Miscellaneous:
MISCELLANEOUS: Present with 8970 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MESLFPNKGEIIRELLKDPLILKNDSKRSNGSELELDSSDLLQREAILANELNILDNLKTFLNLIKEVKTNLNILELENCYYSLQSLRKKMRNNAAYLKQSFNFQQSISTYVDTLHLELVSTLYKILTNGFWKITENSIQFTPTVEWGKDKVHIEYDTFMDFVAQQYFPKGSLDNQAWFILDMTSADSQEQVRAKLNTIMKEYMNLSRIVSMIKNSIFISGKEISYENEKNILVFSKSSSHGQHCVSTVLTSFEAVCDFMLDGLAFRDRKTLSYELGPLFNTEFTKFVKNNASIILESLDSPLKNLVSVINNKLTRLVAKSEVTNWTHSGKEIQDLLMNKQLYYNLLLDKVLESHISEIRSIFEDPKKSWQNLEVVELTTSNTNTMSEKIGKNDSDVQNEKELHNAVSKDDDWNWEVEDDDADAWGDEIDVNIDDEEEKTNQEKEKEPEEEENAWDEAWAIDENIDDASLENGKEHLKAHDVGSLDKDHIEVTQLPKLFLAISQNFKSSFADSHVDEQYFAYKYNLLQTSYMAMCTANFSHNWCQLYVDMRYLIERDEKLYRIKELTRNLLETKLNMKYRIVCQLIRHQLTEFRENERNPSWDATIEKLLPYILKEIVRPLQKIRGEEGSRYLLSFLNFLYNDCVTKEILKWQIISEVNSENLGELVSLLVNNTDIQLLAKEPSYKKMREKFATMGKFLPLHLKEIMEMFYNGDFYLFATDELIQWIELLFADTPLRRNAIDDIYEIRGTALDD
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.
Sequence:
MEAGYQRKLTETGGDSGDNVKGLEKETEAKIQNLKTKAGIISDDVDMLLKNVTSVKY
The following text describes a protein:
Function:
Receptor for the C-X-C chemokine CXCL16. Used as a coreceptor by SIVs and by strains of HIV-2 and m-tropic HIV-1.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MFSGNMNHITKVEADLASRASSSVEQTGKAPLLVFIRTNTMAEYDHYEDDGFLNSFNDSSQEEHQDFLQFRKVFLPCMYLVVFVCGLVGNSLVLVISIFYHKLQSLTDVFLVNLPLADLVFVCTLPFWAYAGIHEWIFGQVMCKTLLGVYTINFYTSMLILTCITVDRFIVVVKATKAYNQQAKRMTWGKVICLLIWVISLLVSLPQIIYGNVFNLDKLICGYHDEEISTVVLATQMTLGFFLPLLAMIVCYSVIIKTLLHAGGFQKHRSLKIIFLVMAVFLLTQTPFNLVKLIRSTHWEYYAMTSFHYTIIVTEAIAYLRACLNPVLYAFVSLKFRKNFWKLVKDIGCLPYLGVSHQWKSSEDNSKTFSASHNVEATSMFQL
The following text describes a protein:
Function:
May be involved in the metabolism of insect hormones and in the breakdown of synthetic insecticides.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Sequence:
MLWEFFALFAIAAALFYRWASANNDFFKDRGIAYEKPVLYFGNMAGMFLRKRAMFDIVCDLYTKGGSKKFFGIFEQRQPLLMVRDPDLIKQITIKDFDHFINHRNVFATSSDDDPHDMSNLFGSSLFSMRDARWKDMRSTLSPAFTGSKMRQMFQLMNQVAKEAVDCLKQDDSRVQENELDMKDYCTRFTNDVIASTAFGLQVNSFKDRENTFYQMGKKLTTFTFLQSMKFMLFFALKGLNKILKVELFDRKSTQYFVRLVLDAMKYRQEHNIVRPDMINMLMEARGIIQTEKTKASAVREWSDRDIVAQCFVFFFAGFETSAVLMCFTAHELMENQDVQQRLYEEVQQVDQDLEGKELTYEAIMGMKYLDQVVNEVLRKWPAAIAVDRECNKDITFDVDGQKVEVKKGDVIWLPTCGFHRDPKYFENPMKFDPERFSDENKESIQPFTYFPFGLGQRNCIGSRFALLEAKAVIYYLLKDYRFAPAKKSCIPLELITSGFQLSPKGGFWIKLVQRN
The following text describes a protein:
Function:
Plays a role in nuclear translocation of the viral pre-integration complex (PIC), thus is required for the virus to infect non-dividing cells. Targets specific host proteins for degradation by the 26S proteasome. Acts by associating with the cellular CUL4A-DDB1 E3 ligase complex through direct interaction with host VPRPB/DCAF-1. This change in the E3 ligase substrate specificity results in the degradation of host SAMHD1. In turn, SAMHD1 depletion allows viral replication in host myeloid cells by preventing SAMHD1-mediated hydrolysis of intracellular dNTPs necessary for reverse transcription (By similarity).
Subcellular Localization:
Virion. Host nucleus. Note=Nuclear just after virion uncoating, or if expressed in the absence of unprocessed GAG.
Sequence:
MTDPRERVPPGNSGEETIGEAFEWLDRTIEALNREAVNHLPRELIFQVWQRSWRYWHDDQGMSPSYTKYRYLCLMQKAVFIHFKRGCTCLGGGHGPGGWRSGPPPPPPPGLV
The following text describes a protein:
Function:
Regulates the function of the receptor protein kinase WAK1.
Miscellaneous:
MISCELLANEOUS: GRP3 and GRP3S bind to WAK1, WAK3 and WAK5, but GRP2, GRP4,GRP6, GRP7 and GRP8 did not bind to any of the WAK isoforms.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MASKTLLLLGLFAFLFIVSEMAAAGTVKSESEETVKPEQHGGGFGDNGGGRYQGGGGHGGHGGGGYQGGGGRYQGGGGRQGGGGSYCRHGCCYKGYHGCSRCCSYAGEAVQTQSGH
The following text describes a protein:
Function:
Associates with cyclin G and CDK5. Seems to act as an auxilin homolog that is involved in the uncoating of clathrin-coated vesicles by Hsc70 in non-neuronal cells. Expression oscillates slightly during the cell cycle, peaking at G1. May play a role in clathrin-mediated endocytosis and intracellular trafficking, and in the dynamics of clathrin assembly/disassembly.
Subcellular Localization:
Cell junction, focal adhesion. Cytoplasm, perinuclear region. Cytoplasmic vesicle, clathrin-coated vesicle. Golgi apparatus, trans-Golgi network.
Sequence:
MTDLFRSAFGILGGPSDRGNEFVGQQVELGDTKLKVRRVIAEGGFAFVYVAQENSTGKEFALKRLLANDEEKSKEILQEIAILKRLSGHPSIVQFFSAASIGKGDTDHGQSEYLLLMELCPGGQLVDAINQRHMPLSCDDVLQTFYQACRGVQHMHKQTPPVTHRDIKLENFLIGSKKTLKLCDFGSATSKSYQPDSSWSSLKRSTLEDEFARHTTPMYRPPEILDLYENFPINHAMDVWALGCMLYTMCYRQHPFEDSAKLRIINANYTIPEDDEEYMILHDLIRAMLQVDPRNRPPLEVIVAQLQEIAAAREVTLKGPLRMLDSRASPVQHTASPAKRAPEREGAVPDSVDSAGNFLGMMKGAGGNLLRNLKDTSSRVAQTVASYTKSELDISYITSRIIVMSFPAEGLESTYKNGIDDVRSFLETRHSGHYHVFNLSQRTYRPAKFENRVSDCGFPAKRPPNLVLLYHVCRNMYLWMQRDPKNVCVIHCMDGKASSATIVSSFLTFCRLFSTVDVSLYMFSVKRGPPGITQSQKRYMEYISGMLSPTASIMPHQRVLLIKSLRLTPVPLYNKMRSGCRPFCEVFHDEERILSTSQEYERMRGFEVEDASAFIDLNIPVCGDVMVVVYHARSTFGGKVQGKVTGLKMFQFQFNTGFIEPGTKEISFNRYELDFFELDKFAEHFHASLDVVVSEKDRPSQKPPPWTTFETKRLTPKYCFSGQEEWDSVTAQFGQMDAKAQRRLEKERSEQQPSESKPTAPRQTTPPPKQAAPREAPAEAKKPFFQTLDWQEGGPPQTEGHVRLPTQEHETLIDDDDDSDDDDFNSFQAQRLSEMSQNSTVSQSQQSQGQGSGNDANFFQSDINETSQSSTNQENLFADFSSAMSQSEQTTDLLNIGGESTPASQPAVEPDLMAPPPRDPTNFDLLVDSTAELNMGTSPAGNGQSKDTFDPFMQAKPSQPSAPKQTKAQEKPFDNVKFDPFASQPTSQQGTPKATPKQESQPSSAGAKNNLFDPFASFGQPSPSMSGTSSQPSPASASKPLFDPFGAQPRSTPSPTPASTSNLSAPQGGMTRQTHSSDNLLGDLGSFSQNGGPTLKQSNSGPDLMAGWNQGGPRSTPMQSGSNRTPQHSTRPTPPPAKVDPFSNFGNFSSPSPSTAGGPMGGSPAMGGGGQPSPQKQRQSPGFGAGRQQPMMSSQAQSPSHRPFQPQSQTMPQKTATPPPPQAAKPNYFAGGFASSSVIGGREERGKRDGGFMTSKAAKQADFSNLLSDQQKFQASAKSHETKTINDMKRKEIEATTDPNVLKVRDWTQGKENNIRALICSMHQVLWDGEDRWKPVGMHQLVEHNQVKKWYRKAVLSAHPDKQVGTPNEELAKLIFMELSDAWSAFEEAGAQALF
The following text describes a protein:
Function:
Primarily acts as an independent SigF regulator that is sensitive to the osmosensory signal, mediating the cross talk of PknD with the SigF regulon. Possesses both phosphatase and kinase activities. The kinase domain functions as a classic anti-sigma factor-like kinase to phosphorylate the anti-anti-sigma factor domain at the canonical regulatory site, and the phosphatase domain antagonizes this activity.
Sequence:
MGAAGSAGFEGEPSPRGPVRPSGLLDLLNVASIVLDTEGRIVLWSPQAEELFGWSAPEALGQYAARIMVHERHLDLVVRLFGDVMKTGRSWAGAFPVRHKDGSTRLVEFRNMRLVDDRGDVYALGLAADQSTVRRLERDVALSTRVIMQSPIGLAVLDTDLRYVSVNPALERLNGIPAEEHLGRTVRELLPQVDADPLEAAARGVLETGRPVVDLPATGRTPADPDEEHAWSVSLYRLEDALGAVLGVAVSIVDVTEQYRTAAEAEGARRRLAAVADASARIGTTLRLDRTAYELADVAVPGLADVAAVDLLDAVVEGRRSTLGPAEPAVIRALAVRADDAARDALRAADPPGGVARYAPDRLVTECVRTARPVLVSRVTRKDLGRIARSPEAAELLRRAGVHSYLAVPLIARGEVLGALDLKRISNPLPFDEDDLLLARELAARAALQIDNARWYQNARDTALTLQRSLLPSHPPVTGGLEVASRYQPAGGTSEVGGDWFDVIELAGGRTALVVGDVMGSGIAAAASMGRLRTATNTLAALELDPAQLLGHLERTTAGLDQAIATCLYAVHDPHRRRCLIANAGHLPPVRLRAGRPPELLDLPTGVPLGVGGVAFSTTEVGLEPGDRLVFYTDGLVETRRHPLDERLAALLALLEGPDRPLEEVCDLLLRTLHEPENSDDVALLIARATPPARRGGGTLSP
The following text describes a protein:
Function:
May reduce toxic product malonic semialdehyde to 3-hydroxypropionic acid, which is excreted. RutE is apparently supplemented by YdfG. Required in vivo, but not in vitro in pyrimidine nitrogen degradation.
Miscellaneous:
MISCELLANEOUS: The Rut pathway degrades exogenous pyrimidines as the sole nitrogen source at room temperature but not at 37 degrees Celsius, a restriction that is apparently a consequence of an inadequate ability to remove toxic malonic semialdehyde at the higher temperature (RutE/YdfG function).
Sequence:
MNEAVSPGALSTLFTDARTHNGWRETPVSDETLREIYALMKWGPTSANCSPARIVFTRTAEGKERLRPALSSGNLQKTLTAPVTAIVAWDSEFYERLPLLFPHGDARSWFTSSPQLAEETAFRNSSMQAAYLIVACRALGLDTGPMSGFDRQHVDDAFFTGSTLKSNLLINIGYGDSSKLYARLPRLSFEEACGLL
The following text describes a protein:
Function:
Catalytic subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein PAB1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenylation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by XRN1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails.
Subcellular Localization:
Cytoplasm.
Domain:
Contains a pseudo-UCH domain. This ubiquitin C-terminal hydrolase (UCH)-like or ubiquitin specific protease (USP)-like domain is predicted to be catalytically inactive because it lacks the active site catalytic triad characteristic of thiol proteases, with residues at the equivalent structural positions that are incompatible with catalysis, and it cannot bind ubiquitin. It functions as a structural scaffold for intra- and intermolecular interactions in the complex; The linker, or PAN3 interaction domain (PID), between the WD40 repeats and the pseudo-UCH domain mediates interaction with PAN3.
Sequence:
MEGWQEPPRIPLTQICRVSHTAPVATEIGQLTDTLPLTFDLAEDLVWAGDTNGIVSSYYGETLQPYSRFRAGRGRVTSLVSHDRGLVALTTDALHYSTRGGLTRKHVTDPSLGNNLCMTFTHGPTEFVVGGNPGKLVVVNSERGDVTRVVDSPGMATHMAGSSSCVVWGTENGKLVVGDNNLKELHTFQAHQGPFSDVSVQDNVVMTCGFSAASTGHRIDPLIKVWDLRMMRAMAPISYPLAAFVCQTPDSRTLITSPSGQLEFLDHATQQIKLYQAEVALVNGVKLSPRGHHFVVSDTSGQLQLWSDEPQSSFAEFSAPTAFPTPEQSYPPVSIRDTRYPLGAVGMPYYSDTLLSAMPSSIINVGMPPEEVDEDLEVRQIDFVGHAPNYKQQKRNLAQKYSNQRRTSIAAPKFLSEKEKERARRMEDIEDESFFGDEDTCTEASMSSKKVPRLYRKLEIKYSKFGISDFDFSYYNNHTGLSGLETNPFNPLLQLFRFCSPVFNFALRSVARGTPNRLLNEVGLLFDMMHKARGHVCRASNLMHCYDGIAQTRSLAPEDATNIVLFCRFLLEQIGFEQRQTPALFDSFRQLLGATVITVNTFSCGKMAQAESVWYTLELALGSTFYECLERTLDKELHTRAWCDKCRKYQSLHVSKHVESLPQVLTLSVADGNVDVAKSFLVLDGKVSPAAETDNDAYKLVGFICQIQGNGQVAFIRVGDEWYLFNDFLVTKVSEKEAFMKTPWKRTVMMVYAVGADERFDYDSWKNDMDVSALFEERLVNGNNVSRETTDYGYELIKEVPPPKTLCAIDAEFVVLKNEETEIRSDGTKVVLAPRNLCLARVTLLNEDGHPFINDYIAINEHIVDYLTAFSGIEPGDLDPSISRKPLVSLPTSYRRLWLLLNLGCVFVGHGLANDFRTINMQVPPEQVIDTVDLYYIPSERRKLSLRFLAWCVLGKKVQSGNHDSTEDSHTALLLYKKYQDCAPEEFQVLLLDVYRQGRMCNFKVPEA
The following text describes a protein:
Function:
Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA.
Sequence:
MKLVKHIANLGYGSRKQVTQLFRQGAITDAAGEVLYADDQVDHAAIRIDGEPLDPPPGFSVLLHKPSGYTCSTKDTGRLIYELLPPRFRLRAPVLAPVGRLDRETSGMLLMTDDGALLHRIISPKSALDKVYDVTLAEDLRGDEAALFASGTLLLEGETKPLLPAELEVLGARQARLTLHEGRYHQVRRMFAAAGNHVVALHRSRIGGLSLDGLDAGHWRPLGPDDLEVLFGRGDAA
The following text describes a protein:
Function:
Multifunctional protein that plays a critical role in regulating the availability of IGFs such as IGF1 and IGF2 to their receptors and thereby regulates IGF-mediated cellular processes including cell migration, proliferation, differentiation or apoptosis in a cell-type specific manner. Also plays a positive role in cell migration by interacting with integrin ITGA5:ITGB1 through its RGD motif. Mechanistically, binding to integrins leads to activation of focal adhesion kinase/PTK2 and stimulation of the mitogen-activated protein kinase (MAPK) pathway. Regulates cardiomyocyte apoptosis by suppressing HIF-1alpha/HIF1A ubiquitination and subsequent degradation (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MSEVPVARVWLVLLLLTVQVGVTAGAPWQCAPCSAEKLALCPPVSASCSEVTRSAGCGCCPMCALPLGAACGVATARCARGLSCRALPGEQQPLHALTRGQGACVQESDASAPHAAEAGSPESPESTEITEEELLDNFHLMAPSEEDHSILWDAISTYDGSKALHVTNIKKWKEPCRIELYRVVESLAKAQETSGEEISKFYLPNCNKNGFYHSRQCETSMDGEAGLCWCVYPWNGKRIPGSPEIRGDPNCQIYFNVQN
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:
MSRALLRSVLELRTPVTRLPPSFLLPFRPAARFLHQTAQQVEPTSQSDAAAAAATLLKASPPKVTTATTPEAPAAVPTSTPFSQQPPISQQVKELLPVLAAQPGHYTTIHIHGKPYLVTEGDTVKLPFKMPGVAPGDVLRLNRASVIGSRDLTLQGAPYVDERLFECRAIVMGTESEPMRVMIKKKRRCRKKKHVFSKHKYTVLRINQLKINDVSSL
The following text describes a protein:
Function:
Mediates sugar transport across membranes.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endomembrane system; Multi-pass membrane protein.
Sequence:
MFLEIFRVWIGFFSISFIFLPIYLVLDWKKRGTSDGFSAVVLIIPGIIQSFWLRHGWMTNEWTHIIINTVNLTALSFYISAYAYYQSNRKNLIGQLISAVIIVKCAFFYVDSHDAEHTNSAMGTVAAGAQILGLGGRVYEMRRAVKLGTTEYIPAFMQFAVSALMAQWLLFGIVTGNQFIANANVAGLTASAITLYLYFKYPPLTWTVPLFNIPPQNAKKE
The following text describes a protein:
Function:
Functions as an E3 ubiquitin ligase.
Sequence:
MEDQEKGALVESLIETVNEIASISEYRSTVKKQYCNLARRLKLLIPMFEEIKESKEPIQEQTFKALLALKVALHSAKDLLRDGSEGSKIYLVLKREQIMDKYHEVTAQLEQALSGISYENLDISDEVKEQVELVLAQFRRAKGRADTPDVELYEDLLLLFNKSNDAAIDPAVLRRSSEKLQLRGIADLTQESLALHEMVAATGGDPGANIEKMSMLLKKIKDFVQTENPNMDAPGREKNLPPSSSGQTSTNTNHKAPVIPDDFRCPISLELMKDPVIVSTGQTYERSCIEKWLEAGHVTCPKTQQNLNSTALTPNYVLRSLIAQWCEANGMEPPKRPSSSRSNKTTSAYSPAERTKIENLLHKLTSGSPEDQRSAAGEIRLLAKRNADNRVAIAEAGAIPLLVDLLSTPDSRTQEHAVTALLNLSICEDNKGSIISAGAVPGIVHVLKKGSMEARENAAATLFSLSVVDENKVTIGSSGAIPPLVTLLSEGTQRGKKDAATALFNLCIYQGNKGKAVRAGVVPTLMRLLTEPGGGMVDEALAILAILASHPEGKSAIGAAEAVPVLVEVIGNGSPRNKENAAAVMVHLCAGDQKHLAEAQELGIMGPLVDLAQTGTDRGKRKARQLLECMSRFVEQQKQAQAQAEAQTQQPQPSSTANSADS
The following text describes a protein:
Function:
Component of the NOP7 complex, which is required for maturation of the 25S and 5.8S ribosomal RNAs and formation of the 60S ribosome.
Subcellular Localization:
Nucleus, nucleolus. Nucleus, nucleoplasm.
Sequence:
MAGRSKKKGTSGAAKNYITRTRAVKKLQISLPDFRRLCIFKGIYPREPRNKKKVSKGSTAQTTFYYTKDIQYLLHEPLLAKFREHKSVAKKIGRALGRGEAGDAARLEKNLMPKVKLDHIIKERYPTFVDALRDLDDALSMLFLFANLPSSDHIPAKTIALCQRLTREFEHYVITSHALRKSFLSIKGIYYQATIQGQDILWLVPYRFVQRTGGDIDFRIMGTFVEFYTTLLGFVNYRLYTSVGLVYPPKFNAKSDEQGGELAAFQLEGKANATNGASNDHDDDVEINPEAQAKADKIAAMADDEDEQEVEMAEADAEDDDEEENTEGIDKFEPTAPDADILPQPQASSAEIASLFAPFTFYLAREVPRASLEFILKAFGCKRVGWDSILGDGAFTTNESDPNITHQIVDRPPLANGASAAGAEDAATPQVQWPHSTKPGRTYVQPQWVWDCINQGKLLRPDLYAPGAELPPHLSPWVKPKKGEYDPNLPLAAQQPDGEAEAFEDLADEDEDAFEVDDDEDMDAVADREGSVEVGEGMDVADSDDDDEDDSESDAEGGADGFAGFDDESEAESDISEGEAARLQHQRELEAEATGKKLDVKAPTKKEQNAAIRKKFDKKKRAEEEERDRQKMMLSNKKRKLLKRIEYGENKRDTESENLRRKRTRLEKAKAAAERA
The following text describes a protein:
Function:
Catalyzes the non-oxidative deamination of L-phenylalanine to form trans-cinnamic acid and a free ammonium ion (By similarity). Facilitates the commitment step in phenylpropanoid pathways that produce secondary metabolites such as lignins, coumarins and flavonoids (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MSLLLNGSVNGIPHSKPYNYSTLLSRFIESYNELQSYKSGKAVKVDGRTLSVAAVTAAARYHASVELDDCPTARARLAKSRKVITDKVESGTSVYGLSTGFGGSADTRTDQPLLLGHALLQHQHMGVLPSSSQALDVLPLLDPNSSTTMPESWVRGAMLIRMNSLIRGHSGVRWELIEKINEVLSANVTPVVPLRGSISASGDLSPLSYIAGTLVANPAIRVYHGPAAYGARQTSPSSDALTQYNIEPLPLASKEHLGILNGTAFSASVASLALNDAVHLSLLAQVCTAMGTEALAGTRGSYDPFIHATARPHPGQQIEAAHNIFTLLEESKLARLHETEVNIHDDQYSLRQDRYPLRTAPQFLGPQIEDILSALVAITQECNSTTDNPLVDGETGEVHHGGNFQAMAVTNAMEKTRLALHHIGKLLFAQSTELVNPTMNNGLPPSLAATDPSLNYHAKGIDIATAAYVAELGYLATPVSTHIQSAEMHNQAVNSLALISARATLNSLEVLSILMASYIYILCQALDLRALQSEFVSGLKNIINDELVSIFGSFLSASQEDTLSKKLLTIMKSSLEKTTTMDGVDQMLATAASTTTAFVDFFGSSEFTDASLLGSVVALISHFRSQVASRAANLLDQLRRDFLSGERGLAPASSYMGKTRLLYEFVRVTLGVRMHGSENYARFVNGLGVEDVSIGQNISLIHEAIRDGKMQPIVASLFT
The following text describes a protein:
Function:
Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis, it proteolytically cleaves poly(ADP-ribose) polymerase PARP1 at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9 (CASP6, CASP7 and CASP9, respectively). Cleaves and inactivates interleukin-18 (IL18) (By similarity). Triggers cell adhesion in sympathetic neurons through RET cleavage (By similarity). Cleaves IL-1 beta between an Asp and an Ala, releasing the mature cytokine which is involved in a variety of inflammatory processes (By similarity). Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. Acts as an inhibitor of type I interferon production during virus-induced apoptosis by mediating cleavage of antiviral proteins CGAS, IRF3 and MAVS, thereby preventing cytokine overproduction. Also involved in pyroptosis by mediating cleavage and activation of gasdermin-E (GSDME) (By similarity). Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface (By similarity). Cleaves BIRC6 following inhibition of BIRC6-caspase binding by DIABLO/SMAC (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MENTENSVDAKSFKNAETKILHGSKSMDSGMSFDNSYKMDYPEMGLCIIINNKNFHKSTGMAPRSGTDVDAANLRETFTNLKYEVRNKNDLTCEEILELMNSVSKEDHSKRSSFVCVLLSHGDEGIIFGTNGPVDLRKVTGFFRGDYCRSLTGKPKLFIIQACRGTELDCGIETDSGIEDDMACQKIPVEADFLYAYSTAPGYYSWRNSKDGSWFIQSLCAMLKLYAHKLEFMHILTRVNRKVATEFESFSLDSAFHGKKQIPCIVSMLTKELYLYH
The following text describes a protein:
Function:
Beta toxins bind voltage-independently at site-4 of sodium channels (Nav) and shift the voltage of activation toward more negative potentials thereby affecting sodium channel activation and promoting spontaneous and repetitive firing.
Subcellular Localization:
Secreted.
Domain:
Has the structural arrangement of an alpha-helix connected to antiparallel beta-sheets by disulfide bonds (CS-alpha/beta).
Sequence:
KDGYLVGNDGCKYSCLTRPGHYCASECSRVKGKDGYCYAWMACYCYNMPNWVKTWSRATNKCGKRK
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:
MRDLRKLIPRLRGPGTNVLKMKKPLPLHMRTKIREHLNKSDPTVKDDKSAKPELPFGKPADRVPFWHIFKGDYVYVHQGPLKGKWGRVVETNKYTNGITIEGVNVRSVKVPIFLLRNKPEDNQDPVIDIAHEVHYANVRLLAHAKTDAGEPVLIPVKLKKHSSTNLRSIIRPNIEGVQIHTIHLPRPKTEDKPKDPEGKLDTKNPVVSKVTWSPSLSEPPLPPFAIGDLRANWSRRLDRIWGYKKNNDDFTEIAKDLVRAETAAEDLIKKPISPNTYSD
The following text describes a protein:
Function:
Involved in pre-mRNA splicing and cell cycle control.
Subcellular Localization:
Nucleus.
Sequence:
MATTSHMFMYSLTIQPPTAITQAILGQFAGTKEQQIVTASGSKLTIHRPDPTQGKVIPLYTQDVFGIIRTLAAFRLAGSNKDYIIIGSDSGRITIIEYVPSQNRFNRIHLETFGKSGVRRVVPGQYLAVDPKGRACLIASVEKNKLVYVLNRNSQAELTISSPLEAHKPQTLVYSVVALDAGYENPVFAALEVDYSESDQDPTGRAYEEVEKLLVYYELDLGLNHVVRKWTDPVDRTSSMLFQVPGGADGPSGVLVCAEDNITYRHSNQDAFRVPIPRRKGAMENPERKRCITAGVMHKMRGAFFFLLQTEDGDLFKLTLDMVEDDKGQLTGEVKGLKIKYFDTVPLASSLLILKSGFLYVAAEGGNHHFYQFEKLGDDDEETEFNSDDFSADPAAPCTPVYFQPRGAENLNLVEAINSLNPLVDSKVVNISEDDAPQIFTVSGTGARSTFRTLKHGLEVSEIVESELPSVPSAVWTTKLTRADEFDAYIVLSFANGTLVLSIGETVEEVTDTGFLSSAPTLAVQQLGEDSLIQIHPRGIRHILADRRVNEWPAPQHRSIVAAATNERQVAVALSSGEIVYFELDADGSLAEYDERRQMSGTVTCLSLGEVPEGRVRSSFLAVGCDDSTVRILSLDPDTTLENKSVQALTAAPSALNIIAMADSSSGGTTLYLHIGLHSGVYLRTALDEVTGELSDTRTRFLGSKAVKLFQVSVTGQTAVLALSSRPWLGYSDTQTKGFMLTPLDYVGLEWGWNFSSEQCVEGMVGIQGQNLRIFSIEKLDNNMLQQSIPLAYTPRHFIKHPEEPLFYVIEADNNVLSPATRARLLEDSKARGGDTTVLPPEDFGYPRGTGHWASCIQIIDPLDAKAVVGAVELEENEAAVSIAAVPFTSQDDETFLVVGTAKDMTVNPPSSAGGYIHIYRFQEDGKELEFIHKTKVEEPPLALLGFQGRLLAGVGSVLRIYDLGMKQLLRKCQAAVAPKAIVGLQTQGSRIVVSDVRESVTYVVYKYQDNVLIPFVDDSIARWTTAATMVDYETTAGGDKFGNLWLVRCPKKASEEADEEGSGAHLIHDRGYLQGTPNRLELMIHVFTQDIPTSLHKTQLVAGGRDILVWTGFQGTIGILVPFVSREDVDFFQSLEMQLASQCPPLAGRDHLIYRSYYAPVKGVIDGDLCEQYFLLSNDTKMMIAAELDRSVREIERKISDMRTRVAY
The following text describes a protein:
Function:
Removes the 2'-phosphate from RNA via an intermediate in which the phosphate is ADP-ribosylated by NAD followed by a presumed transesterification to release the RNA and generate ADP-ribose 1''-2''-cyclic phosphate (APPR>P). May function as an ADP-ribosylase (By similarity).
Sequence:
MLRRAQTCRSATGNGGLKATVTLQAGFPGVHGVYRHAEVLSNLSVSMRPTFNPFKRGQAALLKLSAGILGRLPSGHTASLPIHTYTVINSAARGHCSFSLPQNRRRRLGLPAEGVPLDPALKNGACASLSVRRWRLFSAAPRAGEGWRHAGTRRVGAAGAAARLPAGQPGAPDAIRREGLRPVHRHHVSLSADTGAAQQVGARRGRAVALVVATGALREAGYDFFRSDNGVWLTDTVPPEYLIRFQIESRTYPGAILRGAHGKNTVLRRWTGIRRLSGCSGIG
The following text describes a protein:
Function:
Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins. Has a role in gonadogenesis (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MADEEISKAFRDLQFKTNETRMRIVQGEQNKKVNHQKMRISESTKRNLIGLNEDLKYYRSVGRMFLLTDKASEIARHETEAKQSKDKIEAIDKQKEYLEKGLVEAESNLRELIQSRR