lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
A major human immunogenic protein detected in patients recovering from meningitidis, where it induces bactericidal antibodies. Binds heparin and heparan sulfate proteoglycan in vitro via the Arg-rich motif. Heparin-binding to this protein protects bacteria against killing by bactericidal antibodies (serum killing). Binds to human cells via the Arg-rich region; binding may require the intact protein as protein fragments do not bind to human cells. Protein binding to human cells is abolished by treatment with heparinase III but not chondroitinase ABC. The bacteria binds a number of human extracellular sialyated and/or sulfated glycans via this protein, including chondroitin sulfate (KD=5.2 nM), heparin (KD=52 nM) and ganglioside GT3 (KD=210 nM). The recombinant protein binds DNA non-specifically; Plays a role in extracellular-DNA (eDNA) mediated biofilm formation. In strain MC58 eDNA stimulates biofilm formation. When NHBA is not processed by NalP there is an increase in positively charged, NHBA- and IgA-derived DNA-binding peptides on the cell surface, resulting in increased DNA-binding peptides and increased biofilm formation; [C2 fragment] Localizes to host mitochondria when applied to the apical side of human endothelial cell layers, where it induces production of reactive oxygen species which lead to increased permeability of host endothelial cells. The C1 fragment (which lacks the first 14 residues of C2) does not have this effect. It is not known if this occurs during Neisseria infections.
Subcellular Localization:
[Neisserial heparin binding antigen]: Cell outer membrane; Lipid-anchor. Cell surface; [C2 fragment]: Host mitochondrion. Note=This fragment is internalized by human cells.
Domain:
The signal peptide guides the autotransporter protein to the periplasm where it is lipid-anchored (presumably) in the outer membrane. Insertion of the C-terminal translocator domain in the outer membrane forms a hydrophilic pore for the translocation of the passenger domain to the bacterial cell surface, where subsequent cleavage by NalP or a host protease liberates C2; The C-terminus forms a beta-barrel with 8 anti-parallel strands.
Sequence:
MFKRSVIAMACIFALSACGGGGGGSPDVKSADTLSKPAAPVVSEKETEAKEDAPQAGSQGQGAPSAQGSQDMAAVSEENTGNGGAVTADNPKNEDEVAQNDMPQNAAGTDSSTPNHTPDPNMLAGNMENQATDAGESSQPANQPDMANAADGMQGDDPSAGGQNAGNTAAQGANQAGNNQAAGSSDPIPASNPAPANGGSNFGRVDLANGVLIDGPSQNITLTHCKGDSCSGNNFLDEEVQLKSEFEKLSDADKISNYKKDGKNDKFVGLVADSVQMKGINQYIIFYKPKPTSFARFRRSARSRRSLPAEMPLIPVNQADTLIVDGEAVSLTGHSGNIFAPEGNYRYLTYGAEKLPGGSYALRVQGEPAKGEMLAGAAVYNGEVLHFHTENGRPYPTRGRFAAKVDFGSKSVDGIIDSGDDLHMGTQKFKAAIDGNGFKGTWTENGSGDVSGKFYGPAGEEVAGKYSYRPTDAEKGGFGVFAGKKEQD
The following text describes a protein:
Function:
This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes. It can also provide electron transfer to heme oxygenase and cytochrome B5. Involved in ergosterol biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein; Cytoplasmic side. Mitochondrion outer membrane; Single-pass membrane protein; Cytoplasmic side. Cell membrane; Single-pass membrane protein; Cytoplasmic side.
Sequence:
MSILDILILMAVLAGTAVYFTHGKLWDKPKAQAAAFQGAGESFVEFANENDVKVGVFFGSQTGTAEDYAHRLAKDITASFGVNAVALDLMDYRFDDLDQLGEDRLVVFVVATYGEGDPTDNATDFMDFIGSDRTEFSNGKGADEQPLEGIRYAVFGLGNHTYQYYNAMGKKVDACMSTLGATRVGLLGLGDDAEGMLEEDYLEWKEDFLADFAGEFELSEKKEEYKPMYRIIEKPEVKSDSPSVFLGELNRQQLQNIPISAPVSSVNPLISCYKKTKELFKSDNRNCLHIEFDIKDSGLSYKTGDYVSVWPMNPSQAVDDLLDVLGLTAKRNTVIVVQPFNTMDKAPVLSPTTYDTVFRYYYDICGVVSRQFLSAIAVYAPTAETKAKLEKLGSDKDRFRKTVLDYHLNLAQVLRLVSPNRPFTNIPFSLLLEDMTHMKPRYYSISSSSLVHPDTVHITAVVSRKEWNEQEHVFYGVATNYLLAHCLHNGHQKKHHPNGLEYQIDGPRAKWAGGVPVFIKKSNFHLAPPNVPIIMVGPGTGVAPFRAFVMERAKLASDGVKVAKTVLFYGCQRSNEDFLYADEWKQYKEQMGDAFEMFCAFSREQDHKVYVQHKMLEHADLISDVIDNGGVFYICGDAERMAKDVTNALAEILTTPKVDGAKRVKELRDNNRFLEDTW
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core, and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane (By similarity).
Subcellular Localization:
Mitochondrion membrane.
Sequence:
MFSTSRIISRINYNFLRKSHYSTKTVAEQAKGRFTPLIQKLSAVQQPIMYWANVSKELVQQVYHSQKIAPPSNTHSPFLFWKSQSSEAWGRNFFIAVEIVGIFCAGQMVGRRKITPYH
The following text describes a protein:
Function:
Aminocarboxypropyltransferase that catalyzes the aminocarboxypropyl transfer on pseudouridine in 18S rRNA. It constitutes the last step in biosynthesis of the hypermodified N1-methyl-N3-(3-amino-3-carboxypropyl) pseudouridine (m1acp3-Psi).
Sequence:
MPRKASVEDLSSDSPEDSRECTSRRVSLFAYDYHQCDSKRCSAKRLEKLHLCRSIPKTAFFKGILLSSEGVYVISRLDRNTVQQHGLATVDCSWNEILADQVPITKLKCRNHRLLPFLLASNQVNYGKPFKLNCAEAFAAGLWICGYRDQALDTIQRFPYAKAFLDLNEELLDRYASCETSEAVLAVQEEVMNQLENEQRERELRKQTTNYQESVSHTSDTYDDSDK
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; This protein is one of the chains of the nonenzymatic membrane component (F0) of mitochondrial ATPase.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MNPLISAAFVIAAGLAVGLASIGPRVGQDTAAGQAVEGIARQPEAEGKIRGILLLSLAFMEALTIYGLVFPC
The following text describes a protein:
Function:
Catalyzes the specific hydrolysis of 1,4-dihydroxy-2-naphthoyl-CoA (DHNA-CoA) to 1,4-dihydroxy-2-naphthoate (DHNA), a reaction involved in phylloquinone (vitamin K1) biosynthesis. Is not active on benzoyl-CoA, phenylacetyl-CoA and aliphatic acyl-CoA thioesters.
Sequence:
MGTFTYERQVYLADTDGAGVVYFNQFLQMCHEAYESWLSSEHLSLQNIISVGDFALPLVHASIDFFAPAHCGDRLLVNLTITQASAHRFCCDYEISQAESAQLLARAQTHHVCIALPERKKAPLPQPWQTAICDLDHP
The following text describes a protein:
Function:
Methylates the 2'-O-ribose of nucleotides at positions 32 and 34 of the tRNA anticodon loop of substrate tRNAs.
Subcellular Localization:
Cytoplasm.
Sequence:
MGKSSKDKRDAYYRLAKEEGWRARSAYKLLQLDEEFNLFDGVTRVVDLCAAPGSWSQVLSRVLIKGEKFGRAGWQEKQAATRNYVLGVKPIEKSLEKLEIKEEAPKPREGVRIVAIDLQPMSPLEGVTTLRADITHPSTIPLMLKALDPDTYDPSATTASSPVDLVISDGAPDVTGLHDLDIYVQSQLLWAALNLALCVLKPGGKFVAKIFRGKDVDLLFAQLKIVFERVRVAKPRSSRASSIEAFVVCEGFCPPPGFTASLDQPLGAGTQIPTPVETQPQVEREARRTVREDGCIELDLGTEGESEEDDVEEGGKRWIAPFLACGDLSAYDSDATYHLPKDRVSLDPIQPPTAPPYRRALEMRKLAGGAYGKTKLK
The following text describes a protein:
Function:
Potentiates primary root protophloem differentiation. Regulates roots architecture.
Miscellaneous:
MISCELLANEOUS: Can complement the protophloem differentiation defect phenotypes of ops, brx and brx ops mutants.
Subcellular Localization:
Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasm.
Sequence:
MNLSADQAPVTAVDELAPPSQPHRLSTSCDLHPEERFSGFCPSCLCDRLSVLDHNAAPPPSSSSRKPPSISAVSLKALFKPSSSGTNNSNGNGRVRPGFFPELRRTKSFSAKNNEGFSGGFEPQRRSCDVRLRDDERNLPINEAASVDKIEEEARESSVSEIVLEVTEEAEIEEDEENGEKDPGEIVEEKSSEIGEEEEELKPMKDYMDLYSQTKKPSVKDFAGSFFSAASVFSKKLQKWKQKQKVKKPRNGVGGGRPQSEIGVGRRSSDTDPRFSLDAGRFSVDIGRISMDDSRYSLDEPRASWDGHLIGRTTAARVPLPPSMLSVVENAPLNRSDMQIPSSPSIKPISGDSDPIIIIPGGSNQTRDYYTGPPSSRRRKSLDRSNSIRKIVTELEDVKSVSNSTTTIDSNSMETAENKGNQNGDKKSRRWGKWSILGFIYRKGKDDEEEDRYSRSNSAGMVERSLSESWPEMRNGEGGGPKMRRSNSNVSWRSSGGGSARNKSSRYSSKDGENGMLRFYLTPMRRSWKTSGGSGGGGGGGGGGGWEKTAAKANSHGHSIARRVMRLY
The following text describes a protein:
Function:
Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA).
Sequence:
MGKTFAVIGDPIDHSLSPNIHSAAFRELNLDCSYIAYRIPKDELGEGIEGLKKIQIAGFNVTIPHKIEMMKYLDKIDESCSLIGAVNTVVSNDGVLKGYNTDMDGFLEPLKKRNIEIENSNVLLLGAGGAARAIVAGFAKEKAKSITIANRTIEKANNLVEFAKKISLDANAITIDQVGESAKDYNIIVNATSIGLQNESSPISFEGVNEKTVVYDIVYLPMNTDFLKKAKEKNATIIFGYEMLLGQAVRAFEIWHGMEAPYNAMKKALLGGF
The following text describes a protein:
Function:
Required for the assembly of the ubiquinol-cytochrome c reductase complex (mitochondrial respiratory chain complex III or cytochrome b-c1 complex), mediating cytochrome b recruitment and probably stabilization within the complex. Thereby, plays an important role in ATP production by mitochondria. Cardiolipin-binding protein, it may also control the cardiolipin composition of mitochondria membranes and their morphology.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MSGMRILTGSVALGGLTYAIWIIFSPGEERKKEILKSLPEANPVRMEETRKRNAIMLQVLKDAAETNDNIARGFGSQK
The following text describes a protein:
Function:
Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA).
Miscellaneous:
MISCELLANEOUS: During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA.
Domain:
Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization.
Sequence:
MIILKADYKKYNVSELEKLRMDEEKFYETFDNAILLQTCNRVEIIFDADSLEEIKGIENIDLEKFDILFGDKAIEHLFRVACGLESMIVGEDQILGQLKNAYLKAKEKGRISKKLEKIILKAIHTGQRARVETKINEGGVSIGSAAVELAEKIFGLEGKNVLLIGAGEMANLVIKALKEKNIKAIIVANRTYEKAEKLAKELGGMAIKFDKLEEALRYADIVISATGAPHPILNKERLKNAGKTIIIDIANPRDTTDDIRELPDIFLFTIDDLRLVAEENLKKRKEEIPKVEMIICEELERLKEFLDKMRFETAIKELGQYIENVRKKEVEKAKKILKNKNKPVEEVLEDFSKALCKRIIYDIIKIFENVEDKEVFECLAKEFKKLGNKNKN
The following text describes a protein:
Function:
Probable methyltransferase involved in the maturation of rRNA and in the biogenesis of ribosomal subunits.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MGKKAKIGKQRKDRYYHLAKETGYRSRSAFKLIQLNRKFSFLQESRVCIDLCAAPGGWLQVASRNMPISSMIIGVDLFPIKPIPNVVSFTCDITTTKCRMQLRKEMKTWKADCVLHDGAPNVGTSWVLDAFTQAQLTLHALKLAVEFLNKGGWFITKVFRSKDYQPLLWVFHQMFRKVHVTKPQASRNESAEIFVVCQGFISPDKIDPKFFDPKYIFKEVVGEETTKQKATILRDPSKVKKAKAEGYAEGDYTLYHPVQVSKYMASEDALELLNNCSELVFDDDSIASHHLTTKEIKICCRDIKVLGRREVRDLLNWHKKYNKEKAQLEEETANQVKEKSKLEGKDEDGESEEDEDDVVAKQLATIKEEERLAGKRKKKDALKKRKKLRERLHKSKELQSNMGDDTQGESLFGLVNIKNAQQLQKVNTDDAGTVANDNDGPPEKQKKQLPSLKPAKTPAVIDQEEELEEGEEEEEDDDDDGSLIDSDLEEDEANALRAEIDRVSGRYDSESDKGSDDMYSDDDDETGNPLMVDLEKMDPEESAKRRTKLWFKKGVFNGLDEEDDEDVEIQQASKSYKQQGGAVLEKKEGSKAMEAEPKSKRSVSFKSTVTSLGDSGDEEEDDLSSESDDEGETRTKQNGLKKKGPGSGPTGGVGSRSRPDEYDSDSDSSDSDYEEESMMRREMDGGEMNEKTNGVNEGKSKKRKMEDSEDKKEAAPAKKSAKIKQHLDPEGLALGTMMATSKKATRQIIEHAYHRYSYGDQDRIPDWLRSDETRHCRRNTPVTKELVAEYRARLREVNARPIKKVAEAKARKKKKQIVKLEKLRKKAEVISDLVDTSETEKMSQMKNLYKKMKIGQTKKKDVKYVVTRKHQSTKRVSRPSGVKGPFKVVDPRMKKDMRGQKRAEARKKRDKKKR
The following text describes a protein:
Function:
Co-chaperone for Hsp70 family members. Plays a role in protein transport into mitochondria and in the regulation of apoptosis via its role as co-chaperone (By similarity).
Subcellular Localization:
Membrane; Lipid-anchor. Cytoplasm. Microsome. Mitochondrion. Nucleus. Cytoplasm, perinuclear region. Note=Primarily cytoplasmic and associated with microsomes. A minor proportion is associated with nuclei and mitochondria (By similarity).
Sequence:
MVKEKEYYERLGVKPDCTEDELKKAYRKMAVKYHPDKNQGPGKDAAEAKFKDISEAYEVLSDPEKRKMYDSYGSEGMKESGFHASSAEDLFSHFFGAGGGGGGFSFGGGGGDDFGGFSFGNMGGMGGMGGMGGGHKKRRKGEDIEHEMNRSLEELYNGKLVKISISRDEVCKTCKGSGSNKPGVTTTCPTCNGSRYVFQKKQVGPGMIQQVQTACHTCHGTGEKIKEEDKCKECKGKRVIQGKKIVQFQVEKGTRDGERIMLQGQGSEYPGVPPGDVIITIREKPNVNFKRNGDNLIYTKRLKLLDSIAGSQFIINTLDQRKLWVNHEKGDIIKQGDMRYIENEGMPIKGTSRKGKLIIAFDIEYPSNLTNDDIEKLSKILPKAATPSVSKSDCKSVGLSKVNFNTNEQSSHGGAGGAYQQHGGAYGHQKQQQQGFNPADFGAQFGGGGPQQAQQCQQQ
The following text describes a protein:
Function:
Part of a heterotetrameric complex that catalyzes the two-step biosynthesis of anthranilate, an intermediate in the biosynthesis of L-tryptophan. In the first step, the glutamine-binding beta subunit (TrpG) of anthranilate synthase (AS) provides the glutamine amidotransferase activity which generates ammonia as a substrate that, along with chorismate, is used in the second step, catalyzed by the large alpha subunit of AS (TrpE) to produce anthranilate. In the absence of TrpG, TrpE can synthesize anthranilate directly from chorismate and high concentrations of ammonia (By similarity).
Sequence:
MNVVVVDNYDSFTYNLVEYLSAQPRDDHAPDVTVLKNTASLAAVRAADPDAVVISPGPGHPDTPRDVGVTTDVLRAVSPRVPTLGVCLGMEAAVHEYGGTVGRAAEPMHGKTTPVSHDETGIFADIQQDFPAARYHSLVCTSIPSCFAVTATTRDGSLPMAIRHRDHPLACVQFHPESVLTGVGHDVIGNFLDAAAAH
The following text describes a protein:
Function:
M cell-type specific protein involved in agglutination during conjugation.
Subcellular Localization:
Cell surface.
Sequence:
MSIALAFFILVLLGFSWASPSALDDTFNVSRSVGLISSSNLESCQSSPLEVGNIYNSTSASEILSTLDAKYITIIGVIGSSNSSIQDLIDSVGNSNNAASSNPTSTVTEYVDRVQTVTEYVTLSCGQAFTSTVDISSSTSSSVINSPTGTAVSSQISTLSMSPSSTPVFSPSASVSSKVASSVSYVSSEPSDSSSSTNTVILTTSVNSPAVSSSETLTSVSITSTESAYTSSSVDIAASTTASSTLPVSTSEATVSFSTDIPATPSTLSSPASSSSSYLVETSSTLTDSVFTTVTATSDSSVITYTLINSVTSSSETTNLPSSSSSLVTIGESSFPSSLLSLLTQSFSTVRSTSSSSTDQLTSASPISSSVISPSVSSPTSSILTNSGSIKSGDHQIVTTSFVQTTTHGSQVETLTYVTTLTETILTTTYDSHTFLTTITPSPSNSISYTNNTFIPSSSIKSSIVYSVTPTSAENYTSSEAFSTSSSLVVIPPVNSSLVTSSTSFTKFSSLSSSQLSTENFTSASSSLSLTNAKSSLSTPSTTIPTSNSSVSLQTSSSLIISSPIISSSLTATSTSTPALTHSITPSNTSYTSSLIPSSSTDYSSSLITVCSNVTSEISSTSLASLISTLTSQQISSNKSSEFVGQTTTEYTTSGSVGFTTTLATQSGSVPGTVLVDVPTPSWITETVTSGSVGFTTTIATPIGTTAGTVLVDIPTPSWVTETVTSGSIGFTTTIATPIGSTAGTVLVDVPTPSWVTETVTSGSVGFTTTIATPIGSTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVVVDVPTPSWVTETVTSGSVGFTTTIATPIGSTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPIGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPVGTTAGTVLVDIPTPSWVTETVTSGSVGFTTTIATPIGTTAGTVLVDIPQQHATTTTTTTFDGFSGYTSSYTGSITETIVIGTPHHSVVDVS
The following text describes a protein:
Function:
Transcription coregulator that can have both coactivator and corepressor functions. Involved in the coactivation of nuclear receptors for retinoid X (RXRs) and thyroid hormone (TRs) in a ligand-dependent fashion. Probable component of a centromeric complex involved in assembly of kinetochore proteins, mitotic progression and chromosome segregation (By similarity).
Subcellular Localization:
Nucleus. Chromosome, centromere. Chromosome, centromere, kinetochore. Note=Localizes to the inner kinetochore domain of centromeres.
Domain:
Contains one Leu-Xaa-Xaa-Leu-Leu (LXXLL) motif, a motif known to be important for the association with nuclear receptors.
Sequence:
MSAKRSLKLDSVKKYNPVEASPLAKKKDLNSYSPTTGTCQISPFSSPTSHNAEDLRNGLSHGDETNSESRLSRRGQPQTAEDAFAELQSNVKSSLVRILKARENLTSLQALEGSRELENIIGVSDSSHILSAEVQKTQALMSQAEELQLLKRNHGQLPAREYAQPASSSAFLQLLLNSL
The following text describes a protein:
Function:
Secreted metalloproteinase that allows assimilation of proteinaceous substrates. Shows high activities on basic nuclear substrates such as histone and protamine.
Subcellular Localization:
Secreted.
Sequence:
MVFVPFFYLLAGLTLASGKPILLPRLAQEASQDVAEHSFDVTLESLGNSTVKAEVTNTGTEGLRLIQRGGILDQFPTRKVNVKGGDSDPKFTGVRVEYILSHLTADGFVQLSPNQTVGSVFDVADLYELSPGQEYTAVAKGLLQYTTLANEKRFLTFSYKSNNISFTAPTDTTKRLEDRSTLVCSDEYNQVVQDAISRAAEMATAAAADARTGSALFQKYFKSTSEDDIEEVAGRLDAIAKEATTTGQLKYYCEPTAEDYCAGNVAAMTYPTLNRVVNCPGYYASTKVSNYCGYLDQAAITLHEYAHADALYSPGTEDIAYGYESVLSLDTEDSKNNADNFAYYASSVYLQCDANEEPGEIGSELDVDVGSSGSGSTQTPTATAEPTYPPGPTSTGTTGTGTGTGIGTDTGTGTGWTWPWGQGWGMNDDSGSGDSGSLTGTTSDTNTGSNTGYGTGYGTDFGTGPSGVYGGWDADKSSDSSAAAVTSAPTAAPVTTTDGQELWNLNDLVNWLVSMYAGDGQMQGQTQGQTQTKTASSNLDSGSGGYNAEAGQSATGTQATQAENDKDCDE
The following text describes a protein:
Function:
The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular Localization:
Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MKKLISVNMNTPTIKALIIIDLDGKRLYSKFYEKNPNVPLHKQHDIETRIAKAVSGKGNSELFLLDKYVVLYRMVSDLIIAALTDPQENELFVSNALNCIVEGFEIIFDKGLDKKIALEFYDKIAIAIDEVIDDGIILEVDSEEMANRVSFKNIKGNETGFGGDGTFTSALNFAKGSLLGLWRGK
The following text describes a protein:
Function:
Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MYVYTVGENISSEMERAYMFRPFTRETLLEIERRIVEEKQHDDALLSPPGSPAHGHSSAGSPSHHSVADRDARPARDAPDSELEAGRSLPTSLGRFPRKLYGRPVEDVDPYYLNKKTFIVVSKKGEIARFSATNGLWLLSPFCTIRGLALYILVHPWFSLLVMMAILVNCVFMTMTAPPEMTEYVFTGVYSFEMIVKILARGFILEQFTYLRDAWNWLDFIVILLAYVTMFVDLGNLSALRAFRVLRALKTISVVPGLKTIVKALIESVKNLRDVILLTVFCLAVFSLLALQLYMGTLLNKCVRHLPTDNGTASNVTDEIYMAHINNETNWYYYNGEWPLCGNASGAGQCPTGYTCLPGIGTNPNHGYTSFDTFGYAMLSSFRLITQDYWENLYQLIIRAAGPWNMLFFVFIIFLGSCYLINLMLAVVAMSYADANDNDDDDDSSSSSSSSSCSCSGSGSCHSGDCCCECVSVASDAERGSNHSLDKTGSKRGSRFSIHNVILRSRSYELLNDSIVQSPTMDSMVRSPDTERTSLPDILSNQSEMDMKVISNEQNVPNGMAPESCHNCKNWQDVRDFKGKTNTEIPWYYDTDDDEDVETKEKLADKLKTWCCNTFWNSWECCSCFKRFQEILSLFVMDPLIDLLITLCIVLNTMFMAMDHYGKSESFELTLKTGNYVFTAIFAAEFFLKLLALGPAVYFSSGWNCFDAIIVILSLAELGLEGVQGLSVLRSFRLLRVFKLAKSWPTLNLLISIIGSSIGALGNLTFILGIVVYIFAVIGMQLFGAEYEKRLDLFDGELPRWSFVDFLHSFLIIFRVLCGEWIENMWVCMLVNGWACIPLFILSMIIGNLVILNLFLALLLSCFSADSLADRPEGDGEPNNLQLAVEKLKRWAKMLLDLCRPSFWRKRRKGKEKFNEANPTDGETSREAVEETVNEQVLDSVYTVNLPEEVPKTLPTVTPSQFLLGSPTPAPLCRFGSNYDVTVVVPTRPMNGHAPIDGAALMKNVDSNQVPVFNHRLSEKGADDLGICNEFGAAQSSQGAENGKPINCKSPNHQDNSEQKSGRPEGESTGTGNVNDDDDEDADVIIDCCPPVCYPCCYKCCACANEERKAGEIWKNVRLKANFIVLHKYFETFIVGMILLSSLALAFEDIYLKDRPALQLGLNIADRLFAVIFCCEMLIKWIAFGYRKYFTNAWCWLDFVIVMISLLGIGAEALGLSNLSAFRSMRTLRALRPLRAISRAEGMRVVVNALVKAIPSIMNVLMVCLVFWLIFAIMGVQLFGGQFFKCVDENNKRLPTNITDNKEECLMKNYTWINSKINFDNVGQAYLVLFQVATFKGWIEIMADAVDVRGVGMQPDRETSLYFYLYFVVFIIFGSFFTLNLFIGVIIDNFNAQKKCMSGEGGESEDLFMTEDQKKYRKAMKKLGSKNAKKAIPRPTNCVQGWFYDTALNQKFDITIMVFICLNMVSMMIEHYRQSDKLKEALELINIIFIAVFTFEAVLKIIGQRWYYFKQPWNIFDFVVVVMSLLGLILADFIAKYFVSPTLLRVVRVARIGRVLRLIRGAKGIRTLLFALALSLPALLNIGLLLFLVMFIFAIFGMSNFAYVRKSNGLNDVINFETFGNSMITLFQVSTSAGWNGILDPLINDGPPNCDPEADTPSSNGDCGNSGVAIFFVVVYLMVSFLIVINMYIAIILDNFSQVRQEVEEGGVTEDDVEMFYAVWERYDPDATEYIQYERLSDFVNELEPPLQIKKPNKITLAYLNIPIMQGERIYSKHLLKALTKFVLGTVGKEDDDDEEDVPGPDEAHKMEEIPISSTLVKRREEVAARVFQRWYRKIMSERKQKEKHTDNRTPHELTEQTEIEQAKSSPGERKRKQTSILPIILKPTLLDPTNLIRSPKLTIRGKKDTNS
The following text describes a protein:
Function:
Utilization of purines as secondary nitrogen sources, when primary sources are limiting.
Sequence:
MSKQVSESDFNRQIVSNYTDVAGEKLGGKVLSFSDEWFAEAANLIKPYAPIREAGKFVDSGAWYDGWETRRHNTEPADWVVCRFGVAAAHIVGTEIDTAYFNGNHAPEISVECTSITSGLNEADEAAALKSASWDTVISKHECGPSQKQFFVLDKPTSKTYTHARLNMYPDGGIARFRLYGSVVPDFSQSKDVEIDLASVLNGGQAVARSDQHFGSADNLLLPGKGENMGSGWETKRSREPGHVDWVVIRLGAPGTINKIVLDTAWFKGNFPQKMTVSAVNLKPGESIAADDDRWVEVLAPVQGAPHVEKEYPVDNKHVFSHVKLTIIPDGGVSRIRVFGNRAE
The following text describes a protein:
Function:
Plays a role in inhibiting the onset of mitosis. Dephosphorylates sty1/spc1 and wis1/spc2/sty2.
Subcellular Localization:
Cytoplasm.
Sequence:
MNFSNGSKSSTFTIAPSGSCIALPPQRGVATSKYAVHASCLQEYLDKEAWKDDTLIIDLRPVSEFSKSRIKGSVNLSLPATLIKRPAFSVARIISNLHDVDDKRDFQNWQEFSSILVCVPAWIANYVTNAEVIGEKFRKESYSGDFGILDLDYSKVSGKYPSVIDNSPVKSKLGALPSARPRLSYSAAQTAPISLSSEGSDYFSRPPPTPNVAGLSLNNFFCPLPENKDNKSSPFGSATVQTPCLHSVPDAFTNPDVATLYQKFLRLQSLEHQRLVSCSDRNSQWSTVDSLSNTSYKKNRYTDIVPYNCTRVHLKRTSPSELDYINASFIKTETSNYIACQGSISRSISDFWHMVWDNVENIGTIVMLGSLFEAGREMCTAYWPSNGIGDKQVYGDYCVKQISEENVDNSRFILRKFEIQNANFPSVKKVHHYQYPNWSDCNSPENVKSMVEFLKYVNNSHGSGNTIVHCSAGVGRTGTFIVLDTILRFPESKLSGFNPSVADSSDVVFQLVDHIRKQRMKMVQTFTQFKYVYDLIDSLQKSQVHFPVLT
The following text describes a protein:
Function:
Down-regulates ESR1 protein levels through the ubiquitination-proteasome pathway, regardless of the presence of 17 beta-estradiol. Also involved in 17 beta-estradiol-induced ESR1 degradation. Controls PGR protein levels through a similar mechanism.
Subcellular Localization:
Cytoplasm. Nucleus.
Domain:
The CUE domain mediates interaction with PGR and ESR1.
Sequence:
MELERIVSAALLAFVQTHLPEADLSGLDEVIFSYVLGVLEDLGPSGPSEENFDMEAFTEMMEAYVPGFAHIPRGTIGDMMQKLSGQLSDARNKENLQPQSSGVQGQVPISPEPLQRPEMLKEETRSSAAAAADTQDEATGAEEELLPGVDVLLEVFPTCSVEQAQWVLAKARGDLEEAVQMLVEGKEEGPAAWEGPNQDLPRRLRGPQKDELKSFILQKYMMVDSAEDQKIHRPMAPKEAPKKLIRYIDNQVVSTKGERFKDVRNPEAEEMKATYINLKPARKYRFH
The following text describes a protein:
Function:
Component of ribonuclease P, a protein complex that generates mature tRNA molecules by cleaving their 5'-ends. Also a component of RNase MRP (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MVRLKNRYLMTEVIWHDNEKSTQLSDSWLFQFISNEVKEKLGELTYEAFKKTLKIIYVNPDTNIFIIRVSFEYYKSLWTALTLITSYYGVPIYFRMVHVGGSIRLCQKAAIKIFGKQISVYDKNKILRNEKGETIDNNNNKNEEPSIKMDSDDDENGGGDDGEDNDSEMKD
The following text describes a protein:
Function:
Plays a role in the inhibition of host apoptosis to facilitate efficient viral replication. Promotes stabilization and inactivation of host TP53 through interaction with host MDM2 (By similarity). Induces host mTORC1 activation by antagonizing the ability of host TSC1/2 to negatively regulate mTORC1. Thus, inhibits a growth regulatory pathway to facilitate viral replication. Prevents premature cell host cell death by blocking host ubiquitin-specific protease 24/USP24-mediated autophagic ferritin degradation in lysosomes thus maintaining lysosome integrity and cellular viability (Probable). Involved in the activation of host ENO2 leading to enhanced glycolysis and UDP-sugar metabolism in order to enable the expression of viral glycoproteins (By similarity).
Subcellular Localization:
Host cytoplasm. Host nucleus. Note=localized in the host nucleus at early times postinfection and then increases in both nuclear and cytoplasmic compartments during the course of infection.
Sequence:
MTTTTHSTAAIMSLLDEAEWRQTQMDVGGLIQASALGKVALRYAVRKLMKRGARLRHDSGLYVCICDPSYEFLQMNLSKISWLERHCPPLDQELIMFGVIEAWEEASVRPTRQLVLFMTPKWDVFAYDSGILFFLAPSMAQFWHGAIVLEYWNALFPVEVRSHVRQHAHTMDDLVMVFHQLDYEKQVLEARRDKNTEGPRTFAKSVNSYVRAILESERRIREGKIPMTFVDRDSLRANSLAHIQATGAQPSHAPAQRVLSAPPSLPSPVSEEDPAAAATPPSSAATTPPSSVVPASVESELSSSPPLPPVVVKDVMYTAGEGDVVQMVVVV