lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Part of the ATP-binding cassette (ABC) transport system ZnuABC involved in zinc import. Binds zinc with high affinity and specificity and delivers it to the membrane permease for translocation into the cytoplasm.
Subcellular Localization:
Periplasm.
Sequence:
MIECYNITFHTFITMISRIMLQKNTLLFAALSAALWGSATQAADAAVVASLKPLGFIASAIADGVTDTQVLLPDGASEHDYSLRPSDVKRLQGADLVVWVGPEMEAFMEKSVRNIPDNKQVTIAQLADVKPLLMKGADDDEDEHAHTGADEEKGDVHHHHGEYNMHLWLSPEIARATAVAIHEKLVELMPQSRAKLDANLKDFEAQLAATDKQVGNELAPLKGKGYFVFHDAYGYYEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVVEAVARGTSVRMGTLDPLGTNIKLGKTSYSAFLSQLANQYASCLKGD
The following text describes a protein:
Function:
Attaches a formyl group to the free amino group of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and preventing the misappropriation of this tRNA by the elongation apparatus.
Sequence:
MRLVFAGTPEPALASLRRLIESPSHDVIAVLTRPDAASGRRGKPQPSPVAREAAERGIPVLRPSRPNSAEFVAELSDLAPECCAVVAYGALLGGPLLAVPPHGWVNLHFSLLPAWRGAAPVQAAIAAGDTITGATTFQIEPSLDSGPIYGVVTEVIQPTDTAGDLLKRLAVSGAALLSTTLDGIADQRLTPRPQPADGVSVAPKITVANARVRWDLPAAVVERRIRAVTPNPGAWTLIGDLRVKLGPVHLDAAHRPSKPLPPGGIHVERTSVWIGTGSEPVRLGQIQPPGKKLMNAADWARGARLDLAARAT
The following text describes a protein:
Function:
Has a dual specificity toward Ser/Thr and Tyr-containing proteins.
Sequence:
MHSLNQEIKAFSRDNLRKQCTRVTTLTGKKLIETWKDATVHVVETETSGGGGCGYVQDLTLDLQVGVIKPWLLLGSQDAAHDLELLRQHKVTHILNVAYGVENVFLSEFTYKTISILDVPETNILSYFPECFEFIEQAKLKDGVVLVHCNAGVSRAAAVVIGFLMSSEELAFTNALSLVKEARPSICLNPGFMEQLRTYRVGKESNGGDQVPAVATDHGP
The following text describes a protein:
Function:
Zinc-dependent transcriptional regulator of cellular adaption to conditions of exposure to heavy metals. Binds to metal responsive elements (MRE) in promoters and activates the transcription of metallothionein genes like metallothionein-2/MT2A. Also regulates the expression of metalloproteases in response to intracellular zinc and functions as a catabolic regulator of cartilages.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MGEHSPDNNIIYFEAEEDELTPDDKMLRFVDKNGLVPSSSGTVYDRTTVLIEQDPGTLEDEDDDGQCGEHLPFLVGGEEGFHLIDHEAMSQGYVQHIISPDQIHLTINPGSTPMPRNIEGATLTLQSECPETKRKEVKRYQCTFEGCPRTYSTAGNLRTHQKTHRGEYTFVCNQEGCGKAFLTSYSLRIHVRVHTKEKPFECDVQGCEKAFNTLYRLKAHQRLHTGKTFNCESEGCSKYFTTLSDLRKHIRTHTGEKPFRCDHDGCGKAFAASHHLKTHVRTHTGERPFFCPSNGCEKTFSTQYSLKSHMKGHDNKGHSYNALPQHNGSEDTNHSLCLSDLSLLSTDSELRENSSTTQGQDLSTISPAIIFESMFQNSDDTAIQEDPQQTASLIESFNGDAESVSDVPPSTGNSASLSLPLVLQPGLSEPPQPLLPASAPSAPPPAPSLGPGSQQAAFGNPPALLQPPEVPVPHSTQFAANHQEFLPHPQAPQPIVPGLSVVAGASASAAAVASAVAAPAPPQSTTEPLPAMVQTLPLGANSVLTNNPTITITPTPNTAILQSSLVMGEQNLQWILNGATSSPQNQEQIQQASKVEKVFFTTAVPVASSPGSSVQQIGLSVPVIIIKQEEACQCQCACRDSAKERASSRRKGCSSPPPPEPSPQAPDGPSLQLPAQTFSSAPVPGSSSSTMPSSCEQSRQAETPSDPQTETLSAMDVSEFLSLQSLDTPSNLIPIEALLQGEEEMGLTSSFSK
The following text describes a protein:
Function:
Acts as a Baeyer-Villiger monooxygenase on a broad range of substrates. Catalyzes the insertion of an oxygen atom into a carbon-carbon bond adjacent to a carbonyl, which converts ketones to esters. Active on diverse carbonyl compounds, whereas soft nucleophiles are mostly non- or poorly reactive. In contrast with other forms of FMO it is non- or poorly active on 'classical' substrates such as drugs, pesticides, and dietary components containing soft nucleophilic heteroatoms. Able to oxidize drug molecules bearing a carbonyl group on an aliphatic chain, such as nabumetone and pentoxifylline. Also, in the absence of substrates, shows slow but yet significant NADPH oxidase activity. Acts as a positive modulator of cholesterol biosynthesis as well as glucose homeostasis, promoting metabolic aging via pleiotropic effects.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane.
Sequence:
MRRTCVIGAGPSGLAASRVLASRGIPFDCYEAGSGIGGLWRYGNDNGMSGVYASLHANISKESMSFSSLPMPDSYPVFPHHTQVLAYLESYAETFGLHGHIGLRTEVTSVRPVEGGGWEVTRRSRGGAEAETDRYTEVVVANGHHWDPRLPDPAVPGAGVFEGSAVHAHAYRSPEPYAGQRVLVVGMGNSGCEIAAEISRSAARTFLSARAVAHVFPKMLLGRPADHWAVSRAAVLPRFLKDPGMALLLRLARGAPALYGLPEPVRRPLAAHPSTSDELLVQLARGAVTAKPGIRSFGRDSVSFTDGSRETVDAVVYATGYSLSFPFLAPAVFAAPDGRTELYLRTVPPRLPGLFFMGLAQPAGAAFPLLEPQAEWIADLIEGEVLLPTPAEMTRSIARARERHDKVYAPSYRHGIEIDICAYRRALRRELRAGRRRARRADARRPDAPRPAPVSDTV
The following text describes a protein:
Function:
Part of the RFX complex that binds to the X-box of MHC II promoters.
Subcellular Localization:
Nucleus.
Sequence:
MEAQAVPEGSGPSTASPRTAPPVTVLVMRQDEAEADGALRPGLAGSEAAADAEDEAGDDDADLLDTSDPAGGGESAASPEELEDEDAEGGGAARRRGSKTCTYEGCRETTSQVAKQRKPWMCKKHRNKMYKDKYKKKKSDQALGSGGPSAASTGNVKLEESTDNILSIVKQRTGSFGDRPARPTLLEQVLNQKRLSLLRSPEVVQFLQKQQQLLNQQVLEQRQQHFPGAPV
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. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity.
Sequence:
MSEHFLLLGLPFLPTGADSFAFQYKNLVSLLGAAGKDVCSFAVPNFKVGTLDSLIEASDELAKLDLQVENSLEKQITIMQEICEEPRDVVATLRFNQTQEMTPAAFVKGFQWSSAQFDSNESILGLVEKFANYFATTEEGVRLVMTKYNETRNKLTTVTRKAQGNLSVKPIRELVTMKNRSHPFIVDTELLTNLFVAVPLSSKREWLNEYWSLNDFVCPDSNCIIAEDSEFVLNSIVVFRRVLEDVKLACRKRRYIVRDSDAADEPSIRDLNDFIKRAESEKKNFGLVLRQRYTGCYVAWVHLKAVRLFVESLLKYGLPPRCISIFLQVDKRKEAEIRKKISQLYPDLSVPFSNTSSVEDGSLQYEYPYVSIKMTNLQRC
The following text describes a protein:
Function:
Catalyzes the three sequential steps of the methylation pathway for the biosynthesis of phosphatidylcholine, a critical and essential component for membrane structure. Uses S-adenosylmethionine (S-adenosyl-L-methionine, SAM or AdoMet) as the methyl group donor for the methylation of phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine, PE) to phosphatidylmonomethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine, PMME), PMME to phosphatidyldimethylethanolamine (1,2-diacyl-sn-glycero-3-phospho-N,N-dimethylethanolamine, PDME), and PDME to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine, PC), producing S-adenosyl-L-homocysteine in each step.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MVLQKGVKGQQLCRKTHTRIRSALLQQPLYFHQIVFHGDHPFSLQPTLDVDFKDCCGAGLRLDWTQADMSFITDYLRLNDPNFLITVVLIMFSPTYWNLVARSEYRSHWVTHLFRSARVGCSVLAVSIMLLGLHRDWWFKQTLYSQPKVSAIQSPVLGYAVIAIGALLVLSSFWALGWYGTFLGDYFGMLMDEPVTSFPFNLVSDPMYVGTTMNFAGVALLEGSLAGLVLAALVGLCYKVALLFEGPFTEEIYRKRDADKRKV
The following text describes a protein:
Function:
Transfers dimethylallyl groups to AMP as part of the biosynthesis of cytokinin phytohormones like isopentenyl adenine or discadenine which controle spore formation and viability.
Sequence:
MKILLIIGSTGVGKTDLSINYSKKYNAPVVVLDRIQCFPELSITSGRPDESEYFGSKRIYLTDLLVEPGNENIKKTFYVNKLINILNEIKNNYDTQNLPNEKGYGCIFEGGSISLLKELLTKINKLPYKITCVIYIRPSDSIDNHKLYKAKIFKRVSQMLFPTEEGNDSQILEVKRILNKGKTVNAQGEINLEYYEKIKQVLISLVGLVGIEDVIHFLDKQYDQKNITSKLDPNYLNEIQSQLIETITLAHYNYALSQIELIDSLIKQLPKSIEYCLKNIEIN
The following text describes a protein:
Function:
Catalyzes the conversion of 7,8-dihydroneopterin into 6-hydroxymethyl-7,8-dihydropterin, a biosynthetic precursor of the vitamin tetrahydrofolate. Can use L-threo-dihydroneopterin and D-erythro-dihydroneopterin as substrates for the formation of 6-hydroxymethyldihydropterin, but it can also catalyze the epimerization of carbon 2' of dihydroneopterin and dihydromonapterin; Catalyzes the conversion of 7,8-dihydroneopterin to 6-hydroxymethyl-7,8-dihydropterin.
Sequence:
MAGDGDEEPPATGGDKLILRGLQFHGFHGVKQEEKKLGQKFVVDVDAWMDLAAAGDSDDIAHTVSYTDIYRIAKGVVEGPSRNLLESVAQSIAGSTLLEFPQISAVRVKVGKPHVAVQGIVDYLGVEILRRRGA
The following text describes a protein:
Function:
May be involved in protection from oxidative damage.
Subcellular Localization:
Mitochondrion.
Sequence:
MFSTKRLKKKSQSVDIPDEGYAGSLVKDLLASPLIKNVARTTIREEKEINTTNIQKARSPRRGELKRGYTIDTGQKKSALERKDVRRISFQRPKGTMEYVVESRDTLNSIALKFDTTPNELVQLNKLFSRAVVPGKVLYVPDPEYISSAESSPSLSPISPLSPTSSEADLEKATKGLDHVHRRHSSSTGLAHGPPRPARVVSSTSEEEEALTEKFLKMNCKYITDGKGIVSGVLLVTPNNIMFDPHKSDRLVQERGCEEYGIMCPLEEVQSAAMCREITDVRLREFVPPDLELEPSVSEVSHLKRAPRLNAADAAHRIRETGNDSASTAPRSTEASLSEDVFTESELSPVRDDALATSSDELQQIKSSGASSESVQTINQAATVTEDQSSAGGTDVKEAGQIEGVGWRDSGIEQSLNTTDVFNEESCENVLENVQRDQSGDEPKSRTTSESLCSDTVAVEDAVKETQKSLEDQSLQASSDVKEGELRTDSDSTAAVEPGAEEGLKSAEEVVPGLRGKQKSKLHKFLCLRVGRAMRKTFVSHASASMQQYAQRDRKHEYWFAVPSERSDHLFGFFVQWTPDVYGEGFGGLTREPGFVVVKKNQDAESGEQDKPVPDITFKDWEVVSVAEYYRRIDALNSEDLRSLCKRLQITTKEEVNSKLMVKSDPEPETFRPNLTEPSVLLQPEHIEKLAKHLPPRTIGYPWSLAFSTSKHGMSMKSLYRAMQSQDSPVLMVIKDSDGQMFGALASQPFKVSDGFYGTGETFVFTFYPEFEVFKWTGDNMFFIKGDMDSLAVGGGGGEFGLWLDGDLYHGRTHSCKTFGNPMLSKTEDFFVQDIEIWAFE
The following text describes a protein:
Function:
Bitter taste receptor. Binds quinine, dextromethorphan, diphenhydramine, diphenidol, chlorpheniramine, diphenidol, chloramphenicol, chloroquine and coumarin, this latter being a weak agonist, as well as epiquinidine, ethylhydrocupreine and quinidine.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSSLFSSFCLVIAIFESVVGLLGNGTIVAVSSTSCIRSKILSSYDVIVIFLSLSRFFLQLWMILDFLLIFFCQPSYYEENLFVTFKTVFIFLNSYSFWFAAWLSVFYCVKVASFTQSFLSWLKQRIASLIPWMLITSSLFSFATSLPFFWDSYNAHSNFTTPLTMTNSSKRITTRKTNLIFLILLCNVGIALPSIMLVFSSILLIRSLWRHTRQMQNNATGFRDPSLEALIGAIKTVFSFLLLYITNFIALILILSDTFVPLSTEEAICVVVVAACPAGQSMVLIWSNPRFRELLSSILHYVNSCVRARCS
The following text describes a protein:
Function:
Catalyzes the final step of de novo phosphatidylcholine (PC) synthesis, i.e. the transfer of choline phosphate from CDP-choline to the free hydroxyl of a diacylglycerol (DAG), producing a PC. It thereby plays a central role in the formation and maintenance of vesicular membranes.
Subcellular Localization:
Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MAAGAGARPAPRWVKALGEPLSAAQLRRLEDHRYSAAGESLFEPPLQLFWTWLLQWIPLWIAPNTITLFGLAINLFTTLVLIFYCPTVTEEAPYWTYLLCALGLFIYQSLDAIDGKQARRTNSCSPLGELFDHGCDSLSTVFMAIGASIAVRLGTHPDWLFFCSFVGMFMFYCAHWQTYVSGVLRFGRVDVTEIQVALVIVFLLSTFGGAMMWDYTIPILEIKLKILPVLGVVGGLIFSCSNYFHVILHGGVGKNGSTIAGTSVLSPGLHIGLIIILAIMIYKKSATNVFEKHPCLYTLMFGCVFAKVAQKLVIAHMTKSELYLQDTVFIGPGLLFLDQYFNNFIDEYVVLWIAMVITSFDMMIYFSSLCLQISRHLHLSIFKTSYQQAPEQVHKHID
The following text describes a protein:
Function:
Catalyzes the conversion of prostaglandin H2 (PGH2) to thromboxane A2 (TXA2), a potent inducer of blood vessel constriction and platelet aggregation. Also cleaves PGH2 to 12-hydroxy-heptadecatrienoicacid (12-HHT) and malondialdehyde, which is known to act as a mediator of DNA damage. 12-HHT and malondialdehyde are formed stoichiometrically in the same amounts as TXA2. Additionally, displays dehydratase activity, toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE) producing 15-KETE and 15-HETE.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Sequence:
MFTTLILIFCCIILYFVYDKWCRTYFQRLGIPGPPSIPVLGNFTEWFVVFHDRFAEYFQKYGKIVGVYNFRKPTLLVSDPDVVRKILVKDFDHFVNRQEAAIKTDLLAGGMLAAKDERWRKLRSLLSPSFTSVKLKSMVPLMRECAEVLVDIFTKREEEGKTIECKELYGPYAMDVIGSCAFGLRVNSQTNQDEPFIKYAKRIFNFNVTNPAFLISMLFPWTAPIFNFFKLGSVPKDIEQFFLGVFEKAIADRQANGDTGKSDFLELMMSAHKEDDDVNIMNDAEDDIADLAQETSWKPKQKTALNRQEIIGNSITFLLAGYETSSTALGFVSYLLATNQHVQDLLVAEVKEMAPSQSDVTFETVTKMEYLNMVIMEAMRIYPPGEVLERVCNKEITYNNITIKKGQYIFIPIWNLQHDSDLWPDPETFDPERFSKDRRGNNHPCGWLPFGIGPHTCIGVRFAMLEIKVAMVCILQKFRFDTCPETEIPPKLGNLSFLTPPNGITLRITPHSRYNLRSR
The following text describes a protein:
Function:
Multifunctional effector that can suppress host BAK1/SERK3-mediated immunity through at least two different pathways. Manipulates plant immunity by targeting and stabilizing host E3 ligase CMPG1. Preventing the normal 26S proteasome-dependent degradation of potato CMPG1, and thus potentially of its protein substrates in the host cell, further abolishes host cell death during the biotrophic phase of infection. Also associates with and affects the function of the dynamin-related protein 2 (DRP2), a plant GTPase involved in immune receptor-mediated endocytosis. The Avr3a(EM) form evades recognition by R3a, thus does not trigger R3a-mediated hypersensitivity and does not suppress INF1-induced cell death.
Miscellaneous:
MISCELLANEOUS: The AVR3a protein of Phytophthora infestans is a polymorphic member of the RXLR class of cytoplasmic effectors with dual functions. AVR3a(KI) but not AVR3a(EM) activates innate immunity triggered by the potato resistance protein R3a and is a strong suppressor of the cell-death response induced by INF1 elicitin, a secreted P.infestans protein that has features of pathogen-associated molecular patterns. The 2 polymorphic residues between Avr3A(KI) and Avr3a(EM) are localized at positions 80 and 103, respectively.
Subcellular Localization:
Secreted. Host cytoplasm.
Domain:
The RxLR-dEER motif is required for the delivery of the effector to the host cell cytoplasm but does not bind phosphatidylinositol monophosphates. The motif is cleaved after the RxLR sequence. The RxLR motif (residues 44 to 47) plays a crucial role in the intracellular processing before secretion. The Glu-rich part localized just after the cleavage site (residues 48 to 59) is required for homodimerization; The conserved, positively charged effector domain (residues 77 to 147), rather than the RXLR domain, is required for binding to phosphatidylinositol monophosphates (PIPs). PIP binding is necessary for accumulation of CMPG1 and Avr3a in host plants.
Sequence:
MRLAIMLSATAVAINFATSSAIDQTKVLVYGTPAHYIHDSAGRRLLRKNEENEETSEERAPNFNLANLNEEMFNVAALTERADAKKLAKQLMGNDKLADAAYMWWQHNRVTLDQIDTFLKLASRKTQGAKYNQIYNSYMMHLGLTGY
The following text describes a protein:
Function:
Synthesizes selenophosphate from selenide and ATP.
Sequence:
MSNNINIKEGEACSIEKKEVRLTELSRTSGAAKIAPGVLSKILSKLPKMESENLIVGIETADDAAVYKINDDTAMIQTLDFFTPIVDDPYMFGQIAAANSLSDVYAMGGKPVVALNIVCFPSCLPIEVLGEILKGGADKVMESGAVVIGGHTVDDNEPKYGLSVTGIVHPDKVLKNYGCKEGEVLITTKPLGIGIINTAIKGDMASKEAKDAAVKSMSTLNKYAGEIITKYNISACTDITGFGFLGHAYEMASASNVTLKFNYKRISYIKEAEEYAEFGLVPAGAYANRDHIEGNFEFKNVPVFMQDILFDPQTSGGLLISCSKEESEKIMKELNKLELKSSIVGEVIRKQDKYIIVE
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:
MFEVGKTLPSKIGEFPPSLYGKPIEDLDDYYRNKYTFMIVAKDKTIFRFSATKGFFIFTPFNPIRRAAMYVLTHPYPFLTVMVVILVNCVFMAIKEEFQAAEKTFTGIYTVEGSVKMLARGFILADFTYLRDAWNWLDFIVVMLAYVTMGIEMGNVAVLRTFRVLRALKTVAVVPGLKTIVGALMEAVRRLRDVMILSVFVLSIFALVGLQLYQGHISRSIKNLTAINVTTALYTLYLFFFRTGSNRRAVPSCCVACTETNQGDCPVNYTCAKGGDNPDFNYTNFDNFGWAMLCAFRLMTQDYWENLYQQVIRTNGPNQVLFFVIVIFLGSFYLVNVILAIVAMSYDDCRKQDQIDADLEEEAEMKAEEAFFEVKYTPSVGSANSLMLANPRYSNGGNGRPVACDKMSVQSEYCCSHNCNQEIYKQKEKSVSRLVLKFEDPTKNKLAIMDNPFICRTPSTATIDLQDVLVLKDLIRNASNKRRCYWLGYEPGMKKKEFLKEKCMQLLFGWECHPLWYKVAHITELFIMDAFVDLFITLCIVVNTVFMAMEHANMHDTLVKVLSYGNYVFTGIFTVEAALKILALGLYKYLQDKWSCFDFVIVILSLVEMGLEKVKGLSILRSFRLLRVFKLAKSWPTLNLLIGIIGRTMGALGNLCFVLAIIIFIFAVMGMQLFGAYYTDDKFPFEVGENRELRWHFKDFFHSFMIVFRILCGEWIENMWNCLRTYGKPCIPFFLLTMIVGNLVVLNLFLALLLSSFGAESLKHSQEEEGPNKLQEAVDRINRFAIYIKSHITYCVKVKVRHKQIANDYFFDERTNYIGQHDANRHGNNNMCVNNNDSSSNTNNNINDNNSNRGVVIVNATPIGNGRIVNAEGDYELNNDDDDLSRAYNKSNHSKRSSVNNNNNNNNNDVPRTTGGPEINEVKVVFVKYPDDCCPRLCMEKCSFWDLLENTLFGKVYWKFRCYMFSLVENNYFETFIILMILASSLALAIEDKNIDTKPLLKHVLKVMDSVFTVIFVFEMIVKMAAYGLKKYFTDAWCWLDFIIVAISLVGWFAEGAGAGNMGAFRALRTLRALRPLRAVSRWEGMKVVVNALIQAIPAIFNVLLVCLVFWLIFSIMGVNLFMGRFGRCLDEEGEMIKIVFESGHYVIQGTNDTLTRELCKKNFSVTRNYTWFNPKVNFDNVLIGYLSLFQIATFKGWMDIMYAAIDSREPTEQPLFEDRVGVYLYFVLFIVFGAFFTLNLFIGVIIENFNMQKKKAGGSMEMLMTEDQKKYYNAMKKLGSKQPTKPIPKPKLTCQLFFFNLTKNQKFDVAIMVVILLNMTTMGLEHYDQPKAMEITLNYINTVFIVIFTLECVMKLLGLRFYYFKEPWNIFDFVVVITSILAMALSSVLNKLPVSPTMLRVVRVFRVGRVLRLVKSAKGIRTLLFSLAVSMPALFNIGLLLFLVMFIYAIVGMSSFMHVKHSAGIDDMFNFETFFNSMIILFQICTSAGWDGVLAGLMNDTPPDCDDKPTESSPNGDCGNSALGMMFLVTYLVITFLVIINMYIAVILENFSQATEDVQQGLTQDDFDMYYELWERFDENATQYIPLDRLCEFVDTLEDPLRLPAPNLYKLVSMDIPICENDMVHCIDILDALTKNFLGTANEDTGELGDLKGPEKKDYHPISTTLKRQREMCVARIIQKSWRNYVNKKRLEHAKEDLYQLDKVSLESYNSRFTSGSKLSILEANSSNGVNVIKTELTTDMDENVRNIFSDTSSGSGSVSSYNGRKTKQEKSDEDNKKLLISFSTVSDSDS
The following text describes a protein:
Function:
Interacts strongly with CDK6, weakly with CDK4. Inhibits cell growth and proliferation with a correlated dependence on endogenous retinoblastoma protein RB.
Sequence:
MAEPWGNELASAAARGDLEQLTSLLQNNVNVNAQNGFGRTALQVMKLGNPEIARRLLLRGANPDLKDRTGFAVIHDAARAGFLDTLQTLLEFQADVNIEDNEGNLPLHLAAKEGHLRVVEFLVKHTASNVGHRNHKGDTACDLARLYGRNEVVSLMQANGAGGATNLQ
The following text describes a protein:
Function:
Essential for the establishment and maintenance of sister chromatid cohesion at centromere proximal and distal regions during S phase. Also required for chromosomal condensation.
Miscellaneous:
MISCELLANEOUS: Present with 7720 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MAKGAVTKLKFNSPIISTSDQLISTNELLDRLKALHEELASLDQDNTDLTGLDKYRDALVSRKLLKHKDVGIRAFTACCLSDILRLYAPDAPYTDAQLTDIFKLVLSQFEQLGDQENGYHIQQTYLITKLLEYRSIVLLADLPSSNNLLIELFHIFYDPNKSFPARLFNVIGGILGEVISEFDSVPLEVLRLIFNKFLTYNPNEIPEGLNVTSDCGYEVSLILCDTYSNRMSRHLTKYYSEIIHEATNDDNNSRLLTVVVKLHKLVLRLWETVPELINAVIGFIYHELSSENELFRKEATKLIGQILTSYSDLNFVSTHSDTFKAWISKIADISPDVRVEWTESIPQIIATREDISKELNQALAKTFIDSDPRVRRTSVMIFNKVPVTEIWKNITNKAIYTSLLHLAREKHKEVRELCINTMAKFYSNSLNEIERTYQNKEIWEIIDTIPSTLYNLYYINDLNINEQVDSVIFEYLLPFEPDNDKRVHRLLTVLSHFDKKAFTSFFAFNARQIKISFAISKYIDFSKFLNNQESMSSSQGPIVMNKYNQTLQWLASGLSDSTKAIDALETIKQFNDERIFYLLNACVTNDIPFLTFKNCYNELVSKLQTPGLFKKYNISTGASIMPRDIAKVIQILLFRASPIIYNVSNISVLLNLSNNSDAKQLDLKRRILDDISKVNPTLFKDQIRTLKTIIKDLDDPDAEKNDNLSLEEALKTLYKASKTLKDQVDFDDTFFFTKLYDFAVESKPEITKYATKLIALSPKAEETLKKIKIRILPLDLQKDKYFTSHIIVLMEIFKKFPHVLNDDSTDIISYLIKEVLLSNQVVGDSKKEIDWVEDSLLSDTKYSAIGNKVFTLKLFTNKLRSIAPDVPRDELAESFTEKTMKLFFYLIASGGELISEFNKEFYPTPSNYQTKLRCVAGIQVLKLARISNLNNFIKPSDIIKLINLVEDESLPVRKTFLEQLKDYVANELISIKFLPLVFFTAYEPDVELKTTTKIWINFTFGLKSFKKGTIFERALPRLIHAIAHHPDIVGGLDSEGDAYLNALTTAIDYLLFYFDSIAAQENFSLLYYLSERVKNYQDKLVEDEIDEEEGPQKEEAPKKHRPYGQKMYIIGELSQMILLNLKEKKNWQHSAYPGKLNLPSDLFKPFATVQEAQLSFKTYIPESLTEKIQNNIKAKIGRILHTSQTQRQRLQKRLLAHENNESQKKKKKVHHARSQADDEEGDGDRESDSDDDSYSPSNKNETKKGHENIVMKKLRVRKEVDYKDDEDDDIEMT
The following text describes a protein:
Function:
Chromosomal protein which is recruited to mitotic chromosomes by hcp-3 (CENP-A) and hcp-4 (CENP-C). Involved in chromosome segregation during mitosis, playing a role in chromosome condensation and in maintaining chromosome morphology, rigidity and orientation during mitosis.
Subcellular Localization:
Nucleus. Chromosome, centromere. Note=Localizes to the centromere during mitosis. Co-localizes with hcp-3 (CENP-A) at prophase, metaphase, and anaphase chromosomes. Mitotic chromosome localization is dependent on hcp-3 (CENP-A) and hcp-4 (CENP-C). Localizes along two parallel lines on individual prophase chromosomes. At metaphase, localizes at the poleward faces of the metaphase plate. During anaphase, localizes with the separating groups of sister chromatids.
Sequence:
MSNINEKDLSEFLESNLRSLNDIDDAVATSSAECNYEDYEEFTNSVDLTFFEQDLSGVLKELKKLAESVVISGKKCDIRNIFEESDVATMKFNLFVWYFLENGQRSDSSEEDVDKGVSAASSYIAMCSLPGAISDLYQIGLYNQCLKIIRNCCHTVRIGETVVTKKSSGAKKKKAGGKSDETNVDGEMTVTTGAADPIIGPPRIAVDSAERYLHHLTTQLFAFLHSNTFSIDTPTLMSTLEVVEDIGRLDLDNRTAGRAIRANSVHEFRSLERFTDRYCAFVHSLVESKYKTRAEVAYGRLIRPRLALMPYPDESNKSSKISTERKRSGELHVNLILSRISRNPEARELKYIQTVTVMVYSQCPDLAEFRTNIATFIHKILEALPYTYTYDFVQFMNVLFKGRGAGVKSLSTELSSILISSFDFTAPDPGAIPNLDAEQNEEEDEEEEGEDEEEEEENEQDDVAVKEEEQSDKSDEENDGDNEENVSKKKEEKKKEKKAKEVKEVGRMDAMSVLYNIVYMACLDKAAAMRLHGANSLTKILQSQSHREAFQLFCATINAEMDEKFGAVGDNLSESLEDLNVSGKAPSSKTKKPTDLLLDEQQIIQKFNKLKLMNKGETRVEKDIVYMIVRRLSTDDKAPVKKAACSLLKSYLSYCDEASKFEVVLSILQMLCRDRMVSVRKTGADAFTELMLRDAILFKESLSSKWLHTLISMLNDTDNDVTEHARKLIMKVLTPLLENSSDLTWTLLDTIESVTNHRQYLMSTLKDAVREKLVKRTVMDSMKQHIISGSEKLDGAWMVFSQLCVQFEQNVDFAIETFSRVDLSRESNLVQYMIHVIENNIKKIDDDTKSDLVNTLQGTFRDYCLHPSHSRSIYHCLGKLMDGIGDRSLHGKEFSDFGETLLIKCFDTIVQSFEMFKDKDEWKRNSESQERLLCTALNVASEVFSYSPQLVPRHERLGKTLSLIVNSTENGSSDASTVNPDMPSVHHTRPPTQLSEVPSSQKSSKGGMMSHEGAMFSDKVRAVGVVTLANMILAHDRLLKLMPMLVKQLQYNTAHQIRSNIVLAIGDICSSYKTDRYAPMLAASLCDPSVIVRRHAINQIARLISFGIFRFNGEIMIRMMLASLDANEDVRNDAKLYISEVLQSEEPNFFPLNFVQYMIALTQARRLVGVGHDEDDRGQVDVAIGGGDPLARPSRIAIYTFMIDSLDDRSRFDVKMSICQRIFTPIVNGEYDFSDYNVQCLLDDALLIMASNEMQVKMDVGKNPNENAMDDPSPEVLEAATGFMQKVYLDHYMKTIVPSILSLREFLNQHRSPLQRKCLLAIRMICIEHKNDIDEILQDNRQLKDEMMFELQRVKQRTEEANRILDEYLKRVAEFKKQQKRLSKSPAPMELDAEPVQESAEAVEMGSPARRIEEDQENVEEEVEMRTPQKKNPDADVPRTPLNALRSTTEEKSTPNARLLSPKTIKKIRRSLGALIHTEMRLNPPNLEETKIDDTTINRSKQADKTEEKTIVEEEPMEEAAAEKTVTAENDHVDAEKTVIAVEIPPATEAEEDEVVDVQSESRRSRRRKTPNYDDEESVDADGKIWKKPKIVNKSPEKEVNISANVTLRRSRRGQSTEPPVVKENSNRKRKSVDEEEENVPTSSSGNTENDPLSRGVTPLIFDESKLGAGRHCSTPIRSREDADPSDVTFSLNLSAITEKEDLKNRSKKVKLITFTISSKRMKRKADQCHCINLPSKFVLFISTVCIIVRLSAVFSLN
The following text describes a protein:
Function:
Reversible hydration of carbon dioxide.
Sequence:
MFRLPASHRLSWKSCHSNKFSTSIHLPDERIYPRRVVSTSAKLSPELKDCRYPRNHLARRSFSSSTPTGLPVLKKLLDIMSQPESKTVPFAPSSPTLGNFLDRNHQFASTCDPEVLATTCKGQSPSVFWLGCSDSRVPEGVVIQAGLGEVFVHRNVANVFNPDDTSATAALAYAVNHLKVSHVVVVGHESCGGCAAALAAATAQKPDEESLPATPVDKGEAAIAKWIAPIKNLASIELNKHDHQFSLPKLITLNVENQVKNIIHHEIIQKAWARGQSLAVHGWVYNLSSGKVQDLGLTQSNP
The following text describes a protein:
Function:
Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward EA2 peptide substrate, but has a weak activity toward Muc2 or Muc1b substrates (By similarity).
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Domain:
There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding; The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
Sequence:
MNRIRKFFRGSGRVLAFIFVASVIWLLFDMAALRLSFSEINTRVIKEDIVRRERIGFRVQPDQGKIFYSSIKEMKPPLRGHGKGAWGKENVRKTEESVLKVEVDLDQTQRERKMQNALGRGKVVPLWHPAHLQTLPVTPNKQKTDGRGTKPEASSHQGTPKQTTAQGAPKTSFIAAKGTQVVKISVHMGRVSLKQEPRKSHSPSSDTSKLAAERDLNVTISLSTDRPKQRSQAVANERAHPASTAVPKSGEAMALNKTKTQSKEVNANKHKANTSLPFPKFTVNSNRLRKQSINETPLGSLSKDDGARGAHGKKLNFSESHLVIITKEEEQKADPKEVSNSKTKTIFPKVLGKSQSKHISRNRSEMSSSSLAPHRVPLSQTNHALTGGLEPAKINITAKAPSTEYNQSHIKALLPEDSGTHQVLRIDVTLSPRDPKAPGQFGRPVVVPHGKEKEAERRWKEGNFNVYLSDLIPVDRAIEDTRPAGCAEQLVHNNLPTTSVIMCFVDEVWSTLLRSVHSVINRSPPHLIKEILLVDDFSTKDYLKDNLDKYMSQFPKVRILRLKERHGLIRARLAGAQNATGDVLTFLDSHVECNVGWLEPLLERVYLSRKKVACPVIEVINDKDMSYMTVDNFQRGIFVWPMNFGWRTIPPDVIAKNRIKETDTIRCPVMAGGLFSIDKSYFFELGTYDPGLDVWGGENMELSFKVWMCGGEIEIIPCSRVGHIFRNDNPYSFPKDRMKTVERNLVRVAEVWLDEYKELFYGHGDHLIDQGLDVGNLTQQRELRKKLKCKSFKWYLENVFPDLRAPIVRASGVLINVALGKCISIENTTVILEDCDGSKELQQFNYTWLRLIKCGEWCIAPIPDKGAVRLHPCDNRNKGLKWLHKSTSVFHPELVNHIVFENNQQLLCLEGNFSQKILKVAACDPVKPYQKWKFEKYYEA
The following text describes a protein:
Function:
Functions as an endocytic receptor on a small subset of myeloid cells specialized for the uptake and processing of material from dead cells. Recognizes filamentous form of actin in association with particular actin-binding domains of cytoskeletal proteins, including spectrin, exposed when cell membranes are damaged, and mediate the cross-presentation of dead-cell associated antigens in a Syk-dependent manner.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MHEEEIYTSLQWDSPAPDTYQKCLSSNKCSGACCLVMVISCVFCMGLLTASIFLGVKLLQVSTIAMQQQEKLIQQERALLNFTEWKRSCALQMKYCQAFMQNSLSSAHNSSPCPNNWIQNRESCYYVSEIWSIWHTSQENCLKEGSTLLQIESKEEMDFITGSLRKIKGSYDYWVGLSQDGHSGRWLWQDGSSPSPGLLPVERSQSANQVCGYMKSNSLLSSNCSTWKYFICEKYALRSSV