lhallee/plat_data huggingface dataset:
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.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MSGSGKKVADLAVKAGKAIDWDGMAKMLVSEEARKEFATLRRTFEDVNNQLQTKFSQEPKPIDWEYYRKGIGAKVVDMYKEAYDSIEIPKYVDTVTPEYKPKFDALLVELKEAEQMSLKESERIEKEIAELREMKKKISTMTADEYFAKHPELKQKFDDEIRNDNWGY
The following text describes a protein:
Function:
Acts in a DNA repair pathway for removal of UV-induced DNA damage that is distinct from classical nucleotide excision repair and in repair of ionizing radiation damage. Functions in homologous recombination repair of DNA double strand breaks and in recovery of stalled replication forks. Plays a critical role in meiosis.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body. Barrier septum. Chromosome.
Domain:
The flexible hinge domain, which separates the large intramolecular coiled coil regions, allows the heterotypic interaction with the corresponding domain of smc6, forming a V-shaped heterodimer.
Sequence:
MDGLRPSKRRKSNPLYSDYALGSIVRIKLVNFVTYDYCELFPGPYLNLIIGPNGTGKSTIVSAICIGLGWPPKLLGRAKEAREFIKYGKNTATIEIEMKYRDDETVTITRQISQDKSSSFSINREACATSSITSLMDTFNVQLNNLCHFLPQDRVAEFAQLDPYSRLMETERAIDHEGLLPAHEKLIDLRKREREILQNKNQGQSTLNSLKDRQQALEKEVNIFKEREKIKSYIEMLGLAKMLVIYREKTNVFNQLRADKKKLKKDLKDLVEEFQPILDKGEELRSDLKLKDDTFNDYSSASMELNTSNLRARASFSNFMENEKKLYEKVNTNRTLLRNANLTLNEAQQSVKSLTERQGPRPSDNGVQDLQEKMQEVNAEKLQHENEKLESSHELGSIRTLKAQKLIDLDNIKRELSYYNDATKRKLDFMSSAPGWEDAYQTYQLLKEYESAFEAPAYGPIYMNLKCKEKGFAALIEGFFRTDTFRTFIMSNYNDYLKLMDLITSKTKYTPTIREFSSERKKKIEDFEPPCSREKLQSFGFDGYVIDFLEGPEVVLVALCHMLKIHQIPIAKRELPPASVNALNNFRLANGDPVLKTYLAGSSIHLVFRSAYGDREITRRTDPLPSRSIYFSENVEMDLVKRKEEQLNAQLSQLENLQNEERKLQEKVNEHESLLSRTNDILSTLRKERDEKLIPIHEWQQLQERIEHQTLLLRQREKVPEQFAAEIEKNEDIRKENFEALMNSVLKVKENSIKATNNFEKMLGSRLNVIEAKYKLEKHEMDANQVNARLTEVQDRLKDITDKLASAREDAMSLYGSVVDSLQTQSSDRQTAITELNEEFATSSEVDNKISIEETKLKFMNVNSYVMEQYDARKKEIEELESKMSDFDQSVEELQDEMNSIKEDWVSKLEENVQCISDRFSKGMSGMGYAGEVRLGKSDDYDKWYIDILVQFREEEGLQKLTGQRQSGGERSVSTIMYLLSLQGLAIAPFRIVDEINQGMDPRNERVVHRHIVNSVCDNAVSQYFLVTPKLLPDLTYHRNLKVLCICNGAWLPATFRTSLSTYFEKLKKSALISSS
The following text describes a protein:
Function:
Part of the ABC transporter complex Rv2686c/Rv2687c/Rv2688c involved in fluoroquinolones export. Confers resistance to ciprofloxacin and, to a lesser extent, norfloxacin, moxifloxacin and sparfloxacin. Probably responsible for energy coupling to the transport system.
Subcellular Localization:
Cell membrane; Peripheral membrane protein.
Sequence:
MTALNRAVASARVGTEVIRVRGLTFRYPKAAEPAVRGMEFTVGRGEIFGLLGPSGAGKSTTQKLLIGLLRDHGGQATVWDKEPAEWGPDYYERIGVSFELPNHYQKLTGYENLRFFASLYAGATADPMQLLAAVGLADDAHTLVGKYSKGMQMRLPFARSLINDPELLFLDEPTSGLDPVNARKIKDIIVDLKARGRTIFLTTHDMATADELCDRVAFVVDGRIVALDSPTELKIARSRRRVRVEYRGDGGGLETAEFGMDGLADDPAFHSVLRNHHVETIHSREASLDDVFVEVTGRQLT
The following text describes a protein:
Function:
Subunit e, of the mitochondrial membrane ATP synthase complex (F(1)F(0) ATP synthase or Complex V) that 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. ATP synthase complex consist of a soluble F(1) head domain - the catalytic core - and a membrane F(1) domain - the membrane proton channel. These two domains are linked by a central stalk rotating inside the F(1) region and a stationary 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. In vivo, can only synthesize ATP although its ATP hydrolase activity can be activated artificially in vitro. Part of the complex F(0) domain.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MLIDHPFSLEGDGLPPLAVLKHKRGIVAQLRDTEHKERLFGQWTGLGVTSEAQWTQPAPQELRPHKAPPQGQPRRGTGLHSEARACGACSYPRRAPLRPCPPTQARTLSASSFPFLQPCPFRPFSNSSAWRLLFLLPGRGSTGKMVQPVKVSPLIKLTRYSFLVLGMVYGAKRYAYLKPRAEADRKLAAEKKQKEEEIKKIQQSLEEARGDSILK
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.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side. Cytoplasmic vesicle, COPI-coated vesicle membrane; Peripheral membrane protein; Cytoplasmic side.
Sequence:
MDGNCTLLLNNPYRDFRVEDVSKSLSQTDVKSKITALTKIITAELNGDHHPELLMEVIRNAMPCTEHQIKRLVLIYLESIDKMDKGELRPELILAINGLLQDLNHPNEYIRGITLKFLCHVSEKEIIQPLVNAILENMTHKHVYVRKATANAIGHIYQVDPSLVEHAGDILRKALKEEKDSMTRVVIFSVITRYLPEHAIKFLISIAQQITTFSEPFIMVVLKFIRLIYKSTPQFKSKYIEILGCLISSNSLMVKLEVASIFPLITGNAHVVTQSIQTLVDVVCSSSDVNVKIIGIQRIKMICSRYPKVIKGSCISSLLRMLSIPSIRKDVLQLVMTSLAPRNAGEIVTALRKEIGKDDTGFVVEVLVALRKCKEVNEGVEIDDVMFEALTTPELAKEAIEYIEYRLQGEQRENTVARLIDFIEEVSDNKTLRSIIWMICEYCSHYDEVISMFKRLIVELPNKEETFIEKDIEEKETEEEKKDNGIIESKTVVLADGTYGSVIETFDKQTEKNKFFQKVGLRTMIEQMDSLVISSLAIGIAKICSKVTGKEGNCIRAKGIQILLEVIKIEKKNETHNKMSQDCKEIIQNIIFIISGKKTEYNEQMKQIEEIEKNIRKEVEEGAKRKEHKDIHQIDEKIHYEIFNTADEEENEEKESRIEQIKGERKLERLNNIVQLTGYSDPFYIEAIVTVTHFDITLDCLIMNQTPSTLQNITIELIPHGGMTVKTKPSPVTLGPGDFVRVSLGVKVDATTVGVISGYVNYDIADKNVTYNALDANLILNELRIEYLDQMRPCDVDIEVYQKKWMEYEWENKIPVDTECTDLKEYADLLCSIAKLQCITPAIMFCDSIGFLSANFYAKNLFDEDALINLSAEKIGNKISGWVRIRSKTQSLAINLGDRIVANQKRVSPK
The following text describes a protein:
Function:
Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits.
Subcellular Localization:
Cytoplasm.
Sequence:
MEFKHKKKYGQNFLNNKDEILNKIIEVSNIDDNDEILEIGPGQGALTSLLVERVKKITCVEIDKDLENTLRKKFSSKENYTLVMEDVLEVDLRRYINQGTKVVANIPYYITSPIINKIIENKDLIDEAYIMVQKEVGERICAKSGKERGILTLAVEYYGESEYLFTIPREFFNPIPNVDSAFISIKFYKDDRYKNKISEDLFFKYVKAAFSNKRKNIVNNLVTLGYSKDKIKEILNQIEISENERAENISIDKFIELIKIFEGR
The following text describes a protein:
Function:
Isomerase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B. The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK. Finally, prhA leads to berkeleydione via the berkeleyone B intermediate. PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione. Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable).
Sequence:
MASNSTREKLIALAHKFCSIISSGDMEAVLALRTESCLTYQCCPSFSTRPLNNQETREYFEEWKHIGWNSKFWIIDEGTMVVDEAAKKIAFRAACSADTIGGPYENENLVILQATDDCALVDGIWEFFDAVRKQDLMNRLAAKQAAKGLDSWCANTHSGDDKGVPANNESKVAA
The following text describes a protein:
Function:
APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoproteins are amphipathic molecules that interact both with lipids of the lipoprotein particle core and the aqueous environment of the plasma.
Subcellular Localization:
Secreted. Secreted, extracellular space. Secreted, extracellular space, extracellular matrix.
Sequence:
MRVWTVLLGAVLLLAACQADVQDVETKVKAKWEETVEVFREYVNRLSLATDDITEQITSSQMGKEMDMLIKDXVAELHAYRKDVEERLGPQAVVMRERLHTDVTVLGERLRVDMEEAKTRVQQYLGEARQVAGQNLEDVRSRVGTYLRKLRKRLAKDTEELRRKLEAYSKEATQHLETVREDLEPLREKGQQRLETLQQALRDQGQRLREQLEVRAQEMRGSLDRAATQLQEWLEPFLEDIRTQMQGLLDKLQXKEQQ
The following text describes a protein:
Function:
Kinase that phosphorylates MYL2 in vitro. Promotes sarcomere formation in cardiomyocytes and increases cardiomyocyte contractility (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MSGTSKESLGHGGLPGLGKTCLTTMDTKLNMLNEKVDQLLHFQEDVTEKLQSMCRDMGHLERGLHRLEASRAPGPGGADGVPHIDTQAGWPEVLELVRAMQQDAAQHGARLEALFRMVAAVDRAIALVGATFQKSKVADFLMQGRVPWRRGSPGDSPEENKERVEEEGGKPKHVLSTSGVQSDAREPGEESQKADVLEGTAERLPPIRASGLGADPAQAVVSPGQGDGVPGPAQAFPGHLPLPTKVEAKAPETPSENLRTGLELAPAPGRVNVVSPSLEVAPGAGQGASSSRPDPEPLEEGTRLTPGPGPQCPGPPGLPAQARATHSGGETPPRISIHIQEMDTPGEMLMTGRGSLGPTLTTEAPAAAQPGKQGPPGTGRCLQAPGTEPGEQTPEGARELSPLQESSSPGGVKAEEEQRAGAEPGTRPSLARSDDNDHEVGALGLQQGKSPGAGNPEPEQDCAARAPVRAEAVRRMPPGAEAGSVVLDDSPAPPAPFEHRVVSVKETSISAGYEVCQHEVLGGGRFGQVHRCTEKSTGLPLAAKIIKVKSAKDREDVKNEINIMNQLSHVNLIQLYDAFESKHSCTLVMEYVDGGELFDRITDEKYHLTELDVVLFTRQICEGVHYLHQHYILHLDLKPENILCVNQTGHQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYEFVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNFIVNCSWDFDADTFEGLSEEAKDFVSRLLVKEKSCRMSATQCLKHEWLNNLPAKASRSKTRLKSQLLLQKYIAQRKWKKHFYVVTAANRLRKFPTSP
The following text describes a protein:
Function:
Catalyzes the oxidation of methanol to yield formaldehyde. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA) can serve this function in vitro and is reduced to 4-(hydroxylamino)-N,N-dimethylaniline. It is also able to use ethanol and formaldehyde with an activity comparable to methanol, and has a weak activity with methylamine as substrate.
Sequence:
MAIELNQIWDFPIKEFHPFPRALLGVGAHDIIGVEAKNLGFKRTLLMTTGLRGSGIIEELTGKIEYQGVEVVLYDKVESNPKDYNVMEAAALYQQERCDSIISIGGGSSHDAAKGARVVIAHDGRNINEFEGFAKSTNKQNPPHIAVSTTAGTGSETSWAYVITDTSDMEHPHKWVGFDEATIVTLAIDDPLLYYTCPQHFTAYCGFDVLAHGSEPYVSRLDFAPSLGNALYSVELVAKHLREAVFEPRNLKAREGMMNAQYIAGQAFNSGGLGIVHSISHAVSAFFDSHHGLNNAIALPRVWEYNLPSRYERYAQLATAMGVDTRNMTTVQAADAAVEAAIRLSQDVGIPDNFSQVRVDSYDKNRMNTGKYAGKGEVIKGDDKSVLAISEHIQGDWCTPGNPREVTVDSMIPVVGHAINGTY
The following text describes a protein:
Function:
T-cell activation.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MDTSHTTKSCLLILLVALLCAERAQGLECYQCYGVPFETSCPSITCPYPDGVCVTQEAAVIVDSQTRKVKNNLCLPICPPNIESMEILGTKVNVKTSCCQEDLCNVAVPNGGSTWTMAGVLLFSLSSVLLQTLL
The following text describes a protein:
Function:
Catalyzes the sequential NAD-dependent oxidations of L-histidinol to L-histidinaldehyde and then to L-histidine.
Sequence:
MISRIDLRGDALPEGPALRDLLPRADFDVSVALEKVRPICEAVHHRGDAALIDFTEQFDGVRLERVRVPAEELTRALEGLDPEVRAALEESIRRARLVHREQRRATHTTQVVPGGSVTEKWVPVERVGLYVPGGRSVYPSSVVMNVVPAQEAGVGSIALASPAQAEFGGIPHPTILAACALLGVDEVYAAGGATAVAMFAYGTESCPPANMVTGPGNIWVAAAKRFFTGKIGIDAEAGPTEIAVLADSTADPVHVASDLISQAEHDPLAAAVLVTDSAELADAVEKELQPQVEATKHIEDRIRPALAGRQSAIVLVDGLDEGLRVVDAYGAEHLEIQTADAAAVADRVKNAGAIFVGPWAPVSLGDYAAGSNHVLPTGGCACHSSGLSVQSFLRGIHIVDYTRDALAEVARHVVTLAEAEDLPAHGAAIKARFEWKVPESK
The following text describes a protein:
Function:
Required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in mitochondrial tRNAs that read codons beginning with adenine. Probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Involved in mitochondrial genome maintenance.
Subcellular Localization:
Mitochondrion.
Sequence:
MRLRPIFWTGTTCTRASIRPQWSFRRQLMTLAIETSCDDTSVAIVEKKVENGRAVAQLHFHKKVTANNAEYQGVHPLVSLRSHQENLADLVSEAISHLPPKTASRDHDFEHGGLEAQRPEAVLDVTKKRLPDFVSVTRGPGMRSNLFTGLDTAKGLAVAWQAHALTPRLVSALEPSATPTLEPDFPFLSVLASGGHTLLIQSASLNDHHLLGTTNDIAVGEYLDKVARILLPTELLQSTRSTMYGALLEKFAFEGNASQTVDSQKSKSTCNTGSAPRTSTFSSATASSSQQYLDSSSHDYTWYKVPPNHEEALKTAMTKWGWAFNQPLVTAHCGLKVNDIELSFSGLLTAVERVIGYQTDPVTRKRTKIERTLDEISLEEKKHIAREAMRAAFEHVAYRVVLALRSLASDPAPRSVVLAGGVAANSFLRHILASTLCARGFSHINLYFPPPSFCTDNAAMIAWTGIEMFEAGHTDTLSIRAIRKWPLNQLLDPVVDG
The following text describes a protein:
Function:
Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome. usp103/U1-C is directly involved in initial 5' splice-site recognition for both constitutive and regulated alternative splicing. The interaction with the 5' splice-site seems to precede base-pairing between the pre-mRNA and the U1 snRNA. Stimulates commitment or early (E) complex formation by stabilizing the base pairing of the 5' end of the U1 snRNA and the 5' splice-site region.
Subcellular Localization:
Nucleus.
Sequence:
MPRYLCDYCQVWLTHDSQSVRKAHNAGRAHIQNVQDYYTKVAQEEAQKQLEERASSGFLKKGNGSLDLPYAYAFPPKYNVFNLGCPPPPYIVSANTYMAPKGMNAMNAAAFVPMMPAVNLTNQVAFSAPQTTASSNTQLTQQQQSLPQTNEHQRARTHSNANNHFTKTHHQGQRSHQRFVRA
The following text describes a protein:
Function:
Potentiates insulin signaling.
Sequence:
MAGVLCPTEEDRSSRAALRMLPPQPCPDESGAYRRMSGPTLSQVQEEPAAEPPQPPASAAEDDVRKRGYLRKQKHGHKRYFVLRSQSHLGPARLEYYDNEKKFRSGQRSGCHPKRVIPLYLCFTVSRRADAKNKHLVALYTKDEYFAMAAENEQEQDGWYQALSELINESKGACLDTEELEENYGTLRPGTVFKEVWQVNVKPRGLGQAKNLSGVYRLCLSSKAVHLVKLNSDVACVHLLLMNIRRCGHSENYFFIEVGRSSSTGAGELWMQVDDCVVAQHMHETFLDTMKALKAYSEFRPRSKSQSSCTNPISFITTRRYLGNLPPSQTGLQRRARTESMVGTPPSAKNNSFRFRTSSEGEGTMTRPFRSVTGSLSHLNTARINLGKQEGAGRYVRAPFNSGYQSRSASLPVSHFPSATSPISVCSSSGHGSASETLTRPSSSSVCGSPSDGGFISSDEYGSSPGDLRYFRVRSNTPDSLGNTPPIQEENTLSDYMSMSTHSQPDSRDDYMEADKCFRKRTYSLTKHTNSASKQKSQTAISLGEDSEEINKQFAFAESPKLKDSSLVDDYSNGVIDSVCNQSRSKASDDGYMPMMPSNLYDSDYLPMAPKTVSAPKQINRCPSQADSKGYMMMFPINSSPVKNVFGGAATKSNLEKLSNGGYMDMSYGNSTKQIHDSNLNNNSRGLSSYFSLPRSFKSLTKQTTDQNEYVPMSSPGKLLHLGAENGVDVCKDGAVHDIAKIELKSSSSILDQQVKRPNKLTLGIRGSNTIPRMFDHSAPAEPTSPGEYINIDFSDKASSTPYSLSADGSPSSLGSSCDHRQSPLSDYMSVDIDVQSPKATAEQSNSLTDISLYACTVVSRMQPNAEYAKLPCGTACVSKTDNIMDDYTTMTFNMAMTPPRSFASETENGTKVDSPSSIVNRLCIGELTSLNSGFSLPNPLPEPIAGPKVIRADSQGRRRHSSETFASSSTVTTSSSCFTESGKRHSSASFDNVWLKPDENSCEQENKMSRHCSTGFQNGLNYISLSMHNGVCEPTSPDCHQHQNGSRNLESGGYVSIDFTRCDCLKCPTSRKD
The following text describes a protein:
Function:
In addition to polymerase activity, this DNA polymerase exhibits 5'-3' exonuclease activity.
Sequence:
MNKERLLILDSNSLLNRAFYALPDLMTGEGIHTNAIYGFVNMLLKMKEEINPDYIVAAFDRKAPTFRHEEYKDYKAGRKKMPEELAQQFPIVKELLSALAINIFEIDGFEADDLIGTLSVFAEEKGIEVYIVTGDKDALQLATDNVKVVITKKGITEKEIYDKNRMVEEFGVTPKEFIDVKGLMGDTSDNIPGVPGIGEKTAFKLIKEYKSIETVLENIENIKGKKLKENLHEYREQAIFSKKLATIICNVPIDMSLEDIKSKEEYDINKVREMFERLEFKSLMNKVGKSDEEETVEEEVSYKNIVSLEEFKDLKNNIIKYKENDLYLYFELEDIVLFSKSRVKTLYANFKDEVYRIDFEMLIKNTKEQFIEVCKEIFESKEIKKITYDAKNPRTILRKLGIEFNGIKFDINLAAYLIDPVRKEYEISSLASEYLFKNINREDEFLKIKEVNIMPNLYKVLEEKIKEQDMEELLYKVEQPLTETLSAMETEGFKVDKDILLQLEKKFKGEIESTQLEIYSMSEEEFNINSPKQLGKILFEKLDLPVIKKTKTGYSTNAEVLDKLRDKHPIIDKITYYRQLTKIYSTYIEGLKAAIDEDGKIHSNFNQTVTATGRLSSTEPNLQNIPIKYEMGREIRKVFIPNTGDSVILSADYSQIELRVLAHISDDKNMISAFNEHDDIHTKTASEVFKVPIEEVTPLMRGNAKAVNFGIVYGIGDFSLSQDLNITRKEAKQYIDAYLERYPNVKLYLENIVEEAIEKGYVSTILNRRRYIKEVKSSNKIVKAAGERLAMNSPIQGSAADIIKLAMVNVHRKLKEDNFKSSIILQVHDELILNVHKDELEKIKALVKKEMEQVLELKVGLDVDINIGNNWYEAK
The following text describes a protein:
Function:
Component of the CENPA-NAC (nucleosome-associated) complex, a complex that plays a central role in assembly of kinetochore proteins, mitotic progression and chromosome segregation. The CENPA-NAC complex recruits the CENPA-CAD (nucleosome distal) complex and may be involved in incorporation of newly synthesized CENPA into centromeres. Part of a nucleosome-associated complex that binds specifically to histone H3-containing nucleosomes at the centromere, as opposed to nucleosomes containing CENPA. Component of the heterotetrameric CENP-T-W-S-X complex that binds and supercoils DNA, and plays an important role in kinetochore assembly. CENPT has a fundamental role in kinetochore assembly and function. It is one of the inner kinetochore proteins, with most further proteins binding downstream. Required for normal chromosome organization and normal progress through mitosis.
Subcellular Localization:
Chromosome, centromere, kinetochore. Nucleus.
Sequence:
MASLPEDDLTTRTLLKRVLATEPPHTPLPVPGHDRKPKLETRRRSLRLSGPPLPPPETPATSSPSMTLRNRMKERVRRSMRITRASSSRPPESQASSRPAPPRRDKMDEETPRTILRNIMQTAPEASMLVPNSPAPAVEEVQPLQESRQSSLDLQLPELEPLVPMARAQLGTGRKRRKLRLSEFERGVDQGLAASVGAPSLTIPAEEPLASANTSSLTKSFNLSLTALVLPESVKRPGLARRPRTRKAISLEAFEQGLEKTPLPTQEAAQAASADSWVVADTLLGDTQLFLQASPWDQSRPHHSQVQPAGEGKQDPDKADAHQTRSPSSAASRLSPARQVDGASRSLDGAQVSRQSLGIRHSARFTPTRNKDIREAGAEPGHRSGMELAAVGEREARAVEEEGQVAGLAGKGKAAPLAGEDVATTAMGEREGTPLAGEDGTSAVTGEGKAASLAEEDEAHILEAEEEAEVAESVEEEKEGEVVSEEDGATVEEEESEEAESIEEEEGDEVAAMGEEEDEVTPLVEKDEAVTVGEEEDEAVTTEEEAEAIEEDEVMEEDEPEPLVEEDGLATTEEEEVETEAEGSEEHTGAVQEAEISLKTPAFIQAKRQQAFAPSASPSPARSPPKSFPTKQARARGPARAPRPPRTPGSALLSHYAKIFGFYAKMPVEKAAYKVVEKSLDRYFRQLGDDLEVFTSHAGRKTVEAEDLELLMRRQGLVTDDVSLHVLVERHLPMEYRRLLIPCATSGNRVSPALGQRKL
The following text describes a protein:
Function:
Catalyzes the phosphorylation of ceramide to form ceramide 1-phosphate (By similarity). C.elegans contain specific sphingoid bases, which are unique or different in structure compared to the sphingoid bases found in other animals. Two examples of these distinctive compounds are: 15-methylhexadecasphinganine and 15-methylhexadecasphing-4-enine.
Sequence:
MPNSKKSKKGGDQQHVTIVPVEPVKGENVDTVAYSSRSRISGESGHLIADVQSPHAKKHRIIFDRDHNVFEFRLLDGSAKHIIVYRLDELLSTTCYPFKIKNGVPIIPTKPTTSDKTLYFNFVYKKDKQKWRLKQIPVIFYTTSERDYWHSLIDTTLRRVKNRPKNIIIFINPFGGNGKAQKIFKDNVDAFFWLTPGLRYKVVLTERANHARDYIVEMPPEQWSAIDGLVSVGGDGLFNELLSGALLRTQTDAGRNIDNPSSHLVTPHIRFGIIGAGSANSIVSTVHETNDHATSAVHIAIGSECNVDVCTVHQHQKLIRISANAISYGWLGDVLRDSEEYRCLGPIRYQWSALRTTIRHPIYRGMVQFSLSHKENVNPKDQLPPCLEPCPVCMKPQGNDKYDYHWHAEFTHVICCVIPTVTPFTPYGLAPFTGIGDGTLDLALVPRISRFHNMQFMRKVAMYGGKQLYELDPSLNCYRVTKWSYQPDADQEDPGVWNLDGEILEQPKDEPLHFKLHPQLISFFGRDAAMVKPTKRSFIKKRKSSIVYQ
The following text describes a protein:
Function:
Monokine with inflammatory and chemokinetic properties. Binds to CCR1, CCR4 and CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-alpha induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV).
Subcellular Localization:
Secreted.
Sequence:
MKSSTAAIAVLIVAALCYQVSSTPLAVGSNGRCCYKFLNRALPSSKVMMYEYTGSRCPYRGVIFTTFEGKKCCANPEEKWVQDILNVEKHTDGSK
The following text describes a protein:
Function:
Recognizes and hydrolyzes the peptide bond at the C-terminal Gly of ubiquitin. Involved in the processing of poly-ubiquitin precursors as well as that of ubiquitinated proteins.
Sequence:
MSDSKLVVFGSFTEDETRSLLLKKSSKNAEKSVEKKELQFGSVNFVTVKVSGGLHGESSIELDSPKGSNSVLSSNTIKKDDEVQSVKIVNTHLPGVLRTPKENGSLDGSTHGSHINGAEEVNQDNIGSSSLLISQNQYGPSLPISSLKLQNTEQNGGSMDSSLFAAKDDFRKASNGPVMSCRNLLPRGLINPGNLCFLNATLQALLSCSPFVQFLQELRTRNIPKVGYPTLTAFAEFIAEFDMPNGSSLEKDIATLESGRPFRPAMFEDILKKFTPDVPSSISGRPRQEDAQEFLSSIMDQMHDELLKLEGQSSSINGNKLSLVSSAESDEWETVGRKNKSAVTRTQSFVPSELSDIFGGQLRSLVKARGNKASATVQPFLLLHLDIHPEAVRTIEDALCLFSAPESLEGYRTSTTGKAGVVTASKSFKIQTLSKIMILHLKRFGYGKQGSTKLLKPVHFPLELVLSRELLVSSSNEGRKYELVATITHHGREPSKGHYTADTRYPNGQWLRFDDASVTAIGANKVLHEQAYVLFYKQVE
The following text describes a protein:
Function:
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Sequence:
MSSIIILLFSLLLFTSPSTSSGHHQTPPPLSPSPPPAARIRLACKATRYPDVCVSSLSKPGQVPSNPNPSQIIHSAISVSLENLKTAQSEVKSILDASVGNLNRTNAANKYLQQLSYSLHRTRATYQALTRGKIKDARAWMSAALVSRSPLKYVNGTKEVVETMSSLNEFINVTSNALSMMVSYDNFGDNVSSWTPPATERDGFWDKTGGPKVGAGPTLGFPSGLKEDVTVCKNGKCRYQTVQDAVNAAPANNGVRKFVIKINEGVYEETVTVPFDKKNVVFIGDGIGKTVITGSLNAGMLGITTFDTATVGVLGDGFMARDITFQNTAGPDTHQAVAFRSDSDFSLLENCDFLGNQDTLYVHGLPSVFQDCEILIAPRQLQPEKGENNAVTAQGRIDPAQSTGFVFLNCSITGTDEYMKLYKANPKVHKSYLGRPWKDYSRTVFIGCNLGALINPDGWLPWSGDLSLKTLYYGESKNTGPGSDRSKRVSWSSEIPDEHVDKYSVANFIQAEEWPKSG
The following text describes a protein:
Function:
Catalyzes the transfer of a methyl group onto N-acetylserotonin, producing melatonin (N-acetyl-5-methoxytryptamine).
Sequence:
MASTQSSIKIFCNLGAKKTNTVTIAAVIINQIVYTATTLGIFEELTNSLRPMTACMLALKLGLDADATERLLNALSALSLVEKSFNSSNSAVYRSSTCAEKYLVNSSPFTMKPLIHKVGDLYAVFGQLTKGIKEGRQQLNTALGKGDQCFKKGNGLYSDDKKRMEFLSTMQMFSYADAPHVLKAFDLKQYKTAIDLGGGTGAFGLTLAKKYPSMHVTVADLHDVVKMADQFLPKDVPENLHYEIKDFFEDSLTPADLYILSNVVHDWDVEHLDKLLTKVYHAIKPGGALLVLEKILNENKDGPLSTLILDLGMLVTVNGRERTAAEYKQLFSEYGFKNIRIKVLPEARLRDAILMEKLLLPTEMKEEEISLGEMRKVVDDLK
The following text describes a protein:
Function:
Part of the insoluble cornified cell envelope (CE) of stratified squamous epithelia.
Subcellular Localization:
Cytoplasm. Note=Constituent of the scaffolding of the cornified envelope.
Sequence:
MSHQHTVPVTVPAVVQESLKTVCSPAQTQQEQTKQPTPYPAQCQVFTDTQEKGFPKHEEKEANPVKDLPEQESEHHQQPGPQKQQLQVKKPEQELQEQELHSEKQPQEPQGLLCLGQQQQREPQEQEQHLRQHQQPQQESQGQGLCLGQQQDVLAPQELHMGQHQKEKLQEPELPLGQQQKTPEEQELILGEKQQKLHLVERHQEPQEQELHHGQKQKQQQPQEQELQLVQHQKQKQHEPELCLRKQQQQESHERELHLGKQQQQESHEPELHLGKQQHQESHEPELHLGKQQHQESCEPELHLGEQQHQEQQQHQESCEPELHLGKQQHQETQESELQLGKQQKPHEPDMVLDPKEKQKLHDPELHLGKQQHQESQESELQVEKKQHEKSPEPELHLGKQQELHEPDMTEDQKEKQSLHEPELHLGKQQESHEPDMTEDQKEKQSLYEPELHLGKQQEQQIEYEGYQRSKSLNQLLKQEKASRGQELDDSHLEQEKELLDQRLDQELVNKDEQLERKKHKLENLTQKEKQIKQLVPSTDRVQETQPIQPVKEDSLTTKKQQHSHEVQ
The following text describes a protein:
Function:
Putative transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MLNSYSPLQSPSSSITLPPLFHINNNNNNNNNNNNNNGHNNDKQNVNKLGLKLNINGYDSGFSPFSPNHSIANNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNIQSPKNNNSNNNKLNESCGSLNSSNDNNFNSGNDDNSLKRVRVFSNQNQNQNQNQNQNQNQNQNQNQNQNQNQKDSWNIHFGEIVNIVLELESVLSCKNENINQINQIKSSEKSMRSALYKKEIEILELKDKLNNSSATFNSLKVIQPIKLEKSPRTLNNSSDSISENINNNNNNNNNNNNNNNNNINESNINTSPTHELSGSSGTLGGYSKSHILSILDDLDSESSNISSDSEDDEQPRKVPRDLNYKPNNNINYANNNNNNNNNNNNNNHNNNINNNNNNNNNNNNNSNNYHHSIGSITNSVNIKPSKDQTSNDWAAATEALLNLHTNKNNNNNNNNNNNNNNNYHSNNNNYSNSPNTTPPYQNSNQQFNNNQPQSQQQQQSQQQQQQQQQYQNSINKNITTTTNNNNNNLTSSSNNQAVVYGNTSPNQSSANGNNENVIGVPFTGSIVKRKKRGKLPGEATSILKKWLFEHNMHPYPTEEEKVALANSTFLSFNQINNWFTNARRRILPRQLDRKVFGSPLFSHFSITK
The following text describes a protein:
Function:
Facilitates the differentiation and the cornification of keratinocytes.
Sequence:
VAKLSNPTETEVNRRCIKSLIAVFQKHAGRDGNNSKLSKAESLIFMNTELGAFTKNPKDCGVLDHMMKKLDLNSDGQLDFQEFLNLIGGLVIACHESFLKSVSCQK
The following text describes a protein:
Function:
May play the central regulatory role in sporulation. It may be an element of the effector pathway responsible for the activation of sporulation genes in response to nutritional stress. Spo0A may act in concert with spo0H (a sigma factor) to control the expression of some genes that are critical to the sporulation process.
Sequence:
MNKTNIIVADDEKLIREGLKIILSTYNDIEVVGLAGDGREALSLCKEKDVQVVLMDIRMPNCDGVLGTRIIKEQFPHIKILILTTFNDKEYIHEALKFGASGYLLKDSSNELIYEGIKACVKGNVVVHPDVANNIILNTTYEKELNDDDISLRYNLTEREINIIRQIANGLSNKEIAEKIYLSEGTIKNNISTILSKLDLRDRTQIAIFAFKNNIVN