lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Snake prothrombin activator that attacks the hemostatic system of prey. This non-catalytic subunit is functionally similar to blood coagulation factor V. It serves as a critical cofactor for the prothrombinase activity of the catalytic subunit, which is similar to the blood coagulation factor X. The complex converts prothrombin to thrombin by sequential cleavage at two positions, Arg-320 followed by Arg-271. Cleavage at Arg-320 produces an active intermediate known as meizothrombin. Meizothrombin is the 'second' substrate for prothrombinase, and it docks in an altered manner to present the second cleavage site (271). Cleavage at Arg-271 releases active thrombin from its pro-fragment. This order of events is reversed if the protease component of prothrombinase is used on its own, suggesting that the 271 site is inherently more accessible to proteolysis.
Miscellaneous:
MISCELLANEOUS: In contrast to blood coagulation factors that circulate as inactive zymogen in plasma, venom prothrombin activators are always found in the active form in the venom. Hence, catalytic and non-catalytic subunits are found naturally in venom as stable complexes.
Subcellular Localization:
Secreted.
Sequence:
MGRYSVSPVPKCLLLMFLGWSGLKYYQVNAAQLREYRIAAQLEDWDYNPQPEELSRLSESELTFKKIVYREYELDFKQEKPRDELSGLLGPTLRGEVGDILIIYFKNFATQPVSIHPQSAVYNKWSEGSSYSDGTSDVERLDDAVPPGQSFKYVWNITAEIGPKKADPPCLTYAYYSHVNMVRDFNSGLIGALLICKEGSLNANGAQKFFNREYVLMFSVFDESKNWYRKPSLQYTINGFANGTLPDVQACAYDHISWHLIGMSSSPEIFSVHFNGQTLEQNHYKVSTINLVGGASVTANMSVSRTGKWLISSLVAKHLQAGMYGYLNIKDCGHPNTLTRKLSFRELRRIMNWEYFIAAEEITWDYAPEIPSSVDRRYKAQYLDNFSNFIGKKYKKAVFRQYEDGNFTKPTYAIWPKERGILGPVIKAKVRDTVTIVFKNLASRPYSIYVHGVSVSKDAEGAIYPSDPKENITHGKAVEPGQVYTYKWTVLDTDEPTVKDSECITKLYHSAVDMTRDIASGLIGPLLVCKLKALSVKGVQNKADVEQHAVFAVFDENKSWYLEDNIKKYCSNPSSVKKDDPKFYKSNVMYTLNGYASDRTEVLGFHQSEVVQWHLTSVGTVDEIVPVHLSGHTFLSKGKHQDILNLFPMSGESATVTMDNLGTWLLSSWGSCEMSNGMRLRFLDANYDDEDEGNEEEEEDDGDIFADIFSPPEVVKKKEEVPVNFVPDPESDALAKELGLLDDEDNPEQSRSEQTEDDEEQLMIASVLGLRSFKGSVAEEELKHTALALEEDAHASDPRIDSNSARNSDDIAGRYLRTINRRNKRRYYIAAEEVLWDYSPIGKSQVRSLPAKTTFKKAIFRSYLDDTFQTPSTGGEYEKHLGILGPIIRAEVDDVIEVQFRNLASRPYSLHAHGLLYEKSSEGRSYDDNSPELFKKDDAIMPNGTYTYVWQVPPRSGPTDNTEKCKSWAYYSGVNPEKDIHSGLIGPILICQKGMIDKYNRTIDIREFVLFFMVFDEEKSWYFPKSDKSTCEEKLIGVQSSHHTFPAINGIPYQLQGLMMYKDENVHWHLLNMGGPKDIHVVNFHGQTFTEEGREDNQLGVLPLLPGTFASIKMKPSKIGTWLLETEVGENQERGMQALFTVIDKDCKLPMGLASGIIQDSQISASGHVEYWEPKLARLNNTGMFNAWSIIKKEHEHPWIQIDLQRQVVITGIQTQGTVQLLKHSYTVEYFVTYSKDGQNWITFKGRHSETQMHFEGNSDGTTVKENHIDPPIIARYIRLHPTKFYNTPTFRIELLGCEVEGCSVPLGMESGAIKNSEITASSYKKTWWSSWEPFLARLNLEGGTNAWQPEVNNKDQWLQIDLQHLTKITSIITQGATSMTTAMYVKTFSIHYTDDNSTWKPYLDVRTSMEKVFTGNINSDGHVKHFFKPPILSRFIRIIPKTWNQYIALRIELFGCEVF
The following text describes a protein:
Function:
Plays a redundant role in promoting the expression of calcium channel CACNA1S at the cell membrane, and thereby contributes to increased channel activity. Slows down the inactivation rate of the calcium channel CACNA1C.
Subcellular Localization:
Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side. Cytoplasm, cytosol.
Sequence:
MSGHRPYFNLKREVCHIDWSVLLRARPEEDAADGFRQPCSKRLFYLILDVEKIYNLTLGICNLNKKPVRSERLPISSRAYSLDVDLSQSGFERTAMTTESNEIMESDSQLQRSPSNVPLQPVTSKLQRLKRSLSFKTMMRSKSVENFFQRSYSDARLPPDFITDPPPPSPPLMPGSPLVGERSPSISPSLSPNPSISSHSPSLSLSPSLPAKPYRPQINHCFQDHVFRKPTNCQHCKQMIVGNSKQALRCKTCKMAAHLWCTSELSQQPCHGKSGAFKRNFSSPMLVNDQLSVVKEVLPSQETARMRVDPVYAALRYGTSLAQMSRSSFGSLSESPTRSLGEGGEERQQRQCSMEEEITLETGDTLVADEEMEKEVDESSEQAQVLSEDSSAKIPKRIEVHSIHTYVALYKFLPQEQNDLELHPGDRVQVIDDSNEEWWKGKSGDKIGFFPSNFVQRVRPGERVWRVVQGTSGNRERGHMAVRESQICVGKRDDGEVFVKLSSGKKRGLVPADSIEEI
The following text describes a protein:
Function:
Ethanolamine phosphate transferase involved in glycosylphosphatidylinositol-anchor biosynthesis. Transfers ethanolamine phosphate to the first alpha-1,4-linked mannose of the glycosylphosphatidylinositol precursor of GPI-anchor.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MFGTNRKVFVLISFGFFVHGLVLKAAFDIYFSSPIDNGMTPILSTNKPPAKRLVLFVADGLRAEGIFGENQTENAPNLNKIKQTRGSWGIAHTRVPTESRPGHVALLGGIYEDPSALLKGWKVNPVDFDSVINQSRNAWCWGGPSIINMFNKDDLPHIHLHSYDSSLEDFGNNNTIGLDLWVFDEVNSFIQQQKTCDVCEFKQTGNLFFLHLLGIDTAGHAFKPNSLEYKKNIRFVDENIVKIEHLFETIFPDKSTSYVFTADHGMTNWGSHGSGSDHETTTPLIAWGAGIKIEKKRKDVQQIDIAPLLSALIGINYPINSLGRLPVDYLATSLDNLAQMMISNVLQLVETFNIKRNRRMRNAIRFVPFQGVTTQELESRIAHLKHLSSLQQFDSLKTESEKLIEFLIEGSDYYHNYYQLPILVSITVGIVAWIVYLATFNVRVSQNTSRRKITIYFEVLVFVPLYLNVLYLLIIQSLPLMYYVYFMFPIFMVQILVRRHVFISEALRQVKSSGFRAALGQFVVYLIGLRLLVQGFHNRKSLSIVMYLVLVSVFYSKSLRHTSRYQKTLWTICCVSVSLFPFLPEMTTTFNTTSYLLGYILWCMAACKLISCQKSSKVISVQFGMVVLTPLYTLSVEKGLVTSDSPLKNFALIWSLAPIVAILFSPIQIFSRLCSIFIGFGTFYLMVTSNYENLFLFFYVCLLYVWLILESRLDYKNLGEATFERRFEGNTSQSSDDFRRAFFFVVLIFIGFFGTGNIASLNSFDPMWVRCFLTIFSPFKMAGLILLRIIVPFLFTSCAYRAVNLLCKSNTLNMFCIVLMFSDLMLLELLYYITNIGSWLEIGMSLSKFIIMEAFVIIILILYGFAYLLTSVKVKL
The following text describes a protein:
Function:
Acts as a chaperone during the assembly of the 26S proteasome, specifically of the base subcomplex of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD5:PSMC2:PSMC1:PSMD2 module which probably assembles with a PSMD10:PSMC4:PSMC5:PAAF1 module followed by dissociation of PSMD5 (By similarity).
Domain:
Rich in dileucine repeats, which have been implicated in trafficking of a variety of transmembrane proteins.
Sequence:
MAAQAVSLLREVARLEAPLEELRALQSVVQAVPLHELREQAAELRLRPLFSLLNQNNREQTALCVSILERLLQAVEPIHLARNLRLDLQRGLTHPDDSVKTLTLSQIGRIVENSEAVTEILNNAELLKQIVYCIGGENLSVAKAAIKSLSRISLTQAGLEALFESNLLDDLKNVMKTNDVVRYRVYELIIDISSVSSESLNYCTTSGLVTQLLKELTGEDVLVRATCIEMVTSLAYTHHGRQYLAQEGVIDQISNIIVGADSDPFSGFYLPGFVKFFGNLAVMDSPQQICERYPVFLEKVFEMADSQDPTMIGVAVDTVGILGSSVEGKQVLQKTGTRFERVLMRVGYQAKNASTELKIRCLDAVSSLLYLSPEQQTDDFLGMTESWFSSMSRDSLELFRGISNQPFPELHCAALKVFTAIADQPWAQRLMFNSPGFVEFVMDRSVEHDKASKDAKYELVKALANSKTVAEIFGNSNYLRLRAYLSEGPYYVKPVATTAVEGAD
The following text describes a protein:
Function:
Extracellular signaling peptide that represses primary root growth rate. Negatively regulates the number of leaves and flowering, and modulates leaf morphology. Regulates systemic nitrogen (N)-demand signaling. Mediates up-regulation of genes involved in N uptake and assimilation pathways.
Subcellular Localization:
[C-terminally encoded peptide 2.1]: Secreted, extracellular space, apoplast. Note=Accumulates in xylem sap; [C-terminally encoded peptide 2.2]: Secreted, extracellular space, apoplast. Note=Accumulates in xylem sap.
Sequence:
MKLFIITVVTILTISRVFDKTPATTEARKSKKMVGHEHFNEYLDPTFAGHTFGVVKEDFLEVKKLKKIGDENNLKNRFINEFAPTNPEDSLGIGHPRVLNNKFTNDFAPTNPGDSPGIRHPGVVNV
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor. Essential for the catalytic activity and assembly of complex I.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MVYFIFITFFCLVGGLAVVACNPSPYFGAAGLVLSSVAACTVVVEFGGSFVSLILFLIYLGGMLVVFAYSVALASDPFPEGIWDMSVGAYFTGYLVFLVGFLAVFGGDSFFYNFGVIGSEASGFNVVRGDFEGVSLLYGLGGAGLVICGWGLLLTLFVVLELTRGMSRGGLRVI
The following text describes a protein:
Function:
Glucosyltransferase that adds he final branching glucose to complete the final heptasaccharide structure in the N-linked protein glycosylation pathway.
Miscellaneous:
MISCELLANEOUS: N-linked protein glycosylation in C.jejuni consists in the transfer of a heptasaccharide (GalNAc-alpha1,4-GalNAc-alpha1,4-(Glcbeta1,3)-GalNAc-alpha1,4-GalNAc-alpha1,4-GalNAc-alpha1,3-bacillosamine) from a membrane-anchored undecaprenylpyrophosphate (Und-PP)-linked donor to the Asn side chain of proteins at the Asn-X-Ser/Thr motif.
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MPKLSVIVPTFNRQVLLEKAIKSIQNQDFKDLEIIVSDDNSSDDTKSVVQNLQKDDDRIKYFLNQNYKQGPNGNKNNGLDQASGEFVTFLDDDDELLSGALSTLMQKANEGYAHVFGNCLIEKEGNLSKEFSGKGLEKDSEISKKDFLMAKFSGEFFSVFKKSLLENKRFNEEFYGNEATLWVNLYKEKSFYIHKAFRIYRIFRQDSVTLGASKNAYRVYLGYLELAKILENELRMSKDKDYKKTCASYYKMAAYYAKLAKNYKALYKCLFKSLSIKINAPALILLILSIIPNNMIEKLSKIRVALCKN
The following text describes a protein:
Function:
Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity. Involved in both the HOG and the PKC MAP kinase signaling cascade necessary for adaptation to stress conditions due to high osmolarity or cell wall perturbation.
Miscellaneous:
MISCELLANEOUS: Present with 10200 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MAIDYSKWDKIELSDDSDVEVHPNVDKKSFIKWKQQSIHEQRFKRNQDIKNLETQVDMYSHLNKRVDRILSNLPESSLTDLPAVTKFLNANFDKMEKSKGENVDPEIATYNEMVEDLFEQLAKDLDKEGKDSKSPSLIRDAILKHRAKIDSVTVEAKKKLDELYKEKNAHISSEDIHTGFDSSFMNKQKGGAKPLEATPSEALSSAAESNILNKLAKSSVPQTFIDFKDDPMKLAKETEEFGKISINEYSKSQKFLLEHLPIISEQQKDALMMKAFEYQLHGDDKMTLQVIHQSELMAYIKEIYDMKKIPYLNPMELSNVINMFFEKVIFNKDKPMGKESFLRSVQEKFLHIQKRSKILQQEEMDESNAEGVETIQLKSLDDSTELEVNLPDFNSKDPEEMKKVKVFKTLIPEKMQEAIMTKNLDNINKVFEDIPIEEAEKLLEVFNDIDIIGIKAILENEKDFQSLKDQYEQDHEDATMENLSLNDRDGGGDNHEEVKHTADTVD
The following text describes a protein:
Function:
Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34.
Subcellular Localization:
Cytoplasm.
Sequence:
MLRNDTITAIATPPGEGSIAIVRVSGPDAISISDRIFSGNIAGYASHTAHLGTVSHNAVCIDQALVLVMRAPRSFTGEDIVEFQCHGGYFACSQIVNALLAEGARAALPGEFSQRAFLNGKIDLIQAEAIQQLIAADNIDAFRIAQNQFQGHTSQAISSISSLIIEALAYIEVLADFPEEDIETEDSLPKHRIMEALSITDELLSSFDEGQRLAQGTSIVLAGLPNAGKSSILNALTQKNRAIVTDIPGTTRDILEENWVLQGKNLRLIDSAGLRETENLVEKEGIARAREAMSQAEGILWVVDASQPLPEFPTILYQKPTILLWNKCDIVSPPQIEVPFQQISVSAKTGEGLLELKQALQKWLNTTQLGKSSKIFLVSARHHSLLHSVYTCLTAALNGFTEHLPNECIALDLRQALHSIGNLSGSEVTENVLGEIFSKFCIGK
The following text describes a protein:
Function:
Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MQIDDSGEEPSSKIMAPSSVSPSISVLLHPLVVMNISDHFMRFLAQESSEDSQIIGALIGTQKGRTVEISNSYELDCNFNTGKPFLNVDYFKDREEKFRELTDEFMFIGWYTIGSSPNETDLNIHQQFCQIYDSPLLLKLNPNCNYATNLPVAIFETVVDAVDNQAKILFLEIPYTLATEDSERIGVDHIAKTSYSETTSTSSAADNLLAQYNAIKMLHTRVKLLTDYVKAVRAGKLSYKHEILRDISSMCQRLPIAKSKQFTVESVNQYNDVLLMACLAAITQGCKNSDEFITKANDLYEASGHRMRTFFY
The following text describes a protein:
Function:
Membrane-bound UDP-glucosyltransferase (UGT) which catalyzes the C-glucosylation of kermesate and flavokermesate to produce carminate and flavokermesate 7-C-beta-D-glucoside (dcll) respectively. Carminate is used as a deterrent against insect predators.
Miscellaneous:
MISCELLANEOUS: Carminate, also known as cochineal dye, is used as a fabric and cosmetics dye and as a natural food coloring.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Note=Localization to the endoplasmic reticulum membrane is critical for its activity.
Sequence:
MEFRLLILALFSVLMSTSNGAEILALFPIHGISNYNVAEALLKTLANRGHNVTVVTSFPQKKPVPNLYEIDVSGAKGLATNSIHFERLQTIIQDVKSNFKNMVRLSRTYCEIMFSDPRVLNIRDKKFDLVINAVFGSDCDAGFAWKSQAPLISILNARHTPWALHRMGNPSNPAYMPVIHSRFPVKMNFFQRMINTGWHLYFLYMYFYYGNGEDANKMARKFFGNDMPDINEMVFNTSLLFVNTHFSVDMPYPLVPNCIEIGGIHVKEPQPLPLEIQKFMDEAEHGVIFFTLGSMVRTSTFPNQTIQAFKEAFAELPQRVLWKFENENEDMPSNVLIRKWFPQNDIFGHKNIKAFISHGGNSGALEAVHFGVPIIGIPLFYDQYRNILSFVKEGVAVLLDVNDLTKDNILSSVRTVVNDKSYSERMKALSQLFRDRPMSPLDTAVYWTEYVIRHRGAHHLKTAGAFLHWYQYLLLDVITFLLVTFCAFCFIVKYICKALIHHYWSSSKSEKLKKN
The following text describes a protein:
Function:
Glycosyltransferase which elongates the O-linked glucose attached to EGF-like repeats in the extracellular domain of Notch proteins by catalyzing the addition of xylose.
Subcellular Localization:
Membrane; Single-pass type II membrane protein.
Sequence:
MRRYLRVVVLCVACGFCSLLYAFSQLAVSLEEGAGGGGGKPQAAVASWLAGGGRGAVRGAGVAGPAAHPGGSDRCKDFSLCYWNPYWMLPSDVCGMNCFWEAAFRYSLKIQPVEKMHLAVVACGERLEETMTMLKSAIIFSIKPLQFHIFAEDQLHHSFKGRLDNWSFLQTFNYTLYPITFPSENAAEWKKLFKPCASQRLFLPLILKEIDSLLYVDTDILFLRPVDDIWSLLKKFNSTQIAAMAPEHEEPRIGWYNRFARHPYYGKTGVNSGVMLMNMTRMRRKYFKNDMTTVRLQWGDILMPLLKKYKLNITWGDQDLLNIMFFHNPESLFVFPCQWNYRPDHCIYGSNCQEAEEEGIFILHGNRGVYHDDKQPAFRAVYEALRNCSFEDDNIRSLLKPLELELQKTVHTYCGKIYKIFIKQLAKSVRDRYARSPKEK
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Sequence:
MFRIGRIFPISVPPAHPNPLTRVFFDVDVGGTPLGRIVFQLFDNIAPKTATNFLRIAQGVQVDGKKLHYEGSQINKILPFRGIWGGALGGSIYGRTFPDENYSIKHNRAGLLTTSNPKINSNDAGFIITLGPAEWLDKKSVAFGEVIYGIQHVRAIEKLGGLSGAPKKSVVIKQSGVITEHEYHKYDVIEEPNIWNLQSHH
The following text describes a protein:
Function:
Key regulator of mitochondrial quality that mediates the repairing or degradation of unhealthy mitochondria in response to mitochondrial damage. Mediator of mitochondrial protein catabolic process (also named MALM) by mediating the degradation of damaged proteins inside mitochondria by promoting the accumulation in the mitochondrial matrix of hydrolases that are characteristic of the lysosomal lumen. Also involved in mitochondrion degradation of damaged mitochondria by promoting the formation of vacuole-like structures (named MIV), which engulf and degrade unhealthy mitochondria by accumulating lysosomes. The physical interaction of SPATA18/MIEAP, BNIP3 and BNIP3L/NIX at the mitochondrial outer membrane regulates the opening of a pore in the mitochondrial double membrane in order to mediate the translocation of lysosomal proteins from the cytoplasm to the mitochondrial matrix. Binds cardiolipin. May form molecular condensates (non-membrane-bounded organelles) within mitochondria that compartmentalize and promote cardiolipin metabolism.
Subcellular Localization:
Cytoplasm, cytosol. Mitochondrion outer membrane. Mitochondrion matrix. Note=Localizes to the cytosol under normal conditions. Relocalizes to mitochondrion outer membrane following cellular stress. May form molecular condensates in the mitochondrial matrix. Colocalizes with BNIP3 and BNIP3L at the mitochondrion outer membrane.
Sequence:
MAESLKKLAKSESLQALQDKVTYWVNDYNSNSCDQNLNYCIELIEQVAKVQAQLFGILTVTAQEGGNNEGVETIKCRLLPLLQTSFSSVNMGKTAESEMCATQDFQLRSKNRDNSPDQDQHQSDNESFSETQPTQVQDDLAESGKSLEGAKNGSTISLLAAEEEINQLKKQLKSLQAQEDARHKTSENRRSEALKSDHRSTKRTQDQRPQDVVSNYEKHLQNLKEEIAVLSAEKSGLQGRSARSPSPSTGTRSHRRGRSRSHSRSRSHSRSNSPCTTVAKIRSPSPNRAKMSSVARKAALLSRFSDAYSQARLDAQCLLRRCIDRAETVQRIIYIATVEAFHVAKMAFRHFKIRVRKMLTPSNVGSNTDFETAVSEYIVCHLDLYDSQSSVNDVIRAMNVNPKISFPPEVDFCLLTDFIQEICCIAFAMQSLEPPLDIAFGADGEIFNDCKYRRSYDSDFTAPLVFYHVWPALMENDCVIMKGEAVTKRGAFWSSVRPVMRCRSRSLSPICPRNHFGISTVSRSRSPSPIRCTFARY
The following text describes a protein:
Function:
ESCRT-III-like protein involved in cytokinesis, nuclear envelope reassembly and endosomal tubulation. Is required for efficient abscission during cytokinesis. Involved in recruiting VPS4A and/or VPS4B to the midbody of dividing cells. During late anaphase, involved in nuclear envelope reassembly and mitotic spindle disassembly together with the ESCRT-III complex: IST1 acts by mediating the recruitment of SPAST to the nuclear membrane, leading to microtubule severing. Recruited to the reforming nuclear envelope (NE) during anaphase by LEMD2. Regulates early endosomal tubulation together with the ESCRT-III complex by mediating the recruitment of SPAST.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasmic vesicle. Midbody. Nucleus envelope.
Sequence:
MLGGGFKSERLRVNLRLVINRLKLLEKKKTELAQKARKEIADYLSAGKDERARIRVEHIIREDYLVEAMEILELYCDLLLTRFGLIQSMKELDPGLQEAVSTLIWAAPRLQSEVAELKIVSDQLCAKYSKEYGKLCRTNQIGTVNDRLMHKLSVEAPPKILVERYLIEIAKNYNVPYEPDAMVRPEVCPGEEADLIDVDSDFKKPGAGGGGGGGGGFTAPAMGMPMPMPMPMPMPTAFNYPPPKGAEPFNGPVGTYDGFSNFQAPMRGGQPPQLPSCPPTYESVIPGPTPAGQVYDNSTLPELPSVPDTLPASSFGAKANTSEDIDFDDLSRRFEELKKKT
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MPGVIMNQDNINGRGLGLHDQLNGVSSAPAGSSQLGNPVGLHNGSLPTNGVQHPDSRGSDENYRTKMMLSASGDPPELQHIVQGFFPLAKLLNRSAQQCWNDLADLVAELAEIQVPSHDSNFSPISPNTKVLGNQSPENVRKKLRALEFAQKKRGEFIKLLVLSQWSRQAADVSRLIDIQNFIRTQHQAYAGALQCMGDMKRDLVRAQVANPDLNTALEVLLRGEVVSMPDLGYRPPKPLTPKSTLKKMRKINRVISTRLALHDDIPLAFQKYRVHDGRVTFVVPGEFELDLSIGEEDVTSQFFFVDIRFLFSPSPSIPAGRMLSELDIKINDTLRNGGLSECFNWLHNLILTNKINILARQASELSRSLWSNVLRSELLHRTLVLQYWASKPNTKSWLEIGIRRGPRESTIGGMRPPSLGLRWIRDGQEVNSDDVEFDTDSLSVDRLLRSAIALHISHILSSAFRRISEKLLYSNGSLSLHAYLTRTEPGDCQLDVQLTASRRLRVAIEPLSGAIVLAATPNTLERVDTDRNMDRSTIDDIVSRVGRLRCAAAIEEVESQVKMLGFISVSPRNVRIDARSLFPANVLRFSFFWHHHWERSWLLAATSSMDGDKWWVVQTPSADSVTINRSLDAAVHHASSAVRSAQVICNLLLPAEQPDYSSLADLGHCLSGFLAIYANARFLQDLQFIKIWPHLEHLRIGPGLQVPDLNIEYEATKLPEALRVALPAGFKRKTFVKKTIRLAFHGIDRCRKVAIMVAYGNLSTSFPALGDLVAEDDHSLVLQKTGTGFALRLLASPGYPVVVALLESLQRLECVLSVYEILRRKKMDARFLSLSRLGFAYGPNKELLAQLDIGETQPQLPTEMDPLKLAFRTGHLFHYRLSISFDHSNPHRRIQGPLASNLNRPTAEAGLDTLTEILSFTLPLMQALDRFMANPSRNESSIVHVTVRNATSFQIHYPYEKCRLRLVAHQHQNQPVWVLRDVLSFQDGSCEPEFKHKLQERLYNSKGTGWRGLGNGVIAEPDHIGDLLDELDRCLASTKANTTPKALDSRTSHDAPAANNQSPAIRPEKSVEAADMHGGFVNRNLQQKAGPASQKTDVITID
The following text describes a protein:
Function:
[Isoform Terminase large subunit]: The terminase large subunit acts as an ATP driven molecular motor necessary for viral DNA translocation into empty capsids and as an endonuclease that cuts the viral genome to initiate and to end a packaging reaction. The terminase lies at a unique vertex of the procapsid and is composed of two subunits, a small terminase subunit involved in viral DNA recognition (packaging sequence), and a large terminase subunit possessing endonucleolytic and ATPase activities. Both terminase subunits heterooligomerize and are docked on the portal protein to form the packaging machine. The terminase large subunit exhibits endonuclease activity and cleaves the viral genome concatemer once the capsid is full (headful packaging). Once the capsid is packaged with the DNA, the terminase complex is substituted by the tail.
Domain:
[Isoform Terminase large subunit]: The N-terminus contains an ATPase domain. The ATPase domain binds to dsDNA in a sequence non-specific manner. The C-terminus contains an endonuclease domain. The terminase nuclease domain binds ssDNA but not dsDNA.
Sequence:
MEQPINVLNDFHPLNEAGKILIKHPSLAERKDEDGIHWIKSQWDGKWYPEKFSDYLRLHKIVKIPNNSDKPELFQTYKDKNNKRSRYMGLPNLKRANIKTQWTREMVEEWKKCRDDIVYFAETYCAITHIDYGVIKVQLRDYQRDMLKIMSSKRMTVCNLSRQLGKTTVVAIFLAHFVCFNKDKAVGILAHKGSMSAEVLDRTKQAIELLPDFLQPGIVEWNKGSIELDNGSSIGAYASSPDAVRGNSFAMIYIDECAFIPNFHDSWLAIQPVISSGRRSKIIITTTPNGLNHFYDIWTAAVEGKSGFEPYTAIWNSVKERLYNDEDIFDDGWQWSIQTINGSSLAQFRQEHTAAFEGTSGTLISGMKLAVMDFIEVTPDDHGFHQFKKPEPDRKYIATLDCSEGRGQDYHALHIIDVTDDVWEQVGVLHSNTISHLILPDIVMRYLVEYNECPVYIELNSTGVSVAKSLYMDLEYEGVICDSYTDLGMKQTKRTKAVGCSTLKDLIEKDKLIIHHRATIQEFRTFSEKGVSWAAEEGYHDDLVMSLVIFGWLSTQSKFIDYADKDDMRLASEVFSKELQDMSDDYAPVIFVDSVHSAEYVPVSHGMSMV
The following text describes a protein:
Function:
[Ubiquitin-like protein FUBI]: May have pro-apoptotic activity; [Small ribosomal subunit protein eS30]: Component of the 40S subunit of the ribosome. Contributes to the assembly and function of 40S ribosomal subunits (By similarity).
Miscellaneous:
MISCELLANEOUS: FAU encodes a fusion protein consisting of the ubiquitin-like protein FUBI at the N terminus and ribosomal protein S30 at the C terminus; MISCELLANEOUS: [Ubiquitin-like protein FUBI]: Lacks the typical lysine residues that participate in Ub's polyubiquitination. However contains a C-terminal di-glycine signature after its proteolytic separation from ribosomal protein S30 and could theoretically be conjugated onto target proteins.
Subcellular Localization:
[Small ribosomal subunit protein eS30]: Nucleus. Cytoplasm.
Sequence:
MQLFVRAQELHTLEVTGQETVAQIKDHVASLEGIAPEDQVVLLAGSPLEDEATLGQCGVEALTTLEVAGRMLGGKVHGSLARAGKVRGQTPKVAKQEKKKKKTGRAKRRMQYNRRFVNVVPTFGKKKGPNANS
The following text describes a protein:
Function:
Required for the assembly of cytochrome c oxidase.
Subcellular Localization:
Mitochondrion intermembrane space.
Sequence:
MATQVPPSTTPTPFANRPAPPTKDLEIPEDYKKTFRGRGTVSKFVDPCEAARKASLDCLERTQYNRSECTDFFTAYKECKGNWLAQRKEDRMKGRDTV
The following text describes a protein:
Function:
Heterodimerizes with pms1 to form MutL alpha, a component of the post-replicative DNA mismatch repair system (MMR). DNA repair is initiated by MutS alpha (msh2-msh6) or MutS beta (msh2-msh3) binding to a dsDNA mismatch, then MutL alpha is recruited to the heteroduplex. Assembly of the MutL-MutS-heteroduplex ternary complex in presence of rfc and pcna is sufficient to activate endonuclease activity of pms1. It introduces single-strand breaks near the mismatch and thus generates new entry points for the exonuclease exo1 to degrade the strand containing the mismatch (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MDFLKSLPPLQTTDSNSTTAAVNTTTTTATNTATTTATNTATTTTTTTTTNLNNLINESKKKIHRLTQEVVNKISAGEVIQRPSNALKELLENCLDAKSTTITVTVKDGGMKFLQIQDNGSGIRLEDMGIVCERFTTSKLTKFEDLRSIQSFGFRGEALSSISHVSHLKILTKTADSPCAYRACYLNGKLTPPSPNEQSSDPKPCAGVNGTQITVEDLFFNTPSRKNVLKNTVDEHSRIVLLMKKYAINNPTVSFILKKQGDPTPEVHTSGGQNSLEKDVIGSLYGTDLSKELKIITIDPNNPNPNNDDDDNISGSQIKNSNLNRLDFTMKGFFSSTNYNSKKINFILFINGRLVDSKNLKTGLEQVYSKYLPKGTHPFMFIRLLVPPKNIDVNIHPTKSEVKILHEEQIIEFIQQKVDQELSISSNSKTFSTQILLPGFDQDNVSSSQKKQKNSQSSSTQTKSTNNNNNPTSRKEPIEYAKDKIRSDSKSQTLDAFLNPMDYNNNNDSSIDDNDGSGIGRYDDVDGSAGAAGAGGKFNDNLIFNDNSENEAPRDIDNPLSSVTPIKSKEQRQQQSTTTTTTTTTTTATTKSNSPASKNDIKKLQEHTFITPRKTRKYKQVELTSIKTLISEFQSNVHDGLKEFFNDCVFVGCLDHSYALVQFGKKLYLINLENITKELFYQLSLLRFSDFDSIKFSQSLSIYSLLLVSLDSPLSGWMESDGPKDKIADYLTKLLISKKELLNEYFSIEINEDGELVGIPQVLDHYVPCTDNLPIFLLKLATEVEWEFEKECFAGIVKEISSFFKIEPSFLKLRDTQVNNQQQTNSTTTTNNINFIKKDGKEWIIQHLIFPAFRKLSPPKKFANDGSVIQITTLDNLYKVFERC
The following text describes a protein:
Function:
Mu-conotoxins block voltage-gated sodium channels (Nav). This toxin inhibits tetrodotoxin(TTX)-sensitive sodium channels, but does not affect TTX-resistant sodium channels. Reduces the amplitude of currents without changing the activation and inactivation kinetics of currents.
Miscellaneous:
MISCELLANEOUS: Negative results: does not have the ability to interact with the G-protein coupled somatostatin type 3 receptor (SSTR3).
Subcellular Localization:
Secreted.
Domain:
The cysteine framework is V (CC-CC).
Sequence:
MRCLPVFIILLLLIPSAPSVDAQPTTKDDVPLASLHDNAKRALQMFWNKRDCCPAKLLCCNP
The following text describes a protein:
Function:
May be involved in recombination.
Subcellular Localization:
Cytoplasm, nucleoid.
Sequence:
MFFRNLTLFRFPTTLDFSEIETLLPQVQLKPVGPLEMSSRGFISPFGRDEQDVLSHRLEDFLWLTVGGEDKILPGAVVNDLLERKVAEIEEKEGRRPGGKARKRLKDDLIHELLPRAFVKSSRTDAILDLQHGYIAVNTSSRKSGENVMSEIRGALGSFPALPLNAEVAPRAILTGWIAGEPLPEGLSLGEECEMKDPIEGGAVVKCQHQELRGDEIDKHLEAGKQVTKLALVMDDNLSFVLGDDLVIRKLKFLDGALDQLEHSEGDGARAELDARFALMSAEVRRLFLLLEDALKLSKAEA
The following text describes a protein:
Function:
Involved in the degradation of asparagine-linked glycoproteins. May hydrolyze of N-acetyl-beta-D-glucosamine (1-4)N-acetylglucosamine chitobiose core from the reducing end of the bond.
Subcellular Localization:
Lysosome.
Sequence:
MKYFFIIFIIFLYINKITCINNKPCPCSNQKLCEPVSVGYRKEFLGFSVNNTHYPYYDWDILTTIGVFYDEPIEDELLCLAHSKDVRLVYSAYYPVDQLGNYTQRTEWINEKVEQVVSTYADGVNFDVEDPITNATIAQWYTELVDETNKAFKSINPYYSVTVDIAWSPNCIDDRCYDYVGLSKVSDYMVVMDYDLRSRVYGVSVCTASANSPPELIIEGLLNFTKLGISPDVLVMGLPFYGYNYSCINSNSTFDSKECVIPAGSYLGCNCTDAVGNEVNYDLIMDMLQDDSIKKSPLGWDRDLQSPFFNFIDPSTNSKHQMWFDNPESLEYKVKMARKYELRGVSVWNIDQLNTHNQKQSDPMWESLGIFFK
The following text describes a protein:
Function:
Plays a role in the regulation of phosphate uptake.
Subcellular Localization:
Cytoplasm.
Sequence:
MGILDNELRKLKEKILILGCLVEEGIRKSVKALIDRDIDLAKQVISRDNLINGLEVEINEECIRLIALRQPMAKDLRFITTAMKICTDLERMGDFAVNIAERAIELAQEPFLKPFVNIPKMAEITESMVEDAINAFVKEDVDLCYEVIKRDDQVDELLENNHNELFGLMVKNPDIIPLALKRMFIAKYLERISDHATNIAEMVIYMVEGKMIRHTFVTEEIHKLCLEDFMSRQK