lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
Subcellular Localization:
Cytoplasm.
Sequence:
MANHPIDQELTSPAEEELTPREIVAKLDEHIISQKNAKKAVAIALRNRTRRKKLDPEMREEIYPKNIIMIGPTGVGKTEIARRLSKLCGAPFLKVEATKYTEVGYVGRDVESMIRDLAVISMNLVKQEFRTKVEETAKQKAEEALLDILLPFPGENKHGSGQITGFATSSTLADEEDRKTHFLETREFMRKKLKTGKLDDQEVELDLPNPSVSQVPMLQVFGAGNLDDLDNQLQNVLGDILPKKNKKRKLKIPEALKALEESEAEKLLDPDKVQREALRRVEEMGIIFLDEIDKIAGREGKSGADVSREGVQRDLLPIVEGATVNTKIGPVKTDHILFIAAGAFHMTKPSDLIPELQGRFPIRVELEKLSREDFEKILTAPCSSLTRQYEALLSTDGIQLEFSLDGIQEIARIAYDMNEKHENIGARRLNTILERLLEEVSFEGPDLPESQRKVRIDGKYVTDRLQGVIQNKDLSQYIL
The following text describes a protein:
Function:
Required for assembly of the mitotic spindle.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MMMVARVATAEHVGSAGASLPQTPGSRSFALGAHPGPQKRIGGPAQGQTAFITPLVTPDGIYSRPSSPYMQASPLLKGSESGGSAGSPQSPDAPSSASGASVGNAIGSGYTGNVSVAIRIKPSESSTKDPWYASNDRLIHTEFGEFQFDHVFTKGVCNQEVYQALGVPIIDKLFEGYNATIFAYGMTGSGKTFTMSGNKQEPGLIPQCVGNIFDRISSEHHGASLAYEVKVSYLEIYNEKIYDLLNYVDRQAGSTGQPSRNATGLKIRDDSKYGVKVVDLTEQLVSSHEDVMKWIATGDRNRKTGETDFNTRSSRSHAIVLLRLTRYDLKTGSEATSTLSLCDLAGSERAVTQIVRRKEGAFINKSLLALGTVIAKLSMLGSQANGLQPSPAAGHIPYRDSKLTRILQPALTGDSIITTICTIDSKAESSTETTNTVRFASRAKNIALNVRKNEMDSHAEKDTIIQNLRKQLDEQHETIVMLRRSAAAPSGNGSTSPLDSPGVGGTSLSERTHNMEKGLLEVENSILKTKLEHCEKLLDKDMMVLEDPHVREIVEMLPLDIASVLESKVQGMESQLRQYRVYVQKLESDLLKAQRNIITTHSVQFNRQSTANVQEKYGSDVDIELLLEEQEAELMELRNALKRKDKMIEALQSARRLRDSALSPTTTVLLQRKESVIDPRDPQPV
The following text describes a protein:
Function:
S-crystallins are structural components of squids and octopi eye lens. Contains relatively little if any GST activity.
Sequence:
MPSYKLVYFNGRARAETARLAFVASGIEFEDVRVEAEKWPELKPKTFSGYLPYLEVDGKVLVESMAIARFVAREGKLAGGCNYEQAQIDSIVDILSYVVEKVYKVVYYAKGEEKERLHKELVEKTAPETFKLLEKFLQDQDFFVHNKLSLADLHFYTVLESMTPAYEDWPKLSPKLKALFDRVATEPKIAEYLKKRPVTEY
The following text describes a protein:
Function:
The RuvA-RuvB-RuvC complex processes Holliday junctions during genetic recombination and DNA repair. Endonuclease that resolves Holliday junction (HJ) intermediates. Cleaves cruciform DNA by making single-stranded nicks across the junction at symmetrical positions within the homologous arms, leaving a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C>G/A)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange, although there is some flexibility in the position cleaved. The cleavage reactions can be uncoupled; incision requires the presence of two consensus cleavage sequences, although they do not have to be identical. The presence of a 5'-phosphate in a half-cut site accelerates cleavage of the second site, ensuring the second cleavage occurs within the lifetime of a single RuvC-HJ complex. Binds to cruciform DNA in a sequence non-specific manner; An in vitro resolvase system that forms and processes HJ has been reconstituted with DNA substrates, RuvA, RuvB and RuvC. RuvA-RuvB increases the rate of strand exchange (branch migration), dissociates the RecA filament and allows RuvC to cleave in both orientations at the cruciform junction. HJ-RuvA-RuvB-RuvC complexes resolve Holliday junctions and also undergo branch migration, providing evidence for a coupled branch migration/HJ resolution reaction.
Miscellaneous:
MISCELLANEOUS: The dual incision reaction has defined structure and sequence requirements which must be satisfied for efficient nuclease activity. These requirements are biologically important since they serve as a control mechanism that prohibits the nuclease from cutting DNA at structures that could bear a physical resemblance to a Holliday structure.
Subcellular Localization:
Cytoplasm. Note=In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours.
Domain:
Each subunit has a cleft approximately 20-25 Angstroms wide and 20 Angstroms deep, which is sufficient to accommodate dsDNA. Residues thought to be catalytically important (Asp-8, Glu-67, Asp-139 and Asp-142) line this cleft.
Sequence:
MAIILGIDPGSRVTGYGVIRQVGRQLSYLGSGCIRTKVDDLPSRLKLIYAGVTEIITQFQPDYFAIEQVFMAKNADSALKLGQARGVAIVAAVNQELPVFEYAARQVKQTVVGIGSAEKSQVQHMVRTLLKLPANPQADAADALAIAITHCHVSQNAMQMSESRLNLARGRLR
The following text describes a protein:
Function:
Transmembrane component of the tectonic-like complex, a complex localized at the transition zone of primary cilia and acting as a barrier that prevents diffusion of transmembrane proteins between the cilia and plasma membranes. Required for ciliogenesis and sonic hedgehog/SHH signaling.
Subcellular Localization:
Cell projection, cilium membrane; Multi-pass membrane protein.
Sequence:
MVVLEVFTKNIKISYKSTLLSKASVLALIFGVLSLVLPFIFAYKSKGLWLKRDTFYEQPDVKFRGEYIFVATTNNYNKSVITCSNLPHFDNVLRPLDTCSVIKVRETDRNFDGKTEELDLSLQVNLPVNTHLTSFCIIIPFNYKLQVCPLEMQTAIIFQELLPFYISKYSLVANVVVTQTSPLICHRKNTNTLFNYPVIVDNGDLNNYDINTIITNFSKRNISTSLRDVYKSFSPGKTQNFVLNLNIEFPEDRIYYKPGFWQVLKWAWIHTIFLAGD
The following text describes a protein:
Function:
Involved in the catabolism of quinolinic acid (QA).
Sequence:
MTTTAPVAPADALVEADVARALAEDIGSGDVTAALLPDAPDTAYLLCKQDAVIAGRPWFDATHRALDPQVQIAWRIQEGDRVGAGTVLATLHGRSRSLVSAERTSLNFLQTLSATATTTAAYVAAVAGTGARILDTRKTLPGLRAAQKYAVRCGGGDNHRIGLFDTVMLKENHIRAAGSLSAAVHAARVQQPQLPLVVEVETLEQLREALQVGCTRILIDDFDPAMRRAAVQIVAALPPAQRIPLEVSGSVDLAGIRAIAQDGVDCISIGGLTKHVQAVDLSLKLGPAPY
The following text describes a protein:
Function:
Neurotrophin which may function as a ligand to the Toll-related receptor Tollo. Involved in a Tollo and JNK signaling pathway that positively regulates neuromuscular junction (NMJ) growth in presynaptic motorneurons. May function by activating Tollo to promote the phosphorylation of JNK.
Miscellaneous:
MISCELLANEOUS: 'Spaetzle' means 'noodles' in German.
Sequence:
MALTNFSLPFGALGQPWGVTIAPLHPIHQLASNTNNLLYSPADHQQQTPAEAAADPEYFKNNPYAPPQSGGYQYQNTAGRRKQSNAYLPPTAPNAVRNSVYHIQQVQQTQQQQTQQQHQQQDQHENSVSFQSSSSRSSSSSTTGQSSIQLTQTHASGRGPAEGSYSRYPGQQAQPPQQQQPQQKQYFNAHGSASATFTKNSGSFSITSFGSRQQQQQPPQPQQPPPSQQQQPPPAPPPQRSRQAKPEAQPAQTYGVAPPENYPERAPGFTRVQAGQGSRTQVHAVLDYDVEEGEEDEEEDGEEEGQFYEGQENDKSNNNQMPTVTPIQGPIYLKNGTVPVVPLFSYPKLNNGSFLQIPIWWTALSVALGLDVRGDVIKGVPCIKRYHQLFCPTAGNSYPIDKIERFIDDNKALMRRMYGDFEMNMEGPGGGGGRQQGKVRKRRFIDEPDIFIPPGAFAANAGETVEAGDSYFGQLRKKRQAAAGGSRNRGGSAGGSGNGNTNANRQPGNKNGSSGTGRLDACESKIEIVTPYWASNSAGKIRAIVNTQHFEQAIHQEVCSNTQTPRCEGECGCEQKYKWHRLLAYDPDNDCKGIFMDWFLFPSCCVCRCNP
The following text describes a protein:
Function:
PsaA and PsaB bind P700, the primary electron donor of photosystem I (PSI), as well as the electron acceptors A0, A1 and FX. PSI is a plastocyanin-ferredoxin oxidoreductase, converting photonic excitation into a charge separation, which transfers an electron from the donor P700 chlorophyll pair to the spectroscopically characterized acceptors A0, A1, FX, FA and FB in turn. Oxidized P700 is reduced on the lumenal side of the thylakoid membrane by plastocyanin.
Subcellular Localization:
Plastid, chloroplast thylakoid membrane; Multi-pass membrane protein.
Sequence:
MMIRSPEPEVKIVVDRDPVKTSFEEWARPGHFSRTIAKGPDTTTWIWNLHADAHDFDSHTGDLEEISRKVFSAHFGQLSIIFLWLSGMYFHGARFSNYEAWLSDPTHIGPSAQVVWPIVGQEILNGDVGGGFRGIQITSGFFQIWRASGITSELQLYCTAIGALIFASLMLFAGWFHYHKAAPKLAWFQDVESMLNHHLAGLLGLGSLSWAGHQIHVSLPINQFLDAGVDPKEIPLPHEFILNRDLLAQLYPSFAEGATPFFTLNWSKYAEFLSFRGGLDPITGGLWLSDIAHHHLAIAILFLIAGHMYRTNWGIGHGLKDILEAHKGPFTGQGHKGLYEILTTSWHAQLSLNLAMLGSTTIVVAHHMYSMPPYPYLATDYGTQLSLFTHHMWIGGFLIVGAAAHAAIFMVRDYDPTTRYNDLLDRVLRHRDAIISHLNWVCIFLGFHSFGLYIHNDTMSALGRPQDMFSDTAIQLQPIFAQWVQNLHAGAPSVTAPGATTSTSLTWGGGELVAVGGKVALLPIPLGTADFLVHHIHAFTIHVTVLILLKGVLFARSSRLIPDKANLGFRFPCDGPGRGGTCQVSAWDHVFLGLFWMYNSISVVIFHFSWKMQSDVWGTISDQGVVTHITGGNFAQSSITINGWLRDFLWAQASQVIQSYGSSLSAYGLFFLGAHFVWAFSLMFLFSGRGYWQELIESIVWAHNKLKVAPATQPRALSIIQGRAVGVTHYLLGGIATTWAFFLARIIAVG
The following text describes a protein:
Function:
Component of the 40S subunit of the ribosome. Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome in the nucleolus, many ribosome biogenesis factors, an RNA chaperone and ribosomal proteins associate with the nascent pre-rRNA and work in concert to generate RNA folding, modifications, rearrangements and cleavage as well as targeted degradation of pre-ribosomal RNA by the RNA exosome.
Subcellular Localization:
Cytoplasm.
Sequence:
MNDRRREGAIHSVRGVVQAVRWRVRHLGGQPGGVLERRGVRHRGGQPGRGPRTAAGGNQPSGRGPGAAEKEESGIGAGRPGGVLVRRGGELGIGAGSRGGRGGVRHRGGQAGRGPRAAEGESQASGRAGRAGSWRGGARGARSFGRRHQREREEEQRRRRRRLRGPSAPLSVLPPGLPALRRSPDKMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKSYTTPKKNKHKRKKVKLAVLKYYKVDENGKISRLRRECPSDECGAGVFMASHFDRHYCGKCCLTYCFNKPEDK
The following text describes a protein:
Function:
Can function as a Delta(5) fatty acid desaturase and behaves as a (8-3) desaturase. Introduces a double bond in the fatty acid chain 5 carbons away from carboxy terminal to biosynthesize polyunsaturated fatty acids (PUFAs) endogenously (PUFAs are essential for membrane structure and many cellular and physiological processes). Acts on a variety of substrates such as dihomo-gamma-linoleoyl-CoA ((8Z,11Z,14Z)-eicosatrienoyl-CoA, 20:3n-6) to generate arachidonoyl-CoA ((5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA, 20:4n-6). Also acts on a number of other substrates, including fatty acids that do not contain a double bond at the 8 position like (11Z,14Z,17Z)-eicosatrienoyl-CoA (20:3n-3) to produce (5Z,11Z,14Z,17Z)-eicosatetraenoyl-CoA (20:4n-3). Unlike plants, Caenorhabditis elegans desaturases seem to use fatty acyl-CoAs as substrates (By similarity).
Miscellaneous:
MISCELLANEOUS: HPO-19 and T05H4.4 are cytochrome b5 reductases required for PUFA desaturation in Caenorhabditis elegans. HPO-19 knockdown or mutation alters FAT-4 desaturase activity.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MVLREQEHEPFFIKIDGKWCQIDDAVLRSHPGGSAITTYKNMDATTVFHTFHTGSKEAYQWLTELKKECPTQEPEIPDIKDDPIKGIDDVNMGTFNISEKRSAQINKSFTDLRMRVRAEGLMDGSPLFYIRKILETIFTILFAFYLQYHTYYLPSAILMGVAWQQLGWLIHEFAHHQLFKNRYYNDLASYFVGNFLQGFSSGGWKEQHNVHHAATNVVGRDGDLDLVPFYATVAEHLNNYSQDSWVMTLFRWQHVHWTFMLPFLRLSWLLQSIIFVSQMPTHYYDYYRNTAIYEQVGLSLHWAWSLGQLYFLPDWSTRIMFFLVSHLVGGFLLSHVVTFNHYSVEKFALSSNIMSNYACLQIMTTRNMRPGRFIDWLWGGLNYQIEHHLFPTMPRHNLNTVMPLVKEFAAANGLPYMVDDYFTGFWLEIEQFRNIANVAAKLTKKIA
The following text describes a protein:
Function:
Nucleolar component of the spliceosomal ribonucleoprotein complexes.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MAGLTLFVSRLPPSARSEQLEELFSQVGPVKQCFVVTEKGSKACRGFGYVTFSMLEDVQRALKEVTTFEGCKINVTVAKKKLRNKSKEKGKNENSESLKKEPKPKKTKVADKKARLIIRNLSFKCSEDDLKTIFAQFGAVLEVNIPRKPDGKMRGFAFVQFKNLLEAGKALKSMNMKEIKGRTVAVDWAVAKDKYKNTQSASAPGEEKRPEPKDQKLGKENVREEENVGEEAEEEGEDEDDMEEEEEEEEEEDEEDEEEEEENKESKVMKAVQIQKRAVKRAAPAEGSEEEHSDEDGDLEDGESIDSGEEQAQSDTNTEEQEDEDVQVSKKKKRKLPPDVNEGKTVFIRNLSFDSEEEELGELLQQFGDLKYVCIVLHPDTEHSKGCAFAQFMTQEAAQKCLEAASPETEGGGLKLDGRQLKVDLAVTRDEAAKLQTKKVKKPTGTRNLYLAREGLIRAGTKAAEGVSAADMAKRERFELLKHQKLKDQNIFVSQTRLCLHNLPKAVDDKQLRKLLLNATRGERGVRIKECRVMRDLKGVHGKIKGQSLGYAFAEFQEHEHALVALRHINNNPEIFGPQKRPIVEFSLEDRRKLKIKELRIQRSLQKMKSKSMTGEPQQNQPELGKDQQRNAGQNHTQEPSQAPLQQKGKAGSISWTGFQTKAEVEQVELPDGKKRRKVLVLPSHRGPKIRLRDKGKVKSLPPKKPKPQINQWKQEKQKLSSKQSFYFKVKEALASHPTQEVCVPGKSDPCCTILQSSISEIP
The following text describes a protein:
Function:
Essential for the fidelity of chromosome transmission. Required for the DNA replication block checkpoint. Component of the RFC-like complex CTF18-RFC which is required for efficient establishment of chromosome cohesion during S-phase and may load or unload POL30/PCNA. During a clamp loading circle, the RFC:clamp complex binds to DNA and the recognition of the double-stranded/single-stranded junction stimulates ATP hydrolysis by RFC. The complex presumably provides bipartite ATP sites in which one subunit supplies a catalytic site for hydrolysis of ATP bound to the neighboring subunit. Dissociation of RFC from the clamp leaves the clamp encircling DNA.
Subcellular Localization:
Nucleus. Note=Associates with chromatin.
Sequence:
MPSVDIDASQWQKLTQSREKQTTVITPLGMMMLEIQGELELPKDFASLARRDSPNEGRFSEQDGETLIRFGSLQIDGERATLFVGKKQRLLGKVTKLDVPMGIMHFNSKDNKVELVDVMKYKVIFKDRPLPIM
The following text describes a protein:
Function:
Toxic component of an atypical, type II toxin-antitoxin chaperone (TAC) system. Upon expression in M.smegmatis inhibits colony formation and cell growth. Ectopic expression in wild-type M.tuberculosis has no effect on cell growth; ectopic expression in a triple higB1-higA1-Rv1957 (delta TAC) disruption mutant causes growth arrest, killing a considerable proportion of the cells. Increased ectopic expression leads to decreased levels of IdeR- and Zur-regulated genes as well as cleavage within the mRNA region of tmRNA (transfer-mRNA), strongly suggesting it is an endoribonuclease; also degrades E.coli and M-smegmatis tmRNA. Its toxic effect is neutralized by coexpression with antitoxin HigA. Neutralization of HigB1 toxin in E.coli or M.marinum also requires SecB-like chaperone Rv1957, making this the first toxin-antitoxin chaperone (TAC) system.
Sequence:
MPPPDPAAMGTWKFFRASVDGRPVFKKEFDKLPDQARAALIVLMQRYLVGDLAAGSIKPIRGDILELRWHEANNHFRVLFFRWGQHPVALTAFYKNQQKTPKTKIETALDRQKIWKRAFGDTPPI
The following text describes a protein:
Function:
ATP dependent phosphorylation of adenosine and other related nucleoside analogs to monophosphate derivatives.
Subcellular Localization:
Nucleus.
Sequence:
MSRRVFGLSIKSFRLFRRTPIHPPAFQHFSGGVFRTSFRSFCDCQEHRRMDLPEGILMGFGNPLLDITCTVEDNVILEKYGLEANAAIIADEKHDALFDELMNMENVIYSAGGACQNSMRIFQWIVQTPFRAVFIGSVGKDKLGDRIEKRAKSDGLLTLYQLKEELPTGSCAVIINGPNRSLVANLGAASLFSDDWIDEDDNICALDRAEYFYFTGFFLAVCPPAVERVARMCCETNRIMILNFSAVFVLQMQKEALGNILQYVDIIICNKEEAIAFSDTNDWKTKNIFEIGSRLQQMPKENTRPRLVMITDAVCPVLVFQDNDRVLEYPVPPVKQGEIFDTNGCGDAFVGGFLAMYVQRMPLDYCIRTGIFASQQVLHVVGVQIDKLPKFSEKCI
The following text describes a protein:
Function:
Probable transcription factor involved in plant development.
Subcellular Localization:
Nucleus.
Sequence:
MNYPYEDFLDLFFSTHTDPLATAASTSSNGYSLNDLDIDWDCDFRDVIESIMGDEGAMMEPESEAVPMLHDQEGLCNSASTGLSVADGVSFGEPKTDESKGLRLVHLLVAAADASTGANKSRELTRVILARLKDLVSPGDRTNMERLAAHFTNGLSKLLERDSVLCPQQHRDDVYDQADVISAFELLQNMSPYVNFGYLTATQAILEAVKYERRIHIVDYDINEGVQWASLMQALVSRNTGPSAQHLRITALSRATNGKKSVAAVQETGRRLTAFADSIGQPFSYQHCKLDTNAFSTSSLKLVRGEAVVINCMLHLPRFSHQTPSSVISFLSEAKTLNPKLVTLVHEEVGLMGNQGFLYRFMDLLHQFSAIFDSLEAGLSIANPARGFVERVFIGPWVANWLTRITANDAEVESFASWPQWLETNGFKPLEVSFTNRCQAKLLLSLFNDGFRVEELGQNGLVLGWKSRRLVSASFWASCQTNQ
The following text describes a protein:
Function:
A small protein (arrest peptide) encoded upstream of inducible ornithine carboxylase gene (speF) that controls expression of downstream genes (speF and patE) by nascent chain-translational arrest and transcriptional attenuation. In the presence of ornithine a toeprint due to ribosomal arrest can be seen on the speFL transcript. Only L-ornithine (not other tested amino acids) has this effect. It is thought that in the presence of ornithine, ribosomal stalling on speFL prevents binding of Rho transcription termination factor to a downstream rut site allowing transcription of the operon. In the absence of ornithine, ribosomes terminate translation and are recycled, exposing the rut site allowing Rho to bind and prematurely terminate transcription. The presence of a pair of rare Arg codons could slow down translation to prevent polysome accumulation and to expose the rut site to Rho (Probable).
Miscellaneous:
MISCELLANEOUS: Changing the amino acid sequence by 2 frameshifts with minimal nucleotide changes indicates the peptide sequence, but not mRNA structure is important.
Domain:
An N-terminal sensor domain binds ornithine already present in the ribosomal exit tunnel; upon ornithine binding the downstream effector domain compacts in the exit tunnel, causing a shift of 23S rRNA U2585 which blocks the action of peptide chain release factor 1 (prfA), causing ribosome stalling.
Sequence:
MENNSRTMPHIRRTTHIMKFAHRNSFDFHFFNAR
The following text describes a protein:
Function:
Putative gamma-glutamylcyclotransferase.
Sequence:
MRKNEMGDKTNLIFSYGTLKRGFPNHTLIEDLIRTGDASFIGVYKTLSPYPLVCGPYRVPFLLNFPDKGKQVYGELYAVTPLGLAKIDDLEGLSKGHYERLPLRVVKEDEDENIKEVEAYYGHRNYAEEMWKRNGMIGQEVYSKTVAEGYVKRIDRPRDTTFLDQIRSFLSSTTSL
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MDQETQTQTPPPRLQRENVGVFQEEEEELSLKQEPETPEESEPSEAEESSDEGSERQGSSQNRLWVQRGGRSGLQWSHAHEETLDSDQQLSSEEEPDLVVIKEEEDDFFVDQAEEQVRLKQEFGTFTVTRPNEENDHSGPEPSRARLLFGSSSLAERKGEGGRKDSVPNRVTVGDPSRKQNSQTGKQVNKAPGSSAGPAPTTQSFKHYDACGKSFLCDKCGKGFRQQGHLNSHIRIHTGEKPYLCKTCGKSFSQSSVFRNHIMIHTGEKPFSCKICGKLLRYSSSLTGHMKIHTGEKPYVCKVCGKRFCHSSGLVSHTRSHTGEKSYSCQVCGKCFSHNSTLLRHTRTHTGERPFPCQTCGKRFNNNSHLTIHMRTHTGEKLFSCDACGKSFSHGSTLQRHARMHTGEMPSSCKVCGKLFRYSSSLARHMKIHAGDKP
The following text describes a protein:
Function:
Component of the ESCRT-II complex (endosomal sorting complex required for transport II), which is required for multivesicular body (MVB) formation and sorting of endosomal cargo proteins into MVBs.
Subcellular Localization:
Cytoplasm. Endosome.
Sequence:
MNRLRPIDTTNLTINAQLFFNETIIESQVGIGIYDGKNKDDRYQDGTLYLTSHRLIYVDRTNPHRHSCFLDISLIRQTEYWIGFLKSSPKITLLLGTRRSSFNQTSQDSPSADDQRKLTSDQNDIINHPAASHWTCHVCGFSNPPELKCGLCGIPRDLSSTTKSASNSRPPSSLRDLSSLSTSFQHTPSHTRSLSNLRGISTQAEPIETLSSPSHELERIQQVKNKEIPCPSCTFLNHPSMARCEMCDSILGTVQLDRLSLNNSSESTLADSDLQHSRATTPAPPSSFPADSYIRLSFRKGGDKTFYFSLKKALQSKSWNTNGLKSDFESAKPSARLEQEGSTQGQHENPSYVSKPIGIDRILKTMDSQQQAHQTELTEGLQDLQALMAKAKEMVQLSQSINAKLTSLESVPKTGEETETPDQKAGLIRSSLVKLGLPTPAVTPDMISNDQAYAKELAKELAGLLTRTMAGQSAIMFHGFHDLAVGIRPLDEIWCIWNRARGISLVSPADMISACHHLPEYTVPEIRLRTFKSGLRVLHTPYFSVHEFEHRLLRRLRNTREEGAEEEDGHVDTTSDLIDPLDGTKLMKMSTLEIAQSERLNLNLTNELIESIEQTPSHPSEYHHHHPLSFDKCSLVRDFDPQTGLTFWFENQISDYHWEESNSS
The following text describes a protein:
Function:
Hydrolyzes glycerol-phospholipids at the terminal phosphodiesteric bond.
Sequence:
MVPRLLHGTLHATIYEIDKIRTGCADCCGPTSPQKLTKRVLNNVKKLFFCAPKISATKLYATIDLDKARVGRTRIAENEPSNPHWNDTFRLYCAHEVSNIIFTVKDENPVSATLIGRAYLPVEEVLNRYIVDRWVPIVDEERHPISGHSKIHVRLQFYSVKQDSNWSRGITSLAFGGLPYTFFKERQGCQVTLYPDADISDDDITNYLKSQGLFEPQRCWEDIFDAISNAKHMIYIAGWSVYTKITLIRNPRRPKVGGELTLGELLKKKASEGVNVLLLVWDDITSDEVLKRDGLMSTHDQETADYFKNTDVHCCLCPRNADSGKTVIQGFQVGTMFTHHQKTIVVDTEIPGGMSHKRMIVSFLGGIDLCDGRYDTRDHSLFRTLDTVHKQDFYQPAFPGSSIAKGGPREPWHDIHCRLEGPVAWDVLYNFEQRWRKQIGNRFIYSINELDKFIIRPTEVTASRDRETWNVQIFRSIDGGAVTDFPVKPDEASEVGLVTGKNNVIDQSIHDAYISAIRRAKNFIYIENQYFIGSCYGWKPTTDIKLEDIGALHLIPKEISLKIVSKIQAGERFTVYVVLPMWPEGIPESDSVQAILDWQKRTMEMMYTDICNALKAKGNTNADPREYLTFFCLGNREVEKPGEYKPPQKPVPDTNYARAQEFRRFMIYVHSKMMIVDDEYIIIGSANINQRSMDGARDSEIAMGGYQPYHLASNQPPRGKIYGFRMSLWCEHLNYADDSFADPSSLECVRKVNGMADESWKLYSNDTFDIDLPGHLLRYPIDINSNTGQITTLPGFKFFPDTKAAILGNKSQFLPPILTT
The following text describes a protein:
Function:
Host defense peptide that exhibits antimicrobial and antifungal activity (By similarity). Exhibits antimicrobial activity against E.coli, S.aureus and C.albicans (in vitro) (By similarity). Has high lipopolysaccharide (LPS)-binding affinity, and may thereby be involved in immunoregulation through LPS neutralization (By similarity).
Subcellular Localization:
Secreted.
Sequence:
MNLCLSSLLFFLVILLPSGKGMFGNDGVKVRTCTSQKAVCFFGCPPGYRWIAFCHNILSCCKNMTRFQPLQAKDPWVH
The following text describes a protein:
Function:
Hydrolyzes the N-acetamido groups of N-acetyl-D-glucosamine residues in chitin.
Subcellular Localization:
Secreted.
Sequence:
MARYARVATLAACLLFACALADGHRWRRQADETAKKDESLEQELCKDKDAGEWFRLVAGEGDNCRDVIQCTASGIQAIRCPAGLFFDIEKQTCDWKDAVKNCKLKNKERKIKPLLYTEEPLCQDGFLACGDSTCIERGLFCNGEKDCGDGSDENSCDIDNDPNRAPPCDSSQCVLPDCFCSEDGTVIPGDLPARDVPQMITITFDDAINNNNIELYKEIFNGKRKNPNGCDIKATYFVSHKYTNYSAVQETHRKGHEIAVHSITHNDDERFWSNATVDDWGKEMAGMRVIIEKFSNITDNSVVGVRAPYLRVGGNNQFTMMEEQAFLYDSTITAPLSNPRLCPYTMYFRMPHRCHGNLQSCPTRSHAVWEMVMNELDRREDPSNDEYLPGCAMVDSCSNILTGDQFYNFLNHNFDRHYEQNRAPLGLYFHAAWLKNNPEFLEAFLYWIDEILQSHNDVYFVTMTQVIQWVQNPRTVTEAKNFEPWREKCSVEGNPACWVPHSCKLTSKEVPGETINLQTCLRCPVNYPWLNDPTGDGHY
The following text describes a protein:
Function:
Required for the insertion and/or proper folding and/or complex formation of integral membrane proteins into the membrane. Involved in integration of membrane proteins that insert both dependently and independently of the Sec translocase complex, as well as at least some lipoproteins. Aids folding of multispanning membrane proteins (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDTIASLFSFITWPVSWVIVQFHTVYGAIFGPDTGWAWGLSIVSLVILIRICLIPLFVKQIKATRGMQTLQPEMKKIQERYKNDKQRQSEEMMKLYKETGTNPLSSCLPILAQSPFFFALYHVLNGIASGDTIGKINQPLLESAQKAHIFGAPLAAKFTDGASKVESLGASLTDVRVITAVMIVLMSASQFFTQRQLMTKNVDTSVKTPFMQQQKMLMYVFPVMFAVFGINFPVGVLVYWLTTNVWTMGQQMYVIRNNPTPGSKAQASYLERLHKSVTEHGRTRRRGEKAIVKAIVAKGRDRNEAERKFINGLNKAGLAAQADGNVVKNDAAVAVQSEDGSTVTTTAQPKRQQPKRQSKSQRQAKPAGETEPKTSLTKSDEPQDAEPAGKQDAKPAAGAKKPAQKSGGGGRSKAQSGQRKGPQRPKSPSKK
The following text describes a protein:
Function:
Pleiotropic regulator of mitotic progression, participating in the control of spindle dynamics and chromosome separation. Phosphorylates different histones, myelin basic protein, beta-casein, and BICD2. Phosphorylates histone H3 on serine and threonine residues and beta-casein on serine residues. Important for G1/S transition and S phase progression. Phosphorylates NEK6 and NEK7 and stimulates their activity by releasing the autoinhibitory functions of Tyr-108 and Tyr-97 respectively.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSVLGEYERHCDSINSDFGSESGGCGDSSPGPSASQGPRAGGGAAEQEELHYIPIRVLGRGAFGEATLYRRTEDDSLVVWKEVDLTRLSEKERRDALNEIVILALLQHDNIIAYYNHFMDNTTLLIELEYCNGGNLYDKILRQKDKLFEEEMVVWYLFQIVSAVSCIHKAGILHRDIKTLNIFLTKANLIKLGDYGLAKKLNSEYSMAETLVGTPYYMSPELCQGVKYNFKSDIWAVGCVIFELLTLKRTFDATNPLNLCVKIVQGIRAMEVDSSQYSLELIQMVHSCLDQDPEQRPTADELLDRPLLRKRRREMEEKVTLLNAPTKRPRSSTVTEAPIAVVTSRTSEVYVWGGGKSTPQKLDVIKSGCSARQVCAGNTHFAVVTVEKELYTWVNMQGGTKLHGQLGHGDKASYRQPKHVEKLQGKAIHQVSCGDDFTVCVTDEGQLYAFGSDYYGCMGVDKVAGPEVLEPMQLNFFLSSPVEQVSCGDNHVVVLTRNKEVYSWGCGEYGRLGLDSEEDYYTPQKVDVPKALIIVAVQCGCDGTFLLTQSGKVLACGLNEFNKLGLNQCMSGIINHEAYHEVPYTTSFTLAKQLSFYKIRTIAPGKTHTAAIDERGRLLTFGCNKCGQLGVGNYKKRLGINLLGGPLGGKQVIRVSCGDEFTIAATDDNHIFAWGNGGNGRLAMTPTERPHGSDICTSWPRPIFGSLHHVPDLSCRGWHTILIVEKVLNSKTIRSNSSGLSIGTVFQSSSPGGGGGGGGGEEEDSQQESETPDPSGGFRGTMEADRGMEGLISPTEAMGNSNGASSSCPGWLRKELENAEFIPMPDSPSPLSAAFSESEKDTLPYEELQGLKVASEAPLEHKPQVEASSPRLNPAVTCAGKGTPLTPPVCACSSLQVEVERLQGLVLKCLAEQQKLQQENLQIFTQLQKLNKKLEGGQQVGMHSKGTQTAKEEMEMDPKPDLDSDSWCLLGTDSCRPSL
The following text describes a protein:
Function:
Promotes chromosome condensation and nuclear envelope dynamics during mitosis. Activity appears at metaphase-anaphase transition.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
Sequence:
MEKYKILECIGHGSFGRIYKVQRLKDGALLAQKEIHFGNITRQEKQYIADEVNILRNLKHPNIVQYCGEELNRSAQVINLYMEYCGHGDLANLIQRYKEEKKRFTEQEVLKFFTQLLLALYRCHYGENAPACDSQWPREIFHPKQSVLHRDIKPANIFLDENNSVKLGDFGLSKLLDNTRVFTQSYVGTPYYMSPEIIRSSPYSAKSDVWALGCVIFEICMLTHPFEGRSYLELQRNICQGNLSCWDHHYSDDVFLLIRHCLEVNSDLRPTTYQLLRSPILSDIRSKLESERVVLEQSDLLHKKHQMLIQLENDLQFREQRLSARESELENVIASRLAQREEILRRELEKQLRDMDARYQRHMQTVVNSMQKMRVTSPVDHNEQPESSTAEMFVDCTIEASQSPLLHIPKLGISKPLQTLSCPGFTLTTQQPILKRPTLRKELSSRALHTTATLMKYRANASSLRTTPIDKDGQITSLQQKNGTSNQVADCMNKLLHTSLDGKKLSPSELCNKFSDGEGLPNRKVSKLSVESDETAVSASSGESVPTDSTLTDTKSKSVFVHPPSPQSLYVEKLEKLNIRSDEVSKPSKASKTLHGYALPSLASPYDVHAEEKIARENEMDGNFKTMKINQHPDEYVLRTPKKIQLLEGQKRSPVKQLGRLGYNKLRRSAMDNAGLELRKAASTSNYTSLQSRTLPGSWRDDEEEIPRPFLRKMLDARMMRA
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MAVASIWRRAWKRLRSRGSSEDDADGRGGRLRPTGGEGDADGGGGWQRPTGGYISSFGTTNTASTITPFNSHGEAQPRDIHASMAPSTAPMEENAEEELDIDVDQELEEDRVEKLEHLKGLAVQFRGDNRSALERWLLELDVPWVIHLAPGTHESSGSVVATHGFQFLVQSWILALHKIRGSILTSLDGWSRQRQDQDEGRTSKQPSASEFAQLVQAIVLKMLPFVDIAVAKTTHWPGVVAQKLQVLIDMHDALSMASQHVLSLLSCYVQEECSNDKMRELLSADLTKLDEAIWDTAVEMRNNIMAWSWTDDSSSCDIHKVSHSIVSYTKVLWANCKSVNRILHAAVLRGEFVSENKNLNHVTNLITQMVSSLEREPSTNSSPGSFPDESLRFLFLINNFKEGLSLYFDQWTHALQTS