lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Bifunctional inositol kinase that acts in concert with the IP6K kinases to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respectively called InsP7 and InsP8, may regulate a variety of cellular processes, including apoptosis, vesicle trafficking, cytoskeletal dynamics, and exocytosis. Phosphorylates inositol hexakisphosphate (InsP6).
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MDQDQEIKMKIRSHSVEREKTESQSQFTDEIEDDKIVIIGVCCMAKKSQSKEMQEILNRINPEFFKIEIFSEQMILEDPIESWPIVETLISFYSDGFPLNKAIAYVDLRKPFIINDLKKQQLLWDRERVYTLLKKNKVPVPKHYFVFKNPNKYIIDDYNRKEIEKKCKPRKNDQEIIEEEDNVDSVISFLQNEDSSQHLKSVQTAKQLSELLLPPRQDTMEDKNKNKMKQGMRSYDARSLSAVIDIKKDNKDLQITKIEECDDYLLINGQKLVKPFVEKPFDAEDHNIYIYYNSRDGGGCKKLFRKVGNQSSIFDPAQNSIRNDNENYIYEVFLPTNGFDIKVYTVGEFYAHAEARKSPVLDGKVVRSQNGKEMRYPVCLTMEEKMMAIKIVNIFGQNICGFDLLRSNNKSYVCDVNGWSFVKGNAKYYQDCATILQNMILAKLRPTLLQKQISDINLVKGFYKNSFRPSSKDIDSKEQNSELRSVVAVFRHGDRTPKQKMKMRTSNVLFLSFFDEVVDPSKEIKLKHPKQLLKLLNLTRECIAKTSCRDNIIKLLQMKSVLELGGHFEGINRKVQIKPLKTQKIDKNGSIVDFPVEVLLILKWGGELTQLGEEHAARLGKIFRHDMYPTEKDGLLRLHSTYRHDLKTFSSDEGRCQYTAAAFLKGLLGYEGEVTPILATMVQKNEVAQDLLDCNNLEIEEEAEIKNILQKMLTSDEDMLTQIYQHFPDCIMTSTQHDLISKFKSPKSMLIQLHTYIKQLTKNIRQIQNKIIRHHIHLDKNYYITPSDMEQGAQTMFESENLTLFFKRWYKLEYDFLQKDKFNISKIPDIYDSVKYDMLHNQDKLQFYENSKEFYCLAELLSHFMVPFEYGITTKQKLSIAKRVVGPLCNKIKQDLLWWNKPESKNQQQEEDYWKFRQTDESDLNSPWRHVRTRLYFTSASHLYSLFNILYYGLGHYLIEDEFKQKQLQQILMLQYLSNIVIKLYEDLSSEKGDPNRFRIELSVSDGIQMSFPIDKNMPSKSDNIHINQSLRLDQLEDFLNQIIDCAFGDDVQSQ
The following text describes a protein:
Function:
Metalloprotease.
Sequence:
MLSSKLFCVLFFCLGLSNGWPQFDFMNQMGFGGGFNNGPHPNSRPGSRPNSPLGDIFGNINGMVKGITDQIGKIAQGLDVNNDLGKMAHGPPPPQSEWVEHARRFCRRFPGHPKCRGQLPQFNDIGSMLNGILVDSGKWLPKVPFINIRDPLSGINSDLKNALNGIQVQFGQISQQFANNIRNICQQMNCKQQQQKNVQMKQAILKQTVDFEKKVFGNNVADKMNLRFDRTLQLKQALLEKAQLKGVVAPEDNGVFDKDLLLTETQANFMLNELGKGGEGAIPMPGSAKAKRASIFFEQNLIQKWPSTSPIPYTFDSSLDNLDQNDVRGAISEIEQKTCIRFKYFASPPKGNHINYQKVNSPSFCGLSYIGRVEPANPVYLSFQCGNGRGIAVHETMHALGVNHQHLRMDRDKHIKVDWSNINPQQYDAFVVADSKLYTTYGVKYAYDSIMHYNAYTGAVNIAKPTMIPLVNQQANIGLLGQRAKMSNADVEILNKMYCKSAGCDDKNVYCGAWALQDLCNNPNHNVWMRSNCRKSCNFC
The following text describes a protein:
Function:
Possesses antifungal activity and is active against a relatively broad spectrum of filamentous fungi. It inhibits spore germination at high concentrations and at low concentrations delays growth of hyphae which subsequently exhibit abnormal morphology. Spz C-106 in the hemolymph controls expression of the antifungal peptide by acting as a ligand of Tl and inducing an intracellular signaling pathway. Part of a psh-dependent Toll pathway, which may function in activating the systematic immune response in response to localized melanization of the tracheal system.
Subcellular Localization:
Secreted.
Sequence:
MMQIKYLFALFAVLMLVVLGANEADADCLSGRYKGPCAVWDNETCRRVCKEEGRSSGHCSPSLKCWCEGC
The following text describes a protein:
Function:
Probable methyltransferase.
Sequence:
MLKPSLNAAAKWMIRNTIVSNESLTPEINLHLITIASPLWMSTPDACPLPDPYWAFYWPGGQGLSRFILDNKPLFQGSEIVDFGAGCGSASISASICGAKKILANDIDRYALLSTKLNFHLNNLRDSKIQYSSINFLDDKNERMSTQFFTDSKNIRKFILLGDMFYDSDFAELLFSWLKKIQDAHMVRVLVGDPDRHPLAESEYLQRYKTKFTKNQLAEFSLPGYVIKEHYGFNTAKVFELKFQ
The following text describes a protein:
Function:
Plays a role as a marker and a regulator of neuronal differentiation; Up-regulated by a variety of neurogenic signals, such as retinoic acid, epidermal growth factor/EGF and NGFB/nerve growth factor. Induces apoptosis, growth arrest and the expression of cyclin-dependent kinase inhibitor CDKN1B. Plays a role as a tumor repressor and inhibits cell growth and tumorigenicity of medulloblastoma (MDB). Acts as a probable substrate-specific adapter for a BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex towards HDAC1. Functions as antagonist of the Hedgehog pathway on cell proliferation and differentiation by affecting the nuclear transfer of transcription factor GLI1, thus maintaining cerebellar granule cells in undifferentiated state, this effect probably occurs via HDAC1 down-regulation, keeping GLI1 acetylated and inactive. When knock-down, Hedgehog antagonism is impaired and proliferation of granule cells is sustained. Activates the caspase cascade.
Sequence:
MLGAMFRAGTPMPPNLNSQGGGHYFIDRDGKAFRHILNFLRLGRLDLPRGYGETALLRAEADFYQIRPLLDALRELEASQGTPAPTAALLHADVDVSPRLVHFSARRGPHHYELSSVQVDTFRANLFCTDSECLGALRARFGVASGDRAEGSPHFHLEWAPRPVELPEVEYGRLGLQPLWTGGPGERREVVGTPSFLEEVLRVALEHGFRLDSVFPDPEDLLNSRSLRFVRH
The following text describes a protein:
Function:
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Subcellular Localization:
Nucleus. Note=Localizes to the nucleus of germ cells.
Sequence:
MCLVNEFVSNSNMKPALNVSGDEKELILQLRRYLEEKLTYLLDQNGTVSIGVSGGSMPRVFSKAILSLPQEQLNWKRIRIFMVDERNVDLDSEESNQGEYLRLFPNELRDVFVPMQIFKDPCLTAQHYEISLRKYLLPEQLNNTARFDILFLGVGPDGHTASIFPGKERLEKITELNWVSVITDSPKPPPSRITLTLQTLQHAKNVAFIICGKQKAEIVRGICDRDQKYPAAQARPFNDKLTLFLDEDAATGVPDRDSSDSDSPPPFDG
The following text describes a protein:
Function:
Essential cell division protein that coordinates cell division and chromosome segregation. The N-terminus is involved in assembly of the cell-division machinery. The C-terminus functions as a DNA motor that moves dsDNA in an ATP-dependent manner towards the dif recombination site, which is located within the replication terminus region. Required for activation of the Xer recombinase, allowing activation of chromosome unlinking by recombination (By similarity).
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Note=Located at the septum.
Domain:
Consists of an N-terminal domain, which is sufficient for the localization to the septal ring and is required for cell division, followed by a linker domain, and a C-terminal domain, which forms the translocation motor involved in chromosome segregation. The C-terminal domain can be further subdivided into alpha, beta and gamma subdomains. The alpha and beta subdomains form the DNA pump, and the gamma subdomain is a regulatory subdomain (By similarity).
Sequence:
MESKPKEFKPTWNLQNGKMILPYVLLFAGIILTLSLGSFDAGERGVEYNFFGRLGYYISYGMFFMFGAASFLPGLFTIGLGSLRLVKEEFELTNRLFSIPVFLLCYTVTLQVTGHVSTIPFASQGGFVGQLLSSGLEFVFGSTGKILIHLVFYFYGLILLLNESPLHFIGRILGTAGAKYKEGFKSGFGKRGESLGSLFQSAVEKFQKKESVPPWISTNTNEKNSLNQSYSLSNPHTHSYERNLGNKQPSELQNTLHSTFGKEGKLSDFLSKVDTGPTVTSKNSRIRFQNHGAFSGNFEEQGKVFRFESVSSSLSEKIREEKNFQKTPSRWEILDFRTSSFSNIISEKEPSVTLVVPSESEIKKEWNQTNPILQSEEIPDKFLFEEKEKVEQTDSGLENECYEEESVDSEENLSEEETLSSETSTEKDISENFKTSTISNSKEVSPNHTSNSSIHSLEKSEEKLELGLPFPPTTLVPEVKSKRSIYHVPLKSLKTTTTKIQDPLFKIEADKVARKIEEIIRQYGYESQVVSMERGPIITRYELTPPLGVKLGRITSLSDELRLYLAVKNIRIVAPIPGKSTIGIEVPNSIREDVFLGDILHQNLSLRPKKDLSILIGKDISGKLVGIDLNKLPHLLVAGTTGSGKSVCLNSMISSLVVHLSPEEVRFIMIDPKMVELTLYEDIPHLLMPVITDPKKATRALAWAIQEMEARYHSVSKLKCRDFKTYNEKVEQGAHRDGYKKMPYIVIFIDELADLMMVSGKDLEDAITRITQKSRAVGIHLIMATQRPSVDVITGLIKANCPARMAFHVAQKTDSKIILDQNGAESLLGKGDFLYKSPTAADLIRIQSPYVSEEEIEKIVEEARKFGKPSYVDFNLDEETESSVVDEGDEELFEQAWEIVRTDRKASASYLQRRMRIGYNKAARLMELMEERGYVSPQIGSKGREILK
The following text describes a protein:
Function:
Required for cytoplasmic pre-assembly of axonemal dyneins, thereby playing a central role in motility in cilia and flagella. Involved in pre-assembly of dynein arm complexes in the cytoplasm before intraflagellar transport loads them for the ciliary compartment.
Subcellular Localization:
Cytoplasm. Dynein axonemal particle.
Sequence:
MAADKKSDLKLTKDESDRFKKAFENEEFRKMFFDYAKEISDPENRKKYEEEIAMMEMERGVDVKFLHPKPGFVVKTAYKDTKKKVLINIAWSDAVAKATATSKKVSPDGSKRPGQQWSIPYSLAPIREDLDKAHNSCDVCDAVFHQEIYEKSQNDQRLKQLLIDTALDGIEREFKKKLDRKNLKFPKLAYKGVPSPTVIRNKSKEACIAILTNEYASFSYLNRHRTPPDDQDSPIKFPNPYKAVDELKERQEQRKHQAKDNSKSKQDPTAPKYTIVQRSNFDLKDYRDSRDSAPSTRPNELSVSIELPLLDSATGLDLDVFETYITLQHKDPNYNLSAALPYPVDTDNGSAKFDTLKKCLIVTLPVLPSKETNNPVTYIAKTLALSSVALQIQDSSESKPIKNEVNSPQYTYSQTDDEVVFVIHVQDIDSSTMKSKFLERQFSLEFSATEATNTTEREIKHFSLYTEFIDGCFNINSCNIDIKPYNLVVKLIKDSSYKYQWSKFMAGISPCELEEKFFITPENIEMLSQENENDNWANGSDYKVAAEVAEKTSEQLVVNIDVEKVKSSMTDSYEKDVTKSSVDHNGDQKSYKNEQEISNANKSEEKITLATSENLITSSSAVKATPKDDSISSIDDLKSIETSVDIRNNDATKTSPDTKVLISPVEDIPSLTSADDNEIVNKVLDNDDNSQNQQAKTNLDLSQAKTSIRITKDLSSKFKNNLIFELDD
The following text describes a protein:
Function:
Catalyzes the aldol condensation of dihydroxyacetone phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and the reverse reaction in glycolysis.
Sequence:
MLVNIKQMLQHAKQHHYAVPHININNYEWAKAVLTAAQQAKSPIIVSTSEGALKYISGHQVVVPMVKGLVDALKITVPVALHLDHGSYEGCKAALQAGFSSIMFDGSHLPFQENFTKSKELIELAKQTNASVELEVGTLGGEEDGIVGQGELANIEECKQIATLKPDALAAGIGNIHGLYPDNWKGLNYELIEAIAKATNLPLVLHGGSGIPEADVKKAIGLGISKLNINTECQLAFAKAIREYVEAKKDLDTHNKGYDPRKLLKSPTQAIVDCCLEKMQLCGSTNKA
The following text describes a protein:
Function:
Single-stranded DNA-dependent ATP-dependent helicase.
Subcellular Localization:
Nucleus.
Sequence:
MNQGAPGKPSDLEEAKTCAELMIQRRIFSESKDEIALVVCGSQKTNNSLSSDNEYTHIDVVANLQPVSFGLLEKLGSVKSTQHMCDFVDAVVVALDVLMDQTKNQKFAGRKVVLLSNLGGAFDDSQQNVIANGMKNSSLSLTVVCPFDIENGEDDTAKLSPSQRKAVGYVSKILKTVEGDAYTFSQAVPALTTYEKKRVRPTPWNANLEIGPDLSIPISSYIKISEAKPKTWKQCVAQRPDVPVRCDATLYRNDEKETEVEKAETVAGYRYGTTLVPFSDEDRDSLECTRGGRGLQVLGFTDAANIKRHYYMGDKTSYVLARKGDESAEAAMSALIQALEKSKMVAIVRYAFSERSSPRMGFLSPRIKDEYECLVFVQLPYMEDLRRFTFAPLDANKDNIPTEEQLSVFDDLIAAMDLSEVEVNGEPQELFKSSQTCNPYLQRFYQCVQHRALHPKDPLPEVAPHVADALKPPKAITELARPVLEKMASLFPLHEVVPEKRKQDNTVTKNGGGTVTNASVSSDEPAAKKSRADFSMADLVATATTKVDVVNPVEDFKKLLADKDHRFDDVCSQLEGVILKLFDDTLGRAVYAKAVRCLRAYREASLEKSDPGKFNDFMNKLKSLYSIKREELWELLIKEAVQPVGKAECSKSALEDDEVERFYVVEKEAEEKKEDEPKDEDDLLDMM
The following text describes a protein:
Function:
Possible sulfate transporter.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MSSPSENHLLGPKTSFIDNRTSTSRPLHEIPSYQSLARRSSTWKRANIPQQKPSLVRRINYYIPVLHWLPNYSLRNIIWDVLAGCSTACLSVPIALSFAQTFLGVPPIYILTGTAIGPILYCLFTACPLISIGPEAGMCLLIAENIHQRVLSKADVPQETAILVTGLIAFIAGIINLAAGLFRLGFLDALVSPVLLRGCILSISMIIMINQGSVFFGFSGVKYKGSDFPIDKLMFLIRNMSKANIYTTILSCITISLLIGCRNLKSKLSAKYPRIVSIPDAVIILLLGSFLSKKFDWHSNYGIAILGEIKTTILLPKLPLPEKNKLHFITQSLQTGVMCSFLAFIDTVIAVKAISLQTNNLIRSNRELISLGAANIGSSLFCGLPICGGYLRTKCNIMSGARTQVATIACSVLILLATFFIMPVFSTVPTCMLASMVVSLGVSLFADAAVEIFKLARIRVWWELGIIFSIATCTMMFGLETGIIFGLSITVMQIIRHSTRSRIMFRSPTSNGTAEFILEDAASTLSHRTNPSSTAVESAPRILVVRIPEPLFFANVSQLEDRLNRLEKYGHPRMHPGETPYRRIEDIEVVVFDMVGVSSIDSSALFAFQRILKEYVEHQVEVHLVSLDPQVLHIFEKHGLLDLIGGYDHVQDSIKKVDALCDIELGV
The following text describes a protein:
Function:
High-affinity transporter for guanine and hypoxanthine.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSGDILQTPDAPKPQGALDNYFKITARGSTVRQEVLAGLTTFLAMVYSVIVVPGMLGKAGFPPAAVFVATCLVAGFGSLLMGLWANLPMAIGCAISLTAFTAFSLVLGQQISVPVALGAVFLMGVIFTAISVTGVRTWILRNLPMGIAHGTGIGIGLFLLLIAANGVGMVIKNPIEGLPVALGAFTSFPVMMSLLGLAVIFGLEKCRVPGGILLVIIAISIIGLIFDPAVKYHGLVAMPSLTGEDGKSLIFSLDIMGALQPTVLPSVLALVMTAVFDATGTIRAVAGQANLLDKDNQIINGGKALTSDSVSSIFSGLVGAAPAAVYIESAAGTAAGGKTGLTATVVGALFLLILFLSPLSFLIPGYATAPALMYVGLLMLSNVSKLDFNDFIDAMAGLVCAVFIVLTCNIVTGIMLGFVTLVVGRVFAREWQKLNIGTVIITAALVAFYAGGWAI
The following text describes a protein:
Function:
Antagonizes telomeric silencing in yeast. May recruit SIR4 to non-telomeric sites or repression.
Miscellaneous:
MISCELLANEOUS: Present with 1620 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Domain:
The LisH domain mediates tetramerization and interaction with SNT1.
Sequence:
MSITSEELNYLIWRYCQEMGHEVSALALQDETRVLEFDEKYKEHIPLGTLVNLVQRGILYTESELMVDSKGDISALNEHHLSEDFNLVQALQIDKEKFPEISSEGRFTLETNSESNKAGEDGASTVERETQEDDTNSIDSSDDLDGFVKILKEIVKLDNIVSSTWNPLDESILAYGEKNSVARLARIVETDQEGKKYWKLTIIAELRHPFALSASSGKTTNQVTCLAWSHDGNSIVTGVENGELRLWNKTGALLNVLNFHRAPIVSVKWNKDGTHIISMDVENVTILWNVISGTVMQHFELKETGGSSINAENHSGDGSLGVDVEWVDDDKFVIPGPKGAIFVYQITEKTPTGKLIGHHGPISVLEFNDTNKLLLSASDDGTLRIWHGGNGNSQNCFYGHSQSIVSASWVGDDKVISCSMDGSVRLWSLKQNTLLALSIVDGVPIFAGRISQDGQKYAVAFMDGQVNVYDLKKLNSKSRSLYGNRDGILNPLPIPLYASYQSSQDNDYIFDLSWNCAGNKISVAYSLQEGSVVAI
The following text describes a protein:
Function:
K(+) channel that conducts voltage-dependent outward rectifying currents upon membrane depolarization. Voltage sensing is coupled to K(+) electrochemical gradient in an 'ion flux gating' mode where outward but not inward ion flow opens the gate. Converts to voltage-independent 'leak' conductance mode upon stimulation by various stimuli including mechanical membrane stretch, basic pH, heat and lipids. Homo- and heterodimerizes to form functional channels with distinct regulatory and gating properties (By similarity). At trigeminal A-beta afferent nerves, the heterodimer of KCNK2/TREK-1 and KCNK4/TRAAK is mostly coexpressed at nodes of Ranvier where it conducts voltage-independent mechanosensitive and thermosensitive currents, allowing rapid action potential repolarization, high speed and high frequence saltatory conduction on myelinated nerves to ensure prompt sensory responses. Permeable to other monovalent cations such as Rb(+) and Cs(+) (By similarity).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Cell projection, axon. Note=Localizes at the Ranvier nodes of myelinated afferent nerves.
Domain:
Each subunit contributes two pore-forming domains 1 and 2 which assemble to form a single pore with M2 and M4 transmembrane helices lining the central cavity and M1 and M3 facing the lipid bilayer. The transmembrane helices are bridged by the selectivity filters 1 and 2 carrying a signature sequence TxTTxGYGD that coordinate the permeant ions. Up to four ions can simultaneously occupy the selectivity filter and at least two elementary charges must translocate across the filter to convert it into the open conformation; Channel opening is brought about by a conformation change that involves buckling of the second transmembrane helix and affects the position and orientation of the fourth transmembrane helix.
Sequence:
MRSTTLLALLALVLLYLVSGALVFQALEQPHEQQVQKDLEDGRDQFLKDHPCVSQKNLEGFIKLVAEALGGGANPETSWTNSSNHSSAWNLGSAFFFSGTIITTIGYGNIALHTDAGRLFCIFYALVGIPLFGMLLAGVGDRLGSSLRRGIGHIEAVFLKWHVPPGLVRMLSAVLFLLIGCLLFVLTPTFVFSYMESWSKLEAIYFVIVTLTTVGFGDYVPGDGTGQNSPAYQPLVWFWILFGLAYFASVLTTIGNWLRAVSRRTRAEMGGLTAQAASWTGTVTARVTQRTGPSAPPPEKEQPLLPSSLPAPPAVAEPAHRPGSPAPAEKVETPPPTASALDYPSENLAFIDESSDTQSERGCALPRAPRGRRRPNPTKKPSRPRGPGRLRDKAVPV
The following text describes a protein:
Function:
Catalyzes the reversible isomerization between hydroxypyruvate and 2-hydroxy-3-oxopropanoate (also termed tartronate semialdehyde).
Sequence:
MRHLTSGLNRKSPFQALHSKVLAVSGKDSDFHYPCACTPRLPPAPDLARWAYPRPLFACNTALLSGCNIAKFPGNIEAGELGLAAVPGRQDEFRTGLNEAVRWASDLGCDRIHIMAGRVPLGLERQNIEEEMEETFIENLQYAADILAQAGMVGLLEPINSLISEPRYFLNTPQHAASILQKVKRPNLKLQMDLYHWQIMGGNLTQNIKTYFPLIGHVQIAQVPHRNEPDSPGELNFMYLFDLLQELGYQGYVGCEYKPQGDTAKGLGWMKKYLKYCHVDNKTN
The following text describes a protein:
Function:
Component of the adaptor protein complex 2 (AP-2). Adaptor protein complexes function in protein transport via transport vesicles in different membrane traffic pathways. Adaptor protein complexes are vesicle coat components and appear to be involved in cargo selection and vesicle formation. AP-2 is involved in clathrin-dependent endocytosis in which cargo proteins are incorporated into vesicles surrounded by clathrin (clathrin-coated vesicles, CCVs) which are destined for fusion with the early endosome. The clathrin lattice serves as a mechanical scaffold but is itself unable to bind directly to membrane components. Clathrin-associated adaptor protein (AP) complexes which can bind directly to both the clathrin lattice and to the lipid and protein components of membranes are considered to be the major clathrin adaptors contributing the CCV formation. AP-2 also serves as a cargo receptor to selectively sort the membrane proteins involved in receptor-mediated endocytosis. AP-2 seems to play a role in the recycling of synaptic vesicle membranes from the presynaptic surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-[LI] endocytosis signal motifs within the cytosolic tails of transmembrane cargo molecules. AP-2 may also play a role in maintaining normal post-endocytic trafficking through the ARF6-regulated, non-clathrin pathway. During long-term potentiation in hippocampal neurons, AP-2 is responsible for the endocytosis of ADAM10. The AP-2 beta subunit acts via its C-terminal appendage domain as a scaffolding platform for endocytic accessory proteins; at least some clathrin-associated sorting proteins (CLASPs) are recognized by their [DE]-X(1,2)-F-X-X-[FL]-X-X-X-R motif. The AP-2 beta subunit binds to clathrin heavy chain, promoting clathrin lattice assembly; clathrin displaces at least some CLASPs from AP2B1 which probably then can be positioned for further coat assembly (By similarity).
Subcellular Localization:
Cell membrane. Membrane, coated pit; Peripheral membrane protein; Cytoplasmic side. Note=AP-2 appears to be excluded from internalizing CCVs and to disengage from sites of endocytosis seconds before internalization of the nascent CCV.
Sequence:
MTDSKYFTTNKKGEIFELKAELNNEKKEKRKEAVKKVIAAMTVGKDVSSLFPDVVNCMQTDNLELKKLVYLYLMNYAKSQPDMAIMAVNSFVKDCEDPNPLIRALAVRTMGCIRVDKITEYLCEPLRKCLKDEDPYVRKTAAVCVAKLHDINAQMVEDQGFLDSLRDLIADSNPMVVANAVAALSEISESHPNSNLLDLNPQNINKLLTALNECTEWGQIFILDCLSNYNPKDDREAQSICERVTPRLSHANSAVVLSAVKVLMKFLELLPKDSDYYNMLLKKLAPPLVTLLSGEPEVQYVALRNINLIVQKRPEILKQEIKVFFVKYNDPIYVKLEKLDIMIRLASQANIAQVLAELKEYATEVDVDFVRKAVRAIGRCAIKVEQSAERCVSTLLDLIQTKVNYVVQEAIVVIRDIFRKYPNKYESIIATLCENLDSLDEPDARAAMIWIVGEYAERIDNADELLESFLEGFHDESTQVQLTLLTAIVKLFLKKPSETQELVQQVLSLATQDSDNPDLRDRGYIYWRLLSTDPVTAKEVVLSEKPLISEETDLIEPTLLDELICHIGSLASVYHKPPNAFVEGSHGIHRKHLPIHHGSTDAGDSPVGTTTTTNLEQPQVIPSQGDLLGDLLNLDLGPPVNVPQVSSMQMGAVDLLGGGLDSLVGQSFIPSSVPATFAPSPTPAVVSSGLNDLFELSTGIGMAPGGYVAPKAVWLPAVKAKGLEISGTFTHRQGHIYMEMNFTNKALQHMTDFAIQFNKNSFGVIPSTPLAIHTPLMPNQSIDVSLPLNTLGPVMKMEPLNNLQVAVKNNIDVFYFSCLIPLNVLFVEDGKMERQVFLATWKDIPNENELQFQIKECHLNADTVSSKLQNNNVYTIAKRNVEGQDMLYQSLKLTNGIWILAELRIQPGNPNYTLSLKCRAPEVSQYIYQVYDSILKN
The following text describes a protein:
Function:
Component of the exocyst complex.
Sequence:
MEVYGAYGDGVARIREAVLENQLQMKQVEQSLLGFQKGLLGVEREMLPVYKLTEQLRGTQKNIDLSVQELRQINENFVAAHELAPVLLNGSKFDQDEYVKSLQKLLVAITFLEGHRSYEGSVKALDQAKELLGQVRRKCMADFASVTELLREYGKQRFDVIRMFLGEDPSGSSMGFDLSTPVTALAKCVKDIEVTIEAEKVLAGLIFSNEELANGAFRYSTLQVLESWKKDIDSSLRSPKQLDAVKLLLVHDLLLERVEVLEAAVLPPLLLRDREGKGLDDPWVLSKAVSEIVNELAVTAKQKLFTFQPGLVEASGDRTVTRDGNVHPISSHTINFLRKICDQAKPLKVLLTKDSDVTPVSFVDTVVTQLIEALISKADQLKGREGLKRLFLVNNFGYVTNSLPHCAQSDDSDLEAQIHGIIKPRVEAMRNDALTHFIQLSYITFKEYLNDPTEPLQFAKGGSVLTLESGRLLKEKFSKFNDQLEELHKTQRTYVVAEVPIRQHLIRTAVDTIIPVYKAFYEKYSVIQFSRKHASRYLKYPPQAVQALLKELFSGEASPGDKHSEVSSS
The following text describes a protein:
Function:
Probable component of the HRD1 ubiquitin ligase complex that mediates the rapid degradation of misfolded endoplasmic reticulum (ER) proteins, a process called ER-associated degradation (ERAD).
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MIRLQTYAAFSLMATATAVYYAFSSREQFYPAMVYLSTSKICFVLLLNTGLVAMCVAWQLVKRLFLGTLREAEVERLNEQAWREVVEILFAVTIFRQDFSVSFLAMVAALLLVKALHWLAQKRVEYIETTPSVPMLSHARIVSFMLFLLVVDCLFLSNSLRSLIHKREASVAIFFSFEYMILATSTVSTFVKYIFYVSDMLMEGQWEKKAVYTFYLELISDLVHLSLYMLFFIAIFLNYGVPLHLIRELYETFRNFRIRIADYVRYRKITSNMNERFPDATADELNASDATCIICREEMTTAKKLLCGHLFHVHCLRSWLERQHTCPTCRAPILPPDNGRTAARPHGVHPGVQPVPGNGTPGSERAAGENISRRQAKLEAAASAASLYGRSFAYPPANNLNRYSTPPQSTSNGPQSGEASTSNQSPKGHATADPSAPTFYARGAVSSVTTTRELESSLQKAYENAIKSQIEMLQIQLQMFQHGATSSATNNENGEHTKSD
The following text describes a protein:
Function:
Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).
Subcellular Localization:
Cytoplasm.
Sequence:
MTSSNLIKQLQERGLVAQVTDEDALAERLAQGPISLYCGFDPTADSLHLGHLVPLLCLKRFQLAGHRPVALVGGATGMIGDPSFKASERKLNTEDTVNEWVEKIRHQVSPFLDFDCGENSAIAANNYDWFGGMNVLTFLRDIGKHFSVNQMINKEAVKQRLNRDDSGISFTEFSYNLLQAYDFACLNKNHGVALQIGGSDQWGNITSGIDLTRRLHQQQVYGLTVPLITKADGTKFGKTEGGAVWLDPKKTSPYKFYQFWINTADADVYRFLKFFTFMSLEEINALEEEDKNSGKAPRAQYVLAENVTGMVHGPEGLAAAKRITDSLFSGDLHDMTEADFAQLAQDGMPTVELNRDADLQQALVNAELVPSRGQARTMIGSNAVAINGEKQADPEYVFTDADRLFGRYTLLRRGKKHYCLISWL
The following text describes a protein:
Function:
Component of the receptor for IL20, IL22 and IL24. Component of IL22 receptor formed by IL22RA1 and IL10RB enabling IL22 signaling via JAK/STAT pathways. IL22 also induces activation of MAPK1/MAPK3 and Akt kinases pathways. Component of one of the receptor for IL20 and IL24 formed by IL22RA1 and IL20RB also signaling through STATs activation. Mediates IL24 antiangiogenic activity as well as IL24 inhibitory effect on endothelial cell tube formation and differentiation.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MKKLLVVLAACSVVGIATTERSSCLKRVAFSSTNFENILTWETEADILPGTVFDVQYKQYGEKAWLNKRECQSITQPFCNLTHETENFTEHYYARVRATGHRCSSNWVRSERFEPRKETIIGAPEVECIPHVRSIKFLIHSPYTPLRGEDGHQLNIEDIYSKFSTVDYHLTIFNQRTHQKWKKNEHNKEFEVSNLDPDTEYNGTVHLYLLERSSKSQVFWVKTLPDNTWLFYCFVALGFCAGLVFAALGYVIYKYIKQHSAQPMSLDFRGLSSFQPLTLTVEHIIKPINVSKPSLLIPEAQFSQVGQCLDKALELPQPFHPSSGTYQQQDNLSVFQGAHLLCSVSAAPAGYAPQTSEQSTANLPMTYGVCVDGIDHSNKNNFLPNQLLKEVLSDSSAGGKLISHTLGKSCSCWNYREQQPNVALWDSSAMRDSALVHGSPQQIQQLLLRTDGAEGEEHLPQLLLPSVEQGGCYRQQTAELPLLLSSVTVDTDCAQDDESQSRPSAAHFLSVSNGNNLPGENTEWWVSPDSENKVQFQETWEAAQELNCMKLDNVVSQDTTSEYRNGISLTTLFKDLNLKVLWDQADENTEFC
The following text describes a protein:
Function:
Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratogenic properties. OtaC catalyzes the oxidation of 7-methylmellein (7-MM) into 7-carboxymellein (By similarity). The pathway begins with the highly reducing polyketide synthase otaA that catalyzes the formation of the isocoumarin group during the initial stages of biosynthesis, starting from one acetate and 4 malonate units, to originate the characteristic pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The newly identified cyclase otaY might be involved in the polyketide cyclization reaction during the initial steps of the OTA biosynthesis. 7-MM is then oxidized into 7-carboxymellein (also called ochratoxin beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by the otaB gene is involved in the linking of phenylalanine to the dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the production of ochratoxin B (OTB), which is the non-chlorinated analog of OTA and which subsequently serves as the substrate of the halogenase otaD for chlorination activity to form the final molecular structure of OTA, containing a chlorine atom in the C-5 position of the molecule (Probable).
Subcellular Localization:
Membrane; Single-pass membrane protein.
Sequence:
MSIDTLLYTSLAVGAVYLASVALYELYWSPLAHIPGPKLAACTRLYEFFYDVVCGGQYTFKIADLHKQYGPIIRISPREIHIHDPNYYETLYATNSPRNKDPWFTAHFGVDESAFSTLDYRLHRSRRAMIAPFFAKARMDGAQPLIKANLAKLIRHLDAHASSQSVLKVEVAYNSFTGDVITGYTSYRSFEYLETTDMVPIWSETVRNLVESGMLSRHLPGFFPLLAWAGSRCIAAVYPKLLPVIAFRMKCAQEVNFMWTNSEEGKKEAIQSGCSEPALFPELVSRASSAPDITEERLLHEFITIVAAGTETTAHTMTVCTFHIAHNQSILDKLREELDNRFHSNADMDLQTLEQLPYLTGIIYEGLRLSYGLSHRLQRISPIDPLKYKDIAIPPNTPVGMSSALMHHDESIFPQSHEFIPERWTDPNDRRRLNKYMVSFSKGSRQCIGMNLAFAELYLGIATLFRRYDMKLHDTTLDDVQLHGDKMLPRAKNGSKGVRVTLRRAQSVG
The following text describes a protein:
Function:
Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
Domain:
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence:
MQIPGKVLVEPRDYRSFCFRGEGRANFVISARHRLTGVRIVWRFAKARKSGLLTVKARSELVNSYMERIVAPFFDEQYLVGMNIVEFDTVDVHQLAKIPSLPANQKIETFEELFDLPDEYSFLPLNTFQRVHGTTILTNPKRLTSLQMLDATQLPTTISDEGHSSTITVEIKPKQGFFQHHPNVNVAHCNNCILQIEKSCGHSHFSEMYDFCPMDLFSGNYSRMHKAIHSLFLVPHRNLRIFIDGNQVHSDEKPLEEAVFSETLFPRNEATSEDLISALCLALSGNQSKKKFRLRNSSVLGQILRAQKVDEIGIVQAHAIYDRMDHHTKTALLDKSSLTRAGLEAILERKSLENEHLLQQLRRYFLAATMKDCSIMISLRLIQSCPSPRRDIIRLPNGRVFAFTIKIVDLDPKTAKNLINCHPRFMSGVKIIRLDQESAEHDRKFKPCV