lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalytic subunit of the glycosylphosphatidylinositol-anchor (GPI-anchor) transamidase (GPI-T) complex that catalyzes the formation of the linkage between a proprotein and a GPI-anchor and participates in GPI anchored protein biosynthesis. Recognizes diverse proproteins at a C-terminal signal peptide (CSP) region that lacks consensus sequence and replaces it with a GPI-anchor via a transamidation reaction. Transamidation catalysis reaction follows a two-phase mechanism. In the acyl-enzyme phase, the carbonyl group of the proproteins's omega-site undergoes a nucleophilic attack forming an enzyme-substrate thioester bond. Followed by a general acid catalysis that allows CSP releasing, regenerating the carbonyl, and forming the acyl-enzyme intermediate. In the GPI-anchor attachment phase, the amino group of the GPI-anchor's ethanolamine phosphate, the one on third mannose (EtNP3), mediates a nucleophilic attack on the carbonyl of the acyl-enzyme intermediate, replacing the CSP, allowing GPI-anchor attachment to the omega-residue, therefore forming the product and freeing the enzyme.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MAVTDSLSRAASTLAAVLLLSFGSVAASHIEDQAEQFFRSGHTNNWAVLVCTSRFWFNYRHVANTLSVYRSVKRLGIPDSHIVLMLADDMACNPRNPKPATVFSHKNMELNVYGDDVEVDYRSYEVTVENFLRVLTGRIPPSTPRSKRLLSDDRSNILIYMTGHGGNGFLKFQDSEEITNIELADAFEQMWQKRRYNELLFIIDTCQGASMYERFYSPNIMALASSQVGEDSLSHQPDPAIGVHLMDRYTFYVLEFLEEINPASQTNMNDLFQVCPKSLCVSTPGHRTDLFQRDPKNVLITDFFGSVRKVEITTETIKLQQDSEIMESSYKEDQMDEELMEPLKYAEQLPVAQIIHQKPKLKDWHPPGGFILGLWALIIMVFFKTYGIKHMKFIF
The following text describes a protein:
Function:
Functions as a Ras GTPase-activating protein. Plays an important role in the expansion and functions of natural killer T (NKT) cells in the liver by negatively regulating RAS activity and the down-stream ERK signaling pathway.
Subcellular Localization:
Cytoplasm. Cytoplasm, cell cortex.
Sequence:
MDPPSPSRASQTQPVAPSPLTSYRWHSGGGAEKGAGGFRWGRLAGWGRAQSHQETTASSQPAPRSLFRRVLSAPPKESRTSRLKISKSLWGKNKSPPLDSEPEPENPEPEPELEPLATQIPEAPTPDVPVWNIEAFTLLDGKLVLLGNEDEGPRQPRMGSASSESSIHVASGNLKDPDRTPGKTDPEAAGPHQIHNVRGLLKRLKEKKKAKSELGASASRDGPPSALGSRESLATISELDLGAERDVRVWPLHPSLLEEPHCFQVTWAGGSRCFSCRSAAERDRWIEDLRRHFQPSQDNVEREETWLSVWVHEVKGLPRAAAAAPGVRTELWLDGALLARTTPRAGPGQLFWAERFHFEALPPARRLSLRLRGAGPGDAVLGRVALALEELGIPRAPAAGLERWFPLLGAPAGAALRARIRARRLRVLPSERYKELAEFLTFHYARLCGALELALSAQAKEELAAAMVRVLRATGRAQALVTDLGTAELARSGGREALLFRENTLATKAIDEYMKLVAQDYLQETLGQVVRRLCASTEDCEVDPSKCPASDLPQHQSRLRNSCKEVFENIIHSYNWFPAELGTVFSGWREACKARGSEALGPRLVCASLFLRLLCPAILSPSLFGLALEHPAPGPARTLTLIAKVIQNLANRAPFGEKEAYMSFMNTFLEDHGPAMQHFLDQVATVDADTAPSGYQGSSDLALQLAVLHAQLCTIFAELDQATRDNLEPLPTILHAIEEGRPVPVTVPMCLPAPRTQGHSSISAGEKPGFLAPRDLPKHTPLISKSQSLRSVHGAGSWARPRLEEEQPPRLPRPVKRTQSVPAGRPARRRPSAGPRPRPKGSLHAGPAPRGRPWTGASASLPRKPSVPWQRQMDQPRDKDQALGTHRPVGKLAELQCEVAALRQDLKMLSGLVESLSTHIRSLSEQQEQLRTQLQLLDSRLREGTAKLDPGRDRSTNEGHRLKSLECRLAEIESTQAQLKDTIQNLQLLPRTSESQSQPVPLKAPCINGDTT
The following text describes a protein:
Function:
Cilium-specific protein required for cilia structures.
Subcellular Localization:
Cell projection, cilium.
Sequence:
MCERGFARRREEVTGLNRITEKGLKDICKRDKLYQTPRLNDVLYLHFQGYQCIENLDEYTELKSLWLESNAISEIQNLTKLTKLKCLYLQNNLITKMENLEFNRELDTLNLSQNHIRKIENIGTDILPVLNTLNITSNYLTDSASLAALVECKTLSVLDLSNNRIDDILIVKIFEQMPSLKVLVLQGNPVVSRLPQYRKTLILACKELTYLDSRPVFPRDRACAEAWKREGYEGERKEVQRWNRAERRKTRESVNSTIRMRNRHLKPEDQVPLLTSSDSEEEQKGISSAEKAQKRAEMEYGSVDTMWDEVSGESQASEHSTTSSTSAEDNESAGSQADHIAERISNRRVKPLEGRPKVLYDEAASGDEKAVTTTDSKKDSNAEDLPELKDITEALLQSDTASKPPLQPTLLQSDSGSEMDNTADLEQTCQTLLQVAQGNDDGDPTPKQIKSQMIDEMYESFGSDLFEEHPLPIDQLLNESTKKYQLEAKVCCEEETTKTPRDLYKEFIEEVTWRPKSKEQLEREQECVDASEKCAHDLAEMGSHLEEDLQELRDFTENLSSDVQEQAKDPSESDEEPTEEEMEVKSQLLKEQFQDRKKRLKEAIEERKTMQKNLEARKEDLNKSYNLFAKIMDDATDNVPKRVFGAGCDVPSKDWDKEECMQQLPLTSMEDSINGRPSSNDEDILTRPLTELTSAEAAEEICSQLDRKLAGEEEALRQLLCDLENENEILYSIETQIKYAESISVEDSQSQMVCASLLNDLISDVIYKDITEMGPNSYPLGPIESDEEYTYSEEPKLEKMVPPHLENPAGGKSLRECVDTFKEFFASKGNDKPRQESHTHLEKIRAAKALLKSKSLAEFSKDTPESLDAQLAKDEDRRKRHVAASAGRCFAKREKYDDTLEVVDNRLMVVKKDTGELEELPPPPELISDSESEKEVEEDDDAYDTAEETLQEYPRVPWTTPYKPKPRKAAEHLVNEAMQRVLAEQFSELPDDTKENEPQEDEFFSLEAKETFGNLDSEFFQKLDLDKVTTANNAEAATECMRSYNELKACMKSGSTELQLTSEENEMLQEMLSSNEDLEAKHKSNDDPLVERDNELLNKMMQRMKEHEERARELQEQLEKEKEEENSGPIKLSMGEGSMLYQRWSPLSLTEIIDPQAEEGGRQAEEGGAQQEEGGAQSEEGDDQAGVPQAEEGVTQGEESVLQEEETHAENGVAQAEGRVLQSPVIYPIIGYEDIDDDDAASDFTTDYSSDDEVAVVVPPKISPAMLKAYYYDGFEEDMRMVRENEARTRRGLRAIMQKEKQMWKDNEEEMAADMAPSASPKEEHIPEVKSETETAKPTVETAKDKWAKIASRLNEFLDPEAMEQLESHEFGESDGEDDVDLTGLQNYDEESETECESALKETTEIGDSEKQENKTQDETLDPKDTEAITDEWSPYQTSFEENRTAFCDRHNKLTMITEQTSDVGDPETETTKLICQWEKIIPEDSKIGDGPTEKFLDQKAQDNTENTDERPENPKNFITLDYFVDTEPSESLEDTEATETPEVSTEQTLKTEQMEFNLDVLNDDGDVVIKEVTVEAQVTYQ
The following text describes a protein:
Function:
Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
Subcellular Localization:
Mitochondrion.
Sequence:
MIALLRWGIARPSAPLRWSRCFATSTEKGDEGWQTVIGLEIHAQIKTGKKLFSKASTSYGHVPNTNVDVHDAAFPGTLPVLDINAIRLSIMTALALNCQINPRSTFDRKHYFYHDIPASYQITQHYNPLAWNGHLEIREGDNGSKRTFNIGIKQLQVEQDTAKSQTVGDAVLVDLNRAGTGLMEIVTDPDMRSPEEAGAFVKKLQGLLRRVGSADGDMEKGNLRVDVNVSVHRPGMPFGTRCEIKNINSVRFLQAAIESERQRHIAHYCTSPLEPLAQETRGFNELTLQTYSLRSKEEATDYRYMPDHNLPAIIIDDGYLDSLWKNLPEMPWQSVERLVKTYGVTKRDAETLLGLDEYSAQGIAYFEEVVEQDKKIAKKATNWIAHELLGQLGKAIRPWTPTIVPAPLMHELVTAVESREITGTTGKAIVKHFVSLPESASLPPSFAELLAELGLTPSAASVEDLTETCKKAMNNQPKAVADFKKGNEKVVMRLVGEVMKLSGGKADAMKAKDILLDLLKD
The following text describes a protein:
Function:
Serine/threonine-protein kinase that may function as a signaling receptor of extracellular matrix component. Binding to pectin may have significance in the control of cell expansion, morphogenesis and development.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MAVEYSKQLFLMVVVAVFYTKAATQPMSLPNCTAKCGSIKIPFPFGITKDCSLDNAFLINCNKTSSTASNSTKHVAFLSKTNQRVLNISLNGELHVAWPVARHCYPKKSKPTTPDIKMPHFHVSPTQNKLIAVGCDTMGLLEAIDSKGNTYTTACVALCNRLSDIVANESCSGPGCCEISIPKGRVFTEVAYISEHGLNNNQALVQPFNPCGYTFLVENGAYRFAITDLQKLKKRNFPVLLDWAVGNQTCQQARKDLSTYACKADKSKCYDAPTHKSGYLCRCRDGYWGNPYLNHGCQDVDECKESNDCFKGATCTNLPGSYHCLCPKGYEGDGKRCSQKSITKSRKEYILVTALSVSVSLVGLLVGSFYAYWALKKIKIIKLKEEFFKQNGGLLLEQQIVKHGGSSKTLKIFTIEELNEATSNFNEGKILGQGGQGTVYKGVLEDKSIVAIKKSKISDPNQIESFINEVAVLSQINHRNVVKLVGCCLETEVPLLVYEFIPNGTVYEHIHDQNESRKLTWKTRLRIAKETAGVLAYLHSAASTPIIHRDVKSTNILLDENTSQPIYHRDIKSTNILLDENTSQPIYHRDIKSTNILLDENLTAKVADFGASKIVPLDKTQITTLVQGTLGYLDPEYFHTSQLTEKSDVYSFGVVLAELLTGEKALSFGRPEVDRNLAMYFVSWIKEDQLLHILDKNIDEKNIEHLKEVALIAERCLRVKSEERPTMKEVAMGLEGILVTEENENMINATPSVINVEDGDGGSGFNYSYST
The following text describes a protein:
Function:
Acts in the modification of cell walls via demethylesterification of cell wall pectin.
Subcellular Localization:
Membrane; Single-pass membrane protein. Secreted, cell wall.
Sequence:
MKPVNYGRLAPSEPGGSSPPVDQPEHATPHPSRKRGVILLSLLSIVLIIASAVSATLLIGLRTRASSSQPSPVLARKPTKAISKTCSKTRFRSLCVNSLIDFPGSSAASEEELVHISFNVTLQHFTKALYLSSEISYLQMDTHVRSAYEDCLELLDDSVDALSRSLYTVAPSLDGNTGEQIQPGGSAEDVVTWLSAALTNHDTCTEGFADLNGAVKDHMSEKLKDLSELVSNCLAIFSAVDSGDFSGVPIQNRRRLMDAEISEENADNLPNWLGRKERRLLSLPVSAIQADIIVSQDGNGTCKTIAEAIKKAPEYSTRRTIIYVKAGRYEENNLKVGRKKWNLMFIGDGKGKTVISGRKSIFDNITTFHTAAFAATGAGFISRDITFQNWAGPAKHQAVALRVGADHAVVYRCNIIGYQDTLYVHSNRQFFRECDIYGTVDFIFGNAAVVFQNCSIYARKPMPLQKNTITAQNRKDPNQNTGISIHACRLYAMPDLRAANGSFQTFLGRPWKLYSRTVYMLTYMGDHIHPRGWLEWNATFALDTLYYGEYMNYGPGGPVGQRVKWPGYRVINSTIEASRFTVGEFIYGSSWLPSTGVAFLAGLAV
The following text describes a protein:
Function:
Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by MOCS3. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
Subcellular Localization:
Cytoplasm.
Sequence:
MQLTLEFGGGLELLCDSVKIHNINVDPKNGADKLTMKDLLAWVRNNLIKERPEMFMKGDSVRPGVLVLVNDCDWELSGQLDTTLEEKDVVVFISTLHGG
The following text describes a protein:
Function:
Extracts misfolded glycoproteins, but not glycoproteins undergoing productive folding, from the calnexin cycle. It is directly involved in endoplasmic reticulum-associated degradation (ERAD) and targets misfolded glycoproteins for degradation in an N-glycan-independent manner, probably by forming a complex with SEL1L. It has low mannosidase activity, catalyzing mannose trimming from Man8GlcNAc2 to Man7GlcNAc2.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type II membrane protein.
Sequence:
MQWRSLVLGLLLLRLGLHALLALLPALAPGLCLRLRLPFPFPPRSAALGPPGAARPLPGGGSSHWGSLRGGGGAAGRDEYETRYSAAFPPQLRARLRDAARGMFAFGYDSYMQHAFPSDELDPLHCCGRGPDRDDPSNLNINDVLGNYSLTLIDALDTLAVMGNSSEFQKAVKLVIDTVSFDKDSTVQVFEATIRVLGSLLSAHIIITDAKQPFGDMTIKDYDNELLHMAHDLAVRLLPAFENTKTGIPYPRVNLKKGVPPNSNNETCTAGAGSLLVEFGILSRLLGDSTFEWVARRAVKALWSLRSNNTGLLGNVVNIQTGHWVGKQSGLGAGSDSFYEYLLKSYILFGEKEDLEMFIDAYQNIQNHLRRGREACNEGEGDPPLYVNVNMFTGQLMNTWIDSLQAFFPGLQVLIGDVEDAICLHAFYYAIWKRYGALPERYNWQLQAPDVPFYPLRPELVESTYLLYQATKNPFYLHVGMDILQSLEKYTKAKCGYATLHHVVEKTKEDRMESFFLSETCKYLYLLFDEDNPVHKSGNKYMFTTEGHIVSVDERFRNSLWQDILPGEEGTEKVKPNELKAVNFSSNCNRVPDERRYLLPLKSNYMRQIDRMVGLI
The following text describes a protein:
Function:
Trifunctional enzyme that catalyzes three distinct reactions as part of the 'de novo' inosine monophosphate biosynthetic pathway.
Sequence:
MADRVLVIGSGGREHALAWKLAQSPHVKQVLVAPGNAGTASDGKISNSAVLISDHAALSKYCKDQKIGLVVVGPEVPLAAGIVDDLTAAGVRCFGPTAKAAQLESSKSFSKAFFDRHNIPTARWKSFTNAKEACDFITSATFPALVVKASGLAAGKGVIVATNKAEACKAVHEIMQDKTFGAAGETVVVEELLEGEEVSCLCFTDGVTVASMPPAQDHKRLMDGDQGPNTGGMGAYCPAPQLSKDLLLKIRNSVLQKTVDGMRNEGIPYVGVLYAGLMLTKEGPKVLEFNCRFGDPECQVILPLLESDIYEVIQATVDRKLSSCMPVWLEDSSAVTVVMASEGYPGSYPKGLEITGFSQAKDLGLVVFHAGTAMKDGKVVTSGGRVLTVTAIKKDLMSALKEANRGVEVIRFKGAIYRKDIGYRAIDFLKQTSGLTYKDSGVDIAAGNTLVQKIKPLAAATSRSGCNAELGGFAGLFDLKEAGYKDPILVSGTDGVGTKLKIAQLCNKHDTIGQDLVAMCVNDILAQGAEPLFFLDYFACGKLDVGMAQTIIAGIAEACKLAGCALLGGETAEMPGMYPPGEYDLGGFAVGAVERGEMLPQLNRIANGDVILGVASSGVHSNGFSLVRKIVEKSSLDFSSPSVGGSPNQTLGEQLLTPTKIYSKVLLPVLRTGHVKAYAHITGGGLLENIPRVLPASFGVVLDALSWKIPKIFSWLQKEGNLSEEEMARTFNCGIGAVLVVPKEQAGNILKDIQIHEEAWMIGKVVQRQGESAYVEVNNLLRALHANRLQSSPSQPSKAQPSKTRVAVLISGTGTNLEALIASAIKPTSYAQLVLVVSNKAGVEGLKRAERAGIPTKVIDHKQFSSRTEFDSAVDKVLEEFSVELICLAGFMRILSGPFVRKWDGKILNIHPSLLPSFKGAHAHRLVLEAGVQITGCTVHFVAEEVDAGAIIFQEPVPVKAGDTEETLSERVKQAEHRAFPAAMQLVASGAVKLGANGKLIWDVEKH
The following text describes a protein:
Function:
S100A12 is a calcium-, zinc- and copper-binding protein which plays a prominent role in the regulation of inflammatory processes and immune response. Its pro-inflammatory activity involves recruitment of leukocytes, promotion of cytokine and chemokine production, and regulation of leukocyte adhesion and migration. Acts as an alarmin or a danger associated molecular pattern (DAMP) molecule and stimulates innate immune cells via binding to receptor for advanced glycation endproducts (AGER). Binding to AGER activates the MAP-kinase and NF-kappa-B signaling pathways leading to production of pro-inflammatory cytokines and up-regulation of cell adhesion molecules ICAM1 and VCAM1. Acts as a monocyte and mast cell chemoattractant. Can stimulate mast cell degranulation and activation which generates chemokines, histamine and cytokines inducing further leukocyte recruitment to the sites of inflammation. Can inhibit the activity of matrix metalloproteinases; MMP2, MMP3 and MMP9 by chelating Zn(2+) from their active sites. Possesses filariacidal and filariastatic activity. Calcitermin possesses antifungal activity against C.albicans and is also active against E.coli and P.aeruginosa but not L.monocytogenes and S.aureus.
Subcellular Localization:
Secreted. Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Note=Predominantly localized in the cytoplasm. Upon elevation of the intracellular calcium level, translocated from the cytoplasm to the cytoskeleton and the cell membrane. Upon neutrophil activation is secreted via a microtubule-mediated, alternative pathway.
Domain:
The hinge domain contributes significantly to its chemotactic properties.
Sequence:
MTKLEEHLEGIVNIFHQYSVRKGHFDTLSKGELKQLLTKELANTIKNIKDKAVIDEIFQGLDANQDEQVDFQEFISLVAIALKAAHYHTHKE
The following text describes a protein:
Function:
Probable disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May act as a dithiol oxidase. Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
LTVWDCWCWSRVCWEILFLVILVCWGAEGRVLELDERFLKVESQGLWLVMFYAPWCGHCKNLEPTWIEVGAELAKGNSEVSVARLDATKYSAITSKYQVRGFPTIKFFKHGTTFDYDGPRSKENIVSFVSRAKGPSVVDIRNHAEFLQIKQRSTVFFAYVGAADTNLRKMFDETANSLFTSIDFYSIRDVSILKGMKIETTPTVVVFKDKKFYEMPANPMSSDFVQMWIRSEQFPSYNALTGMSYHSLRGAGLRFAVAAVNKNDKFNTTMKDIALKRNYPYTFCWVEGNGIVNSMTYGTISVPNLVVFDTNSYEYYTLCEEGDCESKLNEKEVTKFFKDIKDGVIEPKGGRGFWQQTKRFVTDAIGSVVGFFRESPIIASLVILLPTVVISGLCVCLCSITDGQEDGEQYTDDEDEEEDDLPPYNPDDLEQNTELEEELLHEDLAIGDSSEGVRQRVNIKPQEETG
The following text describes a protein:
Function:
Oxygenase component of the salicylate 5-hydroxylase (S5H) multicomponent enzyme system which catalyzes the 5-hydroxylation of salicylate to gentisate. Active only on substrates with a ring-substituted carboxylate group with an adjacent hydroxyl group. Primarily active against salicylate and substituted salicylates, but not against 2-hydroxycinnamate, 3-hydroxycinnamate, 2-hydroxyphenylacetate, 3-hydroxyphenylacetate, 2-hydroxybenzophenone, 1-hydroxy-2-naphthoate, 4-methoxysalicylate or 2-hydroxyacetophenone.
Sequence:
MSEPQRLKPVFPQDPKWPGEGSSRVPFWAYTREDLYKRELERLFYANHWCYVGLEAEIPNPGDFKRTVIGERSVIMVRDPDGGINVVENVCAHRGMRFCRERHGNAKDFFCPYHQWNYSLKGDLQGVPFRRGVKQDGKVNGGMPKDFKLEEHGLTKLKVAARGGAVFASFDHDVEPFEEFLGPTILHYFDRVFNGRKLKILGYRRQRIPGNWKLMQENIKDPYHPGLLHTWFSTFGLWRADNKSELKMDAKFRHAAMISTRGQGGKNEEVVSGVDSFKEQMKVNDPRLLDIVPEPWWGGPTAVMTTIFPSVIIQQQVNSVSTRHIQPNGHGSFDFVWTHFGFEDDNEEWTQRRLIQANLFGPAGFVSADDGEVIEWSQEGFEQKPTHRTVIEMGGHEIGDTDHMVTETLIRGMYDYWRKVMGE
The following text describes a protein:
Function:
Plays a structural role to facilitate the assembly and ensure the full activity of the enzyme catalyzing the decarboxylation of isocitrate (ICT) into alpha-ketoglutarate. The heterodimer composed of the alpha (IDH3A) and beta (IDH3B) subunits and the heterodimer composed of the alpha (IDH3A) and gamma (IDH3G) subunits, have considerable basal activity but the full activity of the heterotetramer (containing two subunits of IDH3A, one of IDH3B and one of IDH3G) requires the assembly and cooperative function of both heterodimers.
Subcellular Localization:
Mitochondrion.
Sequence:
MAALSGVRWLTRALVSAGNPGAWRGLSTSAAAHAASRSQAEDVRVEGSFPVTMLPGDGVGPELMHAVKEVFKAAAVPVEFQEHHLSEVQNMASEEKLEQVLSSMKENKVAIIGKIHTPMEYKGELASYDMRLRRKLDLFANVVHVKSLPGYMTRHNNLDLVIIREQTEGEYSSLEHESARGVIECLKIVTRAKSQRIAKFAFDYATKKGRGKVTAVHKANIMKLGDGLFLQCCEEVAELYPKIKFETMIIDNCCMQLVQNPYQFDVLVMPNLYGNIIDNLAAGLVGGAGVVPGESYSAEYAVFETGARHPFAQAVGRNIANPTAMLLSASNMLRHLNLEYHSSMIADAVKKVIKVGKIPSAVPSFLLHPLPFSWAI
The following text describes a protein:
Function:
Functions as a scaffold protein and likely plays a role in N-methyl-D-aspartic acid receptor (NMDAR)-mediated synaptic excitatory transmission (By similarity). May be involved in synapse formation in cone photoreceptor cells (By similarity). May play a role in the regulation of tight junction formation. Binds phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2). May play a role in the regulation of NOD2-mediated NF-kappa-B activation in immune response.
Subcellular Localization:
Cytoplasm. Basolateral cell membrane. Cell junction, tight junction. Postsynaptic density. Note=Colocalizes with CTNNB1, CDH1 and PKP4 at the basolateral membrane. Colocalizes with TJP1 at tight junctions. Its recruitment to cell-cell contacts requires CDH1. Colocalizes with NOD2 to the basolacteral membrane in intestinal epithelial cells.
Domain:
The FERM and PDZ 2 domains are necessary for localization to the basolateral cell membrane. The FERM domain binds to phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) and is sufficient for membrane localization.
Sequence:
MQPLTKDAGMSLSSVTLASALQVRGEALSEEEIWSLLFLAAEQLLEDLRNDSSDYVVCPWSALLSAAGSLSFQGRVSHIEAAPFKAPELLQGQSEDEQPDASQMHVYSLGMTLYWSAGFHVPPHQPLQLCEPLHSILLTMCEDQPHRRCTLQSVLEACRVHEKEVSVYPAPAGLHIRRLVGLVLGTISEVEKRVVEESSSVQQNRSYLLRKRLRGTSSESPAAQAPECLHPCRVSERSTETQSSPEPHWSTLTHSHCSLLVNRALPGADPQDQQAGRRLSSGSVHSAADSSWPTTPSQRGFLQRRSKFSRPEFILLAGEAPMTLHLPGSVVTKKGKSYLALRDLCVVLLNGQHLEVKCDVESTVGAVFNAVTSFANLEELTYFGLAYMKSKEFFFLDSETRLCKIAPEGWREQPQKTSMNTFTLFLRIKFFVSHYGLLQHSLTRHQFYLQLRKDILEERLYCNEEILLQLGVLALQAEFGNYPKEQVESKPYFHVEDYIPASLIERMTALRVQVEVSEMHRLSSALWGEDAELKFLRVTQQLPEYGVLVHQVFSEKRRPEEEMALGICAKGVIVYEVKNNSRIAMLRFQWRETGKISTYQKKFTITSSVTGKKHTFVTDSAKTSKYLLDLCSAQHGFNAQMGSGQPSHVLFDHDKFVQMANLSPAHQARSKPLIWIQRLSCSENELFVSRLQGAAGGLLSTSMDNFNVDGSKEAGAEGIGRSPCTGREQLKSACVIQKPMTWDSLSGPPVQSMHAGSKNNRRKSFIAEPGREIVRVTLKRDPHRGFGFVINEGEYSGQADPGIFISSIIPGGPAEKAKTIKPGGQILALNHISLEGFTFNMAVRMIQNSPDNIELIISQSKGVGGNNPDEEKNSTANSGVSSTDILSFGYQGSLLSHTQDQDRNTEELDMAGVQSLVPRLRHQLSFLPLKGAGSSCPPSPPEISAGEIYFVELVKEDGTLGFSVTGGINTSVPYGGIYVKSIVPGGPAAKEGQILQGDRLLQVDGVILCGLTHKQAVQCLTGPGQVARLVLERRVPRSTQQCPSANDSMGDERTAVSLVTALPGRPSSCVSVTDGPKFEVKLKKNANGLGFSFVQMEKESCSHLKSDLVRIKRLFPGQPAEENGAIAAGDIILAVNGRSTEGLIFQEVLHLLRGAPQEVTLLLCRPPPGALPELEQEWQTPELSADKEFTRATCTDSCTSPILDQEDSWRDSASPDAGEGLGLRPESSQKAIREAQWGQNRERPWASSLTHSPESHPHLCKLHQERDESTLATSLEKDVRQNCYSVCDIMRLGRYSFSSPLTRLSTDIF
The following text describes a protein:
Function:
mRNA-binding protein that may play a role in modulating the expression of cytoplasmic mRNA.
Miscellaneous:
MISCELLANEOUS: Present with 6490 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MSQEEKVDAKATLKTEISNNKKNDKQELELDELVGKLSIEGTPQVSQKLSKEEKHAHQLEADSRSIFVGNITPDVTPEQIEDHFKDCGQIKRITLLYDRNTGTPKGYGYIEFESPAYREKALQLNGGELKGKKIAVSRKRTNIPGFNRHYNSQNQYFQQWQWNYPLMAYPNPDTFPYYPPYPPNQSPNQNFGYNKNNYYRSPYNNKNRTFQKKHFNSAKDSTKNIRSTSQKPVVMPSDNVKSSTQEKDSK
The following text describes a protein:
Function:
DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. This subunit is less well bound than the others.
Subcellular Localization:
Cytoplasm.
Sequence:
MSSVYIVEEHYIPYSVAKKLLTDVIRSGGSSNLLQRTYDYLNSVEKCDAESAQKVIEELSNIVSREDVRAILASICPTTSDEVRSILVMDTNKTYTSEDIQKIIDIIRKYIKS
The following text describes a protein:
Function:
Mediates both low-affinity uptake and efflux of sugar across the membrane.
Subcellular Localization:
Endomembrane system; Multi-pass membrane protein.
Sequence:
MGLLRFLCGVLGTAFSILISAFLLVIRSPSSFIALFVLRAFPVSNIGNAVGLFLFLAPIMTFKRIIRSQSTEQFSGVPYVISLLNCLFYTWYGLPFMSSDNLLISIVSGIGVKERAKIIGHCSLALILFITFAFVSPFALHGKTRKLLCGITLDISSTIMYASPLSVMMSVIKMKFMPFSLLLFTFLCGIFRLTYGLLSRDLFLIVPNGLGTGLGAAQLILYAIYCKNRSHMANEITDEFAETDLEKTDQMQKLSCLA
The following text describes a protein:
Function:
Plays an important role in bacterial chemotaxis signal transduction pathway by accelerating the dephosphorylation of phosphorylated CheY (CheY-P).
Subcellular Localization:
Cytoplasm.
Sequence:
MISLEQAKELVQLLEQGRQDDANRLFTYVYESANNPMFKEIGMLTRDLHEALKNFQIDERFSEIATDEIPDARERLHYVIQKTEVAANKTMDAVDRCMPIADKLHESLLLIRPEWNGLMNGRIELMHFKSLCHRIDDLLSQVEGDSSELRGELTEILMAQDFQDLTGQIIKRVINLVNEVEKRLVEILTVFGAAQKEQKADKATVASIEPEGPILNPHERIDAVSSQDEVDDLLSSLGF
The following text describes a protein:
Function:
Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) to catalyze the transfer of a sulfo group to position 3 of glucosamine residues in heparan. Catalyzes the rate limiting step in the biosynthesis of heparan sulfate (HSact). This modification is a crucial step in the biosynthesis of anticoagulant heparan sulfate as it completes the structure of the antithrombin pentasaccharide binding site.
Subcellular Localization:
Golgi apparatus lumen.
Sequence:
MAHLLFSAFFLAAQTHAVPKEYFQQTEGEVLDSLKLQVGLLANETENYPPQVKPPGTNRRIPQSIIIGVRKGGTRALLEMLDIHPNIVVAATEVHFFDWDENYVKGFDWYKNLMPFSYEHQITVEKTPGYFTSPLAAERIHEMNSSIKLLLILRDPTERVISDYTQVYYNRLENRKPVQVIEDIVIRNGALNTKYKAIQRSLYDLHMENWLKYFSLDQIHIVDGDTLIKDPLPELQKVEKFLSLPPRIMPSNFYFNQTKGFYCIRSDGRERCLHESKGRPHPVVNNTVLEQLRAYFREHNNNFYRMVNRSFNWH
The following text describes a protein:
Function:
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:
Chromosome. Nucleus, nucleolus.
Sequence:
MNRVKKKPTGSLVLLKKKKSKKQQVPVDSDNEAYDSMVDNGTDEDDDDDDDGGGELNGAGQNGNASGEESDSMGSGHESGAFVRAPKPSKKKAVKALKRKVVAHEDDEAHRKRLKEMKELYKPPTMEEINRLKETENYYHSNLFRMQTEEMLKEVRVPSKVGRFSHVWVEQFKQFLHTIEDGASDRWLHELEYDGVQFPLPLGSMQHAQEVLGKERFRYVQQHQVRVIGGCDGMLRTSFGKPLVVDLLMVMPEKCLHKEDYLNLRYHCKRAHYLCTIAERLLQQAGNDKVVSNIRFEPLKGDHTKPVLVMEPADERFARKVHFQLHVVADSSKFPKKRFLPHRNNVRPTMIGGQAETVSTEEYENLPTPHYNTSILYDVRLVKNVELLESIIQSESVREAIVLLKVWIRQRHFDRGRYGFDGALVTFYVAYLLQNKRIYPNMSSYQIIRLFWNQLAGSSWDKEGISFDNSSREMLVSFFRYYDVVFIDPLGTLNLAANLPVDLYRRVRHESALAIRLLDNRQINSFLALFLASYPSFAQYDHIVMVNDSKLVTATIESFAEDAEKLDYFCDAQALFTRMVERLLRKGLGARAAYLVPLASTLKEGESAMPIKPRLALGLSLNGSEAFNLVDKGPEAIDAEASEAFRSFWHGKAELRRFKDGSITESCVWGETSDPIGQKRLIVRAIVKFLLQAHFDMPENKIVYLAEQFEAAVTPFPVQELHETIEERSLAVIRTFDTLGRVMRDLERLPLTINAITGTDPVFRYTDPDPPRPTASGMQSSNGETVFLSGKPIRATIQLAASGKWPADLEAIRRLKTAFYLRIAEDVNTSRKLKGQVQAQAYNDYLDVLFEKYLFRFEIIHQREIGILREYLSSNKVTRLQKDTDESVALEMRATILPQLTGFLHGLHQQYFSFGSVAAIAKRWLYSQLIDPYLWPDECTELLLAALYLNQPLQPPIQPQTGFLRWLQFIASTDWSKEMIVVNLTDKLSSETIDELEKDFFERRHSFPPLTIVTPCDAGKYGLFGRRAPTLEILNRVTLLAKAATHLVETDFRTLRNNIQDFFEPSVEGYNVIIHLHAHIVTPIGIRKSHEIGVHKTPGLSVNSTDKEPAAGLDPVRSYLQELREAYGQFAIFFYDPCGGDRIAVLWRPQALEEKPFTTSNVNGRKFTNDGTLQLNVDALVRDFEILGEGLVSSVEKMH
The following text describes a protein:
Function:
Involved in DNA damage tolerance by regulating translesion synthesis (TLS) of templates carrying DNA damage lesions such as 8oxoG and abasic sites. May act by stimulating activity of DNA polymerases involved in TLS, such as PRIMPOL and polymerase delta (POLD1).
Subcellular Localization:
Mitochondrion matrix. Nucleus.
Sequence:
MAACVARRCLSFLGRYRRGAVQSSLGFELRPAETVLSRSVCVCCLQQKRTLTSRNRPEGKVLEPVGVFEVPKQQGKYETGQLFLHSVFGYRGIVLFPWQARLYDRDVASPVSEKVDTSAAHGSKEVKGKTHTYYQVLIDARDCPHISQRSQTEAVTFLANHDDSRALYAIPGLDYVSHEDILPYNSTDQVPIQHELFERFLSFDQTKVPPFLARETLRAWQEKNHPWLELSDVHRETTENIRVTVIPFYMGMREAQNSHVYWWRYCIRLENLGVEVVQLRERHWRIFSLSGTLETVRGRGVVGREPVLSKEQPAFQYSSHVSLQASSGHMWGTFRFERPDGSHFDVRIPPFSLESNKDEKTPPSGLHW
The following text describes a protein:
Function:
Stimulates guanine exchange activity of SOS1. May play a role in membrane ruffling and remodeling of the actin cytoskeleton. In the cochlea, is required for stereocilia maintenance in adult hair cells.
Subcellular Localization:
Cell projection. Cytoplasm.
Sequence:
MKAFHRYPFTPSSCHCSGVTRSDSKLSAKALYEQRKKYSNSNYITHEISQYHVEHLSTFMMDKSESIITVDDAIKKLKLLDSKDKIWTQEMLLQVTDKAVKLLDCDTQEELENFPLPTIHMCQTVLNQTRYTSVLLLVCQDKDQHRPDIHFFHCDEVDAEMVHADIDSALGDTKHGKNMRPQTLKVNQEKMKHHRETILPPGPRGPPPPVKGRVSAPVSMQDKRSSGQHDSEFHENLPQRIEKDVQILNCALDDIEIFVARLQKAAEAFSQLKQRNKSKKNKKKGPAEGMLTLRAKPPSEAEFIDSLQKLKLALNLLTKLRKHIQNPNASELVHFLFGPLELVLQTCGSPDLARSIISPHLSKDTVDFLRGHLTPKETTIFELLGDGWTKPRAEWPRDQCAPPYYPKFRNGWEPPAELFLTASWETEGPSGQFAGQHGPPFSPDYRQHSSEDYYGTHSSNSSNGSYSEKPNNRKFAKIRYNFVARNANELSVLQDEILEVLEDDKQWWKLRNRSGQAGYVPFNVLDVVKIEDPDVPYNQKSFMTSPSGSASREDSFNKGITKDKAMDEVNNELLKKITASKTQPPKLIHVKRTPSTQVPLTSDSNPGQVTAWLNAKGFSKPTVDCLGILTGAQLFSLNKDELKAVCGDEGGRVYFQVTVQKEQVEKSSGSSELQEIMKRRQERIDSGGTD