lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Adhesion G-protein coupled receptor (aGPCR) for glucocorticoid hormones such as cortisol, cortisone and 11-deoxycortisol. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of downstream effectors, such as adenylate cyclase. ADGRG3/GPR97 is coupled to G(o)/GNAO1 G proteins and mediates signaling by inhibiting adenylate cyclase activity. May also signal through G-alpha(q)-proteins; additional evidence are however required to confirm this result in vivo. Plays a role in the regulation of various processes including B-cell development, inflammation or innate immunity. Regulates migration of lymphatic endothelial cells in vitro via the small GTPases RhoA and CDC42. Antibody ligation leads to the production and activation of antimicrobial mediators like reactive oxygen species (ROS) and myeloperoxidase (MPO) as well as enhanced bacteria uptake and killing by granulocytes. Additionally, collaborates with protease-activated receptor 2/PAR2 to stimulate neutrophil-driven antimicrobial responses and endothelial cell activation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
The Stachel sequence (also named stalk) in the C-terminal part of the extracellular domain (ECD) functions as a tethered agonist (By similarity). In the inactivated receptor, the Stachel sequence (also named stalk) is embedded in the GAIN-B domain, where it adopts a beta-strand conformation (By similarity). On activation, the Stachel moves into the 7 transmembrane region and adopts a twisted hook-shaped configuration that forms contacts within the receptor, leading to coupling of a G-alpha protein, which activates signaling (By similarity).
Sequence:
MATPRGLGALLLLLLLPTSGQEKPTEGPRNTCLGSNNMYDIFNLNDKALCFTKCRQSGSDSCNVENLQRYWLNYEAHLMKEGLTQKVNTPFLKALVQNLSTNTAEDFYFSLEPSQVPRQVMKDEDKPPDRVRLPKSLFRSLPGNRSVVRLAVTILDIGPGTLFKGPRLGLGDGSGVLNNRLVGLSVGQMHVTKLAEPLEIVFSHQRPPPNMTLTCVFWDVTKGTTGDWSSEGCSTEVRPEGTVCCCDHLTFFALLLRPTLDQSTVHILTRISQAGCGVSMIFLAFTIILYAFLRLSRERFKSEDAPKIHVALGGSLFLLNLAFLVNVGSGSKGSDAACWARGAVFHYFLLCAFTWMGLEAFHLYLLAVRVFNTYFGHYFLKLSLVGWGLPALMVIGTGSANSYGLYTIRDRENRTSLELCWFREGTTMYALYITVHGYFLITFLFGMVVLALVVWKIFTLSRATAVKERGKNRKKVLTLLGLSSLVGVTWGLAIFTPLGLSTVYIFALFNSLQGVFICCWFTILYLPSQSTTVSSSTARLDQAHSASQE
The following text describes a protein:
Function:
Positive regulator of the Rab7 guanyl-nucleotide exchange activity of the Mon1-Ccz1 complex, possibly by enhancing its endosomal membrane association. As part of the Mon1-Ccz1 complex involved in endolysosomal biogenesis possibly by mediating Rab conversion, the replacement of Rab5 with Rab7 during late endosome maturation.
Miscellaneous:
MISCELLANEOUS: 'Bulli' is the nickname of a classical German bus from the 1970s (the Volkswagen Type 2 van), which facilitated cargo trafficking.
Subcellular Localization:
Late endosome. Note=Colocalizes with Rab7, but not Rab5 positive endosomal structures.
Domain:
The C-terminal Mic1 domain consists of an alpha-solenoid structure that acts as a protein interaction scaffold for the CCZ1-MON1 complex.
Sequence:
MDNSNGIHYIELTPNPIRFDAVSQLTNVFFDDSNKQIFAVRSGGATGVVVKGPGSPDDVVISFCMSDRGGAIRSIKFSPDNQILAVQRKENSVEFICFQGDQPLLQDIITHQVKTLIHGFVWVHNREVALISNTGVEVYTVVPEKRQVRSVKSLSIGIKWFAWCCDANVALLCTSEGNSLIPVLVKQKVITKLPKVDLGNPSRDVQESKVTLGQVYGVLAVLILQSNSTTGLMEVEVHLLNGPGLAPRKCHVLRLSLLGRFAINTVDNLIVVHHQASGTSLLFDISLPGEVINEITYHTPITPGRSIKPFGLKLPSLSPDGQILQCELYSTHWVLFQPNIVIDAKLGCMWFLNLCIEPLCQLISDRIRLTEFLLQRSNGKQMLLKVIGQLVDDQYKGTLLPVLETIFSRINKIYASWVQLELQNQTAQPSNVKTTTLKQSTPPIVLIEQLDMVQIFQRIARRPYTESILMLYLQSLNKFNIAAQEELSKMIISELISNRSFDTLRRLVSYSMLLESKSVACFLLSHSNVDTAISQVAIDMLGRIEAHEIIIEVMLGQGKVIDALRLAKNSMGLEKVPARKFLEAAHKTKDDLIFHSVYRFFQMRNLKLYETLSFPKAEQCTEFIQHYNNTFPADNPTRQPVS
The following text describes a protein:
Function:
Probably involved in the defense reaction of plants against pathogens.
Sequence:
MSTHHQTPIDQLLTCQMGSFTLIFFLTTLATITHAQNSPQDYLNAHNSARAQVGVGNMVWNATVAAYAQNYANQRIGDCNLVHSGGPYGENLAEGSGTFTGTAGVNLWIDEKRYYEYITNTCTNGQVCGHYTQVVWRNSIQLGCARVQCTNNGWWFIICSYYPPGNYAGQAPY
The following text describes a protein:
Function:
Iron-sulfur (Fe-S) cluster binding motor protein that has a role in chromosome segregation during mitosis (By similarity). Required for mitotic chromosomal positioning and bipolar spindle stabilization.
Subcellular Localization:
Nucleus. Chromosome. Cytoplasm, cytoskeleton.
Sequence:
MVREEEKGIPVRVVRCRPLVPKETSEGCQMCLSFVPGEPQVIVGSDKAFTYDYVFDPSVEQEEVFNTAVAPLIRGIFKGYNATVLAYGQTGSGKTYSMGGTYTASQEHDPSMGVIPRVIKLLFKEKEQRQDWEFVLKVSYLEIYNEDILDLLCSSRERSSQISIREDPKEGIKIVGLTERNVASARDTVSCLEQGNNCRTVASTAMNSQSSRSHAIFTICIDQKKKNDKNSSFHSKLHLVDLAGSERQKKTKAEGDRLKEGININRGLLCLGNVISALGEENKKGGFVPYRDSKLTRLLQDSLGGNSHTLMIACVSPADSNLEETLNTLRYADRARKIKNKPIVNVDPQAAELNHLKQQVQQLQVLLLQAHGGTLPVSINSMAPSENLQSLMEKNQSLMEENEKLSRGLSEAAGQTAQMLERIIVTEQENEKMNAKLEQLQQHAVCKLDLQKLLETVEDEELKENVEVIRNLQQVLAQFQSESAAAAEAATEMANAEQDAAGEAETGQVTKRSSDDFTTQHALRQAQMSKELVELNKALALKEALAKKMIQNDSQLEPIQSQYQTNIKDLELEVSNLQKEKEELILALSMAKKDVNQAKLSERRRKRLQELEGQINELKKKLNEQAKLLKLKESTERTVSKLNQEIREMKNQRVQLMRQMKEDAEKFRQWKQQKDKEVIQLKERDRKRQYELLKLERDFQKQASVLRRKTEEAAAANKRLKDALQKQREAADKRKESQNRGMEGVAARVKSWLANEVEVLVSTEEARRHLADLLEDRKILAQELLQLKEKKESGENPPSKLRRRTYSITDLQASEMDLSLSKQIESLETEMELRSAQIADLQQKLLDADNGDRVKQRWDNIATILEAKCALKYLLGELVSSKVQESKLESSLQQSKTNCSDIQKMLIEERNHATEMEAEFQNQLLLQEQQHQQEVLYLLSQFQQKEAPGKGVEDSLSEQEKQMQERLKFQEKELEKMREICEKNQELLQENDVLKQKMLLVQVASGQKLRRDQQVSPESPDSPFDYIPPKPKTRRQTVAKPRAPTPEMNVEELFSDSEESGEEEDAEWVPVKAAKGTKKSATGCFCKGRCGNRQCGCRKQKVGCTAGCSCDSTKCRNRDPGFQDATVCEDQTKDSEGSFKLEDLRDVTAGETFFQPVYSPPTMKVLKDITDQGVFMKKPSTAASLLVRDEESQENQLPFVKKKKRMLSSNTSFFSGCTPIKEEID
The following text describes a protein:
Function:
Causes loosening and extension of plant cell walls by disrupting non-covalent bonding between cellulose microfibrils and matrix glucans. No enzymatic activity has been found (By similarity).
Subcellular Localization:
Secreted, cell wall. Membrane; Peripheral membrane protein.
Sequence:
MELLKRKLYAKILMMVMVIWIAPMTNGHDHASHVPGGRPGAHPSHGAHPAHGAHPSHGAHPSHGAHPSHGAHPSHGALPSHGGQVPHSGWGHGRATFYGDINGGETQQGACGYGDLHKQGYGLETAALSTALFNNGSRCGACYEIMCEHAPQWCLPGSIKITATNFCPPDFTKPNDNWCNPPQKHFDLSQPMFLKIAKYKAGVVPVKFRRVPCAKIGGVKFEIKGNPHFLMILPYNVGGAGAVRAMQIKGTRTQWIAMKKNWGQIWSTGVVLTGQCLSFRLTTSDGVMKEFIDVTPPDWKCNGQSFDGKVNF
The following text describes a protein:
Function:
Monoterpene synthase that catalyzes the formation of geraniol from geranyl diphosphate.
Miscellaneous:
MISCELLANEOUS: Exclusively observed in the geraniol chemotype of this organism.
Subcellular Localization:
Plastid, chloroplast.
Domain:
The Asp-Asp-Xaa-Xaa-Asp/Glu (DDXXD/E) motif is important for the catalytic activity, presumably through binding to Mg(2+).
Sequence:
MSCARITVTLPYRSAKTSIQRGITHYPALIRPRFSACTPLASAMPLSSTPLINGDNSQRKNTRQHMEESSSKRREYLLEETTRKLQRNDTESVEKLKLIDNIQQLGIGYYFEDAINAVLRSPFSTGEEDLFTAALRFRLLRHNGIEISPEIFLKFKDERGKFDESDTLGLLSLYEASNLGVAGEEILEEAMEFAEARLRRSLSEPAAPLHGEVAQALDVPRHLRMARLEARRFIEQYGKQSDHDGDLLELAILDYNQVQAQHQSELTEIIRWWKELGLVDKLSFGRDRPLECFLWTVGLLPEPKYSSVRIELAKAISILLVIDDIFDTYGEMDDLILFTDAIRRWDLEAMEGLPEYMKICYMALYNTTNEVCYKVLRDTGRIVLLNLKSTWIDMIEGFMEEAKWFNGGSAPKLEEYIENGVSTAGAYMAFAHIFFLIGEGVTHQNSQLFTQKPYPKVFSAAGRILRLWDDLGTAKEEQERGDLASCVQLFMKEKSLTEEEARSRILEEIKGLWRDLNGELVYNKNLPLSIIKVALNMARASQVVYKHDQDTYFSSVDNYVDALFFTQ
The following text describes a protein:
Function:
Involved in inositol deacylation of GPI-anchored proteins which plays important roles in the quality control and ER-associated degradation of GPI-anchored proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MCSVLRFQRNMASWVKRHVFTFDLGDIQEKRGSDSGSGQSRSTADRYFNAVFGLGLLLFCIVCMAYLSPFLGSDLPQCRSVTMYPSYALVQGFDRRFSRLGRKYHLYLYREAGKDNGFSDDNEIHLDGIPVLFIPGNAGTYKQVRSIAAATANLYYGEMRDALNNNNTKNLDFFTADFNEDFTAFHGRTMLDQAEYCNDAIRYILSIYELSDKYRASGEPLPTSVLVVGHSMGGIVARVMTTLKNHIPQSINTILTLSSPHSTAPATFDGDILKIYNAMNAFWESKFRDRDKDPFYAENVSVISITGGVLDSVLPADYTSLEGIIPSDNGFTTYTTTIPWVWTPIDHLAIVWCDQLRIVVAKLLLELVDRTSASKTRPLPDRMRLARRSLLSGLESSASADFHLWDNEDYIFQPKVAPGALTTAQEMSPILLNVETYDTLNEYNYLAIPHNEPNLRFSLLTSLENLEELHILFCQNYNEHNSNGPIEYSSRCVSPSQDFIHVPRSFENSKYPSESSVGSASLPFKALHFNQTLLSKYDFIKFRKPSKSSFKDEDFVLVELSTTDWQTTVNCNPFQLLLSSAKFAHNASSAPFIQTFRFPYLSSSLVSYKLDVSYTGENLVFEPFIAQSIDSPFETKWHLRLRDSVTITIHSEAPFIPFESHYDKSVKLRLIAPPDCNINLSLSINWYMTLKFLFIRYRLAVAALPLSLVSFVLANQFALYYSSSFFPDFSTTLRAVTSKFWLKLTLSSILLTPILNISFIQRLIHSLDPSGVNSPFLIRKKNIMTAAYYLGIREIFMCWIGPLLSCITLSLVYMLAFGISTLESCVRRVSCYMSTAISKTRMKEIWLKDECEYEEGLVLRRRIGSGIMILAVVLYVPYQLVFVLLFLVQLNTVIKLNINYFNTKRHSNLRNYNSSYLLLMLCVLPINAPMVFVFLHNFGRRWVTSFRSHHNCLAILPIILLVCDNAGLRIPRSHCIERISKLITIGSFLYLSLYSVIYGIRNLFWAHHLVNLISGWLLFTSLDLTSNN
The following text describes a protein:
Function:
Catalyzes the irreversible cleavage of the glycosidic bond in both 5'-methylthioadenosine (MTA) and S-adenosylhomocysteine (SAH/AdoHcy) to adenine and the corresponding thioribose, 5'-methylthioribose and S-ribosylhomocysteine, respectively. Also cleaves 5'-deoxyadenosine, a toxic by-product of radical S-adenosylmethionine (SAM) enzymes, into 5-deoxyribose and adenine. Thus, is required for in vivo function of the radical SAM enzymes biotin synthase and lipoic acid synthase, that are inhibited by 5'-deoxyadenosine accumulation.
Sequence:
MKVGIIGAMEEEVTLLRDRIENRQTLARAGCEIYTGQLNGIDVALLKSGIGKVAAAMGTTLLLEHCQPDLVINTGSAGGLDSSLKVGDIVVSNEVRYHDADVTAFGYEPGQMAGCPAAFVADEDLIALAENCIQQLKLNAVRGLICSGDAFINGAEPLARIRAAFPTVAAVEMEAAAIGHVCYLFNTPFVVVRAISDVADQASHLSFEEFLVVAAKQSTLMIKAMLTTLAQRG
The following text describes a protein:
Function:
Part of the Sec protein translocase complex. Interacts with the SecYEG preprotein conducting channel. SecDF uses the proton motive force (PMF) to complete protein translocation after the ATP-dependent function of SecA.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MRKEIDFMGKSKIFITISLILIAISIVSIFTKGFNFGVEFTGGSEIIVRFENKEVTENDIRAAISQISEEFANARIVEVRSAGDPSNVQKYSIIVPKTYEPDEKQKIQEEMEKLLSGKVVSFNEISGTAAEEIRRGTWTAILVALVVLLIYITIRFRFIFGVAAVVALIHDVLITMGFFSLFGYEINVAAVAAFLTLLGYSLNDTIVLSDRIRENMRRYRGRNMVNIVNMSINQVLARTINTSLTTFFVVFVLLLFAGNAVKPFAFGMTVGTIVGTYSSLYVASPIIVKWTKQ
The following text describes a protein:
Function:
May be involved in cell wall biosynthesis.
Subcellular Localization:
Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MDEGVSQLVDAYTGLMLCLGCCANIGDDTEAWEFKGNQEQARRYRKLTANDQNTCLSMLVCYCSLAGLSGKLIKSEDQYRPMHASGPDSCTSKYMQHCFWKSTRKPPSSQFLSALREYEALHQRCVQGQNLTETFITGTAPEGCQYLVWKELDGKGNQLVSLVSAFVYSLLTHRILLITPQESLNLLLCEPFPRSSWQVPSGFPYDAMQSKGGSQGDFFQRAQNLTGRGSESLLDTDFKNIPRHLFVSLSNISPPPHHDRRFFCPAEQKLLGRIPWLLFRSNQYMIPGLYFLPEFRKALNHLFPDREVFLHAGRYLLNPSNDIWGRITKFYDGYLAGADKRVGIQVRSWTPEYKPVISDHILKCAVDTNILPNLTRKATAIPTHNSYKKITILMTALTVQYHLDLREHYMRHENVGGESQ
The following text describes a protein:
Function:
Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters.
Sequence:
MSVFETAVFIVQNLPKDGPVKTSTDEKLNFYGLFKQSTHGKCDVPKPSFFDVQGVYKWNAWKKLESMTSEEAKNAYVEAIVQKIRDVQKTYKTEEWMKGDVYDLLAPKFEILGILETKKTEDESEKQEDVLIEQIQKEDCQPKNETVKIQENEESMNSSACVLSDNEYADALDDEIQSRSSSFTEPHTSSRHRVTRQGSPSLRNTCHRLEKELKVITESIDNLGKAVEERHNLLISLMKKSTVYILVPKSTSWKTVMFFVFWPFVANFLLRWLRRFLGYV
The following text describes a protein:
Function:
Regulates the expression of a number of genes involved in biofilm formation and stress response. Target genes include six stress-response transcriptional regulators: csgD, which is a master regulator of biofilm formation, appY, sxy, ycgF, fimB and rcdA itself. This indicates that a large number of genes must be regulated indirectly via these transcriptional regulators. Acts by binding to the upstream region of its target genes.
Miscellaneous:
MISCELLANEOUS: Has a strong cooperative DNA-binding mode, leading to aggregation of RcdA-DNA complexes.
Sequence:
MRRANDPQRREKIIQATLEAVKLYGIHAVTHRKIATLAGVPLGSMTYYFSGIDELLLEAFSSFTEIMSRQYQAFFSDVSDAPGACQAITDMIYSSQVATPDNMELMYQLYALASRKPLLKTVMQNWMQRSQQTLEQWFEPGTARALDAFIEGMTLHFVTDRKPLSREEILRMVERVAG
The following text describes a protein:
Function:
This promotes the activity of RNA polymerase II.
Subcellular Localization:
Nucleus.
Sequence:
MGKSLSLGPNLRYPITITKFLKKHGDQISKQDSLLEYKFKWKLMVGDPLGDQWEEEQTSYGEWDSPAEGTLEKWLIKEGMTIERDGPVVDVEESCSHAVQFAGLCGMCGKDMTEVSWASNALDTDRARINMIHDQTHLTVSHDEASKAEEELQRRLLKNRKLSLVVDLDQTIIHACIEPTVGEWQRDVNSPNYEAVKDVRSFQLNDDGPRGLASGCWYYIKMRPGLAEFLTKISEMYELHVYTMGTRAYALSIAKIVDPGKKLFGDRIISRDENGNVTAKSLARLFPQSTHMVAIIDDRADVWPMNRPNLIKVVPYDFFTGIGDINSSFLPKREGLPKVPTPKKKHHSKSETSTSEIAIETPTGEVAKPTEHQGENKFTEGAQEESSSEKPVLPKLNTLDDESSLQEQAAEQEKFLEQQLLDRPLLHKQEAIDEADKKQEEAGKEVEDGTMEHHTHRHGVLKDDDVELTYLQQHLTDLHRAFYEEYDKALVNVPGGRVAQLKPGHQRKVNVKNEAADLKVVPNIAVVMPRLKSEIAQQIDSFGGKIHKKVSKRVTHVVASSQKTRTQKVREAAKYPHIKIVTQQWLTQSMSKWKKEDESDYLVDISPADRRPSGDMTNVSSPGDDSEESSDYTESDDYDDDDMKSELDGEGVMPDEPRGDISPTKDLNWSSIDDELAEFMGDDESGTESDTSFTSNNSRTSRTSSRRGQKRTFDDATDEDDSEEESTMAKKQRVANSRTTSLKTVKTPTSASESSLLTPGVTGDETDEVDQLSTQESDHSFEDDLEAEMQAAFDQQFEDEAAAAAG
The following text describes a protein:
Function:
Plays an important role in chromosome cohesion during both mitosis and meiosis. In prophase of meiosis, it is involved in the formation of the synaptonemal complex (SC) and specifically, in the diplotene and diakinesis phases of prophase, it stabilizes the association of homologous chromosomes during synapsis and sister chromatid cohesion. It regulates cohesin subunits to promote meiotic chromosome cohesion and localizes non-SMC (structural maintenance of chromosome) cohesin subunits to chromatin prior to or during pre-meiotic S phase. Implicated in influencing either the stability or loading of meiotic-specific cohesin subunit, rec8. Controls cell cycle exit and cell fusion to prevent the premature differentiation into adult cells. Specifically, regulates hypodermal seam cell identity.
Subcellular Localization:
Nucleus.
Sequence:
MNVLVQGAVHALGYYEDGKYSREPDCYESIRDLIRYLREDGDDHTARIECGRHNLVEQDLVPMVKCEDLTDDEFDIAIRLMVNLCQPAISTMRGKPPADRDQWKMYWELEENLRRAKTAFSDAHFFTAIKKRIDNYFIDTEYEDRDERLRLVVERIVLLIKYVFSINPDTSEGRRTRIEDSSHDRVIIAFLESGIDKTLMHIANQPREKEFHVTILDIFALILKEQTAEDLATKSEEVSTAEQKKTEEEFRKIIENHVVKETQKRKSFSRFGGSYTIKGLKGISANSSQVVFKPIQNVEKHNFLDDRKAKKRAPRNRRPFEIDTNSHFASSEVRGMLRDMVIRIIETCFNRLMKSSKTTVFVQVQKTSQINYFFLIKFVLRFVRLSRQDHLLERISECIGVEAFHENNVQLTEYVENATTLKGVEAKSHGLKAQYALGAYNELVLLHRYIYEHAKEENERKFAKRALEHIVNVEEYRELPIFIIKKFSSSVLSNNFLRELVLTTHHYMKLVERFVKTGALKKVTKKVKVRKATKKSKMSEEDVRSEFDGMSKKDLDRLWEESKGLVLQILKKEVPEMRGMNPIDSQLDVPVDAQQKFAKLSIQRSLRSRGFPAAVGLYHASRALWPESFKRGLTDFQDSPGEEDQLQELEQLLKADMKKVAKDLKKAESCKTCDEDPAYKKYDKMDATALQSLWEQSTDTLARILSHELPESESTSPVNWQLDITPDVQQKFAMLAIQRALRARDLPAAVGLYHTSRKLWPGDEAIFGAPGIGVEEEIAELKAILEADLHEVAREMKVAEDRAEDPDEEDPAEPYDSEQEEEEEVPAWKVEEIDFQFDSYVCKFSNVDVLKWYVFLLNDFSKNSTELNQALVKMLHRIAFDLKLPIKLYQVSLFQVFSKVNEHFTHLSKDLRKSSRLYELYQFGFHLLKKFFSKFTGDLAIEALFWKGPRECFEIENGYGSWVKSREADIRVWTEDLEIELRNLYEEYRTMETRDGIDVLDFIEHNLSRARSRKKVAKKLIEFGFDLLGAKWKNSDKARMDSVLPIGDIQKWYDEWKEAGARGDLVNVLQEKLNEDLGMEISRKKILKQLAHMDILYEKPKKEKPLPQWDTGLIEELKKLKEQYDDIPDALNMLGVNIVRYVMKRLSEKKPTRQVERHLESLGATIPERSKKSEKNGKKFDDFLNDDDDDSENDVGGGSEDDEEEEIVMKSKRIIPDSEDEEEHIEQEEAQKKLEKVAEKPNTLMGMIAGRKRKLAQLESDSSDESDDDDSAEKEEKKLPAAEDDSDLEEDAVIYKRSYVDALLTGGSIAGNGITETRRDTSEEREDDDDEDPFTKKLTFKRRIVMSDNEDEA
The following text describes a protein:
Function:
Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate.
Sequence:
MYKVLITDPIAPEGIELLQKDPEVEVYNEPDISYEELLEIIKDFDAIITRSRTPVTKELLERAEKLKVVGRAGVGVDNVDIEEATKRGILVVNTPGANTIGATELTMMHMLTIMRNGHKAHESMLNYKWDRKKFMGEELYGRILGIIGLGNIGSQVAIRAKAFGMKVMAYDPYIPREKAEKLGVKLVDNLHDMLREIDVLTIHAPLTHETKNMIDEKEFEIMKDGVYIVNCARGGIINEKALIKYMESGKIKGVALDVYSKEPPPPEFIDELKRLADKVNISLSPHIGANTYESQRNVAVIVAQQVLKALKGQTVEYAVNAPFPDLSVLTLIKPYLDLAEKLGKFLVQWTEEGIREVHIEVRGDIAEYFQPISSAVLKGILEEVVDFPVNIINAFYVAKDRGIKVEELSSEETPDFKHYIKVVVKADGKEKVVAGTVLEGQIPRITEIDRYKVDIEPEGILLVFENKDVPGVIGKIGSILGEANINIAGFRLGREKKGGIAIGILNLDEPASEEVLSRIKEIPEILFVKHIVL
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MEEEKLAEISGVCLPLASLRLLVPPLHLLSSFMWQVLQHKSLVHYGKLEELVCVLTEALPQLMAFRQRVQLMLGLRARMVLELCRGAADSRIMQTQLDRMQIPAAPAGHTGPDADLWASVSNFKALVSALLKDPVEKAYFFQEVFPVEYGDRFDTALKELMWELLSCLEKLLPVPEFRQTVSWLSAAPVGLEECVRIDSKHLQLLLQNHQLFSGSETPKGKLGSRSSGECIVSSLSVPPSARMCVSSEPLLLHVQPAAVTILSSDTIIVTDYTEVELTEELMEPMQEEESGGEEQEPTAEQHSCTNPPPPQQNNTDPPPPQQNNTDPPPPQQNNTDPPPPQQNNTDPPPPQQNNTDPPPPQQNNTDPPPPQQNNTDPPPPQQNNTDPPPPQQNNTDPPPLQQNNNDPPPPQQNNTDPPPHCAQHPPQEHTHITQKLPGQTDITQKPPGQTDITQKPLGQTDITQKPLGRRGRGRQRKSTEPMGKTGGGAAEELRAGAPHGQDREGCADPAAPLATSEPSSASCRTRRSSKAAPPVAANPRARYACDICGRKFTRRSDVQRHQLTHTGERPFHCGQCQKTFQHSWDLSKHCRKQHGEARFSCSVCQSDFTNLRLLTAHHKQSHGGAVPHYCSICGETAGSPSALAQHRRSHSAAQLYRCPQCGEAFDTLLQRSLHRQSHRPRQRHQCPQCPKSFTRSSDVRRHQLSHSGERPHHCTVCGKSFGLRSGLLKHQATHTGERPHCCTVCGKSFTQLSILLRHQRMHTGERPYLCSQCGKRFLSLGELLKHDKTHAEDRPHTCPQCPKSFKYKRALQEHMLAHTGVRPYPCRYCGKMFAKPFALNRHHLIHTGERPFSCAHCERTFLTSTELALHERTHTGERPFPCTACPRRFRSSSELARHRRTHSGPRPHACRYCPKAYSSASRLRSHTRTHTSEKRSGGPHVEVHVTLTE
The following text describes a protein:
Function:
Required for box C/D snoRNAs accumulation involved in snoRNA processing, snoRNA transport to the nucleolus and ribosome biogenesis.
Sequence:
MDNLLVSYNDSDESDVEENIESYKNELESRASTILKESIENHEISINENGEITIELNKHNNNNNNNNNNNNNNNNNNNNNNNNNNNNNKVNEINNVNSKKRNIDSLYKDDSETTTTTTTTNNEENNTKIGKIGDICNVCTIEKSKYKCPGCSILFCSLICSNKHKIDTKCTGVRKDNHFIPLNKFKDSDIVNDFNFLDKINRVNENGKAIVANSFIKFKSKHLQQFAFRKNINLYIMPKEMSRHKENTTSFKKPKNLLLWRIEWLFLDDDFKWSDPSIQDSMIMNDLLQKHIDDPVNIYNLKNNLKKLNSNRDYRNPNENFTVLMKRERDSKNQYYRFDLTKTFDENFQFKEIIEFPTLLVFTNNSKNLSNYNIISLEDQSIIEKQQLEIIKANLSFKTKYDPNLTNTEDQSKRFKPNNNNNNNKNGNKKNDRFKNKNNNNNNNNNNNNNNNNNDDNDNNNNNNKDNE
The following text describes a protein:
Function:
Mannosyltransferase involved in glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MWPQDPSRKEVLRFAVSCRILTLMLQALFNAIIPDHHAEAFSPPRLAPSGFVDQLVDGLLGGLSRWDAEHFLFIAEHGYLYEHNFAFFPGFPLALMVGTELLRPLRGLLSLRSCLLISVASLNFLFFMLAAVALHDLGCLVLHCPHQAFYAALLFCLSPASVFLAAGYSEALFALLTFSAMGQLERGRVWTSGLLFAIATGVRSNGLVSVGFLMHSQCQGFFSSLTMLNPLRQLFKLMASLFLSVFTLGLPFALFQYYAYTQFCLPGSARPIPEPLVQLAVDKGYRIAEGNEPPWCFWDVPLIYSYIQDVYWNVGFLKYYELRQVPNFLLAAPVAILVVWATWTYVTTHPWLCLTLGLQRSKNNKTLEKPDLGFLSPKVFVYLVHAAVLLLFGGLCMHVQVLTRFLGSSTPIVYWFPAHLLQDQEPLLRSLKTVPWKPLAEDSPPGQKVPRNPIMGLLYRWKTCSPVTRYILGYFLTYWLLGLLLHCNFLPWT
The following text describes a protein:
Function:
Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly (By similarity). Also involved in the nuclear import of the histone H3-H4 dimer together with importin-4 (IPO4): specifically recognizes and binds newly synthesized histones with the monomethylation of H3 'Lys-9' (H3K9me1) and diacetylation at 'Lys-5' and 'Lys-12' of H4 (H4K5ac and H4K12ac) marks in the cytosol (By similarity). Does not participate in replication-independent nucleosome deposition which is mediated by ASF1A and HIRA (By similarity). Required for gonad development.
Subcellular Localization:
Nucleus. Cytoplasm, cytosol.
Sequence:
MAKVSVLNVAVLENPSPFHSPFRFEISFECSEALSDDLEWKIIYVGSAESEEFDQILDSVLVGPVPAGRHMFVFQADAPNPSLIPETDAVGVTVVLITCTYHGQEFIRVGYYVNNEYPDPELRENPPPKPDFSQLQRNILASNPRVTRFHINWDNNPDSLEAIENQDPNVDFSLSLSCTPVKSLGLPSCIPGLLPENSMDCI
The following text describes a protein:
Function:
S-adenosyl-L-methionine-dependent protein-lysine N-methyltransferase that monomethylates 60S ribosomal protein L1 (RPL1A and RPL1B) at 'Lys-46'.
Miscellaneous:
MISCELLANEOUS: Present with 468 molecules/cell in log phase SD medium.
Sequence:
MAFKLWLLDEETIYEHVFERYTQLEGQSGKLAQDLGIQDRRGGVLEITFEPSGLEGGRKKKRVRRRNKASSVEEDQNVAVDSYHVSVGQSISSLRSSRDNGNSTTGYVLWSTTPFFINWLLYSTSAAPFRLGSQVEVTCGSSCEGHKLELPRLVDLTGADRGKRGILELGAGISGILPVILGNFVDTYVSTDQKGILNKLKDNIMENLSQLTRKRCISRSLRLELPTVEPVGDADITAASLPSKSTLHLEVAALDWEKINLQDKKTHSLHPELSLIGETCSSVYVIAMDVIYNEYLIDPFLKTLKQLKHWLQTTYNLQFHVLVGIHLRSQEVTTLFLEKAIIEYDFTVYDIVDQVIQESRFNFYLIT
The following text describes a protein:
Function:
Involved in the unfolded protein response (UPR) during endoplasmic reticulum (ER) stress. Acts as a negative regulator of the EIF2AK4/GCN2 kinase activity by preventing the phosphorylation of eIF-2-alpha at 'Ser-52' and hence attenuating general protein synthesis under ER stress, hypothermic and amino acid starving stress conditions. Co-chaperone of HSPA8/HSC70, it stimulates its ATPase activity. May inhibit both the autophosphorylation of EIF2AK2/PKR and the ability of EIF2AK2 to catalyze phosphorylation of the EIF2A. May inhibit EIF2AK3/PERK activity (By similarity).
Subcellular Localization:
Endoplasmic reticulum.
Domain:
The J domain mediates interaction with HSPA8; Binding to misfolded proteins is mediated by a hydrophobic patch forming a large groove within the first two TPR repeats.
Sequence:
MVAPGSVTSRLGSVFPFLLVLVDLQYEGAECGVNADVEKHLELGKKLLAAGQLADALSQFHAAVDGDPDNYIAYYRRATVFLAMGKSKAALPDLTKVIELKMDFTAARLQRGHLLLKQGKLDEAEDDFKKVLKSNPSENEEKEAQSQLVKSDEMQRLRSQALDAFESSDFTAAITFLDKILEVCVWDAELRELRAECFIKEGEPRKAISDLKASSKLKNDNTEAFYKISTLYYELGDHELSLSEVRECLKLDQDHKRCFAHYKQVKKLNKLIESAEELIKEGRYTDAISKYESVMKTEPGVHEYTIRSKERICHCFSKDEKPVEAIRVCSEVLQVEPDNVNALKDRAEAYLIEEMYDEAIQDYETAQEHNENDQQIREGLEKAQRLLKQSQRRDYYKILGVKRNAKKQEIIKAYRKLALQWHPDNFQNEEEKKKAEKKFIDIAAAKEVLSDPEMRKKFDDGEDPLDAESQQGGGGNPFHRSWNSWQGFSPFSSGGPFRFKFHFN
The following text describes a protein:
Function:
Catalyzes the transfer of a geranylgeranyl moiety from geranylgeranyl diphosphate to both cysteines of proteins with the C-terminal sequence -XXCC, -XCXC and -CCXX.
Sequence:
MTEHMFLSGLYFGKCALAAAGQDDHLAAQKVRIHACRRDDGGYAGNEVYPSHLLYTYSAVQLAILYNQPELLDADALEAFVWSRLLPSGAYYGNDPSDTDTRFSYCALATLALVDKLQPEAINVRQAGEFVLACQNDDGGFGLRPGCESHAGQTFCCVAALQLCGLLEKANHDTLKGFLLRRQQADGGFNGRPEKASDGCYAWWVLATMAILGPSVLGAIDKAAAIKALFRLQTPAGGFSPRPDESPDLFHTHFAIAALGVLGHESVAPMDPCFCVPRTALQRYRRSLDQTQATTTDAS
The following text describes a protein:
Function:
May be involved in several stages of intracellular trafficking.
Subcellular Localization:
Endosome membrane; Peripheral membrane protein. Note=Detected in endosome-derived secreted vesicles (exosomes) from malignant pleural effusions.
Sequence:
MDKALKEVFDYSYRDYILSWYGNLSRDEGQLYHLLLEDFWEIARQLHHRLSHVDVVKVVCNDVVRTLLTHFCDLKAANARHEEQPRPFVLHACLRNSDDEVRFLQTCSRVLVFCLLPSKDVQSLSLRIMLAEILTTKVLKPVVELLSNPDYINQMLLAQLAYREQMNEHHKRAYTYAPSYEDFIKLINSNSDVEFLKQLRYQIVVEIIQATTISSFPQLKRHKGKETAAMKADLLRARNMKRYINQLTVAKKQCEKRIRILGGPAYDQQEDGALDEGEGPQSQKILQFEDILANTFYREHFGMYMERMDKRALISFWESVEHLKNANKNEIPQLVGEIYQNFFVESKEISVEKSLYKEIQQCLVGNKGIEVFYKIQEDVYETLKDRYYPSFIVSDLYEKLLIKEEEKHASQMISNKDEMGPRDEAGEEAVDDGTNQINEQASFAVNKLRELNEKLEYKRQALNSIQNAPKPDKKIVSKLKDEIILIEKERTDLQLHMARTDWWCENLGMWKASITSGEVTEENGEQLPCYFVMVSLQEVGGVETKNWTVPRRLSEFQNLHRKLSECVPSLKKVQLPSLSKLPFKSIDQKFMEKSKNQLNKFLQNLLSDERLCQSEALYAFLSPSPDYLKVIDVQGKKNSFSLSSFLERLPRDFFSHQEEETEEDSDLSDYGDDVDGRKDALAEPCFMLIGEIFELRGMFKWVRRTLIALVQVTFGRTINKQIRDTVSWIFSEQMLVYYINIFRDAFWPNGKLAPPTTIRSKEQSQETKQRAQQKLLENIPDMLQSLVGQQNARHGIIKIFNALQETRANKHLLYALMELLLIELCPELRVHLDQLKAGQV
The following text describes a protein:
Function:
Subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments and in some cell types, is targeted to the plasma membrane, where it is responsible for acidifying the extracellular environment. Subunit C is necessary for the assembly of the catalytic sector of the enzyme and is likely to have a specific function in its catalytic activity.
Sequence:
MVYYLIGAPHKSNEQTAWLETEKHVLTSGISRQAKGRILQTEIGKFKLGNLDHLMFINDSLLKQESVVESLLKKIERQYLDVTEKVSYDFIIELKEGPQSIENFLFQFKWNDQTFPRASALSELVKAISSRATHVETDLRQKSTSYQELKNQSQQVARKEGNLMVRDLVDVLKEPIVKPRDFIYSDYLTTLVAIVPKTQIQEWLACYEFLCENVVPQSARQFQIEDKDNLTIWRVVIVRQSFDKDHDIEVADKGDDDKGKKQRQTPVEEFIQKARDKLRITVKEFEYKSQESKEREKLRLDLKSKSDHMNTTLKQACEKAFSDLYITYMHLKVLRLVVDIAMRFGAAEPNIQCILKPDQGKEKKVQQSLLKLFADPSQVGLYGTKEELEDTEDFFPFVYVPINIP