lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis. In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes (By similarity). When secreted, interacts with NK cell-activating receptor NCR3/NKp30 acting as an inhibitory ligand which antagonizes NK cell attack (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Secreted. Note=Secreted by a non-classical secretory pathway and associates with the cell surface. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion.
Sequence:
MADSFSLNDALAGSGNPNPQGYPGAWGNQPGAGGYPGAAYPGAYPGQAPPGAYPGQAPPGAYPGQAPPSAYPGPTAPGAYPGPTAPGAYPGQPAPGAFPGQPGAPGAYPQCSGGYPAAGPYGVPAGPLTVPYDLPLPGGVMPRMLITIMGTVKPNANRIVLDFRRGNDVAFHFNPRFNENNRRVIVCNTKQDNNWGKEERQSAFPFESGKPFKIQVLVEADHFKVAVNDAHLLQYNHRMKNLREISQLGISGDITLTSANHAMI
The following text describes a protein:
Function:
Chondroitin sulfate- and hyaluronan-binding proteoglycan involved in the organization of interphotoreceptor matrix; may participate in the maturation and maintenance of the light-sensitive photoreceptor outer segment. Binds heparin.
Subcellular Localization:
Photoreceptor inner segment membrane; Single-pass type I membrane protein. Photoreceptor outer segment membrane; Single-pass type I membrane protein. Secreted, extracellular space, extracellular matrix, interphotoreceptor matrix.
Sequence:
KKMFSFSWKTSLSILIFVLIEGGHQTAQTYLPSGKIQESRVSVSPYRMSLQSSEEKPLDYRKNKWQRLFRQKRTTLFPNGVKICPDETVAQTVANHLKYFKVRMCQEAVWEVFKTFWDRLPRREEYGHWMTLCEEGTISIFEMGTNFSQSEEHQSLITKVGPEERYTVSFVYTDTAANASSPRVASFQDFSDSDSERPDDSINNEIETLTETPPKLATEQVAEFIMHLSGKEYIEELQDPSSRHHQELTQQFISEVEKSFDGLPGYKDIHVLEFSRFFFFLLNLSGIDVRYAVTFDSEAISNITWEMINLHSNKVENHGLVERENKPTAVYTINNFRDYIAESLNRNFVLGNSSLKPDLDSLQFINVKDVFFPQTEDPLWNVGSPSLLVTQPLILDKTLQAEWPSADESAARSSSPLDFTKPGLIFGTLPSTGSELWPKSESPPPDLVSPSKLPLPWKVGSTSPPEVLEGSSLTLHSVTPAVPQTGLPLAPEKRTSGPVLLGEGPTNVEEPGDFFPFDLLTSNPPSHLVPMPSVDDSELPLSSLSTLASPSMLDSIDIEITTPFGLDPLASPNKDQLEANIFQPETYPESGPIFESQSGSGSGHELLPGPWSKPSLHHGTGPPSESWFENEESTVAFVSTNDRLEKIEFSQEEKPKEILESSSTELSDIDVSTGKSSMELLWTGLSKFNVTQSTTSFPRRPTKDTLASTAKNIDTLLSRVSISESTKLSPTLSSTNLEDDMIMNVQDISLELDPVGTGYYQPELNQEESSKMPTNMPSTERAYPNYSQTKGPLVVFFSLRVMNMLFSEDLFNKNSPEYKALEQRFLELLVPYLQSNLTGFQNLEILNFRNGSIVVNSRVKFAKPVPHDVNNAVYTILEDFCNTAYQTMNLAIDKYSLDVESGDQADPCKFQACNEFSECVVNRWSGEAECICYPGYQSLQELPCQSVCELQPHFCLNDGKCDIIPGHGAICRCRVGENWWYRGEHCEEYMSESQVIGIAVASVIGFLLVVMAVLFFLAKTLVDHDSISPFCGRDQNDCPSSLENAVRYNPVFESDVTGYDQYGRSYPQLTSYSPALGEEPADLSREEIRQLYEHSELSSEEIQERIRMFELYAKDQQFAEFVRQHQM
The following text describes a protein:
Function:
May be required for DNA interstrand cross-link repair. Also required for checkpoint mediated cell cycle arrest in early prophase in response to mitotic spindle poisons. Possesses beta-lactamase activity, catalyzing the hydrolysis of penicillin G and nitrocefin. Exhibits no activity towards other beta-lactam antibiotic classes including cephalosporins (cefotaxime) and carbapenems (imipenem).
Subcellular Localization:
Nucleus. Note=In some cells it may be found in typically 1 or 2 discrete nuclear aggregates of unknown function which also contain TP53BP1. Also found in multiple discrete nuclear foci which increase in number following treatment with ionizing radiation or interstrand cross-linking agents. These foci overlap with those formed by the MRN complex (composed of MRE11, RAD50 and NBN) and BRCA1.
Sequence:
MLEDISEEDIWEYKSKRKPKRVDPNNGSKNILKSVEKATDGKYQSKRSRNRKRAAEAKEVKDHEVPLGNAGCQTSVASSQNSSCGDGIQQTQDKETTPGKLCRTQKSQHVSPKIRPVYDGYCPNCQMPFSSLIGQTPRWHVFECLDSPPRSETECPDGLLCTSTIPFHYKRYTHFLLAQSRAGDHPFSSPSPASGGSFSETKSGVLCSLEERWSSYQNQTDNSVSNDPLLMTQYFKKSPSLTEASEKISTHIQTSQQALQFTDFVENDKLVGVALRLANNSEHINLPLPENDFSDCEISYSPLQSDEDTHDIDEKPDDSQEQLFFTESSKDGSLEEDDDSCGFFKKRHGPLLKDQDESCPKVNSFLTRDKYDEGLYRFNSLNDLSQPISQNNESTLPYDLACTGGDFVLFPPALAGKLAASVHQATKAKPDEPEFHSAQSNKQKQVIEESSVYNQVSLPLVKSLMLKPFESQVEGYLSSQPTQNTIRKLSSENLNAKNNTNSACFCRKALEGVPVGKATILNTENLSSTPAPKYLKILPSGLKYNARHPSTKVMKQMDIGVYFGLPPKRKEEKLLGESALEGINLNPVPSPNQKRSSQCKRKAEKSLSDLEFDASTLHESQLSVELSSERSQRQKKRCRKSNSLQEGACQKRSDHLINTESEAVNLSKVKVFTKSAHGGLQRGNKKIPESSNVGGSRKKTCPFYKKIPGTGFTVDAFQYGVVEGCTAYFLTHFHSDHYAGLSKHFTFPVYCSEITGNLLKNKLHVQEQYIHPLPLDTECIVNGVKVVLLDANHCPGAVMILFYLPNGTVILHTGDFRADPSMERSLLADQKVHMLYLDTTYCSPEYTFPSQQEVIRFAINTAFEAVTLNPHALVVCGTYSIGKEKVFLAIADVLGSKVGMSQEKYKTLQCLNIPEINSLITTDMCSSLVHLLPMMQINFKGLQSHLKKCGGKYNQILAFRPTGWTHSNKFTRIADVIPQTKGNISIYGIPYSEHSSYLEMKRFVQWLKPQKIIPTVNVGTWKSRSTMEKYFREWKLEAGY
The following text describes a protein:
Function:
Catalyzes the sodium-dependent transport of glutamate.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MPTLHLDALSTTALALLLLALGSQLKKRSRWLTRLCVPSPVIAGFGFAFLVWLLRDRGWLDIGLDTSLQTPLMVAFFTTVGLGGSLGLLRKGGKTLLVYLSACWALAILQNLIGVGSAGLLGLDPLLGIMAGAVSLEGGFGAAAAFGPVAEGLGAQGATTVALASATFGMVAGGLLGSPVARWLIERNRLPVQAESDNRLEALGQQERRQHAAATLDGNLLLRLLTCVLLVMVLGFWLGDALEERLGLVLPSYVGAMFIAIVLRNLDDRLGWLRIPDHAVGTLGDVCLGIFLTMAMMSLKFWELENLGLPLLGVLFIQVAVLLLLTIFVLFRLLGRNYDAAVLCAGFLGHGLGATPNAVANMGAVCEHYRVFSHKAFIIVPLCGAVLIDLVAIPAITWFINAFS
The following text describes a protein:
Function:
Catalyzes the ATP-dependent translocation of sphingoid long-chain bases (LCBs) from the cytoplasmic site toward the extracytoplasmic side of the membrane (flip-flop). Involved in the establishment of the functional lipid asymmetry of the plasma membrane. Regulates intracellular levels of LCBs, sphingolipid precursors that are growth inhibitory at increased levels.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MDGVSLLNQYLPSWTPTSLPTSTSISTINPTNTAGLALTLLELQNAIQTETNTISLYFLSRAARGVAASYTIISGQQYLATATATQDFPEVTSAMVNATLSLKQLEWKANLYAINLSVPFNAFFAAMFGVTLICLLGIGFSTKTKYFTICLACGTILEVIGYVARTLAHYSWSDPNLFLCQIVSLTVAPAFIMAGVYYLLSQMIIIHGEQYAILKPIMVSIIFIFCDVVSLFVQASGGAAAAVSLRSFKDTELGTYIMVGGIGFQVVSMTLFLYFLFDFVYRSFFTANSNIKYSFSTYCSLLFNTKKGRLLRQDLEPFYDVGYKHIRQRSLFNYMPLVIIISVGFIYIRCIYRVIELSEGWRGYLITHEEYIFALDALMVLLTCITYVFFHPGLVFGKQMTAQISVSANKSESAADHESHCGNSRMYNYSKNHSNSPQSSHDEKFIMDQRQKYYNPYFLPTKFSQYNSHSCPSSETYTYSSYNSKLETKSESSWQNS
The following text describes a protein:
Function:
Polycomb group (PcG) protein. Catalytic subunit of some PcG multiprotein complex, which methylates 'Lys-27' of histone H3, leading to transcriptional repression of the affected target genes. PcG proteins are not required to initiate repression, but to maintain it during later stages of development.
Subcellular Localization:
Nucleus.
Sequence:
MASSSKASDSSSQRSKRSDQGTGRDAAAASVVAIHGKLTQLVRQIQSKRLAHIKDKLEANRKTLQRHTCALFDVAAATEVASRGTEGGNALSQRAAEFQSRPAGSDLANGMGERDVVYVQEENPAAGTLVLSGSGSGGAAQRTVLRFVKLPLIERIPPYTTWIFLDKNQRMADDQSVGRRRIYYDAAGDEALICSDSDEEIPEPEEEKHFFTGGEDQLIWKATQEHGLNREVVNVLSQFIEATPSEIEERSEVLFEKNEKHSGSSDKIQRQLSLGKTMDAILDSFDNLFCRRCLVFDCRLHGCSQNLVFPCEKQPYSFEPDENKKPCGDQCYLRRREGFQDAHYDDLGGCATYTMESRTASHKVDVNILSESEDSNREEDNIKSMTFVGTSGSKIISSMSAEKSTTPPSADTSETENVSSDLPLSSLGKHKISKHGPRYRERSPGKRQKVFTSDVSFASNILNKLSIPEIRDTRLESRESGGDKLRILDESTKKSSSKDIWGGSTTSTTENVGRDSNNVTSTKNFMEHTLSCWSPLERDLYLKGIEIFGKNSCLIARNLLSGLKTCMEVANYMYNNGATMAKRPSKSTLGDFAETEQDYMEQDMAARTRIYRRRGRNRKLKYTWKSAGHPTVRKRIGDGKQWYTQYNPCGCQQMCGKDCPCVENGTCCEKYCGCSKSCKNKFRGCHCAKSQCRSRQCPCFAASRECDPDVCRNCWVSCGDGSLGEPPARGDGYQCGNMKLLLKQQQRILLGRSDIAGWGAFIKNPVSKNDYLGEYTGELISHKEADKRGKIYDRANSSFLFDLNDQFVLDAYRKGDKLKFANHSSNPNCYAKVMLVAGDHRVGIYAKEHIEASEELFYDYRYGPDQAPAWARRPEGSKKDEASISHHRAHKVAR
The following text describes a protein:
Function:
Functions as a negative regulator of the PI3 kinase/PI3K activity associated with endosomal membranes via BECN1, a core subunit of the PI3K complex. By modifying the phosphatidylinositol 3-phosphate/PtdInsP3 content of endosomal membranes may regulate endosome fusion, recycling, sorting and early to late endosome transport. It is for instance, required for the delivery of cargos like BST2/tetherin from early to late endosome and thereby participates indirectly to their degradation by the lysosome. May also play a role in aggrephagy, the macroautophagic degradation of ubiquitinated protein aggregates. In this process, may regulate the interaction of SQSTM1 with ubiquitinated proteins and also recruit MAP1LC3C. May also be involved in maintenance of normal mitochondrial structure and organization.
Subcellular Localization:
Cytoplasm, cytosol. Cytoplasmic vesicle, autophagosome membrane. Early endosome membrane; Peripheral membrane protein. Late endosome membrane. Lysosome membrane. Mitochondrion.
Sequence:
MPAVGCPQQPRTQGGSGAAGTCPARGHRDRGATMDALLRSVEKDLSINRWQLAAASDGTHVTALVPHKWLANLRERRALPALCPRPEGLSEVEVRTFLQRSVQKLPAGWTRVEIHGLCKERLTWPLRVPPVADPRGGGAETLHGFMQRVASQNYRNLWGRAHCLYVRPYRHAHAPPAVPVLDALRAALQKAYGCPILQVGRSVPSASPAKGISSVPSSCPNVLQAEALLESAEMLYIIYPYVQYCLHDIVTFSPAKLTNSHAKILFLLFHVLQAMRACHQAGLACGAFSLRDVAVDEKLCSRLRVNFREYEGPRKEETNAEADLERVNEQSGAGMRGDVARCYTCQQELRDLVLQWVHGRVSNFDYLMHLNSLAGRRMGDPNYHPVLPWVVDFTTKNGKFRDLRKSKFRLNKGDKQLDFTYEMTKQAFVAGGSSGEQLHVPHHISDVLSDITYYVYTARRTPKSVLCCHVRSQWEPNEYPASMERMQSWTPDECIPEFYTDPSIFRSIHPDMPDLDVPSWCSSYEEFIEVHRMLLESREVSQDLHHWIDLTFGYKLQGKDAVKEKNVCLHLVDNHTHLTTYGVVQLFDQPHPRRMVGPACTPAEAPAIARPLLQNIKETVILEDIPCPVTDAVNGLVLEATPTETTWSGEKPITGEDDLEQGTEALDSISVSSRAPDQPCSSSAQPSTLPAYPTEGKASGVRPLRRSKAGAADQADRDDMKITLPEGFNPLQALEELEKLDNFLVKGLSSDMQLMEQPGEEPLLGLSDLFQRDMQALGILIAEIIFAPRIRPSKPDASLLERFLMVRNLCRYHPKEIPAPLQHVLHILLQLSVPVEKLLKTRLGKDTVQLFEYKPISQGLPPPCPTQLLSPFSSIIPFPTYFPALHKFIFTYQAKKIEDEGQGRELVFQLWQQLEGILSEITPEGLEILLPFILSLMSEENTAVYAAWYLFEPIAKSLGPKNANKYLLKPLIGAYETPCSRHGRFYLYTDCFVAQLIVRLGLQSFILNLLPHILQILVGIESSREESKSLLGAAEDDESGGGSPMSCMFGEEIKMDVEHSSTALDLLDYTSGVSFHDQAYLPESEDFQSGLYVGESLQPQEQESLSLGRLSDKSSASEVSLGEDRPADGDSQKDKSSLKSVDSSQDLKQSEDSEEEEEEREEEERDDTAVDAELVGAVDVGVSVDAGTSVDVTLADDGSEPEDGEGEELPDHSDDKEQTILLDTACKMVRWLSAKLGPTVTSRFIARNLLRLLTSCYIGPTRQQFVPSNDENGPLSTGNIYQKRPVLGDQVSKPVLACLLHVAYLYGEPVLTYQYLPYISYLVAPGSGSGGGRLNSRKEAGLLAAVTLTQKIVVCLSDTTLMDILPKISQEVLLPVLGFLTSLSVGFPSGAQARVVLCIKTISLIALICLRIGQEMVQQHLSDTVRNFFGAFSLLQELQDQGLTAESLSGCEVPVMEVPLREGKLLALDPAVLLELQKVFNPEMAYITYIPFSCLLGDVIRTVVPNHSLVEKLASLYLENVNPKNLQVVGLEQAPSMAGSDQDMRGTEAFSSPQEDSHSGTFGSVLVGNRIQVPVDTQREGLGLLRLSAGTDGFIPSSSSEENTLKHDLPRSTHVLCGNWLAYWQYEIGVSQHDPRFHFHQIKLQSFSGHSGAIKCVAPLSSEDFFLSGSKDKTVRLWPLYNYGDGTSEVPPRFTYSEHKKSVFYVSQLEASQHVVSCDGTVHIWDQFTGKLIRTFDELDSKAPITAVTTMPPPYHSISVASADSVLRFIDHRKPGLQHEFRLAGGVNAGLIRCLAVSPNGRSVMAGFSSGFIVLLDTRTGLIMRGWPAHEGDILQIKAAEGNVLISSSSDHSMTVWKELEQKPLHHYKSASEPIHAFDLYGNEVVTGTVANKIGVYSMLESSALPVSTTKLSSENFRGTLTSLAVLPMKCHLLLGSDNGVIRLLA
The following text describes a protein:
Function:
Necessary for the splicing of pre-mRNA. Has a role in the recognition of the branch site (5'-UACUAAC-3'), the pyrimidine tract and the 3'-splice site at the 3'-end of introns.
Subcellular Localization:
Nucleus.
Sequence:
MENKQFAVRDDEENSHKENKNRSGKPFNGGKHLERENLQVSEKSNDLTDNFQVCPLIILGRNCPSSEDEFKDGVSLGRSRVVIEHETRRDEENLQDRKKSKISTDNLQVSPVTSPSLNVPSAECKWRSLERSSVVINQEMGRDGENDRTHKLDSSENSKTLEKDGETQENTGSSGKRRRSTWELESKEGEKDLVEGEGAGKRRKSGWAEDDTKIKMMGPIKLPDFVEELAVGLENDPEVQALNAQLLEINRKLRSGVVLYENKPYEPKSPSPEPIYDNLGIRINTRDCRAREKLTKERQEVISRLVQKNPSFNPPVDYKPSKLYNKLYIPVKEYPDFNFIGFLLGPRGNTLKRMERETGARIVIRGKGSVKEGRALQKHHVKLESLHDEDLHILVEADNQQSLDAAVSILEKLLNPMNGGRNKHKHEQLKELSLINGATRGKDFVRLYKEKGHKEYACPNRNSTFKANVFCLLCRDSGHLTVGCPLKCSNLGTQIDKEYHSCLLENGGGLGWPINVTRAHKAPRFALGSTLTFDHKPKKEIDISKLYVSYLHPFMNSEHLIELFAPFGQIEDAIVIKDRVTGASKGYGFVKFVYAVSAFQAITCMNGFRIGGKTLAVRVAGWPPHTSVVLMIQHSGFLHHFAKGGNDDKLGFSSSFDKVGSGRGLGFPFPFGKGAMDIGLEFSSSLGKDGFDSKGSNDNELFFFP
The following text describes a protein:
Function:
Required for the function of some acidic activation domains, which activate transcription from a distant site. The exact mechanism of action is not yet known (By similarity). ADA2 stimulates the acetyltransferase activity of GCN5 on free histones or nucleosomes, probably by opening up the promoter region. Mediates auxin and cytokinin signals in the control of cell proliferation and might be involved in repression of a freezing tolerance pathway at warm temperature. Involved in the positive regulation of salt-induced gene expression by maintaining locus-specific acetylation of histones H4 and H3.
Subcellular Localization:
Nucleus.
Domain:
The middle domain of ADA2b is sufficient for interaction with the HAT catalytic domain of GCN5.
Sequence:
MGRSRGNFQNFEDPTQRTRKKKNAANVENFESTSLVPGAEGGGKYNCDYCQKDITGKIRIKCAVCPDFDLCIECMSVGAEITPHKCDHPYRVMGNLTFPLICPDWSADDEMLLLEGLEIYGLGNWAEVAEHVGTKSKEQCLEHYRNIYLNSPFFPLPDMSHVAGKNRKELQAMAKGRIDDKKAEQNMKEEYPFSPPKVKVEDTQKESFVDRSFGGKKPVSTSVNNSLVELSNYNQKREEFDPEYDNDAEQLLAEMEFKENDTPEEHELKLRVLRIYSKRLDERKRRKEFIIERNLLYPNPFEKDLSQEEKVQCRRLDVFMRFHSKEEHDELLRNVVSEYRMVKRLKDLKEAQVAGCRSTAEAERYLGRKRKRENEEGMNRGKESGQFGQIAGEMGSRPPVQASSSYVNDLDLIGFTESQLLSESEKRLCSEVKLVPPVYLQMQQVMSHEIFKGNVTKKSDAYSLFKIDPTKVDRVYDMLVKKGIAQL
The following text describes a protein:
Function:
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Localization:
Cell membrane; Single-pass membrane protein. Membrane.
Sequence:
MSAIAKFFRNVSSEMHKVTWPTRKELLTYTVTVVITVVLFALFFMLIDFGIEQIIKLIV
The following text describes a protein:
Function:
RNA-binding protein that binds specific mRNAs including the ASH1 mRNA, coding for a repressor of the HO endonuclease. Part of the mRNA localization machinery that restricts accumulation of certain proteins to the bud and in the daughter cell. Required for the delivery of cortical endoplasmic reticulum into the emerging bud (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MTDTPNSPSKSTTKSASSSTKVIDSLHSKIDELTDELTALKQSHQELTKKHSITAKKNDSFVDQLANAKHENDMLSALLKRKERRILDLEDQFNELTSQNESLVLSNKNMKIRCENLQSNSNANIAEFERLKISYDALIASQMEYKNHYQQELNSLQTAFDNYKLENTRRFEELQTSIVSNDKDIDTLLDSLTNKRKAMDNIYVNKNNKVLQLLGNLAHLAKLHGQDTKSQVEQNVSVIEQLLAKHPDLQEKILEKEKIEVDLAEIIAHSNDVLANSSFDEDTTLINSPDLENNQNFNTTHSTSGSATPNSNSHSLQSKKRKNYKRNSLILKESPPIISENVPSSLPKKPQVNNNLINIPKARSKFNTPPTTPRQFTNHNNDFEVTHQWNGNNNINNHRRNNSVDSRSDNSQHRRNNSYDSRSDHGQHRRQPSQQNNNYNNNNYNNNNNNNNNNSNNGFVKRSGSVRNVNNYNNNNGNANNNGNNHGNKSKRRSTYNNNNNNNSKRNSQLFDNNFVLNV
The following text describes a protein:
Function:
Dol-P-Glc:Glc(2)Man(9)GlcNAc(2)-PP-Dol alpha-1,2-glucosyltransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. The sequential addition of sugars to dolichol pyrophosphate produces dolichol-linked oligosaccharides containing fourteen sugars, including two GlcNAcs, nine mannoses and three glucoses. Once assembled, the oligosaccharide is transferred from the lipid to nascent proteins by oligosaccharyltransferases. In the lumen of the endoplasmic reticulum, adds the third and last glucose residue from dolichyl phosphate glucose (Dol-P-Glc) onto the lipid-linked oligosaccharide intermediate Glc(2)Man(9)GlcNAc(2)-PP-Dol to produce Glc(3)Man(9)GlcNAc(2)-PP-Dol.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MIEVNKHVPDDYMDEVFHGPQSRHYCHGAFEVWHPKITTFPGIYYLATVYGWCRWAVQAALLKQPLDMDAACATPYLRTLNVVLSVACLLVLRAILLQLQQQQQHPQQTQQTQQTQHQQKQPQQQQQGQRLQSRSHGAARPASAPVSASLHAALLALYPLHWFFSFLLYTDVASLLGLLLAHLAALRRHYLLAALAGGAAVLCRQTNAVWAAFVLGEAALRELGLATAVALPCGSNSSAAAAAVGGAGSSTAVAEKEAALATAEVAEAEAGLVGELKVAAARAWRRRGQLVAALWPLLLPPAGFVAFLIRNGGSVVLGDKEAHKPVRHGAQLLYFAGWSALMLWPQLWPAAGALAAAARRRPLLAGVTAAAGLAAAAGVVHVSTLVHPYMLADNRHYVFYLWRRLINRHRLARYALAPAYVAACALLVAAARRRVSRLWLAGFAVCLVAQLLPAWLLELRYFTPGFFLLALHLPPPSPRQAAGLAATYLAVDGASAALFLYRPYTFADGSVARFLW
The following text describes a protein:
Function:
Hydrolase that can remove conjugated ubiquitin from proteins and may therefore play an important regulatory role at the level of protein turnover by preventing degradation.
Subcellular Localization:
Cytoplasm.
Sequence:
MISIRIRSKTGVENLKVDSQLQIIDFQKIIDEKTSTKPEHQKILHGFPPKSLDLSNPNAPISNFLSNGDTITIENTTALTSPTPAPAVTLSSNSTSNKNNSNNKSEPYMSEEEVGNGFATRRITDDDNSCLFSAVAYVLEDKSRWKGGQLRQLIAQVVRSDPFEYNEGFLGKSNAGYCNWILNPNHWGGAIELSILSNHYKVEIAAFDISTQIMYCYGEDKNYTERVYLIYDGIHYDALSICLTRNGGEDFDITRFSVDDKESLNKLKKFVENEKKLGKYTDTTNFMLLCLDCNKTLKGEKEAAIHASLSGHGNFTEKK
The following text describes a protein:
Function:
Component of the 43S pre-initiation complex (43S PIC), which binds to the mRNA cap-proximal region, scans mRNA 5'-untranslated region, and locates the initiation codon. This protein enhances formation of the cap-proximal complex. Together with EIF1, facilitates scanning, start codon recognition, promotion of the assembly of 48S complex at the initiation codon (43S PIC becomes 48S PIC after the start codon is reached), and dissociation of aberrant complexes. After start codon location, together with EIF5B orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex. Is released after 80S initiation complex formation, just after GTP hydrolysis by EIF5B, and before release of EIF5B. Its globular part is located in the A site of the 40S ribosomal subunit. Its interaction with EIF5 during scanning contribute to the maintenance of EIF1 within the open 43S PIC. In contrast to yeast orthologs, does not bind EIF1.
Sequence:
MPKNKGKGGKNRRRGKNENESEKRELVFKEDGQEYAQVIKMLGNGRLEAMCFDGVKRLCHIRGKLRKKVWINTSDIILVGLRDYQDNKADVILKYNADEARSLKAYGELPEHAKINETDTFGPGDDDEIQFDDIADDDEDIDDI
The following text describes a protein:
Function:
GTPase activating protein (GAP) for RSR1 which is involved in the polarization of yeast and hyphal cells. Directs the site of new daughter cell growth in yeast and hyphal cells. Important for hyphae to maintain linear growth and necessary for hyphal responses to directional cues in the environment (tropisms). Required for correct localization of the septin rings and stabilization of the polarisome at hyphal tips. Involved in cell adhesion.
Subcellular Localization:
Cytoplasm, cell cortex. Cell tip. Cell septum. Note=Enriched just behind the apices of hyphal tips, appearing as a faint ring at the membrane with a relatively reduced intensity at the extreme tip. Also enriched in the concave angle of some curved hyphae and shows discrete localization to septa.
Sequence:
MPPAYQSAFHKIISRDKGVFEGHNFLVSVDTINWIHVNTLTITEQGQLFSSDSKDNHYLLLQSLQSCFIQIYPDSNISGSGKSSISQPPPTTSTRRNLLRKSSNLNSSDQSHSKSSEDNEHQPPAILIKTFDNDKLYIRIPSKANFGNLLSCLMVWQNLKPQGLAKKWYCENKVIEGFNPNAPIYELLVCRFKIYGPLPNKYKNLNIVPGPKAPVYQQKMDDFKANFDNSYIITPQISSDNHNSINEGWFYAMGALNSHGILNFISELDGTLLYSIDIKQILSSEIREMHNSIFNSSNILFIGQLKELRYNNVIRTLSTLTPDQLLTPFLTRDGKIIPNNQRILIEFPLHIDLEDWFVGLNYFAKREYIGSFDNESKLIHNVEHPQLYDFSKANFRVSKKMSIDIIEAKFENTETNKSGKIYAEVRMWGFPWSRTAIVNHTNNPFWKEEFSTDLPISTQMVHILIKKCSFNDSSYSTGDKLIGTVYVTPDILTKQIKTTSTIMTSSESSQAIQMNTVPLSSMASNSNAGLDIVRLTINDPNNIPIGKLLLEVHLQEYHILSPSVFKPLEKMLVNAPMKDLIKFCNENVPSSDFERVSLVLLDIFQSLEVEDDWFKSLMEVELVNVDIMTRKNYHQRNSQDQAVSNSKTQQQSSHNNVFNTLFRGSSIFSKSLEKYNLRIGQEYLEKVFGDFFAKISNEKKNCEVDPRYVRIQERALRKGKSIHEATGLENGQNEDVSDDDDDDDDNSSDDDADYNAEKERERNERIKQMVEENFQNLYGYVEEIWYKIYITSNDLPDQIKLQLKNFRTKVELVCDPEDKVTSLNCLSAFIFLRFFCPAILNPKLFYLAKNHQTGSTQRTLTLIAKILLNFANRQEFSPHKEPHLVRMNVFLRKHTPEIYDYFDKLTGRKNDFNEKILDLSHEVKRFDLGLDKTSNELPTTPYLIDKYLRLTEIVHLLDYSKYVKNIGNNNNGSMSNLGTPVNSPSRDMEREQDRSRSRSQSGTPDLDPILNLSDLKLNYENKYQIGSLEFEKSEFLELTGDNETEGFIKSLCKGNEEIFSFINSNITLKDIQKQSTKIMNKIQELEIYLENYEFPNNYKDQIIWDSFTDDIMNKCWLDTSRNCLIYSDHVPSSNNQYKKLVDHAFSGLKLKFNDHQKLNGNSTMNSLINNGGMGNRNGHDVNGHNNNNNNNNNNTGDGYNETDRNQRLSSTFSTISIGSAIKPNTSKNPFKKWLRKN
The following text describes a protein:
Function:
Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for another nucleotide sugar. May couple UDP-alpha-D-glucuronate (UDP-GlcA) or UDP-alpha-D-xylose (UDP-Xyl) efflux to UDP-alpha-D-glucuronate (UDP-GlcA) influx into the ER lumen, which in turn stimulates glucuronidation and excretion of endobiotics and xenobiotics.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MRPAFAVGLVFAGCCSNVIFLELLARTHPGCGNIVTFAQFLFIAVEGFLFEANLGRKPPAIPIRYYAIMVTMFFTVSVVNNYALNLNIAMPLHMIFRSGSLIANMILGIIILKKRYSMFKYTSIALVSAGIFICTFMSAKQVTVQTGLSDKDGFQAFAWWLLGIAALTFALLMSARMGIFQETLYRQFGKHSKEALFYNHALPLPGFIFLASDIYDHVVLFNKSELYQVPVIGVTMPVMWFYLLMNVVTQYVCIRGVFILTTECTSLTVTLVVTLRKFVSLIFSILYFQNQFTMWHWLGTSFVFIGTLMYTEVWKNLGTTKSELQKDDKKD
The following text describes a protein:
Function:
Negatively regulates the PAK1 kinase. PAK1 is a member of the PAK kinase family, which has been shown to play a positive role in the regulation of signaling pathways involving MAPK8 and RELA. PAK1 exists as an inactive homodimer, which is activated by binding of small GTPases such as CDC42 to an N-terminal regulatory domain. PAK1IP1 also binds to the N-terminus of PAK1, and inhibits the specific activation of PAK1 by CDC42. May be involved in ribosomal large subunit assembly.
Sequence:
MATSKAPDNVFDVILGTYEEFVLGYSLEKQGKDKYSLRQTFTNHSHLGSVRCIAANDRFVASGSTDETVRLFNMRTRCEMGALMQHDGTIADVQFYKSSHLFSASEDKTICIWNTGSWQCLKTLRGHKAEVTSLAVHPTGKLLLSVSKDRTLRTWNLVKGRNAYITNIKVAADFVDWSPAGDHFVVGLGKSLDVYSAEKAGKVHSIDFGKRLCCVAFLTNDVLVLGGDGGSVEIHNIKKKSVYHMFTAHSTRVKAAAVVNVSKKTLLVTAGSEGSVRVWKVNMKKLDNDPTLLCEAKCGCRITCMALHMPEAGDESECEQSEEKEEVVEGETSSEEDQETKPPLPKRRKMAAR
The following text describes a protein:
Function:
Catalyzes the synthesis of activated sulfate.
Sequence:
MATLQPRSTLAPWLRNRTTLSSSQGCSNLSGLQFPSAKRKSRGVLEIARRPGLTVCSSNSKGVRLQETSVTKEDRRKLLHQKGCIVWITGLSGAGKSTLAFTMDRTMMAMGKLTYVLDGDNIRHGLCKDLGFSAADRQENIRRVGEVATLFADAGLITLVSFISPYKRDRDIVREMVPPGHFIEVFMNVPLEVCERRDAKGLYKLARAGVIKGFTGIDDPYEKPETPEITIHDVDEKGGPVSPDQMAWTVIQYLADKGFFSE
The following text describes a protein:
Function:
Involved in the biosynthesis of phenazine natural products including myxin, an N(5),N(10)-dioxide phenazine antiobiotic, which has antimicrobial activity. O-methyltransferase, which converts iodinin (1,6-dihydroxyphenazine N(5),N(10)-dioxide) to myxin (1-hydroxy-6-methoxyphenazine N(5),N(10)-dioxide). Catalyzes both monomethoxy and dimethoxy formation of phenazine natural compounds. Acts on a wide variety of substrates, catalyzing O-methylation of phenazines with non-, mono- or di-N-oxide. Highest activity with 1,6-dihydroxyphenazine (DHP) as substrate. Less active with monohydroxy-containing and monohydroxy-monomethoxy-containing phenazines. Least active with non-phenazine substrates, such as 8-hydroxyquinoline and 6-hydroxyquinoline. Is not able to convert 1-hydroxyphenazine to 1-hydroxy-N5-methylphenazine (pyocyanine), hence does not function as an N-methyltransferase.
Domain:
Contains an N-terminal dimerization domain. The C-terminal region contains the S-adenosyl-L-methionine binding site.
Sequence:
MTENNRAGAVPLSSILLQMITGYWVTQSLYVAAKLGIADLVADAPKPIEELAAKTGAKAPLLKRVLRTIASIGVFTETEPGIFGITPLAALLRSGTPDSMRPQAIMHGEEQYRAWADVLHNVQTGETAFEKEFGTSYFGYLAKHPEADRVFNEAQAGYTKQVAHAVVDAYDFSPFKTVIDIGAGYGPLLSAILRSQPEARGILFDQPHVAQAAGKRLAEAGVGDRCGTVGGDFFVEVPADGDVYILSLLLHDWDDQRSIEILRNCRRAMPAHGKLLIVELVLPEGEEPFFGKWLDLHMLVLLGAQERTADEFKTLFAASGFALERVLPTASGLSIVEARPI