lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Demethylates proteins that have been reversibly carboxymethylated.
Sequence:
MSGLQRSFVKSKLSKLPPIPPFSEADEEGQEHQDPDSNAASRLSKRRQQTDAFAPRTAEGCFEEALEVNVPLASGSASFRVYYTPPRPKPPTLSRSSHQAALGPPHNLGINVESPTLPTLKPGIGSSTDECDEEEQESCHLSKQSTASSQGTLFVLHHGAGFSALSYALTAAEITRISRGEVGVLAYDCRGHGRTRMFGVRSNPLDMSIDVLCSDLTSLLLTMFPEMDQMPSLVLVGHSMGGSVVVSAAHALSAKGFSRLSGVAVLDVVEGTAMDALSVMRSVVLGHPSGFDSVEAAIRWHVDSKTIANLDSARISVPPLIEPDPAFSCANTSANEEKDEQQEVLDDDASSETAQPSNHQYAYRWRADLLATEPYWSSWFRGLSSRFLTVRTARLLLLAGTDRLDRELMIGQMQGKYQLEVIADVGHSLHEDAPDRTARILVDFWRRNERIHLPLKHIKKVGEA
The following text describes a protein:
Function:
Required for formation of the SPO11-mediated double-strand breaks (DSBs) that initiate meiotic recombination. May mediate the interaction between SPO11 subunits during meiosis. Also needed for homolog chromosome pairing, synaptonemal complex formation, and for the proper timing of the first meiotic division. Not required for mitosis and mitotic DNA repair mechanisms.
Miscellaneous:
MISCELLANEOUS: Despite weak sequence similarities, may correspond to the subunit B of a SPO11-containing topoisomerase 6 complex specifically required for meiotic recombination. Retains some of the structural features of the ancestral archaeal Top6B subunit (AC O05207).
Subcellular Localization:
Nucleus. Note=Associates with chromatin during prophase. Recruitment to chromatin depends on REC104, SPO11 and SKI8.
Sequence:
MARDITFLTVFLESCGAVNNDEAGKLLSAWTSTVRIEGPESTDSNSLYIPLLPPGMLKIKLNFKMNDRLVTEEQELFTKLREIVGSSIRFWEEQLFYQVQDVSTIENHVILSLKCTILTDAQISTFISKPRELHTHAKGYPEIYYLSELSTTVNFFSKEGNYVEISQVIPHFNEYFSSLIVSQLEFEYPMVFSMISRLRLKWQQSSLAPISYALTSNSVLLPIMLNMIAQDKSSTTAYQILCRRRGPPIQNFQIFSLPAVTYNK
The following text describes a protein:
Function:
Specifically methylates the N4 position of cytidine in position 1402 (C1402) of 16S rRNA.
Subcellular Localization:
Cytoplasm.
Sequence:
MLNNQQIHQSVLINEVIHNLNINPCGNYLDLTAGFAGHSQKILEKLTTGTLTINDVDKESINFCQKLFFKNNNVVIIHDNFANFPVHLKQLSITKFDGILMDLGVSSHQLNQPNRGFSFKNDGPIDMRMDQSNQKNTALTVLKNLTEQKLSLILKKYGDIKHPKPIAIGLKKAVQTEKNLTTTQLAKVVKECATGFEKYQSRNYLAKVFQAIRIYLNDEITNLKTALTFIPNLLKNNSRFLVIVFHSIEEKIVRNFIAKLTSFIQPEALPIKLTPAYQLITKKPILPSQKELELNPRSRSAKLFVIQKN
The following text describes a protein:
Function:
Small subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia.
Sequence:
MMSSPAKAAKLALEDGTVYTGTSLGAEGETTGEVVFNTSMTGYQEILTDPSYRGQLVTMTYPEMGNYGINSIDLENRGTSLAGFIIRNESRMHSNYRSEGSLSDYLNSQGVVGIAGIDTRALVRRIRSEGAMRGVLSTTDLDDASLVAKAKASPGLVGRDLVQEVMPTQLEKWTNELDDWTIREIREAAKDASIGDDSRPHVVCMDFGMKWNIPRHLRSRGNRVTIVPGNASADDILKMDPDGVFLSNGPGDPEPLTYAHKAIGELLGQVPVFGICLGHQLLSVACGAKTFKLKFGHRGANQPVLDLETGKVEITSQNHGFAVDDQGLPDCLEVTHRNLNDDTIAGVRHKDTGAFAVQYHPEAAAGPHDSHYLFSRFQEQLNEKCGVTA
The following text describes a protein:
Function:
Intramembrane glycolipid transporter that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. 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. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side of the endoplasmic reticulum membrane and finishes in its lumen. RFT1 could mediate the translocation of the cytosolically oriented intermediate DolPP-GlcNAc2Man5, produced by ALG11, into the ER lumen where dolichol-linked oligosaccharides assembly continues. However, the intramembrane lipid transporter activity could not be confirmed in vitro.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MKRSRKSTKPLHLDKDFPRQNVVTRTETNDEVGLKSDSISKSLNSTFKGVRYMLVQQLLSRGMTFSMNMFLIRRSPVEMIGIVDKLDLLMATVLFLSRESIRMALLRNTSTESIIHKNQSKKLDSVHLQHSTDDGIQNQLAFNMSVIPLIGASMFVGGCILYDSANWFLFGASISVAKYMYLVAALIELIAEPSFILLQRGLLYAERVKTEGAAFLLQCLTTMVLFLFLTRSSKDNTISVVDGVWAHACAQIVFASVLLVGYTSYAHYTRLMPFRTLRMVGINQGSPKVFLDPYYANIAMTFFFQGVVKHLLTVGDRLVLVATGVGNASQGTYRLVSDLGSLVARIVFQPIEEASRAFFSKNLTNPSAADISKTLCESFEYLQSVIQLHIILGGFFVFLAPNYTHILLQLYNKFDPTTSFVLGVYCIYVPIMGINGILEAFFQGVGEEAAVRRQSYYMLWFWAVFVSTSYILISIVQMGTVGLIVSNAINMSMRIIFCFVFIQHFFQLNNSIGVLLPLKERNKLSCTFQEMLSPIALIPARMSVWILFGLSWFATYWSSFAYLIWGKLFGTLIHVAVGVICGIALLVAL
The following text describes a protein:
Function:
Transcription factor that mediates regulation of both acid- and alkaline-expressed genes in response to ambient pH. At alkaline ambient pH, activates transcription of alkaline-expressed genes (including RIM101 itself), mainly by repressing transcriptional repressors of those genes, and represses transcription of acid-expressed genes. Required for meiosis, sporulation and invasive growth.
Miscellaneous:
MISCELLANEOUS: Present with 1822 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MVPLEDLLNKENGTAAPQHSRESIVENGTDVSNVTKKDGLPSPNLSKRSSDCSKRPRIRCTTEAIGLNGQEDERMSPGSTSSSCLPYHSTSHLNTPPYDLLGASAVSPTTSSSSDSSSSSPLAQAHNPAGDDDDADNDGDSEDITLYCKWDNCGMIFNQPELLYNHLCHDHVGRKSHKNLQLNCHWGDCTTKTEKRDHITSHLRVHVPLKPFGCSTCSKKFKRPQDLKKHLKIHLESGGILKRKRGPKWGSKRTSKKNKSCASDAVSSCSASVPSAIAGSFKSHSTSPQILPPLPVGISQHLPSQQQQRAISLNQLCSDELSQYKPVYSPQLSARLQTILPPLYYNNGSTVSQGANSRSMNVYEDGCSNKTIANATQFFTKLSRNMTNNYILQQSGGSTESSSSSGRIPVAQTSYVQPPNAPSYQSVQGGSSISATANTATYVPVRLAKYPTGPSLTEHLPPLHSNTAGGVFNRQSQYAMPHYPSVRAAPSYSSSGCSILPPLQSKIPMLPSRRTMAGGTSLKPNWEFSLNQKSCTNDIIMSKLAIEEVDDESEIEDDFVEMLGIVNIIKDYLLCCVMEDLDDEESEDKDEENAFLQESLEKLSLQNQMGTNSVRILTKYPKILV
The following text describes a protein:
Function:
Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein.
Subcellular Localization:
Cytoplasm.
Sequence:
MRPILLEEWSSLLLGMEIPRSGKKVTGVAIDSRFVLPGDVFFALPGNRTSGHLFLKQAAQSGAVAAVVASDYHGPSYGLQLLRVADPREALRAAGRTQGALFYGEVIGITGSVGKTTTKNFANQLLSSVYKVFMSPKSYNSQLTLPLSVLMADGDEDFLLLEMGVSEPNNMKNLLEIIEPTIGVITHIDVQHAVHFLDKGAQGIVEEKSLLLERCGLQLIPKDSSWFQFFAKKNSAADRFSFSMSNETADFYYRAIHSEGVLISAPDGDIELPAVFPYSPAYMNFIIAVALAWITNVPMDRLEQVSQSLFLPAMRFEQQEHNGIRVINDAYNASPDAMLAALDAVPVPPEGGKIIFILGHMAELGRYSDECHIAAARKAVTKAHIIFFVGEKWFPVRDIVRDADCQIGFYSAVSEIMDAVKALVQQGDVVLLKGSRSLELETLLPCFSIS
The following text describes a protein:
Function:
Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling. The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each subunit contributing transmembrane segments that coassemble into an open channel that specifically allows the passage of PEX5 through the peroxisomal membrane. PEX12 also regulates PEX5 recycling by activating the E3 ubiquitin-protein ligase activity of PEX10. When PEX5 recycling is compromised, PEX12 stimulates PEX10-mediated polyubiquitination of PEX5, leading to its subsequent degradation.
Subcellular Localization:
Peroxisome membrane; Multi-pass membrane protein.
Sequence:
SCCEHSNVDMGELGNEVSTALTSHDANLPSPFEVLAQDNLNDSVDPAIKYIVKVLAQNSPHRFGWCYVWFDELFAAVKLLIQQHFLSNYNSTFAEYYYELQRKVVGKSNANIFRFGTKISFKTLAVLVLLPYIMTKFKSLYLSVKEEADVSTVKSLSKLKRAIYYAYPLVHMSWHTSVLYYNFMFAIGKTQFHSPFYKLLNTKLFVKSPLDSLYNENIIYLFSATGITKLCTQLMTGGVHVGVFALQFVDWWYNSEGNEDLKQMLSNPIPKPPENTLKETKIPVPSGKICPLCNKSRRNETVLQTSGYAFCYTCVYKFVNKHGACPVTGYTTNICHLIRIYYSATH
The following text describes a protein:
Function:
Plays a role in translation initiation. Ribosome-dependent GTPase that promotes the joining of the 60S ribosomal subunit to the pre-initiation complex to form the 80S initiation complex with the initiator methionine-tRNA in the P-site base paired to the start codon. Together with eIF1A (EIF1AX), actively orients the initiator methionine-tRNA in a conformation that allows 60S ribosomal subunit joining to form the 80S initiation complex. Is released after formation of the 80S initiation complex. Its GTPase activity is not essential for ribosomal subunits joining, but GTP hydrolysis is needed for eIF1A (EIF1AX) ejection quickly followed by EIF5B release to form elongation-competent ribosomes. In contrast to its procaryotic homolog, does not promote recruitment of Met-rRNA to the small ribosomal subunit.
Subcellular Localization:
Cytoplasm.
Sequence:
MGKKQKNKSEDSAKDDIDLDALAAEIEGAGAAKEQEPQKSKGKKKKEKKRQDFDEDDILKELEELSWEAQGIKADRESAAVKPTENNEEESTSKQDKKKKGQKGKKQSFDDNDSEEWEDKDSKSKKTAKSKVEMYSGSDDDDDDFNKLSKKAKGKVQKSNKRGDGSEEDEDNSKRVKERSRVNSSGESGDESDEFLQSRKGQKKNQKNKPSPNVESGNEDDDSSFKIKTVAQKKAEKKERERKKRDEEKAKLRKLKEKEELETGKKDQSKQSQKKSEEEAVKSKVTLDTGAVPASEEKGETPTAAEDDNEGDKKKKDKKKKKGEKEEKEKEKKKGPSKATVKAMQEALAKLKEEEERQKREEEERIKRLEELEAKRKEEERLEQEKRERKKQKEKERKERLKKEGKLLTKSQREARARAEATLKLLQAQGVEVPSKDSLPKKRPIYEDKKKKKTLQQLENKEVSEPIELSAAVEVVEQGVPEKEETPPPVEPEEEEETEDTGLDDWEAMASDEEREKEEENTVHIEVKENPEEEEEEEEEESEEEESEEEEEEEGESEGSEGDEEDEKVSDEKDAGKMLDKKPSKEMSSESEYDSDDDRTKEERAYDKAKRRIEKRRLEHSKNVNTEKLRAPVICVLGHVDTGKTKILDKLRHTHVQDGEAGGITQQIGATNVPLEAINEQTKMIKNFDRENVRIPGMLIIDTPGHESFSNLRNRGSSLCDIAILVVDIMHGLEPQTIESINLLKSKKCPFIVALNKIDRLYDWKKSPDSDVAATLKKQKKNTKDEFEERAKAIIVEFAQQGLNAALFYENKDPRTFVSLVPTSAHTGDGMGSLIYLLVELTQTMLSKRLAHCEELRAQVMEVKALPGMGTTIDVILINGRLKEGDTIIVPGVEGPIVTQIRGLLLPPPMKELRVKNQYEKHKEVEAAQGVKILGKDLEKTLAGLPLLVAYKEDEIPVLKDELIHELKQTLNAIKLEEKGVYVQASTLGSLEALLEFLKTSEVPYAGINIGPVHKKDVMKASVMLEHDPQYAVILAFDVRIERDAQEMADSLGVRIFSAEIIYHLFDAFTKYRQDYKKQKQEEFKHIAVFPCKMKILPQYIFNSRDPIVMGVTVEAGQVKQGTPMCVPSKNFVDIGIVTSIEINHKQVDVAKKGQEVCVKIEPIPGESPKMYGRHFEATDILVSKISRQSIDALKDWFRDEMQKSDWQLIVELKKVFEII
The following text describes a protein:
Function:
Cytokine that binds to TNFRSF18/AITR/GITR. Regulates T-cell responses. Can function as costimulator and lower the threshold for T-cell activation and T-cell proliferation. Important for interactions between activated T-lymphocytes and endothelial cells. Mediates activation of NF-kappa-B. Triggers increased phosphorylation of STAT1 and up-regulates expression of VCAM1 and ICAM1. Promotes leukocyte adhesion to endothelial cells. Regulates migration of monocytes from the splenic reservoir to sites of inflammation.
Subcellular Localization:
Cell membrane; Single-pass type II membrane protein.
Sequence:
MSLSHMEDMSLSHSSPQGTHRLSWKQWLLYSTTVTLLLICSFSTLILTFLPFKTASEPCVAKFGPLPSKWQITYPKLPCVNKTADEKLEILQNGLYLIYGQVAPNTAYKEPAPFEVRLYKNEDIIQALTNNSKIQNVGGTYELHAGDILDLIFNAEHQVLKNTTYWGILLLANPQFIS
The following text describes a protein:
Function:
Catalyzes the radical-mediated synthesis of 7,8-didemethyl-8-hydroxy-5-deazariboflavin (FO) from 5-amino-6-(D-ribitylamino)uracil and L-tyrosine.
Sequence:
MPQPVGRKSTALPSPVVPPQANASALRRVLRRARDGVTLNVDEAAIAMTARGDELADLCASAARVRDAGLVSAGRHGPSGRLAISYSRKVFIPVTRLCRDNCHYCTFVTVPGKLRAQGSSTYMEPDEILDVARRGAEFGCKEALFTLGDRPEARWRQAREWLGERGYDSTLSYVRAMAIRVLEQTGLLPHLNPGVMSWSEMSRLKPVAPSMGMMLETTSRRLFETKGLAHYGSPDKDPAVRLRVLTDAGRLSIPFTTGLLVGIGETLSERADTLHAIRKSHKEFGHIQEVIVQNFRAKEHTAMAAFPDAGIEDYLATVAVARLVLGPGMRIQAPPNLVSGDECRALVGAGVDDWGGVSPLTPDHVNPERPWPALDELAAVTAEAGYDMVQRLTAQPKYVQAGAAWIDPRVRGHVVALADPATGLARDVNPVGMPWQEPDDVASWGRVDLGAAIDTQGRNTAVRSDLASAFGDWESIREQVHELAVRAPERIDTDVLAALRSAERAPAGCTDGEYLALATADGPALEAVAALADSLRRDVVGDEVTFVVNRNINFTNICYTGCRFCAFAQRKGDADAYSLSVGEVADRAWEAHVAGATEVCMQGGIDPELPVTGYADLVRAVKARVPSMHVHAFSPMEIANGVTKSGLSIREWLIGLREAGLDTIPGTAAEILDDEVRWVLTKGKLPTSLWIEIVTTAHEVGLRSSSTMMYGHVDSPRHWVAHLNVLRDIQDRTGGFTEFVPLPFVHQNSPLYLAGAARPGPSHRDNRAVHALARIMLHGRISHIQTSWVKLGVRRTQVMLEGGANDLGGTLMEETISRMAGSEHGSAKTVAELVAIAEGIGRPARQRTTTYALLAA
The following text describes a protein:
Function:
Is essential for the biogenesis of the T-pilus, which is required for virulence and T-DNA transfer to plant cells. When is associated with virB9, might function as a nucleation center for recruitment of VirB proteins during assembly of the T-DNA transfer machine (By similarity).
Subcellular Localization:
Cell outer membrane; Lipid-anchor. Note=Also associated with the T-pilus when is a homodimer, possibly at the pilus base.
Sequence:
MKYCLLCLALALGGCQTNDKLASCKGPIFPLNVGRWQPTPSDLQLSNVGGRHEGV
The following text describes a protein:
Function:
Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases.
Subcellular Localization:
Cytoplasm.
Domain:
The MATH/TRAF domain binds to receptor cytoplasmic domains.
Sequence:
MSIYSKFTINDVLLNKESLQKKNKYTCPICFELIYKKSIYQCSSGHYACQECWEKSLEIKQECMICRCKVKSFKNLSRCLVIEQNFSKKECNCIYSFHLDYFIDGANQENEDEENEDEENEDDEDENEDEENGEDDEDKDEDEENENENEENKDEENEKRKLIKDEENGCKEIINVDQLDRHIQNCKFKFVKCSHIGCDRVLRLNSLKEHENQCGFKLVKCEYCACDGIIQVQLENHYDECPKFVIGCPQGCLNFFERDQIKSHIENDCNNSTIQCKYYEYGCKVEMKRSELQRHLENVNHQLFMGKLIDKLSSTLDQSMKIQELLLKEIEKSKITCSELQRKNDELSSLITEIDDNYFNKNDFINSWKLTSQGYTNKWIISNYSNLVENTPHPEYIYSPSFDIVSREFVISIYPNGSLTGKDHLSLFLHNNNEDPNKLEFTLELVNLLDKSKSITRKGLEVFEEIERKGWSKFLASKLINKKNGWLSDDDKLTINIYVKILYDDIEPLES
The following text describes a protein:
Function:
Negatively regulates B-cell proliferation following stimulation through the B-cell receptor. May play an important role in maintenance of marginal zone (MZ) B-cells.
Subcellular Localization:
Cell membrane; Single-pass membrane protein.
Sequence:
MLECFESSPVAVAVGVSLLVLLLLCGIGCAWHWNRRESTPFTLPKFMQRRSSRQKDVTKTVSSSAYVISPSMKASVESKGHKSTAKRNKMHGNYENVEVCPPCTEGTTEKALYENTQPSNLEEHVYGNQTDPLYYNFQKPSPPPPQDDDIYILPDCD
The following text describes a protein:
Function:
Essential subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch. It probably represents a stabilizing cofactor required for the assembly of the gamma-secretase complex.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MEMRLNAASIWLLILSYGATIAQGERTRDKMYEPIGGASCFRRLNGTHQTGCSSTYSGSVGVLHLINVEADLEFLLSSPPSPPYAPMIPPHLFTRNNLMRLKEAGPKNISVVLLINRTNQMKQFSHELNCPNQYSGLNSTSETCDASNPAKNWNPWGTGLLHEDFPFPIYYIADLDQVTKLEKCFQDFNNHNYETHALRSLCAVEVKSFMSAAVNTEVCMRRTNFINNLGGSKYCDPLEGRNVYATLYPRKPAIENNLETVHTNEKFILVTCRLDTTTMFDGVGLGAMDSLMGFAVFTHVAYLLKQLLPPQSKDLHNVLFVTFNGESYDYIGSQRFVYDMEKLQFPTESTGTPPIAFDNIDFMLDIGTLDDISNIKLHALNGTTLAQQILERLNNYAKSPRYGFNLNIQSEMSAHLPPTSAQSFLRRDPNFNALILNARPTNKYYHSIYDDADNVDFTYANTSKDFTQLTEVNDFKSLNPDSLQMKVRNVSSIVAMALYQTITGKEYTGTKVANPLMADEFLYCFLQSADCPLFKAASYPGSQLTNLPPMRYISVLGGSQESSGYTYRLLGYLLSQLQPDIHRDNCTDLPLHYFAGFNNIGECRLTTQNYSHALSPAFLIDGYDWSSGMYSTWTESTWSQFSARIFLRPSNVHQVTTLSVGIVVLIISFCLVYIISSRSEVLFEDLPASNAALFG
The following text describes a protein:
Function:
Component of the UFM1 ribosome E3 ligase (UREL) complex, a multiprotein complex that catalyzes ufmylation of endoplasmic reticulum-docked proteins. The UREL complex plays a key role in ribosome recycling by mediating mono-ufmylation of the RPL26/uL24 subunit of the 60S ribosome following ribosome dissociation: ufmylation weakens the junction between post-termination 60S subunits and SEC61 translocons, promoting release and recycling of the large ribosomal subunit from the endoplasmic reticulum membrane. Ufmylation of RPL26/uL24 and subsequent 60S ribosome recycling either take place after normal termination of translation or after ribosome stalling during cotranslational translocation at the endoplasmic reticulum. Within the UREL complex, DDRGK1 tethers the complex to the endoplasmic reticulum membrane to restrict its activity to endoplasmic reticulum-docked ribosomes and acts as an ufmylation 'reader': following RPL26/uL24 ufmylation, DDRGK1 specifically binds to ufmylated RPL26/uL24 via its UFIM motif, resulting in stable association between the 60S ribosome and the UREL complex, followed by dissociation of the 60S ribosome subunit from the endoplasmic reticulum membrane. The UREL complex is also involved in reticulophagy in response to endoplasmic reticulum stress by promoting ufmylation of proteins such as CYB5R3 and RPN1, thereby promoting lysosomal degradation of ufmylated proteins (By similarity). Required for stabilization and ufmylation of ATG9A (By similarity).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Domain:
The UFM1-interacting motif (UFIM) specifically recognizes and binds ufmylated RPL26/uL24, resulting in stable association between the 60S ribosome and the UREL complex.
Sequence:
MVEPAVLYAVAAVFVAVLLFLAVKLRGGQEQQPADDGQRRGAPRPRTDAERAAGAPRRVRGARQRLQAARRINQQDSEGDSDSDEGRPEIDIPEGMKVGAKKMKKLEMKAEKKAAREAAEQEREERKQREKMLEEKRKQEEEEEKLEEERRAEEERKAKEEKAAREHEEYLMMKEAFTVEEEGHEEILDEDATENLLQDFIDHIKAVKVVLLEDLAAQFNMRTQDCIQRVQELREQGRLTGVIDDRGKFIYISQEELQAVAKFIKQRGRVSITDLVESSNQLIHLIPDTEQVIRVQSS
The following text describes a protein:
Function:
Orphan nuclear receptor that binds to a response element containing the sequence 5'-TCAAGGTCA-3'. Acts as a regulator of embryonic stem cell pluripotency by mediating repression of POU5F1/OCT4: binds to the DR0 element within the POU5F1/OCT4 promoter and inhibits POU5F1/OCT4 expression during embryonic stem cell differentiation. Involved in the regulation of gene expression in germ cell development during gametogenesis (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MERDEPPPSGGGGGGGSAGFLEPPAALPPPPRNGFCQDELAELDPGTISVSDDRAEQRTCLICGDRATGLHYGIISCEGCKGFFKRSICNKRVYRCSRDKNCVMSRKQRNRCQYCRLLKCLQMGMNRKAIREDGMPGGRNKSIGPVQISEEEIERIMSGQEFEEEANHWSNHGDSDHSSPGNRASESNQPSPGSTLSSSRSVELNGFMAFREQYMGMSVPPHYQYIPHLFSYSGHSPLLPQQARSLDPQSYSLIHQLLSAEDLEPLGTPMLIEDGYAVTQAELFALLCRLADELLFRQIAWIKKLPFFCELSIKDYTCLLSSTWQELILLSSLTVYSKQIFGELADVTAKYSPSDEELHRFSDEGMEVIERLIYLYHKFHQLKVSNEEYACMKAINFLNQDIRGLTSASQLEQLNKRYWYICQDFTEYKYTHQPNRFPDLMMCLPEIRYIAGKMVNVPLEQLPLLFKVVLHSCKTSVGKE
The following text describes a protein:
Function:
Transcription factor that regulates the expression of the gene cluster that mediates the biosynthesis of monodictyphenone, a prenyl xanthone derivative.
Subcellular Localization:
Nucleus.
Sequence:
MTSSEGPGIPAIKTPPVKLRGSCHACALSKLKCSQDKPTCSRCVKRGTACQYLASKRAGRKQGSKTGSFKSFYNMKTDYSTSINKDDDRRELMEVSTELMQYALQQDRSLEVYRRNQYHQRTPSYPESIPSLLSSTGPGTSATSPLTLGPPDYDGYLASPISLSLLDVPDMDYFPGADMSANVMDGFPDPPSFFPSGEPIPTLQENILKTSFADSPVPANSPSVPPTPDVTSVGTPRQCFCFPRALTLLRELFPNPSLSCVTPSSESGSASPPTVQQVITKNEQTLRDITEIIECSCSEDGYTITIITLAAFKVLAWYSAVAHISPISEDSQALEEIDRTPAVVRGYNIDGEDQGRMAAQLVLSELHRVQRLVGNLYQRLKDQVSGGKPARLSTTGVNDSNHYSLPFHLLERLAVDLGAQLRSLSSEIVDRLRRG
The following text describes a protein:
Function:
Molecular chaperone; assists the folding of proteins upon ATP hydrolysis. Known to play a role, in vitro, in the folding of actin and tubulin.
Subcellular Localization:
Cytoplasm.
Sequence:
MISGKTETYVDNKRKDDVRQANIMAAKAVADAVRTSLGPRGMDKMLSTSSGEVIITNDGATILLKMEVLQPAAKMLVELSKSQDIVAGDGTTTVVVIAGALLKQCIALLGKGVHPTIISDAFHRASLKAVEVLTSMAIPVELSDREALVKNASTSLNSKVVSQYSSLLAPLAVDAVLNVVDPARPDSVDLRDIKVIKKLGGTVDDTEMIKGLVFDKKASHTAGGPTRVENAKIGLIQFQISPPKTDIEQNVIVSDYTQMDRILKEERNHILGMIKKIKATGCNVLLIQKSILRDAVTELSLHYLAKAKILVVKDVERDEIEFISKTLNCLPIANIEHFRAEKLGQAELVEEVSVGDGRIVKISGIKNMGRTTTILVRGSNQLVLDEAERSLHDALCVVRCLVNKRFLIAGGGAPEIEVSRQLGAWAKTLQGMESYCVRAFAEALEVIPYTLAENAGLNPITIVTELRNHHANGEVNTGINVRKGQITNILEENVVQPLLVSTSAVSLATECVRMILKIDDIVTVR
The following text describes a protein:
Function:
Involved in disulfide bond formation. DsbG and DsbC are part of a periplasmic reducing system that controls the level of cysteine sulfenylation, and provides reducing equivalents to rescue oxidatively damaged secreted proteins such as ErfK, YbiS and YnhG. Probably also functions as a disulfide isomerase with a narrower substrate specificity than DsbC. DsbG is maintained in a reduced state by DsbD. Displays chaperone activity in both redox states in vitro.
Subcellular Localization:
Periplasm.
Sequence:
MLKKILLLALLPAIAFAEELPAPVKAIEKQGITIIKTFDAPGGMKGYLGKYQDMGVTIYLTPDGKHAISGYMYNEKGENLSNTLIEKEIYAPAGREMWQRMEQSHWLLDGKKDAPVIVYVFADPFCPYCKQFWQQARPWVDSGKVQLRTLLVGVIKPESPATAAAILASKDPAKTWQQYEASGGKLKLNVPANVSTEQMKVLSDNEKLMDDLGANVTPAIYYMSKENTLQQAVGLPDQKTLNIIMGNK
The following text describes a protein:
Function:
[Isoform Peroxisomal]: Catalyzes the transamination of glyoxylate to glycine and contributes to the glyoxylate detoxification; [Isoform Mitochondrial]: Catalyzes the transamination between L-serine and pyruvate and weakly contributes to gluconeogenesis from the L-serine metabolism.
Subcellular Localization:
[Isoform Peroxisomal]: Peroxisome; [Isoform Mitochondrial]: Mitochondrion matrix.
Sequence:
MFRMLAKASVTLGSRAASWVRNMGSHQLLVPPPEALSKPLSIPKRLLLGPGPSNLAPRVLAAGSLRMIGHMQKEMFQIMDEIKQGIQYVFQTRNPLTLVVSGSGHCAMETALFNLLEPGDSFLVGTNGIWGIRAAEIAERIGARVHQMIKKPGEHYTLQEVEEGLAQHKPVLLFLTHGESSTGVLQPLDGFGELCHRYQCLLLVDSVASLGGVPIYMDQQGIDILYSGSQKVLNAPPGISLISFNDKAKSKVYSRKTKPVSFYTDITYLSKLWGCEGKTRVIHHTLPVISLYCLRESLALISEQGLENSWRRHREATAHLHKCLRELGLKFFVKDPEIRLPTITTVTVPAGYNWRDIVSYVLDHFNIEISGGLGPSEDKVLRIGLLGYNATTENADRVAEALREALQHCPKNKL
The following text describes a protein:
Function:
Lipid transfer protein required for autophagosome completion and peroxisome degradation. Tethers the edge of the isolation membrane (IM) to the endoplasmic reticulum (ER) and mediates direct lipid transfer from ER to IM for IM expansion. Atg2 binds to the ER exit site (ERES), which is the membrane source for autophagosome formation, using basic residues in its N-terminal region (NR) and to the expanding edge of the IM through its C-terminal region. The latter binding is assisted by an atg18-PtdIns3P interaction. Atg2 then extracts phospholipids from the membrane source using its NR and transfers them to atg9 to the IM through its predicted beta-sheet-rich structure for membrane expansion.
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MPKRLLQYALSRLEILDTDALDLENLDIAWGKNSTFEFKDVGLRLKKLETLLQLPSTIALSKAKVLLLRLTIPVDVYSSPILVEVDGVDVQLRVKEEKGANSSRTNHDRLRKKSTSRSPGPDPALPTAEDLAASFLQTEPREEKAELEAAILGETQDISESITSSEDGDLEVPVGTGTALSLPAFMARFLQGIVDRLQVRVHGITFNVDVDIPAEGPTPNRTTDPVTVQLKIDDVDIEGVTHDIESAQTRGGKDITSLFKEGKKLICLSNIRGALITEANLFQTLSRSSSILSPAVPHSDISESRRTTEMRRSSEETQAMSVGSVRAFDGVASPSPRPSPASSLRASETSLPEIRRPSTPPRPLKISPSLKASIAASDGGRFDDASEDGHSNRSVSVHEDIDSSEMGDSILHNSAYLDQITESQLLDDHEGDDMRSSPSQYEQERHSAPSENSRTSTPRASTHISPSSSRTLGFNQFPSINRAHNMLQSTMLPPRPHTRFSLERVSHSQPTLPSSTAPLDRSYPVQQPESPLEVDAMSEADSSVSSTLNEEAGDDLAQSQLFSHEDAESMYMSAVSYTSAAPIPGGWADSGTESEDAKSPPATPRGPDAGREKLDNLENARHAVPLDGASDTTPLEQSTILPSGSLHKSARSISSMHPETPRRSPPLYQASSDISVESTASADDYSRMTKQIFSLDQIAIYIPAMNNPSSDPVDAVAESALFGSTFDGHSDSSRSRTMDLPGAFSTHLPREQPSRPSPRPALRTPVQPAKKIEEEKLIEVDVGNLLARFDVSVGRLIYKLVCQIQESMKQEPQAVASSKPTSSSTEPHLKISAKEISLRFLEQLQGTLGSRAAESQAKTLDSDVLLRTTLKGLDVSRKPSDSITKTSITLQKFLFGYAQENIISFNANLQMRASVRDLAASAGIDVSVDMYQSSDGTRFEVQTLPLHVAVDLQRLDETFSWFGGLSSVLNLGSSMASNATVTSNPVPKPKSRGVRFNTPIGPDDKTAAAQNKADVRIGGFILDLVGTECSVGVETSAVKLVSREEGIGVAINKIRLSGPHLKHSNEDPAILVDVSSTRVELLNAPKDNDIDRLLALIAPSKSKYDQDDDILLDTLLRQRQQGSVLRLTMDDLQVKMGNLQELSYLPDLGEEVARLSTVTKYLPDDDRPGLLSLVSVKKLGVNVDVNNTLGSLQLKATDLEVAQIPIPSLVAFSVATVSAYRNYSEELIGAGTDQTFMEPSLRTPTIMARLIGDEMEPIVRIKLWNLRIEYRVPTLMVLLGLADNATENDMSASIMASVATLRDLAQPRTSKGKGKSVEKASASSNSAAKPMTIDVVLTDCIVGLNPLGLPSKILVVLTEAHVAAVLPKDQNASATAELSKASLLVIDNVAHLATNVPSNRKRNSFDGGSNQVADLTTMGYVSVSYISSAKATVLLSVDDDGQNCLDVELRDDLFVLESCADSTQTLIGVLGKLAPPAPPPSKESKYRTKVIPVKDLLASLSGDAFGTAEGNYDFDNDFGDFGDVAEEHEGDLGFDSDYYKDETEEGYRQAVLEDIGEPLASLNLTTRDTRDGVLLDSFVEDSEIGNEALSFHEDHFGTGSVLEGSAHRWNSAKNTYDTSNESKVKKSPLKVCVRDVHIIWNLFDGYDWQATRDAISKAVQDVESKAIEKRARNERRPAFEQDIDDDEDTEIGDFLFNSIWVGIPNNRDPRELAAAINQELNDNATETESIATTNYTITPSRQGTGRKPKKLRLNRSKHHKITFELRGVCVDLVAFPPFSGETQSSIDVRVLDLEVFDHVPTSTWRKFATYMQDAGEREKGSNMVHIEILNVKPVSYLAASEIVLKVTILPLRLHVDQDALDFITRFFEFKEESDVIPGAPSEEPFLQRVEVNSVQVKLDFKPKRVDYAGLRSGHTTEFMNFLILDEADMTLRHTIIYGISGFEKMGKCLNDIWMPDIQRNQLPGILAGLAPVRSIVNVGGGFKDLVVIPMHEYKKDGRIVRSISKGAAAFAKTTGTELVKLGAKVAIGVQTVLQGAEDFLGPQDASIPHGNSSEDEEERKQISLYANQPVGVFQGLKGGYAGLQRDLVMARDAIIAVPGEVMEGGSAKGVLRAVRKHAPTVILRPAIGVAKGAGQVLMGATNSLDKRNLERADAKYKKH