lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Transcription factor playing important roles in primary neurulation and in the differentiation of stratified epithelia of both ectodermal and endodermal origin (By similarity). Binds directly to the consensus DNA sequence 5'-AACCGGTT-3' acting as an activator and repressor on distinct target genes. xhibits functional redundancy with GRHL2 in epidermal morphogenetic events and epidermal wound repair (By similarity). Exhibits functional redundancy with GRHL2 in epidermal morphogenetic events and epidermal wound repair but is essential to form the epidermal barrier with TGM3 as critical direct target gene among others. Despite being dispensable during normal epidermal homeostasis in the adulthood, is again required for barrier repair after immune-mediated epidermal damage, regulates distinct gene batteries in embryonic epidermal differentiation and adult epidermal barrier reformation after injury. Plays unique and cooperative roles with GRHL2 in establishing distinct zones of primary neurulation. Essential for spinal closure, functions cooperatively with GRHL2 in closure 2 (forebrain/midbrain boundary) and posterior neuropore closure (By similarity). Also required for proper development of the oral periderm. No genetic interaction with GRHL3, no functional cooperativity due to diverse target gene selectivity.
Miscellaneous:
MISCELLANEOUS: GRHL genes (GRHL1, GRHL2 and GRHL3) show a paradoxical lack of redundancy despite their extensive sequence identity in the DNA-binding and protein dimerization domains and the fact that the core consensus DNA binding sites are identical. They have related, but remarkably different functions during embryogenesis because of their differential spatiotemporal expression patterns during development.
Subcellular Localization:
Nucleus.
Sequence:
MSNELDFRSVRLLKNDPVNLQKFSYTSEDEAWKTYLENPLTAATKAMMRVNGDDDSVAALSFLYDYYMGPKEKRILSSSTGGRNDQGKRYYHGMEYETDLTPLESPTHLMKFLTENVSGTPEYPDLLKKNNLMSLEGALPTPGKAAPLPAGPSKLEAGSVDSYLLPTTDMYDNGSLNSLFESIHGVPPTQRWQPDSTFKDDPQESMLFPDILKTSPEPPCPEDYPSLKSDFEYTLGSPKAIHIKSGESPMAYLNKGQFYPVTLRTPAGGKGLALSSNKVKSVVMVVFDNEKVPVEQLRFWKHWHSRQPTAKQRVIDVADCKENFNTVEHIEEVAYNALSFVWNVNEEAKVFIGVNCLSTDFSSQKGVKGVPLNLQIDTYDCGLGTERLVHRAVCQIKIFCDKGAERKMRDDERKQFRRKVKCPDSSNSGVKGCLLSGFRGNETTYLRPETDLETPPVLFIPNVHFSSLQRSGGAAPSAGPSSSNRLPLKRTCSPFTEEFEPLPSKQAKEGDLQRVLLYVRRETEEVFDALMLKTPDLKGLRNAISEKYGFPEENIYKVYKKCKRGETSLLHPRLSRHPPPDCLECSHPVTQVRNMGFGDGFWRQRDLDSNPSPTTVNSLHFTVNSE
The following text describes a protein:
Function:
This protein is involved in the repair of mismatches in DNA. It is required for dam-dependent methyl-directed DNA mismatch repair. May act as a 'molecular matchmaker', a protein that promotes the formation of a stable complex between two or more DNA-binding proteins in an ATP-dependent manner without itself being part of a final effector complex.
Sequence:
MTDRIRALDDATVARIAAGEVVERPASVVKELVENSLDAGAASVDVSVDAGGTDRIVVADDGRGMTGDDLRMAVRQHTTSKLDDASGLDGVGTLGFRGEALYTIGSVAELTVTTRPRNAGDTGARITVDHGDAGSVAPAGHPAGTTVEVTDLFGETPARRKYLKRAATEFGHVNRAVTRYALANPDVAVSLTHDGREVFATTGTGDVQDAALAVYGREVAQSLRTVDADPAADSVERVHGYVSDPEVTRSTREYLATFVNGRAVTDAVLREAVLDGYGDQLAPDRYPFAVLFVDCEGVDANVHPRKLEVRFEDEAGVKAAVEAGVRDALLDAGLVRAGAPRGASKPGDAEISPEHSPTDRDAGAAGGGDAAGQSDGNGQRTAASGATSESPASAFETGGGDEAADSAASTDGTRERPGSGTESRTGRFDAPAENARLPTGAGGPEADDQDTTSERDSLPDLRVLGQLHDTYVVAEAGDGLVLVDQHAADERVHYERLQARVDGASQALVAPAELELTAGEAAVFEAALGGLRELGFDAELAGRTARVTAVPAVLADALDAELARDVLSSFLADADGTPVADAADAVLADLACSPAIKGNTSLAEGSVVALLDALDACENPYACPHGRPTIVEVDGDELAARFERDYPGHAGRRREDAGN
The following text describes a protein:
Function:
May be involved in MAP kinase activation, epithelial sodium channel (ENaC) down-regulation and cell cycling.
Sequence:
MGTPASVASDPPGRAAPSARGRKRASANIFQGVGLPELRSLFQSGGAERPEERARLVWRYAGQRRMARALRQLRRRRAARPLGQPGACTSLQVLAIHQFLHDSHQQEELLQPFPVPGSPLSHKKGPQTHKQSWSCAGWPSAGCTAARNLTEHRGKSQARAAAVTCRMDGP
The following text describes a protein:
Function:
Phosphorylates Ins(1,3,4,5,6)P5 at position 2 to form Ins(1,2,3,4,5,6)P6 (InsP6 or phytate).
Domain:
The EXKPK motif is conserved in inositol-pentakisphosphate 2-kinases of both family 1 and 2.
Sequence:
MGKINASHSSYCYDSMLKRSDDKYLRSCSRIEPIDDPNEDDYDDDDDDDDGEDEHEQQSQRTRPAVWRQEKLDEELGHRASGVLDDERETRTIRYDLPEILERIDENRLMYRAEGNANIVLSLSDNKHVLRMRKSTVECREGKADSNVDLRRFVKYSQVIASQFSPCYVPAPKLAHLNTYNLQAFNERLRCFRPAMRLGKEIRELDGILYPDVAFLPKWLYPARVRDLSQDSKISSTPTTTHYQTYCVEIKPKQGWLAYEFCDNIPLPPEPLSNGGGDLRKCRYCLHQYLKLQKKSIAKISKYCPLDLYSGKPVRVLQAVKGLIGAPQNNFKILKNGKVVYDDKREKSMFNRILREMFPRDGRTKDERSTIFMNLIKEILLKDFTTNDEHCDRKLLSIKKDRKKKDKNQLHERACNPVNQQFLPQSCALRQILDVQLLVKSSISTIDPSKLNKSRSDPYSYIDEMYEKYLTYQEDALYDGRGSSRTTWPNGSFCAEYLSEEEQYQLGATALDCSIMITFRRLSGAEESSLTDAARNHIVSIEGMKFIVNVTITDLDPKSHKHYAKYVEQLASSAVAYRDFISKLRR
The following text describes a protein:
Function:
Plays a role in resistance to Gram-positive bacteria B.thuringiensis and M.nematophilum and Gram-negative bacteria S.boydii or S.flexneri infection and to fungus C.neoformans infection. Plays a role in susceptibility to Gram-negative bacterium S.typhimurium infection.
Sequence:
MAHKSIVIFSVLAVLCHSASVKVPPIVDSSLPVKFSEVIAEPAPNVPSNLASYAYALDIYVQTTLSQLQCIKQAGYCAVFVRAYNPAGQGSFDTSSCVTIQNAYKAGLGIEIYMTPQPVSNKQGYQQLDEIIQGLTARAITVRAIWIQVTSPTNWPNNANSNINFINSIVSRARQSGLTVGIYTSYYDWNQITTGWSNIGNDVLLWYWNVYSGGVTGETPANFNDFRKFGCWTAPSVKQFAQDETVCGITVNRDVYLAGNVLKAVEEDGKIYAGGFVQGSLKI
The following text describes a protein:
Function:
Non-SCF-type F-box protein involved in the endocytic with the vacuolar sorting pathway. Acts as a repressor of YPT52 by inhibiting the formation of active, GTP-bound, YPT52. Involved in the defense mechanism against methylmercury toxicity.
Miscellaneous:
MISCELLANEOUS: Present with 3080 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus. Cytoplasmic vesicle membrane; Peripheral membrane protein.
Domain:
The F-box domain is required for interaction with SKP1 and defense against methylmercury toxicity.
Sequence:
MAFQDQDIFIVFSHASLFLNQNDLLSLSLTSKKMHDMIAIPRLYSNIHITKNPVLRTNKWFLDGGKTYVSGYRSVLKTGDKNDIFLYDRIERLLETSHLKCIKQLTIDEDLFHNREEGLQLLQRLVNEITDLDVIESLDIKDPTLFELCSAKYYRLSSLKKRVVYGETGFDGIKLWQNFKSLKWQLPESLDLQNVIIPEVGVMLMKQLNGGELEIKDEAYSSLRVFEYFDSLNLRFKNLRRLKLNHVHKQGDGSATSMRLSSRAFKDVVNLSNLKALELEFSCEVDDCECDDDFLQDITGNLVSLTSLGFIEKTFTKKGYHYMDEKWDLVVNKFILNLPNVSKDLRLLSIRHDPPLNGKGIDTVDGNLLRRKKLYEKVLPKLTSLETIIAPTVLQSITSYEMYACDLLWNGCKCAFCSKYLPLFDKYIMNHQYFSTPDARYLDIIPIVFAAYTGKSLAKRFDPQKNWDLDLLQYAPEDTTWNFHGFERIHHFASYECYFDESSFEPLATIISHFFYPYMNYLIKILPNLRQTMLSGIYFSVSPELHTYETIYD
The following text describes a protein:
Function:
Catalyzes the dephosphorylation of diacylglycerol phosphate (DGPP) to phosphatidate (PA) and the subsequent dephosphorylation of PA to diacylglycerol (DAG).
Subcellular Localization:
Vacuole membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MEAVGKHVKLFWNVYSDYAVLIAISLSYFVFDVLMLPFTRQFSLEDITISHPFALHEQVPTKYLGIICVFFPALVLYGFGKLRNNSLLFWKSLMGLLYSTMVCGLCVSLLKNAVGRPRPDFLARCQPFESTPKTGLVDVLSCSVPWSDKVLQDGFRSFPSGHTSFSFAGLGFLAIFLAGQLKMFRNKTSSWKVVVPLVPLSIASWIGLSRSQDYRHHKEDIAVGALFGFAIAYVVYRQLFPPLDHHNADILYVQAELDEGYTNVHSAGNSSATNAEQMV
The following text describes a protein:
Function:
Component of the PEX13-PEX14 docking complex, a translocon channel that specifically mediates the import of peroxisomal cargo proteins bound to PEX5 receptor. The PEX13-PEX14 docking complex forms a large import pore which can be opened to a diameter of about 9 nm. Mechanistically, PEX5 receptor along with cargo proteins associates with the PEX14 subunit of the PEX13-PEX14 docking complex in the cytosol, leading to the insertion of the receptor into the organelle membrane with the concomitant translocation of the cargo into the peroxisome matrix.
Subcellular Localization:
Peroxisome membrane; Single-pass membrane protein.
Sequence:
MAEQSPSSAPQGGSGGNESFDNLVIQAPQLMREDYIQNAVKFLSHPRVKGSPVFHRRSFLEKKGLTSEEIDEAFRRVPDPKTNGTDAAAASMQQANNPSQSVALQPYTEVQPQAATTTATVGPIAPNTNVQFSWVNALLGAGLFLGLGASAAITLKKFFIPSLKSWTRRVVAEGDENANDELASKLCEEIREAIKVSTSAFSDIARTNQEVLASKDEDRKVLMKLTETFESQANVFKSLNETLNHIRENQFSRRNQLEEHVQPAPWNGPIDYQGRAFQQTNMYATPPNNSFDPGRNSFMPLAAEPSYGPFPGSYSEQRVQRPGGYGFQPQTSNDRLSVGTRGSYQGGSSNHHAGNAMDDPAAVAAEFQRRWVPPQPPGVIMPEAAAAIRQARLVPRQQPGDGHLSTDVPRPLESAMATTEHVNGAPEAPGGELPSHDGGTMTANASSCGGSEEQQQEAA
The following text describes a protein:
Function:
Plays an important role in centriole assembly and/or stability and ciliogenesis. Involved in early steps of centriole duplication, as well as in the later steps of centriole length control. Acts in concert with POC1A to ensure centriole integrity and proper mitotic spindle formation. Required for primary cilia formation, ciliary length and also cell proliferation. Required for retinal integrity. Acts as a positive regulator of centriole elongation.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, cilium basal body. Cytoplasm, cytoskeleton, spindle pole. Note=Component of both mother and daughter centrioles. Localizes to the basal body and centriole adjacent to the connecting cilium of photoreceptors and in synapses of the outer plexiform layer. Localizes to the inner scaffold in the central region of centrioles.
Sequence:
MASATEDPVLERYFKGHKAAITSLDLSPNGKQLATASWDTFLMLWNFKPHARAYRYVGHKDVVTSVQFSPHGNLLASASRDRTVRLWIPDKRGKFSEFKAHTAPVRSVDFSADGQFLATASEDKSIKVWSMYRQRFLYSLYRHTHWVRCAKFSPDGRLIVSCSEDKTIKIWDTTNKQCVNNFSDSVGFANFVDFNPSGTCIASAGSDQTVKVWDVRVNKLLQHYQVHSGGVNCISFHPSDNYLVTASSDGTLKILDLLEGRLIYTLQGHTGPVFTVSFSKGGELFASGGADTQVLLWRTNFDELHCKGLNKRNLKRLHFDSPPHLLDIYPRTPHPHEEKVETVETTETSGRTLPDKGEEACGYFLNPSLMSPECSPTTTKKKTEDMSDLPSESQRSIPLAVTDALEHIMEQLNVLTQTVSILEQRLTLTEDKLKDCLENQQKLFSAVQQKS
The following text describes a protein:
Function:
Probable transcription factor. Involved in stress responses. Plays a repressive role in cell expansion by counteracting the positive role of CPR5 in this process, but does not regulate cell proliferation or endoreduplication.
Subcellular Localization:
Nucleus.
Sequence:
MVGTKRVADSIDTNSDDTLTRNREVEVEAMLSRRKQLRTTTTRTTTTRTTPLSLSSSASKMNWSKNDELVILGGIVDYENETKLSYRSDWDALYRYIKDCVEAKFSKIQLINKVKNMKRKFTYNQGRSNHGEQLSFTNTDDDEIFKLSLIIWDKNESEYVSNENIDQAKDVPSGEPETNDVPCEEQDDRDVPCEEQERANIEIDNGVREKLDQAKDVPCVEQESEDVPCVEQERVSIEIDNGEKEKLDQTMDCEEQENTDVLCEEKGDKDVPCEEQENKDVPCEEQERVSIEIDNGEEEMSSEEDGVDEVGVMEDTLDSGISFQGLGKNGVKDKSEEDDVVELGVLQEIFKEDTFFQSLGRYQQKLLLQNLENVGVERRKELINEWKALFVDEQRLCVKKLTFAAKLANLGVSP
The following text describes a protein:
Function:
Catalyzes an essential step in the conversion of oligo-mannose and hybrid to complex N-glycans.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein.
Sequence:
MANLWKKQRLRDTGLCRLGILFAVTLSIVLMLVSVPRTALNGSSIDDDLDGLDKDLEAKLNASLLSVARGNRMSLRLHRRNHFSPRNTDLFPDLAKDRVVIVLYVHNRAQYFRVTVESLSKVKGISETLLIVSHDGYFEEMNRIVESIKFCQVKQIFSPYSPHIYRTSFPGVTLNDCKNKGDEAKGHCEGNPDQYGNHRSPKIVSLKHHWWWMMNTVWDGLEETKGHEGHILFIEEDHFLFPNAYRNIQTLTRLKPAKCPDCFAANLAPSDVKSRGEGLESLVAERMGNVGYSFNRSVWENIHQKAREFCFFDDYNWDITMWATVFPSFGSPVYTLRGPRTSAVHFGKCGLHQGRGDEGDCIDNGVVNIEVKETDKVVNIKEGWGVRVYKHQAGYKAGFEGWGGWGDDRDRHLCLDFATMYRYSSSSASP
The following text describes a protein:
Function:
Catalyzes the hydrolytic deamination of adenosine to inosine in double-stranded RNA (dsRNA) referred to as A-to-I RNA editing. This may affect gene expression and function in a number of ways that include mRNA translation by changing codons and hence the amino acid sequence of proteins; pre-mRNA splicing by altering splice site recognition sequences; RNA stability by changing sequences involved in nuclease recognition; genetic stability in the case of RNA virus genomes by changing sequences during viral RNA replication; and RNA structure-dependent activities such as microRNA production or targeting or protein-RNA interactions. Can edit both viral and cellular RNAs and can edit RNAs at multiple sites (hyper-editing) or at specific sites (site-specific editing). Its cellular RNA substrates include: bladder cancer-associated protein (BLCAP), neurotransmitter receptors for glutamate (GRIA2 and GRIK2) and serotonin (HTR2C), GABA receptor (GABRA3) and potassium voltage-gated channel (KCNA1). Site-specific RNA editing of transcripts encoding these proteins results in amino acid substitutions which consequently alter their functional activities. Edits GRIA2 at both the Q/R and R/G sites efficiently but converts the adenosine in hotspot1 much less efficiently. Can exert a proviral effect towards human immunodeficiency virus type 1 (HIV-1) and enhances its replication via both an editing-dependent and editing-independent mechanism. The former involves editing of adenosines in the 5'UTR while the latter occurs via suppression of EIF2AK2/PKR activation and function. Can inhibit cell proliferation and migration and can stimulate exocytosis; [Isoform 1]: Has a lower catalytic activity than isoform 2; [Isoform 2]: Has a higher catalytic activity than isoform 1.
Miscellaneous:
MISCELLANEOUS: [Isoform 1]: Alu insert from position 465 to 505. May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay; MISCELLANEOUS: [Isoform 5]: Likely expressed from an alternative promoter. Contains a region highly similar to the so-called ssRNA-binding R-domain of ADARB2.
Subcellular Localization:
Nucleus. Nucleus, nucleolus. Note=Shuttles between nucleoli and the nucleoplasm; [Isoform 1]: Nucleus. Nucleus, nucleolus; [Isoform 2]: Nucleus. Nucleus, nucleolus.
Sequence:
MDIEDEENMSSSSTDVKENRNLDNVSPKDGSTPGPGEGSQLSNGGGGGPGRKRPLEEGSNGHSKYRLKKRRKTPGPVLPKNALMQLNEIKPGLQYTLLSQTGPVHAPLFVMSVEVNGQVFEGSGPTKKKAKLHAAEKALRSFVQFPNASEAHLAMGRTLSVNTDFTSDQADFPDTLFNGFETPDKAEPPFYVGSNGDDSFSSSGDLSLSASPVPASLAQPPLPVLPPFPPPSGKNPVMILNELRPGLKYDFLSESGESHAKSFVMSVVVDGQFFEGSGRNKKLAKARAAQSALAAIFNLHLDQTPSRQPIPSEGLQLHLPQVLADAVSRLVLGKFGDLTDNFSSPHARRKVLAGVVMTTGTDVKDAKVISVSTGTKCINGEYMSDRGLALNDCHAEIISRRSLLRFLYTQLELYLNNKDDQKRSIFQKSERGGFRLKENVQFHLYISTSPCGDARIFSPHEPILEGSRSYTQAGVQWCNHGSLQPRPPGLLSDPSTSTFQGAGTTEPADRHPNRKARGQLRTKIESGEGTIPVRSNASIQTWDGVLQGERLLTMSCSDKIARWNVVGIQGSLLSIFVEPIYFSSIILGSLYHGDHLSRAMYQRISNIEDLPPLYTLNKPLLSGISNAEARQPGKAPNFSVNWTVGDSAIEVINATTGKDELGRASRLCKHALYCRWMRVHGKVPSHLLRSKITKPNVYHESKLAAKEYQAAKARLFTAFIKAGLGAWVEKPTEQDQFSLTP
The following text describes a protein:
Function:
Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MATPGGDKPLYPQIPRAQQVSMNIQNDTSRDEEVALRNVTHGSTFQCTVCGAQNQILMEHRRPVIVSKMAVNETQIAAGVQARATQVQGLLAQRKNEEAVRAALEDPPLQSKNDAVKDENAKAVMAALLACNKGEMQRAIDSLSSVQEDSLMKYVMRFLGVASQSAAMLEWHQKLSAKAGAGCIMRAFTERKQV
The following text describes a protein:
Function:
Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Melanosome membrane; Single-pass type I membrane protein. Mitochondrion membrane; Single-pass type I membrane protein.
Sequence:
MEPKWWLFMVLLLLGTVVQAHDGHADEDDDDEEDNDVIDVEEDLEDGIEEIEDSKPGDGATLPPSPKVIYKALVPTGEVYFVGAFDKGMLVGWVLSKVKKDDTDDEIAKYLKWESICKWEVEEMKESKLPGDKGLDYKLHFIFRHKNPKTDIDEEKYAKRPDMDLKTYFTDKKTHLYTLVLNPDNSFEILVDQMVVNSGNLLNDMTPPVNPSREIENPNDQKPEDWDERLKIPDPDAVKLDDWDDTASAKIPDKDATKPEGWLDDEPEYVSDPDAEKPEDWDEDMNGEWEAPQIANPKSPMIDNPNCQGIWKPRKIPNPDFFEDLEPFKMTPFSAVGLELWSMTSDIFFDNFIICKAADGAAEPDEMGQMLEAAEECPWLWVVYILIVALPLFLVVLFCCSGKKQPCAAEYKKTDAPQPDVKEEEEKEEKKEEKEKKDDEEEETEEKLEEKQKSDAEEDAGTVSQEDEDRKPKAEEDEVLNRSPRNRKPRRD
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that mediates ubiquitination of ACC synthases (ACS). Negatively regulates ethylene biosynthesis probably via ubiquitin-dependent degradation of ACS4 and ACS7 enzymes. Regulates lateral root formation and development by controlling ethylene production which inhibits lateral root formation at high concentration.
Sequence:
MRFLSLVGNSFGCSASGERLVSAARDGDLQEAKALLDYNPRLARYSTFGVRNSPLHYSAAQGHHEIVSLLVESGVDINLRNYRGQTALMQACQHGHWEVVLILILFGANIHRSDYLNGGTALHLAALNGHPRCIRILLSEYIPSVPNCWSLLKNKKTSVAGFDSSVLHEVINRAADGGITPLHVAALNGHIETVQLLLDLGASVTQVTVEDGTTIDLIGAGSTALHYASCGGNTQCCQLLISKGACLAAVNSNGWTPMMVARSWHRNWLEEILNPTTEQPQLHLPNVPSPFLCLPLMSIVNIAQECGWRENDCLTPCRDPCAVCLERKCTVAADGCAHEFCTNCALYLSTTSITSSKTSNVTPGSVPCPLCRNGIVSFTKLPHTTATTRTSTSSRTSISLSFCTCSSDVLDTALLTNPHYSCKPVVSRTGSRTPQSARSSAFRSLSCRRFPPSLCLGGSDVDEPRSRLIGGSYSRSGVGFRRSTSQVEGKRSWFSALNHCVTTGGSAC
The following text describes a protein:
Function:
Glucosyltransferase involved in the biosynthesis of the non-bilayer-forming membrane lipid beta-monoglucosyldiacylglycerol which contributes to regulate the properties and stability of the membrane. Catalyzes the transfer of a glucosyl residue from UDP-Glc to diacylglycerol (DAG) acceptor to form the corresponding beta-glucosyl-DAG (1,2-diacyl-3-O-(beta-D-glucopyranosyl)-sn-glycerol). It can only use UDP-Glc as sugar donor. Two types of DAG (dipalmitoyl-DAG (DPDAG) and 1-oleoyl-2-palmitoyl-DAG (OPDAG)) can be used as sugar acceptors, but OPDAG is preferred.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MPQFPWKDNDAELSPLEAFLAEWDDPEAEEEDFRNDFFRGSEGRRKKAAVMLMAIWTVVITLHYWVWGSWLVWALTGALSLQALRLMKATPEEAPPLLTGDASTVPYPQVCLMVAAKNEEAVIGKIVQQLCSLDYPGDRHEVWIVDDNSTDRTPAILDQLRQQYPQLKVVRRGAGASGGKSGALNEVLAQTQGDIVGVFDADANVPKDLLRRVVPYFASPTFGALQVRKAIANEAVNFWTRGQGAEMALDAYFQQQRIVTGGIGELRGNGQFVARQALDAVGGWNEQTITDDLDLTIRLHLHQWKVGILVNPPVEEEGVTTAIALWHQRNRWAEGGYQRYLDYWRWICTQPMGWKKKLDLFSFLLMQYLLPTAAVPDLLMALWQRRFPLLTPLSYLAIGFSCWGMYYGLKRLTPSEGESPWQQMPALLARTIGGTIYMFHWLIIMPAVTARMAFRPKRLKWVKTVHGAATEDALELKQS
The following text describes a protein:
Function:
Involved in cellular auxin homeostasis by regulating auxin metabolism. Regulates intracellular auxin accumulation at the endoplasmic reticulum and thus auxin availability for nuclear auxin signaling.
Subcellular Localization:
Endomembrane system. Membrane; Multi-pass membrane protein.
Sequence:
MDILGVTFIAVSKVIVAVLVGVFTTDSIPNSKITLHNFAFLISSLLLASLTLSNTAKSIDLDVLFRCSILILFSLISIASGLLWGAVLDVLFFRLDPKYSGIPEELRKDVRLELLYDRVTDEGAEAHCLPSSSPTTKGPGTKAKRKKTSVPYVVVVLSEHFREVGVTGSEIVNALEVPDERQEDCAGYRYAAWVGCSTQNGVTLPLSLMSNVASSISFIDMTHSAAYIFVFSISYMLYLWSACPAIVEAGQKAAKKQRLIREILLKHKRMMARCDATTQTLSLPVSQVLESAEDLEEDVEVDSCDSEAGQARRLECQVDRFTQLYLAVSDPSSSSTSCSDNTSSLEAGGVANTDGCSSRADRHVHSATYSFDLITSLQSSFTQMRRLARISGKRGAAEVTFKILGTPATRSPTAADERAFAMSTAEQLPYDWAAAGYIRFKYESELKALRTKSASEKVQQLGRASWVLVKKLMTSPPFLSVVLGIVIGIVPPVRRLSEHWPLPMVMDAIRLIGEGSIPSSLLLLGANLAVSSSANAAESAEVRLRHAEQNTEYPLLPEEWQLLGEDVAYARWYDAQHTDMEFDLHESFSLQTLMQRGLLHASMMPGGASAASAAPMGDDTDEEGGGAKKGTFMDGVQRTLSLKGIRPAFVWGIIIFRMLISPTLSFFLLIFLIDKMPFLFGGRGSLDKTLIMVLMVELAAPTAINSTLLFNAYKFMTYQWAKMLFFQYILCVLSMVMWASIGLSYVSSL
The following text describes a protein:
Function:
Functions in two distinct reactions of the de novo folate biosynthetic pathway. Catalyzes the addition of a glutamate residue to dihydropteroate (7,8-dihydropteroate or H2Pte) to form dihydrofolate (7,8-dihydrofolate monoglutamate or H2Pte-Glu). Also catalyzes successive additions of L-glutamate to tetrahydrofolate or 10-formyltetrahydrofolate or 5,10-methylenetetrahydrofolate, leading to folylpolyglutamate derivatives.
Sequence:
MDYQNTLKYLYESTPMFQQIGGKAYKPGLETTHKLDEHLGHPHQQFRTIHIAGTNGKGSCSHTIAAVLQAAGYKVGLFTSPHLIDFRERIRINGEMIPEDYVVSFVEEHRSFFEPLHPSFFELTTAMAFRYFADQQVDVAVIEVGMGGRLDCTNIITPDLCVITNIGFDHMQYLGHTLTKIAKEKAGIIKEDVPVVVGKVSGTVKRVFTMKAKAMNTFITFSEELKSFTHVQYLSYDNLKESRADLQELLEEEIKLQQIQTLPMKMMQFVSLINPADAIRAIDRIMDKRKDAISIHNSSFMTGLYYELSGLYQTENCLTILAALDILKNLGYEICNKDYHTGFSNVCEMTGLMGRWQKLQSYPDLICDTGHNADGFKSIRKQLKYIHEKLHQELHIVFGMVSDKDISSVLELLPKDATYYFTKASVKRAMPEDELMKMASEAGLKGTSYPTVVDAVRAAKENCPPKDFIFVGGSSFIVADLLANRDTLNLH
The following text describes a protein:
Function:
Involved in endoplasmic reticulum-associated protein degradation (ERAD). Acts as a platform to recruit both UBQLN1 and VCP to the ER during ERAD.
Subcellular Localization:
Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MHWFQGSIPEAIIASRNRKCIFVVVVTAEDEDSQQLLTRLEEENVSSVFNSFVSISLKSGSGEANMFSQLYPLVVLPAIYMIGLQGSPLEVIGGLVDIPTLLSRAQKALKVHDEQQNVAQASQISEAEVLQTTSENIEPSQEEETTESGNPGNSEDGPSGLSLEARLERADQLLAAVREKKIEEEREKEKIKERERRELGKQLQQFKEAQREREQRELADSRQKEKREEKEALEKIRQNIAQDRIDRAARYQAAQTSEEERRRAAQSAQEQLQRERASAARSAFSRLQFRLPDGSTRTEQFSSDVKLSSVNEFIDQQIKPPFRPYSLSTTFPRREFHESDMQQTLRELDLTPSAALLIIPVAGTGFKPQTNGSAGNTWLSAIFAPLFGIWNWIWGFFANPPPRVTHQDSTAQPQPNSQGVRRRRPDSNIHRLSDASPGDSSDDNGTWNGNSTQQL
The following text describes a protein:
Function:
Key component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. In the SEC complex, AFF4 acts as a central scaffold that recruits other factors through direct interactions with ELL proteins (ELL, ELL2 or ELL3) and the P-TEFb complex. In case of infection by HIV-1 virus, the SEC complex is recruited by the viral Tat protein to stimulate viral gene expression.
Subcellular Localization:
Nucleus. Chromosome. Note=Associates to transcriptionally active chromatin but not at snRNA genes.
Sequence:
MNREDRNVLRMKERERRNQEIQQGEDAFPPSSPLFAEPYKVTSKEDKLSSRIQSMLGNYDEMKDFIGDRSIPKLVAIPKPTVPPSADEKSNPNFFEQRHGGSHQSSKWTPVGPAPSTSQSQKRSSGLQSGHSSQRTSAGSSSGTNSSGQRHDRESYNNSGSSSRKKGQHGSEHSKSRSSSPGKPQAVSSLNSSHSRSHGNDHHSKEHQRSKSPRDPDANWDSPSRVPFSSGQHSTQSFPPSLMSKSNSMLQKPTAYVRPMDGQESMEPKLSSEHYSSQSHGNSMTELKPSSKAHLTKLKIPSQPLDASASGDVSCVDEILKEMTHSWPPPLTAIHTPCKTEPSKFPFPTKESQQSNFGTGEQKRYNPSKTSNGHQSKSMLKDDLKLSSSEDSDGEQDCDKTMPRSTPGSNSEPSHHNSEGADNSRDDSSSHSGSESSSGSDSESESSSSDSEANEPSQSASPEPEPPPTNKWQLDNWLNKVNPHKVSPASSVDSNIPSSQGYKKEGREQGTGNSYTDTSGPKETSSATPGRDSKTIQKGSESGRGRQKSPAQSDSTTQRRTVGKKQPKKAEKAAAEEPRGGLKIESETPVDLASSMPSSRHKAATKGSRKPNIKKESKSSPRPTAEKKKYKSTSKSSQKSREIIETDTSSSDSDESESLPPSSQTPKYPESNRTPVKPSSVEEEDSFFRQRMFSPMEEKELLSPLSEPDDRYPLIVKIDLNLLTRIPGKPYKETEPPKGEKKNVPEKHTREAQKQASEKVSNKGKRKHKNEDDNRASESKKPKTEDKNSAGHKPSSNRESSKQSAAKEKDLLPSPAGPVPSKDPKTEHGSRKRTISQSSSLKSSSNSNKETSGSSKNSSSTSKQKKTEGKTSSSSKEVKEKAPSSSSNCPPSAPTLDSSKPRRTKLVFDDRNYSADHYLQEAKKLKHNADALSDRFEKAVYYLDAVVSFIECGNALEKNAQESKSPFPMYSETVDLIKYTMKLKNYLAPDATAADKRLTVLCLRCESLLYLRLFKLKKENALKYSKTLTEHLKNSYNNSQAPSPGLGSKAVGMPSPVSPKLSPGNSGNYSSGASSASASGSSVTIPQKIHQMAASYVQVTSNFLYATEIWDQAEQLSKEQKEFFAELDKVMGPLIFNASIMTDLVRYTRQGLHWLRQDAKLIS
The following text describes a protein:
Function:
Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytosol. Mitochondrion. Nucleus.
Sequence:
MDMETVKEYLENSANIDGDELPLRFFERLIMHGLRVDLIETSRVICTFKVSPRLLNGSNYLHGGVTATLVDLVGSAAVYTVGAPFTGVSVEINVSYMDAAYADEEIEIEARALHVGKAVAVLSVEFRKKNTGKIIAQGRHTKHLSLPSKM