lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Required for the first step of diphthamide biosynthesis, a post-translational modification of histidine which occurs in elongation factor 2. DPH1 and DPH2 transfer a 3-amino-3-carboxypropyl (ACP) group from S-adenosyl-L-methionine (SAM) to a histidine residue, the reaction is assisted by a reduction system comprising DPH3 and a NADH-dependent reductase. Facilitates the reduction of the catalytic iron-sulfur cluster found in the DPH1 subunit.
Sequence:
MDFELNYEISRTVDYLRAGNFTRVALQFPDELLKDSPRVAKALRSELGAGVRLFVMADAAYGSCCVDEIGASHVDAECVVHYGHACMSPTSTLPAMFVFGKASIDIKDCADLIGHCLSSTNKPILVLYGLEYSHALMHLKAVVAESLVLSHSNWGPMVKYSDVIGSVINPSQDCTTEKDQIRSLNGSITNAGFTSGRDEKKILKFGNGRRMENGTCFELGGLTWSIPSDHKIEDYLLFWIGPENSAFTNVVLTFNNCEIIRYDADERRLLEDTSCQRRILKRRYYLVEKAKDANIVGILVGTLGCAGYLSIIQQMKELIKGAGKKSYTLVMGRPNSAKLANFPECDVFVYVSCAQTALLDSKEFLAPIITPFEAALAFGRGRQWTGEYVLNFHDLMVSSGPEAVSGTKEARFSFIKGGYMEDIQPEENGEHEERSLALAETTEKALNLQSQHPNTIMFKGAARSGSEFFAARSYQGLNRQYENLAPQSYVIGRSGRASGYADEKMQEK
The following text describes a protein:
Function:
Chromatin reader component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. YEATS2 specifically recognizes and binds histone H3 crotonylated at 'Lys-27' (H3K27cr). Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors.
Subcellular Localization:
Nucleus.
Sequence:
MSGVRRALAEKDPDYEEIAVAPPSKRHRAAEQSARDIAVQKIETIIKEQFAVEMKNKEHEIEVIDQRLIEARRMMDKLRACIVANYYASAGLLKPGEGTRSCDATILNHPSIKKFLESPSRSSSPAHQGSDAPSANHSESDSLSQHNDFFLDKDSGSLDADERLANSLDQRQSRSAGRDSLGVSSSQKPGQRNAGLSNDETSRLYVKKTIVVGNVSKYIPPDKREENDQSTHKWMVYVRGSRREPSINHFVKKVWFFLHPSYKPNDLVEVREPPFHLTRRGWGEFPVRVQIHFKDSQNKRIDIIHNLKLDRTYTGLQTLGAETVVDVELHRHSLGEEYLFSQSSESDLSDAPASLPLPLSIPAPVKASSPIKQLRDSSPDASVDKGFPGNAETERHATFYSLPSSIERTPTKLATQKVPFGSHGNSAFQPIAASCKIVPQGQIPSPAESPGKSFQPITMSCKIVSGSPISTPSPSPLPRTPTSTPVHMKQGSASSVINNPYVIVDKPGQMVGAAATSTGSPTSKLSSVCQASHGAGSPIPKSHGSSFVTSAVKQEDSLFATMPPLCPIGSHSKVQSPKSVTGGLGAFTKVIIKQEPGELPQQPQVSAAGPTTQTSVQQYVTVKGSHMLALSPQKPAVSTSEGTAQSKVVGVPVGSALQSTVKQAVAISGGQILVAKSGSSVAKAVGPKQVVTQGVAKAIVSGGGGTIVAQPVQTITKAQVTSTGAQKSTSQGSVMATLQLPATNLANLANLPPGTKLYLTTNSKNPSGKGKLLLIPQGAILRATNNASLQSGGSTNSGGGGTQSTSSNLSQHLTYTSYILKQTPQGTFLVGQPSPQSSGKQLTPASVVQGSVGVGASSTQGQALKVITGQKTALFTQATASGQTSLMKISDGSLKSVSASSQLSKPGTTVLRVSGGVITTAAAPAVALPTNGVAQQIDNAGSSSSSSGAPTAKTSGQQHQVCINQTQSASSVASKTATSTVVSVASLVTTPTPVTGKAAVSGLLKIHSNQSSPQQAVLTVPSQLKQLGVNTASGGVQTILMPMNKVIQSLSTSKVSAVTAVTSASTAVSSPSVASITKVKMEPDSTGQNCTSVGTQEGQAAVKTEENSELGNYVINIEYLENTQQLLTAIVKKVPLIAEKSEDVSSYCAGSVEQYYSWNIGKRRAAEWQRAMTVRKILQEIIEKHPRFHSITPLKTKHVVQWCRCHGYTPPDPETLRNDEDSIEDVLTQIDSEPEYPSSYSSGEDLCRKLEELQQFLKQEPEHEEEVDVLNFSEPLKINIKKEQEEKQEEMKFYLASLPASEFVRETAEKIGISFQPAEVQRNVYASVIEDMILKATEQLMSDILRQALAVAYQTTPHNRTPREITVMNIHKAICNIPFLDFLTNKHMKILNEEQ
The following text describes a protein:
Function:
Catalyzes the phosphorylation of D-glycero-alpha-D-manno-heptose 7-phosphate at the C-1 position to form D-glycero-alpha-D-manno-heptose 1,7-bisphosphate.
Sequence:
MKTIRTQTPLRLGLAGGGTDINLYCDKYTGYVLNATISLYIHCTLIKREDGKIIFDSPDTNSYCEYESKEFLGNDGKLDIFKSIYNRIVKDFTKKPLSFSLHTYSDVPSGSGLGGSSTLVVGVIKAFAEWLNLPLGEYEIAKLAYEIEREDLGIVGGAQDQYAATFGGFNFMEFYNNKRVIVNPLRIKNWIASELEARTVLYFTNITREAKDIEEHKKGKLGDEKSLEAMHAIKQDAIKMKEALFRADFGTLAQILGKSWRSKKIISEIVSNDELERIYKLAIDNGAYSGKTSGAGAGGFMFFFVDPTKKYNLIKALRKEQGYVQDFSFTKEGVKSWRI
The following text describes a protein:
Function:
Component of the sequence-specific heterotrimeric transcription factor (NF-Y) which specifically recognizes a 5'-CCAAT-3' box motif found in the promoters of its target genes.
Subcellular Localization:
Nucleus.
Sequence:
MTSSLHYHSDGSENEQPEKQSEAHSESSSPATGMSVPGIATPNMHYVMPTQLGNGNAMLQAQTAYPYPDPYYRSIFAPYDAQPYPTQPYPAQPMVHVQLMGIQQAGVPLPSDAIDEPVFVNAKQYHGILRRRQSRAKAESEKKLLKARKLKDEYQLCWTISARPNIIQLPYLHESRHLHALKRARGCGGRFTAKKTDNQQKQDESGDNSQVNINLESEKNEVASAENAS
The following text describes a protein:
Function:
May promote appropriate targeting of ribosome-nascent polypeptide complexes.
Sequence:
MTGSTETRHNEKDVKEPQVDSDADSDNEAIEHQLTEEQRRVAEAAGLGDHIDKQAKQSRSEKKARKLFSKLGLKQVTGVSRVCIRKSKNILFVINKPDVFKSPGSDTYIIFGEAKIEDLTQHAQMSAIENMKPTREAPQLKTVEEDDNEDVEEDSTGIEEKDIELVISQANTTRNKAIRALKDADNDIVNAIMSLTM
The following text describes a protein:
Function:
Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P).
Sequence:
MSKLSYQEVLSQIQYGLISSCQPVDDGPMDKPEIVSAMAQASVMGGRSGLRIEGVDNLKATRPFVNVPIIGIVKRDLPDSPVRITPFLQDIEDLANAGADIIAVDGTSRPRPVDIESAVKKIHEMGCLAMADCSNLEEGLYCKALGFDIVGSTMSGYTGGAVPEEPDYQLVKDLKSAGCFVMAEGRYNTPELAKVAIEIGADCVTVGSALTRLEHIVSWFANSVKSAR
The following text describes a protein:
Function:
Has a role in nuclear-cytoplasmic transport of proteins and mRNAs.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAALAASTVDSQRQKDDQATKAGEEFAKLFYDTLEKRRHLLSNLFLDTANVLWNGNAYSGKADIGKFYEGLPTCETDLAACDSQPIRDDFVQGQTTIHVIAAGRIKFSGKRWTPFSESFLLTAQGTVWKIVVDTFRFQEPAPI
The following text describes a protein:
Function:
Required for the formation of keratin intermediate filaments in the basal epidermis and maintenance of the skin barrier in response to mechanical stress. Regulates the recruitment of Langerhans cells to the epidermis, potentially by modulation of the abundance of macrophage chemotactic cytokines, macrophage inflammatory cytokines and CTNND1 localization in keratinocytes.
Sequence:
MPNPLNHSDLEEIFQPSPALRRYKGEGEDLLLRITEPPSSSELCYCLSKTSPLLGPSALRITMSRQSSVSFQSGGRRGFSASSAITPSVSRTSFSSVSMSRAGGGGGGGGYGRVSVGGSGGGFGSRSLYNFGMSKRISMGGSGGFRSGYGGRVGGGYGFGGGAGSGFGFGGGAGGGLGLGGGAGFGGGYGGAGFPVCPPGGIQEVTVNQSLLAPLNLQIDPTIQRVRTEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGHKTTRQNLEPLFESYINNLRRQLDSILNDRGRLDSELRNMQDTVEDFKNKYEDEINKRTTVENDFVILKKDVDTTYMSKVELEAKVESLGDEVNFTRTLFEMELSQMQGHVSDTNVVLSMDNNRNLDLNSIIAEVKAQYEDIANRSRTEAESWYQTKYEELQQTAGRHGDDLRNTKHEISEMNRMIQRLRAEIDNIKKQCANLQASIADAEQRGELALKDARAKLAELEDALQKAKQDMARQLREYQELMNVKLALDIEIATYRKLLEGEECRLSGEGVGPVNISVVTSSVSSGYGSGGGYGSGGGYGSGGGYGLGGGLGGGSGGYSYSSGGGGGLSVGGSGFSSGSGRGLGLSLGGGGGSSSSVKFVSTTSSSSRKSFKS
The following text describes a protein:
Function:
Probable essential component of SCF (SKP1-CUL1-F-box protein) E3 ubiquitin-protein ligase complexes, which mediate the ubiquitination and subsequent proteasomal degradation of target proteins. Regulates cell proliferation during embryonic and larval development.
Sequence:
MQVEEPVILYKLRSTDGQRFLADRRTIGMIGRIEDLFRNAGLDLIPADQLQPIQLEIPATVMRKVIEWCDHHKHDPPYDESEPETNDIPDWDASFLMVRHNMLFDIIRAARDFTVPGLFAMCCRVVGQNPREIIDGLVNDEEEEQPVYPVVAAAA
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MAFNPLLSLLKADAIFLGQLSKSSFCATSRAFSVFYFTRFKRSAYVSAPFGIEPHDEKELKTIDDNVHSNNLSWQKIQEHEVIRELYRKAAYELPGLTPYTQSFKKPADSQIFRFESDVQMSSFEKMNPKVVVTFKVTNIPLLEEKQRHVLRLLVGPRYNPEEDLVRISSDKYSSALQNKYHLIKILTSLIEESKRNAEKFSHVPLNTGHWKYKKCDKRMPQEWLADATTLTSKKKTTIGKQSHNTVLERESIATTDE
The following text describes a protein:
Function:
Methyltransferase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of the alkyl side chain (Probable). PynA subsequently forms the amide bond between the acyl chain and L-serine. Although pynA has a terminal reductase domain, it appears to require the thioesterase pynI for the release of the straight-chain intermediate from pynA via the formation of a tetramic acid pyranonigrin J. The methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I via N-methylation. The FAD-dependent monooxygenase pynG catalyzes an epoxidation-mediated cyclization to form the dihydro-gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the alcohol to the ketone and enolization to yield the characteristic tetramic acid-fused gamma-pyrone core of pyranonigrin H. Pyranonigrin H is substrate of pynH for dehydration-mediated exo-methylene formation from the serine side chain to produce pyranonigrin E, before the oxidase pynE reduces the exo-methylene of pyranonigrin E into a pendant methyl to form pyranonigrin G. The FAD-linked oxidoreductase pynB performs the reverse reaction and converts pyranonigrin G back to pyranonigrin E.
Sequence:
MSPSTINPESSPLHTYYFSMVEMSIMKLFLDHKIFTLIPTTPGASIPVTTLTTTLNASPSLLTRLTNFLIASGVLSSPQPGHIAHTPKSLQFTDPTSYQALFFAHIFDFFLVPAVKWPGYMAEHGLNEPTSASRTPFGYAAGYPDKTLYEILETMPKRAAQFNATMAASFQPMPVLGMYDFSWIEKLADEERMAIVDVGGGKGQALKEILGAYPGIRPEQCVLFDVDDVIREAVAEAERDDDETWRTVRKIPGSFFSEQPVKGAAVYHIRRVLNDWPDEDCVTILRRIRDAAAPNSRVLISEQILQEEPSLAVAALDLWMLNFGGKRRSEGMFGELAQRTGWKVNGVFRDKESDTGVVELVVA
The following text describes a protein:
Function:
The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Energy is transferred from the carotenoid and chlorophyll C (or B) to chlorophyll A and the photosynthetic reaction centers where it is used to synthesize ATP and reducing power.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MKSHISPISAPTNHPSATTMTAPRNPSLPPLALATPPSTSLSKYSPSLPFLRRPQFLTGEFAGDVGFDPLGLSSSSEKVLYYREAEIKHARLAMLAAAGWPLSELLDRPLTQQLDSSFNLSLSPALDATDRVPSVLNGGMLSDAISPIWWGVCLGAAAAVDLKGIQNARYSDAVDVNSGISSVNGEQQTYRPGDYNWDPLNLYPTDEEGQFRMQLAEIKHGRLGMLAITGFAVQEYVFGDGVVDETPGFFEPFNLF
The following text describes a protein:
Function:
May act as a GTPase-activating protein for Rab family protein(s).
Sequence:
MSSGSASTASTAGGTTTSADGTTSSSFWRNNSRTIPGRPTTVTNRIGSGRTIGAGSSGGSSSFQDYQDSVSDAWDLGDDEFCIISGVVDTRISKRASQTAALNVIKTHKSGAGGSVSKPQTSVHLDTQELLTGPATNPIEQQQSGGGDAHLEAELRIESLDIQSQSQQQQHQQHQQQQQQQQSSNDGVGYAHDQRLRQRFHAYPGRPQLLKLSSNVASKDVECESKYEKFSNILEAPLLNLIALKELSWSGVPRKMRAVTWRLLSGYLPTSLERRQTVLERKRVDYRKLVQQYFDADCRDESQQDTYRQIHIDVPRMNPHVALFQQKLVQEMFERILFIWAIRHPASGYVQGINDLVTPFFIVFLQEAVGPDKDLEQCQLSDLSIEQRDIIESDSFWCLSKFLDCIQDNYIFAQLGIQAKVNQLKELIQRIDGTLHRHLQMHGVDYLQFSFRWMNNLLTRELPLYCTIRLWDTYLAESDGFAVFQLYVCAAFLLHWREQLLQEKDFQGLMLLLQNLPTHNWMDSHIGVLVAEAFRLKFTYADAPKHLEAKS
The following text describes a protein:
Function:
Functions together with ADGRA2 to enable brain endothelial cells to selectively respond to Wnt7 signals (WNT7A or WNT7B). Plays a key role in Wnt7-specific responses: required for central nervous system (CNS) angiogenesis and blood-brain barrier regulation (By similarity). Acts as a Wnt7-specific coactivator of canonical Wnt signaling by decoding Wnt ligands: acts by interacting specifically with the disordered linker region of Wnt7, thereby conferring ligand selectivity for Wnt7. ADGRA2 is then required to deliver RECK-bound Wnt7 to frizzled by assembling a higher-order RECK-ADGRA2-Fzd-LRP5-LRP6 complex. Also acts as a serine protease inhibitor: negatively regulates matrix metalloproteinase-9 (MMP9) by suppressing MMP9 secretion and by direct inhibition of its enzymatic activity. Also inhibits metalloproteinase activity of MMP2 and MMP14 (MT1-MMP).
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Domain:
The Kazal-like domains mediate the serine protease inhibitor activity.
Sequence:
MATVRASLRGALLLLLAVAGVAEVAGGLAPGSAGALCCNHSKDNQMCRDVCEQIFSSKSESRLKHLLQRAPDYCPETMVEIWNCMNSSLPGVFKKSDGWVGLGCCELAIALECRQACKQASSKNDISKVCRKEYENALFSCISRNEMGSVCCSYAGHHTNCREYCQAIFRTDSSPGPSQIKAVENYCASISPQLIHCVNNYTQSYPMRNPTDSLYCCDRAEDHACQNACKRILMSKKTEMEIVDGLIEGCKTQPLPQDPLWQCFLESSQSVHPGVTVHPPPSTGLDGAKLHCCSKANTSTCRELCTKLYSMSWGNTQSWQEFDRFCEYNPVEVSMLTCLADVREPCQLGCRNLTYCTNFNNRPTELFRSCNAQSDQGAMNDMKLWEKGSIKMPFINIPVLDIKKCQPEMWKAIACSLQIKPCHSKSRGSIICKSDCVEILKKCGDQNKFPEDHTAESICELLSPTDDLKNCIPLDTYLRPSTLGNIVEEVTHPCNPNPCPANELCEVNRKGCPSGDPCLPYFCVQGCKLGEASDFIVRQGTLIQVPSSAGEVGCYKICSCGQSGLLENCMEMHCIDLQKSCIVGGKRKSHGTSFSIDCNVCSCFAGNLVCSTRLCLSEHSSEDDRRTFTGLPCNCADQFVPVCGQNGRTYPSACIARCVGLQDHQFEFGSCMSKDPCNPNPCQKNQRCIPKPQVCLTTFDKFGCSQYECVPRQLACDQVQDPVCDTDHMEHNNLCTLYQRGKSLSYKGPCQPFCRATEPVCGHNGETYSSVCAAYSDRVAVDYYGDCQAVGVLSEHSSVAECASVKCPSLLAAGCKPIIPPGACCPLCAGMLRVLFDKEKLDTIAKVTNKKPITVLEILQKIRMHVSVPQCDVFGYFSIESEIVILIIPVDHYPKALQIEACNKEAEKIESLINSDSPTLASHVPLSALIISQVQVSSSVPSAGVRARPSCHSLLLPLSLGLALHLLWTYN
The following text describes a protein:
Function:
Catalytic component of the COMPASS (Set1C) complex that specifically mono-, di- and trimethylates histone H3 to form H3K4me1/2/3. Binds RNAs which might negatively affect its histone methyltransferase activity. COMPASS recognizes ubiquitinated H2B on one face of the nucleosome which stimulates the methylation of H3 on the opposing face.
Subcellular Localization:
Nucleus. Chromosome.
Domain:
The RxxxRR motif forms an adapter helix that bridges the nucleosome and ubiquitin.
Sequence:
MPYSSQQNGYTSASTSRLSEQTSSHSRSSREDRHLTEKGRRPPSPEARHRSDRDYDRRRSTEYVRDDDYRRSSRSSHDSRYADAYDHWRSARSAYSPTPRDDRRDEARNDLSSTKRHRSPEHSTSRLRHRSPESAHRRQNGTANRLDSKPDRGGDRKTGEALDSGRSRWSQRAYEYDDWRNERPSARYERYRHDREPHRSRREDEYETKRSRDDSNGNSIYAPTRRSRSRSRSRSRSRDRYRSRDHSRERRRERSRDRSNGTYSSRDDRRPKADRSAHTIKRDEHSTRLNGTSEDSKDLRHESQRRVSASVQSASEGPASTPVARAVYIKHAEVDQEAPAPPTTRDYHSCPQRWPDQADSAVRASSAPNGSATAPSRSDRPPANGSSGRHSPRSLPTREKAEEARTSSTRRPSSQTNDNVNNSRDPLTQRKATSERSFGHVLLPHELPVECRGKNYMATATYKEGVKSIYKSAADKHLVDVDTRDPRRLGKKSSRYRESLHSASFRWDSNSRGKKPLPPPRNLVLTNLSGLLQPHQILLHILPHGRIESSKLEIDPKIGQSLGIFRVTFAHDFDEHGKPLESMPAGQNPQHGAKVAKAACLALNGRMIGQTRAQAFLDRDGEVIAERIKAKLAENEHKLRPTIVPPAPPAAASSSPATPSTTKQSMPPPQVPRGPKVFMPAAPSPSYASSPASARANTDRYEYSATSHSRYRSSYEESRKLASSETYHRRRGTEEYDTYNRSKPYADAQVPAGSRSETRKDIKRPDEEILNELRDKKRPYVHIPRPKNCDIDVTSVEAQLRSTAPIWVREGQKGFYAAFHTSKEANQCKVVNETLTIGGYTLQVDVRSAPSQHAPSQQIRTPSGKHASVPLSMPAPPKQERKAIDTGLRPPTADEKLKVDWSAAELQDAVFRMLQKELADTFVRDVKSRVVGPYLTAYLKPDGEGGKMLAKATMKKPVIPTSINDHGTTLFEATGEARLPSFRKLAGAHPKKKASDADTTTSQAKRDQTDAKKKRGHTHRSKVHRDRDVSSSENESDDMERGMVVAARRNSYTRSKSSTKRRGAAAWLLEASDAEAGTDDVDSTETDALSRSVSASVEPTGEEQIEVDVGAKAKKIPKVKAATVSKKKGTTAARKKLDVAPPEAVVEADQGSETATPETDVPIKTAAAKAKVKPAKTSAKAKSALVDPFEAGLVEDSEDCHYLRLALEHLSRTGELASEHTLPDEIELEVEAEEQAMAAGGIPKHSTGSARTEGYYRIPPEQKAMHLPDRNKATEDVDTSSNAQILQSARNNRADSRRLVLGIEQHKRETATDTDIFKFNQLRTRKKQLKFAKSPIHDWGLYAMELIPAGDMVIEYVGEVVRQQVADEREKQYERQGNFSTYLFRVDDDLVVDATHKGNIARLMNHCCTPNCNAKILTLNGEKRIVLFAKTAIRAGEELTYDYKFQSSADDEDAIPCLCGSPGCRRFL
The following text describes a protein:
Function:
Constitutes the active form, which associates with RELA/p65 to form the NF-kappa-B p65-p50 complex to form a transcription factor. Together with RELA/p65, binds to the kappa-B consensus sequence 5'-GGRNNYYCC-3', located in the enhancer region of genes involved in immune response and acute phase reactions.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MDDTHYQIGFVVNEPMTFPSAYDDLPYMPEAFEVKHEPFVQETVDGPYIQIIEEPKQRGFRFRYECEGPSHGGLPGASSERNRRTYPTVKVLNFVGNARVEVQLVTHTDPPRVHAHSLVGRHCNESGVCSVDVGPSDFTAQFSNLGILHVTKRGVVEVLTKRLKEEKRKVKGPGYKFSDAEENALMQEAKELGKNMDLNIVRLKFTAYLQDSNGSYTRALKPVVSNPIYDSKSPNASNLKISRMDKTSGSVLGGEEVFLLCDKVQKDDIDIRFYEEEDEWEALGDFSPTDVHKQYAIVFKTPPYRCTNIDRPVTVFLQLKRKKGGDCSEPKQFTYVPHNQDKEEVQRKRMKALPDHYGGWRGGPQGGAGGFGGPGSGTGGGGGMGGGFPFNPMDNSSFFVGGCGGFGGGAQMSDSPPQTDGANTQSQSNSQIRQQLIQIALHNRANLAAKCNARALLQYSSTGDARPLLALQRHLCGVQDENGDTPLHLAIIHQKTVVAEQLIKALNSSPQQKFFNKLNKLSQAPLHLAVITKQPKLVEMLMKSGADPSLLDREGRTVLHLAAHTGDDVILRLVLSLLGEHHSHLINSADFTGQYPVHLAVKKDGERCLRLLVEAGAKINMPEQKSGCTALHLAVRDNLLKLACNLITELKADVNACTYGGNSPLHLAASQGSPHLCSMLIAAGADKRIENDEPLFLSSSSSDEDEESEKKLSEDMVQQVHCLSISSERGVFNPRKRPAAGHTPFDLAKSQKVRDLLDGRKGPKPNSLSPKRTKISTEEVNQDLDNEVLSKLCGILIHDDVPWRELAEKLGMLTLTHLYQDSASPCQKLLESYQLSGGPVDGLVEALQALGVREGVRLLRDSQPREDKQSSDSTEDSGFGSQSIGEEMANPAVGNH
The following text describes a protein:
Function:
Recruits TFIIH to the initiation complex and stimulates the RNA polymerase II C-terminal domain kinase and DNA-dependent ATPase activities of TFIIH. Both TFIIH and TFIIE are required for promoter clearance by RNA polymerase.
Subcellular Localization:
Nucleus.
Sequence:
MSSSLERQQASFMSSMSAASSKLAGTKRALAPPSPSPSVGSVASAVAAGSGTPRKAADRVDTPAHNIVYSQPAATGTGLNIITQVTYAIAWLRGKDEPRTYLEILGHLSGLHWSPSYQEEFVEAMRRTREIQWIPDPNLSEQTWQSGTYLHRPKVPGVRNKTQLLAYLQKKTDASCVGVKELKDGWPDCEKAINELEAEHKILVIRVKKEGSPRYVWLDDPSLFHEVDPELKVMWQKVEVPGTDTIVQRLKAASQKPASEDPRDKMTAAPKAEKKKRAQRRTGKATNTHMEHLLKDYSHMKR
The following text describes a protein:
Function:
ATP-dependent carboxylate-amine ligase which exhibits weak glutamate--cysteine ligase activity.
Sequence:
MPARRSAARIDFAGSPRPTLGVEWEFALVDSQTRDLSNEATAVIAEIGENPRVHKELLRNTVEIVSGICECTAEAMQDLRDTLGPARQIVRDRGMELFCAGTHPFARWSAQKLTDAPRYAELIKRTQWWGRQMLIWGVHVHVGIRSAHKVMPIMTSLLNYYPHLLALSASSPWWGGEDTGYASNRAMMFQQLPTAGLPFHFQRWAEFEGFVYDQKKTGIIDHMDEIRWDIRPSPHLGTLEVRICDGVSNLRELGALVALTHCLIVDLDRRLDAGETLPTMPPWHVQENKWRAARYGLDAVIILDADSNERLVTDDLADVLTRLEPVAKSLNCADELAAVSDIYRDGASYQRQLRVAQQHDGDLRAVVDALVAELVI
The following text describes a protein:
Function:
Regulatory subunit of lactose synthase, changes the substrate specificity of galactosyltransferase in the mammary gland making glucose a good acceptor substrate for this enzyme. This enables LS to synthesize lactose, the major carbohydrate component of milk. In other tissues, galactosyltransferase transfers galactose onto the N-acetylglucosamine of the oligosaccharide chains in glycoproteins.
Subcellular Localization:
Secreted.
Sequence:
LKWLIEDVALALSWRRSSHSVSRSWRHWSLSATWGVLDSVWHLGSWRLGVNVLVICVTFHSSGFNTQIKVSNNGNTEYGIFQISNNGWCAEKQEDVAKSTCGILCSKLLDDDINDDIVCAKKIIEQPKGIDYWKAHKTFCLENLDQWRCLN
The following text describes a protein:
Function:
Tubulin-folding protein; involved in the final step of the tubulin folding pathway.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSEKFVELRKEFLTKLYKSTPSEQTSRSEKETWLEEKSKYLGEMTRELNEVQDQIAPYDRRVCMEQLVDLTRRLQQIRHDILPRQPFRFQRALHVKSSQKPVKNITVNAEAPEVYFENDTLYLANLKNQNIGDNVIPYPNNKAVKVSAKSLRSCNISISNCSSVNLHNATKCNFTFPTIQGSIHLSDINDSTICVSCHQFRLHHSTNLRVHLRCKTSPVIEESKEISFSYKDEHPILDFTWARSDPSPHFRITSDLFDA
The following text describes a protein:
Function:
Cytoplasmic protein that plays a role in the proper assembly of dynein arm complexes in motile cilia in both respiratory cells and sperm flagella.
Subcellular Localization:
Cytoplasm.
Sequence:
MDADQEKDLQKFLKNVDEITNLIQEMNSDDPVVQQNAVLETEKRLLLMEEDQEEDECRTTLNKTVISPPQTAVKSAEEVNSEAFLASVEKDAKERAKRRRENKVLADALKDKGNEAFAEGNYETAILHYSEGLEKLKDVKVLYTNRAQAYMKLKNYEKALVDCEWALKCDEKCTKAYFHMGRANLALKNYSVSRECYKKILEINPKLQTQVKDYLNQVDLQEKADLQEKEAHELLDSGKNTAVNTKNLLETLSKPDQIPLFYAGGIEILTEMIKECTEQTLFRMHDGFSIISDNEVVRRCFSTAGKDAIEETVCVSVLKLWQAVCCGNEENQRVLVMHPDRARLLATLLSSKVLAIRQQSLALLLQLAQTESGRSLIISHLDLTRLLEALVSFLDFSDKEANTAMGLFTDLALEERFQVWFQANLPGVLPAVTSVLKTDPKVSSSSALCQCIAIMGNLSAEPATRGHMAACEEFGDGCLSLLARCEENVALFREVIYTLLGLMMNLCLQAPFVSEVWAVEVSRRCLSLLNSQDGGILTRAAGVLSRTLSSSLKIVEEALQAGVVKKKKKKKKKKKKK
The following text describes a protein:
Function:
Anorexigenic peptide. Increases the pigmentation of skin by increasing melanin production in melanocytes; Endogenous opiate; Endogenous orexigenic opiate; Stimulates the adrenal glands to release cortisol.
Subcellular Localization:
Secreted.
Sequence:
GPRLCRTVRSGGATRTSPRGQCHPECLRACKLDLSAEAPVIPGNGHLEPLSENVRKYVMSHFRWDQFGRKNGSGGSVAGLRDLLLPRPGAGAGIGGDPRAAPPSVPQPRDLPLTKRSYSMEHFRWGKPVGRKRRPVKVHPNGVEDESAEEFRRGLAGDVDYSEEAEPVLPREPGRELEQEAGDGERRWEEEEEEREEEDGEVRGEEEREEEAGDGEVYRMRHFRWGRPAKDKRYGGFMTSERGPMPLVTLFRNAIANSAHKKGQ
The following text describes a protein:
Function:
Catalyzes the transfer of pyrophosphate from adenosine triphosphate (ATP) to 6-hydroxymethyl-7,8-dihydropterin, an enzymatic step in folate biosynthesis pathway.
Sequence:
MHKVFIAIGSNIGDRRKNIETALKKMEELGLRIIKKSSIIETEPYGYKDQDKFLNGVVLVETGFDPFELLELLLNIEKEMGRERKIKWGPRNIDLDIIFYDDLVIDTENLKIPHPDAHNRTFVMGPLSEIAPDFVHPVLKKRVEEIYKELIEKNA
The following text describes a protein:
Function:
Serine/threonine-protein kinase which may phosphorylate the same targets substrates as PKH1 and PKH2, 2 upstream activators of PKC1.
Sequence:
MTSRKRSPHDFIFKEELGHGSYSTVFKALDKKSPNKIYAIKVCSKKHIIKEAKVKYVTIEKNTMNLLAQKHHAGIIKLYYTFHDEENLYFVLDFAPGGELLSLLHKMGTFNDIWTRHFTAQLIDALEFIHSHGIIHRDLKPENVLLDRDGRLMITDFGAAATIDPSLSGDSAKFNSDSNGSKDNQNCASFVGTAEYVSPELLLYNQCGYGSDIWALGCMIYQFVQGQPPFRGENELKTFEKIVALDYPWGPNNRINNSTSPINPLVINLVQKILVIEVNERISLEQIKRHPYFSKVDWNDKIKIWRGIWQSQGQSLQQTTLGLPNIPQNILPTRQLHVIDTPARSIQITKQKRKKPTKISNTTSSIVVWRKRLGISTGKDDLGTVPSTTPAVTAPNDTNVLTNTAAHSTANIALPPNSQSNQVKRAQLVAPNRIPPKVPVINDNVRNKSIPRTKPNVPPLQTSSIPQKLSTSSASSALSAPSTEIRNQDLTHTLDGRNSIDIHVLKQDYVFIYGIPYEHEGPAMSLNSYNKIDNDLITSLVAQHKEELKNSESFLQVLTLKKSGMLSYKNTVMEGNDDQENKEHQMANIEDTDLSMYDFEFNELTRKGFLILEKYKNRIWFISLPSYSTLSKIPFNAVKSSTINNNENWVDCFFRARQLLEEKQILDKISNVSFDSKASSEPSSPPPISRKERPLSIGNNVTTLSYTAKNGSQNNAPQNDNVGEEKPFRIPSSTKDRPGANSTPSSRHPRVLSSNNAGETPKKMNGRLPNSAPSTNTYTNGSVPAFNHRPSTNVGNNKHNILTSKKQGSSVFSPSSSTTKPQIKTTGYRQPTPSPPLPQMEFPTTREKYSAPSNMVISSSRYEVLHTLNNSQTNFDREIASRGASAAFRSLQKSKKKK
The following text describes a protein:
Function:
Transcriptional activator that regulates SEMA3C and PLXNA2. May regulate genes that protect epithelial cells from bacterial infection. Involved in gene regulation specifically in the gastric epithelium. Involved in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression. Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions.
Subcellular Localization:
Nucleus.
Domain:
The GATA-type zinc fingers mediate interaction with LMCD1.
Sequence:
MALTDGGWCLPKRFGAAAADAGDSGPFPAREPSSPLSPISSSSSSCSRGGDRGPCGASNCRTPQLDTEAVAGPPGRSLLLSPYTSHPFAAAHGAAAPGVAGPGSALSTWEDLLLFTDLDQAATASKLLWSSRGAKLSPFAAEQPEEMYQTLAALSSQGPAAYDGAPGGFVHSAAAAAAAAAAASSPVYVPTTRVGSMLPGLPYLQGAGSGPSNHAGGAGAHPGWPQASADSPPYGGGGAAGGGAAGPGGAGSATAHASARFPYSPSPPMANGAARDPGGYVAAGGAGAGSVSGGGGSLAAMGGREHQYSSLSAARPLNGTYHHHHHHHPTYSPYMGAPLTPAWPAGPFETPVLHSLQSRAGAPLPVPRGPSADLLEDLSESRECVNCGSIQTPLWRRDGTGHYLCNACGLYSKMNGLSRPLIKPQKRVPSSRRLGLSCANCHTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMKKEGIQTRKRKPKNINKSKACSGNSSVPMTPTSSSSNSDDCTKNTSPPTQSTASGVGASVMSAVGESANPENSDLKYSGQDGLYIGVSLSSPAEVTSSVRQDSWCALALA
The following text describes a protein:
Function:
Bifunctional enzyme localized in the lumen of the endoplasmic reticulum that catalyzes the first two steps of the oxidative branch of the pentose phosphate pathway/shunt, an alternative to glycolysis and a major source of reducing power and metabolic intermediates for biosynthetic processes. Has a hexose-6-phosphate dehydrogenase activity, with broad substrate specificity compared to glucose-6-phosphate 1-dehydrogenase/G6PD, and catalyzes the first step of the pentose phosphate pathway. In addition, acts as a 6-phosphogluconolactonase and catalyzes the second step of the pentose phosphate pathway. May have a dehydrogenase activity for alternative substrates including glucosamine 6-phosphate and glucose 6-sulfate. The main function of this enzyme is to provide reducing equivalents such as NADPH to maintain the adequate levels of reductive cofactors in the oxidizing environment of the endoplasmic reticulum. By producing NADPH that is needed by reductases of the lumen of the endoplasmic reticulum like corticosteroid 11-beta-dehydrogenase isozyme 1/HSD11B1, indirectly regulates their activity.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MKCPGVWGMLTVTMCVVFLGCPQAQELQGHVSVILLGATGDLAKKYLWQGLFQLFLDEAGKGHSFSFHGAALTAPKQGQELMAKALESLSCPRDMAPSRCAELQAQFLRLSRYRQLKTAEDYQALGRDIEAQVQQEGLREAGRMFYFSVPPFAYADIARNINSSCRPGPGAWLRVVLEKPFGHDHLSAQQLATELGSFFQEEEMYRVDHYLGKQAVAQILPFRDQNRRALDSLWNRHHVERVEIIMKETVDAEGRTSFYEEYGVIRDTLQNHLTEILTLVAMELPANVSCSEAVLRHKLQAFRALRRLQRGSAVVGQYQTYSEQVRRELRKPAGSPSLTPTFAGVLVHVDNLRWEGVPFILMSGKALDERVGYVRVLFKNQAFCAQSEKHWAPAQSRCLPRQIIFYIGHGELGHPAVLVSRNLFRPFLPAQSWREVEDRPGLQLFGRPLSDFYAFSPVKERDAYSILLSHIFHARKESFVPTEHLLASWVFWTPLLESLAREVPRLYPGGADSGRLLDFEFSGSHLSFSLGQPEQLVPGPGSTPRPSDFQVLGAKYRESPLISAWPDELISKLASDIEAAAVQAVRRVGTFHLALSGGSSPIALFQQLASGHYGFPWAHTHLWLVDERCVPLSDPESNFQGLQAHLLQHVRVPYYNIHPMPVNLHQRLCAEEDRGAQAYASEISALVTNCSFDLVLLGMGTDGHTASLFPQSPTGLDGEQLVVLTESPSRPHQRMSLSLPLINRAKKVAVLVMGRTKRDITLLVSRVGREPKKWPISGVLPTSGQLVWYMDYEAFLG