lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis (By similarity). In human cytomegalovirus, forms two distincts complexes to mediate viral entry, a trimer and a pentamer at the surface of the virion envelope. The gH-gL-gO trimer is required for infection in fibroblasts by interacting with host PDGFRA, and in glioblastoma cells by interacting with host EPHA2. Thsi trimer may also be required in other cell types using host TGFBR3. The gH-gL-UL128-UL130-UL131A pentamer is essential for viral entry in epithelial, endothelial and myeloid cells via interaction with host NRP2.
Subcellular Localization:
Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane; Single-pass type I membrane protein. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN).
Sequence:
MRPGLPSYLIILAVCLFSHLLSSRYGAEAVSEPLDKAFHLLLNTYGRPIRFLRENTTQCTYNSSLRNSTVVRENAISFNFFQSYNQYYVFHMPRCLFAGPLAEQFLNQVDLTETLERYQQRLNTYALVSKDLASYRSFSQQLKAQDSLGEQPTTVPPPIDLSIPHVWMPPQTTPHGWTESHTTSGLHRPHFNQTCILFDGHDLLFSTVTPCLHQGFYLIDELRYVKITLTEDFFVVTVSIDDDTPMLLIFGHLPRVLFKAPYQRDNFILRQTEKHELLVLVKKDQLNRHSYLKDPDFLDAALDFNYLDLSALLRNSFHRYAVDVLKSGRCQMLDRRTVEMAFAYALALFAAARQEEAGAQVSVPRALDRQAALLQIQEFMITCLSQTPPRTTLLLYPTAVDLAKRALWTPNQITDITSLVRLVYILSKQNQQHLIPQWALRQIADFALKLHKTHLASFLSAFARQELYLMGSLVHSMLVHTTERREIFIVETGLCSLAELSHFTQLLAHPHHEYLSDLYTPCSSSGRRDHSLERLTRLFPDATVPATVPAALSILSTMQPSTLETFPDLFCLPLGESFSALTVSEHVSYIVTNQYLIKGISYPVSTTVVGQSLIITQTDSQTKCELTRNMHTTHSITVALNISLENCAFCQSALLEYDDTQGVINIMYMHDSDDVLFALDPYNEVVVSSPRTHYLMLLKNGTVLEVTDVVVDATDSRLLMMSVYALSAIIGIYLLYRMLKTC
The following text describes a protein:
Function:
Sequence-specific RNA-binding protein that regulates translation and mRNA stability by binding the 3'-UTR of target mRNAs.
Sequence:
MDSPMTARMLKMSDDNNKRNAETRFVGIANAPTTPSPFLHPDHVAVGSPISRVPLSPSPAPPPPPPPSPRFRLDPADPMWAHDFSLANDFSRINLFDHATQTDHNMPFQPYASYFNETGPLPYHRHHVNNTQTNMGLDPYASCFNETGTFRTLPYHPHVNNAGLFDKGYTFPIPDDHVYHHLVDQRRRQPQGTSDNNYQILGDRYAVASQSLGGGGGRVKSPIRFSQITPPYQYPPNANITPSHYYVAAKEKAELSPFLSPRRIIGEDPAAAFRCDNNGVFLQGRDAKHYFENEYGSYRRSPRYDDDAIHGVGRSVVRKNFYSSAAAPSGQRSGGDFSSVPMLQDFYSVPDAQCYIYNMAKDQNGCRFLQRMVAEGTYQDICMVFEGIIGNVVELMIDSFGNYLVQKLLDVCTDDQRLQIVLMLTNHPAQLVRVSLNTHGTRVVQKLIETLTSTEQVSLVKSAIQPGFLDLIKDLNGNHLIQRCLQCLSCQDNQFIFDAAVKFCVEIATHQHGCFVLQRCIHHSVGKNRDKLVTEICKHGLLLAQDAFGNYVVQYVIESDTAAVSAKLLSQFKENFVMLSTQKFSSHVVEKCLQHIGDSRSRIVRELLSVPRFEQLLQDQYANYVIQSALLFTKGPLHASLAEAVRLHKTLCTSPYCKRIFSGNLLKK
The following text describes a protein:
Function:
Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. Stimulates 26S proteasome activity.
Subcellular Localization:
Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Nucleus. Chromosome, telomere. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles (By similarity). Also found around the pericentriolar matrix of mitotic centromeres (By similarity). During interphase, a small fraction of TNKS2 is found in the nucleus, associated with TRF1 (By similarity).
Sequence:
MSGRRCAGGGAACASAGAEAVEPSARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLTGDYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLNCHNKSAIDLAPTAQLKERLSYEFKGHSLLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNENVQQLLQEGASLGHSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDAAKKGCLARVKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTAAMPPSALPTCYKPQVLSGVRGPGATADALSSGPSSPSSLSAASSLDNLSGSFSELSAVVSSSAAEGATGLQRKEDSGIDFSITQFIRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISGQQGLNPYLTLNNSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGVFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPIHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIVRPEGMVDG
The following text describes a protein:
Function:
Involved in the hydrocarbon hydroxylating system, which transfers electrons from NADH to rubredoxin reductase and then through rubredoxin to alkane 1 monooxygenase.
Subcellular Localization:
Cytoplasm.
Sequence:
MHPIVIVGTGLAGFNTVKEFRKLDKETPIVMLTADDGRNYSKPMLSAGFSKGKTADDLCMATPEKVAEQLNVDVRTGVHVAGIDATNKRVLLPDDHLDYSKLVLALGADTWTPPLEGDAVGEVFSVNDLMDYGKFRAAVEGKKTVTILGGGLIGCEFANDLSNGGFKVSLVEPMGRCLPLLLPEQASEAVGRGLADLGVQFHFGPLAKAVHHGDNGQLVTELSDGSQLESDVVLSAIGLRPRISLAKEAGLDTNRGILTDKSLRTSAEHIYALGDCAEVQGHVLPYVLPLMASARALAKTLAGETTEVSYGVMPVTIKTPACPVVVCPAAEGSEGAWEVEAEGNTVQALFRSKDGSLLGYALTGEAVKEKMKLNKELPAIMP
The following text describes a protein:
Function:
In tandem with Hm1, NADPH-dependent HC toxin reductase (HCTR), which inactivates HC toxin, a cyclic tetrapeptide produced by the fungus Cochliobolus carbonum to permit infection and acting as an inhibitor of host histone deacetylases (HDACs), thus conferring resistance against C.carbonum race 1 in resistant cultivars (e.g. cv. B73 and cv. Wisconsin 22). Catalyzes the production of 8-hydroxy derivative of HC-toxin via the reduction of the 8-keto group of 2-amino-9,10-epoxy-8-oxo-decanoic acid, an amino acid of the HC-toxin (By similarity).
Miscellaneous:
MISCELLANEOUS: Plants susceptible (e.g. cv. Pr, cv. K41, cv. K44 and cv. K61) to the fungus Cochliobolus carbonum race 1 contain a transposon insertion (Drone) in Hm1 and a deletion in Hm2 due to a loss of resistance. However, the compatible cultivar Missouri 21A (cv. MO21A) possesses other defects in Hm1 and Hm2 alleles coming from different mutational events.
Sequence:
MNSSSSEVQVCVTGGAGFIGSYLVKKLLEKGYTVHATLRNTGEDRAAAAAGPRRGGASAVVPLFEADLFDAATFAPAIAGCQFVFLVATPYGLEAAGSKYKSTAEAAVAAVRVILRQCEESKTVKRVIHTASISTASPLKDKEAEGSGDGYKDFISESCWTPLNVDYHLRSAHFDKYILAKLRSEQELLSYNGGESPAFEVVTLPLGLVAGDTVLGHAPETLEHAVSPVSREELSFKFLRLLQSLLGSEPLVHVDDACEALLFCMERPSIAGRFFCAAAYPSIHDITDHYASKFPHLDVLRATEAVAVAVQPEVDRLGELGFRYKYGMEEILDSSVACAARLGSLDAAKLNVPDTVSSK
The following text describes a protein:
Function:
Involved in G1/S and or S phase progression. Interacts with CDC28.
Sequence:
MNCIPSPISERKIQINNEDCIGKENAFHTIPRESSINLTPHSTNEKKVLSEVNSNKIDSLQLPRGKLQRDSTHLEKTRKRQLSNDSTDPIEPKTVKKIKCHQWKNLDSIEMDDPFMVAEYTDSIFSHLYEKEIQMLPTHNYLMDTQSPYHLKSSMRALLIDWLVEVHEKFHCLPETLFLAINLLDRFLSQNVVKLNKLQLLCITCLFIACKFEEVKLPKITNFAYVTDGAATVEGIRKAELFVLSSLGYNISLPNPLNFIRRISKADNYCIETRNMAKFIMEYSICCNKFIHLKPSYLAAMSMYIARKIKNENSKWDETFIHYSGGIDIESDPAFKDFISELVEDIAVPDTNLDSLRLKYKKPKHGMVYFKVFDWCKQKR
The following text describes a protein:
Function:
E1-like activating enzyme involved in the 2 ubiquitin-like systems required for autophagy.
Subcellular Localization:
Cytoplasm. Preautophagosomal structure.
Sequence:
MAAGSGVPPDNTLPLLQFVPWQSAVDVGFWQKLAARKLAELRLSEAEQPLAGHFTASTHTQLSSPLHVGPDAWAGGVSEGAVRGGRAVAPGSCVLTNTLDGFKQADKKALLQAAAAKVWAAIVSGQAERDSALLNRFFLLTFADLKKWDFVYCVPPPLGEAMARACLAWKQAPPPAPPPDAVAGPPGDAVSDLAARLEASSVEDPGDVAAASVGGGSPFFLLHCAEGEQVTAHSLEHWSALQQQAGTVVAVYLDPCHLASHPGWPLRNLLALAVVRWRVRTLPVLALKETRGRPDWDRSLATTVHLPDLPEWRATGAPCPAAVGWERSAAGALGPRVAALGAALDPVQLAGAAVDLNLQLMRWRLLPSLDLPRLTATRCLLLGTGTLGCAVARTLLAWGVRDITLVDSGVVSFSNPVRQSLFTHADCLAGGRPKAEAAAAALRAIFPGAQASGVRLSIPMPGHAVGAREAPAVLAACAQLEQLIQTSDAVFLLTDTRESRWLPTLLAAAHNKLAINAALGFDTFLVMRHGAGPLAAPPPAPSADAPAAAGAAAPPLRLGCYFCNDVVAPLDSTAGRTLDQQCTVTRPGLAPMAAALAVELLVALRHHPAGLHAPADSTPPGAAFPAGATAQPLGLVPHQVRGFLAFFSQLLVTGHAFDKCTACSAAVVREYHHRGPDFLLQAFNTPTFLEDLTGLTALRAATDELLAEWEAGDDSAADADDF
The following text describes a protein:
Function:
Probably involved in the priming of starch granule formation. May play a regulatory role in the control of starch accumulation in plastids. Is necessary and sufficient to establish the correct number of starch granules observed in chloroplasts.
Miscellaneous:
MISCELLANEOUS: Plants over-expressing SS4 have increased levels of starch in leaves and display a higher growth rate than wild-type.
Subcellular Localization:
Plastid, chloroplast. Plastid, amyloplast. Plastid, chloroplast stroma.
Sequence:
MTTKLSSFCFLTHGLAGISCEREHGSSRRFFYLPSRRLVSTSCKMRQQRGFDSSKRQEVKKGSPKPILSINSGLQSNNDEESDLENGSADSVPSLKSDAEKGSSIHGSIDMNHADENLEKKDDIQTTEVTRRKSKTAKKKGESIHATIDIGHDDGKNLDNITVPEVAKALSLNKSEGEQISDGQFGELMTMIRSAEKNILRLDEARATALDDLNKILSDKEALQGEINVLEMKLSETDERIKTAAQEKAHVELLEEQLEKLRHEMISPIESDGYVLALSKELETLKLENLSLRNDIEMLKSELDSVKDTGERVVVLEKECSGLESSVKDLESKLSVSQEDVSQLSTLKIECTDLWAKVETLQLLLDRATKQAEQAVIVLQQNQDLRNKVDKIEESLKEANVYKESSEKIQQYNELMQHKVTLLEERLEKSDAEIFSYVQLYQESIKEFQETLESLKEESKKKSRDEPVDDMPWDYWSRLLLTVDGWLLEKKIASNDADLLRDMVWKKDRRIHDTYIDVKDKNERDAISAFLKLVSSPTSSGLYVVHIAAEMAPVAKVGGLGDVVAGLGKALQRKGHLVEIILPKYDCMQYDRVRDLRALDTVVESYFDGKLYKNKIWIGTVEGLPVHFIEPQHPSKFFWRGQFYGEQDDFRRFSYFSRAALELLLQSGKKPDIIHCHDWQTAFVAPLYWDLYAPKGLDSARICFTCHNFEYQGTASASELGSCGLDVNQLNRPDRMQDHSSGDRVNPVKGAIIFSNIVTTVSPTYAQEVRTAEGGKGLHSTLNFHSKKFIGILNGIDTDSWNPATDPFLKAQFNAKDLQGKEENKHALRKQLGLSSAESRRPLVGCITRLVPQKGVHLIRHAIYRTLELGGQFVLLGSSPVPHIQREFEGIEQQFKSHDHVRLLLKYDEALSHTIYAASDLFIIPSIFEPCGLTQMIAMRYGSIPIARKTGGLNDSVFDIDDDTIPTQFQNGFTFQTADEQGFNYALERAFNHYKKDEEKWMRLVEKVMSIDFSWGSSATQYEELYTRSVSRARAVPNRT
The following text describes a protein:
Function:
Produces ATP from ADP in the presence of a proton gradient across the membrane.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MISPMQQVVIAVRKRESDNVITALQDAGVLHLRPIAEGPLSTGNLAGQDAQERREDERLLARAESTIAELGAYRPAPAPLPAQSEWETVVEGAAQPVSHLAKRRQELQSDLEVDRTYGDAVRALARMVGTLDRSRRVALVPFLIGATENLGELDGALRESLGDRYTVASEVVGANRVGVIATLSADRDAARAALSKARLGELRLPGRFDTMPLGAAADELGRVRQGGDDMQRALNAERDRLAQQHGPALYAVRDALKDRVAVHDVRAVSARGKYSLAMQGYVPADRIPALQSTLSRFGDAVSYEVFPVDEHHDQDVPVELKNSGYVTPFQNTVMGLMSLPKYGSFDPTWVVALFVPLFFGIIMADIGYGLLFLAFGMWLLGKARRNEGWDLSLFGAYLPPATLRDLGFVTNVMAGWTILWGFLTGEFFGTLFEHLGVFYMNNDLLNRLWGWTGVHWGAHAAEGGHSTGLLPIVFPRLDTENFGNIALVFALCFGILQVLWGWGIRVQQGLKHNDQAHVWEGLAMFGGVGALILLGFISKAGADFGALSNFGDWRVLLMILGFVLFIVGYLRVAKQFPLLPVELVSQGGSVVSYARIFAVGLVSAILAKLCTDLGWSLSQQIGFLGIILGIVIGALLHFFVLALTLIGHILQPIRLHMVEFLNPTGFNNETSPRYAPLRRLSPASDAGQVK
The following text describes a protein:
Function:
Negative regulator of Yorkie (Yki) in the Hippo/SWH (Sav/Wts/Hpo) signaling pathway that plays a pivotal role in organ size control and tumor suppression by restricting proliferation and promoting apoptosis. The core of this pathway is composed of a kinase cascade wherein Hippo (Hpo), in complex with its regulatory protein Salvador (Sav), phosphorylates and activates Warts (Wts) in complex with its regulatory protein Mats, which in turn phosphorylates and inactivates the Yorkie (Yki) oncoprotein. The Hippo/SWH signaling pathway inhibits the activity of the transcriptional complex formed by Scalloped (sd) and Yki and the target genes of this pathway include cyclin-E (cycE), diap1 and bantam. Inhibits nuclear localization of Yki. Regulates salivary gland degradation in a PI3K-dependent manner and Yki- and Sd-independent, mechanism.
Subcellular Localization:
Cytoplasm, cytosol. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Colocalizes with mats and cyclin E at the centrosome.
Sequence:
MHPAGEKRGGRPNDKYTAEALESIKQDLTRFEVQNNHRNNQNYTPLRYTATNGRNDALTPDYHHAKQPMEPPPSASPAPDVVIPPPPAIVGQPGAGSISVSGVGVGVVGVANGRVPKMMTALMPNKLIRKPSIERDTASSHYLRCSPALDSGAGSSRSDSPHSHHTHQPSSRTVGNPGGNGGFSPSPSGFSEVAPPAPPPRNPTACSAATPPPPVPPTSQAYVKRRSPALNNRPPAIAPPTQRGNSPVITQNGLKNPQQQLTQQLKSLNLYPGGGSGAVVEPPPPYLIQGGAGGAAPPPPPPSYTASMQSRQSPTQSQQSDYRKSPSSGIYSATSAGSPSPITVSLPPAPLAKPQPRVYQARSQQPIIMQSVKSTQVQKPVLQTAVAPQSPSSASASNSPVHVLAAPPSYPQKSAAVVQQQQQAAAAAHQQQHQHQQSKPPTPTTPPLVGLNSKPNCLEPPSYAKSMQAKAATVVQQQQQQQQQQQQVQQQQVQQQQQQQQQQLQALRVLQAQAQRERDQRERDQRERERDQQKLANGNPGRQMLPPPPYQSNNNNNSEIKPPSCNNNNIQISNSNLATTPPIPPAKYNNNSSNTGANSSGGSNGSTGTTASSSTSCKKIKHASPIPERKKISKEKEEERKEFRIRQYSPQAFKFFMEQHIENVIKSYRQRTYRKNQLEKEMHKVGLPDQTQIEMRKMLNQKESNYIRLKRAKMDKSMFVKLKPIGVGAFGEVTLVSKIDTSNHLYAMKTLRKADVLKRNQVAHVKAERDILAEADNNWVVKLYYSFQDKDNLYFVMDYIPGGDLMSLLIKLGIFEEELARFYIAEVTCAVDSVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRWTHNSKYYQENGNHSRQDSMEPWEEYSENGPKPTVLERRRMRDHQRVLAHSLVGTPNYIAPEVLERSGYTQLCDYWSVGVILYEMLVGQPPFLANSPLETQQKVINWEKTLHIPPQAELSREATDLIRRLCASADKRLGKSVDEVKSHDFFKGIDFADMRKQKAPYIPEIKHPTDTSNFDPVDPEKLRSNDSTMSSGDDVDQNDRTFHGFFEFTFRRFFDDKQPPDMTDDQAPVYV
The following text describes a protein:
Function:
One of 3 paralogous diadenylate cyclases (DAC) in this bacteria, catalyzing the condensation of 2 ATP molecules into cyclic di-AMP (c-di-AMP) (Probable). Upon expression in E.coli leads to c-di-AMP synthesis. Overexpression of the hyperactive mutant (L44F) in the absence of c-di-AMP phosphodiesterase GdpP leads to growth defects in log phase (long curly cell filaments) that disappear upon sporulation; spore formation is normal, showing sporulation is insensitive to the excess c-di-AMP. In B.subtilis c-di-AMP is a second messenger that mediates growth, DNA repair and cell wall homeostasis; it is toxic when present in excess.
Domain:
The N-terminus (residues 1-69) is thought to form 2 alpha-helices that allow dimerization and probable hexamerization; this region inhibits DAC activity of the rest of the protein.
Sequence:
MKAMRYEQISENAFKGKIQVYLEQILGDASLILKTLHEKDQCLLCELDDLGHVFQDMQGIASSFYLQSYIEEFTPAFIELAKAIKALSEHKHGALIVIERADPVERFIQKGTSLHAEISSSLIESIFFPGNPLHDGALLVRENKLVSAANVLPLTTKEVDIHLGTRHRAALGMSGYTDALVLVVSEETGKMSFAKDGVLYPLISPRT
The following text describes a protein:
Function:
3-beta-HSD is a bifunctional enzyme, that catalyzes the oxidative conversion of Delta(5)-ene-3-beta-hydroxy steroid, and the oxidative conversion of ketosteroids. The 3-beta-HSD enzymatic system plays a crucial role in the biosynthesis of all classes of hormonal steroids.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein.
Sequence:
MAGWSCLVTGGGGFLGQRIICLLVEEKDLQEIRVLDKVFRPEVREEFSKLQSKIKLTLLEGDILDEQCLKGACQGTSVVIHTASVIDVRNAVPRETIMNVNVKGTQLLLEACVQASVPVFIHTSTIEVAGPNSYREIIQDGREEEHHESAWSSPYPYSKKLAEKAVLGANGWALKNGGTLYTCALRPMYIYGEGSPFLSAYMHGALNNNGILTNHCKFSRVNPVYVGNVAWAHILALRALRDPKKVPNIQGQFYYISDDTPHQSYDDLNYTLSKEWGFCLDSRMSLPISLQYWLAFLLEIVSFLLSPIYKYNPCFNRHLVTLSNSVFTFSYKKAQRDLGYEPLYTWEEAKQKTKEWIGSLVKQHKETLKTKIH
The following text describes a protein:
Function:
Transcription factor involved in specification of neuronal cell types and which is required for inner ear and hypothalamus development. Binds to the 5'-CAAGTG-3' core sequence.
Subcellular Localization:
Nucleus.
Sequence:
MSKAAAPCRPSASLKFTIDNILNLKPSGTSSDSSGLRDELREDTAGQQRPDQSVSIRTCSADSEPGIQRTGARYESGDSSCDDSISSSAAAEALQGGSPSKRSKVITKKKTRTIFSKRQIFQLESTFDMKRYLSSAERACLASSLQLTETQVKIWFQNRRNKLKRQISTEIDGPASDFPEAAKPVAAGQLPALYKESSLLGRCLLPVPLPVVYPGGGAPYLCFSSASKYFSLYDGDV
The following text describes a protein:
Function:
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
Subcellular Localization:
Nucleus.
Sequence:
MAEAVFHAPKRKRRVYETYESPLPIPFGQDHGPLKEFKIFRAEMINNNVIVRNAEDIEQLYGKGYFGKGILSRSRPSFTISDPKLVAKWKDMKTNMPIITSKRYQHSVEWAAELMRRQGQDESTVRRILKDYTKPLEHPPVKRNEEAQVHDKLNSGMVSNMEGTAGGERPSVVNGDSGKSGGVGDPREPLGCLQEGSGCHPTTESFEKSVREDASPLPHVCCCKQDALILQRGLHHEDGSQHIGLLHPGDRGPDHEYVLVEEAECAMSEREAAPNEEEPLTIVKLWKAFTVVQPTFRTTYMAYHYFRSKGWVPKVGLKYGTDLLLYRKGPPFYHASYSVIIELVDDHFEGSLRRPLSWKSLAALSRVSVNVSKELMLCYLIKPSTMTDKEMESPECMKRIKVQSRSVVQAGVQCCDLGSLQPLPAGFKRFSCLSLLSSWDYRHAPPHTANFCIFSRDGVSLCWPGWSGTPDLK
The following text describes a protein:
Function:
Component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to TFIIK, in RNA transcription by RNA polymerase II. In NER, TFIIH acts by opening DNA around the lesion to allow the excision of the damaged oligonucleotide and its replacement by a new DNA fragment. In transcription, TFIIH has an essential role in transcription initiation. When the pre-initiation complex (PIC) has been established, TFIIH is required for promoter opening and promoter escape. Phosphorylation of the C-terminal tail (CTD) of the largest subunit of RNA polymerase II by the kinase module TFIIK controls the initiation of transcription.
Subcellular Localization:
Nucleus.
Sequence:
MPRAQKGLLLVECDPTVKQLILNMDEQSPGIVIEEIDEERLLVNESRLEQVKAELERRLEENTYQVEE
The following text describes a protein:
Function:
Involved in the biosynthesis of tetrahydromethanopterin, a coenzyme used in methanogenesis. Catalyzes the reduction of dihydromethanopterin (H(2)MPT) to tetrahydromethanopterin (H(4)MPT). Ferredoxin may serve as an electron donor.
Sequence:
MSFQRIAWGITGAGHFLDRSYQVFKELKLRNPELSVNTYVSRAAEEVLRMYGLEQKLVKISGGDYLEEIFRESEQGSSSPKVGRFALDRYDALFVTPATSNTVSKIAYGIADSLVTNAVSQAVKGRVPVFVVPVDIEGSIISEMPYNIDRKQCKHCETCPPRENCPHEAISEKNGVTDQIDLLKCKGCGICKELCPYNAIKGGPVEVLVRDVDMRNVEIVKSLQGITVLESPEAILELF
The following text describes a protein:
Function:
Lipolytic acyl hydrolase (LAH).
Domain:
The nitrogen atoms of the two glycine residues in the GGXR motif define the oxyanion hole, and stabilize the oxyanion that forms during the nucleophilic attack by the catalytic serine during substrate cleavage.
Sequence:
MDFVSKKKIWNQESQCSFRNLRRGVWFTTCPTVCSHLQSPFTSTTPLAPASGLSQRWHGFAKHPIQIMHPDSVARFYTAPRAKSVGVLSQAASLLSLSTNSMSPEARKLEEAAEATPLSPDLPPIICFPGGGMFFYWMIGVVNILQDEIDMTTAHMSGASAGALASVLAACGVDMRRAAEHAFQLSIDEKLWDRKLKLALVWGRLIRQWLWDLLPDNAAELCNGRIHLFVLELPGLRTGLHCKRVPVTDFKDKADLIDCALASVHIPIFINGHIWTEYRGSRCVDGSINADRLALNIDPRRHTLYVDPYEDPEMKERGNRFLELYGDNPGPEGTWEWINHMMQRGEEHARRISSAGQLEPWTHSSLKMEAGG
The following text describes a protein:
Function:
Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.
Sequence:
MDVIKTQQISARTIEKVIVHPLVLLSIVDHYNRVAKDTSKRVVGVLLGSSSRGTVDVTNSYAVPFEEDDKDTSIWFLDHNYHESMFHMFKRINAKEHIVGWYSTGPKLRENDLDVHALFNGYVPNPVLVIIDVQPKELGIPTKAYYAVEEVKENATQKSQQVFVHVPTEIAAHEVEEIGVEHLLRDVKDTTISTLATEVTAKLTALKGLDARLREIRTYLDLVIEGKLPLNHEILYHLQDVFNLLPNLNVNELVKAFAVKTNDMMLVIYLSSLIRSVIALHSLINNKLLNKEHEKAEDSKPVDIPLITES
The following text describes a protein:
Function:
Transcription factor that binds RNA polymerase II and inhibits the elongation of transcripts from target promoters. Regulates transcription elongation in a TATA box-dependent manner (By similarity).
Subcellular Localization:
Nucleus.
Domain:
The FF domains preferentially binds peptides with the consensus sequence [DE](2-5)-[FWY]-[DE](2-5) and mediate interaction with HTATSF1 and probably bind the phosphorylated C-terminus of the largest subunit of RNA polymerase II; The WW domains bind Pro-rich domains.
Sequence:
MAERGGDGGEGERFNPGELRMAQQQALRFRGPAPPPNAVMRGPPPLMRPPPPFGMMRGPPPPPRPPFGRPPFDPNMPPMPPPGGIPPPMGPPHLQRPPFMPPPMGAMPPPPGMMFPPGMPPGTAPGAPALPPTEEIWVENKTPDGKVYYYNARTRESAWTKPDGVKVIQQSELTPMLAAQAQVQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQAQVQAQAVGAPTPTTSSPAPAVSTSTPTSTPSSTTATTTTATSVAQTVSTPTTQDQTPSSAVSVATPTVSVSAPAPTATPVQTVPQPHPQTLPPAVPHSVPQPAAAIPAFPPVMVPPFRVPLPGMPIPLPGVAMMQIVSCPYVKTVATTKTGVLPGMAPPIVPMIHPQVAIAASPATLAGATAVSEWTEYKTADGKTYYYNNRTLESTWEKPQELKEKEKLDEKIKEPIKEASEEPLPMETEEEDPKEEPVKEIKEEPKEEEMTEEEKAAQKAKPVATTPIPGTPWCVVWTGDERVFFYNPTTRLSMWDRPDDLIGRADVDKIIQEPPHKKGLEDMKKLRHPAPTMLSIQKWQFSMSAIKEEQELMEEMNEDEPIKAKKRKRDDNKDIDSEKEAAMEAEIKAARERAIVPLEARMKQFKDMLLERGVSAFSTWEKELHKIVFDPRYLLLNPKERKQVFDQYVKTRAEEERREKKNKIMQAKEDFKKMMEEAKFNPRATFSEFAAKHAKDSRFKAIEKMKDREALFNEFVAAARKKEKEDSKTRGEKIKSDFFELLSNHHLDSQSRWSKVKDKVESDPRYKAVDSSSMREDLFKQYIEKIAKNLDSEKEKELERQARIEASLREREREVQKARSEQTKEIDREREQHKREEAIQNFKALLSDMVRSSDVSWSDTRRTLRKDHRWESGSLLEREEKEKLFNEHIEALTKKKREHFRQLLDETSAITLTSTWKEVKKIIKEDPRCIKFSSSDRKKQREFEEYIRDKYITAKADFRTLLKETKFITYRSKKLIQESDQHLKDVEKILQNDKRYLVLDCVPEERRKLIVAYVDDLDRRGPPPPPTASEPTRRSTK
The following text describes a protein:
Function:
Collagen-like protein, which provides an organic scaffold for otoliths onto the sensory epithelium of the inner ear. Acts as a scaffold for biomineralization by sequestering calcium (By similarity).
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Note=Localized in both the surrounding otoconial matrix and otoconia.
Domain:
The C1q domain mediates calcium-binding.
Sequence:
MPSLRLLAILTTLLAVVLIATQSSATRTTRRPKPQNTKKPPRGGGTGGGGGGGDQPARLGFRQTTTTMAPSSSLGTDETTEDTMTDAYSLSPTDSTTYAGDAYPTEFHTDSMALPGAGMGNYTLDYSHCYLNVCECCPPEKGRGPPGERGPPGPGAERGLPGVPGEKGDVGLMGPPGLDGMPGATGLEGDKGDKGDQGDTGMPGAPGILGKEGPKGDLGPKGEKGETGLPGLKGDLGERGKPGWNGTQGEKGDLGKIGPAGPSGLTGPMGQNGQKGEMGECPTGEKGEKGEAGLPGPPGPRGLVGTPGVNGTNGLPGPVGLRGQLGSPGGKGEAGGRGPPGLRGMPGPKGEKGPKGPRGVRGPKGPQGETAEQIRSAFSVGLFPSKSFPPPGLPVKFDKILYNEEEHWDPMLSKFNCTHPGVYVFSYHITVRNRPLRAALVINGVKKLRTRDSLYGQDIDQASNLALLRLASGDQVWLETLRDWNGVYSSSEDDSTFTGFLLYADPKA
The following text describes a protein:
Function:
Putative phospholipase.
Sequence:
MMCTATVMRTPSAVLCLLLAATLTLSTPVAVRGEVLKDATPTVVTVWYNATSGGFYATDGLASGKYAAIVNVSNTFNKTGWDVVTAVANDGFMHLPGEAEPSAERVLLAYKAVGFGEGYATYESMKASINNTFEGPEGLSALLSDAPQAQHWIEEHVRYMDAAKFESSAFYTQLRNMLALIDGMVAGYNARAPADERLDRMKLLMYNMQAEIGDIVRATSPAEVLDDMRQMMPRWFVDTHCSAFVKVVKDDIYFGHATWSSFNTMLRQYKTYAFGGRFVTMSSYPGLAHSVDDWYMTHKRLAVMETTNVIHNATLLRNHVGSSSVATFLRAMIANFIAVDAPSWVSNFSRESSGAYNNQWMVLNMGAVESEAMFKNMAPNTFWVLEQLPGTAPPLGITSKDMTSVLNTTGYWASYNRPYFPNVYNLSGTLKMQEEYGDFYSYKNYSRARIFERDQGSVVDIESMKRLMRYNNYTKDPFSLIPNCTGAVGMDDDGNVTNVCKPPYSAMLSIAARGDLNPPGNATEYGPLVRSVGHVNSGAIDAKIATWTGMVKNPESYTAHVVCGPTTDNQPPFQWVDGMFDPMPPTYGLLKLYNFSFVVMETPIRPSGGSNSWRSTGIIAVVAALVVGVIAVVLMRPRRRTEEDELLPEEAEGLIDPQN
The following text describes a protein:
Function:
Catalyzes the dephosphorylation of undecaprenyl diphosphate (UPP). Confers resistance to bacitracin.
Miscellaneous:
MISCELLANEOUS: Bacitracin is thought to be involved in the inhibition of peptidoglycan synthesis by sequestering undecaprenyl diphosphate, thereby reducing the pool of lipid carrier available.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSWFESLVLGLVQGLTEFLPVSSSAHLRLTAAFSGWHDPGAAFTAITQIGTEAAVLIYFRKDIGRIIAAWTRSLTDKSMRHDPDARMGWLVIVGSIPIGVLGLTLKDQIEGPFRDLRITATMLIVVGVIIGIADRMAARDEKGGRHRAPQQRKELENLGVRDGLIYGLCQAAALIPGVSRSGATISGGLFMGYRREAAARYSFLLAIPAVLASGVFELKDAMESDHVSWGPTLFATVIAFATGYVVIAWFMKFISTKSFMPFVWYRIALGIVIIVLVSVGVLSPHAAESGG