lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probable component of the transcriptional machinery present in the inner capsid. Displays dsRNA binding activity and may play an important role in the sorting of viral RNA and virion assembly. Together with the RNA-directed RNA polymerase P1 and capping enzyme P5, forms an transcriptional complex positioned near the channels situated at each of the five-fold vertices of the core.
Subcellular Localization:
Virion. Host cytoplasm. Note=Located inside the inner capsid. Found in the interior of spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging (By similarity).
Sequence:
MSAIVGLCLLSEKVVLSRSLTDEVSKLYKLNRGNVKEPRKYATERMSTQSKPVALQVPVSTIILDYKNEDFIKQNPTYSAMDIIGSPSNTAPQTAFQSIMPSLSALFNTPFIQGAFRHRIISSMGPEISYLVMVIGPPSGFMDTPNVSSAQSSVHTVSNADVDLNDIIAINSTMAKSTKLVSASTLQAMLVNDVYDRCMDLDGILLSQALPFFRNYVNVQSKGSLPPAVAACLNTPIKELFSMGSGKREPLALEFRKDNEGQCIGIVLPKGHEGDTLSSRYPAVFINESEPFSDKERSELSELKRTDSDAYEKLYSETISKHVSDGSYGNRVIISHKMSRLSNGGVKIIGRFKISDFNTVKKNLSSRSGEIDSAKEQWEALSGNGLVTDSNISMLHDKILDTITSNKPGVVLRDGNKKSENIVVCFKNGFPNKKHSLLQLTKNGISVVSLDELTDAGILVESTGPDRVRRSPKVLANKLSSFKGRKVTLDVDNMSTEALIQKLSTL
The following text describes a protein:
Function:
Extracellular matrix protein that seems to be a ligand for ITGA8:ITGB1, ITGAV:ITGB1 and ITGA4:ITGB1. Involved in neurite outgrowth and cell migration in hippocampal explants. During endochondral bone formation, inhibits proliferation and differentiation of proteoblasts mediated by canonical WNT signaling. In tumors, stimulates angiogenesis by elongation, migration and sprouting of endothelial cells. Expressed in most mammary tumors, may facilitate tumorigenesis by supporting the migratory behavior of breast cancer cells.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MSLQEMFRFPLGLLLGSVLLVASAPATLEPPSCNNKEQQVTVSHTYKIDVPKSALVQVEADPQPLSDDGASLLALGEAGEEQNIVFRHNIRLQTPQKDCELAGTVQDLLARVKKLEEEMVEMKEQCSAQRCCQGATDLSRRCSDHGTFSLETCSCHCEEGREGPACEQLACPGACSGHGRCVDGRCLCHEPYVGADCGYPACPENCSGHGECVRGVCQCHEDFTSEDCSERRCPGDCSGHGFCDTGECYCEEGFTGLDCAQVVAPQGLQLLKSTEESLLVSWEPSSQVDHYFLNYYPLGKELSGKQIRVPKEQHSYEILGLLPGTKYIVTLRNVKKDIFSSPQHLLATTDLAALGTAWVTEETEHSLDVEWENPSTEVDYYKLRYGPMTGQEVTEVTVPKSSDPKSRYDITGLHPGTEYKITVVPMRGTLEGKPILLNGRTEIDSPTNVVTDRVTEDTATVSWKPVQAVIDKYVVRYTSADGDTKEMAVHKDESSTVLTGLKPGEAYKVYVWAERGNQGSKKADTNALTEIDSPANLVTDRVTENTATISWDPVQATIDKYVVHYTSADNQETREVPVGKEQSSTVLTGLRPGVEYTVHVWAQKGDRESKKANTNAPTDIDSPKNLVTDRVTENMATVSWDPVQATIDKYMVRYTSADGETREVPVGKEHSSTILTGLRPGMEYMVHVWAQKGDQESKKTDTKAQTDIDSPQNLVTDWVTENMATVSWDPVQATIDRYVVRYTSAKDGETREVPVGKEQNSTVLTGLRPGVEYTVHVWAQKGAQESKKADTKAQTDIDSPKNLVTDRVTENTATVSWDLVQATIDRYVVRYTSANGETREVPVGKEQSSTVLTGLRPGVEYTVHVWAQKGNQESKKADTKAQTEIDSPKNLVTDRVTENMATVSWDPVQATIDKYVVRYTSADGETREVPVGKEHSSTVLTGLRPGMEYMVHVWAQKGDQESKKADTKAQTEIDPPRNLRPSAVTQSGGVLTWTPPSAQIHGYILTYQFPDGTVKEIQLGREDQRFELQGLEQGATYPVSLVAFKGGLRSRNVSTTLSTVGARFPHPSDCSQVQQNSNAASGLYTIYLHGDSSRPLQVYCDMDTDGGGWIVFQRRNTGQLDFFKRWRTYVEGFGDPTKEFWLGLDKLHNLTTGTPTRYEVRVDLQTANESAYAIYDFFQVASSKERYKLTVGKYRGTAGDALSYHNGWKFTTFDRDNDIALSNCALTHHGGWWYKNCHLANPNGRYGETKHSEGVNWEPWKGHEFSIPYVELKIRPHGYSKEPVLGRKKRTLGGRLRTF
The following text describes a protein:
Function:
V region of the variable domain of immunoglobulin light chains that participates in the antigen recognition. Immunoglobulins, also known as antibodies, are membrane-bound or secreted glycoproteins produced by B lymphocytes. In the recognition phase of humoral immunity, the membrane-bound immunoglobulins serve as receptors which, upon binding of a specific antigen, trigger the clonal expansion and differentiation of B lymphocytes into immunoglobulins-secreting plasma cells. Secreted immunoglobulins mediate the effector phase of humoral immunity, which results in the elimination of bound antigens. The antigen binding site is formed by the variable domain of one heavy chain, together with that of its associated light chain. Thus, each immunoglobulin has two antigen binding sites with remarkable affinity for a particular antigen. The variable domains are assembled by a process called V-(D)-J rearrangement and can then be subjected to somatic hypermutations which, after exposure to antigen and selection, allow affinity maturation for a particular antigen.
Subcellular Localization:
Secreted. Cell membrane.
Sequence:
MAGFPLLLTLLTHCAGSWAQSVLTQPPSASGTPGQRVTISCSGSSSNIGSNYVYWYQQLPGTAPKLLIYSNNQRPSGVPDRFSGSKSGTSASLAISGLRSEDEADYYCAAWDDSLSG
The following text describes a protein:
Function:
TRAP proteins are part of a complex whose function is to bind calcium to the ER membrane and thereby regulate the retention of ER resident proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGRKGKSMFTQEELELMNTQKYTTPSAVYMTWAAISSTLPALLFSTVMVMNPVDNIIVFVAFAAVAAAALFFAYQNTSRKIRDGLAAKHSEEVRAMVTENYKSMDKKQKEGVHLDSLVVEKQSELSEKESCFLSLSYNNALFAFLLVVFSFYVFRSLSGQWNYGLSVTSTSILVALFSTGSKA
The following text describes a protein:
Function:
Involved in active transport of urea.
Subcellular Localization:
Membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
MTETVLNQGYGYGIVIGLGFAFAIVMILVTYVLKRYVGEVQDSEHFTTASRSVKTGLISSAVVSSWTWPGTLLTSAGMAYEYGVCGSMWYSFAFTVQITFFTVIALQVKRVAPGAHTIVEIVKARFGQASHAVFLFYALGTNIIVSAMLLLGGSQAISAITGMHVVAAGFLLPLGVWLYTVSGGLKSTFLSDWTHTVIVYIVILITLFVAYTSSVHIGSIDKMYDLLTEVSKTNPSTGYKGSYLTVTNRDAVFVGWNIVIGGFATVFCDPSYGQKAIAAKPISAMKGYFAGGLAWLIVPWAMGSAAALSCLALTNNPVSVTYPDPVSSKQVSEGMPLLYGMTALMGKNGAAAGVLILFMASTSATSAELVAFSSVMTYDVYRNYFRPNASGKELVRVTHVFVTIFAVCMGALAVLFNYIGITISWIITFIGIALGPAVFGITLTLFWKKMNKYGMIIGCPMGSITGVVCWVGSCYKFSNGVVNKTTLNTPYANAVGNFTGLFSGLIYIVLISYFFPNKSDDLNNLNEKFVLGDDATAEEIVDAETEKKQLDRSLRIGIFVSWIIFFILVIIVPLPMYGSKYIFSKLFFRGWIIVIIIWTLIAALYITFYPLYESRDTIVYLCKLAIGKAKAPEPMNYVDAVEVEIESLSDDDKEKKANDFL
The following text describes a protein:
Function:
Involved in sulfonamide (sulfathiazole) and bicyclomycin resistance. Probable membrane translocase. A transporter able to export peptides. When overexpressed, allows cells deleted for multiple peptidases (pepA, pepB, pepD and pepN) to grow in the presence of dipeptides Ala-Gln or Gly-Tyr which otherwise inhibit growth. Cells overexpressing this protein have decreased intracellular levels of Ala-Gln dipeptide, and in a system that produces the Ala-Gln dipeptide overproduction of this protein increases export of the dipeptide.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MTTRQHSSFAIVFILGLLAMLMPLSIDMYLPALPVISAQFGVPAGSTQMTLSTYILGFALGQLIYGPMADSFGRKPVVLGGTLVFAAAAVACALANTIDQLIVMRFFHGLAAAAASVVINALMRDIYPKEEFSRMMSFVMLVTTIAPLMAPIVGGWVLVWLSWHYIFWILALAAILASAMIFFLIKETLPPERRQPFHIRTTIGNFAALFRHKRVLSYMLASGFSFAGMFSFLSAGPFVYIEINHVAPENFGYYFALNIVFLFVMTIFNSRFVRRIGALNMFRSGLWIQFIMAAWMVISALLGLGFWSLVVGVAAFVGCVSMVSSNAMAVILDEFPHMAGTASSLAGTFRFGIGAIVGALLSLATFNSAWPMIWSIAFCATSSILFCLYASRPKKR
The following text describes a protein:
Function:
Required presynaptically at the neuromuscular junction. Implicated in synaptic vesicle endocytosis.
Subcellular Localization:
Membrane; Peripheral membrane protein.
Sequence:
MAFAGLKKQINKCNQYVTEKMGGAEGTKLDLDFMDMERKTDVTYELVEELQIKTKEFLQPNPTARAKMAAVKGISKLSGQAKSNTYPQPEGVLGDCMLTYGRKLGDDSMFGNALVEMGESLKQMADVKYSLDDNIKQNFLEPLHHLQTKDLKEVMHHRKKLQGRRLDFDCKRRRQAKDDEIKTAEDKFAESLHLAQMGMFNLLENDVEQISQLATFAEGLLEYHVQCTEILKHLNEILLEKKEEAANRPKVEFVPKTLADLHIEGVSDGVNGIHHNNINTNHHNFTNSGHQFKRPAPKTIPIKQSDPFDPWSFPPASPLPSPMKSPARTPMNRQPCCTALYDFDPENPGELGFKENDVITLLNKIDENWFEGSLHGRTGYFPVNYVKVDVPLP
The following text describes a protein:
Function:
Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramembraneous catalytic core and F(0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F(0) domain. Minor subunit located with subunit a in the membrane. The K chain binds the dimeric form by interacting with the G and E chains.
Miscellaneous:
MISCELLANEOUS: Present with 1320 molecules/cell in log phase SD medium.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MGAAYHFMGKAIPPHQLAIGTLGLLGLLVVPNPFKSAKPKTVDIKTDNKDEEKFIENYLKKHSEKQDA
The following text describes a protein:
Function:
Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors. Requires the other members of the gamma-secretase complex to have a protease activity.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Golgi apparatus membrane; Multi-pass membrane protein.
Sequence:
DSTGKQLALDFANGLVIVTVIGTMTFGIVLLYKYRCMKFLMGYMAFSSMTLLGVLGAELFNVAIEKYRIPIDWFTFVFSMFNFAVVGVTSIFYAKGIPPYITQTYLICSSVIIAWQLSHFDTISTWTLLIMLALYDLCAVLTPVGPLRLLVNLMSDEDSPEMPGLLYEAQIPEGLKRPVMGGRNKDDNGDEGEHDDSSQSPPASMSAERYQQPSIKENGVPGRTSSDVSASQGDDSAPGVEMSSAVNRTRNDSYDSVTLDQSENNATTTPDLAPAHASSSAKTAMIPFAIAELFSNTIKLGLGDFIFYSVLVAKSAQYSFACFVSSFLVVLAGLGGTLVLLAVFKHALPALPISIFLAVTFYVFTRFIIEPW
The following text describes a protein:
Function:
F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation; Key component of the F(0) channel; it plays a direct role in translocation across the membrane. A homomeric c-ring of between 10-14 subunits forms the central stalk rotor element with the F(1) delta and epsilon subunits.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein.
Sequence:
MYLAVLTNLAQVQSSTVLAVGIMIGLAALGAGLGLAIMAGKFLESAARQPELIPVLQVRMFITAGLIDAAFIISVAVGLLFAFANPLAQVFIERLSQAAG
The following text describes a protein:
Function:
Microtubule-binding protein essential for cytoskeletal organization (e.g. rootlet microtubule bundles) and flagellar basal body/centriole assembly.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=Localized at the cartwheel, the first ninefold symmetrical structure appearing during basal body/centriole assembly near the proximal end of the organelle.
Domain:
Coiled-coil domains are critical for microtubule binding via the formation of a two-stranded coiled-coil structure in homodimers.
Sequence:
MAIDVDRTLAVLRRKLEALGYSDPLEPASLQLVQKLVEDLVHTTDSYTAVKQQCAKQAQEIAAFDTRLESVRQDSVRLQSENSQLHVLVMQHAERHEREAREHYTAVKRLEDTIAELSYWKHAAAEKLASADKENAGLRKRCEELAKLTDRLASGAATPQSVAPKISSRSPIRVAPPPSPPRPRQATVDVLQAANGRILSLQRQLADATAELQELRQRVAEDEDQIRRRDVEIDRLGTRAGTDTNVLALRARNEANESMILQLNGTVESLAARVRELEAVEVRCEELQGALRRAEMDRDQAEERYSRSARDHDALSREVLGLRRDLAALQDTNNRAAGLLAADAAGASTPDTTAGAPALRQRLADSRADVERLSGQLAAADMERRNLAQQLSALRSELDDTQFLLAEAQSRAAGLAAAQAVAESEARRLAGEAAAREGRLRELDSQLAVVLSDLEARQAGFAALEKDRAEANARAEELARRLDEVERSAASERAAAAAAQQSVSRLDSELRVVRGSAAALEAEAAALRQELQDVSVGKVRATSALSSTEDEAVRARQQAEALRMQLTAERRAAEELRAGHDTLQLEVDRLGGQLALQQQEAELLRQQLAAARGELAASEAAASGAEQKLSGLGALSQRLEEMGEQARRAQAATAEAEAEAVRLRAAVSEAKEGQARAERGLREARREVEGAREAEALVRAQLREVEAQAEGTSKALKAAEADRDRALMDARLAAGDLASLRDQLAAETSSAADAGSTARQMAARLSAAERAAAAAQEERERAAVAAEEAEAAAAAARGREEEARAQGREWAERARRAEALVAEYEADVAQLRAARDSDAAALRSLEDTVAAARRDLDARRSEVEQLTTLSLRGDATVQEYMANLKAMSTDLRAAEMRAADLAGEAAAAQDAAASWRSEAEQLRGLLRQMDADRDNLQHELDAKAERLVAQEQQLAGAQAAEQEAARLLALAEGRLALTDNRAREGEAEAAAVRAQLAAALDSVRALSGEGEALREELRAVSEDLEALVRENQVVGGELAAVAAQRDSAAEEARRLGGRRASAEQLLRAKEAEAEDLRRVYEALAAEHRRLQGGVGALEREGAMREAALQAKAAEVSSLAESQRAAQATINQYVMDLQAFERQVDSLSRQLSQAEADGEELVRQREALLEEIRAAQQVRLGLERHREELQRQVASLDSQVAIGRARLEDSNSEAASLNQRLAMERSRVAELEGLLAGMRAREFRSDFASDRAGGQLAVMVDRNRALEEQVASLQHQVGALQASREAQDRELSRLRGEALALAASTAASLEGRTAAAGGAAAGAAKDQAAALDRLTSERDAAQDEAARLRGALAAAEAAAASASTAAAVSIPAAGSGSEAAAVLRVRCSELERRNTELMQELRTLQDTCRQQESLLSAAQNELSALQAEHRRLVELVARLDQDKAAAAAEAAAARQQVATATRRVATAEQEAAAGAARLQSQLRDEQGRRRQAERDFLELLSSIEGAGGEAAAAAVAAAHGEGAAELASRRLRELQTQVDALEAEKAGLEEATQRTRATLGAMSGQMAAIQAEYDATNTALAGLAGAMAAGAQGQGQVQGPAGTAPAAAAGAPGPQPGQAQAGGFGGAHGGGSISLSGGPRR
The following text describes a protein:
Function:
Acts as a transcriptional activator by binding to an A/T-rich sequence, the FLAT element, in the insulin gene promoter. Required for development of the roof plate and, in turn, for specification of dorsal cell fates in the CNS and developing vertebrae.
Subcellular Localization:
Nucleus.
Sequence:
MKTEEAPSCLQQATPVLGYGSESKMREVCAGCNTPISDRFLLRVNERSWHEGCVKCAACLQPLSGTCYCRNRQLYCKHDYEKLFQTKCSGCLKAVAPSEFIMRVLENVYHVHCFSCCECERRLQRGDEFVLKEGQLLCRSDYEKEREMLSAISPAPTESVKSEDEDGNHPHGKTGEEGKDHKRSKRPRTILTTQQRRAFKASFEVSSKPCRKVRETLAAETGLTVRVVQVWFQNQRAKMKKIARRQQQQQQQQQEQEQLGNPRLGSGRGNGRSSRQSNEDSEDGASVHGIDGLMVPYSRIAQQQLLPLDQNSYSTDLYRQGLTPPQLPGDHLHPYDSEGVFHDMDSDTIGHLGDCLLSAAEANLLQTRVGNPIDRLYSMQSSYFTS
The following text describes a protein:
Function:
Exhibits acyl-CoA:lysocardiolipin acyltransferase (ALCAT) activity; catalyzes the reacylation of lyso-cardiolipin to cardiolipin (CL), a key step in CL remodeling. Recognizes both monolysocardiolipin and dilysocardiolipin as substrates with a preference for linoleoyl-CoA and oleoyl-CoA as acyl donors. Also exhibits 1-acyl-sn-glycerol-3-phosphate acyltransferase activity (AGPAT) activity; converts 1-acyl-sn-glycerol-3- phosphate (lysophosphatidic acid or LPA) into 1,2-diacyl-sn-glycerol-3- phosphate (phosphatidic acid or PA) by incorporating an acyl moiety at the sn-2 position of the glycerol backbone (By similarity). Possesses lysophosphatidylinositol acyltransferase (LPIAT) activity. Possesses lysophosphatidylglycerol acyltransferase (LPGAT) activity (By similarity). Required for establishment of the hematopoietic and endothelial lineages.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Domain:
The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate.
Sequence:
MVSWKGIYFILFLFAGSFFGSIFMLGPILPLMFINLSWYRWISSRLVATWLTLPVALLETMFGVRVVITGDAFVPGERSVIIMNHRTRVDWMFLWNCLMRYSYLRVEKICLKSSLKSVPGFGWAMQVAAFIFIHRKWKDDKSHFEDMIDYFCAIHEPLQLLIFPEGTDLTENNKARSNDFAEKNGLQKYEYVLHPRTTGFTFVVDRLREGKNLDAVHDITVAYPYNIPQTEKHLLLGDFPKEIHFHVQRYPADSLPTSKEDLQLWCHRRWEEKEERLRSFYQGEKNFHFTGQSTVPPCKSELRVLVVKLLSIVYWALFCSAMCLLIYLYSPVRWYFIISIVFFVLQERIFGGLEIIELACYRFLHKHPHLNSKKNE
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MNSSKWKSPFQRKKRERQQPAARAHLGILEKKKDYIERAKIYHKHEKEIDDLRRAAELRNPNEFYYSMIGDMKEKPVEYKSKPREDFTKEQRLLLETRDINYIIAKMQTQKNKLEKLKIRLPIKTQGSTKIYSSVEEAIKATKGKEVEEENPEEEDTPDVKQLKEEIENREFILQKLQEVYDEMKLQADTKNDENYDTYEDDDGNVHHVWKPIRKR
The following text describes a protein:
Function:
Multiubiquitin chain receptor involved in modulation of proteasomal degradation. Involved in nucleotide excision repair.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MVKITFKTVQNKLFTVDAQDSDTVADLKKKIQETQTFPVENQKLIYSGKILNDASSVESLKIKEKDFLVVMVSRPKATPAATPAAPATPAPSTPAPAPAASEQASVANPAVPAPSAPAAESAPASAPAPAAESAQPSAVESGLGGSFVTGPALQAAIDGMVEMGFERDQVIRALRASFNNPDRAVEYLMSGNIPSVEGTAPAAPAPAAPSTPSAAAAPAQPAAPSEPAAQPVASAPPASAGGSADNLFAAAEAAMNRDRGVPAAAGAPGLPGAPGLPGAGAGMPGGMGGGDQLSAIRQMVQQNPAMIQPLLQQIATEHPELAQLIAQNPEALYELLGGGGGEGDDDDEFGEGPVMRVNLTQEEAAAVERLEALGFDRQTVLQAYMLCDKNEELAANFLFENMEEDQ
The following text describes a protein:
Function:
DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. This DNA polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain is the DNA polymerase (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MFVNLHTNSYYNFLNSALSPKKLVNLAINDQQKAVAITDPNLFGAVEFFITCKQNNIKPIIGLNLTVEYQKNDVKLLLIAKSNKGFQTLNKIALIQQKLEINSLVDQLTDIAVIICSLTTWKSTYKDVYQAKGIEINQTPIAILANAVNCEKTNSDQVVLTVLKQMKQNQTGKITTFDWDLKQKLNQISINENLKVKSEIQPFLDQKTAQQLFSETELNNLNDLVNRCELDLEHLKAASLSLTDNDAAVLESLCQTNLKQFLDKNQDLNKKAYQLRLEKELNVINKLNFASYFLVVNDLVNYAFKKDILIGSGRGSAVGSLVAFLLNITKIDPVQHQLIFERFISTHRQDLPDIDIDIMENKRAEMINYLFEKYGKENCAQIVTFQRFKTRSAVKEVAKLFNDYGISDMILGVLPKDQTITFTDLKATEDSALQLCLQQFGLIVELALAIVDFPRQSSIHASGIVIASNSLIKTIPLLQLDNNHFLTQVSMEWLSFFNLNKFDLLGLINLTMISDVITQIKPSNQTVNQFLNTISWTDQNTFINLVNEDTLGIFQLESFGMKKLLVQIKPKTINQLAIVLALYRPGAQDNINLFINRLHNGYDQSDIDPRILPIVKNTYGVLIFQEQIINIVKVVANYSLEEADSFRRAISKKDVKLIQKNKRNFFERAVQNNFDLKTTTKIFSYIERFANYGFNLSHALGYALLSYWTAWLKTNYPVYFYLWLLNHFQSSKDKQKLIIRTLEKSGIEIYPPLLNKAQPNSVIENKKIYLGLNLIKGINDRYIQNLQKVQHLIQTQNNLQLTDVVSWCLDKTIGDIPLKDLLLLKTMGCFDFFEYTYDFNDAKDFWIKSDHLLFTRMPLEKKDSNFWIKQFFTN
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MPKPGIGELLWESCPLTPSPDFLKRPSRDLGTLDWLCKSPASAFESEPLTFKDVAIEFSLEEWQCLDTAQRDLYRNVLLENYRNLVFLGIAVSKPYLITCLEQKKEPWNIKRHEMVARPPVMSFHFAQDLWPEQNIKDSFQKVTLRRYGRCEYENLQLRKGYKHVDECMGHKGGHNTVKQCLTATPSKIFQCNKYMKVFDKFSNSNRYKRRHTGNKHFKCKECGKLFCILSQLTQHRRIHTRVNSYKCEECGKAFNWFSTLTKHKRIHTGEKPYIYEECGKAFNQSSQLTRHKIIHTEEKPSKYEECGKAFKQASHLTIHKIINTGEKPYKCEECDKVFSQSSHLTTQKILHTGENLYKCEECGKAFNLFSNLTNHKRIHAGEKPFKCKECGRGFNISSNLNKQEKIHTGEKPDKCEECDKAFNQSLKLTAHKKILVEGKPYKCEECGKVFNQFSTLTRHKIIHTGEKPYKCKECGKAFNQSSNLTEHKKIHTAEKSYKCEECGKAFNQHSNLINHRKIYTGEKPYKCEECGKAFNRSSTLTRHKKIHTGEKPYKCEECGRAFSQSSNLTEHKKIHTGEKPYKCEECGKAFNRFSTLTKHKRIHTGEKPYKCEECGKAFNQSYQLTRHKVIHTKEKLNKCEEFGKPFKQSSHLTIHKIIHTGEKPYRCEEHGKVFNQSSHLTTQKIIHTGENLYKFEEHGKAFNLFSNITNHKIIYTGEKPHKCEECGKAYNRYSNLTIHKRIHTGEKPYQCAECGKAFNCSSTLNRHKIIHTGEKPYKCKECGKAFNLSSTLTAHKKIHTGEKPYKCEECGKAFNQSSNLTTHKKIHTSEKPYKCEECGKSFNQFSSLNIHKIIHTGEKPYKCGDYGKAFNLSSNLTTHKKIHTGEKPYKCEECGKT
The following text describes a protein:
Function:
Catalytic subunit of the DNA primase complex and component of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex - primosome/replisome) which play an essential role in the initiation of DNA synthesis. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands.
Sequence:
MAEYNQGMLPDLLPVYYKKIFPHNFFYRWLSYGGEPKSYYTNREFSFTLMDDVYIRYLSFSDGLEFEKELIKTSPFKIDIGAVFSHRPKDQKTLKPGSFQAMEKELVFDIDMTDYDDVRSCCSGADICHNCWPLMAVGVQIIDRALREDFGFEHRLWARALPSNARSAIVDYLTLVKGGENQVKKVNLSSLSLHPHIQESLSILNDRFFEDYAICKQNFLNDDSKMLKMMKMLPDDLQTMIKKFLDQQDPSKLNSKNRWEALKIHADKKRSQLIDLSNEKKPPKDIREQLRKHSHLVEEIKLQYCYPRLDANVTKGVNHLLKSPFCIHPKTGRVCVPFCAEEVWQFNPFTVPTITQLCNELDNLDVTDAKKKKDFPLCKSLNDAVEVFKKFVEDLEKSFLKKRKEQNDMTLQF
The following text describes a protein:
Function:
Monoglutamylase which modifies tubulin, adding a single glutamate on the gamma-carboxyl group of specific glutamate residues of target proteins. Involved in the side-chain initiation step of the polyglutamylation reaction but not in the elongation step. Preferentially modifies beta-tail tubulin over the alpha-tubulin. Involved in side-chain glutamylation of tubulin in sensory cilia. Together with ttll-5 and ttll-11, required for male mating.
Sequence:
MSSGYSSAPSVSHTSSEADLNRIESYEDGVDEEASDEQRMCGLSELVTSCLTSSKSSRQKDSFEDDDDVPIEIVGTLKKSKSKKKKQCPPNITIEKKNGNSSPFLKSSQFTDVPPTIRFYTKGTKVTKPARKIQSRLTWCHNSLLPIVMRQTLSASHFTIVDESLFHIGYWGRHLKSAQYKALQPHQKVNHFPGAFHIGRKDRLWMHIRNRLEHFGEEFEIMPFTYILPTDRQELLKYLETDVNRHVIIKPPASARGSGITVTRKPKDFPTTATLVAQHYIERPLTINRAKFDLRLYAYVPTFEPLRVYIYDQGLVRFASVPYNPSVTNISNKYMHLTNYSINKLAEADGIANKPVPKWALHQLWDYFDQMGVNSQKIQKEIEDVIVKAFISCEKPIREHMSRFLEQEFICYELFGIDIILDEDYKPWLLEVNISPSLHSGTSLDVSVKAPLAKDVLNLAGIHVPPSFDKLHTADYSCRPRNGTKTREQLVKEASWVAAYRDQHGAIDNRIFKRLTPEDTRALVEFEDELDRIGDFKLVFPTAQTAHYQKFFAEPIYMNILLQQWQIAQEGDRSIGIDRLEQLCRQKHMQSDQEISF
The following text describes a protein:
Function:
Involved in nucleolar processing of pre-18S ribosomal RNA. Has a role in the nuclear export of 40S pre-ribosomal subunit to the cytoplasm (By similarity).
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MGGSQLKNLKAALKANGLTGQTNVKKSSKKKGKSPREFDREERQKTIERIREQFNPFDVKTNRNKKVGVMRESAAKLAVGKPGITKQAGEDQRKMFYEAKKSSKNRSGGVLDKRFGEKDKNLTSEEIMLERFTKERQRQSSTKRSLFNLDDSDGGEDENVYGEKLTHYGKSLSLEDDFDEGDLGLQHSDSEDFRLKQAGKRNMADQYGDEGLGDDALQEPARKKTKAEVMQEVIAKSKFYKHERQKAQEKLVQDIEGLDDDFESIMSELRTLPKTKPSQTEISTSTDIAPDYDIKVKELVLEKRAAPADRTKTDEEIKKEYEDKQKELEQKRLDRMNGIFNIEDQKDAGVEDLGEEFWEDSDSEEGEYGEYIKAIPDSDDDVDFEKDNNDDNEYDATSNGRPSARVIPSVPCPQIHDDLLNFLKSYPIEEHPSLVKRIVKTYQPKLAEGNKEKLGKFTAVLLRHILFLAEEDYSVNVKEIASLQNELVSILKTLSEKFTIPLSEDCRNIISDIQTRFKESQFYGLSPSDLVFFSVVGMLFSTSDHYHLVITPCLLLIAEFLEQIRFNSLQKLIFGSILVRIAIQYQRISKRYIPELTYFLQTSLRSLIPSTKGETLENKEKQEDNLSIVGSDINWSKVAPSLELHSLFSEDLEKQESIKLSVLVNNLESIDWCITNIWKDLTAFPEIINPFKDILNVAAEVYPGTSKPKQLVEKIEKLLKFQERLPLTLQQHKPLAIPSNTPKFEENFNPDKKSYDPDKTRSELNKMKAQLKKERKFTMKEIRKDTRFEARQGIEEKKKEYADYHSKMARIVNQISTEEGAEKNKYEREKKLRNTKR
The following text describes a protein:
Function:
Involved in TGF-beta pathway.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MFHPGMTSQPSTSNQMYYDPLYGAEQIVQCNPMDYHQANILCGMQYFNNSHNRYPLLPQMPPQFTNDHPYDFPNVPTISTLDEASSFNGFLIPSQPSSYNNNNISCVFTPTPCTSSQASSQPPPTPTVNPTPIPPNAGAVLTTAMDSCQQISHVLQCYQQGGEDSDFVRKAIESLVKKLKDKRIELDALITAVTSNGKQPTGCVTIQRSLDGRLQVAGRKGVPHVVYARIWRWPKVSKNELVKLVQCQTSSDHPDNICINPYHYERVVSNRITSADQSLHVENSPMKSEYLGDAGVIDSCSDWPNTPPDNNFNGGFAPDQPQLVTPIISDIPIDLNQIYVPTPPQLLDNWCSIIYYELDTPIGETFKVSARDHGKVIVDGGMDPHGENEGRLCLGALSNVHRTEASEKARIHIGRGVELTAHADGNISITSNCKIFVRSGYLDYTHGSEYSSKAHRFTPNESSFTVFDIRWAYMQMLRRSRSSNEAVRAQAAAVAGYAPMSVMPAIMPDSGVDRMRRDFCTIAISFVKAWGDVYQRKTIKETPCWIEVTLHRPLQILDQLLKNSSQFGSS
The following text describes a protein:
Function:
Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with G at the virion surface. Upon G binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis.
Subcellular Localization:
Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass membrane protein.
Sequence:
MVVILDKRCYCNLLILILMISECSVGILHYEKLSKIGLVKGVTRKYKIKSNPLTKDIVIKMIPNVSNMSQCTGSVMENYKTRLNGILTPIKGALEIYKNNTHDLVGDVRLAGVIMAGVAIGIATAAQITAGVALYEAMKNADNINKLKSSIESTNEAVVKLQETAEKTVYVLTALQDYINTNLVPTIDKISCKQTELSLDLALSKYLSDLLFVFGPNLQDPVSNSMTIQAISQAFGGNYETLLRTLGYATEDFDDLLESDSITGQIIYVDLSSYYIIVRVYFPILTEIQQAYIQELLPVSFNNDNSEWISIVPNFILVRNTLISNIEIGFCLITKRSVICNQDYATPMTNNMRECLTGSTEKCPRELVVSSHVPRFALSNGVLFANCISVTCQCQTTGRAISQSGEQTLLMIDNTTCPTAVLGNVIISLGKYLGSVNYNSEGIAIGPPVFTDKVDISSQISSMNQSLQQSKDYIKEAQRLLDTVNPSLISMLSMIILYVLSIASLCIGLITFISFIIVEKKRNTYSRLEDRRVRPTSSGDLYYIGT
The following text describes a protein:
Function:
Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MSLISGIASILAIGLLSPVQSILALILLFVTVAINLYTSGYVLMGILYILVYVGAIAILFLFILSLLNIEYKPTGGMHPLVIVLILIPLIPLDIAFEPIAIVESVSTTYNELSIVGTLFYSEYAPMLVIIGIILIVSVIGAIAMTR