lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3' to 5' direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase.
Sequence:
MKKELSFALNYALNKGFQIHPNAFKILENVDVKKLEKIIKEIVREKTKQKLFQINQDDLETYLGIKDDPSLENEVKVLLDPTDKITTGEGVKGYNALFSSRFNKLKRIISDRPEARMLKSLTFVKNERSEDDMYVCGLVTSRNSERNVTKLVLEDPSGSFEGIIFDTELQKTADTLLVDQFVMARVSVGKNSGFIIKDLIFPDIPDQATNKSESEAYAVFLSDLHIGSKYFMEEELTEFFSWISSPDPTAKKIRFILIGGDMVDGVGIYPNQNKELVCQTIEEQLKKVESLIDQIPKNIKIIIMPGNHDPGRRALPQPAIPKKYNSGLWDRENVIMVGNPAVVSLNGVKVMMFHGQSIDDIVKTTPGLSYDKPTNVMKHLLRARHLSPIYGSQTPIAPEMQDLMVIEDIPDIFHVGHVHKAQLDMYKGILLVNSGSWQKQTPFQASVGMTPNPGIALLVNLKTFQVFHQNYNSNLDNILQS
The following text describes a protein:
Function:
Essential for spermatogenesis and male fertility. May play an important role in sperm head and tail formation. May act as a tumor suppressor by inhibiting cell proliferation (By similarity).
Subcellular Localization:
Cytoplasm.
Sequence:
MDSESKEEQQCTASSAVMSSLETQFLSVPHQLESASLSWSIRKSLHSSTVLMDDCHFGFPTRSLRAGFHALPPLPEPQTLRLRPASLRTQEISHLLARVFRNLYTAQVIGDDLSDSLIKARGSEDARHEEFLDQLQQARAIYKQRLDEAAMLERHIMQARARDIAETEHTTKQSRLQVVETPVKLPPVKTAFRWCLDSKLMRKHHLISTEDYYTDPVPFCPAPKDKSTLGCSKLTFSCEQRFLRKSELDREAEEHCRQLTECDDFEYTVDSLGSISKAKERTTDSVKKTSRPKNKKWMEHLQVPQRALDRRLLASMENRNHFLKNPRFFPPNTPHGGKSLIVPLSKPERRASLNAEPEWSCTDAPVFLAKPSVGFFTDYEIGPVYEMVIALQNTTSTSRFLRVLPPSSPYFALGLGMFPGKGGIVAPGMTCQYIVQFIPDCLGDFDDFILVETQSPHTLVIPLQARRPPPVLTLSPVLDCGHCLIGGVKITKFICKNVGFSVGKFCIMPQKSWPPPSFRAVATTGFVEQPPFGVMPSVFELAPGYAILLEVLFLPTGLGQAEETFIIVCDNCQIKEVVVVGTGQLVALDLIHISGGKNEPDPGELKDLTAQYFIRFEPENVQSTPKKQLIIRNAT
The following text describes a protein:
Function:
Essential subunit of both the farnesyltransferase and the geranylgeranyltransferase complex. Contributes to the transfer of a farnesyl or geranylgeranyl moiety from farnesyl or geranylgeranyl diphosphate to a cysteine at the fourth position from the C-terminus of several proteins having the C-terminal sequence Cys-aliphatic-aliphatic-X. May positively regulate neuromuscular junction development downstream of MUSK via its function in RAC1 prenylation and activation.
Sequence:
MADDVYSSDENEENYVFYRDREEWKDVTPVPQEEGPHPVVQIAYSDRFKDVFDYFRAVLKADERSERAFSLTKDAIGLNAANYTVWHYRRLLLQDLKKDLWEEMKFVKDVIEDQPKNYQVWHHRRVLVEWLKDASKEMQFTEEILNMDAKNYHCWQHRQWCIREFKLWDGELDFVNNLLCEDLRNNSAWNQRFYVINNSTGITPELLDMEVSYTIQMIKRAPNNESAWNYLKGILMAAGAEISSYPKLMDTCQELRASGVHTPYLLAFLLDCHEEMLETGSGVKEDNLDKAVQLCNQLAQEEDTIRKEYWNYCRRSLQLKYGTAEETL
The following text describes a protein:
Function:
Involved in cytoplasm to vacuole transport (Cvt), pexophagy, mitophagy and nucleophagy. Recruits mitochondria for their selective degradation via autophagy (mitophagy) during starvation. Works as scaffold proteins that recruit ATG proteins to the pre-autophagosome (PAS), the site of vesicle/autophagosome formation. Required for the Cvt vesicles completion.
Subcellular Localization:
Preautophagosomal structure membrane; Peripheral membrane protein. Vacuole membrane; Peripheral membrane protein. Note=During pexophagy, accumulates in the vacuolar membrane region, where the peroxisomes contact the vacuole.
Sequence:
MDIYQASDGGLYRLDAYLDSYDDIDAVYQDVSAATGIADHNVLLFLEDGRELKSDVLFDIKNQAGPSYNTGPPIKVYMYNRETFWTDVETWAVQMQEDVQLPPPLDLSSFNGIQHPFLVAHDHLSHLKSLSDTQSKALQIAYANLSQHLQPLVDEFQSFASRVEASFKTEEELIKSSKLDMALLPKLVINPALLKKKDDEGKVRTMGDYVNAKKMEQVRESCRVLHVENVDRFNSLAASLDGLVSQSEAETAAFNDRSAEIENEFAEGLARLEVALGQLSQLSGSGTADVHQDFVELDQAMRDDLVALTAVKNEFTFDIHLHLRQVAHFQSQIHELIEPLRKFDADLLASKDRSAFPHLYRLHQIPFAYAAAVSEVVRRRDFGQMLTEWTKRLRGTLNTFTQVEAKRREQVNKESLSQLPFSVPVLSETQGPKIEVTLVTGVEGLGNKAFGYEEVEKLASWLEQMRNDPEVIANMEEGDAERLQAMQTSIEGLIMKFDTTADELDRMVEQGVFQPKSQSRSASSSRAMLHLSSQLRAVNKDKTVYEKRLQELEESHQNHLKQLTEQHEKREQALQMRQGELQEELARLRTDLSDEMLARQALSAELEEKTREQEDQKDQMDMLAGLQAELTQEKDRATDLGVRLQEALMDVDGLKIAEQTLITQLQELQEERKKALEGEKEAQAMVKNLESQLAGIKAELEAVTGQLTQAQEDREAALRNQSAEADKLMRDRIAEADGDRAVLEHQHLTLTRELDNLKLETEKKLSAAQNTAIRQVDGLKAELSLTKAQMRELQRKELTLTDELAVVRDTMRVLSQEKGHGAEHAREAVSLVTRYYEACQRLLHAINTSTTISGSAAQPRSHSPQPLNQPPSKPQISPPSNQAASTSLSTSSKDEMRESVSLVAAQGFDLVEFTEAVTKTIGLVKKWSKSCRQYRDQARNKISFTNFAKGDLALFLPTRNTASRSWAAFNISAPHNFLRVDDILQEQLKSREWIIARIVKTDEAVASGGESLETNPFGLADGLRYCVHTVEEYNIGTSRPYRRNVSSSFTDSQIIPSSRRSRSSGGGNAFKNAGMTSIRDGPGQAEMQGEYFPPMREMGEDVSISETTEQKVGSVGDGQNNSQDPSSTAGSLQPSLESSPVKAVPSLPWPSLPSSNVGQEGRMPISSDHISKTITPPPSAVTSQIQSLGRISSRSLKDSSSTLGHPTSSPSRGEYPSSLNPANFTARPPSVASSNSSYPRGIGLGPGPGGKATPAPAMTVTTSHDKGGEALLDGTQSPSRMTSPASEAPSSPEKGKKTHNPRASPSNFNALGTTPGDTPGGNPAILSGLATLGKRRESKSSIQSDGKVSAIDILRKIDKSSGSNLKDGDM
The following text describes a protein:
Function:
Sliding clamp subunit that acts as a moving platform for DNA processing. Responsible for tethering the catalytic subunit of DNA polymerase and other proteins to DNA during high-speed replication.
Sequence:
MSVRALFPKGKEPRYAFEVLIRMLPEAVLNFSSDGISLKALDPTKTALLDLTFYATALEDYSIDEETKVGIIFTTIKDVIKRIGATEKLELEVDKERNRFSFYIYPKKGREVGLVRRFSFPIVQVLEEEIPELAVSFDASFEIDSAVLDDILAMVDEVSDWIQITVSPDKVLFRGVGEGGKAAETELSYDSESVFNISAGEAASAKYSVEMLRDISGKMKSLSKRVKVELSANKPIRLTYEFTSGVFTATIAPRVD
The following text describes a protein:
Function:
Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate.
Sequence:
MQSFAHFSLFCALNSSIMKKNIAIFASGSGSNAENIIRYFQKSDSVEVSLVLSNKSDAYVLERAHRLKVPCNVFPKEDWIAGDEILAILQEYRIDFIVLAGFLVRVPDLLLHAYPDKIINIHPALLPKFGGKGMYGDKVHQAVVAAGEKETGITIHYINEHYDEGNIIFQATCPVLPDDSPEEVAKKVHALEYEHFPHVVEETISIKY
The following text describes a protein:
Function:
Structural subunit of the major fimbriae. These long, filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. They play an important role in the invasion of periodontal tissues. Fimbriae and their constituents are major virulence factors. FimA proteins from different strains have highly divergent sequences, and this has been used for classification. The sequence-based classification correlates with pathogenicity.
Miscellaneous:
MISCELLANEOUS: Strain ATCC BAA-308 / W83 seems to lack fimbriae, probably due to very low expression of the fimA gene; MISCELLANEOUS: The name (major fimbrium subunit) does not indicate the abundance of the protein, but is derived from the greater length of the major fimbriae. In strain ATCC 33277 and strain 381, major fimbriae are 300 - 1600 nM in length and about 5 nm in diameter. In contrast, minor fimbriae are only about 80 - 120 nm long. This length difference is observed only in a small number of strains, including strain ATCC 33277 and strain 381, and is due to a loss of function mutation in FimB, a protein that restricts fimbrial length in other strains.
Subcellular Localization:
Fimbrium. Cell outer membrane. Note=Synthesized as palmitoylated precursor. The lipidated propeptide is removed during processing to the mature protein.
Sequence:
MKKTKFFLLGLAALAMTACNKDNEAEPVVETNATVSFIIKSGESRAVGDDLTDAKITKLTAMVYAGQVQEGIKTVEEDGGVLKVEGIPCKSGANRVLVVVANHNYELTGKSLNEVEALTTSLTAENQNAKNLIMTGKSAAFTIKPGSNHYGYPGGTASDNLVSAGTPLAVTRVHAGISFAGVEVNMATQYQNYYSFKPADAKIAALVAKKDSKIFGNSLVSNTNAYLYGVQTPAGLYTPDAAGETYELEASLNTNYAVGAGFYVLESKYDASNELRPTILCIYGKLLDKDGNPLTEPALTDAINAGFCDGDGTTYYPVLVNYDGNGYIYSGAITQGQNKIVRNNHYKISLNITGPGTNTPENPQPVQANLNVTCQVTPWVVVNQAATW
The following text describes a protein:
Function:
Phosphomevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (By similarity). Erg8 converts 5-phosphomevalonate to 5-diphosphomevalonate (By similarity). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphate, which is also an important intermediate in the biosynthesis of ubiquinone, dolichol, heme and prenylated proteins. Activity by the mevalonate kinase erg12 (AFUA_4G07780) first converts mevalonate into 5-phosphomevalonate. 5-phosphomevalonate is then further converted to 5-diphosphomevalonate by the phosphomevalonate kinase erg8 (AFUA_5G10680). The diphosphomevalonate decarboxylase mvd1 (AFUA_4G07130) then produces isopentenyl diphosphate. The isopentenyl-diphosphate delta-isomerase idi1 (AFUA_6G11160) then catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its highly electrophilic allylic isomer, dimethylallyl diphosphate (DMAPP). Finally the farnesyl diphosphate synthase erg20 (AFUA_5G02450) catalyzes the sequential condensation of isopentenyl pyrophosphate with dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate (Probable).
Sequence:
MLPLPPAVTALSAPGKVLLTGGYLVLDRSYTGTVFALDARIHVIVQQLRRNHRREAASGSAHGRSDTPQAEGNVHGDKEDEGTIVVHSPQFVDAVWEYSIQRCEDGGGVLVKQRNDGPRNLFVETSLNFALTYISYVADSKDFGSLSITILADNDYYSETAFSKASGLRSSSRFVDFGVRLQEAHKTGLGSSAALVTALVSSLVIHRTMQPDDLGPGRDKLHNLAQAAHCAAQGKVGSGFDVAAAIYGSCLYRRFSPSILESVGDAGSPGFEERLFRIVEDADPQHPWDTECLDFGMKLPRGMQMVLCDVECGSQTPSMVRKVLEWRKQNQKEADMLWGALQSNNERLRLELRRLAQSPDEHTLSDFENVRTYIQRSRNHIRSMTQKSDVPIEPRVQTELLDALSELEGVIGGVVPGAGGYDAIVLLIQDNPDVITRLKAFFETWESKAEDDFGGKIGKVRLLGVRHGSEGVKNEMLEQYAGWV
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MRGNYELVASLDGLSPKPDLETQIKSEEEPGVGDGGHPAPKGVPTSALPDGGPDGERGSVLQSPAGPVEPPGARPPPPPSPAPPASPSPAPREEPPPAPPERESPGGPRPPPPREPDPPGRGRRHGVAAEAPPPSPGRPAPRAPGAGQREPGGPTRPVPPEDSPAGGAAHADEAGDVRGSPSGAFPAGARPSRVGGRDGRGPAARPAAAPGPPARGRAFVCGQCGKGFNHKQDLARHQRTHTGERPYPCPDCGRRFVQKTHLMTHFRIHTGERPFPCPDCEKSFRKKTHLVRHRHTHLGVRPFSCPHCPKSFGQREDLGRHLRCHSGEQPFACPECGQRFTWKKNLVTHQRRHGGERPFACPECGERFDRKRGLAVHRKTHGEEGPAGPRPGPRLPPPPREKAFPCPVCERRFGHKQDLIRHQRVHTGERPFACPECGKRFSQKAHLVTHTRVHTGERPYPCARCDRRFSKKTHLSRHQRVHAEEGPGPGGAGPAWRPGPAGPPQDLACPERGKGFGREARPDARRRGRAGAHPCPWPRCGQSFCRESALLAHQKSHHGSRPHPCPECGKRFGLKQDLVRHQRIHTGERPFPCVLCGKRFNQRAHLLTHQRTHTGERPFPCPDCERRFGKKAHLVRHQRVHAAQQPRLHLLGMGTLPLGDPGLPGGALRDETIYIFRV
The following text describes a protein:
Function:
Isoform Bcl-X(L) also regulates presynaptic plasticity, including neurotransmitter release and recovery, number of axonal mitochondria as well as size and number of synaptic vesicle clusters. During synaptic stimulation, increases ATP availability from mitochondria through regulation of mitochondrial membrane ATP synthase F(1)F(0) activity and regulates endocytic vesicle retrieval in hippocampal neurons through association with DMN1L and stimulation of its GTPase activity in synaptic vesicles. May attenuate inflammation impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release; Isoform Bcl-X(S) promotes apoptosis; Potent inhibitor of cell death. Inhibits activation of caspases. Appears to regulate cell death by blocking the voltage-dependent anion channel (VDAC) by binding to it and preventing the release of the caspase activator, CYC1, from the mitochondrial membrane. Also acts as a regulator of G2 checkpoint and progression to cytokinesis during mitosis.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytosol. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane. Mitochondrion matrix. Mitochondrion membrane. Nucleus membrane; Single-pass membrane protein; Cytoplasmic side.
Sequence:
MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEGTESEMETPSAINGNPSWHLVDSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIAAWMATYLNDHLEPWIQENGGWDTFVELYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK
The following text describes a protein:
Function:
Plays an important role in maintenance of mitochondrial morphology and in mediating either calcium or potassium/proton antiport (By similarity). Mediates proton-dependent calcium efflux from mitochondrion (By similarity). Also functions as an electroneutral mitochondrial proton/potassium exchanger (By similarity). Required for the maintenance of the tubular shape and cristae organization (By similarity).
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein.
Sequence:
MLLQSCGRRACRLPRALRRQAPLGNLGDRACLSCTSLRLANKMTVHFKYCTSVAPVYAYSKKDHYCCWTKGLERTYFTLMSSSGSWTPLAAMGVLGPKYLPVRWWHSSRSLQDDSIVEKSLKSLKDKNKKLEEGGPVYSPTEVEVVKKSIGQRIVDELKHYYHGFRLLWIDTKIAARMLWRILHGNTLSRRERRQFLRICADLFRLVPFLVFLVVPFMEFLLPVALKLFPNMLPSTFETKSKKEERLKKQLRVKLELAKFLQDTIEEMALKNKAAKGNVTKDFSTFFQKIRETGERPSNEEILRFSKLFEDELTLDNLTRPQLVALCKLLELQSIGTNNFLRFQLTMRLRTIKADDKMIAEEGVDSLTVKELQAACRARGMRALGVTEERLREQLKQWLDLHLNQEIPTSLLILSRAMYLPDTLSPADQLKTTLQTLPESVAKEAQVKVAEVEGEKVDNKARLEATLQEEAAIRKENEEKEMERITEAAEKAKETLQVAAMKLESAVDLEPAVLQVKESQVAMDSKQELAKADMETLKDTAPVLEGIKGEEITKEEIDMLSDACNKLQEQKKSLTKEKEELEELKGDIQEYNEDLQEIKELSKAGQEEVVEESKASKRLTKRVNRMIGQIDKIINELETNQKTVDVKLDRGDSPPAGENLISIAELINAMKQIQKIPEEKLTRIAEALDENKDGKIDIDNVVKVVELIDKEDVDIGTSQVAEIMALLQKEEKLEEKEKAKEKQDKEAAEVKN
The following text describes a protein:
Function:
Pseudokinase which may act as an adapter for kinases sad-1 and par-4 and thereby is involved in several developmental processes. Regulates cell-autonomously both neuronal polarity and synaptic organization when bound to sad-1. Required for sad-1 localization to synapses. Required to establish germline stem cell (GSC) quiescence during dauer development, to promote cell shedding during embryogenesis and to control asymmetric cell division of the Q.p neuroblast lineage, probably when bound to par-4. May be involved in maintaining the integrity of the early embryonic cortex when bound to par-4.
Subcellular Localization:
Perikaryon. Nucleus. Cell projection, dendrite. Cell projection, axon. Synapse. Cytoplasm, cell cortex. Cytoplasm. Note=Localizes in punctate structures along the neurites of GABAergic motoneurons. Co-localizes with sad-1 at synapses. Co-localizes with par-4 at the cell cortex of the early embryo. Cell cortex localization is regulated by par-4.
Domain:
The protein kinase domain is predicted to be catalytically inactive.
Sequence:
MADTTILDTTCSSTLAANVEFSHATDSAIGISLKNATITEAEGVPNLKETGYDCVRYMGTCNGGQIYLGRERKKLKDYVAIKKFAIDDVDDYAAIAKESSNLRLMHHPNIIELCECFVYERSIYQITPAMNLGSLFDIVFEYMKWGINEKSAAAITRQLLDALSYLHQRRYIHRDLKPKHILIDSSGNVKLSGFRFMIELNHHLDCVFEFDAHLQNQLYYLAPEVLAQNIHGYTSKSDIYMLGISICEAINGVMPFGELEPLEMLHRKLNGQVPRPVDMISLKDDQKMGLDISHRPQEHLTRRFSKEMHEFIANCLDYDPQQRGSASDLKSSAWLGSKIHKNLGPVDVRQELNLDYAHFDLSLWEQEPLIPMEPDQKYEIVFDYSPIS
The following text describes a protein:
Function:
Has a role in nuclear-cytoplasmic transport of proteins and mRNAs.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MAQFWKKGASFINWYFNKLNTNPEDLEIVYNNDSIVQFNKQTFQGRNEEGKLKIIEYLSSPDMKKAKYKIVDYTTQPSIENCIFIMVQGYVIPDEAHPEVDQSFDFSIFVHLAKQDNAFLVLNQFYAISEDLD
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MAAATGLKFEPIPRRYDTVGRRRWPSVKCTGPRFQAVTIMLMPPIRLPILPQVRTPLHAALRSCVGPLGLVFAYSCSYNLLLFAPSIYLLQIYDRVLSSRSGETLLLLTLIVAITVVVGGVFDALRRAVLGRLGAWLDDRLRPCVISAGLESALRSDWTQASGAYRDLTVLRQFVESGASPMLFDALWAPLFLLVLVLIHPLLGVVGACCVAFLFALTVAGELVTEDVLLRSGAALSRSCGRLQTAASNIHMIRAMGMLDSAARMIHRDAQHARREHDVALRRGEIVSLAAKPVRALSQVLIMGAAAWLVLDHGKSPAIIFASTLMFSRALAPVESAVAGWKSLVTAVSACQRLGALLAAFPVARQQSPEVSPLQARSGLVVDNVDVRLAGTNHLLLNGVSFSLMPGECLGIIGPSGSGKSLLGQVIAGLSMPTHGRVVLDNTDVSLFREGLKGDRLGYLPQDINLLGDTINDIIARLDDADRRKVIEAAKLVGIHGAIMRLPLGYDTVVQSEATFSRGYRQRLGLARAFFGSPRLIVLDEPNASLDYGGERMLLDAIERMKLAGVILVVITHRMGLLAATDKIAIMEDGAVAAFGDSEDIFERHLSRPQVTSQIAP
The following text describes a protein:
Function:
Acts as a guanine nucleotide exchange factor (GEF) for RhoA GTPases. Its activation induces formation of actin stress fibers. Also acts as a GEF for RAC1, inducing production of reactive oxygen species (ROS). Does not act as a GEF for CDC42. The G protein beta-gamma (Gbetagamma) subunits of heterotrimeric G proteins act as activators, explaining the integrated effects of LPA and other G-protein coupled receptor agonists on actin stress fiber formation, cell shape change and ROS production. Required for EPB41L4B-mediated regulation of the circumferential actomyosin belt in epithelial cells.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton. Cell membrane. Apical cell membrane. Note=In unactivated eosinophils, distributed around the cell periphery in the perimembranous region. In activated eosinophils, relocates to the tip of the nucleopod, a membrane structure formed during activation when the nucleus moves to one end of the cell, and is also concentrated in membrane protrusions at the opposite end of the cell. Localizes to the apical cell membrane in epithelial cells.
Sequence:
MGDDQEDDFPRRLSESMEDLSLDLGALQGSEYLQDLGLGAPSHSQPGETPDSRPTGEEPGRDSLFSSLAGSQDLSRRRSWERSRSCSESWRRLSLDASAVDEEPCLPRTLASLALNLPGGGLKTWTQGCLSGGGTPAESPGKECDSPKKRGRSRSVPVSFYEIRSPEISPGLEVPTPPVQGLEPPVLECMEKDHVEPDHVLIVQQVLQELRQYHGARQRACMSASPGGAHSNLTWFEFLSESEDGAGKNEKSDKSTSVKRRLSCLRSRVTRQKEKGKSPAHLKDKGQDARERRECVNGHQLLQGTFSGPSSCPLCGKPFLSSASLKEHPRGTLLSDGSPALSRNVGMTVSQKGGPQPTPSPAGPGTQLGPITGEMDEADSAFLKFKQTADDSLSLTSPNTESIFVEDPYTASLRSEIESDGHEFEAESWSLAVDAAYAKKQKREVVKRQDVLYELMQTEVHHVRTLKIMLKVYSRALQEELQFSSKAIGRLFPCADDLLETHSHFLARLKERRQESLEEGSDRNYVIQKIGDLLVQQFSGENGERMKEKYGVFCSGHNEAVSHYKLLLQQNKKFQNLIKKIGNFSIVRRLGVQECILLVTQRITKYPVLVERIIQNTEAGTEDYEDLTQALNLIKDIISQVDAKVSECEKGQRLREIAGKMDLKSSSKLKNGLTFRKEDMLQRQLHLEGMLCWKTTSGRLKDILAILLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASLQGPEMYEIYTSSKEDRNAWMAHIQRAVESCPDEEEGPFSLPEEERKVVEARATRLRDFQERLSMKDQLIAQSLLEKQQIYLEMAEMGGLEDLPQPRGLFRGGDPSETLQGELILKSAMSEIEGIQSLICRQLGSANGQAEDGGSSTGPPRRAETFAGYDCTNSPTKNGSFKKKVSSTDPRPRDWRGPPNSPDLKLSDSDIPGSSEESPQVVEAPGTESDPRLPTVLESELVQRIQTLSQLLLNLQAVIAHQDSYVETQRAAIQEREKQFRLQSTRGNLLLEQERQRNFEKQREERAALEKLQSQLRHEQQRWERERQWQHQELERAGARLQEREGEARQLRERLEQERAELERQRQAYQHDLERLREAQRAVERERERLELLRRLKKQNTAPGALPPDTLAEAQPPSHPPSFNGEGLEGPRVSMLPSGVGPEYAERPEVARRDSAPTENRLAKSDVPIQLLSATNQFQRQAAVQQQIPTKLAASTKGGKDKGGKSRGSQRWESSASFDLKQQLLLNKLMGKDESTSRNRRSLSPILPGRHSPAPPPDPGFPAPSPPPADSPSEGFSLKAGGTALLPGPPAPSPLPATPLSAKEDASKEDVIFF
The following text describes a protein:
Function:
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
Subcellular Localization:
Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side. Endoplasmic reticulum membrane; Peripheral membrane protein.
Sequence:
MKIKELQKTVNIAWSPAQQQQILLAAGTAAQQFDSNANSTLELYSPNFSDATYDLELRASVSSQYKFQKLIWSPVGPHPSGLIVGGCEAGQINIYSADKLLAGKEEPLLKRQDKHTGAVSGLDFNPFQNNLLASCASESEILIWDLNNPETSMSPGTKTQPLEDVKNVAWNRQVQHILASVFSTRCVIWDLRKSQQIIKLSDSQSRVRWHAIEWHPEAATQVWLASEDDQAPVVQLWDLRYATAPAKTYQIHERGVLGMSWCLQDNDLMVSCGKDNRIYCWNPNTKIPEGEILSEVATTASWYSDVQFCPRNPALIASASLEGAVSIYSLHGGTHHLVQTANKIADSFPGMDQFAQEPIPQQATQVVYHDLAHAPKWMKRPCGVAFGFGGKLVSFNGTSKTVKVQQLTTESALVDRANALERSLVDANYSDYCRQRADETPDQHGRYIWYFIKANFELNPKEEMLNLLGYNKDDIDSKFNKFIKETDGNSHSDVDTLTTRISTLTHSDSSEVECDQSTNYSTDNSQTQDNKFDGNAIDSQNHNDFATPPRPQFKVPSGDHSDSLIAEAILTGNVDAAVELCLEAQRIPEALIIASTAGIETLNRTQTRYLLQQKNELSHVISALVSRDWLDFVNRCTVDSWKEALVAALKHSERKVVDICERLGDRLLSECASSAEFTRNAMLCYICAGSIDKLVTAWYQLKRLEQQNPGYKPNTTELQDLAEMVMLMCKSLEQQGISVDLAGRFAGFLTEYGGLLASQGALTAALQYITTLGGGAAASESDVLQSLRDRINNAVNLDYTQPQAAVAAAPHGYQPTRGRGSFSQPQPSAPMPYGQPPNQYAQPSWPAQVPPLQTSYPGAQQPQAPPQIFNPQPVKPEPLAQPPRPLSNASSSGGPPPAGGASSSGGSGLSGRSKYVLDPSVAAPTSSYGMPYNPVPAPVPSAVPFGGGGVPGPAPQPASVPTYNSNAFNTNPIAAAQPYNPSPLMPAQQNQFVPGVNPIETMPPPAVPPVIQNVQRNPTPPPGWNDPPALKSSRAPKPKPVVEPSAAIFHPLFPVDPNQNQNGYVDPSQYQHAAPLGGVPNTYYNPAAFNNNPQQQQQHQQSYLQPQQPAPGIQQPNWQGQQQTIGYTEQPAPIQQQRQPAPPKEKPPLPEEYIYLQTVLEELKNRCLGATNDPRTKRKFVDVVKRLENLYDCLRDGKLTPTTVQYLNQIVQYIQISDYANAMEIHTQIAFGTDFAQCAGFMQGLKVLLQSASELQLVLR
The following text describes a protein:
Function:
Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. Participates in AID/AICDA-mediated somatic hypermutation (SHM) and class-switch recombination (CSR), 2 processes resulting in the production of high-affinity, mutated isotype-switched antibodies.
Subcellular Localization:
Nucleus.
Sequence:
MELKMKKRMKKLERWLMHYYKLIYLIRLDESNEDDADAVHHALKVIDMLLEIKGDIVEEDVISSSLFQWVLKRSCQRGVFDANKQYASELLSVILQQSEKAKTRLSDKVDGMDLLLRALASYKKKDPSSGDESEFMENMFDCLCAALMWKGNRKAFLEGEGLQLMNLMLRERKQSRQSALKVLDHATTGPEGADNCAKFVEILGLRTLFPLLMRTPVKGKRKDTTPDEHEEHVVAILSSLMRWCEDASRVRIMQKFTEHEHEKVDRAVELMFKYKERVQRWESKQKEQDDFEAYYLDKMDAGLYTLQNVVYVLGEVCVHMNSARMRAIKLLKMKSGEERLTKHLIPILAEYQENLGESADTERNRMDILIAKLTASEKAAASGN
The following text describes a protein:
Function:
Essential splicing protein required for U2 snRNP binding to pre-mRNA during spliceosome assembly.
Miscellaneous:
MISCELLANEOUS: Present with 1830 molecules/cell in log phase SD medium.
Subcellular Localization:
Nucleus.
Sequence:
MARTKSRKRSGNNQNKNASVVNNKAEIAAMIDARRLEQKKKGGVTNSKGKTNKVVDAKLEKEFKDVLQRFQVQENDTPKEITKDEKNNHVVIVEKNPVMNRKHTAEDELEDTPSDGIEEHLSARKRRKTEKPSLSQLKSQVPYPQIIEWYDCDARYPGLLASIKCTKNVIPVPSHWQSKKEYLSGRSLLGKRPFELPDIIKKTNIEQMRSTLPQSGLDGQDEKSLKEASRARVQPKMGALDLDYKKLHDVFFKIGANWKPDHLLCFGDVYYENRNLFEETNWKRMVDHKRPGRISQELRAIMNLPEGQLPPWCMKMKDIGLPTGYPDLKIAGLNWDITNLKGDVYGKIIPNHHSRSKKQGRNYFGALISFETPEFENSKEDTQANAENGRQDDKIDDEVEHKLDHFQEDISEVTSAEEKLERNEEESEKQLYTVLK
The following text describes a protein:
Function:
Guanine nucleotide-exchange factor (GEF) for RHO1 that stimulates the exchange of RHO1 GDP-bound form into GTP-bound form. Required for signaling of cell wall defects to RHO1.
Domain:
The DH domain mediates interaction with RHO1.
Sequence:
MYRYNRSSPFERTPEKRVSRQESQRKSIELPKLPPLNTRNSFLDDSDNGTDNISIGWTPISDTQQFQSPVPQAFTFTSKHSARGNGTSSSESTPKSTKYVKERRPPPPPPLLYSTESIRIDSPMVSPSSQSRERSPNKLSFIGNSEERHHMEYISNHSRILKSPFANGFSPNSPKSPRDSSKQQAHFSDESDLRCHEREKALPPIPFTTTLLLSPFDDEDSEFFTKPPPPLSTSRNVSGNSRVSEALESVYSDSDYTFNNSNARQSSFNSLLGAKPLELAPSITAPTQPFSIQSIDEHKLYQCDNVYKLSAIYEWILKVYFEWFNECVFTKIDLFQIVQLLLEFQMPTNFDQDTIDSNVDNIMASFISQKAVRFDIINDEEVAVVVGGLDITGVFTELLPCYSFIDNTYGSTNSLICYSNVCTHGQSSGFRKEIKLSEIINKSVGLWTEYWHLTPDDLAEINPREVQRQSFIFDLIILEERSLNMATAAVEIYGKRFDKSLLPDEPEFKALAFDIFEPLIQLHTEFLLTPIFWKLKTRGKFIDGVGKIYSKWCGEAKNIYLNYAKAMATVHEIIMWEKKNKTKFVTWLKEIDNSVEITRSKMYHDVIFFGGFFKSLQNMPVTLRSILKNTDPSMEDYEYLKIVIKEVEKLNFEVNQVHGLAIDHRKLVRFSKQLVLSTNSSNATSYVNVGGSTNANDDDAIQDKLALGLTYPERKLVLSGTVYKKRDLWLDPTPVYIALLDNCLLITEEISKGETQKYKLIERPIPIDYLSLEKRKIPGTSKQPLRNYSQKEHKSPMHNFSTPINSMRPLLKSSGNHMSTAYGDRKTSNTEISNANPNTDEFSFKIRNTATGESFKFFTESAEVLNQWIDAIMESFKRNAENHDLNAFEFTVLSSEFAYFDKDAPVNLPVAPEGSEIDVALKAYAQKANKDSCSWSKTTRILCCEDVKFEGRIYLFVATTDGIYVKYRDDYGSGFVKILELNDVKRMEANVKLGLLFVLDNRKLCYFNISTVVSRYLAQGNTLDENCIVGTVIRDKVRFFKIADDFGNSKHLFFERKGKIVILTPEFDQLTNQVKYFKFYKEYKLPSSSNNILNNEIEDIAIFRKSFAVCTKKTVILYQDSFEDNGIVLPSFLNDKDMMAHLRHPHLNSLPFKSATDSKKRPSIESLTEEAKKDIATCKAIPVNFFQISQSSFFALVYDEAVVKINCYGEMSDWRKDILLLDFCCTGASFHGNHLILVGDNLIQIYDLKNVEQNLGELVPVQIIKGKKIKLASSERREKTILVLSHPNILNRQLLVACNPVAMADHQ
The following text describes a protein:
Function:
Phosphorylates D-xylulose to produce D-xylulose 5-phosphate, a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis.
Sequence:
MMSRPDDDKLFLSIEISTQQTKVIVINNGWRVVYEDAVTFETDLPQYKTKSGVTYHEDGKTVTAPVLMWIEAVDLILERMKENSVDFSKIVAVSGAAQQHGSVYWRYGSEGLLTNLDSNLPMHKQLKDAFTILDSPIWMDASTEEECREIEEKMGGGEKLSLITGCRAFHRITANQIKKIYKHHHQEYLQTEVISLVSSFACSLMLRRYASIDLPDGSAMNLLHLKERTWSERCLQAYGMDGLAMKLRPLVPCGKCLGNISPYLVVRYGFNPRCKVKAFTGDNPASMIGMKACTRDAVISLGTSDTLSFSMDEYNSKPCLGGLVMINPLNPNIYMIMLCFKNGSLTRSKVKDNCGLGSWREFDEALERGVPGNHGHIGIYYDLPEIHPPVHGVMRLGPTNLVMTSFEPEIEIRALVEGQVAVKKLHALKMGINLDGVERILATGGASASKPTLQIIADVFDKPVVTKDIKNSACLGGAYLAKFGFKDPDNDDGGAAGDDDEDGGGGSGGGCFGNNDDDGDDDDDCLNTIFPNKDAVKVSYCFIIVNIIIIIIIIIIFVVFVIIIVVVVVVVVVVVVVVVVVT