lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Co-chaperone that binds to the molecular chaperone HSP82 and stimulates its ATPase activity. Binding to HSP82 promotes a conformational switch in the catalytic loop of HSP82, facilitating the interaction of the catalytic 'Arg-380' with ATP in the N-terminal nucleotide-binding domain. Although not essential, it confers thermotolerance when intracellular levels of HSP82 are limiting.
Miscellaneous:
MISCELLANEOUS: Present with 13939 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm.
Sequence:
MVVNNPNNWHWVDKNCIGWAKEYFKQKLVGVEAGSVKDKKYAKIKSVSSIEGDCEVNQRKGKVISLFDLKITVLIEGHVDSKDGSALPFEGSINVPEVAFDSEASSYQFDISIFKETSELSEAKPLIRSELLPKLRQIFQQFGKDLLATHGNDIQVPESQVKSNYTRGNQKSSFTEIKDSASKPKKNALPSSTSTSAPVSSTNKVPQNGSGNSTSIYLEPTFNVPSSELYETFLDKQRILAWTRSAQFFNSGPKLETKEKFELFGGNVISELVSCEKDKKLVFHWKLKDWSAPFNSTIEMTFHESQEFHETKLQVKWTGIPVGEEDRVRANFEEYYVRSIKLTFGFGAVL
The following text describes a protein:
Function:
Microtubule inner protein involved in the attachment of outer dynein arms (ODAs) to dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, flagellum axoneme.
Sequence:
MTDRNRDKKSTSPSNSDTEMKSEQLPPCVNPGNPVFSCMLDPKTLQTATSLSKPQMIMYKTNSSHYGEFLPIPQFFPCNYTPKEQVFSSHIRATGFYQNNTLNTAPDRTRTLDFPNIQHTL
The following text describes a protein:
Function:
Subunit of STT3A-containing oligosaccharyl transferase (OST-A) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). Within the OST-A complex, acts as an adapter that anchors the OST-A complex to the Sec61 complex. May be involved in N-glycosylation of APP (amyloid-beta precursor protein). Can modulate gamma-secretase cleavage of APP by enhancing endoprotelysis of PSEN1.
Subcellular Localization:
Endoplasmic reticulum. Membrane; Multi-pass membrane protein.
Sequence:
MFGFAGVVLSPVEAQKVVRYLAQVGRETPAATNMETLYRVPFLVLECPNLKLKKPPWVHMPSAMTVYALVVVSYFLITGGIIYDVIVEPPSVGSMTDEHGHQRPVAFLAYRVNGQYIMEGLASSFLFTMGGLGFIILDRSNAPNIPKLNRFLLFIGFVCVLLSFFMARVFMRMKLPGYLMG
The following text describes a protein:
Function:
Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate.
Miscellaneous:
MISCELLANEOUS: In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes.
Subcellular Localization:
Cytoplasm.
Sequence:
MTGSIRSKLSAIDVRQLGTVDYRTAWQLQRELADARVAGGADTLLLLEHPAVYTAGRRTETHERPIDGTPVVDTDRGGKITWHGPGQLVGYPIIGLAEPLDVVNYVRRLEESLIQVCADLGLHAGRVDGRSGVWLPGRPARKVAAIGVRVSRATTLHGFALNCDCDLAAFTAIVPCGISDAAVTSLSAELGRTVTVDEVRATVAAAVCAALDGVLPVGDRVPSHAVPSPL
The following text describes a protein:
Function:
Forms a fork protection complex (FPC) with TOF1 and which is required for chromosome segregation during meiosis and DNA damage repair. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors (By similarity).
Subcellular Localization:
Nucleus.
Sequence:
MDNDYESPWGLSQLEAPADSQNIDSQPLNDDELGINTEVQVKRTRHVAKLDDTRMMDDKGLPALKHLCTKVNLKGNGHEVGDLGRLLDMYQMWSHDLFPKGQFKSLYPLTSKAGRTATVRGLRLAWIDEEQRKKQTADVATAVDELEDITDFRDRGRHFETEPRYSRQSEPPVETSVNVDNPDDLFVGMDSVDHRLVSDEDVDIQAEVSRREDDEDREQDVSELLEGARAQRDKDNSRSSGRLSLFDLGGSGSPSESDRGGSTLEGDIFGTGSLDPTPPPASETSTQAPAAQPPATQPPQAPAPTQPPSNQAPVKAPPQPMRQMDDLELDMLADFEPDFEDQEQHEPEPDPEDYEDDEAMAVMREMGL
The following text describes a protein:
Function:
Forms a fork protection complex (FPC) with swi3. FPC coordinates leading and lagging strand synthesis and moves with the replication fork. It is required for programmed fork-pausing which is necessary for mating-type switching. FPC stabilizes replication forks in a configuration that is recognized by replication checkpoint sensors. It is involved in termination at the mat1-proximal polar-terminator of replication (RTS1) and also required for activation of the Rad53-like checkpoint kinase cds1.
Subcellular Localization:
Nucleus. Note=Associated with chromatin during S phase. Nuclear accumulation requires swi3.
Sequence:
MELDEVIQGIVSAIGGFDYSDDEKVYVLGDEALACLKDLKRYLQVVDEKYKVWQIRSLLSSLQLVTNDICPILSDWDKDITNYRNWRIALACVELLVPLTWPLETEHETFRENVDVLYNLRQAQSNYKNSILSYKKGSVLSAILAVLLKPLSTPAESRTLRDKGIIRIVLLLFRNILQIDELKTKNETIISFAKAHILDLIVTLVSNLDEFEHFDVYILEIVYNLIRGCKPSALFSDASLTNSQTELNSLLLKESTQNRYLKRNAHTRHNRFGTMLSVQTEDRRFTIASQNIKTDGLDELDSHKRFRKRGTRRKHFDDINKSFFINTEAGTALRNFAVEFLEAGFNPLFQSLLKDLEREDPRVLPIHKMQLLYVQSFFLEFMRFSSKPKKTEEIYSNDYSFGLAASVFDQRALIMHNRLMVESFEMKQWSTFQASMLSMTQLLFTLRSMTLCSSEIYQRIADNLLSNIFYQEEILLLVYSALKHFKTQSFGYLDAITELTIVLLKELEKFSSAKQYLYVKKRRRNQKSVDSNVLESDEDEESSLINANAAVEDRLFDFGRYESRYCDNGCIDSFVLFLQCYQDLDSKQIHRAISFFYRIFVKQKCHVYLYRLDFLRVLDKMFNDHVYFSTTNSARQDFEQFFVYYMRKLSDALKDVPALFIELPFPKLTDTFYYLEYGKSPLFSIHGSRKGPLYETVPGLSHLEKVAAVVACLINENKSDLLDELKVQLNCLISERKLITLADENKYINEGGNDGERMGKNLKGDTDSFNTALLKDGKFRLLLELCGFEESDNNIDVQALWKLPNSVIIDELVEHAMLLRRFTDDPPTFEGTKPEDLLVRKQRGNVRLPSSSEGETSDEEIEFEADDPITFANRREALNKITDRKRKKMKTNETIIDHTTRKKKENHLRSAKYIVDSDDDSETDIAFFQSEAALREKNAQKASALFKRIDDLEMEGKLQEIEQLSENSSSD
The following text describes a protein:
Function:
Autophagy factor required for autophagosome formation.
Subcellular Localization:
Cytoplasm. Preautophagosomal structure. Note=Under starvation conditions, it is localized to puncate structures primarily representing the isolation membrane; the isolation membrane sequesters a portion of the cytoplasm resulting in autophagosome formation.
Sequence:
MNCRSEILEVSVEGRQVEEAMLAVLHTILLHRSTGKFHYKKEGTYSIGTVGTQDIDCDFIEFTYVRVSSEELDRALHKAVSEFKDALRNSGSDGIGQVSLEFYQKKKSRWPFSDECIPWEVWTIKVNVVSLANEQERQICREKVGEKLGEKIINIVEVMNRHEYLPKMPTQSEVDNVFDTSLKDVQPYLYKISYQITDSLGTSVTTTMRRLIKDTLAL
The following text describes a protein:
Function:
Required for nuclear membrane fusion during karyogamy.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus membrane; Multi-pass membrane protein.
Sequence:
MNIVLLIYCLAMVVAHDLQLFGDFKFELSDNWRNDCAKKALEPIINQCAEGIETISPFQQKSIAIQLSICEFENAEISYPSECRSQNLDTCILLLEKSPQYWTTFSGYYREIRNICHQVSLPFAKDQILQVYGNITEFYRTLMDEMTNSSKYTENMQNELKAKFDKLIGVIDLILADREKNREDLKSSFNMFKNNFEKSLNNALVVMKHSYEDANSNVKELESHLNYFINDMSQVYILINEKALEVKSQQDRIKEHNADILNQIEEIKKNLDNAYEEASEVQISNNQLVHDIQSSLDYSLFTVSNLNSHLQLSINDFIEKNEDIRSRAPIIFEEIFGLFLNHLNESGQLAMDSFEAALDLSLNMLHQKLNQTERSIDNLNSKVSDLAHFADSLKKYASSIFNVPNYVRTSMNHKIQQWREFGNIMVVGGVFFFVVLTLLVLSFIRTQVMKVFRFAFIGIPMITGIALAIFILRLLSMPMKVVDID
The following text describes a protein:
Function:
Catalyzes the adenosylmethionine-dependent methylation of the exocyclic amino group (N(2)) of guanosine at position 10 of various tRNAs. Acts via a two-step process that leads to the formation of either N(2)-monomethyl (m(2)G) or N(2)-dimethylguanosine (m(2)(2)G).
Subcellular Localization:
Cytoplasm.
Sequence:
MFYYVEILGTLPEMGKAEVEALAELGVGNVEKVDYLLVSGSVKHIGVFERLGLAHEYGLLLYEGDDIKDILDFAKGLEWRNIINGTFAVRRERMRNCMHEVNDLDKKIGGIIHSQGLRVNLSRPDTVVRVYCGNKIWLGIRIREFKGKEFEDRKADRRPFSRPIALPPRIARAMVNLTKATREVLDPFMGTGGMLIEAGLIGLKVYGLDIREDMVEGAKINLEYYGIRDYVVKVGDATKIEEVFPGKTFEAVATDPPYGNSTTLPMDRNELYKRSLESIHSVLEGRLAIAFPADFDARDVAESIGFKVLGRFYQRVHSSLSRYFYVMEV
The following text describes a protein:
Function:
GTPase activating protein. May play a role in clathrin-dependent retrograde transport from early endosomes to the trans-Golgi network (By similarity).
Sequence:
MTGKSVRDVERYQAVLGSLLSEEENKYCADCQAKGPRWASWNIGVFICIRCAGIHRNLGVHISRVKSVNLDQWTQEQIQCMQEMGNGKANRLYEAFLPENFRRPQTDQAVEGFIRDKYEKKKYMDRSIDINTFRKEKDDKWKKSNEPVSERKLEPIVFEKVKMPQKKEETQQSRKSSPKSTEPVIDLLGLDAPVPSTLTNGRPCSLEKDLDLFASVGLNSDSRKVSGSMPTSGSAGSVPENLNLFPEPGGKGEEAGKKQLSKDSILSLYGSQTPQLPAQGAMFMAPAQMAYPAAAYTSFPGVPPSSSMMGGMMAPSVGVMAQHGAAGMVTPMAIPAGYVGNVQAAVIGVPNGMMAAQQAGYVAGMAAVPQPVYGVQPAQQLQWNITQMTQQMAGMNFYGANGVMGYGQSMGGGGAQGSNQSLSTQLWK
The following text describes a protein:
Function:
Probably involved in the regulation of chromatin states (Probable). Contributes to RPP7-mediated and basal immunity, especially against Hyaloperonospora arabidopsidis isolate Hiks1. Regulates negatively EDM2-dependent floral transition.
Subcellular Localization:
Nucleus.
Sequence:
MEAQIHILEQEAYSAVLRAFQAQADEFSWDKATVMTNLRKELRISDDENRQLLNNVHNDDLIKRIRDSRPRGGNQVVRHQSLDVHPSPTFSASRKKQKTFQSYPSIGSTRSKSFNNRVVSANEPAEALIGRKVWTKWPEDNSFYEAVVTQYNANEGRHALVYDINTVNETWEWVDLNEIPTKDIRWDGEEDGVTLNVGHGGGTTRGNRRTLSHGGRGRGPRTQPRREHLATENGGGRKFFGEIELFNTDSLVKEVERVFDSNLPDPHELDKAKKLLKEHEQALIAAIARLTDASDYESDGEEPYSHELPMLLG
The following text describes a protein:
Function:
May be involved in the mitochondrial lipid metabolism.
Subcellular Localization:
Cytoplasm.
Sequence:
MENSNKISLHPEQKKWKAPKGPKPIHHKNKNLIGLGRTIANQRSKENSIQYLPDGEMRFTTDKKEANWVKLRSVTQENALDEFLSTAELADTDFTADKNQQVKIIKVGNTSIVNSNGLLSTDEMLAMRQKHMMFENKLTIPKRPKWNKNQSKIEIDRQENLAFLSWRRELAQLTENNDLLLTPFERNLEVWKQLWRVVERCDLIVQIVDARNPLFFRSIDLDKYVTSLSDPDNNKAKNNLLLVNKADMLTRDQRIAWAEYFKLKKINYVFFSAAKANELLEKEREELENIQNSTGSSSSSSRNTNNNAAAAAVDAEQEEGEANDSIRILKIEELEKLFMDSAPKFEVDPEFPDRKLQIGLVGYPNVGKSSTINALVGSKKVSVSSTPGKTKHFQTIHLSPDVLLCDCPGLVFPNFAYTNAELVCNGVLPIDQLREHIPPVSLVCQRIPKFFLEAVYGIHIPIQKVEDGGNGEYPTARELLNAYARARGYMTQGFGSADEPRAARYILKDYVNGKLLYVNPPPKEATNKNEWILPNLQESRIFNRELYTLNHLPESRQHQIVSAMQHKHIPVDEFNLEKDLTKLNFSQHIAAITGSGDSKDEDNKLRDNNQSQSEAKTLFYGGKQAALESAGDELDREFFAMNNISGKFATPFHKKNNSNTEKNSNKKHNKKNKKQDKKVRVVGY
The following text describes a protein:
Function:
Component of the high affinity leucine, isoleucine, valine, transport system (LIV-I), which is operative without Na(+) and is specific for alanine and threonine, in addition to branched-chain amino acids.
Subcellular Localization:
Cell inner membrane; Multi-pass membrane protein.
Sequence:
MPEIYHYLQQLVNGLTVGSTYALIAIGYTMVYGIIGMINFAHGEVYMIGSYIAFIAITLLAMMGLDSVPLMMLAAFAASIIVTSAFGYSIERVAYRPLRGGNRLIPLISAIGMSIFLQNAVMLSQDSKEKAIPTLLPGNFVFGESSMNGVVISYMQILIFVVTFLVMFGLTLFISRSRLGRACRACAEDLKMTNLLGINSNNIIALTFVIGAALAAVAAVLLGMQYGVINPGIGFLAGIKAFTAAVLGGIGSIPGAMLGGLLLGVAEAFGADVFGDQYKDVVAFGLLILVLLFRPTGILGRPEVEKV
The following text describes a protein:
Function:
Has an integral role during the infection of macrophages in the mammalian host.
Subcellular Localization:
Membrane.
Sequence:
MLTTHFRCCISPRVSGAYSLFPLFLPCIKRKRLMMLPACVIPMHGALKLAILLMLVWCCSLCLAKSGDRCMFDEIAAKAGRPRVLALRRTKAGMENVKYDRTGSVDPEWQHIRIVVFAEDMKDRSRYCTSAGQERPTFFGETATCSQEDILTAAKRDIAVTKLLPSAVQMHMDRLLVDPITEPLVFPPFDGSVCSEFKVPSSHFSEGVPDADMVMYAAAGPTPEGVAAWATGCITLDDGRAVAGVTNLGPGSISLSETSIRTAAHEIAHILGFNFRAMNDAGMVQRIPGVRGKVDVTLISSPRTLQKAREHYNCPDAPGMELEDEGGSGTALSHWERRNAKDEIMSGISSPGRYTALTMAAFEDLGYYRGAWGSEEPMGWGNNSGCELLNESCLVNGVTAHPDMFCNETVSKLVCNSERDGLGRCNVIKHENPLPPQYHYFSDPSRGAPSHLLMDYCPSIDAFSNTPCADGETKFMRGSLIGPSSMCLKAEGLRDSQGVIGDVCADVRCDGGEVSIRYLGDDAWHPCPEGSHIKPTTTFTDGVIVCPTYSEVCIKATVVVRPSSASYRSSVPQSLLLTLFAIVYAAC
The following text describes a protein:
Function:
This virulence factor of S.pyogenes specifically cleaves the human serum chemotaxin C5a at '68-Lys-|-Asp-69' bond near its C-terminus, destroying its ability to serve as a chemoattractant.
Subcellular Localization:
Secreted, cell wall; Peptidoglycan-anchor.
Sequence:
MRKKQKLPFDKLAIALMSTSILLNAQSDIKANTVTEDTPVTEQAVETPQPTAVSEEVPSSKETKTPQTPDDAEETIADDANDLAPQAPAKTADTPATSKATIRDLNDPSQVKTLQEKAGKGAGTVVAVIDAGFDKNHEAWRLTDKTKARYQSKEDLEKAKKEHGITYGEWVNDKVAYYHDYSKDGKTAVDQEHGTHVSGILSGNAPSETKEPYRLEGAMPEAQLLLMRVEIVNGLADYARNYAQAIRDAVNLGAKVINMSFGNAALAYANLPDETKKAFDYAKSKGVSIVTSAGNDSSFGGKTRLPLADHPDYGVVGTPAAADSTLTVASYSPDKQLTETAMVKTDDQQDKEMPVLSTNRFEPNKAYDYAYANRGMKEDDFKDVKGKIALIERGDIDFKDKVANAKKAGAVGVLIYDNQDKGFPIELPNVDQMPAAFISRKDGLLLKDNPQKTITFNATPKVLPTASGTKLSRFSSWGLTADGNIKPDIAAPGQDILSSVANNKYAKLSGTSMSAPLVAGIMGLLQKQYETQYPDMTPSERLDLAKKVLMSSATALYDEDEKAYFSPRQQGAGAVDAKKASAATMYVTDKDNTSSKVHLNNVSDKFEVTVTVHNKSDKPQELYYQATVQTDKVDGKHFALAPKVLYEASWQKITIPANSSKQVTVPIDASRFSKDLLAQMKNGYFLEGFVRFKQDPTKEELMSIPYIGFRGDFGNLSAVEKPIYDSKDGSSYYHEANSDAKDQLDGDGLQFYALKNNFTALTTESNPWTIIKAVKEGVENIEDIESSEITETIFAGTFAKQDDDSHYYIHRHANGEPYAAISPNGDGNRDYVQFQGTFLRNAKNLVAEVLDKEGNVVWTSEVTEQVVKNYNNDLASTLGSTRFEKTRWDGKDKDGKVVANGTYTYRVRYTPISSGAKEQHTDFDVIVDNTTPEVATSATFSTEDRRLTLASKPKTSQPVYRERIAYTYMDEDLPTTEYISPNEDGTFTLPEEAETMEGATVPLKMSDFTYVVEDMAGNITYTPVTKLLEGHSNKPEQDGSGQTPDKKPEAKPEQDGSDQAPDKKPEAKPEQDGSGQTPDKKPETKPEKDSSGQTPGKTPQKGQPSRTLEKRSSKRALATKASTRDQLPTTNDKDTNRLHLLKLVMTTFFFGLVAHIFKTKRQKETKK
The following text describes a protein:
Function:
Histone demethylase that specifically demethylates 'Lys-4' of histone H3, a specific tag for epigenetic transcriptional activation, thereby acting as a corepressor. Acts by oxidizing the substrate by FAD to generate the corresponding imine that is subsequently hydrolyzed. Demethylates both mono- and di-methylated 'Lys-4' of histone H3 (By similarity). May be involved in H3 demethylation in mitotic cells including gut and embryonic cells. Participates in the transcriptional repression of the presenilin protein hop-1. May act via the formation of a multiprotein complex that remodel or modify the chromatin. Together with met-2, set-17 and set-26, required for transgenerational fertility. Plays a role in developmental growth and lifespan regulation in response to ultraviolet-induced damage.
Subcellular Localization:
Nucleus.
Sequence:
MSSDTGSEYLDEEIRGDELGPSIDDNALAAAASAARLPFDRPTDHELAFFPELWEHKTAVEVFLLLRNSTLATWQYNPLKECTALDVRNNVFPPFNSDLDLIQNIVHYLSRHGLINFGRYVRSTKISRFLVRDRRSVIVIGAGAAGISAATQLESFGFDVIVLEARNCIGGRIHSFKSKSGEIMETGGDTLRKIEDSPMATLLHQVNFEEHGVFDFTSVFVEGRPLNEEKIHLFLDHYKSAHGALNYQAHQCEHRDDQGSFISRQQAYENLLSMCERGTLIKYYNFCKSLETVARAREHHFNQMKQLRMTALMAENQLKKMEEEGNLEQDPVLRRSLKRDIATSLEKFEEVADAFETADNHWQRLNEHPQAKQYMHPGSEFATFNFMLGFEEYLVGAQLEKVQFSCDSMQNKENGVAARLTEGIAELLTQLSEKRKLDIRLKHRVLDIDYSGFEHVLLKVQRENGDIEEMKAAFVVSTLPIGVLKKTIIADERAPTFTPSLPDKKVEAIRNIGCGSVNKCILEFDRVFWTANGGRNQFVTVSPNIKTRGSMNIWSSVPGSKVLCTYIVGEEAMLELPDDVIIQNAMINLQKAFGNNCPRAPISAHITRWHDDELAFGSGAFMSLRTETTSFDDVMEPLKTSDGMSRVYFAGEHTCSSYTSTIQGAWMSGARAAADISNDHIGIGFVDISGTRGQRGDEEEELLIEVDIDGKIPEKDENEAVADIPNAPNAPNAQKPEEIPKIAEEIELVAEAEKAEKAEVQLEPLVPTVE
The following text describes a protein:
Function:
The central subunit of the protein translocation channel SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug. The plug probably moves laterally to allow the channel to open. The ring and the pore may move independently.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MQTVSSPKQKLNFGQRLLTLLQNRDFMVSLVLTVVLLILFRVLAIIPLPGIRINESVLDRNSNDFFSLFNLLGGGGLNQLSLFAVGISPYISAQIIMQLLSTDLIPPLSKLVNSGEVGRRKIEMITRIITLPFALVQAFAVIQIATNAGTGSSPISLANSGSEFIAFYIIAMTAGTYMAVFLGDTISKKGVGNGITLLILSGILSQLPQGFIAAYNVLSGIVITLTPQLTAAISFFIYFLAFLVLLFATTFITQATRKIPIQQSGQGLVSEVKTLPYLPIKVNAAGVIPVIFASSIMSIPVTIAQFQPQTESRWFVEDYLSLSTPVGIFLYAVLVILFSFFYSYIQINPERLAKNFEKSGRFIPGIRPGNDTEKHIARVLIRINFIGAPFLTVIAIIPYIVSYFIRLPNSLSLGGTGIIIIVTAVVEFISALRSAATATNYQQLRRNLAIEVQQTAKQDSLEQLQKEAPGIGNLW
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase which accepts ubiquitin specifically from endoplasmic reticulum-associated UBC6 and UBC7 E2 ligases, and transfers it to substrates promoting their degradation. Mediates the degradation of a broad range of substrates, including endoplasmic reticulum membrane proteins (ERQC), soluble nuclear proteins and soluble cytoplasmic proteins (CytoQC). Component of the DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded cytoplasmic domains. ERAD-C substrates are ubiquitinated through DOA10 in conjunction with the E2 ubiquitin-conjugating enzymes UBC6 and UBC7-CUE1. Ubiquitinated substrates are then removed to the cytosol via the action of the UFD1-NPL4-CDC48/p97 (UNC) AAA ATPase complex and targeted to the proteasome. Also recognizes the N-terminally acetylated residue of proteins as degradation signal (degron). N-terminally acetylated target proteins include MATALPHA2, TBF1, SLK19, YMR090W, HIS3, HSP104, UBP6 and ARO8. Catalyzes ubiquitination of mislocalized tail-anchored proteins that are extracted from the mitochondrion membrane by MSP1: following extraction, mistargeted proteins are transferred to the endoplasmic reticulum, where they are ubiquitinated by DOA10 and degraded by the proteasome.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein. Nucleus inner membrane; Multi-pass membrane protein.
Domain:
The RING-CH-type zinc finger domain is required for E3 ligase activity.
Sequence:
MDVDSDVNVSRLRDELHKVANEETDTATFNDDAPSGATCRICRGEATEDNPLFHPCKCRGSIKYMHESCLLEWVASKNIDISKPGADVKCDICHYPIQFKTIYAENMPEKIPFSLLLSKSILTFFEKARLALTIGLAAVLYIIGVPLVWNMFGKLYTMMLDGSSPYPGDFLKSLIYGYDQSATPELTTRAIFYQLLQNHSFTSLQFIMIVILHIALYFQYDMIVREDVFSKMVFHKIGPRLSPKDLKSRLKERFPMMDDRMVEYLAREMRAHDENRQEQGHDRLNMPAAAADNNNNVINPRNDNVPPQDPNDHRNFENLRHVDELDHDEATEEHENNDSDNSLPSGDDSSRILPGSSSDNEEDEEAEGQQQQQQPEEEADYRDHIEPNPIDMWANRRAQNEFDDLIAAQQNAINRPNAPVFIPPPAQNRAGNVDQDEQDFGAAVGVPPAQANPDDQGQGPLVINLKLKLLNVIAYFIIAVVFTAIYLAISYLFPTFIGFGLLKIYFGIFKVILRGLCHLYYLSGAHIAYNGLTKLVPKVDVAMSWISDHLIHDIIYLYNGYTENTMKHSIFIRALPALTTYLTSVSIVCASSNLVSRGYGRENGMSNPTRRLIFQILFALKCTFKVFTLFFIELAGFPILAGVMLDFSLFCPILASNSRMLWVPSICAIWPPFSLFVYWTIGTLYMYWFAKYIGMIRKNIIRPGVLFFIRSPEDPNIKILHDSLIHPMSIQLSRLCLSMFIYAIFIVLGFGFHTRIFFPFMLKSNLLSVPEAYKPTSIISWKFNTILLTLYFTKRILESSSYVKPLLERYWKTIFKLCSRKLRLSSFILGKDTPTERGHIVYRNLFYKYIAAKNAEWSNQELFTKPKTLEQAEELFGQVRDVHAYFVPDGVLMRVPSSDIVSRNYVQTMFVPVTKDDKLLKPLDLERIKERNKRAAGEFGYLDEQNTEYDQYYIVYVPPDFRLRYMTLLGLVWLFASILMLGVTFISQALINFVCSFGFLPVVKLLLGERNKVYVAWKELSDISYSYLNIYYVCVGSVCLSKIAKDILHFTEGQNTLDEHAVDENEVEEVEHDIPERDINNAPVNNINNVEEGQGIFMAIFNSIFDSMLVKYNLMVFIAIMIAVIRTMVSWVVLTDGILACYNYLTIRVFGNSSYTIGNSKWFKYDESLLFVVWIISSMVNFGTGYKSLKLFFRNRNTSKLNFLKTMALELFKQGFLHMVIYVLPIIILSLVFLRDVSTKQIIDISHGSRSFTLSLNESFPTWTRMQDIYFGLLIALESFTFFFQATVLFIQWFKSTVQNVKDEVYTKGRALENLPDES
The following text describes a protein:
Function:
Most abundant structural protein of the nucleocapsid produced during the infection cycle. The monomers are arranged in stacked rings around the nucleoprotein core.
Miscellaneous:
MISCELLANEOUS: Expressed late in infection.
Subcellular Localization:
Virion.
Sequence:
MALVPVGMAPRQMRVNRCIFASIVSFDACITYKSPCSPDAYHDDGWFICNNHLIKRFKMSKMVLPIFDEDDNQFKMTIARHLVGNKERGIKRILIPSATNYQDVFNLNSMMQAEQLIFHLIYNNENAVNTICDNLKYTEGFTSNTQRVIHSVYATTKSILDTTNPNTFCSRVSRDELRFFDVTNARALRGGAGDQLFNNYSGFLQNLIRRAVAPEYLQIDTEELRFRNCATCIIDETGLVASVPDGPELYNPIRSSDIMRSQPNRLQIRNVLKFEGDTRELDRTLSGYEEYPTYVPLFLGYQIINSENNFLRNDFIPRANPNATLGGGAVAGPAPGVAGEAGGGIAV
The following text describes a protein:
Function:
May monitor slit diaphragm protein assembly, a specialized adherens junction characteristic of podocytes. In case of podocyte injury, it shuttles into the nucleus and acts as a transcription regulator. Plays a role in the regulation of cell morphology and cytoskeletal organization (By similarity). Acts as a transcriptional corepressor for snai1 and snai2/slug and plays a role in regulating neural crest development (By similarity).
Subcellular Localization:
Cell junction, adherens junction. Nucleus.
Sequence:
MDEYDEDPGRRASKLMETLSIYDVYQDGMYGEPNPDMEKTKRMNGSSSTPGNKVYSAAPVRSVNGNRASVPLDFCSPQREAVYPDPDVYCTKSEVALPCYSGASDRLRRYTHAEVQGHRYSTGCAYDGLVLGKQVAVSGARSNSLCMSSPDGRYTATSPRSSLASSHSSQDQSKHTSPRSSISSPRSSLVSPGQGEGTSVISPRSSYASTASDTSKHSSPRTSLNSYDCGSKPSSNRTSGISMGYDQRHISPRSSTTSPRSSYSDSRFTPAGGHDPESAAVHGIPMASPRSSICSQPAVAANCVVSPRSSISSHSSRSSRSSRGSMSAYPELQLPMLGPGLPEDALLQDFTEPNGLHNNRVHLQTFPVLEEPQQQNSEVNIGFNYCKAGAGGQRFKLPYQVTPSRDSGPSQAERRLEALTLELEKELEIHMKKEYFGICVKCGKGVYGASQACQAMGNLYHTNCFTCCSCGRRLRGKAFYNVNGKVYCEEDFLYSGFQQTAEKCFVCGHLIMEMILQALGRSYHPGCFRCVICKEGLDGVPFTVDVENNIYCVKDYHTVFAPKCASCNQPILPAQGSEETIRVVSMDKDYHVDCYHCEDCGLQLNDEEGHRCYPLEGHLLCHRCHLHRLKTPLAPHPPPSYPLHVTEL
The following text describes a protein:
Function:
Probably plays a role in cartilage scaffolding. May act by antagonizing TGF-beta1 (TGFB1) and IGF1 functions. Has the ability to suppress IGF1-induced proliferation and sulfated proteoglycan synthesis, and inhibits ligand-induced IGF1R autophosphorylation. May inhibit TGFB1-mediated induction of cartilage matrix genes via its interaction with TGFB1. Overexpression may lead to impair chondrocyte growth and matrix repair and indirectly promote inorganic pyrophosphate (PPi) supersaturation in aging and osteoarthritis cartilage.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix.
Sequence:
MVGTKAWVFSFLVLEVTSVLGRQTMLTQSVRRVQPGKRNPSIFSKPADILESPGEWTTWFNIDYPGGKGDYERLDAIRFYYGDRVCARPLWLEARTTDWTPAGNTGQVVHGSPREGFWCLNREQRPGQNCSNYTVRFLCPPGSLRRDTEHIWSLWSPWSKCSAACGQTGVQTRTRTCLAETVSLCSEATEEGQHCMGQDCTACDLTCPMGQVNADCDACMCQDFMLHGAVSLPGGAPASGATVYLLTKTPKLLTQTDSDGRFRIPGLCPDGKSILKITKVKFAPIVLTMPKTSLKAATINAEFVRAEIPYMVMNPETKARRAGQSVSLCCKAKGKPSPDKYFWYHNDTLLDPSHYKHESKLVLRNLQQDQAGEYFCKAQSDAGAVKSKVAQLIVIAPDETPCNPVPESYLIRLPHDCFQNATNSFYYDVGRCPVKTCAGQQDNGIRCRDAVQNCCGISKTEEREIQCSGYTLPTKVAKECSCQRCTETRSIVRGRVSAADNGEPMRFGHVYMGNSRVSMTGYKGTFTLHVPQDTERLVLTFVDRLQKFVNTTKVLPFNKKGSAVFHEIKMLRRKEPITLEAMETNIIPLGEMVGEDPMAELEIPSKSFYRQNGEPYTGKVKASVTFLDPRNISTATAAQSDLNFINDEGDTFPLRTYGMFSVDFRDEVTSEPLNAGKVKVHLDSTQVKMPEHISTVKLWSLNPDTGLWEEESDFKFENQRRNKREDRTFLVGNMEIRERRLFNLDVPESRRCFVKVRAYRSERFLPSEQIQGVVISVINLEPRTGFSSNPRAWGRFDSVITGPNGACVPAFCDDQSPDAYSAYVLASLAGEELQAVESFPKFNPNAIGVPQPYLNKLNYRRTDHEDPRVKKTAFQISMAKPRPNSAEESNGPIYAFENLRACEEAPPSAAHFRFYQIEGDRYDYNTVPFNEDDPMSWTEDYLAWWPKPMEFRACYIKVKIVGPLEVNVRSRNMGGTHRRTVGKLYGIRDVRSTRDRDQPNVSAACLEFKCSGMLYDQDRVDRTLVKVIPQGSCRRASVNPMLHEYLVNHLPLAVNNDTSEYTMLAPLDPLGHNYGIYTVTDQDPRTAKEIALGRCFDGTSDGSSRIMKSNVGVALTFNCVERQVGRQSAFQYLQSTPARSPAAGTVQGRVPLRRQQRASRSGQRQRGAVASLRFPRVAQQPLIN
The following text describes a protein:
Function:
Hydroxylates HIF-1 alpha at 'Asn-799' in the C-terminal transactivation domain (CAD). Functions as an oxygen sensor and, under normoxic conditions, the hydroxylation prevents interaction of HIF-1 with transcriptional coactivators including Cbp/p300-interacting transactivator. Involved in transcriptional repression through interaction with HIF1A, VHL and histone deacetylases. Hydroxylates specific Asn residues within ankyrin repeat domains (ARD) of NFKB1, NFKBIA, NOTCH1, ASB4, PPP1R12A and several other ARD-containing proteins. Also hydroxylates Asp and His residues within ARDs of ANK1 and TNKS2, respectively. Negatively regulates NOTCH1 activity, accelerating myogenic differentiation (By similarity). Positively regulates ASB4 activity, promoting vascular differentiation.
Subcellular Localization:
Nucleus. Cytoplasm. Cytoplasm, perinuclear region.
Sequence:
MAATAAEVAASGSGEAREEAEAPGPAWDESQLRSYSFPTRPIPRLSQSDPRAEELIENEEPVVLTDTNLVYPALKWDLEYLQENIGNGDFSVYSASTHKFLYYDEKKMGNFQNFKPRSNREEIKFHEFVEKLQAIQQRGGEERLYLQQTLNDTVGRKIVMDFLGFNWNWINKQQGKRGWGQLTSNLLLIGMEGNVTPAHYDEQQNFFAQIKGHKRCILFPPDQFECLYPYPVHHPCDRQSQVDFDNPDYERFPNFRNVVGYETVVGPGDVLYIPMYWWHHIESLLNGGITITVNFWYKGAPTPKRIEYPLKAHQKVAIMRNIEKMLGEALGNPQEVGPLLNTMIKGRYN
The following text describes a protein:
Function:
Cyclic nucleotide-regulated potassium channel activated by cAMP.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MSPPKRSAARAAAAAPTWRRPVAPTVPRRPRRLRRSKKPWRAREAVGLVPRGRGLRDPNLRDRLYELLEHDPLAYSVGSRFIQLIIGVIVLDVVAMVLASVPDLDAQFGALFSAIKVFAVIVFALEYAARLWTVAGHTQRKASALSDRLSYAFSALGIIDLMAFLPAAIVLATGRHATLAALGVLPFFKLIRYSPAMRSLLAAVHAERRALIGCIVILIGVVLTFASLLYAIERDVQPDKLGTIPQAMWWAIVTLGTVGYGDVVPVTTLGKFVSVFAIISGFAMIALPVAIISTAFAEEVKRRDFVVTWGMLARVPLFSHLSASEIADIMRLLRARTIEQGEILVRRGDAATSMYFITAGEVEIALPTQNVRLTDGTFFGEIALLHKTKRSGTVTATRKTRLLVLDAQDFHALIERMPTLAAHVHKTAKARLEETGDLAAAELAQAEREGTDR