lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia axoneme, which is required for motile cilia beating. May play an important role for the maintenance of myelin-axon integrity (By similarity). May affect intracellular Ca(2+) homeostasis.
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton, flagellum axoneme. Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, cilium axoneme.
Sequence:
MPPTRDPFQQPTLDNDDSYLGELRASKKLPYKNPTHLAQQQEPWSRLNSTPTITSMRRDAYYFDPEIPKDDLDFRLAALYNHHTGTFKNKSEILLNQKTTQDTYRTKIQFPGEFLTPPTPPITFLANIRHWINPKKESIHSIQGSIVSPHTAATNGGYSRKKDGGFFST
The following text describes a protein:
Function:
May act as a specific coactivator for the mammalian TEFs.
Subcellular Localization:
Nucleus.
Sequence:
MEEMKKTAIRLPKGKQKPIKTEWNSRCVLFTYFQGDISSVVDEHFSRALSNIKSPQELTPSSQSEGVMLKNDDSMSPNQWRYSSPWTKPQPEVPVTNRAANCNLHVPGPMAVNQFSPSLTRRASVRPGELWHFSSLASTSSLEPGYSHAFPARHLVPEPQPDGKREPLLSLLQQDRCLARPQESAARQNGNPGQIAGSTGLLFNLPPGSVHYKKLYVSRGSASTSLPNETLSELETPGKYSLTPPNHWGHPHRYLQHL
The following text describes a protein:
Function:
Terpene synthase that converts its substrate farnesyl diphosphate (FPP) into the sesquiterpene (E)-beta-farnesene as major product. Is also able to convert FPP into delta-elemene, beta-elemene, (E)-beta-caryophyllene, 9-epi-(E)-caryophyllene, and a yet unidentified sesquiterpene.
Domain:
Contains several highly conserved motifs that are important for catalytic activity including the aspartate-rich 'DDxx(x)D/E' motif and the 'NDxxSxxxD/E' motif, both of which are involved in complexing metal ions to coordinate the binding of the isoprenyl diphosphate substrate in the active site.
Sequence:
MNLTLKDFHVPNEWNVKSINDNSFIQECYQKAIEMNIYDKSDEKGKAVMYHALTVCPAFWPTVTYDQLVLSGYLMLWLILFDDDLDTVFIPDDEATEIINRTELIFLEGILPTNPTKKEEFTLFFRNQVLKMSGNRLDMFNLFLNYTIQWIHSIIPLNKTIEPHMDLFLFIRKLNVGVYPLIGLSCIFFSNDKIDQSLFLNPRWLKLCEATSIVTALYNDCVSYAKEVKGNAGVNNCLWFLQKKNNTSIQDTFKYICEKSNMYIKEFQNHEEKLLNQYNNIQPLATLLNSLKYIMNGKYYWSMNTARYASPSSPFIEIQNAVSPDNKLINNEL
The following text describes a protein:
Function:
Hydroxysteroid dehydrogenase involved in the biosynthesis of dafrachonic acids. Catalyzes the dehydrogenation of cholesterol or its derivatives and the isomerization of the double carbon bond on the sterol ring. Modifies sterols into a Delta(4)-3-keto-sterols such as cholest-4-en-3-one, precursor of Delta(4)-dafachronic acid. Contributes to the production of Delta(7)-dafachronic acid in the XXX cells. Dafachronic acids act as ligands and bind directly to the nuclear hormone receptor (NHR) daf-12 suppressing dauer formation and inducing reproductive growth. Acts in parallel to AKT-1 to promote reproductive development via DAF-16/FoxO and DAF-12.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSIKRLSMRLKKGIHRSWNRMTSLEAGLEEEKEIKIVEEPEPRPWKVLITGGAGHLAENLVAKLEEMTRDSIRPKIREMLEKEMPAVISTKVDKEVEKRLPMYIQIVLVDVLEPRGRVLKHHVAFVKCSFDDECTMKTALEQVDTVYHLAAVGMTGQYARDRKACMDINAVGTMNLLIWARNSGVQRFIYTSSVGVVFSGEPMYNATEEVGYPDDFYNYYCESKAHAERIVQKASGHRMRTTVLRFNGIYGPGEKRVTERVVKFMLTGMWIATCKPNGVEAQTQLSSVANCIQGLVKAELALRWSDTPHGQIYNIMDKTPVGTFSFWTPLNIALGFSSSMITVPATPIRLFAYLSQIIADRMRIDPIVSVLEVDLLLVNNTFNIEKAERDLGYEPSVSAIPEIIEHYLHRLPPDVVRPKGRSDFYVKVAVLVLGTILIFVAVFSFTFWMYLIFQRLSRWNPF
The following text describes a protein:
Function:
Catalyzes the conversion of caffeic acid to ferulic acid and of 5-hydroxyferulic acid to sinapic acid. The resulting products may subsequently be converted to the corresponding alcohols that are incorporated into lignins.
Sequence:
MASLLNSKNLNCENESIEKREDQETIEDDGDDDESFMYAMQIAISIALPMALQCAIDLGVFEVLQKAGKGAQLSADDIVSRLSNINNPKAFKMLDRILALLASHSLLNCSIIPHEQNHINSFKRYYSMTPVAKFFAPNSDGVSLGPLIALNTDKILLASWSKLKVAIEEGGTPFNKVHGTHLFDYPSLDLRFNQILNTAMSNHTTIVMKKVLECYKGFRDVKRLVDVGGGLGMNINMITSKYTHIQGINFDLPHVIQHAPSYPGVEHIGGDMFESVPNGDTIFMKWILHDWSQENCMKLMKNCYDAIPDDGKVIVLEALLPNMPKNEVAWKSLSQMDILMMTHCSEGKERTKQEFMDMATNAGFRGIKYECCIYNFWIMEFFNLSATAELSEASKVMNDLEVNVKELKKTKIVNGQTAKSIKRKDKIGMNKIKLFHKGKMLKADWDDMMICVPKPKVEQDLAQRIQAITEEDWFKLREEIVRSTGFKYWILRSIATSK
The following text describes a protein:
Function:
Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by positioning DNA ends into the Mre11 active site: ATP-binding induces a large structural change from an open form with accessible Mre11 nuclease sites into a closed form.
Domain:
The two conserved Cys that bind zinc constitute the zinc-hook, which separates the large intramolecular coiled coil regions. The 2 Cys residues coordinate one molecule of zinc with the help of the 2 Cys residues of the zinc-hook of another Rad50 molecule, thereby forming a V-shaped homodimer.
Sequence:
MRPERLTVRNFLGLKNVDIEFQSGITVVEGPNGAGKSSLFEAISFALFGNGIRYPNSYDYVNRNAVDGTARLVFQFERGGKRYEIIREINALQRKHNAKLSEILENGKKAAIAAKPTSVKQEVEKILGIEHRTFIRTVFLPQGEIDKLLISPPSEITEIISDVFQSKETLEKLEKLLKEKMKKLENEISSLQALYTAIWKYLEENDLEVLKSELKTVSEKKKELLKKREELQKEEEQLKRLLEKYRELVKKKERLRVLSLRRNELQKEVIYEQKVKKAKELEPLFREIYLRQREFERFSQELNSREKRYKELESEKEAISKEIPVHRERLSKLEEIGEKIKEELDLLEKVLKASRPLLEQRIRLKENLTRLEEEFRRLVGEKEKREKELLSIEKTENETKNELEKLLDELSILKKDHMKWLAYQIASSLNEGDTCPVCGGVFHGKVEAVEFNIDEFEKLDQKRSELENTLNVLKERKKSLSSLIEDLLMKIEEGKKNLKSIRNQIEKIEEELHRLGYSEDLEEKLDEKRKKLRKIEEERHSISQKITAADVQISQIENQLKEIKGEIEAKRETLKEQREEMDQLKSDFFDRLRKIGIGFEEFRILVKEEVKDAEKELGVVETEIRLLEESLKELESENVRDVSEDYEKVRNQLEALSQEISDLERKEGRLNHLIEETLRRERELKSLEKKLKEMSDEYNNLDLLRKYLFDKSNFSRYFTGRVLEAVLKRTKAYLDILTNGRFDIDFDDEKGGFIIKDWGIERPARGLSGGERALISISLAMSLAEVASGRLDAFFIDEGFSSLDTENKEKIASVLKELERLNKVIVFITHDREFSEAFDRKLRITGGVVVNE
The following text describes a protein:
Function:
Cell surface proteoglycan.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MACVGLLVTVLAASFVGGTLSQVQDDAAVVPTCREVQQAWVYKSLGPKDLVPTAPRIGHDLAVCSKGKTCCTKRMEDKYLEASKKDFQDVVQSTSAYLKYLVSQNAARFQEQFHGLIQKSENETHHLFRNVYKNMAIEANSLIEGFHRKLSFYVNGAELSVTDSVKDFFDTLFPLVYRRLLNPKMTDMSADYTNCVMDLQREVLPFGELPTKISTQLQRSLSAARVFVQALNLGVEVVNTTNHLVLTRDCTKALLKFKYCSHCQGKPLIKPCGNYCMNVMRGCLASVTDINPHWNSYIDVMQSLTKGMKGMYSVETIMATLPDKVSESIMIAMQNGPSLTAKVQKACRRPRQRNRRASQPVLTGGVRRANKPPANLYEHIQTFVRHLAMSKGFYSNLAETICNDDSLAVRPGEEETCWNGLSYGRYTIPVVDNGFQAQRFNPELRVDKEDATIVNIIDKLKHIKELIVSKMAMWVEDPDWDDSGGSGDGPFGDGEYSGDSDDEDYQDSSGSGDGETPAVTDTGSKNEEEMYFEDSTPKQKAAAPGDSRVETINDVDRQNADPNVLNTESSSTAPAATVSLVAMATFIVTAYLRHTL
The following text describes a protein:
Function:
Component of the GID E3 ligase complex recruiting N termini and catalyzing ubiquitination of proteins targeted for degradation. GID E3 is regulated through assembly with interchangeable N-degron-binding substrate receptors induced by distinct environmental perturbations. Required for the adaptation to the presence of glucose in the growth medium; mediates in association with the substrate receptor VID24/GID4 the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1), malate dehydrogenase (MDH2), and other gluconeogenic enzymes.
Subcellular Localization:
Nucleus. Cytoplasm.
Sequence:
MTVAYSLENLKKISNSLVGDQLAKVDYFLAPKCQIFQCLLSIEQSDGVELKNAKLDLLYTLLHLEPQQRDIVGTYYFDIVSAIYKSMSLASSFTKNNSSTNYKYIKLLNLCAGVYPNCGFPDLQYLQNGFIQLVNHKFLRSKCKIDEVVTIIELLKLFLLVDEKNCSDFNKSKFMEEEREVTETSHYQDFKMAESLEHIIVKISSKYLDQISLKYIVRLKVSRPASPSSVKNDPFDNKGVDCTRAIPKKINISNMYDSSLLSLALLLYLRYHYMIPGDRKLRNDATFKMFVLGLLKSNDVNIRCVALKFLLQPYFTEDKKWEDTRTLEKILPYLVKSFNYDPLPWWFDPFDMLDSLIVLYNEITPMNNPVLTTLAHTNVIFCILSRFAQCLSLPQHNEATLKTTTKFIKICASFAASDEKYRLLLLNDTLLLNHLEYGLESHITLIQDFISLKDEIKETTTESHSMCLPPIYDHDFVAAWLLLLKSFSRSVSALRTTLKRNKIAQLLLQILSKTYTLTKECYFAGQDFMKPEIMIMGITLGSICNFVVEFSNLQSFMLRNGIIDIIEKMLTDPLFNSKKAWDDNEDERRIALQGIPVHEVKANSLWVLRHLMYNCQNEEKFQLLAKIPMNLILDFINDPCWAVQAQCFQLLRNLTCNSRKIVNILLEKFKDVEYKIDPQTGNKISIGSTYLFEFLAKKMRLLNPLDTQQKKAMEGILYIIVNLAAVNENKKQLVIEQDEILNIMSEILVETTTDSSSNGNDSNLKLACLWVLNNLLWNSSVSHYTQYAIENGLEPGHSPSDSENPQSTVTIGYNESVAGGYSRGKYYDEPDGDDSSSNANDDEDDDNDEGDDEGDEFVRTPAAKGSTSNVQVTRATVERCRKLVEVGLYDLVRKNITDESLSVREKARTLLYHMDLLLKVK
The following text describes a protein:
Function:
Murein-degrading enzyme. Catalyzes the cleavage of the glycosidic bonds between N-acetylmuramic acid and N-acetylglucosamine residues in peptidoglycan. May play a role in recycling of muropeptides during cell elongation and/or cell division.
Subcellular Localization:
Cell outer membrane; Lipid-anchor; Periplasmic side.
Sequence:
MFKRRYVTLLPLFVLLAACSSKPKPTETDTTTGTPSGGFLLEPQHNVMQMGGDFANNPNAQQFIDKMVNKHGFDRQQLQEILSQAKRLDSVLRLMDNQAPTTSVKPPSGPNGAWLRYRKKFITPDNVQNGVVFWNQYEDALNRAWQVYGVPPEIIVGIIGVETRWGRVMGKTRILDALATLSFNYPRRAEYFSGELETFLLMARDEQDDPLNLKGSFAGAMGYGQFMPSSYKQYAVDFSGDGHINLWDPVDAIGSVANYFKAHGWVKGDQVAVMANGQAPGLPNGFKTKYSISQLAAAGLTPQQPLGNHQQASLLRLDVGTGYQYWYGLPNFYTITRYNHSTHYAMAVWQLGQAVALARVQ
The following text describes a protein:
Function:
Plays a role in spermatogenesis. When overexpressed, prevents nuclear localization of HIF1A (By similarity).
Subcellular Localization:
Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Note=In mature spermatozoa, localizes to the centriole and midpiece. The 27-kDa peptide associates with the fibrous sheath in mature spermatozoa and localizes to the principal piece of sperm tail, while the 55-kDa peptide localizes to the midpiece (By similarity). Detected in the cytoplasm of almost all spermatogonial cells within the seminiferous tubules (By similarity).
Sequence:
MMRSRSKSPRRPSPTARGANCDVELLKTTTRDREELKCMLEKYERHLAEIQGNVKVLKSERDKIFLLYEQAQEEITRLRREMMKSCKSPKSTTAHAILRRVETERDVAFTDLRRMTTERDSLRERLKIAQETAFNEKAHLEQRIEELECTVHNLDDERMEQMSNMTLMKETISTVEKEMKSLARKAMDTESELGRQKAENNSLRLLYENTEKDLSDTQRHLAKKKYELQLTQEKIMCLDEKIDNFTRQNIAQREEISILGGTLNDLAKEKECLQACLDKKSENIASLGESLAMKEKTISGMKNIIAEMEQASRQCTEALIVCEQDVSRMRRQLDETNDELAQIARERDILAHDNDNLQEQFAKAKQENQALSKKLNDTHNELNDIKQKVQDTNLEVNKLKNILKSEESENRQMMEQLRKANEDAENWENKARQSEADNNTLKLELITAEAEGNRLKEKVDSLNREVEQHLNAERSYKSQISTLHKSVVKMEEELQKVQFEKVSALADLSSTRELCIKLDSSKELLNRQLVAKDQEIEMRENELDSAHSEIELLRSQMANERISMQNLEALLVANRDKEYQSQIALQEKESEIQLLKEHLCLAENKMAIQSRDVAQFRNVVTQLEADLDITKRQLGTERFERERAVQELRRQNYSSNAYHMSSTMKPNTKCHSPERAHHRSPDRGLDRSLEENLCYRDF
The following text describes a protein:
Function:
Neisseria acquires iron by extracting it from serum transferrin (TF) in its human host. Acts as a TF receptor and is required for TF utilization. Binds both apo- and holo-TF, via the TF C-terminus.
Miscellaneous:
MISCELLANEOUS: Present in outer membrane vesicle formulations which are used as vaccines in human; MISCELLANEOUS: N.meningitidis cells will only bind to human TF, not bovine or porcine TF, explaining at least in part the bacteria's inability to cause infection in non-human hosts.
Subcellular Localization:
Cell outer membrane; Multi-pass membrane protein.
Domain:
The N-terminal periplasmic domain encodes a plug that inserts into the 22 beta-strand barrel, the extracellular loops extend up to 60 Angstroms away from the outer membrane. Part of the plug (the plug loop, resides 121-139) interacts with transferrin (TF), as does the L3 helix finger in extracellular loop 3 (residues 351-361). When the L3 helix finger inserts into TF it disturbs the conformation of TF and its coordination of iron 2. Electron microscopy suggests that in the TbpA-TbpB-TF complex, TF is captured directly above the loop domain of TbpA in a chamber of about 1000 Angstroms(3) formed by the 3 proteins, where interactions between the proteins serve to abstract iron 2 from TF.
Sequence:
MQQQHLFRFNILCLSLMTALPAYAENVQAGQAQEKQLDTIQVKAKKQKTRRDNEVTGLGKLVKSSDTLSKEQVLNIRDLTRYDPGIAVVEQGRGASSGYSIRGMDKNRVSLTVDGVSQIQSYTAQAALGGTRTAGSSGAINEIEYENVKAVEISKGSNSVEQGSGALAGSVAFQTKTADDVIGEGRQWGIQSKTAYSGKNRGLTQSIALAGRIGGAEALLIHTGRRAGEIRAHEDAGRGVQSFNRLVPVEDSSNYAYFIVKEECKNGSYETCKANPKKDVVGKDERQTVSTRDYTGPNRFLADPLSYESRSWLFRPGFRFENKRHYIGGILEHTQQTFDTRDMTVPAFLTKAVFDANKKQAGSLPGNGKYAGNHKYGGLFTNGENGALVGAEYGTGVFYDETHTKSRYGLEYVYTNADKDTWADYARLSYDRQGIGLDNHFQQTHCSADGSDKYCRPSADKPFSYYKSDRVIYGESHRLLQAAFKKSFDTAKIRHNLSVNLGFDRFGSNLRHQDYYYQHANRAYSSNTPPQNNGKKISPNGSETSPYWVTIGRGNVVTGQICRLGNNTYTDCTPRSINGKSYYAAVRDNVRLGRWADVGAGLRYDYRSTHSDDGSVSTGTHRTLSWNAGIVLKPTDWLDLTYRTSTGFRLPSFAEMYGWRAGVQSKAVKIDPEKSFNKEAGIVFKGDFGNLEASWFNNAYRDLIVRGYEAQIKDGKEEAKGDPAYLNAQSARITGINILGKIDWNGVWDKLPEGWYSTFAYNRVRVRDIKKRADRTDIQSHLFDAIQPSRYVVGLGYDQPEGKWGVNGMLTYSKAKEITELLGSRALLNGNSRNTKATARRTRPWYIVDVSGYYTVKKHFTLRAGVYNLLNYRYVTWENVRQTAGGAVNQHKNVGVYNRYAAPGRNYTFSLEMKF
The following text describes a protein:
Function:
Global transcriptional regulator involved in zinc homeostasis. Represses the transcription of at least 32 genes, including genes involved in zinc homeostasis, by binding to promoter sequences that contain a conserved 26 bp palindrome, in the presence of zinc.
Subcellular Localization:
Cytoplasm.
Domain:
The N-terminal domain binds DNA and the C-terminal domain is involved in metal-binding and dimerization.
Sequence:
MSAAGVRSTRQRAAISTLLETLDDFRSAQELHDELRRRGENIGLTTVYRTLQSMASSGLVDTLHTDTGESVYRRCSEHHHHHLVCRSCGSTIEVGDHEVEAWAAEVATKHGFSDVSHTIEIFGTCSDCRS
The following text describes a protein:
Function:
Is probably involved in a pathway contributing to genomic integrity.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein.
Sequence:
MRFLPLVASALLGLVSAALVAAQAHDTPELNIVTTFPNNPGSIVKNGQANTVVFSIIDAPKERKEDRLLTLQSITGAFLNPNKVDGQRGRVLRNMTTTSFKSRPLRTVFGKAPHLPFDFVPEFKPQELEVEFSLLVNDEQTGKKHRIHAYRGKVQVVEPPKNWFDLQLISVYVIGFAVIVGGAYFILSSYVFGEEKKVAGPKKFEKPDIAKPSGVQDEWIPEHHLRARKVKTSTAGALSSGDDEPSMPKKRGKPRK
The following text describes a protein:
Function:
Serine/threonine-protein kinase involved in various processes such as cell cycle regulation, gluconeogenesis and lipogenesis regulation, muscle growth and differentiation and tumor suppression. Phosphorylates HDAC4, HDAC5, PPME1, SREBF1, CRTC1/TORC1 and CRTC2/TORC2. Acts as a tumor suppressor and plays a key role in p53/TP53-dependent anoikis, a type of apoptosis triggered by cell detachment: required for phosphorylation of p53/TP53 in response to loss of adhesion and is able to suppress metastasis. Part of a sodium-sensing signaling network, probably by mediating phosphorylation of PPME1: following increases in intracellular sodium, SIK1 is activated by CaMK1 and phosphorylates PPME1 subunit of protein phosphatase 2A (PP2A), leading to dephosphorylation of sodium/potassium-transporting ATPase ATP1A1 and subsequent increase activity of ATP1A1. Acts as a regulator of muscle cells by phosphorylating and inhibiting class II histone deacetylases HDAC4 and HDAC5, leading to promote expression of MEF2 target genes in myocytes. Also required during cardiomyogenesis by regulating the exit of cardiomyoblasts from the cell cycle via down-regulation of CDKN1C/p57Kip2. Acts as a regulator of hepatic gluconeogenesis by phosphorylating and repressing the CREB-specific coactivators CRTC1/TORC1 and CRTC2/TORC2, leading to inhibit CREB activity. Also regulates hepatic lipogenesis by phosphorylating and inhibiting SREBF1. In concert with CRTC1/TORC1, regulates the light-induced entrainment of the circadian clock by attenuating PER1 induction; represses CREB-mediated transcription of PER1 by phosphorylating and deactivating CRTC1/TORC1 (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Note=Following ACTH (adrenocorticotropic hormone) treatment and subsequent phosphorylation by PKA, translocates to the cytoplasm, where it binds to YWHAZ.
Domain:
The RK-rich region determines the subcellular location.
Sequence:
MVIMSEFSAVPTGTGQGQQKPLRVGFYDVERTLGKGNFAVVKLARHRVTKTQVAIKIIDKTRLDSSNLEKIYREVQLMKLLNHPNIIKLYQVMETKDMLYIVTEFAKNGEMFDYLTSNGHLSENEARKKFWQILSAVEYCHNHHIVHRDLKTENLLLDGNMDIKLADFGFGNFYKPGEPLSTWCGSPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGSLPFDGPNLPTLRQRVLEGRFRIPFFMSQDCETLIRRMLVVDPAKRITIAQIRQHRWMQADPTLLQQDDPAFSMQGYTSNLGDYNEQVLGIMQALGIDRQRTVESLQNSSYNHFAAIYYLLLERLREHRSTQPSSRATPAPARQPQLRNSDLSSLEVPQEILPCDPFRPSLLCPQPQALAQSVLQAEIDCDLHSSLQPLFFPLDTNCSGVFRHRSISPSSLLDTAISEEARQGPSLEEEQEVQEPLPGSTGRRHTLAEVSTHFSPLNPPCIIVSSSAAVSPSEGTSSDSCLPFSASEGPAGLGGGLATPGLLGTSSPVRLASPFLGSQSATPVLQSQAGLGATVLPPVSFQEGRRASDTSLTQGLKAFRQQLRKNARTKGFLGLNKIKGLARQVCQSSIRGSRGGMSTFHTPAPSSGLQGCTASSREGRSLLEEVLHQQRLLQLQHHSAVSSDYQQAPQLSPVPYVLTPCDGLLVSGIPLLPTPLLQPGMSPVASAAQLLDAHLHISAGPVALPTGPLPQCLTRLSPSCDPAGLPQGDCEMEDLTSGQRGTFVLVQ
The following text describes a protein:
Function:
Might act as an E3 ubiquitin-protein ligase, or as part of E3 complex, which accepts ubiquitin from specific E2 ubiquitin-conjugating enzymes and then transfers it to substrates.
Sequence:
MADIISNVFNENDEFSAPILSDNECAEELQYQEVLAASLEIFNLHMSTTQIEESPESSQGFCEICMETKATNEMFKLENCSRHSFCTDCIAQYVQFMIQDHIFSVTCPGLKCCATIEPVYCKSIIPENVFEKWQGGLSESSLLECEKFYCPYKDCSELLIYDHDQGIIECICPVCHRLLCAACGVPWHTGLDCDKFQNDEKNREDDLKVEELASSSKWMKCPHCKHIVQKADGCIHITCWCGSQFCYICGETWSENHWRCQISE
The following text describes a protein:
Function:
Required for viability of cells lacking mtDNA.
Miscellaneous:
MISCELLANEOUS: Present with 4050 molecules/cell in log phase SD medium.
Subcellular Localization:
Vacuole membrane; Peripheral membrane protein.
Sequence:
MSSNYATPLDDEVFPLSFANYQFTEHVSLGEHYSLNTSEDAKYNNLNGPFVVPRDTGKFDLNTSSASDETVFSLDNPQENNYKHQAMNNVQDCRMAVAAKTTQSCDKLTDLYANAAQQNYRLWLSSF
The following text describes a protein:
Function:
Catalytic subunit of the glycosylphosphatidylinositol-mannosyltransferase I complex which catalyzes the transfer of the first mannose, via an alpha-1,4 bond from a dolichol-phosphate-mannose (Dol-P-Man) to the glucosaminyl acyl phosphatidylinositol (GlcN-(acyl)PI) intermediate to generate alpha-D-Man-(1->4)-alpha-D-GlcN-(1->6)-(1-radyl,2-acyl-sn-glycero-3-phospho)-2-acyl-inositol and participates in the sixth step of the glycosylphosphatidylinositol-anchor biosynthesis.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MGLIVYGMYQDQKFNVRYTDIDYDVYNDASRYLVNGESPYRRATYRYTPLLAEILTLDILLNEQFGKILFSIFDIIIACIQFNLLRQTNSFIMSLLYTAIWAFNPMSIVISTRGNAEAVVCLFVILTFYFLYKRKIWLCSLFFGLSIHMKIYPVLYSLPLFFCLSNFYPSKSFFTKERLIAVFGTAFVLIGLTGYYYYRYGFEFLWETYLYHGTRTDHRHNLSYYLSLSFDFPKSTIQSLISFLPQIFCLIAIGFRYCKKDIIFCCYLMTCIFVAFNKVYTMQYFIWWFVLLPFVVPKIIEGALHHIFLTIFVILQYIASYGIWLYYGYELEFKGKNSMFNIFIAGIIVFIANIILIIWHIYVYSLSDSLRKQKQVNLNEFLFI
The following text describes a protein:
Function:
Catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate and CO(2), with concomitant reduction of NADP to NADPH.
Sequence:
MQNHSNLNDIGVIGLGVMGKNLALNIADNQYRVSVFDLDPVKVNGVLQQEKQERVGQELRITGCANLSEMLASLTKPRILVLSVPAGAPVDGVCAALISAGIEADDIVIDTGNSLWTDTVEREQHYQGQFIFFSSAVSGGEVGARFGPSLMPSGDLGAWQHVAPIWKAIAAKVNPQTGLPIERFEPGNPVTEGEPCTTYIGPAGAGHYVKMVHNGIEYADMQLICEAYQLLHDGLGMSAAEVGEVFERWNQGSLNSYLMGISAEVLKQADPLTGKPLVEMILDKAGQKGTGLWTAVSSLQIGCPAPTIAEAVYARAVSTQKSLRVELSKKLAGPLSPAMDENQKANLIDALESALYCAKVCCYAQGFQLMAMTALEQKWQLDFAEIAKIWRAGCIIRATFLQSITQAYQADANLSCLLMADTFASTLSEKQTEWRIAVAAAIMQGIPVPCISSALAYYDSYRSETLPANLLQGQRDFFGAHTFERLDKPAGEKYHLDWSAQERVLIKL
The following text describes a protein:
Function:
Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.
Sequence:
MTPVKVFGPAQSTNVARVLLCLEEVGAEYEVVNVDFTVMEHKSPEHLKRNPFGQIPAFQDGDLYLFESRAIGKYILRKYKTREADLLREGNLREAAMVDVWTEVETHQYNSAISPIVYECIINPAMRGIPTNQKVVDESAEKLKKVLEVYEARLSQSTYLAGDFVSFADLNHFPYTFYFMGTPYASLFDSYPHVKAWWERLMARPSVKKLAAVMAPQGA
The following text describes a protein:
Function:
Has a role in meiosis.
Subcellular Localization:
Membrane; Single-pass membrane protein. Note=Localizes to the barrier septum and cell tip.
Sequence:
MVESSDENDQASSFASTEDLKELRFVFWFSVLIPIFFIALIIIKRYHSCTYQKNRLLRSIFCCMSIDDEEELETDMYDLPIVEPSITLPKYSASLQENERLVGIEGEREGIDVVLNFSKAGEGGVNPYPSFDTPNARILQLRQLAKLKKHGPRISYHGIGIGRCNGNRVLPPYPEPALLPEAPNTREASNNTYLYGFSNNFINISRTLNLRYPSASASISDSLPPPYQVLSVPSVTSTHAFSNNANQT
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MDLAPSLSSLRLLVSPLRLTSAFMWQIVQDQNVEQFGKLEEFVSVMTNLVPELLSRRQRATLIVGLRAKMILEMCRGELPADLHTVKSHIDQIQTTDLLKVSDTDMESLQDSVLQLVLSLLEDAMKREYFFQEVFPVEYGPDFDKALQVLVGFFLSRLEQLLPVPNFKQLSLLLSCRPGELDGYVDSVCKSHSLLSLLQSDICGTLEKNVLPSIVEDRIVSSLSLPPVGDSVLVNQQNDATLLLEEPKNLLKQTVDKETLAGDPDVRNEGSSSNSESSFRDSDGEKETNADELQECNSKEPDLLSSTNDAHTGDLIFPAAAPPQRPDSFTNSPSKGFHYAGRTVHRCQQCTKYFIYRSDLAKHQETHTKPGAHECLQCGQDFEDSTQLAAHRISSCNTRVFKCVKCRAHFRSLRTLYKHNRMHKEKTTHKCPECGRTFTSLSQLVSHRRGHRTPTIKRNYTCKQCNETFGSYRASLIHQKIHKADAARPSKSDRQPGKCRFCDLTFNIDSELRSHLKTHAEFRPYICDQCGKCFSANSSLLAHLSNHTGEKPLLCSQCGKRFYSKIQLKSHMRCHSGERPHICPYCEKQFSLSGNLKIHIRIHTGEKPYVCHQCGKGFVSAGCLQVHLRSHTGEKPYQCKICGKKFVVSSHLTAHMCFHTGERPHCCMQCGKRFIRRYDLSKHMYTHIGKRPFPCPMCPKAYTCRTHLNRHMKSHSV
The following text describes a protein:
Function:
Acts as a general chaperone in regulated exocytosis (By similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By similarity). Involved in the calcium-mediated control of a late stage of exocytosis (By similarity). May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Membrane; Lipid-anchor. Cytoplasmic vesicle, secretory vesicle, chromaffin granule membrane. Melanosome. Cell membrane. Note=The association with membranes is regulated by palmitoylation.
Sequence:
MADQRQRSLSTSGESLYHVLGLDKNATSDDIKKSYRKLALKYHPDKNPDNPEAADKFKEINNAHAILTDATKRNIYDKYGSLGLYVAEQFGEENVNTYFVLSSWWAKALFVVCGLLTCCYCCCCLCCCFNCCCGKCKPKAPEGEETEFYVSPEDLEAQLQSDEREATDTPIVIQPASATETTQLTADSHPSYHTDGFN
The following text describes a protein:
Function:
May link EHMT1 and EHMT2 histone methyltransferases to the CTBP corepressor machinery. May be involved in EHMT1-EHMT2 heterodimer formation and stabilization.
Subcellular Localization:
Nucleus.
Sequence:
MDGPLAGGLAAPDRPRGPERLPGPAPREDIEGGAEAAEGEGGIFRSTHYLPVTKEGPRDILDGRGGISDGQPHPGLSEALPRATSATHRISSCCWDGGSLDFQPGSPPPHLLGHFPGPPDGQGSWEHPLVQEAREGIPPERRFEDSVIVRTVKPHIELEGSRRFLHHQGEAKLLEKAPRGHPRFDWLQDTDEPAPPQDAGLHLDLPPQPLPLTSFRTVLVPVEDTTKTLDVTVVDTTEHLADLEELAQPSEWGLPRSASEVATQTWTVNSEASVERLQPLPSPIRTGPYLCELLEEVAKGVASPDEDEDEEPAVFPCIECSIYFKQKEHLLEHMSQHRRAPGQEPPADLAPLACGECGWAFADPSALEQHRQLHQASREKIIEEIQKLKQVPGDEGREARLQCPKCVFGTNSSKAFVQHAKLHVRELPGQPAREPFGGGSGADSPGPDATTLTYRPYRTSSGLSGCVFCGFPAPSESLLREHMRLAHAHPHWEEDAEAFEEDPASQPGTSQDAYARFPDAAEDYFGKAEALLAPTWQENPAGYDPSLAFGPGCQQLGVRDFPLSKPLLHGSDPRPPGRPAFPSPLASAPYSLQPSRNKSMVHLQGLPAQLGDRRHPWSEEEEEDIPLVSEMDFSPENGVFPPLAAPGLIPQLALDLKRTFRKALRAAEASRAQQQQLRGMVPLVLLAKLGPQVMAAATRMPPRLQPEELGLGGAHPLDFLLLDAPLGGPLGLDVLLDGDPAVALKHEERKCPYCPDRFHNGIGLANHVRGHLNRVGVSYNVRHFISAEEVKAIERRFSFQKKKKKVANFDPGTFSLMRCDFCGAGFDTRAGLSSHARAHLRDFGITNWELTVSPINILQELLATSAAERPPSPLGCEPGGSPSGFLTSRRPRLPLAVPFPPTWAEDPGPAYGDGLGSEENTMVAMDLGSPPLPKKSLPVPGPLEQVANRLSSKVAAEVPHGSKQELPDLKAQSLTTCEVCGACFETRKGLSSHARSHLRQLGVAESESSGAPIDLLYELVKQKGLPDTPLGLPPGLSKKSNSPKEVVAGAPRPGLLALAKPLDAPAVNKAIKSPPGFSTKGLAHPPSSPLLKKAPLALAGSPTPKNPEDKSPQLSLSPRPASPKAQWPQSEDEGPLNLTLDSDGGRELDCQLCGAWFETRKGLSSHARAHLRHLGVSDPDAKGSPIDVLHGLIRRDGVQIRLPPGRGTLAQLGRPPPTSAALSLLPPPPPAKKAKLKAAGTASPWGKQDLSAAAAAGIFWASDVEPSPLNLSSGPEPARDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWYVNGSPIDTLREILKRRTQSRPGGPPNPPGPSPKALAKVVGSGGPGSSLEARSPADLHLSPLAKKLPPPPGSPLGHSPTASPPPTARKMFPGLAAPSLPKKLKPEQMRVEIKREMLPGALHGEPHPSEGPWVAPREDMAPLNLSSRAEPVRDIRCEFCGEFFENRKGLSSHARSHLRQMGVTEWSVNGSPIDTLREILKKKSKPCLIKKEPPAGDLAPALAEDGPPTAAPGPVQAPLPLVPMAGRPGKPGAGPAQVPRELSLAPITGAKPTATGYLGSVAAKRPLQEDRLLPAEVKAKTYIQTELPFKAKTLHEKTSHSSTEACCELCGLYFENRKALASHARAHLRQFGVTEWCVNGSPIETLSEWIKHRPQKVGAYRSYIQGGRPFTKKFRSAGHGRDSDKRPPLGLAPGGLAVVGRSAGGEPGPEAGRAADSGERPLAASPPGTVKAEEHQRQNINKFERRQARPPDASAVRGGEEANDLQQKLEEVRQPPPRVRPVPSLVPRPPQTSLVKFVGNIYTLKCRFCEVEFQGPLSIQEEWVRHLQRHILEMNFSKADPPPEEPRAPQAQTAAAEAP
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.
Sequence:
MLEIRNLAKSFGGVKATNDVTLDFPDGSLTAVIGPNGAGKSTFFNLITGALRPDSGEVLLDGVDLAGRSPPEIVRHGIGRAFQVASIFKSLTVQETMLAAVSADQRTSAVLHKRFPLPETRDRAEHVMELLGLSGKRNRTAATLSHGDQKLLDIALALVLEPKVLLLDEPTAGMGPEERWRMIDKVRELWETQKITVVFIEHDMDIVFKIAPKIVVLCYGRILATGTPDEIRNNSAVIEAYLGTEHAGAAA