lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Prevents constitutive TNFRSF1A signaling. Negative regulator of PRKN translocation to damaged mitochondria.
Subcellular Localization:
Cytoplasm.
Sequence:
MSALRRSGYGPSDGPSYGRYYGPGGGDVPVHVPPPLYHPLRPEPPQPPVSWRGRGGAPAETTWPGEGAGGDGYYPSGGAWAEPSRAGGGHQEQPPYPGYNSNYWNSVRPRAPYPSTYPMRPELQGQSLNSYANGAYGPPYPPGPATASAASYSGAYYVPGYAQGTYSTDIPSTYRSPGNSPTPVSRWMYPQQDCPTEAPPLRGQVPGYPASQNPAMTLPHYPYGDGNRTVPQSGATGRPQDDAWASSAYGMGARYPWPSAAPSAPSGNLYMTESASPWPGNSSPQPPPSPPPQQPKDSSYSYSQSGQGMNRHSFPCSVRQYESPGAVNNDESDLLDSQVQYSAEPQLYGNTSSEHPSNQVPSNNLPEECFSSDEGTPPSIKKIIHVLEKVQYLEQEVEEFVGKKTDKAYWLLEEMLTKELLELDSVVTGGQDSVRQARKEAVCKIQAILEKLEKKGL
The following text describes a protein:
Function:
Reversibly inhibits the activity of ATP2A2 in cardiac sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates the contractility of the heart muscle in response to physiological stimuli via its effects on ATP2A2. Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in the heart muscle. The degree of ATP2A2 inhibition depends on the oligomeric state of PLN.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein. Mitochondrion membrane; Single-pass membrane protein. Sarcoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MEKVQYITRSALRRASTIEVNPQARQRLQELFVNFCLILICLLLICIIVMLL
The following text describes a protein:
Function:
Has E3 ubiquitin ligase activity, promoting ubiquitination and degradation of target proteins. Involved in activation of the JAK/STAT pathway. Catalyzes ubiquitination of methylated RBM15. Plays a role in quality control of translation of mitochondrial outer membrane-localized mRNA. As part of the PINK1-regulated signaling, upon mitochondria damage, ubiquitinates ABCE1 and thereby recruits autophagy receptors to the mitochondrial outer membrane to initiate mitophagy.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSRSPDAKEDPVECPLCMEPLEIDDINFFPCTCGYQICRFCWHRIRTDENGLCPACRKPYPEDPAVYKPLSQEELQRIKNEKKQKQNERKQKISENRKHLASVRVVQKNLVFVVGLSQRLADPEVLKRPEYFGKFGKIHKVVINNSTSYAGSQGPSASAYVTYIRSEDALRAIQCVNNVVVDGRTLKASLGTTKYCSYFLKNMQCPKPDCMYLHELGDEAASFTKEEMQAGKHQEYEQKLLQELYKLNPNFLQLSTGSVDKNKNKVTPLQRYDTPIDKPSDSLSIGNGDNSQQISNSDTPSPPPGLSKSNPVIPISSSNHSARSPFEGAVTESQSLFSDNFRHPNPIPSGLPPFPSSPQTSSDWPTAPEPQSLFTSETIPVSSSTDWQAAFGFGSSKQPEDDLGFDPFDVTRKALADLIEKELSVQDQPSLSPTSLQNSSSHTTAAKGPGSGFLHPAAATNANSLNSTFSVLPQRFPQFQQHRAVYNSFSFPGQAARYPWMAFPRNSIMHLNHTANPTSNSNFLDLNLPPQHNTGLGGIPVAGEEEVKVSTMPLSTSSHSLQQGQQPTSLHTTVA
The following text describes a protein:
Function:
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MSDSGFEDVDDFQDVPEETTSKPEPPKQESSGFEDATTEIAPAEPEKLDANALAEENKKRFVMELEFVQSLANPQYLNFLASQNYFNDPAFCRFLQYLLYWDTPKYSKYIRYPQCLFFLHQLQDPNFRTFLLNTNNIRNIDTCTYQYWAYYMRNRLDFTLPDDDKIGFVSLLPKTEKKKEHKKHKDKSKHKDKHKLKDKPANPQPAPVPPV
The following text describes a protein:
Function:
Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane.
Subcellular Localization:
Mitochondrion.
Sequence:
MSSLIALGKRQTLLSHNEFLNFKNQKGFCKRFISQLNKKSNFPALAMTVPEATKYLKSVSISVPYVGSYMLSIALKSNRRAPSARGQIAFPHPFQEPPKICVFAKGAAADEALKLGATYVGAEDLVKKIQTEPLEFSKCFAHPNSAELLPQVAKLLGSKRLMPSIKRGTISDELKPLIESALTAVDYRQNDAGSINLPVGKLGFSDKELQENIEALVSNVRFTLAKLPGKVKVTVKHVHLSASHAIAIPLQYK
The following text describes a protein:
Function:
Hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.
Sequence:
MPPQPPAPPVFYSFPDTEVLVDSLANFVVKAQRDAVDKRGKFTIALSRGSLAANLRGLVGQQNVQWDKWEVFFVDEAAVPLEDEDSNYRSNYLSFLSHVPIPREQIHTIDINQLDDLEELADQYEKQLVNHFAASNAARYPTFDLMLLGIGPDGETASLFPGHEILSEKDAWVSFIDDAPRGPARRITMTFPVLNHCYRAVFVATGKEKTEMLHTILDQPEAGLPCSRVRPASPGLVFWFADAAAASATQYPPTTFRWIDNEKEAQEAVDAAKRRAARKLAEADSEAEVLKKSV
The following text describes a protein:
Function:
Hydrogen peroxide (H2O2) sensor. Activates the expression of a regulon of H2O2-inducible genes such as katG, gor, ahpC, ahpF, oxyS (a regulatory RNA), dps, fur and grxA in response to H2O2. Represses transcription of phage Mu mom gene in a methylation-sensitive manner; MomR binds to the mom promoter when it is unmethylated but not if it is fully methylated. Binds DNA in the upstream regions of its target genes; more than one site may be present per gene. OxyR is inactivated by reduction of its essential disulfide bond by glutaredoxin (Grx1, grxA), itself positively regulated by OxyR. Also has a positive regulatory effect on the production of surface proteins that control the colony morphology and auto-aggregation ability.
Miscellaneous:
MISCELLANEOUS: Oxidized OxyR can be reduced and inactivated by glutaredoxin 1, the product of grxA, whose expression is regulated by OxyR itself; MISCELLANEOUS: Identified as a multicopy suppressor of the slow growth phenotype of an rsgA (yjeQ) deletion mutant.
Sequence:
MNIRDLEYLVALAEHRHFRRAADSCHVSQPTLSGQIRKLEDELGVMLLERTSRKVLFTQAGMLLVDQARTVLREVKVLKEMASQQGETMSGPLHIGLIPTVGPYLLPHIIPMLHQTFPKLEMYLHEAQTHQLLAQLDSGKLDCVILALVKESEAFIEVPLFDEPMLLAIYEDHPWANRECVPMADLAGEKLLMLEDGHCLRDQAMGFCFEAGADEDTHFRATSLETLRNMVAAGSGITLLPALAVPPERKRDGVVYLPCIKPEPRRTIGLVYRPGSPLRSRYEQLAEAIRARMDGHFDKVLKQAV
The following text describes a protein:
Function:
Efflux system for nickel and cobalt.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein. Endomembrane system; Multi-pass membrane protein.
Sequence:
MNNHTKRRGIALTVFLVGVNILAWIWAFCVFHHHAVMLSAAILAYSFGLRHAVDADHIAAIDTVTRKLMQQGKTPLGVGAFFSLGHSTIVVLACLAIVVTSMAFRDRIDVLHQYGSLIGTAVSAFFLLAMALLNLFILFNVWRQFRSVTRGESVRAHDEAIPGGLMTRIFQRTFRLVTSSWHMYFVGFLFGLGFDTATEVGLLGISASAANQGLSLWSMMIFPVLFTAGMALVDSLDNFVMVGAYGWAFSHPLRKLYYNMTITAASVIVALAIGGLEALGLIDDALQLSGTFWQTVSTLNDHMGNVGFWVVGAFVLFWLLSVLNYRWRGYDKITLNT
The following text describes a protein:
Function:
Functions as a two-component phosphorelay mediators between cytokinin sensor histidine kinases and response regulators (B-type ARRs). Plays an important role in propagating cytokinin signal transduction.
Subcellular Localization:
Cytoplasm, cytosol. Nucleus.
Domain:
Histidine-containing phosphotransfer domain (HPt) contains an active histidine that mediates the phosphotransfer.
Sequence:
MDGIVQLERQLVDYTASLFHEGFLDDQFNQLQQLQDESNPDFVVEVVTLFFEDADRLLNELTKALGQPSIDFKRLDAHVHQLKGSSSRAYSGGYIPICLTSLFGLSTTIKSLINEVIGKCSIGAQRIHRVCISFRNTCEEQNVEGCLKNLQQVKHEYSLVKSKLETLFRMEQQILAAGGSVSR
The following text describes a protein:
Function:
Small GTPase required for proper localization of RNA polymerase II and III (RNAPII and RNAPIII). May act at an RNAP assembly step prior to nuclear import.
Sequence:
MVLYGQIVIGAPGSGKTTYCDGMQQYLRLLGRDCWVVNLDPANEVPLKPPTQSDDIISLDSVMSELHLGPNGGLLYCMEYIEHHLGEVLKLLRERLGMSNDKNDHSSRAYLLFDLPGQIELTAHSGVVSRIAQRLVRELDLRLVCVQLVDAAVCLTDVSKFIGASLVCTASMMRLELPFVNVLSKMDLLQSSGMSMSAYLDDPEYQRAQQHTRSSTFHRKYHKLHHELCDVVEDFGLLSFLPLSIQDAESVGRVLARIDKCNGYVF
The following text describes a protein:
Function:
Involved in the regulation of cell proliferation in developing shoots and leaves. Does not possess transactivation activity.
Miscellaneous:
MISCELLANEOUS: Plants over-expressing GRF10 exhibit reduced leaf size and plant height.
Subcellular Localization:
Nucleus.
Domain:
The QLQ domain and WRC domain may be involved in protein-protein interaction and DNA-binding, respectively.
Sequence:
MTAEGEAKNPSAGGGGDNPQHQQAAPAPAPAQGEVAQEAAVQGTGQEQERDKADREVQGGAGEKDDGACRDLVLVEDPEVLAVEDPEEAAATAALQEEMKALVASIPDGAGAAFTAMQLQELEQQSRVYQYMAARVPVPTHLVFPVWKSVTGASSEGAQKYPTLMGLATLCLDFGKNPEPEPGRCRRTDGKKWRCWRNTIPNEKYCERHMHRGRKRPVQVFLEDDEPDSASGSKPAAPGKATEGAKKADDKSPSSKKLAVAAPAAVQST
The following text describes a protein:
Function:
Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm (By similarity). Binds LPS. Important for cell envelope stability and essential for growth, cell viability and ability to cause infection in different animal models.
Miscellaneous:
MISCELLANEOUS: Can complement E.coli lptA-depleted mutants. Can functionally replace E.coli-LptA in the Lpt complex to ensure cell viability, although outer membrane biogenesis and functionality appear to be partially impaired; MISCELLANEOUS: Was identified as a promising drug target.
Subcellular Localization:
Periplasm.
Domain:
Adopts the canonical beta-jellyroll structure present in E.coli Lpt proteins.
Sequence:
MRFVNTLPLIFGLTAALGSSMALALPSDREQPIRVQADSAELDDKQGVAVYRGDVVVTQGSTKLTGNTVTLKQDKNGDIEVVTSVGKPAYYEQKPAPDKDVTKAYGLTIQYFVTQNRVVLIDQAKVIQEGNTFEGEKIVYDTQRQIVNAGRATGSQVTSPRPRIDMVIQPKKKAQ
The following text describes a protein:
Function:
May be involved in the transport of sterols.
Sequence:
MDSPLPSLLAKPREQVSALVRKAKKHRHRRSNSLPAEDSHSPERIRKRKVYDPRRYYKNNTDSIEETGQPPEGFLLMWVGHWKRWRRRLCVARTPGVLLYHRNDDNRSVGTIDLQDASIIRLEKERHFMVVTKAGMRHFRTISREFRDQWVDHLLESIQQLKEIKERAARGTQKVPKLITERDIQEKTAEWQERERELTSRMLERLQGLEPEKQAFVNQIHSFQQVFLGAASSLSLSSDTAPVVSQFTDPSSFSSLDRSLKALRPENNSQSSLRSLDSQNHEPLSRGGSGSLSTSPSRGGGLGRSARFFGWAGEKASLRRSGDVSADEGDDVGGSFRDLSGSIGASSKASSSRGNGAGLAAKPAVEANGRSKTATKSPLHKDALSDSEAFSRKAPSRLSAEIHEEGAQAGPSETRPPSNAEPELERFRTAKPDALEDATTAVLVESQQAQEGASVPVGMGTGLPVGGQFTPLQRTWQRLQVSYEEILREEVIRVMELEAENVVLLKSVAQLPKMRSEVHKLRAKLGIPHKSSTEFLVHTEGEEGDLSSDEGAFSEDDGNLTAPDGEERYFEALEVLNQRDYLIRNANEDIVDGGPDDIGNEPPDDGSSDAEEEKEGPYSYVPRKRLPAARPLHRGINVWKMLKDAIGKDLTRISMPATINEPLSGLQRTAEELQYRDLLDKGNACESSVDRLLYVTAFAVTAYEGTLNRVSKPFNPLLGETFEWQSADGRTRLIAEQVVHHPPITAVHVSTTDGAYTCEGEIEISSKFWGQFLEVVPLGLVQTKFPKHGDHYVWNKVATGVHNVLIGKMWLDQHGELVVKNLSTGDTSRTKFLKPSGKEDSAISGKVYNARGELQWTLTGSFMRDMYATPEPGKPEGLVRPFQVWKANPPVEDSFSQYGMTQFAITLNEITPQLALELPPTDSRLRPDQRALEDGEHDRSNEEKARLEEKQRATRKELKAEGKEWQGRWFTQAVPGEVNVKTAKDEGQAAWVFNGEYWKARERRDWSACPDIM
The following text describes a protein:
Function:
Constitutes one of the two catalytic subunit of the tRNA-splicing endonuclease complex, a complex responsible for identification and cleavage of the splice sites in pre-tRNA. It cleaves pre-tRNA at the 5'- and 3'-splice sites to release the intron. The products are an intron and two tRNA half-molecules bearing 2',3'-cyclic phosphate and 5'-OH termini. There are no conserved sequences at the splice sites, but the intron is invariably located at the same site in the gene, placing the splice sites an invariant distance from the constant structural features of the tRNA body.
Sequence:
MAVDLEAQTPVQDSSTTGTTSQPSHDKTANGALRKPRPRRPNFNEIHAKPLPVDVYPLPAFIPHNPISIVRIAISLLSHSIFPPKSHPVVHRAYFSPQTQSIHVTDPVSIRALWEQGFWGKGSLSRSEPQWLAGEKKKRGVQAGKTSAEVTQNRREERKQFKLERARAQREAIEQQLRQEGKLDADGTIEDLVEDGQVSESPKGTLYNPDAGDVVAVGSNDITLEVERMLAEEAADGQALSLDDIKDQEHLQLTPEEAFFLTYTLGALCVVSEDGPTDSYPTWFLLRLYALHGNSPVPEQEMRQLQNVLRKYEHDNIVLSDVSNIPSVEPDSQFILRYVVFHHFRSLGWVVRPGIKFAVDYLLYLRGPAFHHAEFAIMIIPSYSHPYWTEAPEHESGIEARKKELGKKDWWWLHRVNRVQTAVFKTLVLVYVEIPPPWDKDKMEVDIGSVLKQYTVREVILKRWSPNRNRD
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 membrane; Multi-pass membrane protein.
Sequence:
MNLIAAAIAIGLGALGAGIGNGLIVSRTVEGIARQPEAGKELRTLMFMGIALVEALPIIAVVIAFLAFFG
The following text describes a protein:
Function:
Hydrolyzes the N-terminal amino acid residue from a polypeptide chain, with a preference for substrates containing multiple alanine residues.
Sequence:
MKGLERESHFTLNENAMFFECAYSCDNALFLQLDDRSFFITDSRYTQEAKESVQPKNGVLAEVVESSDLVQSAIDLIVKSSVKKLFFDPNQVNLQTYKRLNSALGDKVALEGVPSYHRQKRIIKNEHEIQLLKKSQALNVEAFENFAEYVKKIFDEKESLSERYLQHKVKDFLTREGVYDLSFEPILALNANASKPHALPSAKDFLKAEHSILLDMGIKYERYCSDRTRTAFFDPKDFVFKREQSFKDKERQKIYDIVKEAQEKAISGIRAGMTGKEADSLARGVISDYGYGQYFTHSTGHGIGLDIHELPYISSRSETILEEGMVFSVEPGIYIPGFFGVRIEDLVVIKNSRSELL
The following text describes a protein:
Function:
Has both phosphomonoesterase and phosphodiesterase activity. Cleaves a broad range of phosphate esters.
Subcellular Localization:
Cell membrane; Lipid-anchor, GPI-anchor.
Sequence:
MKPSVATLLATVSLVYAQTATEKEPSLSAIESAAASIQPYSPVSNVEGVAFNRFFQVWLENIDYEDAAADENMKWLASQGILLTNFYAVTHPSEPNYCAAVGGDTFGMDNDNFNQIPANVSTVADLLDTKNIAWGEYQEHLPYPGFQGFNYSNQETYVNDYVRKHNPLVLYDSVTKNSTRLRQIKNFTSFEDDLANKKLPQWAFITPNMTNDAHDTNITFGAKWERSWIAPLLNNSYFMNDTLILLTFDEDGTYSKSNKIFSVLLGGAIPDELKGTQDDTFYTHYSVIASVSANWGLPSLGRWDCGANILEIVANKTGYVNYDVDTTNLRLNETYPGPMSAGEYSKYSPVWPNALTRGDCSAGHGILDIVKETYANTEPTYNYSSPFPYDTASNYNTKVTATKKNVTGTHRSSSSSSPSASSNAAVSAVAPAAGVSGLLLGLALNLL
The following text describes a protein:
Function:
Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation.
Sequence:
MTQKLKAFLLLEKMSGVVESDEVQTQDLPQRGRMALPLKVQSVTVFKYVRLHCLGKGGFGKVFLGKRRSDRISVALKFVPLLRTRCCEVDGTSKPLEVVALEMVTKDPPFPGIIRMLDFYKTRGAWVIVTETPENTQDLFHYITTCKRLCEDTARDFLGQVIQALLHCHSRGVVHMDVKDENLLLDPSTHKLLLIDFGSAVFLEPDKVYDTFHGTAVYAPPERLTQGCYKALPSEVWSLGILLYDMVHGDIPFQNDEEILLGELRFKKDLSEDCVALMQWCLSRAPEERPTLKDILAHPWMSKQDSEMHQGNTESDISPSPRKVKL
The following text describes a protein:
Function:
Catalyzes the condensation of three molecules of isopentenyl diphosphate with farnesyl diphosphate (FPP) to yield (all-E)-hexaprenyl diphosphate (HexPP; C30), the precursor of the prenyl side chain of menaquinone-6. Large subunit Hexs-B catalyzes the condensation reaction and the final product chain length is cooperatively regulated by both the Hexs-A and Hexs-B subunits using the whole size of the hydrophobic cleft as a ruler.
Sequence:
MIALSYKAFLNPYIIEVEKRLYECIQSDSETINKAAHHILSSGGKRVRPMFVLLSGFLNDTQKDDLIRTAVSLELVHMASLVHDDYIDNSDMRRGNTSVHIAFDKDTAIRTGHFLLARALQNIATINNSKFHQIFSKTILEVCFGEFDQMADRFNYPVSFTAYLRRINRKTAILIEASCHLGALSSQLDEQSTYHIKQFGHCIGMSYQIIDDILDYTSDEATLGKPVGSDIRNGHITYPLMAAIANLKEQDDDKLEAVVKHLTSTSDDEVYQYIVSQVKQYGIEPAELLSRKYGDKAKYHLSQLQDSNIKDYLEEIHEKMLKRVY
The following text describes a protein:
Function:
Serine protease inhibitor. Strongly inhibits trypsin (Ki = 0.22 nM) and very weakly inhibits chymotrypsin (Ki = 1200 nM). Does not inhibit bacterial subtilisin.
Sequence:
ERPLCNECFICDRSGDPRCLCEDHVPQCHEGCHQCEKVDTRSGTTMYQCRSFEYYDCANE
The following text describes a protein:
Function:
Component of the elongator complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MKEIQIQCQQSYEISQPLAFTFDELSKVLYVIDKESNIIKYEYNNKQLSIQTTYKVGAQIQNNSKILSFQYLMENDQLIIVYRDGAIVKVYKEEAEVVGQFECGVLGAAWNPNQEQLVVVCGDGKLVSFDVQLEPTKEINIEGILDQLVSISFKNDGKFFSLNYAIQEGRVCETYDVQLEKFRSPSKSDPEGGLVQAIFEKPRNLVNTVSWQPNSQFIAGIQDKQVIFWEKNGLRHLEFNIFEDSTNIKWSPDGIILAIQQGDRITVHLRQNYKWYAKKAFKFEKLIDYTFIENNTLVVFNENSMNIFWLNYHFNNTSIGLSTDYDTLLVSDYKKGVIPPPLCHYQLKVDSQIDLVYYDQFIYIYSYDGTLSIFDNVNLLGKVKLDIDCAHKLICYSDKQQDVIFGHAVFVVHEAESDKLVDVVISPTFEIINIWRKEFSQPTQISALTKKGHQIILHSRFGEKFIYDQSLEESLSEFDLANKEQNVYDVKIQQHNEWLGCLKSNSRLTLNNHLVTNECTSFAFFDHFLAFTINTTDQFHNLYILDLNKPISIDKKSLNISNIERGAKILAVVSLDRLIVQIPRGNLETTAPRVMALHLCKQLYDNKQYKTCFEMIRKHKLDMNLMFDFSGELDVQIVEQLSEQYLQLFIQSLNNEISFELPYVLTAEQYKHQKVLIVDKTLGTSKINYVCQKLIDNMKEETHILTIVTAMLKKEPSEVEDALLKTLKLRQLEQHHEEVPPHLNPATQKPYKKHNKIKSEQVLEYICWLADANKMFEVALGTYDFDLVKQVAQFTQKDPKEYLPMLERYSQIKDPIDMKSTIHIELKNYDKAIKVLSEGNEEQKQKSIELIRKQSRFRIALEVYRNDQVMMRKVKEALGDYLNNQKQYHQASLAYESAGLYEKAVQASSEILDTKRILSFDPKEDYLLNYNQILLAAGRWKDCGQIQEYLKNHEQAIHYYCKAEEWESVAQCLRHKQINIDDHLQLAFSLKVNHLLNQQHLFIQKLERLRIVQEQKKEHGILAPSQVNADFDQMSDVSGKSGMSKSSYTMSVTTGVRKRKPKEKSFLNRNIKEGSPVEEEYLIEFLKDIQVKSADLINSIKKFQNYLIFFNQPKLSLEMSTKTKEYLNTIKPEIKSLLQQQFEEQNQQAVDLYPYKSVVPSEFNQALDDLIK
The following text describes a protein:
Function:
Component of the DASH complex that connects microtubules with kinetochores and couples microtubule depolymerisation to chromosome movement; it is involved in retrieving kinetochores to the spindle poles before their re-orientation on the spindle in early mitosis and allows microtubule depolymerization to pull chromosomes apart and resist detachment during anaphase. Kinetochores, consisting of a centromere-associated inner segment and a microtubule-contacting outer segment, play a crucial role in chromosome segregation by mediating the physical connection between centromeric DNA and microtubules. Kinetochores also serve as an input point for the spindle assembly checkpoint, which delays anaphase until all chromosomes have bioriented on the mitotic spindle.
Subcellular Localization:
Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore.
Sequence:
MDRELERLDQEITLELQKIDGNLSHCFDVITKQVIPRVVAYGQVCDAISDSCEWLGTLCKSSGVVDLKRDVLLERTPVRDSDAHGNAHGDTHGNAHGDAHGEANAERSYGDVAGGEEHNSTVQSEVSDSTMGKYREDDTREQGEDDSVQRQKKRKVSLLIQERYGSSSSVMPSPDKRVPQQSLGSSPVKEQVPLPGTVIHFSTK
The following text describes a protein:
Function:
Plays an essential role in the repair of DNA double-strand breaks by homologous recombination and in the repair of interstrand DNA cross-links (ICLs) by promoting Fancd2 monoubiquitination by Fancl and participating in recruitment to DNA repair sites.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MRSLGEKARFDELELLIQNTPIEKLKETLKSTMTRSEGITYWNYLLRGFNPESKDALAKRFECVRSFMDGLSSTELSYKQTFDLITRLSQDLATFPSEQLAWIVEHCMDGIRQGDAKCVGWKDLLPDALSLLLARPRFLLNGISIDGMEFRDTTVRSIATMQWPASILTPIADMFKTMNLSSGEIVTVLNKFSGALQELSPMELPALCFQLFSMCSTASQLIIPLLALEKYFHRNYYKRLFSDMCSNSTNLDSIDLFSDKELREAEETILHHLNYCTMYKLTEKHLAIMLRNFLHMPDVILTPFMLSAIISMTSINRDPESARISHSILLPFLRNVIKNNEEERTLADYSVWYRDTLQRKQVDLQQVLTVLIDQNKDGKDVITPGLVHLVFYLLKSQSPKMHTLAITFLTKFIRKRFIFGQGIIKLISEWMIVYQEQNQFSECLTLLSVADTYTVSECMKPIQSVLEHMQWLSGEQSMRMMNFILPLLKISNRVRDALIDVLCKAMSSSGIQKRRMAIYGFCMILKQLNNSNAVRQTSSATSFCTQHSISGYSIMTQNTLGSRSNPQRNFDMLTLEIIGMLRNCLQQQFDIRCSLYENLQRAVELNAKLVPHVLQVIDWHFRSFFDTPSAEDAGDDLDTVFRIRYDQLVSSSDDQHMEIQLKDNLGKLIQFVANCLAVFDRAPSGYDTREMNRLMSFCVDRMVANRLPLEEITPPATHLKCALVLQQLNIIEGIICHLLLKSKPQNNAVCQILPLFNQHCKLLESLKALSDASKKAHKQLKQTAKNNSTSTCNLTLNGVPVKTMCTQPDNIWDLAILDKLLHLLLDDVVAFAAPEKTVLLRSNEPLVRYVLSVTASRVESIRLEPDYKQLAYSKRTFKQLTDITKVIYERCIQRLPELWKNFDMQSAALATQCFSECLKTAHETYSKKFEDFVKSFDLASIKGSRNKEVVYTIQDVLDDFMTEYGTDDSICKNEFVSKLPVYLLESLEILLDHIDYQDRAATESYTWLLNFCSKNEILNSEMGLVHRMLFVQRQKTHLGPFFDSVARQLGHVLGVQNEDAPSESVELTLKSISTVTIESCLQHLYAAIQKQLNDVDYFVTKANNLNYKCQVVPEIDQIYWRGNLDSMDRSICTQIIHISRTLLVLTNVCIPLGSLMDGLMKLLIQHYTCLKSLTKHYISSYTSDTSIENIKSTKFELLLRAVGKQLPANIYELITYIEANTLDEEAQQHTKKRKVQAERAKVLRETRLIPKVIMVIEDFNKHIILLSKKTKSKNRLTDYLHLGTMRDFDIKSTDLRAAIERSISDGRNISTEDSNAEDRDEDEDENENVEEDDDAQSTTYPEDLEEKEDECLVIEKKEERRRRRAPSSEAEDPQPKRKRGRKAAEQLEAEDEEQVEEEQPETTLKLRRNKKVEPKTKRSVAIKKPEEQPSHESRTSKRSKGPADKQTAEPAKVDLCVPEVPAEKKKPQPSRRLGIPRTLRK
The following text describes a protein:
Function:
Involved in chromatin organization.
Subcellular Localization:
Nucleus.
Sequence:
MSSEGDSSKNLSSESNEKNEAENTDSSQDAKDAKPDAATENSVEKKEEDAKPKEAPNEASDEADKKPETDKSATDKVENAKGDTKPSEKKEEKTKAKEKDEEENSEQEDEKSEDGGDDEKDVPLLDQPLEKSGKRERKNVQRFNEEFPSETKEVVKVEIPNGSGTSLGAIPRIDASISRFKNEDMRLLHKILFKLQGKVTMIKKNIKKFNGFEFKKGSEEYSKKVASMTKCDVKQLKSICEMLDLQKTGSKDDIVERILDFLLEPKDSGKPVGGGRPKRTAAVRANNRGYSSHDNYSSDERNSGSSSASDEDFEPSDEGSDEKPTVKKRKRVDRKKIDSEDEEESDMESATSDEDSDFQEEPKSKRRKTAKANNKNKGKGTGKRGRPPTKKTTKAGKKKNKDSSEEDEEEEEESEQKEASSSSEDEPLVKKAAKSAQPPTDDEIKTYVKEILEGANLEQITMKTVCQQVYAHYPDFDLAHKKDFIKSTVKSLIST
The following text describes a protein:
Function:
Probable adapter protein and signal transducer that links members of the tumor necrosis factor receptor family to different signaling pathways by association with the receptor cytoplasmic domain and kinases.
Subcellular Localization:
Cytoplasm.
Sequence:
MSTTTTTTISTTQSNIKLKYNIEDIVVDLPSFSKKFECNVCFNYILDTKKKEARQCIEGHIVCLPCWQQSLRGRKECTQCRSPVESVSKLSRNRFMEKEFEETLVKCPYSNQKIIKEAIGTQSINNINPNLIKLDILCDSVVKFKDLDNHLGNECHHRVFKCSCNLYYRIYSSEDHNKQCLLSNVKCEHCSKQIQRRLLQDHYKNDCATHLSKNLSKLSVKCDYQGCETELPIHKISDHITSHMNHLHSTIKQLENKNKEIMEKLEDVKSACNRSILEIVFLKGSLNNVRLGYANSLSSFWAISDYKSKLREYPHRKFLDSNAFNVGPFRFNWRIYPYGCPGNPGQTSLHLTSVELQGLDVTVWFNVRIENDNYLVERCKTFCFNEVHRTENGFPRLITSKELVFECIDKDGDLQIFFDIKIEKVESNEQDPLFS
The following text describes a protein:
Function:
Ubiquitin-binding adapter that participates in inflammatory, antiviral and innate immune processes as well as selective autophagy regulation. Plays a key role in the negative regulation of NF-kappa-B and IRF3 signalings by acting as an adapter for the ubiquitin-editing enzyme A20/TNFAIP3 to bind and inactivate its substrates. Disrupts the interactions between the E3 ubiquitin ligase TRAF3 and TBK1/IKBKE to attenuate 'Lys63'-linked polyubiquitination of TBK1 and thereby IFN-beta production. Also recruits A20/TNFAIP3 to ubiquitinated signaling proteins TRAF6 and RIPK1, leading to their deubiquitination and disruption of IL-1 and TNF-induced NF-kappa-B signaling pathways. Inhibits virus-induced apoptosis by inducing the 'Lys-48'-linked polyubiquitination and degradation of MAVS via recruitment of the E3 ligase ITCH, thereby attenuating MAVS-mediated apoptosis signaling. As a macroautophagy/autophagy receptor, facilitates the xenophagic clearance of pathogenic bacteria such as Salmonella typhimurium and Mycobacterium tuberculosis. Upon NBR1 recruitment to the SQSTM1-ubiquitin condensates, acts as the major recruiter of RB1CC1 to these ubiquitin condensates to promote their autophagic degradation.
Subcellular Localization:
Cytoplasm. Mitochondrion. Preautophagosomal structure. Cytoplasmic vesicle, autophagosome.
Domain:
The C-terminal UBZ-type zinc fingers function as ubiquitin-binding domains.
Sequence:
MTSFQEVPLQTSNFAHVIFQNVAKSYLPNAHLECHYTLTPYIHPHPKDWVGIFKVGWSTARDYYTFLWSPMPEHYVEGSAVNCELAFQGYYLPNDDGEFYQFCYVTHKGEIRGASTPFQFRAASPVEELLTMEDEGNSDMLVVTTKAGLLELKIEKTMKEKEELLKLIAVLEKETTQLREQVGRMERELNHEKERGDQLQAEQKALTKVSQSLKMENEEFKKRYNDVTSKALQLEEDIVSVTHKAIEKETELDSLKDKLKKAQCEREQLECQLKTEKDEKELYKVHLKNTEIENTKLVSEVQTLKNLDGNKENMITHFKEEISRLQFSLAEKENLQRTFLLTTSSKEDTFILKEQLRKAEEQIQATRQEAVFLAKELSDAVNVRDKTMADLHTAHLENEKVKKQLTDALAELKLSAVNKDQEKTDTLEHELRREVEDLKLRLQMAADHYKEKFKECQRLQKQINKLSDQSANSNSVFTKKIGSQQKVNDASINTDPAATASTVDVKPLPSTAETDFDNLTKGQVSEMTKEIADKTEKYNKCKQLLQDEKTKCNKYADELAKMELKWKEQVKIAENIKLELAEVVDNYKLQLAEKEKEISGLTSYWENLSREKEHKRSVENQAERKLEGQNSQSPHQISQCLKTSSEKSGHVPAVSNTQPVLQYGNPYATPETRDGADGAFYPDEIQRPPVRVPSWGLEDNVVCSQPARNLSRPDGLEDPEDSKEDEKVPTAPDPPSQHLRGHGTGFCFDPSFDVQKKCPLCELMFPPNYDQSKFEEHVESHWKVCPMCSEQFPPDYDQQVFERHVQTHFDQNVLNFD
The following text describes a protein:
Function:
Transcription factor which plays a role in mesoderm development, probably by regulating expression of target genes, such as homeobox protein ceh-51. Binds to DNA consensus motif 5'-[AG]T[GC][GT]CACC[TC][AGCT][AGCT][CT][CT]-3' in promoter elements.
Subcellular Localization:
Nucleus.
Sequence:
MSFNYSMNTPSPSMLSFDMDIPITAFLHNSDVFQLFHPDIMEQVVVNKERVFFPTPSFNVLNLESDCLYKMSLRFDKTNNKRFQFNRQTKQWTEYDKVSNHKESEVFVHPSEIRTGDDWMKSPVEFFIKVTNLRSSESDEVICLESQCKYQPTLLIQKVFRDCFGCFQAHGPPVEIKFALLTFIATTRYCSRRIADIKSSLNPFSSQDTKKKNKRNTLKAVSQEENQPIENSSFHQSFSNQYLSKPDLDLKSTTLLQIAPDHSFEPTNFVSSSHFPCWDSIFCQQSFPTPSSSPYSDSLPHFTNEWNTPTFYNENFMSYPNFPNY