lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Cellular oxygen sensor which regulates the stability and the activity of hypoxia-inducible transcription factor, hif-1. In normoxic conditions, hydroxylates hif-1 targeting it for vhl-1-mediated proteasomal degradation. In addition, regulates hif-1 transcriptional activity in a vhl-1-independent manner and independently of its hydroxylase activity. By regulating hif-1 activity, controls several cellular responses. Mediates susceptibility to B.thuringiensis and V.cholerae pore-forming toxins and enteropathogenic E.coli. Mediates susceptibility to P.aeruginosa PAO1-mediated killing by regulating resistance to cyanide produced by P.aeruginosa. Mediates resistance to S.aureus-mediated killing. In addition, plays a role in heat acclimation, neuronal development, behavioral responses to reoxygenation and hydrogen sulfide, iron homeostasis and aging. In neurons, involved in mitochondrion fusion during reoxygenation. Involved in egg laying; [Isoform e]: Regulates the trafficking of the glutamate receptor glr-1, probably independently of hif-1, by regulating lin-10 subcellular localization in response to oxygen levels. May hydroxylate lin-10.
Subcellular Localization:
[Isoform a]: Cytoplasm. Nucleus. Cell projection, dendrite. Note=In interneurons, localizes throughout the ventral cord dendrites; [Isoform c]: Cytoplasm. Nucleus. Cell projection, dendrite. Note=In interneurons, localizes throughout the ventral cord dendrites; [Isoform e]: Cytoplasm. Nucleus. Cell projection, axon. Note=In interneurons, localizes in puncta (which probably correspond to endosomes) along the ventral cord. Localization to puncta is regulated by oxygen levels. Co-localizes with lin-10 in puncta.
Domain:
The MYND-type domain is not required for oxygen-mediated hif-1 degradation or for inhibiting hif-1 transcriptional activity. Susceptibility to S.aureus infection requires the Ser-rich region but not the MYND-type or Fe2OG dioxygenase domains.
Sequence:
MSSAPNDDCEIDKGTPSTASLFTTLMLSQPSSSTAVLQCTYCGSSCTSSQLQTCLFCGTVAYCSKEHQQLDWLTHKMICKSLQTSGMVPSNLMPQAAPAVMAPIPPTVSFDDPALTTSLLLSLQNNPILNQTISNFPPTFSITSKTEPEPSIPIQIPQRISSTSTVPFSSEGSAFKPYRNTHVFNSISSESMSSMCTSHEASLEHMSSASLAMFPTSSTAQSDISRLAQVLSLAGDSPASLALVTTSVPSTASTATIPPPATTTSSATSSGKSETITVGKEKIIQTDDPDIQIIETEGGSKPTVSRTRKRPTPSNSADPKINYKDHNKNVVYSTTLQEHQKHLQNRGLALSIHQAMVLRLRYIAEHVIRSLNEFGWAVVDNFLGSDHYKFTAKEIERLYERGLFSPGQLMEAKHKDEFHIKDIRSDHIYWYDGYDGRAKDAATVRLLISMIDSVIQHFKKRIDHDIGGRSRAMLAIYPGNGTRYVKHVDNPVKDGRCITTIYYCNENWDMATDGGTLRLYPETSMTPMDIDPRADRLVFFWSDRRNPHEVMPVFRHRFAITIWYMDKSERDKALAKGKESDAACASKKENDPTSSSLNSLIGSLLRPRKNPSTHDLSKLDLRLFPSTSSDPALVSAADEDRVDISADFQSTSSLAHPESTDSGVSLSTFNVAHNHMERTTSLQSISDHFRSERSHERRSSTSSDQDLDEGLPPPPSTNPEYYI
The following text describes a protein:
Function:
The heterodimer glycoprotein H-glycoprotein L is required for the fusion of viral and plasma membranes leading to virus entry into the host cell. Following initial binding to host receptor, membrane fusion is mediated by the fusion machinery composed of gB and the heterodimer gH/gL. May also be involved in the fusion between the virion envelope and the outer nuclear membrane during virion morphogenesis (By similarity). Targets host EPHA2 to promote KSHV entry.
Subcellular Localization:
Virion membrane; Single-pass type I membrane protein. Host cell membrane; Single-pass type I membrane protein. Host endosome membrane; Single-pass type I membrane protein. Note=During virion morphogenesis, this protein probably accumulates in the endosomes and trans-Golgi where secondary envelopment occurs. It is probably transported to the cell surface from where it is endocytosed and directed to the trans-Golgi network (TGN).
Sequence:
MQGLAFLAALACWRCISLTCGATGALPTTATTITRSATQLINGRTNLSIELEFNGTSFFLNWQNLLNVITEPALTELWTSAEVAEDLRVTLKKRQSLFFPNKTVVISGDGHRYTCEVPTSSQTYNITKGFNYSALPGHLGGFGINARLVLGDIFASKWSLFARDTPEYRVFYPMNVMAVKFSISIGNNESGVALYGVVSEDFVVVTLHNRSKEANETASHLLFGLPDSLPSLKGHATYDELTFARNAKYALVAILPKDSYQTLLTENYTRIFLNMTESTPLEFTRTIQTRIVSIEARRACAAQEAAPDIFLVLFQMLVAHFLVARGIAEHRFVEVDCVCRQYAELYFLRRISRLCMPTFTTVGYNHTTLGAVAATQIARVSATKLASLPRSSQETVLAMVQLGARDGAVPSSILEGIAMVVEHMYTAYTYVYTLGDTERKLMLDIHTVLTDSCPPKDSGVSEKLLRTYLMFTSMCTNIELGEMIARFSKPDSLNIYRAFSPCFLGLRYDLHPAKLRAEAPQSSALTRTAVARGTSGFAELLHALHLDSLNLIPAINCSKITADKIIATVPLPHVTYIISSEALSNAVVYEVSEIFLKSAMFISAIKPDCSGFNFSQIDRHIPIVYNISTPRRGCPLCDSVIMSYDESDGLQSLMYVTNERVQTNLFLDKSPFFDNNNLHIHYLWLRDNGTVVEIRGMYRRRAASALFLILSFIGFSGVIYFLYRLFSILY
The following text describes a protein:
Function:
Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption is due to local fusion between the inner and outer membrane performed by the spanin complex.
Subcellular Localization:
Host cell inner membrane; Single-pass type II membrane protein; Periplasmic side.
Domain:
The coiled coil region is probably involved in host membrane fusion leading to lysis.
Sequence:
MSRVTAIISALVICIIVCLSWAVNHYRDNAITYKAQRDKNARELKLANAAITDMQMRQRDVAALDAKYTKELADAKAENDALRDDVAAGRRRLHIKAVCQSVREATTASGVDNAASPRLADTAERDYFTLRERLITMQKQLEGTQKYINEQCR
The following text describes a protein:
Function:
Most highly expressed siglec (sialic acid-binding immunoglobulin-like lectin) on B-cells that plays a role in various aspects of B-cell biology including differentiation, antigen presentation, and trafficking to bone marrow. Binds to alpha 2,6-linked sialic acid residues of surface molecules such as CD22 itself, CD45 and IgM in a cis configuration. Can also bind to ligands on other cells as an adhesion molecule in a trans configuration. Acts as an inhibitory coreceptor on the surface of B-cells and inhibits B-cell receptor induced signaling, characterized by inhibition of the calcium mobilization and cellular activation. Mechanistically, the immunoreceptor tyrosine-based inhibitory motif domain is phosphorylated by the Src kinase LYN, which in turn leads to the recruitment of the protein tyrosine phosphatase 1/PTPN6, leading to the negative regulation of BCR signaling. If this negative signaling from is of sufficient strength, apoptosis of the B-cell can be induced.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MDKGLIEGFLLVFSAVYPGFCHTTWKDDPVYFPEQITAWKGSCVLIPCYEKYNSRIKNFLWYHNPVYDKNQSKWTGTIVYQMKDSVNVESHNMRTSRYQESGKCGIVLADVQEGDRGIYKLRIDYGDNLWMTKKSVSLTVSDSTPEFMIKPVEVGRESQKLTLSCYINYYCPDDSIRLSWAGDVKGDEKQIFPKIKESLDNKETIRTETTLSFNPIWTDHNKTIECVLTRGNNKVSKTVVLNIQYPPKNPEVVLQPKKTSYVEGSNVQLRCSINSSNPEVSQITWFKDGNSWAYEKGNNKPNDYIIIDRIKEEHRGSYTCKAANKIGDTPSKPVFINVLYPPKDVRIKPQSPVVEGISASLHCSVGRSNPAVSEYRWYKDTVLQSYRNNQIKFPGIKWTDSGNYTCEARNDIGNVLSQPVPLNVMYAPVNIMISCTPSNPVPEHTKVTLTCKAQAYPTTITYAIYKDGVLLQDSQSLVLHDIQLNNKGKYYCTARNVFGRRTSDIIDLSVTSEWIQGDPDDDDNAAPPPDQAPPPHRAAPLPERAPPPDQAAPPPNQGLSVGTQTENARYDHTELLVTLIHQVNAIRQELAEVRDIVESLQRVIAPPSPPPLAYDCWNKPTHSRNLFAQPRIDGDRNFIRPPPKADWRKPSTNEALFYGITSTVNYIRCSFGILLVLIIFLIVGFHFRDWKNKATDDETESQYINMNQETHFTLTSFSKYYRKNFSRFFLSSTTKTLGQQWTFPKNMKALRGSCVEIPCSYTRPASLKPPNVIWYLFHSYNYIKVFDSQNYRTVSANYRSRTKLVLNALNSCTLHISNVRSEDEDYYYPGVDDYNAYDLSSRTVHLSITDTPNRLNLQVPREMAEGTPITIRCSVEHSCGSIPPTLRWNKRGHLVRTGQQPLSGGTWEAISEIAYTPSYEDDETEIQCSATYPNGQITRQTATLNIKYPPKNIKVLIRQKEIQEEDDVTLSCFSSSKLEINRYEWFKGVEKTKLPAEGKELTVRNVSWVTDPYSCSAWNSQGRAESALTLIPVQFAPKKVQIIKVENQDGSVELKCNFSSSSPGVTHFTWLRNDVPLLTQTEPIIILEDADENSGKYQCIAHNKIGNSSSDKQVSIQFQGETAVDLAMVLGIAAGVIAFVLIILIIYGCISKRKKSPQTDAIFGSIPVPSMAEAPPFKMDDNVYDTINEGKYRVTSDSGSTSPLYSSSRKSKLLKKEDEDFYYYAADNKGQEEPEEVEYAAIGFSQHNQPNEASQQDGHHTEHAVYAILKN
The following text describes a protein:
Function:
Catalyzes cyclization of the linear tetrapyrrole, hydroxymethylbilane, to the macrocyclic uroporphyrinogen III.
Sequence:
MSSADSLPLQGHTVAVTRPDSGGDGGGGRLGELLRAQGAEVLSVPLIRFLPPADPRALWSGLRDLRGVDWLLVTSPQGGRLLGEALAAAGVADLAGTRLAAVGEATARELRARGLPVDFLPTTATALSLGRKLPAQPGQAALHLTSQLSENTLRGELAARGVTYRRLELYHTAPAVLNAAERVALAGVSAVTLASGSAAQGLAALAGPDFDPLRLPVAAIGEQTAAAAWTLGFVSVTTAPQPSLEGLVAAAIKAVRS
The following text describes a protein:
Function:
The PI(3,5)P2 regulatory complex regulates both the synthesis and turnover of phosphatidylinositol 3,5-bisphosphate (PtdIns(3,5)P2). Regulates the synthesis of PtdIns(3,5)P2 by positive activation of FAB1 and by controlling FIG4 localization. Required for FIG4-mediated turnover of PtdIns(3,5)P2 after hyperosmotic shock. Essential for the control of trafficking of some proteins to the vacuole lumen via the multivesicular body (MVB), and for maintenance of vacuole size and acidity.
Miscellaneous:
MISCELLANEOUS: Present with 12388 molecules/cell in log phase SD medium.
Subcellular Localization:
Vacuole membrane; Peripheral membrane protein. Note=Limiting membrane of the vacuole. Localization requires FAB1 and FIG4.
Domain:
The N-terminal domain mediates interaction with FAB1 and VAC7 while the C-terminal domain mediates interaction with FIG4.
Sequence:
MEKSIAKGLSDKLYEKRKAAALELEKLVKQCVLEGDYDRIDKIIDELCRDYAYALHQPMARNAGLMGLAATAIALGINDVGRYLRNILPPVLACFGDQNDQVRFYACESLYNIAKIAKGEILVYFNEIFDVLCKISADTENSVRGAAELLDRLIKDIVAERASNYISIVNNGSHGLLPAIKTDPISGDVYQEEYEQDNQLAFSLPKFIPLLTERIYAINPDTRVFLVDWLKVLLNTPGLELISYLPSFLGGLFTFLGDSHKDVRTVTHTLMDSLLHEVDRISKLQTEIKMKRLERLKMLEDKYNNSSTPTKKADGALIAEKKKTLMTALGGLSKPLSMETDDTKLSNTNETDDERHLTSQEQLLDSEATSQEPLRDGEEYIPGQDINLNFPEVITVLVNNLASSEAEIQLIALHWIQVILSISPNVFIPFLSKILSVLLKLLSDSDPHITEIAQLVNGQLLSLCSSYVGKETDGKIAYGPIVNSLTLQFFDSRIDAKIACLDWLILIYHKAPNQILKHNDSMFLTLLKSLSNRDSVLIEKALSLLQSLCSDSNDNYLRQFLQDLLTLFKRDTKLVKTRANFIMRQISSRLSPERVYKVISSILDNYNDTTFVKMMIQILSTNLITSPEMSSLRNKLRTCEDGMFFNSLFKSWCPNPVSVISLCFVAENYELAYTVLQTYANYELKLNDLVQLDILIQLFESPVFTRMRLQLLEQQKHPFLHKCLFGILMIIPQSKAFETLNRRLNSLNIWTSQSYVMNNYIRQRENSNFCDSNSDISQRSVSQSKLHFQELINHFKAVSEEDEYSSDMIRLDHGANNKSLLLGSFLDGIDEDKQEIVTPISPMNEAINEEMESPNDNSSVILKDSGSLPFNRNVSDKLKK
The following text describes a protein:
Function:
Non-catalytic component of the proteasome.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNKLIDVPIQQPAEVVLGTASVLGIKYEGGVLIAADTLGSYGSMALFKDLERVIKLGKYTIIAGSGEYSDFIELNETLQKKVNGDECCEGKENGYKPSELYSYAQRILYKHRCDQKPLFVTLIVGGVKKDEIFLGQTDMYGTSFTENYVASGIGAHMAMPLLRKEWKDHMSREEAEHLIERCMKILYLNHCWAGNQYLLGVVDSEGSDIIGPITIDTTGKWDIIA
The following text describes a protein:
Function:
Co-chaperone that binds to the molecular chaperone Hsp70 and regulates Hsp70 ATPase activity.
Sequence:
MSQQTPLAYAVAQWLQQSSTSVPADQKAKLQQAAKSVSEAFGVDTSSAEQQAQYGSGPGLQAIFDIFLKTQAKMGAAPAPAAASSSSTAPAAAAATPSDEDLAKAEQLKAEGNKAMSAKDYGAAIEAYGKAIELNPNSPVYFSNRAAAFSQIGQHDSAIDDAKQASKIDPKFGKAYSRLGHALFSSGRYQEAVEAYQKGVEVDPSNEVLKKGLAASKEQLSSSSSSNANDATASRGAADAVSAPSAGADAGAGAGGFPNFGGGAGGMPDLAAMMNNPMIAQMAQNLMSNPDSLASLMNNPMLRQAAERFGSGGGMPDMSSMMNDPALRDMARNFMGGAGRGAGGNGGNNMYG
The following text describes a protein:
Function:
Can mediate activation of JNK and NF-kappa-B. May promote caspase-independent cell death.
Subcellular Localization:
Membrane; Single-pass type I membrane protein.
Sequence:
MALKVLLEQEKTFFTLLVLLGYLSCKVTCESGDCRQQEFRDRSGNCVPCNQCGPGMELSKECGFGYGEDAQCVTCRLHRFKEDWGFQKCKPCLDCAVVNRFQKANCSATSDAICGDCLPGFYRKTKLVGFQDMECVPCGDPPPPYEPHCASKVNLVKIASTASSPRDTALAAVICSALATVLLALLILCVIYCKRQFMEKKPSWSLRSQDIQYNGSELSCFDRPQLHEYAHRACCQCRRDSVQTCGPVRLLPSMCCEEACSPNPATLGCGVHSAASLQARNAGPAGEMVPTFFGSLTQSICGEFSDAWPLMQNPMGGDNISFCDSYPELTGEDIHSLNPELESSTSLDSNSSQDLVGGAVPVQSHSENFTAATDLSRYNNTLVESASTQDALTMRSQLDQESGAVIHPATQTSLQVRQRLGSL
The following text describes a protein:
Function:
Plays an olfactory role that is not restricted to pheromone sensitivity.
Subcellular Localization:
Cell membrane.
Sequence:
MGGCCSNWSPTGKRLCALGSTTALCVFALALGLVWPALIWQIAKREFVLEPGTEVYKNWIEPPIDTYLELYLWNWTNADAYLTEKPHLEQLGPYTFREVHERVNLKWNDNDTLTFQQRRIWYHVPELSAGDYETDRVVTINPVLLTVGYALRNEPEFLFYVDGIIMLNGLATTPFYDVLVREMIFEGYDDTLLTNLLALLALLPEESRPPIDLPPYDRFGWFFGRNGSETYDGTFTIGTGKDSVYNTGVMRLWNGANATDYYRGECGRIRGTTGEVWPPWGRTLTGTPPSVSVFAPDVCSSVTLEYAEEMERYGIDGLRWIGTDRVFDNGLHYPETECQCTAEDVADCPLLDNGAMDVSRCKFGAPATVSYPHFYLANESYLKGISGMQPNEKEHRFEMELEPYTGVPLGVRAQLQVNLDVKQYGMTLLKGIPEVMLPVLWFRQTASLTEELADDIKLILILPDIGVYVAYALGALGIIGLVLAVYFSVTRWKLQSPPQPVEAKTAL
The following text describes a protein:
Function:
Toxic component of a type II toxin-antitoxin (TA) system; overexpression in wild-type temporarily inhibits cell growth, overexpression in a hipAB deletion leads to acute growth inhibition. The toxic effect of HipA is neutralized by its cognate antitoxin HipB. In the ternary phosphoserine-HipA-HipB-DNA complex the DNA is bent about 125 degrees; all HipA in the crystallized ternary complex is phosphorylated. In E.coli phosphorylation of HipA is thought to release HipB from the HipA-HipB-DNA complex, suggesting the complex functions differently in the 2 bacteria. Phosphorylates Glu-tRNA-ligase (GltX, on 'Ser-239') in vivo, with HipB probably acts as a corepressor for transcription of the hipBA promoter (By similarity).
Sequence:
MSTAKTLTLEMHLGDLMIGELSFDATADTFAVHYTKDWQQSGFPLSPTIPLDGTGTSNQISMFLVNLLPENKGLDYLIESLGVSKGNTFALIRAIGLDTAGAIAFVPKGALLPETQLRPIKAEEVIQRIEDPTMWPMEIWDGKPRLSVAGVQPKLNLFYNGKEFAFAEGTLSSTHIVKFEKYHHLVINEFITMRLAKVLGMNVANVDIVHFGRYKALCVERFDRRNIPGEQRVLRRHIVDSCQALGFSVSKKYERNFGTGRDVKDIREGVSFNRLFSLAAKCRNPVAAKQDMLQWALFNLLTGNADAHGKNYSFFMTPSGMEPTPWYDLVSVDMYEDFEQQLAMAIDDEFDPNSIYAYQLAAFMDGLGLPRNLLISNLTRIARRIPQAIAEVILMLPPLDEDEASFVAHYKTQLLARCERYLGFVDEVRDVEV
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum (ER) and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis, and function in nonvesicular lipid trafficking between the ER and mitochondria. MDM34 is required for the interaction of the ER-resident membrane protein MMM1 and the outer mitochondrial membrane-resident beta-barrel protein MDM10.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein. Note=The ERMES/MDM complex localizes to a few discrete foci (around 10 per single cell), that represent mitochondria-endoplasmic reticulum junctions. These foci are often found next to mtDNA nucleoids.
Domain:
Lacks alpha-helical transmembrane segments, suggesting that it resides in the membrane via beta-sheet conformations similar to those predicted for other outer membrane proteins and porin; The SMP-LTD domain is a barrel-like domain that can bind various types of glycerophospholipids in its interior and mediate their transfer between two adjacent bilayers.
Sequence:
MSFRFDRSVFESADFNERLRERLTGALNPKSRRHVERADEAGNEDDSSGHQRKSGGSLDILKNDIIVEKVDFSRIPNLEILDLDVGLGVSSISSGGGGSSMMKGICKISIEGAMLQVRTVIESNLLMLSMADSPEFVTPTLITNDSFSLPITMTFSNIKMEAISKVFFVARNSGIGISFDDVVLDFKFDCSIKILQTTIEKRLKRAMELLFKDTLPTALFNMSQSWFTNSDGSRSSAKHKKDTCDENNQPSAPKIIFEDADLQELSPANMLRLSTLVSSRQTLSLHSTVSSTLSLIPGCLERQNLYRFISRMPSLSNYYSSYVDHKKERAGTPSLLMNKRPSVDYLLRRSSSSGNSLMSSQAYFDKESNLLPMEVLEENAYDLDVITDIQNKLYMRSTDHDEQVNHTKPRRRKIKIGKNKKDKPAYKEEIEQQEPVQSTITVSMPFEEPQIIIEHNDETEAVKEERESVLSSPKLIRSTMDKTYTNSRILNTLLQKNGNLLDEETRLRAQSIDSVAHTKMGYLLGLNHIATPPPPPYY
The following text describes a protein:
Function:
Required for the assembly of axonemal inner and outer dynein arms. Involved in the cytoplasmic preassembly of dyneins into complexes before their transport into cilia. Essential for the development of axonemal dynein motors in the sensory cilium of mechanosensory chordotonal (Ch) neurons and sperm flagellum, and consequently, is required for the mechanotransduction process of hearing and sperm mobility.
Subcellular Localization:
Cytoplasm. Dynein axonemal particle. Note=Detected in the cytoplasm of differentiating motile ciliated cells including the chordotonal (Ch) neurons, spermatocytes and spermatids.
Sequence:
MLWGISSALDLYEEYLRAFKIKDDPLPEDEHAREEAEEAAGDNTLNTLNILICGGADPRHVIKTLAKRYTHRIRPKLNIYLLDGCAEIEARNMLLLGVALEDPESFNLVSKVHLFMDLYGNAVIRPSSHHYMAAKGRTLLKMVTNEEELQRLAPMLNIEGLKYKERDGFEMAFTFWQPQPWNVFEVTAYWEQRSRALLGTRYDHRNGAFDWDLSMTLKERGGQQICSQEYRYWRETGVAFVFPEYEHCKPNKTLAVGLVRNGRNFIHRGYVGDIQTGPFCGFGLRTVEERMHHSVHGDNDYRATDITERNLMEFFHELLTQTAYEHDTTRSRRYGSVQLLMTPLLNHQEEDAAGQAAYDKPWIHVPGVTVHFVSPMEMEQLKKGAAHWNNMFDIVFMAYNYYSFLSKDFFQAMRAQSLFILETKLMTVERKDRVQEYESKAKELMKDAGLKAAINYQAINGKNMWLKYKKTDKDEQEDEAVTEAMPESTFKYDTDTDYGEPAEEYTGLVIEEIPSSNQTVAAIKKEVEAEGPLQPKTNFP
The following text describes a protein:
Function:
Pyridoxal phosphate (PLP)-dependent transaminase involved in the biosynthesis of amidated D-glucuronic acid structures found on the capsular polysaccharide (CPS) of C.jejuni. Catalyzes the transamination of dihydroxyacetone phosphate (DHAP) to (S)-serinol phosphate in the presence of L-glutamate. Less active with L-aspartate. No activity with dihydroxyacetone or L-alanine.
Sequence:
MQANKNIQKLTPYLSIPHKIWNSSQSNILKLDWNEATIPPSPYVIESIKKFLVNGNLNWYPNTKNLYLLDKIAEYTKQINSSFVELFEGSDSAHECIIDVFLDKCDKIGIVSPTYDNFRSRANGVGIETISFTLDDNFNLDFDSLEYFIHEKRIKLLYLCNPNNPTGKSYNIQKIKSLIINNPNVMFIIDEAYYEFTSQSVCDLVEQCNNLIITRTFSKAFALASFRIGYIISHPENIESINKLRNPKSVPMLSQIAANAALEDLQYMRDYVDEVSCARMEFVKFLNTLTTGGGGIFNDSVANFVLIQNENISLFVGFLEKEGIFIRNYSHLISKNCRISIGTRNQMSYVAEKIQEFAKKQGGFHLV
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 pre-initiation complex with RNA polymerase II and the general transcription factors.
Subcellular Localization:
Nucleus.
Sequence:
MATYSLANERLRALEDIEREIGAILQNAGTVILELSKEKTNERLLDRQAAAFTASVLHVEAELSAQIRYLTQVATGQPHEGSSYSSRKDCQMALKRVDYARLKLSDVARTWCSCSALHKHPDRLREEMETPIPNPLPLTLHAAAPGFPQTWPNEDTFFFIQRDKTRTRVSIIIKAITIKTRSDSHWGRQETEEVKPAHVVSQHSAC
The following text describes a protein:
Function:
Component of the zona pellucida, an extracellular matrix surrounding oocytes which mediates sperm binding, induction of the acrosome reaction and prevents post-fertilization polyspermy. The zona pellucida is composed of 3 to 4 glycoproteins, ZP1, ZP2, ZP3, and ZP4. ZP3 is essential for sperm binding and zona matrix formation.
Subcellular Localization:
Secreted, extracellular space, extracellular matrix. Zona pellucida. Cell membrane; Single-pass type I membrane protein.
Domain:
The ZP domain is involved in the polymerization of the ZP proteins to form the zona pellucida.
Sequence:
MDCNLRLAVSCWIMVFSWVSPLTESRQTNSRGSTERHFQPPVGTHGGLQPRLYSVKQQPAPEVPEQHRPVTVICHPDSMEVVVKADMFETGLNVDGGHLRLGSNTLGAGGECGAVQKGEDEFTIWALLSDCGTKLSSTEEKIIYSNVLIYSPEPSADGLLRLEAATIPVECHYDRRYSVDGISLESTWVPSVSTTSVNDQIDFNLKLMTGDWQSERESYTYFLADPINFEVSAIVENHVPLRVYVDHCVATATPDAEANLRYEFIEHKGCLVDAYLTNSGARFLPRTEEHKLRFQLEAFRFYQEPSNQIYITCAVKAVPAVQAVSSQNRACSFIENRWQSIDGGDQVCRSCDVFRRGQEPQAVPSPKMPVNAKDQIGLSQKNIVHNKAEHQPASYVHFWPGAYQSHHSKPQQSNRFMKRDADNKFHQAVQLGPLVVLPSRKVVSVATNFSTWSEKNNTS
The following text describes a protein:
Function:
Transports glutathione-coordinated [4Fe-4S] iron-sulfur clusters in an ATP-dependent manner. Required for optimal parasite growth during erythrocytic stages.
Subcellular Localization:
Mitochondrion membrane; Multi-pass membrane protein.
Sequence:
MRSFYNKCFTNKLISAHSLFCQHVSTLKNNKKECFEDVKRSNRISDEFYSSFLYHSYIENLKSTKEYVYFIYLQDIYYNINIFKNKGRLYISNNGLCNDKLKDNNNNNNINSNNFGNSYNAYTKKKSFYHSFNDLNEAKEIRKKRKNEKSEKNIVEYLLCNIINPNENYHIQNIYNHNLNNNVSIEIHKKNDSVMYHYNNEKKTKTSKMTTDIKLKQINNVYIKYVPYKNKIITLACPNKYYPTLYRYFSSHTNKKEDAEENDKNKNININNVDNRYKEDFMYGCENKNDSEKHKKTTNNNFGDEFEKLKVKELDKILNKLEMLYDNKNNKMNINVKILGYIFKNFLLKNKELKRKIFCSLFFLLCSKMAIIYTPILLSTFIENVNLQKSLSNNIDIYSTNKSSVLLLCAYVFSRVLSSTMNELRNSVFSNISQKISTFVSKLFFYKIHNLNLTYILSKKNGELSFIFNRGCKSITNLLNVMVFQIIPIIIEFILYLYILTYKIHYTVSLVTCFNMFLYVLFTTLITKRRTIIRKHMNKAEQNTFNIFLDSIQNVEQVKYYTNEIHELKKFIKEQKKYEKEAINVQKSLSFLNFGQQIILNTNLFLCMYLTYLNIANDIFPFSYLILVNTLLFQLAMPLNMFGTIYRETKLSLVDIESMIKILVKKIKSPDYGNQMLIKNGNIKFENVYFKYPLNEDINGLEQNYQAKEKDPNIINNINNINNINNINNINNINSINNIYTFESNVKNISSTNMITSSINKLKKWYLDKVKDNKKNVQYNNNDVKKTNPNITKNLNKEIKENINTHLKNHKIINNSPNYNNNNYLFQNFTCNIENGEKVAIIGKSGSGKSSLIKLLLKFYEVNSGNIYIDNKNIDDIDLYTLRKNISVVPQDTILFNNTISYNIKYGNFQCTDKQMIQASIKAELHDKIMKMENKYDTIVGERGTKLSIGEKQRICIARCFLKDSKIIVLDEHASNLDNENKKAIEKALTKLCMGKTTFIITHVMENLKHMDKIIFFCGKNIYVGSHKNLMDDNHFYREYYDSKNNKML
The following text describes a protein:
Function:
ATP-dependent chromatin-remodeling factor that binds and distorts nucleosomal DNA. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Involved in transcriptional repression as part of the NuRD complex. Required for anchoring centrosomal pericentrin in both interphase and mitosis, for spindle organization and centrosome integrity.
Miscellaneous:
MISCELLANEOUS: One of the main antigens reacting with anti-MI-2 positive sera of dermatomyositis.
Subcellular Localization:
Nucleus, PML body. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Note=Associates with centrosomes in interphase and mitosis. Localizes to sites of DNA damage.
Sequence:
MKAADTVILWARSKNDQLRISFPPGLCWGDRMPDKDDIRLLPSALGVKKRKRGPKKQKENKPGKPRKRKKRDSEEEFGSERDEYREKSESGGSEYGTGPGRKRRRKHREKKEKKTKRRKKGEGDGGQKQVEQKSSATLLLTWGLEDVEHVFSEEDYHTLTNYKAFSQFMRPLIAKKNPKIPMSKMMTILGAKWREFSANNPFKGSAAAVAAAAAAAAAAVAEQVSAAVSSATPIAPSGPPALPPPPAADIQPPPIRRAKTKEGKGPGHKRRSKSPRVPDGRKKLRGKKMAPLKIKLGLLGGKRKKGGSYVFQSDEGPEPEAEESDLDSGSVHSASGRPDGPVRTKKLKRGRPGRKKKKVLGCPAVAGEEEVDGYETDHQDYCEVCQQGGEIILCDTCPRAYHLVCLDPELDRAPEGKWSCPHCEKEGVQWEAKEEEEEYEEEGEEEGEKEEEDDHMEYCRVCKDGGELLCCDACISSYHIHCLNPPLPDIPNGEWLCPRCTCPVLKGRVQKILHWRWGEPPVAVPAPQQADGNPDVPPPRPLQGRSEREFFVKWVGLSYWHCSWAKELQLEIFHLVMYRNYQRKNDMDEPPPLDYGSGEDDGKSDKRKVKDPHYAEMEEKYYRFGIKPEWMTVHRIINHSVDKKGNYHYLVKWRDLPYDQSTWEEDEMNIPEYEEHKQSYWRHRELIMGEDPAQPRKYKKKKKELQGDGPPSSPTNDPTVKYETQPRFITATGGTLHMYQLEGLNWLRFSWAQGTDTILADEMGLGKTIQTIVFLYSLYKEGHTKGPFLVSAPLSTIINWEREFQMWAPKFYVVTYTGDKDSRAIIRENEFSFEDNAIKGGKKAFKMKREAQVKFHVLLTSYELITIDQAALGSIRWACLVVDEAHRLKNNQSKFFRVLNGYKIDHKLLLTGTPLQNNLEELFHLLNFLTPERFNNLEGFLEEFADISKEDQIKKLHDLLGPHMLRRLKADVFKNMPAKTELIVRVELSPMQKKYYKYILTRNFEALNSRGGGNQVSLLNIMMDLKKCCNHPYLFPVAAMESPKLPSGAYEGGALIKSSGKLMLLQKMLRKLKEQGHRVLIFSQMTKMLDLLEDFLDYEGYKYERIDGGITGALRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIFDSDWNPHNDIQAFSRAHRIGQANKVMIYRFVTRASVEERITQVAKRKMMLTHLVVRPGLGSKAGSMSKQELDDILKFGTEELFKDENEGENKEEDSSVIHYDNEAIARLLDRNQDATEDTDVQNMNEYLSSFKVAQYVVREEDKIEEIEREIIKQEENVDPDYWEKLLRHHYEQQQEDLARNLGKGKRVRKQVNYNDAAQEDQDNQSEYSVGSEEEDEDFDERPEGRRQSKRQLRNEKDKPLPPLLARVGGNIEVLGFNTRQRKAFLNAVMRWGMPPQDAFTTQWLVRDLRGKTEKEFKAYVSLFMRHLCEPGADGSETFADGVPREGLSRQQVLTRIGVMSLVKKKVQEFEHINGRWSMPELMPDPSADSKRSSRASSPTKTSPTTPEASATNSPCTSKPATPAPSEKGEGIRTPLEKEEAENQEEKPEKNSRIGEKMETEADAPSPAPSLGERLEPRKIPLEDEVPGVPGEMEPEPGYRGDREKSATESTPGERGEEKPLDGQEHRERPEGETGDLGKREDVKGDRELRPGPRDEPRSNGRREEKTEKPRFMFNIADGGFTELHTLWQNEERAAISSGKLNEIWHRRHDYWLLAGIVLHGYARWQDIQNDAQFAIINEPFKTEANKGNFLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNLSQEPAHPAMALHARFAEAECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPATLSRIPPIAARLQMSERSILSRLASKGTEPHPTPAYPPGPYATPPGYGAAFSAAPVGALAAAGANYSQMPAGSFITAATNGPPVLVKKEKEMVGALVSDGLDRKEPRAGEVICIDD