lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Architectural component of nuclear structure that plays different roles in controlling nuclear size and morphology (By similarity). Involved in the organization of multimeric complexes in the peripheral nucleoskeleton (Probable).
Subcellular Localization:
Nucleus matrix. Nucleus lamina. Note=Localizes at the nuclear periphery and is associated to the nucleoskeleton.
Sequence:
MLTPQRSAWSLKSKVSSEKPRSKGKGITKNLDSAATPFPPLGLLNGGDLDRGGEDMEAWKRFKDEGLLDESICYKKDRESLASRIIELEKDLHEYQYNMGLLLIEKKEWSSHFEEMKMRLAEAEEILKREQAAHIIALTESEKREDNLRKALGVEKQCVTDLEKALREMRSEIAEVKYTAEKKMTEAFALEASIEEKRLDTERKLHSADAKLAEASRKSSEINRKLEDVEDRERKVQRELNSINSERKALEKDISEQKEHLREWEKKLQDGQNRLLDGQRHINEREERINEAEGGLKKKEEELEEAKRSIEGTRNTLKRKEEDLDVRLRSLVSKEKEIELKMKNLQKKEKDLHEIAEKLDHREREEIQKLLDEHRATLDTKKREFELELESKRKSVDEELKSKFAAVNKAEKEVNRKQGLISEGEKELESKMDKIKIKEKDLETKSKALKKWEESLKSDEKKLVAEKDQIMKDTHELKVSINELESLRDALNAEQHQIAEEREKLEISKEEREQYIQKQSELKQEIEKYRNMQEELSKGIESLREEREKFEKEWESLDEKKITLQRETKKIHEEKEKLEKWHHKDQERLRNEEANAKADIERQLEDIKLQKEAFENTMKHERLMAQEEVARRLADVTRELELRKHDLEMNMQKKQEEIERKLQGKEREFETRKEAELSRITSLINLNNSKLQKLRIEQDRLDREKEEVELQKKKLQEDQSEIQRDVDTLRQLSKNLKNQRAEFIKEKECFLAAAERCKTCQNCGVSISELEMVGIIQSSAEIENADIVLPSLTDDHIEQHMKNKGSHVTSPQTGSRVFGSGFLQKCTKIFKFSPGKNAETSATTTPLVFGEELDIAASEDAAANDNNPAADVERVTVNPSLVFGEQLDTAASEDAAANDNNPAADVERVTVNPPPLAPVATEQNETEESSLPPENDSPPKQRGGRQSTRRGRGGKTVRRTRTMEAVVDDAKAILGDTLIVEEAKESSQQNDEQSQGASVHTGGTSNTRQKRRRAPASEMTNSEHDVEESESQSQSISIGRGRRKKRQTSAASEVQAPVVERRYNLRHSTVAKNSVAATLAVSDQAKVQTKASHQASHDNNQISMGDDPALEGSHKVTHTVQKTTTASVMEVSSKPAMEETHEENIVVRSVEISEMSASEEAEGEVQGVPPIAEEPATPSSGSSTSGDIGNDDDMDDDDEEERHNASIGKKLWNFFTT
The following text describes a protein:
Function:
Essential subunit of the Sec protein translocation channel SecYEG. Clamps together the 2 halves of SecY. May contact the channel plug during translocation.
Subcellular Localization:
Cell inner membrane; Single-pass membrane protein. Membrane.
Sequence:
MKVTTFIQECKAELEKVQWPTREEVVYSTVVVLVTVFFFSIFLFFADSAFVRLLTWFWELAG
The following text describes a protein:
Function:
Actin-associated protein that may play a role in modulating actin-based shape.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MGAEEEVLVTLSGGAPWGFRLHGGAEQRKPLQVSKIRRRSQAGRAGLRERDQLLAINGVSCTNLSHASAMSLIDASGSQLVLTVQRLADEGPVQSPSPHELQVLSPLSPLSPEPPGAPVPQPLQPGSLRSPPDSEAYYGETDSDADGPATQEKPRRPRRRGPTRPTPPGAPPDEVYLSDSPAEPAPTIPGPPSQGDSRVSSPSWEDGAALQPPPAEALLLPHGPLRPGPHLIPMVGPVPHPVAEDLTTTYTQKAKQAKLQRAESLQEKSIKEAKTKCRTIASLLTAAPNPHSKGVLMFKKRRQRAKKYTLVSFGAAAGTGAEEEDGVPPTSESELDEEAFSDARSLTNQSDWDSPYLDMELARAGSRASEGQGSGLGGQLSEVSGRGVQLFEQQRQRADSSTQELARVEPAAMLNGEGLQSPPRAQSAPPEAAVLPPSPLPAPVASPRPFQPGGGAPTPAPSIFNRSARPFTPGLQGQRPTTTSVIFRPLAPKRANDSLGGLSPAPPPFLSSQGPTPLPSFTSGVPSHAPVSGSPSTPRSSGPVTATSSLYIPAPSRPVTPGGAPEPPAPPSAAAMTSTASIFLSAPLRPSARPEAPAPGPGAPEPPSAREQRISVPATRTGILQEARRRGTRKQMFRPGKEETKNSPNPELLSLVQNLDEKPRAGGAESGPEEDALSLGAEACNFMQPVGARSYKTLPHVTPKTPPPMAPKTPPPMTPKTPPPVAPKPPSRGLLDGLVNGAASSSAGIPEPPRLQGRGGELFAKRQSRADRYVVEGTPGPGLGPRPRSPSPTPSLPPSWKYSPNIRAPPPIAYNPLLSPFFPQAARTLPKAQSQGPRATPKQGIKALDFMRHQPYQLKTAMFCFDEVPPTPGPIASGSPKTARVQEIRRFSTPAPQPTAEPLAPTVLAPRAATTLDEPIWRTELASAPVPSPAPLPEAPRGLGASPSSCGFQVARPRFSATRTGLQAHVWRPGAGHQ
The following text describes a protein:
Function:
Required for the assembly of cytochrome c oxidase.
Subcellular Localization:
Mitochondrion intermembrane space.
Sequence:
MASHPEQQSSSSSADVSSSSWGKVERKFTNKSASEYYDPCQDFADRSLRCMKRNPDDRDMCHDYFQAYRDCKKQWLTQKKLGSSSTAK
The following text describes a protein:
Function:
Probable phosphatase. Involved in the response to sodium and lithium ion stress (but not to potassium or sorbitol stress) by inducing transcription of the sodium pump ENA1/PMR2. Acts through a calcineurin-independent pathway and is functionally redundant with PSR1. Also involved in the general stress response; acts together with WHI2 to activate stress response element (STRE)-mediated gene expression, possibly through dephosphorylation of MSN2.
Subcellular Localization:
Cell membrane.
Sequence:
MGFIANILCCSSDTSKTHRQRQPPETNHNRNRNRKHSSNKAQTQGRKQKATPNGDKMQYSTPEILLSSSDSGSNAGSKTMQENGNSGNGKLAPLSRDHSNNSYDEEKEYEDYNEGDVEMTEVNNAGEEEEEDDEAKEKQDHVVHEYNVDADRNSSINDEAPPQQGLYQVGQEDMNPQYVASSPDNDLNLIPTTEEDFSDLTHLQPDQYHAPGYDTLLPPKLQEFQQKKCLILDLDETLVHSSFKYMHSADFVLPVEIDDQVHNVYVIKRPGVDEFLNRVSQLYEVVVFTASVSRYANPLLDTLDPNGTIHHRLFREACYNYEGNYIKNLSQIGRPLSETIILDNSPASYIFHPQHAVPISSWFSDTHDNELLDIIPLLEDLSSGNVLDVGSVLDVTI
The following text describes a protein:
Function:
Superoxide dismutases serve to convert damaging superoxide radicals, a key form of ROS, to less damaging hydrogen peroxide that can be converted into water by catalase action. May be involved protection against extracellular stress.
Subcellular Localization:
Secreted, cell wall. Membrane; Lipid-anchor, GPI-anchor. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP).
Sequence:
MIFIPIIILIYLVSIAASDKSPKIKKNPRNVVAVADFPFGGDTQVKGNVVFSAKEGKHVNVHIDMTGLPKDEGPFFYHIHERSVPGNGNCEAVGLHFNPYNASPVCDEQKNDAYCQVGDLSGKHGCINTTCFELKYSDPYLSLNRKSKSYIIGKSVVFHYPNLTKIACADIEEANELRLQSLIDEYTQTDDAIQLKELNTPLETDYKFDEVEALSSEIYHSDTDSDPPQQELISTEKLYNKTDNVYSPEETRPSDQNKKSHRHSLLPLAKWKKNSPKNYSNISIHGISSDCLNDGMMVTGSVFGSLVLGIAAGIFV
The following text describes a protein:
Function:
Required for the localization of dynein and dynactin to the mitotic kintochore. Dynein is believed to control the initial lateral interaction between the kinetochore and spindle microtubules and to facilitate the subsequent formation of end-on kinetochore-microtubule attachments mediated by the NDC80 complex.
Subcellular Localization:
Chromosome, centromere, kinetochore.
Sequence:
MSAAVDSEVQRLRCKLKEAEESLQKAAQYGLQLLDDQLDLQNRLEEQRTEMTNSIEALEQEKYSLQRELELRGRMLDSLRSECESIKTQQKMLWVQQEAQLERSYTLEIGEYKNKLEKMKAELDEARLSERQLRHKLELQAEALSSKTEELRMMAERSQETLSSEMMELQMEKAELETAKAALEHELNEMSYREQQLQLAGSHLQRTVERLTREKEDCEKEVVSHFNALEEPVRACSFINRTWDMLLMRMQDPNQLLHLCQTVLLQDTPDMQAHLTVTAALLQYSSSDESQSDESLNSFRGQVQIATLMQMKGCQADPGQLERLQSMLAQKNNEIEALMIKLRRLERAEMTIKAEPSSAPSGEGDSGDMTYYTDLLKMQLSNSVKEAERLGEELSVQRMKALAESQRVLEVERRLFSSERTLRLCQSENIRLQVQLDELRMKYQPNAVNKSQVAKRRREKLPVDVPAEADAPEPKVSTAQFFPDQAHGRLCVIVTTSQLLHATCFVYTTSASLKKQETDKILVLCEECPTQPQICTAKRVQAFASEHTSCAFCLSNTASCIFCTSSNMSPPSGTTVKAEEVDAGAENRREERKKEMRPQPVIHVSSKPTLENQCAQQ
The following text describes a protein:
Function:
CIPK serine-threonine protein kinases interact with CBL proteins. Binding of a CBL protein to the regulatory NAF domain of CIPK protein lead to the activation of the kinase in a calcium-dependent manner.
Sequence:
MLNVGDDTVMCWCANKYITHNTPILTAEASETAQLSLFKRYVLLYYLQMDHETSAKHKALEGMLLDARAEPTDLPLSLLREITNGFSDDLQIGNGGFAVVYKGMLGKGMVAVKRLSERFDIKEIKFNEEVSCLLNVKHKNIVRFLGYCSDTQGIMMNYEGKNVLADVRQRLLCFEYLAKGSLDKYITGPSCGLEWRKRYLIIKGVCEGLYYLHVKQRIVHLDLKPANILLDDNMAPKIADFGLSRRFDEKQSRDFTSKLMGTLGYLAPEFLSGEITFKLDIYSLGVIIIEILTGKKGYHDVEDELDSWGDRLQNTLGDIQLKQVRICAEIGIECTENDPAKRPDIEYIISRLNEKERGASELYQCTPNKVPGETSSKVLGMSWNRLAKSHGDIQLERAETGIECTENKATKGLVTQHITDRLDEAESTGWSIKTSGSNLSVVQVEKDFTELNLWELKVPGETSNEDSISLIQASEQIKTKSTCHTDCHSSASPTEQRCQMEVGTLLMRRYETGKPLAQGNFGKTYFAWNIINGERVVIKVIDKDKVMRGRLMVQKEKKVSIVRKITHPNIVQLSEVMATKSKIYLVLEYARGGELFNKISKGKFSEDVAWRYFHQLISAVGHCHSLGVYHGDLKPENLLLDEVDNLKVSGFGLSALADPKRQDGRLHTTYGTPAYVAPEVLSGRDHDGAKADIWFCGVILLALVAGDLPFQDTTLTDMYTKISRGEYSCPCPLSAELEDLLSMILHQDPSARASVLRIKRSAWFRKHEARDKIYKDGDKTSDLMESINTYRNQTSARLTNMNAFDIISLSSGYDLSSLFEEYGRCEYKFTSMQPAEIIFAKLSELAKQLKVEIKERENGVVKLAAPKEGRSISVFSSDTVYNLAS
The following text describes a protein:
Function:
May play a role during spermatogenesis by repressing transposable elements and preventing their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Directly binds piRNAs, a class of 24 to 30 nucleotide RNAs that are generated by a Dicer-independent mechanism and are primarily derived from transposons and other repeated sequence elements. Besides their function in transposable elements repression, piRNAs are probably involved in other processes during meiosis such as translation regulation (By similarity).
Subcellular Localization:
Cytoplasm. Note=Probable component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis.
Sequence:
MPGRARTRARGRARRRESYQQEAPGGPRAPGSATTQEPPQLQSTPRPLQEEVPVVRPLQPRAARGGAGGGAQSQGVKEPGPEAGLHTAPLQERRIGGVFQDLVVNTRQDMKHVKDSKTGSEGTVVQLLANHFRVISRPQWVAYKYNVDYKPDIEDGNLRTILLDQHRRKFGERHIFDGNSLLLSRPLKERRVEWLSTTKDKNIVKITVEFSKELTPTSPDCLRYYNILFRRTFKLLDFEQVGRNYYTKKKAIQLYRHGTSLEIWLGYVTSVLQYENSITLCADVSHKLLRIETAYDFIKRTSAQAQTGNIREEVTNKLIGSIVLTKYNNKTYRVDDIDWKQNPEDTFNKSDGSKITYIDYYRQQHKEIVTVKKQPLLVSQGRWKKGLTGTQREPILLIPQLCHMTGLTDEICKDYSIVKELAKHTRLSPRRRHHTLKEFINTLQDNKKVRELLQLWDLKFDTNFLSVPGRVLKNANIVQGRRMVKANSQGDWSREIRELPLLNAMPLHSWLILYSRSSHREAMSLKGHLQSVTAPMGITMKPAEMIEVDGDANSYIDTLRKYTRPTLQMGMSCLLVFKVICILPNDDKRRYDSIKRYLCTKCPIPSQCVVKKTLEKVQARTIVTKIAQQMNCKMGGALWKVETDVQRTMFVGIDCFHDIVNRQKSIAGFVASTNAELTKWYSQCVIQKTGEELVKELEICLKAALDVWCKNESSMPHSVIVYRDGVGDGQLQALLDHEAKKMSTYLKTISPNNFTLAFIVVKKRINTRFFLKHGSNFQNPPPGTVIDVELTRNEWYDFFIVSQSVQDGTVTPTHYNVIYDTIGLSPDTVQRLTYCLCHMYYNLPGIIRVPAPCHYAHKLAYLVGQSIHQEPNRSLSTRLFYL
The following text describes a protein:
Function:
Component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Required for the maturation of extramitochondrial Fe-S proteins. Part of an electron transfer chain functioning in an early step of cytosolic Fe-S biogenesis, facilitating the de novo assembly of a [4Fe-4S] cluster on the cytosolic Fe-S scaffold complex. Electrons are transferred from NADPH via a FAD- and FMN-containing diflavin oxidoreductase. Together with the diflavin oxidoreductase, also required for the assembly of the diferric tyrosyl radical cofactor of ribonucleotide reductase (RNR), probably by providing electrons for reduction during radical cofactor maturation in the catalytic small subunit.
Subcellular Localization:
Cytoplasm. Mitochondrion intermembrane space.
Domain:
The C-terminal domain binds 2 Fe-S clusters but is otherwise mostly in an intrinsically disordered conformation; The N-terminal domain has structural similarity with S-adenosyl-L-methionine-dependent methyltransferases, but does not bind S-adenosyl-L-methionine. It is required for correct assembly of the 2 Fe-S clusters; The twin Cx2C motifs are involved in the recognition by the mitochondrial MIA40-ERV1 disulfide relay system. The formation of 2 disulfide bonds in the Cx2C motifs through dithiol/disulfide exchange reactions effectively traps the protein in the mitochondrial intermembrane space.
Sequence:
MATAACFISGGAAPGAALEALLAKETSLSLSSVELVCTQDSASSSTKYTFGMAASTSAHSQAALARVARSMAPGGRLYVYETSTSGSSRLEALKKDLLLSGFVDAAELSSSGAVLISAQLPQWGLGAAAKLSLKRPAVANGAAAAAPAATTAAAVPPKSNVWKLGGDEDGEEEELVDDDALLAPEDKAAVVPKYPDDCEVGAGGARKACKNCSCGRAEAEAEAEAGGGKAKLTADMLDNPTSACGNCYLGDAFRCGSCPYRGLPSFEPGQKVTLGANLLAADV
The following text describes a protein:
Function:
Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis.
Subcellular Localization:
Secreted.
Sequence:
MGLLDKVCLVLLASTLLAVTLAEGLTFLSPQHASQFLSRRRRANSFLEESKGGNLERECIEELCNKEEAREIFENVPETEYFFPKYLACLGAHRSGTLSKLSYLNFDGPVDLRACVNAIPDQCTPLPCNKERSKECIDGKGNFTCICKPGFQGPLCDEDINECVDPVNPNAGCNQKCLNLPGSYRCACEDGYYMLPNKHTCSDRNECEMFPTICGSAVCKNTPGKYECECDNGYRYNSSAKACEDIDECAVRSCSQICVNNPGGYTCYCDGRRKYKLAQDKTSCESIPVCVPLNLETNYELLFLAEQFTGIPVVYLRFKLPDVSRFSAEFDFRTYDGEGVILYAESADSTSWFLLALRDGKIEIQFKNELWTKVTTGGKAINNGEWHIITVEELENIISVKIAKEAVMNINNPRSLFKSSNGILEIKVYIAGLPRKVDNIIKPINPRLDGCIRGWNLMNQGALGVKEVIQGKQSKHCLVTVERGSYYPGGGVARFIMNYNVSTNDEWVANITFNIRSSTGIGVMFSLVNGETVPLAIAIEDLGSDFLQGIVVSIHSATVARLTTKRICTDKNLLISVSITKNTLVLNANSYTDITYASQVELDKQLSILDQAMQENPDTYLGGIPADIPVAATPVSAHYVGCMDVTINNELMDLDGAVSKQNDIRSHSCPLIL
The following text describes a protein:
Function:
Receptor for cAMP. Coordinates the aggregation of individual cells into a multicellular organism and regulates the expression of a large number of developmentally regulated genes. The activity of this receptor is mediated by G proteins.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MENLNTTSTAALTGMTKQENDASYAVLLIADFTSIIGCTLVLLGFWRLKLLRNHITKIITFFCSTSLAKDLISTILTLIEKKQSNGSFQCYLYATVITYGSLACWLWTLCLSFSIYNLIVKREPEPEKFEKYYHVFCWVVPFIMSVIMLSKGVIEVTGNWCWIGNTYVGYRFGLFYGPFLAIWFLAAVLVGLTSRYTYKVIRSSVSDNKDRHMTYQFKLINYIIVFLLCWVFAVINRIVNGLNMFPAWVSILHTYLSVSHGFYASVTFIYNNPLMWRYLASIILIPFTKFGYFVETQQRLEKNKNNNNHSPVGLSNNAQNNNHHHNHNNNHNNNHNNHNNNNNNNNSDFVNNDSSNYYTASMIESFSVQNENSKSINGADNFKQNGASQQDDKDSPNSNNNNNNNNNNNNNNNNNNNNNNNNNNYNNKDIEPIDNCNTNSIPMDNIATRIEIPPQHPTLTPQQSLQEINLNDDDNKINTHQSNKKKDSNV
The following text describes a protein:
Function:
Neddylation of cullins play an essential role in the regulation of SCF-type complexes activity.
Sequence:
MPASWFRDQFRKIQNTKIRQTSRNETRFNFLQQNYSHLLKNPSRHSVRSAERSLPKLPHGFTDPEHDSLSNGHGATSKNNVQSFSCNDRKLPQLLYDTNLNKCSTLFDDYDGSGGLFLYPRETNNSASLNGSPDLLRYKRFQISDSDIDIVFDVYRDPSRDVILTAGVEKFCADLLLRPDDFRILILAWYFGAETMCRFTRFEFQSGFKKLRVRNMTELQDVIFQGCTCQIDFSNDVLESKQQSDDQTPTSTKETKCGLKSRTESQCSTDNDRLYGCIYPNYRSCTCNRSTFTRSVTCSRDKFRDLYKWAYRFSLDMDTGQRTLPLDVALSMWRLIFSQNLNFLSQRATSDATKSSLLTQANPDLNSSDRRDGIVCDRTAQTNTCCQFDDVTNIESARNESRKEARRQANRFNTETSSRQSPSSSQQHQHRPLLALKSGAKKSSATRLISMWLRFLEDERNANVRGITRDTWEMLLTFVEMVRDVRLDYDENEAWPSLFDDFVEWFKEVGGGDDDDNDGDSDDGGECGGGDDDVLVGGGLNNGD
The following text describes a protein:
Function:
May be involved in transcriptional regulation.
Subcellular Localization:
Nucleus.
Sequence:
MLSGKCSSSMPAPYGQHPNLSYPTLAQRDSEAWNTWAGSGVSLFPVGGRAAVAELSHRWRLPHSLGDSKRGARPAGRMKRSKKGTDSAMGGKNKIPLSERILNVTLEIVYVLTGEDYVVSKRSSARVVQSCSDCLLDGFCQRHIPTVSHSSRSVLQKENARKVLELISNIFHMLTEEVAIRHEEAGNYFSSEEWDYLRGNHVFYTEVIKENPQQQPLRSPDDGKEETSSIRSCMDAKVISNNKAHKRWSHTMREEGNPMDNPAVHDPDSPLSKYPMASWEGEHLASSTDPLTGQTQGREASPHIRWCSQNNCSIYYKSLGSKETYSSWEEGESAKCSVKPHTNQIQGTSSPVLASKLHKGSIKKESPSWVQEECSNCRSNALPEPLLESNTPILRNRSLSSYISSGIKEESSSWDSLSYTSNPATEAVQKADTPPPIGATFRKRPLPSYFYSEIKEEMTSWQGVECSELATELIQVTDIPAPNISPTNNSPTNYKSNVIKKALASCVDGPLNYSSSTDPIEVTDTSAHIIGYSINNRLECSEYATDLPYRSNCVQLTAPAIQTIYNYADKPSPSDREIVRNKRTPKGKKKFACLECGKCFTRNTTLLSHQKCHTEGKQLICPECGLCFPHYSGLISHQKSHSGGKAFACSECGLCFTRYSSLVSHQKNHPREKPFTCSECGKRFSRNSNLVRHKRMHTGEKPYSCPECGKCFTRNAALIKHMTAHALGKLFACSQCGLCFTRSASLVSHQKTHAGSEPYTCSECDKYFTNDTDLERHQDIHAGDKIFSCFECGQNFTHHLNFAEHLRSHTGDHAFF
The following text describes a protein:
Function:
Component of the Dom34-Hbs1 complex, a complex that recognizes stalled ribosomes and triggers the No-Go Decay (NGD) pathway. In the Dom34-Hbs1 complex, dom34 recognizes ribosomes stalled at the 3' end of an mRNA and engages stalled ribosomes by destabilizing mRNA in the mRNA channel. Following ribosome-binding, the Dom34-Hbs1 complex promotes the disassembly of stalled ribosomes, followed by degradation of damaged mRNAs as part of the NGD pathway.
Subcellular Localization:
Cytoplasm.
Sequence:
MKLISQSKGTSSSEVCLVVVAQDKEDLFTLYNIINTDDELIFKKKLTLKLDEAGKKKSTELVRLRVKVVSSEFEPQHEFLKYKGITTEDDAGKANVDVALGKFFSFTVDYQYPFTIIKKDFNSYCQKLINEACNLESRSDMAAVVLQEGLAHICLLSSFSTILKQKVEYSLPKKKRSVDVLKFDEKTEKFYKAIYNAMLKHFDLSQLKAVILCSPGFYAKTLYEKILQYAQTNQEKTVIDNKDKFLVAHCSTGYLQGISEVLRDPAYSQKLQNTKNSGQLQVMDAFLKHLNDDDNKSWYGEAEITKACEFGAIETLLITDDWLRADSVSVRNKSLKLIKDVENMGGKVCVFSSMHSSGEELNSLTGLACILKYPIPDLDEHEDED
The following text describes a protein:
Function:
Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed not to be involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone.
Subcellular Localization:
Mitochondrion inner membrane; Single-pass membrane protein; Matrix side.
Sequence:
MENPSTHSDLELFTRELTWDTRTTINRLFSPTFFGAMGFGMALAMNYFQRRPMMSGIQRHIALVAIGVPIGMYADRLNENRLARRDAILIHYIRNHPEDFPVTERVKYKDVLDKWLPRR
The following text describes a protein:
Function:
Hydrolyzes the second messenger cAMP, which is a key regulator of many important physiological processes. May have a role in muscle signal transduction.
Subcellular Localization:
[Isoform PDE7A1]: Cytoplasm, cytosol. Note=PDE7A1 (57 kDa) is located mostly to soluble cellular fractions; [Isoform PDE7A2]: Cytoplasm. Note=PDE7A2 (50 kDa) is located to particulate cellular fractions.
Domain:
Composed of a C-terminal catalytic domain containing two putative divalent metal sites and an N-terminal regulatory domain.
Sequence:
MEVCYQLPVLPLDRPVPQHVLSRRGAISFSSSSALFGCPNPRQLSQRRGAISYDSSDQTALYIRMLGDVRVRSRAGFESERRGSHPYIDFRIFHSQSEIEVSVSARNIRRLLSFQRYLRSSRFFRGTAVSNSLNILDDDYNGQAKCMLEKVGNWNFDIFLFDRLTNGNSLVSLTFHLFSLHGLIEYFHLDMMKLRRFLVMIQEDYHSQNPYHNAVHAADVTQAMHCYLKEPKLANSVTPWDILLSLIAAATHDLDHPGVNQPFLIKTNHYLATLYKNTSVLENHHWRSAVGLLRESGLFSHLPLESRQQMETQIGALILATDISRQNEYLSLFRSHLDRGDLCLEDTRHRHLVLQMALKCADICNPCRTWELSKQWSEKVTEEFFHQGDIEKKYHLGVSPLCDRHTESIANIQIGFMTYLVEPLFTEWARFSNTRLSQTMLGHVGLNKASWKGLQREQSSSEDTDAAFELNSQLLPQENRLS
The following text describes a protein:
Function:
May function as E3 ubiquitin-protein ligase that catalyzes the transfer of ubiquitin onto target proteins. May play a role in DNA repair via its role in the synthesis of 'Lys-63'-linked polyubiquitin chains that recruit proteins involved in repair to sites of DNA damage by alkylating agents.
Sequence:
MDLFRKPKKRNAPVVRKKESSSDEDQDSEVKDVIQKRRRTNPMVQSTKQLDASTRRADNSSDDSDDSDDNQDIAVATHSFAASGDAGPSGPRDQGATATLEVDTDYSHDAQAQFERVQQQLKEGVEKDGKILYKGSALYGAKEAKDTAKGNAASGYNRVGPVRAPQFLRQTVRWDFAPDICKDYKETGFCTFGDSCKFVHDRSDYKHGWEIDEEYEAGKYGAEDDANYEIHEGDDTFPEDCFICGNPFVDPIVTKCKHYFCTGCALKSFQKSSKCPICQQNTENIMNTAKELLTYLKRKKQQQKQEAEKQEEEKDSDDDEKPHECDDHHHHDHEDEPEEPENDSNVPEAEEKSDEEQEIMMEDVEGLEGGENDSESDDDDAEKD
The following text describes a protein:
Function:
Oligosaccharyl transferase (OST) that catalyzes the initial transfer of a defined glycan (a hexose-linked tetrasaccharide composed of a hexose, 2 hexuronic acids and a methyl ester of hexuronic acid in H.volcanii) from the lipid carrier dolichol-monophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation (Probable). Involved in the assembly of an N-linked pentasaccharide that decorates the S-layer glycoprotein and flagellins (Probable).
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Domain:
Despite low primary sequence conservation between eukaryotic catalytic subunits and bacterial and archaeal single subunit OSTs (ssOST), structural comparison revealed several common motifs at spatially equivalent positions, like the DXD motif 1 on the external loop 1 and the DXD motif 2 on the external loop 2 involved in binding of the metal ion cofactor and the carboxamide group of the acceptor asparagine, the conserved Glu residue of the TIXE/SVSE motif on the external loop 5 involved in catalysis, as well as the WWDYG and the DK/MI motifs in the globular domain that define the binding pocket for the +2 Ser/Thr of the acceptor sequon. In bacterial ssOSTs, an Arg residue was found to interact with a negatively charged side chain at the -2 position of the sequon. This Arg is conserved in bacterial enzymes and correlates with an extended sequon requirement (Asp-X-Asn-X-Ser/Thr) for bacterial N-glycosylation.
Sequence:
MSDEQTKYSPSIAELARDWYHIPVLSTIILVMLWIRLRSYDAFIREGTVFFSGNDAWYHLRQVEYTVRNWPATMPFDPWTEFPFGRTAGQFGTIYDQLVATAALVVGLGSPSSDLVAKSLLVAPAVFGALTVIPTYLIGKRLGGRLGGLFGAVILMLLPGTFLQRGLVGFADHNIVEPFFMGFAVLAIMIALTVADREKPVWELVAARDLDALREPLKWSVLAGVATAIYMWSWPPGILLVGIFGLFLVLKMASDYVRGRSPEHTAFVGAISMTVTGLLMFIPIEEPGFGVTDFGFLQPLFSLGVALGAVFLAALARWWESNDVDERYYPAVVGGTMLVGIVLFSLVLPSVFDSIARNFLRTVGFSAGAATRTISEAQPFLAANVLQSNGQTAVGRIMSEYGFTFFTGALAAVWLVAKPLVKGGNSRKIGYAVGSLALIGVLFLIPALPAGIGSALGVEPSLVSLTIVTALIVGAVMQADYESERLFVLVWAAIITSAAFTQVRFNYYLAVVVAVMNAYLLREALGIDFVGLANVERFDDISYGQVAAVVIAVLLILTPVLIIPIQLGNGGVSQTAMQASQTGPGTVTQWDGSLTWMQNNTPAEGEFGGESNRMEYYGTYEYTDDFDYPDGAYGVMSWWDYGHWITVLGERIPNANPFQGGATEAANYLLAEDEQQAESVLTSMGDDGEGDQTRYVMVDWQMASTDAKFSAPTVFYDESNISRSDFYNPMFRLQEQGEQTTVAAASSLKDQRYYESLMVRLYAYHGSAREASPIVVDWEERTSADGSTTFRVTPSDGQAVRTFDNMSAAEEYVANDPTSQIGGIGTFPEERVSALEHYRLVKSSNSSALRSGSYQRSLISEGNTYGLQPQALVPNNPAWVKTFERVPGATVDGSGAPANTTVTARVQMRDLTTGTNFTYTQQAQTDADGEFTMTLPYSTTGYDEYGPDNGYTNVSVRAAGGYAFTGPTSVTGNSTIVSYQAENVAVDEGLVNGAEDGTVQVTLERNEQELDLPGDSSSEDSSSEDGTSDGSQTNESASTSTSASVDASAVSAAA
The following text describes a protein:
Function:
Component of the ribosome assembly machinery. Nuclear paralog of the ribosomal protein P0, it binds pre-60S subunits at an early stage of assembly in the nucleolus, and is replaced by P0 in cytoplasmic pre-60S subunits and mature 80S ribosomes.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MSREQQGRRVAKKEIKNRLITNIQEAAQKYSTVFIFYTPVLRSKFMNIIRKDWRDSIFFFGSNKVMQVALGRTEQDEIKPGYHFIAERLKGTCGLCFTNKKKEEILAYFKTQIHDDFARSGSIATMDFVVPEGPLPFEGSLELHLRKNLLPVELKDGILSCKEEYVVCRKGQKLSPQAARLLEYFDIKMAVFEIRVLSIIQDGKFEELESIGEDETMQMEEEEPIN
The following text describes a protein:
Function:
Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to several ligands including TULP1 or GAS6. Regulates many physiological processes including cell survival, migration and differentiation. Ligand binding at the cell surface induces dimerization and autophosphorylation of TYRO3 on its intracellular domain that provides docking sites for downstream signaling molecules. Following activation by ligand, interacts with PIK3R1 and thereby enhances PI3-kinase activity. Activates the AKT survival pathway, including nuclear translocation of NF-kappa-B and up-regulation of transcription of NF-kappa-B-regulated genes. TYRO3 signaling plays a role in various processes such as neuron protection from excitotoxic injury, platelet aggregation and cytoskeleton reorganization. Also plays an important role in inhibition of Toll-like receptors (TLRs)-mediated innate immune response by activating STAT1, which selectively induces production of suppressors of cytokine signaling SOCS1 and SOCS3; (Microbial infection) Acts as a receptor for lassa virus and lymphocytic choriomeningitis virus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope; (Microbial infection) Acts as a receptor for Ebolavirus, possibly through GAS6 binding to phosphatidyl-serine at the surface of virion envelope.
Subcellular Localization:
Cell membrane; Single-pass type I membrane protein.
Sequence:
MALRRSMGRPGLPPLPLPPPPRLGLLLAALASLLLPESAAAGLKLMGAPVKLTVSQGQPVKLNCSVEGMEEPDIQWVKDGAVVQNLDQLYIPVSEQHWIGFLSLKSVERSDAGRYWCQVEDGGETEISQPVWLTVEGVPFFTVEPKDLAVPPNAPFQLSCEAVGPPEPVTIVWWRGTTKIGGPAPSPSVLNVTGVTQSTMFSCEAHNLKGLASSRTATVHLQALPAAPFNITVTKLSSSNASVAWMPGADGRALLQSCTVQVTQAPGGWEVLAVVVPVPPFTCLLRDLVPATNYSLRVRCANALGPSPYADWVPFQTKGLAPASAPQNLHAIRTDSGLILEWEEVIPEAPLEGPLGPYKLSWVQDNGTQDELTVEGTRANLTGWDPQKDLIVRVCVSNAVGCGPWSQPLVVSSHDRAGQQGPPHSRTSWVPVVLGVLTALVTAAALALILLRKRRKETRFGQAFDSVMARGEPAVHFRAARSFNRERPERIEATLDSLGISDELKEKLEDVLIPEQQFTLGRMLGKGEFGSVREAQLKQEDGSFVKVAVKMLKADIIASSDIEEFLREAACMKEFDHPHVAKLVGVSLRSRAKGRLPIPMVILPFMKHGDLHAFLLASRIGENPFNLPLQTLIRFMVDIACGMEYLSSRNFIHRDLAARNCMLAEDMTVCVADFGLSRKIYSGDYYRQGCASKLPVKWLALESLADNLYTVQSDVWAFGVTMWEIMTRGQTPYAGIENAEIYNYLIGGNRLKQPPECMEDVYDLMYQCWSADPKQRPSFTCLRMELENILGQLSVLSASQDPLYINIERAEEPTAGGSLELPGRDQPYSGAGDGSGMGAVGGTPSDCRYILTPGGLAEQPGQAEHQPESPLNETQRLLLLQQGLLPHSSC
The following text describes a protein:
Function:
Flavin prenyltransferase that catalyzes the synthesis of the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3-polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase is metal-independent and links a dimethylallyl moiety from dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms of FMN.
Sequence:
MKLVLGISGASGIPLALRFLEKLPKEIEVFVVASKNAHVVALEESNINLKNAMKDLRPSGTFFNEQDIHASIASGSYGIHKMAIIPASMDMVAKIAHGFGGDLISRSASVMLKEKRPLLIAPREMPLSAIMLENLLKLSHSNAIIAPPMMTYYTQSKTLEAMQDFLVGKWFDSLGIENDLYPRWGMN
The following text describes a protein:
Function:
Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space.
Subcellular Localization:
Mitochondrion inner membrane.
Sequence:
MASSFWNIAYQQAMKSGVLVAKVYSFLHVTTNYLAFPAYAFGPSMIPTLHPSGNVVLAERISKPSRGDVVVFQSPEDPNKLPTKRVVGLEGDSVSFVVDPGKNDESRTIVVPKGHVWVEGDYIQNSRDSRSFGPVPYGLIQGRLLWRVWPFQDFGPIGPPTTT