lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
[Capsid scaffolding protein]: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging; [Assemblin]: Protease that plays an essential role in virion assembly within the nucleus. Catalyzes the cleavage of the assembly protein after formation of the spherical procapsid. By that cleavage, the capsid matures and gains its icosahedral shape. The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging; [Assembly protein]: Plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging.
Subcellular Localization:
[Capsid scaffolding protein]: Host cytoplasm; [Assemblin]: Host nucleus; [Assembly protein]: Host nucleus.
Domain:
Region of interaction between pPR and pAP is called Amino conserved domain (ACD). The region of interaction with major capsid protein is called carboxyl conserved domain (CCD).
Sequence:
MTMDEQQSQAVAPVYVGGFLARYDQSPDEAELLLPRDVVEHWLHAQGQGQPSLSVALPLNINHDDTAVVGHVAAMQSVRDGLFCLGCVTSPRFLEIVRRASEKSELVSRGPVSPLQPDKVVEFLSGSYAGLSLSSRRCDDVEAATSLSGSETTPFKHVALCSVGRRRGTLAVYGRDPEWVTQRFPDLTAADRDGLRAQWQRCGSTAVDASGDPFRSDSYGLLGNSVDALYIRERLPKLRYDKQLVGVTERESYVKASVSPEAACVIKAASAERSGDSRSQAATPAAGARVPSSSPSPPVEPPSPVQPPALPASPSVLPAESPPSLSPSEPAEAASMSHPLSAAVPAATAPPGATVAGASPAVSSLAWPHDGVYLPKDAFFSLLGASRSAAPVMYPGAVAAPPSASPAPLPLPSYPASYGAPVVGYDQLAARHFADYVDPHYPGWGRRYEPAPSLHPSYPVPPPPSPAYYRRRDSPGGMDEPPSGWERYDGGHRGQSQKQHRHGGSGGHNKRRKETAAASSSSSDEDLSFPGEAEHGRARKRLKSHVNSDGGSGGHAGSNQQQQQRYDELRDAIHELKRDLFAARQSSTLLSAALPSAASSSPTTTTVCTPTSELTSGGGETPTALLSGGAKVAERAQAGVVNASCRLATASGSEAATAGPSTAGSSSCPASVVLAAAAAQAAAASQSPPKDMVDLNRRIFVAALNKLE
The following text describes a protein:
Function:
Adapter protein that plays a key role in adaptive immune response by transducing the activation of NF-kappa-B downstream of T-cell receptor (TCR) and B-cell receptor (BCR) engagement. Transduces signals downstream TCR or BCR activation via the formation of a multiprotein complex together with BCL10 and MALT1 that induces NF-kappa-B and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways. Upon activation in response to TCR or BCR triggering, CARD11 homooligomerizes to form a nucleating helical template that recruits BCL10 via CARD-CARD interaction, thereby promoting polymerization of BCL10 and subsequent recruitment of MALT1: this leads to I-kappa-B kinase (IKK) phosphorylation and degradation, and release of NF-kappa-B proteins for nuclear translocation. Its binding to DPP4 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Promotes linear ubiquitination of BCL10 by promoting the targeting of BCL10 to RNF31/HOIP. Stimulates the phosphorylation of BCL10. Also activates the TORC1 signaling pathway.
Subcellular Localization:
Cytoplasm. Membrane raft. Note=Colocalized with DPP4 in membrane rafts.
Domain:
The linker region, also named autoinhibitory interface, is less inhibitory on its own than that of CARD9. The linker region together with the inhibitory domain (ID) are required to prevent constitutive activation and maintain CARD11 in an autoinhibitory state. Disruption of the inhibitory domain (ID) region triggers polymerization and activation, leading to formation of BCL10-nucleating filaments.
Sequence:
MPGGGPEMDDYMETLKDEEDALWENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPELYKLVTGKEPTRRFSTIVVEEGHEGLTHFLMNEVIKLQQQMKAKDLQRCELLARLRQLEDEKKQMTLTRVELLTFQERYYKMKEERDSYNDELVKVKDDNYNLAMRYAQLSEEKNMAVMRSRDLQLEIDQLKHRLNKMEEECKLERNQSLKLKNDIENRPKKEQVLELERENEMLKTKNQELQSIIQAGKRSLPDSDKAILDILEHDRKEALEDRQELVNRIYNLQEEARQAEELRDKYLEEKEDLELKCSTLGKDCEMYKHRMNTVMLQLEEVERERDQAFHSRDEAQTQYSQCLIEKDKYRKQIRELEEKNDEMRIEMVRREACIVNLESKLRRLSKDSNNLDQSLPRNLPVTIISQDFGDASPRTNGQEADDSSTSEESPEDSKYFLPYHPPQRRMNLKGIQLQRAKSPISLKRTSDFQAKGHEEEGTDASPSSCGSLPITNSFTKMQPPRSRSSIMSITAEPPGNDSIVRRYKEDAPHRSTVEEDNDSGGFDALDLDDDSHERYSFGPSSIHSSSSSHQSEGLDAYDLEQVNLMFRKFSLERPFRPSVTSVGHVRGPGPSVQHTTLNGDSLTSQLTLLGGNARGSFVHSVKPGSLAEKAGLREGHQLLLLEGCIRGERQSVPLDTCTKEEAHWTIQRCSGPVTLHYKVNHEGYRKLVKDMEDGLITSGDSFYIRLNLNISSQLDACTMSLKCDDVVHVRDTMYQDRHEWLCARVDPFTDHDLDMGTIPSYSRAQQLLLVKLQRLMHRGSREEVDGTHHTLRALRNTLQPEEALSTSDPRVSPRLSRASFLFGQLLQFVSRSENKYKRMNSNERVRIISGSPLGSLARSSLDATKLLTEKQEELDPESELGKNLSLIPYSLVRAFYCERRRPVLFTPTVLAKTLVQRLLNSGGAMEFTICKSDIVTRDEFLRRQKTETIIYSREKNPNAFECIAPANIEAVAAKNKHCLLEAGIGCTRDLIKSNIYPIVLFIRVCEKNIKRFRKLLPRPETEEEFLRVCRLKEKELEALPCLYATVEPDMWGSVEELLRVVKDKIGEEQRKTIWVDEDQL
The following text describes a protein:
Function:
Telomerase is a ribonucleoprotein enzyme essential for the replication of chromosome termini in most eukaryotes. It elongates telomeres. It is a reverse transcriptase that adds simple sequence repeats to chromosome ends by copying a template sequence within the RNA component of the enzyme.
Subcellular Localization:
Nucleus. Chromosome, telomere.
Sequence:
MARKRKRSWKAPMVLWQIFKNDARNLAKTIAFIIPRPSPPFTCGRCEGRSCLRCCEDPMSFLIRPDDPLDYVNLLNDCFVVVNGDAPFLDFYPDKRWTQEKLVVRVVEMMSSLRLTASNVICSGFNKRTNSSHIVELLTSSAWGILHERVGDKCMFHLLWHTTIFVPISDKKHLQVAGSPVNYFRKKSKEVKNPQSGRKRKRTYGSKSLSNGEFQGSSIQTAEKQKPFSRPFKWKRDKRHRLHSIPESKEESISRTFCFYEDCLPGSLVCLSNPNQATVPCSCYLMLKAPRKVSNSIEISRQSMFYNMECSSSVLPEGHILNTLVPNFSSSKCLMENIFGLTGANVSSQSVPCSHNVECRLKGSSCLYHKFIKLLKMLIRRARRCNHLKLLEKYCPLPSLDQKAGKSRTIVERSIMDKRGIKRSSGGVAKENHNTPETDNAELESTRPYCLKSQVLEFLWAVCRSLVPPELLGTPSNWRLLKRNIFRFIRLRRFEKFSVMQCMHQLKSLDFPLLSDNSNAWVAKNGSELKFGEAICSEHDIKRELLVNWILWFFSSLVVPLVQANFYVTEGECGKLDVFYYRKPVWQEFIDDAVSCLKGRNYLEMDEAAVRAIIRKRPFGFSRLRLCPKQNGVRLLANLNASSKMLQEKSSKFRCSWMRKSSKARSRIFKSKCVKSPNSVLRGVHAILKGLLLKEPEKLGSTVFDYKDVYTKLRPFIITLKNASTTMPGVPGIFIVAADVSKAFDSVDQDKLLRMMEDVIMEKKYILQQNREIVWLKNHLLVRQSLMLVDETVNLGFTNLVSSVSCRSLSGVVVNQGIFTALLKEHLFSHLYQLLKCNVLQLDKKFYLQKLGIPQGSILSTLLCSLYYGHMEKHVIFPYLEKPLEHSTETLSSRPFDSMDAQNSSEDPVIFPPTYLLLRFVDDFLFISTSKEQASGILSMFRQGFPDYNCYMNQEKFCLNFDIEHQSGILSNRAVTGDDSTLFVPWSGLLINSSTLEILGDYTRYLGKHLSSTLTVRWRGQPGNHLKHKLFSFMRPKCHSIFFDSSINSASVVRLNIYQAFLLSAMKFHCYVSELSDFFRPCRQYCLKIILKSFRHMHRLIEKQMALGRLSSGLCWDRKHKVVRDEVEWLGLTAFIEVLKRKQSRHKALLSMLRSKFFCHRITGKESSELRYAVERSHSSCLWKIKY
The following text describes a protein:
Function:
Catalyzes the biosynthesis and metabolism of eicosanoids. Catalyzes the isomerization of prostaglandin H2 to prostacyclin (= prostaglandin I2), a potent mediator of vasodilation and inhibitor of platelet aggregation. Additionally, displays dehydratase activity, toward hydroperoxyeicosatetraenoates (HPETEs), especially toward (15S)-hydroperoxy-(5Z,8Z,11Z,13E)-eicosatetraenoate (15(S)-HPETE).
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass membrane protein.
Sequence:
MSWAVLLGLLAALLLLLLLSRRRARRPGEPPLDLGSIPWLGYALEFGKDAASFLTRMKEKHGDIFTVLVGGRYVTVLLDPHSYETVVWEPRSKLDFHAYAVFLMERIFDVQLPHYNPSDEKAKMKPTLLHRDLQALTEAMYTNLCTVLLGDTTEAGSGWQEMGLLDFSYSFMLRAGYLTLYGVEALPRTPESQAQDRIHSADVFHTFRQLDLLLPKLARGSLSVGDKDQVCVKGHLWKLLSPARLACRAHRSSWLDSYLQHLEEMGASEEMQARALALQLWATQGNMGPAAFWLLLFLLKNPEALAAVRGELEQILLQAEQPVSQMTTLPQKVLDSMPVLDSVLSETLRLTAAPFITREVMVDLALPMADGREFTLRRGDRLLLFPFLSPQKDPEVYTDPEVFQYNRFLNPDGTEKKDFYKDGKRLKNYSVPWGAGHNQCLGRAYATSSIKQFVFLVLTRCDLELTSPDAEIPEFDLSRYGFGLMQPERDVPIRYRLRP
The following text describes a protein:
Function:
Accessory component of the DNA polymerase epsilon complex (By similarity). Participates in DNA repair and in chromosomal DNA replication (By similarity). Has a role in the entrance and progression through S phase. Has a role in endoreplication. Essential for viability and tissue development.
Subcellular Localization:
Nucleus.
Sequence:
MDVDLLPLRKRITNTFKLCGFLIRSENSSYLAEQLLPFDAAERDKWLTVITENLQSQKLLTPHVERAALEKAINELNRVGLDEGETVFALIDAFTVPRFRYNQRIKKFELDTQPRQLLTAPRMKSDYMQQRYAMLLQKTLRHDLFAPAVIQDGVGAEAQAKKFKLQFAENLLATSAMKEAVVLGLLTQLKEGKFYVEDPTGCVQLDLTGARFHAGFFCEGCFVLAEGNYNNGVLKVDGLGFPPAEPANSSRAFFGTANTWGGESAKLLKYSAGLQELERTNTETTIVFLSDVRLDLPVVMEKLRQLFVGYDSCPPQAIVLMGPFTASTRNHHELRHHLDALGGLAAGCEQLKKQTDLILVPSSEDPTAPNILPRAPIPECLAAGLLKAWPRTQLATNPCRLQYCTQQIVVCRLDLMAKFCRNTLHFPEDTSQIEQHFARTIVCQGHLVPIHPIAMPVHWDYDPALWLYPLPDLIVMGDSCQSFSSSQHGCTVLNTGSFVKSKFAFKVYIPATRTIEDSEIPDELE
The following text describes a protein:
Function:
In association with GSP1, required for nuclear export of both pre-40S and pre-60S ribosomal subunits. Required for the late maturation of the 18S and 5.8S rRNA of the pre-40S ribosomes and for maturation of the 25S and 5.8S rRNA of the pre-60S ribosomes.
Miscellaneous:
MISCELLANEOUS: Present with 8170 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus, nucleolus.
Sequence:
MDQDKVAFLLELEDKLAKIRSQVNSKLENQKHIAIILTAVEENIAGQATNDVSKNIVNYIISFMSLLDQAVDPSTHEIKDIQLASSSTYLLDLIFHYSPKVLLRSKFSEILTKIAPCITAEKANAPLIRAAIGCLESLLIAQDAQAWNNTYDLNVTPKRGLQGILELSLDVRPKVRKRALDAVHAVLLNPPVAPTAEHVAAVFVADFCDKQLAGILNDLSNLSNKQLKAQKTKEDINASVMRSLRLITSVVSTGQWPSSQIEPLCDVLLGVTKSSEQYLVSASFECFESMFKTMAETTISSGLAENKYLRVLDTIFALKPSNVDTLLTKSWIAVVIKGMSTYATHQPLKALRKIPGVFHIMCTYLASETPEVYQAASQCLISILSESVKDDLLLYTPSVDEKVFKNVDEIISQIAKTFIDFLSIRYSHCSREILKILVAAFNKFRYRSNPHFLKSLKIVDTWRVNEEQFMDLRNEIELVIGASISAMGPEMILAEAPLNLDNPSSERPGRAWLLPLIRDYTKNANLATFQNELAPYIKSFQSKFDKVPEESIQLRVFQTIVDQIWSTLPRFCELPMDLRESFTDEFASELSSLLYSEVELRTTICHALKVLAESNVSYAEESSSHNVLLLQRFPISEAQKNIEYLSTKSTNLLAVLFNVYTQTTPNARSYILETIDQYLKITSKEDLEKTFNNVCGLLKNSMNEESSGNVNKEKKKPQLTATLLDLIICMITYLPVSSYSALFSMFSLTVNSADALIQKRAYRIITKLSELKSGSTAVAQFISDIENVMVDSASSVQTSAKAARLTAIKTIVELLPLDHLDFIVRTVAEVILSTKDVNEKSRETAFDTLICMGRKMNEPNGIIKLFQIPGYDPTTPDQSSSISEFFKIISAGLIGESQHMVSSSITGYACLVFEFKNELDSGILMDIYDTIELYLTSNSREIVKSAIGFTKVCVLGLPEELMRPKVPELLLKLLRWSHEHTGHFKAKVKHIIERLIRRFGYDYIEANFPEEDRRLLTNIRKMRNRNKRKDEEVTTGVSDVAATKGSRFMSAFDEAVYGSDEENDNGSDQEENVAGGKMKNGAKQFIVESGDNPLDLLDSQTLAHISSTRPKKFNKNQNRARFNDDAFNFDSEGKLVVKGQPKPSTNVDDPLSAVTSGINAYLEAVKSGPVRGQRNKLKFRKNGKDSDEFGDDDDGEKDSRLMRGRVNQGNKIGKHNKKGPKFKSRKKL
The following text describes a protein:
Function:
Essential protein for male fertility. Component of the SCF(ASK-cullin-F-box) E3 ubiquitin ligase complex SCF(FBL17), which mediates the ubiquitination and subsequent proteasomal degradation of target proteins. Enables the switch in cell cycle control leading to male germ cell lineage formation from microspores after meiosis. Targets CDKA-1 inhibitors the degradation specifically in male germ cells (e.g. KRP6 and KRP7) and thus enables CDKA-1 activation and germ cell S-phase progression. Promotes twin sperm cell production and double fertilization.
Subcellular Localization:
Nucleus. Note=Confined to the male germ cell nucleus of early to mid bicellular pollen.
Domain:
The F-box is necessary for the interaction with ASK proteins.
Sequence:
MQPQPHISPNTATAAISAALESQRSRKNRGSYNCGRCGQPKKGHVCLLTAPPDIPTTPIASEPVSCISAAASSSRSTVLSLTAAPSSRQTFTHLRRALSFDDVDARNSLDESDLDAASMDLDLQLDTDIVQPGRFHAVGLWEVLKRLPPSSLLMAARVCKGWRETSRKMWKAAEELRIRVPERAQIGYIGSLLQKCPRLIRLSLKIESDFDATTLACIAFSCPNLEVLEITTSGAAVNRISGDELSRFVANKRGLTSLKMEGCSNLGGFSLSSSSLSTLWLSDLHSLSKMIFNCPNLTEISLEFSRQEDDSTDLVTMVDGLGRTCTRLQNIHIASLKLSHTVVLSLTAVNFRYLRMLSLVLGINITDASVAAISSGYKNLELLDLSGSSITDTGLGMICDVLPDTLSKLLVALCPNITSSGIQFATAQLPLLELMDCGMTVSDPNSDNPTFVENPSPHKTPGYNQKMFIKHKRLKKLSLWGCSSLDALFLNCPELMDLNLNLCSNLHPESLVLQCPKLQLVYASGCQGLLTGAIRKQVSENFSAGENHMPRKRLADASKRIQALPSLYQETREDGIYAGKRRKLEKEMCTIIH
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. It probably triggers the ubiquitin-mediated degradation of different substrates.
Sequence:
METQSAKKARTPPPNVPQEEESTNASNMPRGGTSQEYTVEADGLGCEICFEPFDDQIFMCKNGHPACGTCCIRMDRLCFCTDPIGDIRCRPLEKILAAMTRPCAYVTYGCKEIVSYSGRRSHEKVCPFAPYHCPFDGCTYQGLEVYTHIRDRHAPSAVIVRGGSQRLDVTLEKKTPFRVLLHRDGASVFLLLNGGDVLCGRSLSLVCMGPRPTGNAGVKYKMEVKRRSDPDAPVLWSSGAAPFVRRLKDFHAKGFLFVPDSYWDSYDSVSVTVHLTDGW
The following text describes a protein:
Function:
Contributes to the organization of the actin cytoskeleton and cell shape. Plays a role in the formation of lamellipodia and in cell migration. Plays a role in the regulation of neuron morphology, axon growth and formation of neuronal growth cones. Through its interaction with CTTNBP2, involved in the regulation of neuronal spine density (By similarity). Plays a role in focal adhesion assembly and turnover. In complex with ABL1 and MYLK regulates cortical actin-based cytoskeletal rearrangement critical to sphingosine 1-phosphate (S1P)-mediated endothelial cell (EC) barrier enhancement (By similarity). Plays a role in intracellular protein transport and endocytosis, and in modulating the levels of potassium channels present at the cell membrane (By similarity). Plays a role in receptor-mediated endocytosis via clathrin-coated pits. Required for stabilization of KCNH1 channels at the cell membrane (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, ruffle. Cell projection, dendrite. Cell projection. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell projection, podosome. Cell junction. Cell junction, focal adhesion. Membrane, clathrin-coated pit. Cell projection, dendritic spine. Cytoplasm, cell cortex. Endoplasmic reticulum. Note=Colocalizes transiently with PTK2/FAK1 at focal adhesions. Associated with membrane ruffles and lamellipodia. In the presence of CTTNBP2NL, colocalizes with stress fibers. In the presence of CTTNBP2, localizes at the cell cortex. In response to neuronal activation by glutamate, redistributes from dendritic spines to the dendritic shaft (By similarity). Colocalizes with DNM2 at the basis of filopodia in hippocampus neuron growth zones.
Domain:
The SH3 motif may mediate binding to the cytoskeleton.
Sequence:
MWKASAGHAVSITQDDGGADDWETDPDFVNDVSEKEQRWGAKTVQGSGHQEHINIHKLRENVFQEHQTLKEKELETGPKASHGYGGKFGVEQDRMDKSAVGHEYQSKLSKHCSQVDSVRGFGGKFGVQMDRVDQSAVGFEYQGKTEKHASQKDYSSGFGGKYGVQADRVDKSAVGFDYQGKTEKHESQKDYSKGFGGKYGIDKDKVDKSAVGFEYQGKTEKHESQKDYVKGFGGKFGVQTDRQDKCALGWDHQEKLQLHESQKDYAKGFGGKYGVQKDRMDKNASTFEEVVQVPSAYQKTVPIEAVTSKTSNIRANFENLAKEREQEDRRKAEAERAQRMAQERQEQEEARRKLEEQARAKKQTPPASPSPQPAEDRPPSSPIYEDAAPLKAEPSYGSSEPEPEYSTEAAGLPEASNQQGLAYTSEPVYETTEVPGHYQAEDDTYDGYESDLGITAIALYDYQAAGDDEISFDPDDVITNIEMIDDGWWRGVCKGRYGLFPANYVELRQ
The following text describes a protein:
Function:
Ribosome preservation factor that protect a small pool of nontranslating, vacant ribosomes in cells under nutrient starvation conditions. Under nutrient-limiting conditions, cells reduce ribosome biogenesis and degrade ribosomes via autophagy (ribophagy) or proteasomal degradation. To avoid excessive degradation during starvation, STM1 binds to and protects 80S ribosomes from proteasomal degradation. Under nutrient-sufficient conditions, TORC1 phosphorylates and inhibits STM1 to prevent formation of dormant 80S ribosomes. Acts as an inhibitor of mRNA translation by promoting ribosome hibernation: clamps the two ribosomal subunits, thereby preventing their dissociation, and inhibits translation by excluding mRNA-binding. Acts via its association with eEF2, promoting ribosome stabilization and storage in an inactive state. May also repress translation by preventing association of eEF3 with ribosomes. Binds specifically G4 quadruplex (these are four-stranded right-handed helices, stabilized by guanine base quartets) and purine motif triplex (characterized by a third, antiparallel purine-rich DNA strand located within the major groove of a homopurine stretch of duplex DNA) nucleic acid structures. These structures may be present at telomeres or in rRNAs.
Subcellular Localization:
Cytoplasm.
Sequence:
MSFQNKNLYDLLGNDVEEDAAPSAPSREVVKKNTSSKKSDAAPASADPAKAKKKKSPTGNEAALKNKNFNKDVAPPQSTATKHSKKPFDRHSRTGKTDSKKKLQQGWGQSDKRELEGEVEGTEDAEAELEAEAEENDESANAIPKKSLQEYLAELELSKQELEGSKKLRQANEGAEQKWTAEEKIEKQQEVFFASTHTKKAKSKAQKEKVFLDIDANFGDEQPQTTRGGFRGGKRGGARGGSRGGAKRGGARGAAKPEVNDKNFPSL
The following text describes a protein:
Function:
NAD-dependent protein deacylase. Catalyzes the NAD-dependent hydrolysis of acyl groups from lysine residues.
Subcellular Localization:
Mitochondrion matrix.
Sequence:
MAATKLHPALRNAIRAGANLPTEVISATFDVQEGIKLLSAFLLRHEPVCVLTGAGISTDSGIPDYRSPGRPPHRPLQHLEFLGSHERQQRYWARSLYGYPRIRDTMPNVGHQAINELQRRGLVGAIITQNVDGLHQRAGSQHVIDLHGRLDQVKCMNCHSITTRDELQSRLLADNKALLDQFSVVHDEAVRPDGDAVLDEDLYGRFTVAACASCGGVLKPNVVFFGGSLDPEDVKRASTAVSEASALFVVGTSLATWSAFRIVRQAVEEAKPVCVLNSGPTRADGVIPEYLRLCMPIGEVLPAALRQL
The following text describes a protein:
Function:
Probable thiol-disulfide oxidoreductase that may play a role in proper chloroplast development.
Subcellular Localization:
Plastid, chloroplast.
Sequence:
MQAAAALCFTPPARHACSPSHLSYKPLNYPLFSYTPPTPSLWSAQTLFRKSICKTPAVGKYVREDYLVKKVSANEIQELIKGERNVPLIIDFYATWCGPCILMAQELEMLAVEYENNALIVKVDTDDEYEFARDMQVRGLPTLYFISPDPNKDAIRTEGLIPIQMMRDIIDNDL
The following text describes a protein:
Function:
Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in binding dynein to membranous organelles or chromosomes.
Subcellular Localization:
Cytoplasm, cytoskeleton.
Sequence:
MSKKENVWNQLLFEKSRQGGFINKNLLILGRKCSGKRSLLDALADVTKTLKNGIRQKGITPIVDYAYLNLIDLRDPDYNTNARLNVYILEEEGQKYLLPQILNHKNIKNTFVVIALDMQEPWTFMEDLDRWIGVLQDMMADLRLSLNELEEMKSNVMQYMSQMDGGQAHEGLLKTNLGIPLMVMVNKSDILERDDKGKDWDQKAEIIQFCLRQFCVNYGATLLFTSVKQKINIKVMYEYVLHRLYNMPFETSQHKNLSDFESLFIPLGQDDINIIKSTFTKLANNAIKYEESVPIVQLKKNLVKEELTVEDDQEFFTKLKEKSSQAPATRPILPIQRQVEQPAQQQQTPPADQPLSARGSQQSEQLRNFYKILTGDPIQQAQQQLQDRMRQRTATDIQPQGSATKTTPLFNSQDQQRLQRIFPKK
The following text describes a protein:
Function:
E3 SUMO-protein ligase; has a preference for SUMO2 and SUMO3 and facilitates UBE2I/UBC9-mediated sumoylation of target proteins. Plays a role in protein SUMO2 modification in response to stress caused by DNA damage and by proteasome inhibitors (in vitro). Required for MCM4 sumoylation. Has no activity with SUMO1. Preferentially transfers an additional SUMO2 chain onto the SUMO2 consensus site 'Lys-11'. Negatively regulates transcriptional activation mediated by the SMAD4 complex in response to TGF-beta signaling. Inhibits EP300-mediated acetylation of histone H3 at 'Lys-9'. Plays a role in regulating the transcription of AR targets.
Subcellular Localization:
Nucleus, PML body. Nucleus, nucleoplasm.
Sequence:
MLLFFFFFFFFWFFFSELGTEPRPCASQENFKHKDYIDHQKDKVALTLARLARHVEVEKQQKEEKNRAFREKIDFQHAHGLQELEFIQGHSETEAARQCVDQWLKMSGLRTSAINSGSKKSFQSGGRMRRSDKSILCPIMHCNKEFDNGHLLLGHLKRFDHSPCDPTITLHGPLANVFACAVCYEHFVTQQQYKDHLLSKAAAADGHSNDLPPQIIQCFACPHCFLLFSTKDECLKHMSAKNHFHQSLKLGDDKGTARPVSFPSFAKKLLVSLCKDVPFLVKCVACHQTLRSHMELSAHFRVRCRNAGPVAIAEKSITQVAKEFLVRGYCSDCNQVFMDEASTQSHKNPGHKMSFANSVEESVLLYCHISEGSRPPCDLHLFNQPKISSLKRILSSKESSAEDCVIPTKKVNLGVDSQGGTARVQRQRSTVTAWFCECSRRFPSEDAVEKHVFSANTMCYKCVVCGKVCEDSGVMRLHMSRFHGGAHLNNFLFWCRMCKKELIRKDAIMAHVTEFHSGHRYFYEMDEVEAAVPSSSTENHLNADKPPSPIAVVDHSPASSPPRGRWQCRICEDMFDSHECVQQHCASLTSHRFHRYSCAHCRKTFHKVETLCRHCQDEHSGEVRMMYCCGLCDLIFNKEEAFLSHYTEQHSGDYVFVPEKTKTSIKTEDDFKIIETSNLLSCGCHESYICKVNRRDDYDRCLQIMLEKGKLWFRCGSCSATAQNLADINTHVCQAHRKVRGDEEQQYVIKCGVCTKAFHNTESAQQHFHRKHAAFQKPVTAHVRADHGSTGQLAASVSHAEKNPRHTSYQKCSDVERSAEHDVCCQNIEEEVELPDVDYLRTMTHIVFVDFDNWSNFFGHLPGHLNQGTFIWGFQGGNTNWKPPLGCKVYNYLNRIGCFFLHPRCSKRKDAADFAICMHAGRLDEQLPKQIPFTILSGDQGFLELENQFKKTQRPAHILNPHHLEGDMMCALLNSISDTTKECDSDDSMGVKGSPVEELRATEDVELEEAIRRSLEEM
The following text describes a protein:
Function:
Binds phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2) at the cell membrane.
Subcellular Localization:
Cell tip. Cell membrane; Peripheral membrane protein. Note=Also localizes to the cell division site.
Domain:
The PH 1 domain interacts with membranes containing phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2/PIP2).
Sequence:
MDPGVSSHLRTASLDEARRLPELERVLKSGWLIKKGHATSTKKQLWAVLRRDQLSFYKDEKEYKTKFIFPTQDISAVAYYKEKSPKTFFLYLNEKIIRLIATSNEDAEEWVHVLRSTTGYRAPFSRHPISYILANSSSRTESEPNVQISDTDFDNISTEPRNQTTSPLDLETGQGDHFCTSLYDLIQFGKLRPPGINEENANYPFNPQEVNTLNKHRHSASLQNLYKLLDENKVLMQGTIHWLHGNLHRWSKCWAVVRGYGMTIYNTNREYKPVKVIPIADIQDVAEINVPESSHKYFFTVITQNKPIEFRVDNEDSLILWVAALKTSIDKANGTFTAC
The following text describes a protein:
Function:
Endonuclease that specifically degrades the RNA of RNA-DNA hybrids.
Subcellular Localization:
Cytoplasm.
Sequence:
MKHGFRYEVQTISPEEVDEYNLNKIMDVTYQRILSKFTRDADMRSCRVVLDDYGVGSTLGRYLNFLRNQGAEVIVENKADERYLEVKVASLVSKRIREEIIERINENPDFQIDGLSVGSGNPNDMQTIKWLEKWYESGRDWPWFIRRSYETVRRIEGKPERSKQIPPIKEELLSEEFLEEFNKGRLSIQSLAIICPHCGSINKSVTFAIYEDDGRKISGIKCPKCKKLIENAGITLRYYCGYVVPDTNIVIRGVISKDLESSRFFEGFTIILPNVVRKEADNKKGKQELGKLAELSSIGRIGLECPGKVEGISKI
The following text describes a protein:
Function:
May play a role in the maintenance of the structure of mitochondrial cristae.
Subcellular Localization:
Mitochondrion outer membrane; Multi-pass membrane protein.
Domain:
Its C-terminal part seems to contain many membrane-spanning sided beta-sheets, that have the potential to adopt a transmembrane beta-barrel type structure.
Sequence:
MSEKTFHKAQTIRAKASGVPSIVEAVQFHGVRITKNDALVKEVSELYRSKNLDELVHNSHLAARHLQEVGLMDNAVALIDTSPSSNEGYVVNFLVREPKSFTAGVKAGVSTNGDADVSLNAGKQSVGGRGEAINTQYTYTVKGDHCFNISAIKPFLGWQKYSNVSATLYRSLAHMPWNQSDVDENAAVLAYNGQLWNQKLLHQVKLNAIWRTLRATRDAAFSVREQAGHTLKFSLENAVAVDTRDRPILASRGILARFAQEYAGVFGDASFVKNTLDLQAAAPLPLGFILAASFQAKHLKGLGDREVHILDRCYLGGQQDVRGFGLNTIGVKADNSCLGGGASLAGVVHLYRPLIPPNMLFAHAFLASGSVASVHSKNLVQQLQDTQRVSAGFGLAFVFKSIFRLELNYTYPLKYVLGDSLLGGFHIGAGVNFL
The following text describes a protein:
Function:
[Capsid scaffolding protein]: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein. Cleavages products are evicted from the capsid before or during DNA packaging; [Assemblin]: Protease that plays an essential role in virion assembly within the nucleus. Catalyzes the cleavage of the assembly protein after formation of the spherical procapsid. By that cleavage, the capsid matures and gains its icosahedral shape. The cleavage sites seem to include -Ala-Ser-, -Ala-Ala-, as well as Ala-Thr bonds. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging; [Assembly protein]: Plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging.
Subcellular Localization:
[Capsid scaffolding protein]: Host cytoplasm; [Assemblin]: Host nucleus; [Assembly protein]: Host nucleus.
Domain:
Region of interaction between pPR and pAP is called Amino conserved domain (ACD). The region of interaction with major capsid protein is called carboxyl conserved domain (CCD).
Sequence:
MNPADHPSVYVAGYLALYGADESDELNIDRKDIRAAIPTPAPLPINIDHRRDCTVGAVLALIDDEHGLFFLGKINCPVMVRTLETAASQEIFSELDNLKPDDKLLYIITNYLPSVSLSSRRLAPGETADETFLAHVALCLLGKRIGTIVTYDLTPEEAIEPFRKLSPNSKATLLSQGKETERLLGEMVWYPSKNAITKALLGTAVNNMLLRDRWQIISERRRMAGITGQKYLQASSFTALTDSMTSNNVSVTHPICENANPGNIQKDEEMQVCISPAQTSETLNAGVLSGCNDFHRLPHSDPASTSDQTNLQSLIEPSMNTQSSRPPGDDFIWVPIKSYNQLVSRNASQPTNIPDIAITSNQPPFIPPALMNTSISGQHSIPSGYAQYGYPTPVGTHNSLLPLGPVNQMGGFQYGPQVYPLSYGQSPLEAKLTALLECMTKEKRPVDEEHRGDDMHTTREERGRRGRKRPYEFDRSIESDLYYPGEFRRSNFSPPQASSMKYEETTGGRHDLSQTGPVLNSLMGAVTSLQKEVERLNGGNLPISNAQSSYGVPNGMHAPVYYSYPPPGTHPTVSWPMGVERPMPSTEGKTSTNSTVIPVPVSDPEAGRNVPITATISQERSDGIQKESIEQSRDTMNASAVAGIHRTSDAGVDVFINQMMAHQ