lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Induces caspases and apoptosis. Counters the protective effect of BCL2; [BH3-interacting domain death agonist p15]: Induces caspase activation and apoptosis (By similarity). Allows the release of cytochrome c (By similarity).
Subcellular Localization:
Cytoplasm. Mitochondrion membrane. Mitochondrion outer membrane. Note=When uncleaved, it is predominantly cytoplasmic (By similarity); [BH3-interacting domain death agonist p15]: Mitochondrion membrane. Note=Translocates to mitochondria as an integral membrane protein; [BH3-interacting domain death agonist p13]: Mitochondrion membrane. Note=Associated with the mitochondrial membrane.
Domain:
Intact BH3 motif is required by BIK, BID, BAK, BAD and BAX for their pro-apoptotic activity and for their interaction with anti-apoptotic members of the Bcl-2 family.
Sequence:
MDSEVSNGSGLGAEHITNLLVFGFLRNNDRDFHQELEVLGQELPVQVYLEGDREDELQTDGSRASRSFYHGRIEPDSESQDEVIHNIARHLAQAGDELDHSIQPTLVRQLAAQFMNGSLSEEDKRNCLAKALDEVKTSFPRDMENDKAMLIMTMLLAKKVASHAPSLLRDVFRTTVNFINQNLFSYVRDLVRNEMD
The following text describes a protein:
Function:
Acts as a component of a SCF E3 ubiquitin ligase complexes.
Subcellular Localization:
Nucleus.
Sequence:
MAQPLPSLSSSPPPWEVILLVAERLDPKTLATASCVCKSWSLSMASDHLWEPIFTANFPSLFNLATAPATSPHVSFRRLFGLGYIAAARRRPAQSKPSLSLSDLVFVISISFTNKDRCSIACDGVNKEEKAPRPQSSLTIVKHGEELPVDRNGLFKFDINLNENGDGAPVVIGAREEVEVVWNIVLEGWRGVFTMIECGGRVGMAPRADGWFSEELPAAGCCPNVVSGGIVGDLRLGLCGNGGGSNKVRIESVSVGMMSVVSWRYVSLDDGLMYLQHFLFNANV
The following text describes a protein:
Function:
Responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids.
Subcellular Localization:
Golgi apparatus membrane; Single-pass type II membrane protein. Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein.
Sequence:
MVQARGIMLKENVKTIGHMIRLYTNKNTTLNGTDYPEANNTSDSLAQTVMYLPENFTYSPFLPCPEKLPYMRGLIDVNMSEISLDEIQEMFSKDLDIEPGGHWKPKDGEPRWKVAILIPFRNRHEHLPIFFRHVIPMLQKQRLEFAFYVVEQTGVQPFNRAMLFNIGFKEAMKDGDWDCIIFHDVDHLPENDRNYYGCGEMPRHFAAKLDKYMYILPYNEFFGGVSGLTVEQFKKINGFPNAFWGWGGEDDDLWNRVHYGGYNVTRPEGELGKYKSIPHHHRGEVQFLGRYKLLRYSRERQYIDGLNNLVYTPTILAMRLYTNITVNLVPELAPVEDY
The following text describes a protein:
Function:
Involved in chromosome condensation, segregation and cell cycle progression. May participate in facilitating chromosome segregation by condensation DNA from both sides of a centrally located replisome during cell division. Not required for mini-F plasmid partitioning. Probably acts via its interaction with MukB and MukE. Overexpression results in anucleate cells. It has a calcium binding activity.
Subcellular Localization:
Cytoplasm, nucleoid. Note=Restricted to the nucleoid region.
Sequence:
MSEFSQTVPELVAWARKNDFSISLPVDRLSFLLAVATLNGERLDGEMSEGELVDAFRHVSDAFEQTSETIGVRANNAINDMVRQRLLNRFTSEQAEGNAIYRLTPLGIGITDYYIRQREFSTLRLSMQLSIVAGELKRAADAAEEGGDEFHWHRNVYAPLKYSVAEIFDSIDLTQRLMDEQQQQVKDDIAQLLNKDWRAAISSCELLLSETSGTLRELQDTLEAAGDKLQANLLRIQDATMTHDDLHFVDRLVFDLQSKLDRIISWGQQSIDLWIGYDRHVHKFIRTAIDMDKNRVFAQRLRQSVQTYFDEPWALTYANADRLLDMRDEEMALRDEEVTGELPEDLEYEEFNEIREQLAAIIEEQLAVYKTRQVPLDLGLVVREYLSQYPRARHFDVARIVIDQAVRLGVAQADFTGLPAKWQPINDYGAKVQAHVIDKY
The following text describes a protein:
Function:
Required for 27S pre-rRNA processing. Has an early role during 60S ribosomal subunit assembly (By similarity).
Subcellular Localization:
Cytoplasm, cytosol. Nucleus, nucleolus.
Sequence:
MSLQTLTKRIRDKNGSREDQIDLANKLFRGEVDVYFPNKEEFIINFLLDRLKENSNLTCVNIGYWQLFLNIWKSDKLSGSFRVSAIRRQSLYPIILNAFEYLIKEFKKDVFLKISDVFVCVYSNLNILYISRSFPDQISLLFSRYCYLIASKIDDLLDSHPNEVFKETLICVIQSAVHSQASSTKAQTQFLHQTLGSILALLCKTQKGDPYFSFLNAVLMKCVLTQHTLDVLLLTKKDSSMTLCSLLNAISFEPINLKAIPLFFIICADSINFHLSSVEKSISQQKASELMYKLFSEHIAFLLSLKNLPEEATLDCMLSICQVFENDNLHRGHSDEYTFAMLEQLLELSVKTLRQNTCWSTSWEMLSSLLAIDFDVLLPHSKILWECIKSVSHQDDIHALKFLKRWVRASAKARILDSFCIDWHLNVQTMSERSILTNRDFITSFSAVAEVSLSQISIKKLVTWLMSSESIMSENSNRFVVYYSLCKSLKRESYPAHLVPNFELFTRSIFNASLKNFNILDERSQALLCMCQISHVQFFSSDMSISASVGMKTLFEDLMAEKSRGLSSTVWSLQLLLCYLEQCLRLNTLHEDTTFPMRVVNYALEYSSKALDKFAENSHLILLDMVDVGKPDLVLTLLCRWLHMVHLYSSRTSITSWIYSIASKFYFIDSLNLETKDSVLESNWERFISSTETYELDSIRDSLIDCLIRLLCYSSNNAIDPVSAPGNLDFDNSAELCSSLTRFTPKNIDFVLKSLIHIPIHSITKNQRTRLLNLLIIHEKLLSDKDNSAHISLRKIIYTLMKTPCSSGFYRDPKIIIDLMQFGKTDLSFHKVHVLIMRSWIQHLDEGNKSEVILKLLQLILADFRELPLETITLIFNALVDSLPTSKHIKNSNDILSSVFTINDMLIDEMTAYLSKKESLCSGTFSCLLACCNSVLRTQNLTSESLNKLHILKVGIEEKAISLKLNELPFLENWILFQCLLSFGGDDFLKVVAYMVYYRRTVGEMSFRVSDFELALSRLSTNDADYAILNILNLLTSNECDEFDYSVLMKVVGVFANYSDCFQRNRHLVHMVLLCCTHVFYNQTLKPATLIDSALDVFLCFVQKTSKFISLDSFNTILTALSTILNLKELECEPKDHANLILKIIQILNGLLFNHRSYMSGRFHVFYSILKSLLYSMVQHDSEMKKIKGIALMNFYKPKKVPIHVVQSFCRLLTTWMNPNLMHDSNKKNSSLTDAERLFVKATTKHFVFLLTDFMSAQTVYQIDIQVKELLTNCFYNVYENLSNHEKQMALVAMNAPSKSLYQKFVNDYLIFAKWNEA
The following text describes a protein:
Function:
Catalytic subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. This subunit contains the active site and the acceptor peptide and donor lipid-linked oligosaccharide (LLO) binding pockets.
Miscellaneous:
MISCELLANEOUS: Present with 3000 molecules/cell in log phase SD medium.
Subcellular Localization:
Endoplasmic reticulum 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:
MGSDRSCVLSVFQTILKLVIFVAIFGAAISSRLFAVIKFESIIHEFDPWFNYRATKYLVNNSFYKFLNWFDDRTWYPLGRVTGGTLYPGLMTTSAFIWHALRNWLGLPIDIRNVCVLFAPLFSGVTAWATYEFTKEIKDASAGLLAAGFIAIVPGYISRSVAGSYDNEAIAITLLMVTFMFWIKAQKTGSIMHATCAALFYFYMVSAWGGYVFITNLIPLHVFLLILMGRYSSKLYSAYTTWYAIGTVASMQIPFVGFLPIRSNDHMAALGVFGLIQIVAFGDFVKGQISTAKFKVIMMVSLFLILVLGVVGLSALTYMGLIAPWTGRFYSLWDTNYAKIHIPIIASVSEHQPVSWPAFFFDTHFLIWLFPAGVFLLFLDLKDEHVFVIAYSVLCSYFAGVMVRLMLTLTPVICVSAAVALSKIFDIYLDFKTSDRKYAIKPAALLAKLIVSGSFIFYLYLFVFHSTWVTRTAYSSPSVVLPSQTPDGKLALIDDFREAYYWLRMNSDEDSKVAAWWDYGYQIGGMADRTTLVDNNTWNNTHIAIVGKAMASPEEKSYEILKEHDVDYVLVIFGGLIGFGGDDINKFLWMIRISEGIWPEEIKERDFYTAEGEYRVDARASETMRNSLLYKMSYKDFPQLFNGGQATDRVRQQMITPLDVPPLDYFDEVFTSENWMVRIYQLKKDDAQGRTLRDVGELTRSSTKTRRSIKRPELGLRV
The following text describes a protein:
Function:
Catalytic subunit in the complex catalyzing the transfer of N-acetylglucosamine from UDP-N-acetylglucosamine to phosphatidylinositol, the first step of GPI biosynthesis.
Sequence:
MPYNIAMVSDFFFPQPGGVESHIYQLSTKLIDRGHKVIIITHAYEDRTGVRYLTNGLKVYHVPFFVMFRSCTFPTVFSFFPIFRNIVIREQIEIVHGHASMSSMCHEAILHARTMGLRTVFTDHSLFGKENTVLRASLDPLMVSVIPNAVVAENFRPLSHPSYPSDPPGKHPPPAPYPLGPHDVITIVVVSRLFYNKGTDLLIAAIPRILASHPNVHFIIAGSGPKAIDLEQMLEKNVLQDKVEMLGPVRHEEVRDVMVRGHIYLHPSLTEAFGTVIVEAASCGLYVVCTQVGGIPEVLPAHMTVFAKPDEDDLVAATGRAIASLRANKVRTEKFHDQVKMMYSWTDVAERTERIYDGIFGVLSEAEFYGYDAADAASWSATRGRAGVQSFALIDRLKRYYGCGIWAGKLFCLCVIIDYLLFLLLEVLAPRDRIDISRSWPKKIPQDSPRRDRETRRDFG
The following text describes a protein:
Function:
Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Acts by mediating the C-terminal thiocarboxylation of sulfur carrier URM1. Its N-terminus first activates URM1 as acyl-adenylate (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to URM1 to form thiocarboxylation (-COSH) of its C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards URM1. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; NFS1 probably acting as a sulfur donor for thiocarboxylation reactions. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. May also be involved in protein urmylation.
Subcellular Localization:
Cytoplasm, cytosol.
Sequence:
MSEPSKEELLARIAQLELENEQLKQQNGKKSQHEQFNKIDDNFSLDEYKRYGRQMIVPQFGSLESQIKLKNSKVLVVGAGGLGSPALLYLSSAGIGKIGIIDPDTVDTSNLHRQVIHNTEMVGEFKCISAQNYINKLNPHVVVEVYPTALNNDNAFGIVSQYDLVLDCTDHPAVRYLINDVCVLLGKTIVSGSGLKSDGQLTVLNFANSGPCYRCFYPQPPSPDSVTSCSDGGVIGPAIGLVGVAMAVETIKIITGYYTKDNFVPFLASYSAYPQQQLRVFKMRKRQKDCAVCGENPQISQRMIEDGTINYKTFCGRATFDPIDDKFRVSPKDYDSVVQNKKKHILIDVRPREQFQITHLPNAINVQWDPTFRKADAIEQYLPDDSTKDDEIYVVCRFGNDSQLAAKKLIGMGYPNVRDIIGGLDKWSDDVDSKIPKY
The following text describes a protein:
Function:
Negative regulator of TLR4 signaling. Does not activate JNK1/MAPK8 pathway, p38/MAPK14, nor ERK2/MAPK1 pathways.
Sequence:
MALPGAEGAVDRPGSPARGAPAASSSSSSASSGGSASASASAGAGLWAALYDYEARGEDELSLRRGQLVEVLSQDAAVSGDEGWWTGQVQRRLGIFPANYVAPCRPAALPASPPARLPPPRPGSPVHVDFELLELKELIGAGGFGQVYRATWQGQEVAVKAARRDPEQDAAAAAESVRREARLFAMLRHPNIIELRGVCLRQPHLCLVLEFARGGALNRALAAANAAPDPSAPGPRRPRRIPPHVLVNWAVQIAQGMLYLHEEAVVPILHRDLKSSNILLLEKIEHDDFCNKTLKITDFGLAREWHRTTRMSAAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTLPIPSTCPEPFAKLMKDCWQQDPHVRPSFASILEQLTAIERAVKTEMPQESFHSMQDDWKLEIQQMFDELRTKEKELRSREEELMRAALQQKSQEELLRRREQQLAEREIDVLERELNILIFQLNQEKPNVKKRKGKFKRSRLKLKDGHRISLPSDFQHKITVQASPNLDKRRSLNSSSSSPPSSPTVIPRLRAIQLTSDESNKTWGRNTVCRQEEFEDVKRNFKKKGCTWGPNSIQMKERADCKERIRPLSDGNSPWSTVLIKNQKTVPLASLFVDQPGVCEETKPASDGLEHRKPKQIKSLSQAYVDLPLWKDGQRENPVEVESWEEGVPVSPATGTPQGTPPNSLSRPSQRKKLESALYGCTVLLASVALGLDIRELAKAQATEEPPAKEEKKKREGIFQWAPKPRSGASPAMRLPTSGEGASSTPSPTLPSAVGLLSMPSLSTKCLLQTDGEDAFESSTHTPGDPDMPTLALCPGFGGRAEEPAPVPGLEVGRSVWGDLPPSFVEQAHGDVPSSASKERAAHHRRTMSDGRAFQPPAGAALVSTPRASELPPAWVWGMPPSWSGPHSDLPREVPPEKQRAIHVVPLPRPSSQRSGAGASPAFPPLGTGSQPAQAGPVVGGPAPAPDQSLDAKERTRAHVPCLLDADVEGQSRDCTVPLCRMGSRAGPPSLYQLEKEFLS
The following text describes a protein:
Function:
Involved in beta-(1-->2)glucan export. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MNQPHSPPGADVPDPAGGPLERATLMGTLAHLWPYIWPGDRFDLKMRVVWSMVLLLAAKLITLTVPFSFKWATDALTGANTAPVLPDNWHLWVIASPLLLTASYGATRILMAVLTQWRDGLFARVAMHAVRKLATITFIHMHELSLRFHLERKTGGLTRVLERGREGIEVIVRMVILQLIPTIVEVSLLLAVLLWQFDWRYVVATLITVAVYMYYTYIATEWRIGIRRKMNDSDTEANTKAIDSLLNYETVKYFGAEAREAQRYDRSVARYEESSVQAYTSLAVLNTGQAVIFTLGLTATMLMCAIGVRNGTNTVGDFVLVNAMMIQLYQPLNFMGMVYREIKQAIIDIEKMFGVLGREAEIKDGPDAQPLVISAGIVRFEDVRFAYEPARPILKGISFEVPAGKTVAIVGPSGAGKSTISRLLFRLYDISGGRILIDGQDIREVTQASLRASIGMVPQDTVLFNDTIRYNIRYGRWDASDAEVEEAARLAQIDNFIRMAPKGYETQVGERGLKLSGGEKQRVAIARTVLKAPPILVLDEATSALDTHTEHEIQGALDRVAKNRTSLVIAHRLSTIVGADEIIVLDQGRIAERGTHAKLLAQGGLYASMWNRQREAEAAREKLAKMADTSEAPNRQPPPVEDALTTPAAAE
The following text describes a protein:
Function:
Arginine methyltransferase involved in the assembly or stability of mitochondrial NADH:ubiquinone oxidoreductase complex (complex I).
Subcellular Localization:
Mitochondrion.
Sequence:
MFISRPVAPSLRLFAKNSLQSITQNSPVRSTALFRCQSNSAVSSSSKPAAKPNELAKVIRDSIKSTGPISASRYMQFCLSHPVHGYYSKGDVFGQKGDFITSPEISQIFGELVAIWFLTRWMEVDSPTRVRIIELGPGRGTLMDDVLRTLFNFPGIAASINSVHLVENSEAMREVQSQTLTPRIKGKDVKLNWYTSIEEIPETKDEFTLFVAHEFFDAMPINVFEKTDMGWREVLIDRDPSYTPNLPTSSTPSGLRFTLSPSPTTLSTILPSTSPRFAKLPSGSRIEVSQDSYKIMHRLGQVVNQGLGGCGLVVDYGADKAFASSFRAFRKHEIVDVFEDPGNCDLTANVDFAYLRESLTGTATPLGPISQAQFLISLGLQPRLRKLLDTAPPERREAIEKGAKRLIDVLGMGSQYQVMGVVSGEPEMKEGIYPFPVKKETVESKVLRP
The following text describes a protein:
Function:
Involved in regulating membrane fusion at the tonoplast and the prevacuolar compartment.
Subcellular Localization:
Vacuole membrane; Peripheral membrane protein. Prevacuolar compartment membrane; Peripheral membrane protein.
Sequence:
MAQIPSLENAPLNLKSIRDKSERELVNLLKDVRGTKCLVIDPKLSGSVSLIIPTSKLKELGLELRHLTAEPVQTECTKVVYLVRSQLSFMKFIASHIQNDIAKAIQRDYYVYFVPRRSVACEKILEQEKVHNLVTVKEFPLYMVPLDEDVISFELELSEKDCLVDGDVSSLWHIAKAIHELEFSFGVISKMRAKGKASVRVADILNRMQVEEPVNSNDVGRPEVDTLILLDREVDMVTPMCSQLTYEGLIDEILHISNGAVEVDSSVMGAQQEGKKMKVPLNSSDKLFKETRDLNFEVVVQVLRQKAMTMKEDYTEINSTQTVSELKDFVKKLNSLPEMTRHIHLAQHLTTFTSKQSFNSQLDMEQTLVEAENYDICYEYIEEMIHKQEPLTNVLRLLVLFSVTNSGLPKKQFDYIRMELLHSYGFEHVVTLNNLEKAGLLKKQEFKSNWLTVKRTLKLIVEDTDTSRPNDIAYVYSGYAPLSIRLIQQAIHSGWRPMEDILKLLPGPHLETKRSGFPSSPSVDSLHGASNGVADGRRSIVLVVFIGGVTFAEISALRYLASKEGMAYDLIVATTKIVNGATLIETFMEKLG
The following text describes a protein:
Function:
Effector that binds transcription regulators in the host plant to suppress the host's innate immune response. Inhibits the host plant transcription regulators CBP60G and SARD1.
Subcellular Localization:
Secreted. Host nucleus.
Sequence:
MRTETASLLLLAALSVAEELTPNDVPLACANMCGPIVELSYKCDVDGTDELRKLKRRKLFSPQQQQQQQQQQQQSAPKAKRQADPEPQAPAPVPSSTNNQQAADVIFIPGSIGKFKTIPTPLPPADTGVPSMAVTPAAPAPTLPVLDLRPTTTPTNLNPNLPILATPILPSVPASTPLATASSTQVPLPVGNEADAGDGVDAGPAPSNSLNGNVGDMVDDAGNLWPGQKGRQAASDLETACICSNTSFNVRRVAGLCGDCLEQVSGDQGPMRAILASCNFTTERYEPEKESLVANVRVEATKPSFTQTAAASYSWRVSGPTWAVVVGAGMLLGMGW
The following text describes a protein:
Function:
Fermentative lactate dehydrogenase.
Sequence:
MKLAVYSTKQYDKKYLQQVNESFGFELEFFDFLLTEKTAKTANGCEAVCIFVNDDGSRPVLEELKKHGVKYIALRCAGFNNVDLDAAKELGLKVVRVPAYDPEAVAEHAIGMMMTLNRRIHRAYQRTRDANFSLEGLTGFTMYGKTAGVIGTGKIGVAMLRILKGFGMRLLAFDPYPSAAALELGVEYVDLPTLFSESDVISLHCPLTPENYHLLNEAAFEQMKNGVMIVNTSRGALIDSQAAIEALKNQKIGSLGMDVYENERDLFFEDKSNDVIQDDVFRRLSACHNVLFTGHQAFLTAEALTSISQTTLQNLSNLEKGETCPNELV
The following text describes a protein:
Function:
Catalyzes the hydrolysis of acyl-CoAs into free fatty acids and coenzyme A (CoASH), regulating their respective intracellular levels. Has acyl-CoA thioesterase activity towards medium (C12) and long-chain (C18) fatty acyl-CoA substrates. Can also hydrolyze 3-hydroxyphenylacetyl-CoA and 3,4-dihydroxyphenylacetyl-CoA (in vitro). May play a role in controlling adaptive thermogenesis.
Subcellular Localization:
Cytoplasm, cytoskeleton, spindle. Cytoplasm, cytosol. Mitochondrion. Nucleus.
Sequence:
MALAAGRAVLEALRSSPGGFDARVLERVEIKAADAGRILCAIRVPANLANGYGTLHGGAIATLIDCVSTMAVLTVGGTNTGVSIDLSITYVSAARIDDELEIESKVLKKGKNVVMLSAEVRRAGKNGEIVASGHHTKYFSRPSLFTSKL
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. Localizes to acetylated damaged chromatin in a ZMYND8-dependent manner, to promote transcriptional repression and double-strand break repair by homologous recombination. Involved in neurogenesis.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Nucleus.
Sequence:
MASGLGSPSPCSAGSEEEDMDALLNNSLPPPHPENEEDPEEDLSETETPKLKKKKKPKKPRDPKIPKSKRQKKERMLLCRQLGDSSGEGPEFVEEEEEVALRSDSEGSDYTPGKKKKKKLGPKKEKKSKSKRKEEEEEEDDDDDSKEPKSSAQLLEDWGMEDIDHVFSEEDYRTLTNYKAFSQFVRPLIAAKNPKIAVSKMMMVLGAKWREFSTNNPFKGSSGASVAAAAAAAVAVVESMVTATEVAPPPPPVEVPIRKAKTKEGKGPNARRKPKGSPRVPDAKKPKPKKVAPLKIKLGGFGSKRKRSSSEDDDLDVESDFDDASINSYSVSDGSTSRSSRSRKKLRTTKKKKKDHQDYCEVCQQGGEIILCDTCPRAYHMVCLDPDMEKAPEGKWSCPHCEKEGIQWEAKEDNSEGEEILEEVGGDLEEEDDHHMEFCRVCKDGGELLCCDTCPSSYHIHCLNPPLPEIPNGEWLCPRCTCPALKGKVQKILIWKWGQPPSPTPVPRPPDADPNTPSPKPLEGRPERQFFVKWQGMSYWHCSWVSELQLELHCQVMFRNYQRKNDMDEPPSGDFGGDEEKSRKRKNKDPKFAEMEERFYRYGIKPEWMMIHRILNHSVDKKGHVHYLIKWRDLPYDQASWESEDVEIQDYDLFKQSYWNHRELMRGEEGRPGKKLKKVKLRKLERPPETPTVDPTVKYERQPEYLDATGGTLHPYQMEGLNWLRFSWAQGTDTILADEMGLGKTVQTAVFLYSLYKEGHSKGPFLVSAPLSTIINWEREFEMWAPDMYVVTYVGDKDSRAIIRENEFSFEDNAIRGGKKASRMKKEASVKFHVLLTSYELITIDMAILGSIDWACLIVDEAHRLKNNQSKFFRVLNGYSLQHKLLLTGTPLQNNLEELFHLLNFLTPERFHNLEGFLEEFADIAKEDQIKKLHDMLGPHMLRRLKADVFKNMPSKTELIVRVELSPMQKKYYKYILTRNFEALNARGGGNQVSLLNVVMDLKKCCNHPYLFPVAAMEAPKMPNGMYDGSALIRASGKLLLLQKMLKNLKEGGHRVLIFSQMTKMLDLLEDFLEHEGYKYERIDGGITGNMRQEAIDRFNAPGAQQFCFLLSTRAGGLGINLATADTVIIYDSDWNPHNDIQAFSRAHRIGQNKKVMIYRFVTRASVEERITQVAKKKMMLTHLVVRPGLGSKTGSMSKQELDDILKFGTEELFKDEATDGGGDNKEGEDSSVIHYDDKAIERLLDRNQDETEDTELQGMNEYLSSFKVAQYVVREEEMGEEEEVEREIIKQEESVDPDYWEKLLRHHYEQQQEDLARNLGKGKRIRKQVNYNDGSQEDRDWQDDQSDNQSDYSVASEEGDEDFDERSEAPRRPSRKGLRNDKDKPLPPLLARVGGNIEVLGFNARQRKAFLNAIMRYGMPPQDAFTTQWLVRDLRGKSEKEFKAYVSLFMRHLCEPGADGAETFADGVPREGLSRQHVLTRIGVMSLIRKKVQEFEHVNGRWSMPELAEVEENKKMSQPGSPSPKTPTPSTPGDTQPNTPAPVPPAEDGIKIEENSLKEEESIEGEKEVKSTAPETAIECTQAPAPASEDEKVVVEPPEGEEKVEKAEVKERTEEPMETEPKGKGAADVEKVEEKSAIDLTPIVVEDKEEKKEEEEKKEVMLQNGETPKDLNDEKQKKNIKQRFMFNIADGGFTELHSLWQNEERAATVTKKTYEIWHRRHDYWLLAGIINHGYARWQDIQNDPRYAILNEPFKGEMNRGNFLEIKNKFLARRFKLLEQALVIEEQLRRAAYLNMSEDPSHPSMALNTRFAEVECLAESHQHLSKESMAGNKPANAVLHKGILKQLEELLSDMKADVTRLPATIARIPPVAVRLQMSERNILSRLANRAPEPTPQQVAQQQ
The following text describes a protein:
Function:
Member of a two-component regulatory system MalK/MalR. Activates transcription of maeA, maeN and yflS in presence of malate by binding to their promoter region.
Subcellular Localization:
Cytoplasm.
Sequence:
MINVLIVEDDPMVGELNKRYLSQIDGFQLKGIASSFQSALHILGEHHIDLILLDIYMPGKNGLELLTELRAQNEAVDVIVISAASELDVIKKTLRYGAVDYLIKPFEFERFQTALSDYRRKQKVYSTHRNMSQKELDAELFQKKEATEKVQLPKGLTKSTLKLIWSSIQSFENESFTTEDLAKHTEISQVSIRKYLKFLEDIQVLNVEMAYGTIGRPVFQYNVNNSNINGIKQYL
The following text describes a protein:
Function:
Catalyzes the oxidative deamination of primary and some secondary amines such as neurotransmitters, and exogenous amines including the tertiary amine, neurotoxin 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP), with concomitant reduction of oxygen to hydrogen peroxide and participates in the metabolism of neuroactive and vasoactive amines in the central nervous system and peripheral tissues. Preferentially degrades benzylamine and phenylethylamine.
Subcellular Localization:
Mitochondrion outer membrane; Single-pass type IV membrane protein; Cytoplasmic side.
Sequence:
MSNKCDVVVVGGGISGMAAAKLLHDSGLNVVVLEARDRVGGRTYTLRNQKVKYVDLGGSYVGPTQNRILRLAKELGLETYKVNEVERLIHHVKGKSYPFRGPFPPVWNPITYLDHNNFWRTMDDMGREIPSDAPWKAPLAEEWDNMTMKELLDKLCWTESAKQLATLFVNLCVTAETHEVSALWFLWYVKQCGGTTRIISTTNGGQERKFVGGSGQVSERIMDLLGDRVKLERPVIYIDQTRENVLVETLNHEMYEAKYVISAIPPTLGMKIHFNPPLPMMRNQMITRVPLGSVIKCIVYYKEPFWRKKDYCGTMIIDGEEAPVAYTLDDTKPEGNYAAIMGFILAHKARKLARLTKEERLKKLCELYAKVLGSPEALEPVHYEEKNWCEEQYSGGCYTTYFPPGILTQYGRVLRQPVDRIYFAGTETATHWSGYMEGAVEAGERAAREILHAMGKIPEDEIWQSEPESVDVPAQPITTTFLERHLPSVPGLLRLIGLTTIFSATALGFLAHKRGLLVRV
The following text describes a protein:
Function:
Metallothioneins have a high content of cysteine residues that bind various heavy metals (Probable). Functions as a metal chelator of copper (Cu) and zinc (Zn). Plays a role in Cu homeostasis in the roots under elevated Cu concentration. Functions cooperatively with the phytochelatin synthase PCS1 to protect plants from Cu and cadmium (Cd) toxicity. Plays a role in Cu homeostasis, specifically in the remobilization of Cu from senescing leaves. The mobilization of Cu from internal sources is important for seed development. Confers tolerance to Cd and plays a role in Cd and Zn homeostasis.
Sequence:
MADSNCGCGSSCKCGDSCSCEKNYNKECDNCSCGSNCSCGSNCNC
The following text describes a protein:
Function:
Cleaves the N-terminal amino acid of tripeptides.
Subcellular Localization:
Cytoplasm.
Sequence:
MKEELLKRFTKYVKVDTQSNEESTVCPTTPGQMELANILVTELKEIGMQEVTVDEFGYVMATLPSNSTKEVPVIGFLAHLDTATDLTGKNVQPQVHENYDGKDIILNKDLNVVLSPKQFPELAGYKGKTLITTDGTTLLGADDKAGITEIMVAMNHLINHPEIKHGKIRIAFTPDEEIGRGPERFDVEAFGAKYAYTMDGGPLGELEYESFNAASAKITFKGNSVHPGTAKNKMVNAVKMAMEFDARIPKDEAPEYTEGYEGFYHLISLNGDVEQARSYYIIRDFDHLKFVERKTHIASIAKELEEKYGEGSVELKLNDQYYNMREKIEPVKEIVDIVSAAMRNLDIEPKISPIRGGTDGAQLSYKGLPTPNIFGGGENFHGKFEYVALESMVKATEVIIEVARLFEEKE
The following text describes a protein:
Function:
Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. mdm10 is involved in the late assembly steps of the general translocase of the mitochondrial outer membrane (TOM complex). Functions in the tom40-specific route of the assembly of outer membrane beta-barrel proteins, including the association of tom40 with the receptor tom22 and small TOM proteins. Can associate with the SAM(core) complex as well as the mdm12-mmm-1 complex, both involved in late steps of the major beta-barrel assembly pathway, that is responsible for biogenesis of all outer membrane beta-barrel proteins. May act as a switch that shuttles between both complexes and channels precursor proteins into the tom40-specific pathway. Plays a role in mitochondrial morphology and in the inheritance of mitochondria.
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.
Sequence:
MREFMNYITNAFYGATGWNEDNKYNELNATSRELIDFPLPRGLRLTLSSLATPHFATSYQLGSVGVVDGSISYLHSSIPLTHIAAQSDKIPLPALLRCYRRLHDLRSPGQQHYILDADPLSGLPPPPQSARALLGAASDAAVAGGALDGGNTDQDLGIYTHSLLYGRLYLPKSLLEGMIIKRFTQALQVQVRAVSEQSLRNGGTILGLVQYDKGKYGLEGLYSTDGGLLGFRGLYNFGGDASSSTCDPWTPTPGENNNNNNNNNNNNNGNAQAGEKERIYGRFSVGGELYYGTLNKSGGMSLGARFATLPAHRGTPLTATLTINPLMGNINATYALLAREYCSLATRVDFNVYSYESEWAVGMELWSNRRPAGFLLGASPSNDFEPEPHPPRKKERSFQAKMEWRLDDPEPEPEPQPTPKTRKNDEYKGVLKARLDNNLRMGLLWEGRAKSLIFSIGTGIDLHKLGEPFRSLGLEVQYSS
The following text describes a protein:
Function:
Removes the phosphate from trehalose 6-phosphate to produce free trehalose. Trehalose accumulation in plant may improve abiotic stress tolerance.
Sequence:
MILSKKAKSTPGAKVENNKFCVSVHFRRVNENNWMELASHVKSVLDKYPKLRVTTGKKVLEIRPDIQWDKGKALEFLLGSLGYTNCEDVFPIYIGDDRSDEDAFKVLRKRGQGLGILVSEIQRDTAASYYLHDPSEVS
The following text describes a protein:
Function:
Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The histones H1.0 are found in cells that are in terminal stages of differentiation or that have low rates of cell division.
Subcellular Localization:
Chromosome. Nucleus.
Sequence:
MTENSTSTPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKRSVAFKKTKKEVKKVATPKKVAKPKKAASKAPSKKPKAAPVKKTKKKPAATPKKTKKPKTVKAKPVKASKPKKAKPVKPKAKSSAKRAGKKK
The following text describes a protein:
Function:
Catalyzes the transfer of galactose to ceramide, a key enzymatic step in the biosynthesis of galactocerebrosides, which are abundant sphingolipids of the myelin membrane of the central nervous system and peripheral nervous system. Galactosylates both hydroxy- and non-hydroxy fatty acid-containing ceramides and diglycerides.
Subcellular Localization:
Membrane; Single-pass membrane protein. Endoplasmic reticulum.
Sequence:
MKSYTPYFMLLWSAVGIARAAKIIIVPPIMFESHLYIFKTLASALHERGHHTVFLLSEGRDIDPSNHYSLQRYPGIFNSTTSDAFLQSKMRNIFSGRLTAVELVDILDHYTKNCDMMVGNQALIQGLKKEKFDLLLVDPNDMCGFVIAHLLGVKYAVFSTGLWYPAEVGAPAPLAYVPEFNSLLTDRMNFLERMKNTGVYLISRMGVSFLVLPKYERIMQKYNLLPAKSMYDLVHGSSLWMLCTDVALEFPRPTLPNVVYVGGILTKPASPLPEDLQRWVDGAQEHGFVLVSFGAGVKYLSEDIANKLAGALGRLPQKVIWRFSGTKPKNLGNNTKLIEWLPQNDLLGHSNIRAFLSHGGLNSIFETMYHGVPVVGIPLFGDHYDTMTRVQAKGMGILLEWNTVTEGELYDALVKVINNPSYRQRAQKLSEIHKDQPGHPVNRTTYWIDYILRHDGAHHLRSAVHQISFCQYFLLDIAFVLLLGAVALYFIVSYVTKFIYRKVKSLCSRSTHSTVNGHYQNGILNGRYKGNGHIKHEKKVK