lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Probably involved in the organization of the actin cytoskeleton. May act downstream of CDC42 to induce actin filament assembly leading to cell shape changes. Induces pseudopodia formation, when overexpressed in fibroblasts.
Subcellular Localization:
Endomembrane system; Peripheral membrane protein. Cytoplasm, cytoskeleton.
Sequence:
MPILKQLVSSSVNSKRRSRADLTAEMISAPLGDFRHTMHVGRAGDAFGDTSFLTSKAREADDESLDEQASASKLSLLSRKFRGSKRSQSVTRGDREQRDMLGSLRDSALFVKNAMSLPQLNEKEAAEKDSSKLPKSLSSSPVKKADARDGGPKSPHRNGATGPHSPDPLLDEQAFGDLMDLPIMPKVSYGLKHAESILSFHIDLGPSMLGDVLSIMDKDQWGSEEEEEAGGYRDKEGPSSIVQAPPVLEVVPPLGRQESKASWDQASMLPPHAVEDDGWAVVAPSPSSARSVGSHTTRDSSSLSSYTSGVLEERSPAFRGPDRVAAAPPRQPDKEFCFMDEEEEDEIRV
The following text describes a protein:
Function:
Catalyzes the formation of L-homocysteine from O-succinyl-L-homoserine (OSHS) and hydrogen sulfide.
Sequence:
MDISRPVFFVTVFDETVMSEVPMSKSPATYRPETRLVHSGTLRSQFGETSEALFLTQGYVYNSAEECEARFKGEDPGFIYSRYSNPTISMFERRMIELEGAEAARSAATGMAAVTTAILAPLKTGDHVVASRALFGSCLYVIQDLLPRYGIETTLVDGLDLDQWQRALRPNTKTFFLESPTNPTLDVLDIPGIAEIAHKGGARLVVDNVFATPIWQSPLALGADVVVYSATKHIDGQGRCLGGIILSSEAFVAEHLHNFMRQTGPSISPFNAWVLLKGLETLAVRVRAQTDTAASVAEVLAGHPKISRLIYPGRADHPQAALVKKQMRGGSTLVGFEVKGGKAAAFRVLNELKLAKISNNLGDAKSLVTHPATTTHQRLKPEDRAALGISEGFIRFSAGLEHADDLIEDLTAALEKA
The following text describes a protein:
Function:
Catalyzes the methylation of glycine and sarcosine to sarcosine and dimethylglycine, respectively, with S-adenosylmethionine (AdoMet) acting as the methyl donor. It has strict specificity for glycine and sarcosine as the methyl group acceptors.
Sequence:
MNTTTEQDFGADPTKVRDTDHYTEEYVDGFVDKWDDLIDWDSRAKSEGDFFIQELKKRGATRILDAATGTGFHSVRLLEAGFDVVSADGSAEMLAKAFENGRKRGHILRTVQVDWRWLNRDIHGRYDAIICLGNSFTHLFNEKDRRKTLAEFYSALNPEGVLILDQRNYDGILDHGYDSSHSYYYCGEGVSVYPEHVDDGLARFKYEFNDGSTYFLNMFPLRKDYTRRLMHEVGFQKIDTYGDFKATYRDADPDFFIHVAEKEYREED
The following text describes a protein:
Function:
Catalyzes the transfer of an acetyl group from acetyl coenzyme A (AcCoA) to an acceptor substrate and releases both CoA and the acetylated product. It prefers L-threonine, L-serine and L-methionine. It can also use O-acetyl-L-serine, L-tryptophan, L-isoleucine, L-valine, L-homoserine, 7-aminocephalosporanic acid, thiamine pyrophosphate and thiamine.
Sequence:
MAQNITLQFVEEKDLENLENVKLLFTEYSNSLNIDLCFQDFNNELKTLPGKYKKPSGSLILAFVDENLAGCVALKKLEGKICELKRLYVRNQFRGLKIGKILLEEIIEEAKKFGYTHMRLDTLPSMKSAQGLYEKFGFYDIEPYTYNPIEGARYMELKL
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase. Together with the phosphatase EPM2A/laforin, appears to be involved in the clearance of toxic polyglucosan and protein aggregates via multiple pathways. In complex with EPM2A/laforin and HSP70, suppresses the cellular toxicity of misfolded proteins by promoting their degradation through the ubiquitin-proteasome system (UPS). Ubiquitinates the glycogen-targeting protein phosphatase subunits PPP1R3C/PTG and PPP1R3D in a laforin-dependent manner and targets them for proteasome-dependent degradation, thus decreasing glycogen accumulation. Polyubiquitinates EPM2A/laforin and ubiquitinates AGL and targets them for proteasome-dependent degradation. Also promotes proteasome-independent protein degradation through the macroautophagy pathway.
Subcellular Localization:
Endoplasmic reticulum. Nucleus.
Sequence:
MAAEASESGPALHELMREAEISLLECKVCFEKFGHRQQRRPRNLSCGHVVCLACVAALAHPRTLALECPFCRRACRGCDTSDCLPVLHLIELLGSALRQSPAAHRAAPSAPGALTCHHTFGGWGTLVNPTGLALCPKTGRVVVVHDGRRRVKIFDSGGGCAHQFGEKGDAAQDIRYPVDVTITNDCHVVVTDAGDRSIKVFDFFGQIKLVIGGQFSLPWGVETTPQNGIVVTDAEAGSLHLLDVDFAEGVLRRTERLQAHLCNPRGVAVSWLTGAIAVLEHPLALGTGVCSTRVKVFSSSMQLVGQVDTFGLSLYFPSKITASAVTFDHQGNVIVADTSGPAILCLGKPEEFPVPKPMVTHGLSHPVALTFTKENSLLVLDTASHSIKVYKVDWG
The following text describes a protein:
Function:
Plays a role in targeting PPP1CA to the nucleolus.
Subcellular Localization:
Nucleus, nucleolus.
Sequence:
MARTKCSGVRRGPGGGKGPLKRLRLAVEGFVRATSESEACENRSAVARSRPGDRKSRKELRKKKRQLRKVRRLQRTVGSGSGDQEGNVGLNGGPETRPRIEMRPTPAKATATPVKASAPSANTKASATQPKANSSYSKGTMTSTQAKAKGAPGKPGPATATARKRALLAANEEEDREIRKLERCLGLHKRKKGDGSSVPLSFARDGLDYILGALEYGRSGGLYESSDEEEEGKVETGQTFLESDPESNSEESEEDPDSQVPQEDQEDVNSQKEGETESGTRGNKGNKKVRFAEVVEKSESSLEDDLEHQESHCVESGEKYIPPQLRSEETVDVQKKEELDRLKKHVKGLINRLSEPNMASISGQLEELYMAHSRKYMNDTLTAVLMDACVTTSTMPSRLMMEHVFLVSILHHTVGTEVGACFLEAVVKKFDDVYRDGGEGKELDNLFTMIAHLYNFHVVQSLLIFDILKKLVGTFTERDIELILLMLKNVGFALRKDDALSLKELITEAQAQAIGAGNKFQDQNRVRFMLETMLALKNNDMRKIPGYNPEPVEKLKKLQRALVRNASSGSETQLRISWDGILNAEQTGRWWIVGSAWSGTPMIENHHTHLQKPLAGTASSKMLELARKQRMNTDVRRNIFCTMMTSEDFLDAFEKLLKLGLKDQQEREIVHILMDCCLQEKTYNPFYAFLASKFCAYERRFQVVEFSELDKPRVHFLRRVLTELLMETEDDDLVVIFSRVSSNPKLGMLREGLKLFISHFLLKPAQPQQSAEKASLLRERAGLASKSLQGKAILRM
The following text describes a protein:
Function:
Responsible for the provision of inositol required for synthesis of phosphatidylinositol and polyphosphoinositides.
Miscellaneous:
MISCELLANEOUS: Present with 2440 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MTIDLASIEKFLCELATEKVGPIIKSKSGTQKDYDLKTGSRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETVITDDPTFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKDYDYKSKLESMGSLILNKSVVALQPGSAREGKNFQTKMATYEKLLSCDYGFVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRVVGANPGEWSIDVDNRTYLAVRGTINNESDEQTKYITDFWNCVDGHLKYD
The following text describes a protein:
Function:
Transcription factor.
Subcellular Localization:
Nucleus.
Sequence:
MIHVEEDETLRKGPWTEHEDVQLAFYVNMFGDRRWDFIAKVSGLKRTGKSCRLRWVNYLHPGLKRGRMTPHEERLVLEYHSKWGNRWSRIARKLPGRTDNEIKNYWRTHMRKKAQEHKRVSSPSSSFSNSSSSSSICTNDPTVQSMPMNETKERSFYDTGGIEMVPASRGKNTNTSMKHNKDTSEEQEKIYSMDEIWKDIDLLENDDLKPSFDHYSDVTPSRIWDYSVNSFWMMDGGQQEFGTDMFFPATSELLTG
The following text describes a protein:
Function:
Catalyzes the last step of tRNA splicing, the transfer of the splice junction 2'-phosphate from ligated tRNA to NAD to produce ADP-ribose 1''-2'' cyclic phosphate.
Sequence:
MPAPDPARRDVLISKSLSYLLRHGALKEQLPIDSDGYVPVSAVLAHNRLKSHRCSFSDLQRIVENNEKKRFHMRPGPDGQEYICATQGHTIEQVLPSADVLTQLIDPGELPAQLIHGTNLRNAVLILDSGCIKRMQRNHVHLSHGVTGKDCVISGMRLSSTVHIYLNTEGILDHLRLYKSRNDVYLTPSDIPVSMFKKVVVRTSRNTKADDVTTLTQRLEQLDVPFEISD
The following text describes a protein:
Function:
Metal-dependent single-stranded DNA (ssDNA) exonuclease involved in mitochondrial genome maintenance.
Subcellular Localization:
Mitochondrion.
Sequence:
MAVNIVALAKVPKHFQRLGKNVSLCGRACVRPKSTKSPKTTTVCQEYDGVTRTPVETVNAATAIKRLNFENLSLFGPVLKSTKQRNLDARIGMRLSYLDERVPRRVRTPKLAYEEQLKSARKVRVIETGYRDLPEVEYADSAQAQQLEAIRAEKEAIKVGRFVRKDVPPSGAAFHIPRDRSDKEVTLDFPIFNFLRDDIAAATVDETGDGAVSLETKTEVSSGYPSVTAILRDTMDPLSRRRLELWKERMVAELGQEGFDIYQQLLLNRGKSLHRSIHELLTGRPRDEVSVEPENEGHWASVRGLLEEIGPVRYLETPVSHPHLMYSGIADCVATYRDELVLIDWKTSKKPKPRLSDTFDNPLQVAAYIGALNYDDNYKIQVKDALIAIAYEDGSPCQVHRMGPAVCQRNWERWLQRLRSYWDLASQDARASL
The following text describes a protein:
Function:
May be involved in transcriptional regulation as a weak repressor when alone, or a potent one when fused with a heterologous protein containing a KRAB B-domain.
Subcellular Localization:
Nucleus.
Sequence:
MDSVAFEDVDVNFTQEEWALLDPSQKNLYRDVMWETMRNLASIGKKWKDQNIKDHYKHRGRNLRSHMLERLYQTKDGSQRGGIFSQFANQNLSKKIPGVKLCESIVYGEVSMGQSSLNRHIKDHSGHEPKEYQEYGEKPDTRNQCWKPFSSHHSFRTHEIIHTGEKLYDCKECGKTFFSLKRIRRHIITHSGYTPYKCKVCGKAFDYPSRFRTHERSHTGEKPYECQECGKAFTCITSVRRHMIKHTGDGPYKCKVCGKPFHSLSSFQVHERIHTGEKPFKCKQCGKAFSCSPTLRIHERTHTGEKPYECKQCGKAFSYLPSLRLHERIHTGEKPFVCKQCGKAFRSASTFQIHERTHTGEKPYECKECGEAFSCIPSMRRHMIKHTGEGPYKCKVCGKPFHSLSPFRIHERTHTGEKPYVCKHCGKAFVSSTSIRIHERTHTGEKPYECKQCGKAFSYLNSFRTHEMIHTGEKPFECKRCGKAFRSSSSFRLHERTHTGQKPYHCKECGKAYSCRASFQRHMLTHAEDGPPYKCMWESL
The following text describes a protein:
Function:
Auxiliary subunit of GABA-B receptors that determine the pharmacology and kinetics of the receptor response. Increases agonist potency and markedly alter the G-protein signaling of the receptors by accelerating onset and promoting desensitization.
Subcellular Localization:
Postsynaptic cell membrane. Presynaptic cell membrane.
Sequence:
MSSDIEPFPAVLELNVGGQAYTTALSTLTKDRDSLLAEIFTGRSESDLAHRDSRGRYFIDRDGQLFRYILDYLRTHKLLLPEDFSETSRLYEEARFYRLAGLMSLLGSSPSPHTNAASNSISSNGTPGKAAGFLTIGYRGTFAFGRDGLADVKFRKVSRILVSGKVSLAREVFGDTLNESRDPDRGQSSRYSARFYLKHIYLEQAFDILAGSGFKFVSCCASGTSSQVGPTETEESKWHHYNEFVFQRP
The following text describes a protein:
Function:
Component of centriolar satellites contributing to primary cilium formation (By similarity). In complex with CFAP263, acts as a regulator of ciliary beating that connects radial spoke 3 (RS3) to the inner dynein arm (IDA) and the nexin-dynein regulatory complex (N-DRC). The complex is positioned parallel to N-DRC and forms a connection between the arch at the base of RS3, the IDA tail and N-DRC (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite. Cell projection, cilium. Note=Colocalized with HAP1 at centriolar satellites. Centriolar satellite localization requires PCM1 (By similarity). Localizes at cilium but not at the ciliary tips (By similarity).
Sequence:
MAEMTEDSKSDTARKQLVELVDLNLTSNAALNAEIDLFDRYISRLDLRTFETVWKWQNLSTEKIPGRKAKVRTPGRQQLLTLEQKCVVAKSVYKKMIEDLKIAKIHSEKQLDNYKATLEEADIHLAEIKKERSHFKRNIVEELEDKKSMTMSAEKVMRYIEDKIKAKDILIEKLHRKNSALLTHKKKQQAQLRQQEEMAEGVTVLDFELLKFENIRFRKQLDEQNLKQVNLKLLAVKTLQTLNSNKEKLHILTNESEMLSSDTALRTKLLVKIEEETEQAEEERHKAEALNRKLRDQLADFHVPHVLQYIKLKESHGQLQKSVREWERKVEIAEMALKTYTKSWDKLRFAAGAGLVPI
The following text describes a protein:
Function:
Catalyzes stereospecific hydroxylation of free fatty acids at the C-2 position to produce (R)-2-hydroxy fatty acids, which are building blocks of sphingolipids and glycosphingolipids common in neural tissue and epidermis. Plays an essential role in the synthesis of galactosphingolipids of the myelin sheath. Responsible for the synthesis of sphingolipids and glycosphingolipids involved in the formation of epidermal lamellar bodies critical for skin permeability barrier. Participates in the synthesis of glycosphingolipids and a fraction of type II wax diesters in sebaceous gland, specifically regulating hair follicle homeostasis. Involved in the synthesis of sphingolipids of plasma membrane rafts, controlling lipid raft mobility and trafficking of raft-associated proteins.
Subcellular Localization:
Endoplasmic reticulum membrane; Multi-pass membrane protein.
Sequence:
MIESEQNNGILLSEVKKHNEKSNAWVVIDGQVYDITSFIYDHPGGSDILVEHLGEDISDVFIDGQLHEHSLVAYNMLKQYSIGQLAGYRKPTTKPTVLEYIKNQQKLKQEKQKDGADINNNNNNNNNSNKISYTSDNSIDEKILNSIDVNKAMVPQLKLLEGKNYLKWIHSQTGLNKIIIFDNSILELFTRWPWWYIFILWIPIITACYIYSIIQEKSSVLVSTVIFFIGLFMWSLIEYILHRFVFHLETSSYWGNFFHFFIHGIHHLTPMDHTRLTFPPVFSVFIGYGAYKLFLNFPDFLQITGIPWALYSGIACGYMLYDTFHYYFHHADIDWLPTIFKTIKTNHLNHHFKDDNRNFGVTSPIFDYVFNTI
The following text describes a protein:
Function:
Acts as an activator of serum response factor (SRF)-dependent transcription possibly by inducing nuclear translocation of MKL1 or MKL2 and through a mechanism requiring Rho-actin signaling.
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, myofibril, sarcomere.
Sequence:
MSIACARIDKTIFKFKEMEQNVATQSKDDVYSKDFTQKKMDKSSSEYGRPKPGTLTEQRAKKAAAHVHREMLTLCEVVEDYGKQEKEGDPIRITFGRLFTIYVNISDKVVGTLLRARKHKMIDFEGEMLFQKRDDHVIITLLLSGAQLKEAIRAHAAANPKE
The following text describes a protein:
Function:
Involved in pre-mRNA splicing. May function at or prior to the first catalytic step of splicing at the catalytic center of the spliceosome, together with ISY1. May do so by stabilizing the catalytic center or the position of the RNA substrate.
Miscellaneous:
MISCELLANEOUS: Present with 556 molecules/cell in log phase SD medium.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MSYNGIGLKSAKGSSTSGHVQRSLASNNRRRPQGSQQQRQQRQNAIKKASHDKASRPLAVQKQIETHMEKREIEVQVSELRDRLEEEETLSEEQIDKKCEALRAKLTNEWQEQQRMSSLYTPRKARLTEEQHRHE
The following text describes a protein:
Function:
Component of the ESCRT-0 complex which is the sorting receptor for ubiquitinated cargo proteins at the multivesicular body (MVB) and recruits ESCRT-I to the MVB outer membrane.
Subcellular Localization:
Endosome membrane; Peripheral membrane protein; Cytoplasmic side.
Domain:
The FYVE domain is involved in the binding to phosphatidylinositol 3-phosphate (PtdIns(3)P) which is required for the association to endosomal membranes; Both IUM domains are necessary for efficient binding to ubiquitin.
Sequence:
MAGWFSSASPLDEQIERATASSLEDIALNLEISDLIRSKGVQPKDAMRSLKRRLENKNPNIQIATLKLTDTCVKNGGTHFLAEIASREFMDNLVSLLKAEGVPLNSSVRDLMLALIQDWAMAAQGRMDLSYLGETYRKLQMEGFQFPPKSAISGSMLESSAPPEWIDSDVCMRCRTPFSFMNRKHHCRNCGNVFDAQCSSKTLPLPHLGILQPVRVDDGCYAKLTSKPFNQGSLADRSTFKNNSITKSNVLEPRAARVESGFDEDLRRALQMSLEEAQNKSSSGYVPQPKPAQAPANTQPQPSTDEEEDADLKAAIEASLRDMEEHKQKYAAALKNNTSAESSRETPAAASLPKNPYELSPVEVENIHLFSTLVDRLQHQPPGTILREPQIQELYESIGALRPKLARSYGETMSKHDTLLDLHAKLSTVVRYYDRMLEERLSSAYSQHNLGYGPVPGGAQYPNIYPSMPSTTAEVRPGAENFYYGNSGVEPPAPARTPYSQPPLERENGVVSSSMHPPLQQPSSGPYWNPNNHSIASPQPNVNAFNSNNTPYPGPGAPSQFYTSSAYQEPEKLFQQPRQGEPESPYQPSPVTNRDSYYQSAGLPSNPVEQQPPVDHGQSPGHAQPADSRSSQSGQPKATEPSAQSYYLPQEQQQQQQQQQQQSAQGTGYQGYPQGNTNYQAPYGGDVSPISAPPPVQYQQPAAPRPVVEESLIEL
The following text describes a protein:
Function:
Stereoselective keto-reductase; part of the gene cluster that mediates the biosynthesis of fumagillin, a meroterpenoid that has numerous biological activities including irreversible inhibition of human type 2 methionine aminopeptidase (METAP2). Within the pathway, the keto-reductase af490 acts as a 5-dehydrofumagillol 5-reductase that stereoselectively reduces 5-keto-fumagillol to 5R-hydroxy-seco-sesquiterpene. The pathway begins with the conversion of farnesyl pyrophosphate (FPP) to beta-trans-bergamotene by the membrane-bound beta-trans-bergamotene synthase af520. The multifunctional cytochrome P450 monooxygenase af510 then converts beta-trans-bergamotene into 5-keto-demethoxyfumagillol via several oxydation steps. 5-keto-demethoxyfumagillol is then subjected to successive C-6 hydroxylation and O-methylation by the dioxygenase af480 and O-methyltransferase af390-400, respectively, to yield 5-keto-fumagillol, which is then stereoselectively reduced by the keto-reductase af490 to 5R-hydroxy-seco-sesquiterpene. The next step is the polyketide transferase af380-catalyzed transfer of a dodecapentaenoyl group synthesized by the polyketide synthase af370 onto 5R-hydroxy-seco-sesquiterpene which leads to the production of prefumagillin. Finally, oxidative cleavage by the monooxygenase af470 converts prefumagillin to fumagillin (Probable).
Sequence:
MLGLPNELSGSQVPGATEYEPGWRRVFKVEDLPGLGDYHIDNQTAVPTSIVCVIALAAAMDISNGKQANSIELYDVTIGRPIHLGTSPVEIETMIAIEPGKDGADSIQAEFSLNKSAGHDENPVSVANGRLRMTFAGHELELLSSRQAKPCGLRPVSISPFYDSLREVGLGYSGPFRALTSAERRMDYACGVIAPTTGEASRTPALLHPAMLEACFQTLLLAFAAPRDGSLWTIFVPTQIGRLTIFPNSSVGINTPASVTIDTHLHEFTAGHKADLPMIKGDVSVYSSEAGQLRIRLEGLTMSPIAPSTEKQDKRLYLKRTWLPDILSGPVLERGKPVFCYELFGLSLAPKSILAATRLLSHRYAKLKILQVGTSSVHLVHSLCRELGSSMDSYTIACESDSSMEDMRRRLLSDALPIKYVVLDIGKSLTEGDEPAAGEPTDLGSFDLIILLKASADDSPILKRTRGLIKPGGFLLMTVAATEAIPWEARDMTRKAIHDTLQSVGFSGVDLLQRDPEGDSSFVILSQAVDHQIRFLRAPFDSTPPFPTRGTLLVIGGASHRAKRPIETIQNSLRRVWAGEIVLIRSLTDLQTRGLDHVEAVLSLTELDQSVLENLSRDTFDGLHRLLHQSKIVLWVTYSAGNLNPHQSGAIGLVRAVQAETPDKVLQLLDVDQIDGNDGLVAESFLRLIGGVKMKDGSSNSLWTVEPELSVQGGRLLIPRVLFDKKRNDRLNCLRRQLKATDSFEKQSALARPIDPCSLFSPNKTYVLAGLSGQMGQSITRWIVQSGGRHIVITSRNPDKDDLWTKELEQRGAHIEIMAADVTKKQEMINVRNQILSAMPPIGGVANGAMLQSNCFFSDLTYEALQDVLKPKVDGSLVLDEVFSSDDLDFFLLFSSISAVVGQPFQANYDAANNFMTGLVLQRRARNLPASVINLGPIIGLGFIQNIDSGGGSEAVIATLRSLDYMLVSERELHHILAEAILIGKSDETPEIITGLETVSDNPAPFWHKSLLFSHII
The following text describes a protein:
Function:
Regulatory subunit (beta subunit) of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)), an enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and participates in PAF inactivation. Regulates the PAF-AH (I) activity in a catalytic dimer composition-dependent manner (By similarity). Positively regulates the activity of the minus-end directed microtubule motor protein dynein. May enhance dynein-mediated microtubule sliding by targeting dynein to the microtubule plus end. Required for several dynein- and microtubule-dependent processes such as the maintenance of Golgi integrity, the peripheral transport of microtubule fragments and the coupling of the nucleus and centrosome. Required during brain development for the proliferation of neuronal precursors and the migration of newly formed neurons from the ventricular/subventricular zone toward the cortical plate. Neuronal migration involves a process called nucleokinesis, whereby migrating cells extend an anterior process into which the nucleus subsequently translocates. During nucleokinesis dynein at the nuclear surface may translocate the nucleus towards the centrosome by exerting force on centrosomal microtubules. Also required for proper activation of Rho GTPases and actin polymerization at the leading edge of locomoting cerebellar neurons and postmigratory hippocampal neurons in response to calcium influx triggered via NMDA receptors. May also play a role in other forms of cell locomotion including the migration of fibroblasts during wound healing. Required for dynein recruitment to microtubule plus ends and BICD2-bound cargos. May modulate the Reelin pathway through interaction of the PAF-AH (I) catalytic dimer with VLDLR (By similarity).
Miscellaneous:
MISCELLANEOUS: Originally the subunits of the type I platelet-activating factor (PAF) acetylhydrolase was named alpha (PAFAH1B1), beta (PAFAH1B2) and gamma (PAFAH1B3) (By similarity). Now these subunits have been renamed beta (PAFAH1B1), alpha2 (PAFAH1B2) and alpha1 (PAFAH1B3) respectively (By similarity).
Subcellular Localization:
Cytoplasm, cytoskeleton. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, spindle. Nucleus membrane. Note=Localizes to the plus end of microtubules and to the centrosome. May localize to the nuclear membrane. Redistributes to axons during neuronal development. Also localizes to the microtubules of the manchette in elongating spermatids and to the meiotic spindle in spermatocytes.
Domain:
Dimerization mediated by the LisH domain may be required to activate dynein.
Sequence:
MVLSQRQRDELNRAIADYLRSNGYEEAYSVFKKEAELDMNEELDKKYAGLLEKKWTSVIRLQKKVMELESKLNEAKEEFTSGGPLGQKRDPKEWIPRPPEKYALSGHRSPVTRVIFHPVFSVMVSASEDATIKVWDYETGDFERTLKGHTDSVQDISFDHSGKLLASCSADMTIKLWDFQGFECIRTMHGHDHNVSSVAIMPNGDHIVSAARDKTIKMWEVQTGYCVKTFTGHREWVRMVRPNQDGTLIASCSNDQTVRVWVVATKECKAELREHEHVVECISWAPESSYSSISEATGSETKKSGKPGPFLLSGSRDKTIKMWDVSTGMCLMTLVGHDNWVRGVLFHSGGKFILSCADDKTLRVWDYKNKRCMKTLNAHEHFVTSLDFHKTAPYVVTGSVDQTVKVWECR
The following text describes a protein:
Function:
Microtubule-dependent motor protein required for mitochondrion morphology and transport of mitochondria in neuronal cells.
Subcellular Localization:
Mitochondrion membrane; Peripheral membrane protein.
Sequence:
PHNERENARGATVIINMIDKTTEISNPAEKNEEPKRFSFDYSYWSHDDFTKRESDGYLVPASPRYADQLRVFKDLGQGVLDNAWKGYNCSLFAYGQTGSGKSYSMVGYGANKGIIPVACQELFNTINEKKSGGDTTEFEINFSMLEIYNEQVRDLLNPKGPSVQKGGLKIRQHPSKGFYVEELKNVPVTSYKDIENRMEEGTRNRTIAATNMNATSSRAHTIVAITFKQKTKAKGNQSMTRTSTMNLVDLAGSERAESTGATGDRLKEGSAINLSLTILGNVIKGELKSSNYLLYFILLSVPFRDSALTKLLKNALDGNSKTIMIAALSPADINYDETLSTLRFADRAKSIKTKAVVNESPTEKLIRELKEENARLLAQLKGAGTVQEVKIRQNEREMEEMKKSWEQKLKESTKSQEATEENRLRDKRKTTPHLWNLNEDPQLTGVVVHFVDPGENTIGNSKAEPEPNIVLNGLSIQQQHAIIKFKNDVVTIFPGPDLAKTVVNGEPVTGETILHHNDRIVFGSNHIYVLNYPAEFKAAQETGKEFREVTWDLIQKEIAKSSGFDMDTKGKSKEELLLQEDLMKIMQFISEANAMSEELNKKVVFEIVLVSPQARGLKEGRTEIFVRMRNLLNDASWLWDKDKFINRKFLMQEMYQNFLQTGENKVDKEDEDPFWEPSDAYVLVGSVQVYLETLAYMFDMEESLNITDFKGNQNGIMSISAVPCKADGSDLEEDADDIESPEDLIGKALYFNLNINNIRGLPMKYNKKVYCKYKFYLDTKEYRTKVVEGTINPDFKYTERFSFPTVTNQVNKATLPSINTSTKIKVNGRIF
The following text describes a protein:
Function:
FAD-linked oxidoreductase; part of the gene cluster that mediates the biosynthesis of pyranonigrins, a family of antioxidative compounds. The first step of pyranonigrins biosynthesis is performed by the hybrid PKS-NRPS synthetase that condenses 6 malonyl-CoA units to an acetyl starter unit, to form a 1,3,5-trioxotetradecane-6,8-dienyl-ACP. The enoyl reductase (ER) domain of pynA is likely to be functional during the first two rounds of polyketide chain extension, to generate the saturated C-C bonds of the alkyl side chain (Probable). PynA subsequently forms the amide bond between the acyl chain and L-serine. Although pynA has a terminal reductase domain, it appears to require the thioesterase pynI for the release of the straight-chain intermediate from pynA via the formation of a tetramic acid pyranonigrin J. The methyltransferase pynC then coverts pyranonigrin J to pyranonigrin I via N-methylation. The FAD-dependent monooxygenase pynG catalyzes an epoxidation-mediated cyclization to form the dihydro-gamma-pyrone moiety, followed by pynD-catalyzed oxidation of the alcohol to the ketone and enolization to yield the characteristic tetramic acid-fused gamma-pyrone core of pyranonigrin H. Pyranonigrin H is substrate of pynH for dehydration-mediated exo-methylene formation from the serine side chain to produce pyranonigrin E, before the oxidase pynE reduces the exo-methylene of pyranonigrin E into a pendant methyl to form pyranonigrin G. The FAD-linked oxidoreductase pynB performs the reverse reaction and converts pyranonigrin G back to pyranonigrin E.
Sequence:
MRLSARGFVWSALLACTASALSEAAATASNSSQTLRTCVSQALVAGDVNTRIIDPSNDTYTDARLGEKIQFNEFPALIAYAKKAEEVASLVRCAQRSGFKAVPRSGGHHFEAWSALNGTLVIDLSHINHVNVSADTTTANVGAGIRQGALYLALDEHNVTFPGGICPTVALGGLVSSGGFSLQMRALGLAAEYVQSARVVLADGSLVTASSSSHEDLFWAIRGGGGGTYGIIVDFDLQLMQFPTSAMVAISWNASSDRYPVAQRFFDWAPVQIPAFTSQVNVYKSSINFLGQYLGGTENELRKLINESGLLNIGTPTVYISGNCDTDNSRLFGYTSYECVPANETNRQIMNVLPEPFSQYSDYPQYQYENEPEDPSIPIAEPWARFNRISKSFFMQKDNILPAADLKTVIDMMGQLDTDSEIWGEWHAWNISSATKADYAFPWREQAYAHLEFQVHGSLTNSTKQATYEKWFADLETYLRPKIGVASYSGEMDAHISTNPFESYYGDSVCRLVEVKKAYDPDNFFTNPDAITPTVPEGISC
The following text describes a protein:
Function:
Cytochromes P450 are a group of heme-thiolate monooxygenases. They oxidize a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics.
Sequence:
MVKFDIEMTKKYGPVHGVYFGRQPLMTIYDTSILKQIMIKEAHLFPNHFNTGLFPPFLDNFLFLLKDEHWKHVRSVFSPIFSSGKMRKMTGKINKCCKTLCKNLKVQADMKRTFDLERIYDAFTMDMIASVGFGVSIDSHNDPNNLFVRMARKLIVNKLTLGLVLKFVAPWLLKPLTRLGVPLFEDDYIHFFTDVIKRTIKQKDDDTADGPQKDLDLLQMLIDAQRASANDENLKRNNDNKNNKDDDDDDDDNNADYKPKNDMSWNDSSAHPKGLSDEDLLAQSLQFFLVGFETVSAALSYLCYNLACHQEHQERLFNEVVQIIGNEDPTYDSIKQLTYLDMCLNETLRMFPFATRADRVASQDVTINGLFIPKGMVVGIPINLLHSDPDYWHEPHVFNPERQGHHYNWKVNTVDPMRFIPFGAGPRNCVGMRLAKWEIRWPLSTSSENSGLVFLKKPT
The following text describes a protein:
Function:
Regulator required for centriole duplication.
Subcellular Localization:
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole. Cytoplasm, cytoskeleton, spindle.
Sequence:
MSYLRASRTSSNLSLAKKPSKTRKKLQARKEWDSSVNDLTVFRATNEELEHRREIHRSKNQWLARWELQNKANYKQSEKENSTQFENSRLALMKEILSDQYLMNDVLERSDRALAVVKDLFGDAPRRHTGFPNVTMAPSCDLETSRAPIVRKKDPPTQLSILSESVMDSQAINEVDKSLSRSEYSDSEAEVSISIQPNMKAERVQQLLTGEGPKSEAFITPHKSEGDPSQTQCALNATTAVNRVKVRRTEEESPKPEESDSIIGRVLNPHGKANKRISLKGKKKRTTNQSQTKDFSTFKASERDLTTSNQSSLGLLNSMIMEVEQDLAEYERQTGREVLSAPPAHGLTGFTLSLVSSLKRVVSYLKESDLLLQREVRERQNLQGELVEQRLMLDALTAEILSLKEGGNIHENHSQTKQCPEVDGDKLTSITQEAKTFPGLNGETCRTSADCGLSKVNQFMDSQDVQDTDEKHSRLGVSKDEFGARLYPQGRPAEEPRLASALPSHVFQQAVLLSPPRQKTVGNLSSHSAVPKRAANRLPSPPADLMTAPVEIEWPESKLFQRSINYKNTAALIERGTMVPGQENSKHVYSSAQGSERVNQHPTESTKEVQGLEIGESQINPLQNEDLVSQMQQLALQNAALKAQLEQIHFSPEGNAPEEAAAEQLHNPEPATDTPARAALVPVSLEMRIAELNRQSAEARNKLLKLIEQQKQSIVVSPTLSPITPQGRRTGSSLDTTPLSSCSTSGRRSSGASNKSESISTSVGSLRSASTGRRSQAANDRGEGWFALSAHIS