lhallee/plat_data huggingface dataset:
The following text describes a protein:
Function:
Catalyzes the formation of chlorobenzoyl-CoA via a 2 step reaction. First 4-chlorobenzoate is adenylated by ATP, followed by acyl transfer from the 4-chlorobenzoyl-AMP intermediate to CoA (By similarity). Benzoate, 4-bromobenzoate, 4-iodobenzoate and 4-fluorobenzoate also act as substrates. Inactive towards 4-nitrobenzoate.
Sequence:
MRTAFELVAWSAHRQPGAVALLDPESGHRLTYSELLKRIEGVATVLASRGVVRDELVATAMANTLDHAIILLALNRLGAIPVIINPRLKADEMVQLIRRDNIRTVIRTVAEGKSGTPADIDGVEELTLSAEVLSEGLRIDGNATPAFEAPRPEDPAFVFYTSGTTGLPKGVVIPHRAIEPRVLFMSTQAGLRFGGHNNLLGLMPIHHVIGFFGVFLGSLAFNGTWIPVTAFDPAQAVKWVEELDVTCLFASPTHFDALLATSEFAPEKLKSVDSVIFAGAAINQSILKRLEKCLQVPIVDIYGTTETMNSLFNPDATQERGLRPGYHSRVQFASVSESPSVALPAGVEGELVVDASADATFTHYLNNPEATAAKIVDGWYRTGDSGYVDDSGRVILTGRIDDMINTGAENVHAEEVEQIISRHPAVVEAAVVGLPDTRWGEVVTAVVVVSEPLTADLLDQVCLDSELANFKRPRRYFVVNELPRNAAMKVSRRTLREYLGAHAADQPNPETGFIQFTIEESQ
The following text describes a protein:
Function:
Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN).
Subcellular Localization:
Golgi apparatus, trans-Golgi network.
Sequence:
MCTGITGSHCRYRFSTLLFPCVCLPLWIQGRVFVKSLTGRGEGAYRCVRIIGVLTFLLFVRFPRFVSGMKTNNLERRRQIRQQLRAFYGDNLTAKDEPVTRESGEPDHSSVSMNTRVNSIPPGLDMDSDSFDVGEYTTELFRVKSLKGVVETDAWLARTASRLETELRELVYRNYSKFISATDTIREIRSDVTEMGGRLHALSGNVENIDDVSKDVSGKLQEHRSRIEKVITKHRMLRKAQFLVGLADTMRLHMERKEHSECVRKWVMGDSFIAKHANIPKMAIVHKECKELAMHLYGVLREEVLSVSMENPDASEVIRRIVGELRLLRATSIFGEDKEITPHAGTDGALAPFEEEILSVLKINVREAFVVAVRSFNATIEAALLIPGLSEMHLEERAGVLMRPRLQEALAQLKSSLAIFHSGSEQLCSLFNQRDESAFSKYIIEEVEPVLTDTIVAITTPLGNLLVAIVDAIAKDGSSLLGSPATVQTDLSTVFTTLAKHLMHYSTTMKGLGVTYLNSAMNQHSEKYAEMVDKSVLGVLLKFVNYLETHVTETNDAQKTKLGDDNASDPQKQQEVCFNMCLSRFVLANAAVAADLKSVSAIIESVTSRRSELIDLQKKNARLTRALLRRGIVLSGQFFLNSALPAFSPATAVDPSASTASEHGGIAVCLRNTVVRLGELYNFLKQGVVPSVDDGNTKCASPPAEKHRGNDSASGSTAGGSQLLYSAPGSGRNAGATRATRLAVCFTRKKEDALQASVERIFSKQSQNNAVLQTMPLEFRAASVVAAIAVYLVKGIVEYVRRVTFTRCGFQCVQTSCTFLLHAFTPTALTSSSPAGTSQSLKVTVSLEEWLSDCGDERLLKGLPFLLNECCTCAYERCGEKVPLTAVVVERLVRSVLEEMEGVSVSAEA
The following text describes a protein:
Function:
Regulates the dendritic spine distribution of CTTN/cortactin in hippocampal neurons, and thus controls dendritic spinogenesis and dendritic spine maintenance. Associates with the striatin-interacting phosphatase and kinase (STRIPAK) core complex to regulate dendritic spine distribution of the STRIPAK complex in hippocampal neurons.
Subcellular Localization:
Cell projection, dendritic spine. Cytoplasm, cell cortex.
Sequence:
MATDGASCEPDFSRTPEDPAGAPAAAAAAAAKKEFDVDTLSKPELRMLLSVMEGELEARDLVIEALRARRKEVFVQERYGRFNLNDPFLALQRDYEAGAGDAEKPVCTNPLSILDAVMAHCRKMQARMSTQLAAAENRQKKLEMEKLQLQTLEQEHKKLSARLEDERGKNKHVVLMLVKECKQLSGKIIEEAQKLEEVMASLEEEKKKTNELEEALTAEKQRSAEMEAQMEKQLSEFDTEREQLRAKLNREEAHTTDLKEEIDKMKKMIEQLKKGNDSKPSLSLPRKTKDKRLVSISVGTEGPTSRSVACQTDTMVDSTDPVKKLPLTVPIKPSTASPLVSGNAKGSVCTNATFVKPVIDRQSSYSDLIAPPTPSLPPPSPNRIEENGPSTGSTPVLPSSTSPLPSNAAPSTSPAPSIASQNYSLASSMHSSHSPCANASLHPGPNPRVQAARFRFQGNANDQDQNGNTTQSPPSRDVSPTSRDNLVAKQLARNTVTQALSRFTSPQVGAAVRPGAPHPVEAGTCPPVGRMSLKTPSVPRVDRGNPPPIPPKKPGLSQTPSPPHPQIKVIMDSSRSSNAGAKVDNKTTTSSPSSSPQGIRVINEENLSKSPSPQLPPKPTIDLTVAPAGCAISAMATSQVGAWPSETPGLSQPACSENPLVIPTTIACSSSINPVSASSCRPCASDSLLVTASGWSPSLTPLLMSGGPASLAGRSTLLQQAAAQGNVTLLSMLLNEEGLDINYSCEDGSSALYSAAKNGHTDCVRLLLNAEAQVNTADKNGFTPLCSAAAQGHFKCAELLIAYHADINHAAEGGQTPLYLACKNGNNECIKLLLEAGTDRNVKTSDGWTPIHAAVDSGNVDSLKLLMYYGVTDNGNLMSDMELDSGFFDLDCREKNSDYRTKPIVPTDLINHADKEGWTAAHIAASKGLKNCLEILCSHGGLEAEKRDKCNRTVHDVATDDCKHLLENLNALKIPLRISISEQHPANYSPDDFETENTICALIIRKQTSWDDLSKAMSQALTNHFQAVSSDGWRNPEDLTLNNTTESNIGLNLSSIRSIKLGNISWSIGQILPQSPWDFMRKNKTDHITVFFSGPQEGCLSSVTYASMIPLQMLQNYLRLVEQYHNVIFHGPEGSLQDYIAHQLALCMKQKQRAAGFTCEIVRAEVDAEFSKHQLVELFISSACLIPVKQPPVSKKIIIILEKLENASLSELLGDFLAPLENRSTENPCTFQKGNGTSESYYFHENCFLMGTIAKSRLQGSDLVVQQHFRWVQLRWDGEPMHGLLQRFLRRKVLNKFRGKVPSPCDPVCKTVDWILAVWHQLNSCLSRLGTPEALIGPKYFLSCPVVPGHAQVTVKWMSKLWNAVIAPRVQEAILSRASVKRQVGLGQTTARKHPSQGQQAVVKAALSILLNKAVLHGCPLPRAELDQYIADFKGGSFPLSMVSSYNNCGKKKGDNNSWRKVNTSPRKKSGHSTSQSWSKQEISPEGTKSKNTLQPNCNRIASLMKQNSLENDQPQGLNLEQRLSLGSDDEVDLVKELQSMCSSKSESDISKIVDSRDDLRIFGCSQNSPGFSAAITNPSLPVSQKDVCPLSSSPTVECSISKPKIELGVSRVKSFLPVPRNKVTQCSPNTKRNSSSSSNTRQIEGNNSKEEIWNSRQNVQIEKTHK
The following text describes a protein:
Function:
E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation (By similarity). May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle. Acts as an inhibitor of the AIM2 inflammasome by promoting autophagy-dependent degradation of AIM2 (By similarity). Mechanistically, undergoes autoubiquitination upon DNA stimulation, promoting interaction with AIM2 and SQSTM1/p62, leading to AIM2 recruitment to autophagosomes (By similarity).
Subcellular Localization:
Cytoplasm. Nucleus. Note=In the nucleus, colocalizes with PAX6.
Domain:
The coiled-coil domain and the B30.2 domain are both necessary for interaction with HN and PAX6. They are also involved in MED15-binding; The B30.2 domain may be involved cellular protein quality control by promoting the degradation of insoluble ubiquitinated proteins.
Sequence:
MAAPDLSTNLQEEATCAICLDYFTDPVMTDCGHNFCRECIRRCWGQPEGPYACPECRELSAQRNLRPNRPLAKMAEMARRLHPPSPVPQGVCAAHREPLTTFCGDDLSLLCPICERSEHWTHRVRPLQEAADDLKGRLEKSLEHLRKQMEDAMLFQAQAEETCALWQKMVESQRQNVLGEFERLRRLLAEEEQQLLQKLEEEELEVLPRLREGAARLGQQSTQLAALISELESRCQLPALGLLQDIKDALCRVQDVKLQPPAVVPMELRTVCRVPGLVETLRRFRGDITLDPDTANPELVLSEDRRSVQRGEQRQALPDNPERFDPGPCVLGQERITSGRHYWEVEVGDQTSWALGVCKETANRKEKGELSAGNGFWILVFLGSFYNSNEPAFSPLRDPPKRVGIFLDYEAGHLSFYSATDGSLLFIFPETLFSGTLRPLFSPLSSSPTPMTICRLIGVSGDTLGPQ
The following text describes a protein:
Function:
May be involved in fusion of retrograde transport vesicles derived from an endocytic compartment with the Golgi complex.
Subcellular Localization:
Membrane; Multi-pass membrane protein.
Sequence:
MSAFVDVVKNAVPTAAAVGSNGSIIEEDETQPICPSLSWKQRLIGCGVCMGIGSLLSLLSFGAILRSDVATFAVVYTLGNVASIGGTLFLAGPKTQVQRMFSEGRWVATTVFVIAMGLTLLAALLLSSALLVLLLCLVQFGAMAWYMMSYIPFARTAVKGCLRGVV
The following text describes a protein:
Function:
Protein O-glucosyltransferase. Catalyzes the reaction that attaches glucose through an O-glycosidic linkage to a conserved serine residue found in the consensus sequence C-X-S-X-[PA]-C in epidermal growth factor-like repeats. Regulates Notch signaling by glucosylating Notch in the ER, glucosylation is required for the correct folding and cleavage of Notch.
Subcellular Localization:
Endoplasmic reticulum lumen.
Sequence:
MEDRLRLRKYVLVWLLIVLHSCYFASCGNAADRAVDPKNSRVWGPGVEMPDRATLPARYFFIEPRDADNQKINESQKYDIHIIGQSRFGSCRYRLNQIDRHDGSSIVRYRLAESCSDVTIHVRHNEAHLTGSPFAIPGTLYSEQCYCPQGSVEEWLETVGCPAGDPQIDMDLIPFRAINFSSLRTRMIQQYDKPGSISHCNYVILRNQVHRRCYGQHTGFSKFMDTILLSLARKFTLPDMEMFVNLGDWPLVKKGGPSRTTGPYPIFSWCGSDDTFDIVMPTYDITESTLENMGRVMLDMLSVQRRGLPWADKHAKAFWRGRDARRERLELVALSRRYPELLNASLTNFFFFRDEESEFGPRVAHISMHEFFDYRYQVNVDGTVAAYRLPYLLAGSSVVLKQDSFYYEHFYRKLVPMRHYIPFEADLSNLVQQIEWARENDEKAREIRDNANAFINANLLPLDIYCYHALLFKEYAKYIVSPIQVQPGMEKIEQPEEAYHCPCERTTLPRDEL
The following text describes a protein:
Function:
May function as an adapter protein or regulator of Ras signaling pathways.
Subcellular Localization:
Cytoplasm. Membrane; Peripheral membrane protein.
Sequence:
MEPVETWTPGKVATWLRGLDDSLQDYPFEDWQLPGKNLLQLCPQSLEALAVRSLGHQELILGGVEQLQALSSRLQTENLQSLTEGLLGATHDFQSIVQGCLGDCAKTPIDVLCAAVELLHEADALLFWLSRYLFSHLNDFSACQEIRDLLEELSQVLHEDGPAAEKEGTVLRICSHVAGICHNILVCCPKELLEQKAVLEQVQLDSPLGLEIHTTSNCQHFVSQVDTQVPTDSRLQIQPGDEVVQINEQVVVREERDMVGWPRKNMVRELLREPAGLSLVLKKIPIPETPPQTPPQVLDSPHQRSPSLSLAPLSPRAPSEDVFAFDLSSNPSPGPSPAWTDSASLGPEPLPIPPEPPAILPAGVAGTPGLPESPDKSPVGRKKSKGLATRLSRRRVSCRELGRPDCDGWLLLRKAPGGFMGPRWRRRWFVLKGHTLYWYRQPQDEKAEGLINVSNYSLESGHDQKKKYVFQLTHDVYKPFIFAADTLTDLSMWVRHLITCISKYQSPGRAPPPREEDCYSETEAEDPDDEAGSHSASPSPAQAGSPLHGDTSPAATPTQRSPRTSFGSLTDSSEEALEGMVRGLRQGGVSLLGQPQPLTQEQWRSSFMRRNRDPQLNERVHRVRALQSTLKAKLQELQVLEEVLGDPELTGEKFRQWKEQNRELYSEGLGAWGVAQAEGSSHILTSDSTEQSPHSLPSDPEEHSHLCPLTSESSLRPPDL
The following text describes a protein:
Function:
PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity).
Subcellular Localization:
Plastid, chloroplast thylakoid lumen.
Sequence:
MASISSFGCFPQSTALAGTSSTTRCRTTVAARLADQSDDFAPLRSSGGNCGCVNNSGEFDRRKLLVSSVGLLIGALSYDSKDGDFASASQFADMPALKGKDYGKTKMKYPDYTETQSGLQYKDLRVGTGPIAKKGDKVVVDWDGYTIGYYGRIFEARNKTKGGSFEGDDKEFFKFTLGSNEVIPAFEEAVSGMALGGIRRIIVPPELGYPDNDYNKSGPRPMTFSGQRALDFVLRNQGLIDKTLLFDVELLKIVPN
The following text describes a protein:
Function:
PPIase that acts as a histone chaperone. Histone proline isomerase that increases the rate of cis-trans isomerization at prolines on the histone H3 N-terminal tail. Proline isomerization influences H3 methylation thereby regulating gene expression.
Sequence:
MSGPVAAGVWGRRVPAGGIPILASIDPSAAFRITMAALDPSAPAQTDEENQVLRATLKLIRVPTDFDDEDDEDDYDPEDIEAITARLREAGALPAEELESSEEDDSENEKNGGPSDPVKAKKAKKAALTKKMQQELEDEMEIDNSLTNGVNGKSKGKAKVTDDDDISDEDEDEDDDDEEPEEFVLCTLNPENHYQQPLDITVREGEEVYLCVNGTHDIYVTGNYIILPEQEDSEDDDEDDGLEQLGYDIGSDEDELEIDGMDEDESDELDDLEDPRITEVDSEEEEVPKLVATSKKANKKRPAESEDDATLDDLMSKANGDEKVSKKQAKKLKKNDGQAVAGAEPAKKAEKADAPSSDKKKVQFAKNLELGPTGSPLTKVEAPKAEAKKEAAKGPRVVSGVTVEDKKEGKGKAAKKGDRVEMRYIGKLKNGKVFDSNKKGKPFAFKLGVGQVIKGWDVGVAGMTPGGERRLTIPAALAYGKKGAPPDIPANSDLIFDIKCISVG
The following text describes a protein:
Function:
Involved in vesicular protein trafficking. Mainly functions in the early secretory pathway. Thought to act as cargo receptor at the lumenal side for incorporation of secretory cargo molecules into transport vesicles and to be involved in vesicle coat formation at the cytoplasmic side (By similarity).
Miscellaneous:
MISCELLANEOUS: The lumenal coiled-coil domain is required for the Golgi subcellular location.
Subcellular Localization:
Endoplasmic reticulum membrane; Single-pass type I membrane protein. Golgi apparatus, cis-Golgi network membrane; Single-pass type I membrane protein. Golgi apparatus, Golgi stack membrane; Single-pass type I membrane protein. Note=Cycles between the endoplasmic reticulum and Golgi via COPI and COPII dependent pathways.
Domain:
The cytoplasmic C-terminal domain contains a functional dilysine-retrieval motif, which is involved in the retrograde Golgi-to-ER transport of the protein.
Sequence:
MFLQSQKLWTMLLILAIWSPISHSLHFDLHSGRTKCIAEDIKSNSMTVGKYNIDNPHEGQALPQTHKISVKVTSNSGNNYHHAEQVDSGQFAFSAVEAGDYMACFTAVDHKPEVSLSIDFEWKTGVQSKSWANVAKKSQVEVMEFEVKSLLDTVNSIHEEMYYLRDREEEMQDLNRSTNTKMAWLSVLSFFVCIGVAGMQFLHLKTFFEKKKVI
The following text describes a protein:
Function:
Microtubule inner protein (MIP) part of the dynein-decorated doublet microtubules (DMTs) in cilia and flagellar axoneme. Forms filamentous polymers in the walls of ciliary and flagellar microtubules.
Subcellular Localization:
Cytoplasm, cytoskeleton, cilium axoneme. Cytoplasm, cytoskeleton, flagellum axoneme.
Sequence:
RKEGRGEGGGEAAGTRTRPRTLLYWATNSLDSDSARELAGLGLGHELCCIGHKLAGLGLGHELTGLGLGHELAGLGLDHELAGLGLGHELTLPLWPRFRLNRSARYTVEKDLSDKEAALNIDTFCANLNNNTPDIRYARNVVKVEENSVSPEEWVDFSDANAAKADRQRNNSQALRALVDRILAQVAADERRQKAAADNALRDRVRETKEAKRALEEHLDKVMEQIGSQEKNIAGLRKAIADQEAPAKVAQTRLEARTHRPNVELCRDTAHLRLMREVNEIARNVCRWVVGTSGGRDRAGHGPDPSDLCQAAGGPGPGRAGAQGPPPETALPRGGDPGQGQLHLHRRGPLPPDARVHRHQRLLTWRNVGRDWLIENNKIIIIIISDPSCLSLIAFRVSALGS
The following text describes a protein:
Function:
Component of the PEX1-PEX6 AAA ATPase complex, a protein dislocase complex that mediates the ATP-dependent extraction of the PEX5 receptor from peroxisomal membranes, an essential step for PEX5 recycling. Specifically recognizes PEX5 monoubiquitinated at 'Cys-11', and pulls it out of the peroxisome lumen through the PEX2-PEX10-PEX12 retrotranslocation channel (By similarity). Extraction by the PEX1-PEX6 AAA ATPase complex is accompanied by unfolding of the TPR repeats and release of bound cargo from PEX5 (By similarity). Required for jasmonate biosynthesis. Necessary for the developmental elimination of obsolete peroxisome matix proteins.
Subcellular Localization:
Cytoplasm, cytosol. Peroxisome membrane. Note=Localizes to the peroxisome when interacting with APEM9.
Sequence:
MVERRNPLVLSSTRSTLRSVLNSSQPSSADGDRVLNKDGDLLRGNARLSAGILRWRKDGENVSDAKLDSLDDSALVGLSTQLLKRLSINSGSLVVVKNIEIGIQRVAQVVVLDPPKTTLEDASLTQVPVSDSLHTMLVFPTYDLMGQQLLDQEVAYLSPMLAFNLSLHISCLKSLVHRGNGVLEKYFEAKCDEEFIGKSAEDGSKIGLDLEPVSQVPGYASHLRVSFVKIPECGTIPSLKVNSSFEAEERQGLIDSALQKYFGTDRQLSRGDIFRIYIDWNCGSSICNPCSQRLCSESDDYIYFKVIAMEPSNERFLRVNHSQTALVLGGTVSSGLPPDLLVYRSKVPMPLQEETVNILASVLSPPLCPSALASKLRVAVLLHGIPGCGKRTVVKYVARRLGLHVVEFSCHSLLASSERKTSTALAQTFNMARRYSPTILLLRHFDVFKNLGSQDGSLGDRVGVSFEIASVIRELTEPVSNGDSSMEEKSNSNFSENEVGKFRGHQVLLIASAESTEGISPTIRRCFSHEIRMGSLNDEQRSEMLSQSLQGVSQFLNISSDEFMKGLVGQTSGFLPRDLQALVADAGANLYISQESETKKINSLSDDLHGVDIHQASQIDNSTEKLTAKEDFTKALDRSKKRNASALGAPKVPNVKWDDVGGLEDVKTSILDTVQLPLLHKDLFSSGLRKRSGVLLYGPPGTGKTLLAKAVATECSLNFLSVKGPELINMYIGESEKNVRDIFEKARSARPCVIFFDELDSLAPARGASGDSGGVMDRVVSQMLAEIDGLSDSSQDLFIIGASNRPDLIDPALLRPGRFDKLLYVGVNADASYRERVLKALTRKFKLSEDVSLYSVAKKCPSTFTGADMYALCADAWFQAAKRKVSKSDSGDMPTEEDDPDSVVVEYVDFIKAMDQLSPSLSITELKKYEMLRDQFQGRSS
The following text describes a protein:
Function:
DNA ligase that catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA.
Sequence:
MNGVEVPAKIQKRIERLRQEINDHNYRYYVLSQPTIPDSVYDELFHELEKLEKKYPETITPSSPTQRVGAEPLKVFEPVHHEIPMLSLDNVFDEKGLRAFDKRIRQRLKLDKPFEYVCEPKMDGVALSLLYENGELIRAATRGDGYTGENVTQNTRTIASVPLQLRGNDYPELVEIRGEVLMPREGFAKFNREAEKRGDKTFANPRNAASGSLRQLDPRITAKRPLIFYGYLIGLLKGKDFPKNHCDVLKWFKDWGIPVISEIKVVGGIEGCLDYYEHLVKTREKMPFDIDGIVIKVNSLQVQAELGFVSRAPRWAIAYKFPAQEKMTVVKAIEFQVGRTGAVTPVARLEPVSVSGVTVSNATLHNFDELYRKDVRVGDTVIVRRAGDVIPEVVGPILAKRPKKAKLIKIPSRCPVCHAEVIKPEGEAVARCVGGLYCRAQLRESIKHFASRRALDIEGLGDKLVELFIQEKLIKDITGIYQLKKSAITALPRMGEKSAENLLTAIEKSKKTTLPRFLYALGIRGVGDTTARTLARHFHELDLLMKASIETLQEIRDIGPVAAENIHAFFHQKNNAELINKLIHLGVHWPQEKAVVKSEIAGKTFVLTGALKSLTREEAEEKIERSGGKATSSVSKNTDYVIVGENPGSKYEKAKALGISLIDEEAFLKLLKS
The following text describes a protein:
Function:
Catalyzes the condensation of pyruvate and acetyl-coenzyme A to form (R)-citramalate. Shows strict substrate specificity for pyruvate. Cannot use alpha-ketoisovalerate, alpha-ketobutyrate, alpha-ketoisocaproate, alpha-ketoglutarate or glyoxylate.
Domain:
Contains a catalytic N-terminal domain and a C-terminal regulatory domain, linked together by a flexible region. The catalytic domain consists of a TIM barrel flanked by an extended C-terminal region. The active site is located at the center of the TIM barrel near the C-terminal ends of the beta-strands and is composed of conserved residues of the beta-strands of one subunit and the C-terminal region of the other.
Sequence:
MTKVETRLEILDVTLRDGEQTRGVSFSTSEKLNIAKFLLQKLNVDRVEIASARVSKGELETVQKIMEWAATEQLTERIEILGFVDGNKTVDWIKDSGAKVLNLLTKGSLHHLEKQLGKTPKEFFTDVSFVIEYAIKSGLKINVYLEDWSNGFRNSPDYVKSLVEHLSKEHIERIFLPDTLGVLSPEETFQGVDSLIQKYPDIHFEFHGHNDYDLSVANSLQAIRAGVKGLHASINGLGERAGNTPLEALVTTIHDKSNSKTNINEIAITEASRLVEVFSGKRISANRPIVGEDVFTQTAGVHADGDKKGNLYANPILPERFGRKRSYALGKLAGKASISENVKQLGMVLSEVVLQKVLERVIELGDQNKLVTPEDLPFIIADVSGRTGEKVLTIKSCNIHSGIGIRPHAQIELEYQGKIHKEISEGDGGYDAFMNALTKITNRLGISIPKLIDYEVRIPPGGKTDALVETRITWNKSLDLEEDQTFKTMGVHPDQTVAAVHATEKMLNQILQPWQI
The following text describes a protein:
Function:
Involved in mitochondrial or peroxisomal functions and amino acid signaling pathways.
Subcellular Localization:
Vacuole membrane; Peripheral membrane protein. Cytoplasmic vesicle membrane; Peripheral membrane protein. Note=Vesicular and vacuolar.
Domain:
May contain a beta-propeller domain involved in specific binding to phosphatidylinositol 3,5-bisphosphate (PIP2), leading to the association of the protein to the membrane.
Sequence:
MKTRNPIVVQRKNGPPRFLHVNFNQDQECFSCATEKGFEIYNTDPIQCSVKRRFSHNGMSGIGYTRMLYRTNYIGLVGGGASPRFSTNKIAIWDDIQQRDSVSIRFNSPVHELFLSRQYIVVVLAQSIDVYTFSGSPSRVCPVISNIHNGIADFVTCSKMRRASGPQDVEHALSQKHVIAGILAYPSGIRPGQIHIADLSNIQTPSVADASATHLPTSIIKAHKNPIHLVKLSPQGTMVATCSVEGTLIRVFSIASGSLIHEFRRGLDRALIYDMQWNGKGDKLAVVSDKFTLHIFQINEDLDKRHLLKGWFPKVKYLQGVWSMCSTKLDRSLLTHDEDTCKVGWIGDEALSLLWQKSGMWEKYVIMEKLREYKVDETLHSGAPDGRRQLYDLVRESWRQL
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:
MGRVPVPRSDSVRVAVRVRPFSQREKNSGSQCVISMHSGNISIRDPKNEERVKTFTFDLTYWSHDGFQKDEDGVLIPSDPASKFAGQSDVFHDIGRGILDSAWRGYNATLLAYGQTGSGKSYSMIGFGTNKGLIPRVCEELFQAIEKQKENLEPQVMFSMLEIYNEQIRDLLSRTKAPGGLRVREDQQLGFFVEGLKWVPCENYAQIEKLVEQGSKIRMTASTNMNASSSRSHMLIAIQFKQVFLDTALTKRSSINMVDLAGSERQRSSGSEGDRLREGSRVNLSLTSLGNVISALADLAMGKKVLHIPYRDSVLTKLLQSALGGNSRTTLIAALSPADICYEETLSTLRYAERAKKVRNRAVINTCPLARASRAENALLLGFRGAGAAEHPACFWAEQQLGNQGTWAQLLEQARREWEEQYEALTQEQKMVRILPHLLNVNEDPQLTGVLKFFIHNGSCDVGRAASNAICLQGLGISDKHASFVNLDGKVTVAPHSKCKVIVNGVPVTGRTKLQHLDRIILGSNSAFLYVGFPSERGAEDLSRFDYDFFQLERAAAEGVSVATLGCVSPGDDQADPSILAVFQDYVKLMPLVVEANQMSEELKKGLTMELKVKNLASSDSRGYDLQKEVMVKVTKQGTHEVWIWSKAKFINRKFLMEELYQRFLESRDSHVAQEDDPFWDPLEVVHLGSAHVWLQPLAHCMMLEEQVEFLNCDGLEEAVLHIRITPCSPEGWAHGEEDMVIDPLELLGKRIDFQTHIVRCLGVKWLKEDGSRGIQMGYGIYDLPNTLYTKPVWKSVNPRIEETVHFAALGASREFLDYLLTNALIVDLWGLQEGCAPLGVSQLDVLLTGEGHIMVDTKTFSSVKDVSQITSNQVPELYQKLLKLEQETELLRDVNRALRGENVFLKASLENAGSAPQAQKLDNPEGATRTAAREAKQVCAQQASSDAQLARALKVFYQGMGVARGQLLRLRRCRPPEDDQMLRPFVHQQSQMLKDLEDLLESSLHKLKADVAFIVKKRKEYLLPSQQ
The following text describes a protein:
Function:
Component of the integrator complex, a multiprotein complex that terminates RNA polymerase II (Pol II) transcription in the promoter-proximal region of genes. The integrator complex provides a quality checkpoint during transcription elongation by driving premature transcription termination of transcripts that are unfavorably configured for transcriptional elongation: the complex terminates transcription by (1) catalyzing dephosphorylation of the C-terminal domain (CTD) of Pol II subunit Polr2A/Rbp1 and Spt5, and (2) degrading the exiting nascent RNA transcript via endonuclease activity. The integrator complex is also involved in the 3'-end processing of the U7 snRNA, and also the spliceosomal snRNAs U1, U2, U4 and U5.
Subcellular Localization:
Cytoplasm. Nucleus.
Sequence:
MNEQQTRRIQKLMKINLKCETPPELVARLANDSIVLDSRITGKSDKEVIDIMISKEEHDVKSIGLMYHILTSGENPDLFGKMIRYVTGGGAEYWHHVLCNMNMILFEVWPFLHLLCKEQLLRLIREAVRQNVKQVENVLMNAFRMSIGSSDFATKQRIFMKLNSMIRENEAWFKSQKACAALVANILTCTTSVIISSPAPISSQDTFRESQLDLVQWVIKSRKIDCLTLGRDFILILIRLGKMPQIEEIWKDIVANPASFGVSNLEEYMTKQNVLQHVRISIELERKVQFMVVNGGKNLLTYFTWLNNKFFRANDGPALRAECVRYVLSMNLDPAKALPNAQENRVQLLHLLISTVPSGPELQWLKLCLFADWFGCDDKNSANLMCVENSFSVVRYALFLTPTGPQQNSIVQGSHCSQFANSLLEFLCKSVDVLLPPAYAEPIRRNVNSAMRFIKDRLQHNLPQILENSKIDRKVSELLRNVFPDFVRNPIGNSSIIRPKKKSTDEEKAIKSSSEPALSEQKSTEKPSFSTEKLSSDSATTKIEKEKLKKAIEEQEEQELNVLIKQLQGEIGTKIAKLKDQWKEFDDDADKCEAVEGLLVSLLTTGDVFDESQQELAAQCLLGIMGSVVADEQSLLPPNEKDLSEAFTHPIYSFLKVLCSPPDNDEASSDVMAAMMAAMREKDSSLTYVFLYFIKGTAGGRPTECIECYKNIAKMSGRSVDEMLASDLQLCAVNDNRLFAYLVPFVFSQFEEEVMSTPALLATLCANLDAIQLRSFVSEIIREEIKIFRKESFPKMVMDSVDWATTPQWVFWHLVHADGVPIEWFLSTIPKFDAVGHDEAIANILLMMKRMDREPWAGLIRALFNRVPNKDDTFTIDAMKVLIEDSEQCQKVAEIVAQLIKKLLGNNDIIGLGVRVHKKGNPMKLTLQQVLEHLQHFSSTCVEKKQRMTETFMSRSHLQEAFASIKVNDKAVVLVKKYGNLFGAMDIIAQDTKEHSSSRTLRGNRQGTSAERQQMQQMHHQKRKPNEDDEQNSKKRKMHNNIIELSDDSDSD
The following text describes a protein:
Function:
Transcription factor acting as central integrator of phosphate starvation responses. Regulates FER1 expression upon phosphate starvation, linking iron and phosphate homeostasis.
Subcellular Localization:
Nucleus.
Sequence:
MTLANDFGYSTAMSSSYSALHTSVEDRYHKLPNSFWVSSGQELMNNPVPCQSVSGGNSGGYLFPSSSGYCNVSAVLPHGRNLQNQPPVSTVPRDRLAMQDCPLIAQSSLINHHPQEFIDPLHEFFDFSDHVPVQNLQAESSGVRVDSSVELHKKSEWQDWADQLISVDDGSEPNWSELLGDSSSHNPNSEIPTPFLDVPRLDITANQQQQMVSSEDQLSGRNSSSSVATSKQRMRWTPELHEAFVEAVNQLGGSERATPKAVLKLLNNPGLTIYHVKSHLQKYRTARYKPETSEVTGEPQEKKMTSIEDIKSLDMKTSVEITQALRLQMEVQKRLHEQLEIQRSLQLQIEKQGRYLQMMFEKQQKIQDNKSSSSEASPKQCNGSFAEVEVGLETLTGDQNESASASRKRVRED
The following text describes a protein:
Function:
Involved in protein export. Participates in an early event of protein translocation.
Subcellular Localization:
Cell membrane; Multi-pass membrane protein.
Sequence:
MLNGVILTLFVFVSLFLVLLVMIQTGKGGGLLGGGSSQSVFGSSTADVLTKATRVTAILFIVLSLLLSFLFAKKEDKLMPETTPTLTAPPEETKSETNTQNPDSTLPKASP
The following text describes a protein:
Function:
The central subunit of the protein translocation channel SecYE. Consists of two halves formed by TMs 1-5 and 6-10. These two domains form a lateral gate at the front which open onto the bilayer between TMs 2 and 7, and are clamped together by SecE at the back. The channel is closed by both a pore ring composed of hydrophobic SecY resides and a short helix (helix 2A) on the extracellular side of the membrane which forms a plug (By similarity).
Subcellular Localization:
Plastid, cyanelle thylakoid membrane; Multi-pass membrane protein. Plastid, cyanelle inner membrane; Multi-pass membrane protein.
Sequence:
MLSRLIISIFIIFETIYLQIFKPVNKTFKQGEAKLKRTLQTLQSRELSEIRKRAISTLCLIFLIRIGTFLPIPGTALNFDLESFQQNNSRNELANILNLLSGGAFLEIGFFTLGILPYMNASFFLQVLTKILPSLERFQKEQEEIAQREFKKWTRYLTVIWAFIQSIVISWIWIRPYALNWDFFLGLKVVVALTLGAVIVMIIAEQITEIGLTNGSSLLIFINIIARIPNSIEQLFNSNINWTFPMISSLILSLSLSFITMFVIIGLQESGRPVPVLIARQEAERQKFNEPITEAERRKTQAYIFFQLLPAGIMPVIFASTIFDLALPAFTNFLLQQGNWGYQLIKSFPFNSLFKDFCYLITIMLFSSNYALTIMINPKTLAENLNSMNALIPGVRPGSETKVYSEQLIHRLNFIGSFVLALVCILPSIVERSLGLPKLQILSPVSISIALGVAVDTTRRITSYLGSSSPFKRDSSKREPLKRDFSKRRSAN
The following text describes a protein:
Function:
Secreted enzyme that regulates the endogenous N-fatty acyl amino acid (NAAs) tissue and circulating levels by functioning as a bidirectional NAA synthase/hydrolase. It condenses free fatty acids and free amino acids to generate NAAs and bidirectionally catalyzes the reverse hydrolysis reaction. Some of these NAAs stimulate oxidative metabolism via mitochondrial uncoupling, increasing energy expenditure in a UPC1-independent manner. Thereby, this secreted protein may indirectly regulate whole body energy expenditure. PM20D1 circulates in tight association with both low- and high-density (LDL and HDL,respectively) lipoprotein particles.
Sequence:
MATVGIQRTLFAALKLLTVLLALVLMIVVITTLTFPSYQTSPPECKTTDPDFIPADEERLARFSSAIQFQTVSYERGVGTPQELLKFVRFIQDGFPTIHSSPLVRREVVGNYSLLYRVEGSDGSLEPYMLASHLDVVPITQETDWEAPPFSGQVRDGYIYGRGTLDDKHNVMGSLEAVEFLLSRGHEPKRTLYLAFGHDEEIGGHFGAKVISDVLTQRGEKIAFILDEGTPVGDGLMPGVDKLVALVSVAEKGFLQLRLEVKEEGGHASMPRSESAIGILSRAISKLEDNPHPNLFGTGPEMRTLEYVATEMTLPYRILTANLWLFSPLVAWVYARKPQTNAFARTTTAVTRFNAGVKDNVISPEAVAVIDHRIHPMSSVEEVMEHDLKVINDPRVKINVINSLEPAPTSPYGKDSPTYMLLQETIQQIYPDALVTPTFMIANTDTRHYWNLSSAIYRFNPCVMTPSDLPRFHGLNERISVRDYERVMNFYYHLIVNMDKPLEVKRHVHDEDL