wanglab/gogpt-training-data huggingface dataset:
Protein: 5-methylphenazine-1-carboxylate 1-monooxygenase (EC 1.14.13.218) (Q9HWG9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the biosynthesis of pyocyanine, a blue-pigmented phenazine derivative, which plays a role in virulence. Catalyzes the oxidative decarboxylation of 5-methylphenazine-1-carboxylate (5-methyl-PCA) to pyocyanine. Can also act on phenazine-1-carboxylate (PCA), converting it into 1-hydroxyphenazine (1-HP). However, PCA is a poor substrate.
Interaction partners:
- Phenazine-1-carboxylate N-methyltransferase
- Phenazine biosynthesis protein PhzB1
- Phenazine biosynthesis protein PhzA1
- Phenazine biosynthesis protein PhzD1
- Probable pyridoxamine 5'-phosphate oxidase
- Trans-2,3-dihydro-3-hydroxyanthranilate isomerase
- anthranilate synthase
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- asparagine synthase
- Phenazine biosynthesis protein PhzA2
Sequence:
MSEPIDILIAGAGIGGLSCALALHQAGIGKVTLLESSSEIRPLGVGINIQPAAVEALAELGLGPALAATAIPTHELRYIDQSGATVWSEPRGVEAGNAYPQYSIHRGELQMILLAAVRERLGQQAVRTGLGVERIEERDGRVLIGARDGHGKPQALGADVLVGADGIHSAVRAHLHPDQRPLSHGGITMWRGVTEFDRFLDGKTMIVANDEHWSRLVAYPISARHAAEGKSLVNWVCMVPSAAVGQLDNEADWNRDGRLEDVLPFFADWDLGWFDIRDLLTRNQLILQYPMVDRDPLPHWGRGRITLLGDAAHLMYPMGANGASQAILDGIELAAALARNADVAAALREYEEARRPTANKIILANREREKEEWAAASRPKTEKSAALEAITGSYRNQVERPR
Protein: Alcohol dehydrogenase class-3 (EC 1.1.1.1) (Alcohol dehydrogenase class-III) (Glutathione-dependent formaldehyde dehydrogenase) (FALDH) (FDH) (GSH-FDH) (EC 1.1.1.-) (S-(hydroxymethyl)glutathione dehydrogenase) (EC 1.1.1.284) (P72324)
Organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides)
Function: Oxidizes long-chain aliphatic alcohols, long-chain hydroxylated fatty acids and S-hydroxymethylglutathione (hmGSH) in increasing order of preference. Shows little or no activity with short-chain aliphatic alcohols.
Subcellular location: Cytoplasm.
Interaction partners:
- S-formylglutathione hydrolase
- Glutathione-dependent formaldehyde-activating enzyme
- aldehyde dehydrogenase
- Zinc-containing alcohol dehydrogenase
- aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Aldehyde dehydrogenase
- Isocytochrome c2
- Alkane 1-monooxygenase
- Pqq dehydrogenase protein
Sequence:
MRTRAAVAVEAGKPLEIMEVNLEGPKAGEVMVEIKATGICHTDEFTLSGADPEGMFPAILGHEGAGVVVEVGPGVTSVKPGDHVIPLYTPECRQCPSCLSQKTNLCTAIRGTQGQGLMPDGTSRFSMLDGTPILHYMGCSTFSNYTVLPEIAVAKVRPDAPFDKICYIGCGVTTGIGAVINTAKVEIGAKAVVFGLGGIGLNVIQGLKLAGADMIIGVDLNNAKKEWGERFGMTHFVNPSEIDGDVVAHLVNMTKTPFDQIGGADYTFDCTGNVKVMRQALEACHRGWGQSIVIGVAPAGAEIQTRPFQLVTGRVWKGSAFGGARGRTDVPKIVDWYMEGKIQIDPMITHILSLEEINKGFDLMHAGESIRSVVVF
Protein: Di-trans,poly-cis-undecaprenyl-diphosphate synthase (EC 2.5.1.31) (Cis-prenyltransferase) (A8B1Z2)
Organism: Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia)
Function: Cis-prenyl transferase involved in the synthesis of dolichol, a long-chain polyprenol that is utilized as a sugar carrier in protein glycosylation in the endoplasmic reticulum (ER). Catalyzes the sequential condensation of isopentenyl pyrophosphate (IPP) with farnesyl pyrophosphate (FPP) to produce a polyprenyl pyrophosphate which contains 11 (major) and 12 (minor) isoprene units.
Interaction partners:
- Farnesyl diphosphate synthase
- Protein farnesyltransferase/geranylgeranyltransferase type-1 subunit alpha
- Protein farnesyltransferase subunit beta
- glutamate--tRNA ligase
- Small ribosomal subunit protein uS2
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
- phenylalanine--tRNA ligase
- Hydrolase
- 3-hydroxy-3-methylglutaryl-coenzyme A reductase.
- phenylalanine--tRNA ligase
Sequence:
MIPMHVAVIMDGNGRWARKQLQERTFGHEQGVSVLESIVDECINCGIRFLTVYAFSTENWSRPPTEVSFLFELLSAAIQRVRTTYRERNVKVQFCGERTTQIPETVIAAMNCIEQDTAACTGLILSVCFNYGGHTEIAQACRSVLADCLEGDAVENIKTRLQMPIEQFIQQIDTHLYANLPPVDLLIRTGCEKRLSNFLPWHLAYAEIIFSDLLWPEFSVRAFKDCLDEFASRTRRFGGVQLSPMTGVYSDTHPHSSTNALSNHD
Protein: Dyslexia-associated protein KIAA0319-like protein (E7EN73)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}.
Interaction partners:
Sequence:
MEKRLGVKPNPASWILSGYYWQTSAKWLRSLYLFYTCFCFSVLWLSTDASESRCQQGKTQFGVGLRSGGENHLWLLEGTPSLQSCWAACCQDSACHVFWWLEGMCIQADCSRPQSCRAFRTHSSNSMLVFLKKFQTADDLGFLPEDDVPHLLGLGWNWASWRQSPPRAALRPAVSSSDQQSLIRKLQKRGSPSDVVTPIVTQHSKVNDSNELGGLTTSGSAEVHKAITISSPLTTDLTAELSGGPKNVSVQPEISEGLATTPSTQQVKSSEKTQIAVPQPVAPSYSYATPTPQASFQSTSAPYPVIKELVVSAGESVQITLPKNEVQLNAYVLQEPPKGETYTYDWQLITHPRDYSGEMEGKHSQILKLSKLTPGLYEFKVIVEGQNAHGEGYVNVTVKPEPRKNRPPIAIVSPQFQEISLPTTSTVIDGSQSTDDDKIVQYHWEELKGPLREEKISEDTAILKLSKLVPGNYTFSLTVVDSDGATNSTTANLTVNKAVDYPPVANAGPNQVITLPQNSITLFGNQSTDDHGITSYEWSLSPSSKGKVVEMQGVRTPTLQLSAMQEGDYTYQLTVTDTIGQQATAQVTVIVQPENNKPPQADAGPDKELTLPVDSTTLDGSKSSDDQKIISYLWEKTQGPDGVQLENANSSVATVTGLQVGTYVFTLTVKDERNLQSQSSVNVIVKEEINKPPIAKITGNVVITLPTSTAELDGSKSSDDKGIVSYLWTRDEGSPAAGEVLNHSDHHPILFLSNLVEGTYTFHLKVTDAKGESDTDRTTVEVKPDPRKNNLVEIILDINVSQLTERLKGMFIRQIGVLLGVLDSDIIVQKIQPYTEQSTKMVFFVQNEPPHQIFKGHEVAAMLKSELRKQKADFLIFRALEVNTVTCQLNCSDHGHCDSFTKRCICDPFWMENFIKVQLRDGDSNCEWSVLYVIIATFVIVVALGILSWTVICCCKRQKGKPKRKSKYKILDATDQESLELKPTSRAGIKQKGLLLSSSLMHSESELDSDDAIFTWPDREKGKLLH
Protein: Serine/threonine-protein kinase RIO1 (EC 2.7.11.1) (EC 3.6.3.-) (Ribosomal RNA-processing protein 10) (Q12196)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the final endonucleolytic cleavage at site D converting 20S pre-rRNA into the mature 18S rRNA. Required for the final steps of cytoplasmic maturation of the 40S ribosomal subunit. The association with the very late 40S subunit intermediate seems to follow RIO2 association with precursors of the 40S subunit and may involve a translation-like checkpoint point cycle preceeding the binding to the 60S ribosomal subunit. Despite the protein kinase domain is proposed to act predominantly as an ATPase. The catalytic activity regulates its dynamic association with the 40S subunit. Has a role in the cell cycle where it is required for entrance into S-phase and in the control of the onset of anaphase. Appears to also be involved in the maintenance of chromosome stability and correct mitotic segregation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11483523, ECO:0000269|PubMed:12135737, ECO:0000269|PubMed:12612080}.
Interaction partners:
- 20S-pre-rRNA D-site endonuclease NOB1
- Protein LTV1
- Serine/threonine-protein kinase RIO2
- Pre-rRNA-processing protein PNO1
- Small ribosomal subunit protein uS3
- Ribosome biogenesis protein TSR1
- Essential nuclear protein 1
- Small ribosomal subunit protein uS5
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS7
Sequence:
MSLEDKFDSLSVSQGASDHINNQLLEKYSHKIKTDELSFSRAKTSKDKANRATVENVLDPRTMRFLKSMVTRGVIADLNGCLSTGKEANVYHAFAGTGKAPVIDEETGQYEVLETDGSRAEYAIKIYKTSILVFKDRERYVDGEFRFRNSRSQHNPRKMIKIWAEKEFRNLKRIYQSGVIPAPKPIEVKNNVLVMEFLSRGNGFASPKLKDYPYKNRDEIFHYYHTMVAYMRLLYQVCRLVHADLSEYNTIVHDDKLYMIDVSQSVEPEHPMSLDFLRMDIKNVNLYFEKMGISIFPERVIFQFVISETLEKFKGDYNNISALVAYIASNLPIKSTEQDEAEDEIFRSLHLVRSLGGLEERDFDRYTDGKFDLLKSLIAHDNERNFAASEQFEFDNADHECSSGTEEFSDDEEDGSSGSEEDDEEEGEYYDDDEPKVLKGKKHEDKDLKKLRKQEAKDAKREKRKTKVKKHIKKKLVKKTKSKK
Protein: Isocitrate dehydrogenase [NAD] regulatory subunit 2, mitochondrial (IDH-II) (Isocitric dehydrogenase 2) (NAD(+)-specific ICDH 2) (P93032)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Performs an essential role in the oxidative function of the citric acid cycle.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Peroxisomal isocitrate dehydrogenase
- Isocitrate dehydrogenase, chloroplastic/mitochondrial
- Cytosolic isocitrate dehydrogenase
- Isocitrate dehydrogenase catalytic subunit 5, mitochondrial
- Isocitrate dehydrogenase catalytic subunit 6, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Aconitate hydratase 3, mitochondrial
- Aconitate hydratase 2, mitochondrial
- Aconitate hydratase 1
Sequence:
MSRQSFSLLKNLRSIASGSKIQTRSVTYMPRPGDGKPRPVTLIPGDGVGPLVTNAVQQVMEAMHAPVYFEPFEVHGDMKSLPEGLLESIKKNKVCLKGGLKTPVGGGVSSLNVNLRKELDLFASLVNCFNLPGLASRHENVDIVVIRENTEGEYAGLEHEVVPGVVESLKVITKFCSERIAKYAFEYAYLNNRKKVTAVHKANIMKLADGLFLESCQEVAKKYPSIAYNEIIVDNCCMQLVARPEQFDVMVTPNLYGNLVANTAAGIAGGTGVMPGGNVGAEYAVFEQGASAGNVGKDTTEEQKNANPVALLLSSAMMLRHLQFPSFADRLETAVKRVIAEGNCRTEDLGGNSTTQEVVDAVIANLD
Protein: Nuclear receptor subfamily 4 group A member 1 (H3BT85)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MWLAKACWSIQSEMPCIQAQYGTPAPSPGPRDHLASDPLTPEFIKPTMDLASPEAAPAAPTALPSFSTFMDGYTGEFDTFLYQLPGTVQPCSSASSSASSTSSSSATSPASASFKFEDFQVYGCYPGPLSGPVDEALSSSGSDYYGSPCSAPSPSTPSFQPPQLSPWDGSFGHFSPSQTYEGLRAWTEQLPKASGPPQPPAFFSFSPPTGPSPSLAQSPLKLFPSQATHQLGEGESYSMPTAFPGLAPTSPHLEGSGILDTPVTSTKARSGAPGGSEGRCAVCGDNASCQHYGVRTCEGCKG
Protein: Uridine 5'-monophosphate synthase (UMP synthase) [Includes: Orotate phosphoribosyltransferase (OPRTase) (EC 2.4.2.10); Orotidine 5'-phosphate decarboxylase (EC 4.1.1.23) (OMPdecase)] (P13439)
Organism: Mus musculus (Mouse)
Function: Bifunctional enzyme catalyzing the last two steps of de novo pyrimidine biosynthesis, orotate phosphoribosyltransferase (OPRT), which converts orotate to orotidine-5'-monophosphate (OMP), and orotidine-5'-monophosphate decarboxylase (ODC), the terminal enzymatic reaction that decarboxylates OMP to uridine monophosphate (UMP).
Interaction partners:
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Uridine-cytidine kinase-like 1
- Thymidine phosphorylase
- Uridine phosphorylase 1
- Uridine-cytidine kinase 2
- Uridine-cytidine kinase 1
- Uracil phosphoribosyltransferase homolog
- UMP-CMP kinase
- UMP-CMP kinase 2, mitochondrial
Sequence:
MEVASQALGPLVTELYDVQAFKFGSFVLKSGLSSPVYIDLRGIVSRPRLLSQVADILFQTAKNAGISFDSVCGVPYTALPLATVICSANHIPMLIRRKETKDYGTKRLVEGEINPGQTCLVIEDVVTSGASVLETVEVLQKEGLKVTDAIVLLDREQGGKDKLQAQGIRLHAVCTLSQMLEILQQQEKIDADMVGRVKRFIQENVFSAANHNGLPPPEKKACKELSFGARAELPGTHPLASKLLRLMQKKETNLCLSADVSEARELLQLADALGPSICMLKTHVDILNDFTLDVMEELTALAKRHEFLIFEDRKFADIGNTVKKQYESGTFKIASWADIVNAHVVPGSGVVKGLQEVGLPLHRACLLIAEMSSAGSLATGNYTKAAVGMAEEHCEFVIGFISGSRVSMKPEFLHLTPGVQLETGGDHLGQQYNSPQEVIGKRGSDVIIVGRGILAAANRLEAAEMYRKAAWEAYLSRLAVQ
Protein: Golgin B1 (A0A8I6AFX2)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPKMFSFQKLRVMQRKLEEHEEALLGRAQVVDLLQKELTSAEQRNQDLSQQLQLLEAEHSTLRNTMEAERQESKILMEKVELEMAERKEELYQLQGQLERAGQAQAELEMQYGTLQQRHETEMEEKTACISLLQKNEQELQSACDALKEENSKLLQEQQEQAAKSAQALQQLEDELQQKSKEISQFVNKPNLEKHETSSQTSLPDVYNEGVQAVMEESVASLQKRVLELENEKGALLLSSLELEELRAENEKLCSRITLLEAQNRAGEADGMVCEVSTAGIALLNRSDSSTEESGQDVLENTFSQKHKELSVLLVEMKEAQEEIAFLKSQLQGKRPEGDYEVLDRKEVQMMESEGLPSVTARDVLCAPRDKNSVPAVEGEQAGMRDQHGTLEAGPLNDTGMELNSPQPDGVDKSLSAPHVCLCHQGELERLKTQVLELETSLHTAKETHEKNLSEKAKEISSLTQLTKEFKESAEEARSTLTAVCEERDQLLYRVKELDVLGELRAQVRELETSLAEAEKQRGLDYESQRAQHNLLTEQIHSLSIEAKSKDVKIETLQRELDGVQLQFSEQGTQIRSLQSQLQTKESEVLEGAERMKDISKEMEELSQALSQKELEIAQMDQLLLEKKKDVETLQQTIQEKDQQVTELSFSMTEKMVQLNEEKFSLGVEIKTLKEQLSLLSRAEGAKKEQVEDSGAESSPKHGPHESSAQEPVCKDALQQELEWLRKESEQRKRKLQAALISRKELLQKVSKLEEELAKVREESTKDSLRESEKRELEEDSKNKDDPEKYGTSEWRELEVSLRLTISEKEVELEGIRRDLKEKAAAEEELQALVQRMTQDLQNKTKQIDLLQEEITENQATIQKFITGTMDAGDGDSAVKETSVSSPPRAGGGEHWKPELEGKIVDLEKEKTQLQKKLQEALISRKAILKKAQEKEKHLKEELKEQKDAYRHLQEQFDGQSKENENIAARLRQLQAKESTDQQLPGTGQQEPTHGSEGLSLEGTEPASESDLHAAQPSHPGETATLQATVSVAQIQDQLKEIEVEKEELELKISSTTSELTKKSEEVLLLQEQINEQGLEIQNLKAASHEAKAHTEQLKQELESSQLKIADLEHLKTLQPELETLQKHVGQKEEEVSYLVGQLGEKEQTLTTVQTEMEEQERLIKALHTQLEMQAKEHEERLKQVQVEICELKKQPKELEEESKAKQQLQRKLQAALISRKEALKENKSLQEQLSSARDAVEHLTKSLADVESQVSVQNQEKDALLGKLALLQEERDKLIVEMDKSLLENQSLGGSCESLKLALGGLTEDKEKLMKELESVRCSKIAESTEWQEKHKELQKEYEVLLQSYENVSNEAERIQHVVESVRQEKQEVYAKLRSAESDKREREKQLQDAEQEMEEMKEKMRKFAKSKQQKILELEEENDRLRAEAQPVGGANESMEALLSSNASLKEELERITLEYKTLSKEFEALMAEKNTLSEETRNLKLQVEAQELKQASLETTEKSDEPKDVIEEVTEAVVGKSQEQDSLSENAKLEDAEATLLANSAKPGVSETFSSHDDINNYLQQLDQLKGRIAELEMEKQKDRELSQTLENEKNALLTQISAKDSELKLLEEEVAKINMLNQQIQEELSRVTKLKETAEEEKDDLEERLMNQLAELNGSIGNYYQDVTDAQIKNEQLESEMQNLKRCVSELEEEKQQLVKEKTKVESEIRKEYMEKIQGAQKGPGSKIHAKELQELLKEKQQEVKQLQKDCIRYLGRISALEKTVKALEFVHTESQKDLDATKGNLAQAVEHHKKAQAELSSFKILLDDTQSEAARVLADNLKLKKELQSNKESIKSQIKQKDEDLLRRLEQAEEKHRKEKKNMQEKLDALHREKAHVEDTLAEIQVSLTRKDKDMKELQQSLDSTLAQLAAFTKSMSSLQDDRDRVIDEAKKWEQRFGDAIQTKEEEVRLKEENCTALKDQLRQMTIHMEELKITVSRLEHDKEIWESKAQTELQHQQKAYDKLQEENKELMSQLEEAGQLYHDSKNELTKLESELKSLKDQSTDLKNSLEKCREHENNLEGIIKQQEADIQNCKFNCEQLETDLTASRELTTRLHDEINVKEQKIISLLSGKEEAIQVAIAELHQQHSKEIKELENLLSQEEEENLTLEEENKRAVEKTNQLTEALETIKKESLEQKAQLDSFVKSMSSLQDDRDRIVSDYRQLEERHLSVILEKDELIQDAAAENNKLKEEIRGLRGHMDDLNSENAKLDAELIQYRRDLNEVITIKDSQQRQLLEAQLQQNKELRNECVKLEGRLKGSEAEKQSLQMSLDALQEENQGLSKEIKSFKEQLTALHEEGALAVYHAQLRVREEEVQKLTAALSSSQKRTVDLQEELVCVQKEASKKVSEIEDKLKRELKHLHHNAGIMRNETETAEERVAELARDLVEMEQKLLTVTKENKDLTAQIQAFGKSMSSLQDSRDHATEELSDLKKKYDASLKELAQLKGRQDLGRESDVLSQAAFPLTTSENISSRLEKLNQQLTSKDEQLLHLSSELESSHNQVQSFTKAMTSLQNERDHLWNELEKFRKSEEGKQRSAAPSAASSPAEVQSLKKAMSSLQNDRDRLLKELKNLQQQYLQMNQEITELRPLKAQLQESQDQTKALQMMKEELRQENLSWQHELHQLRVEKNSWELHERRMKEQYLMAISDKDQQLGHLQNLLRELRSSSQTQILPTQYQRQASSGTSAALDGSQNLVYETDCLRTQLNDSLKEIHQKELRIQQLNSKFSQLLEEKNILSTQLRDANQSLRDSQHHYSNLFNHCAILERQVQQLQATGPLNADVAPGAPQEKDGIHIKTETETTGEEQPSFSEVQQQLCNTKHDLSELKKLLEEERDQRLTAENALSLAKEQIRRLEHSEWESARTPIIGACGSQEQVLLMDLPGSSCRRTRSSAGWKRVLRSLCRSRTRVPLLAAIYFLMIHVLLVLCFTGHL
Protein: Uncharacterized protein, isoform B (Uncharacterized protein, isoform D) (Uncharacterized protein, isoform F) (Uncharacterized protein, isoform G) (Uncharacterized protein, isoform J) (Uncharacterized protein, isoform K (EC 1.1.1.29, EC 1.1.1.79, EC 1.1.1.81)) (Q7KT11)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSAGKAFKVLVTHPEVPQEGIDLLKENCEIVQVQSVPINRAELLEKIRGVDGVLWGGHEPLNAEALDAAGPQLKSISTMSAGIDYVDVPEVKRRKIPLGHTPTVLNTAVADLAVGLLIAASRRFHEGRKTIDNDKWENYHLNWLLGQDIRDSTVGFYGFGGIGQAIAKRLSGFDIDKVLYTTRRRVHKEIEEEFNAKKVDFDTLLAESDFVVIASPLTKDTQGVFNATAFNKMKQTAVLVNIARGKIVNQDDLYEALKANRIFSAGLDVTDPEPLSPKDKLLTLDNVVVLPHIGSATKRTRADMSTIAAHNVLRGLAGEPMLSPAY
Protein: Uncharacterized aarF domain-containing protein kinase At5g05200, chloroplastic (EC 2.7.-.-) (Q9ASX5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast, plastoglobule {ECO:0000269|PubMed:16461379, ECO:0000269|PubMed:22274653}.
Interaction partners:
- non-specific serine/threonine protein kinase
- FAD/NAD
- Probable disease resistance protein At1g62630
- RNA-binding
- Aspartate-glutamate racemase family
- Kinase with adenine nucleotide alpha hydrolases-like domain-containing protein
- Formate dehydrogenase, chloroplastic/mitochondrial
- Receptor protein kinase-like protein ZAR1
- Protein KINASE OF THE OUTER CHLOROPLAST MEMBRANE 1
- Probable disease resistance protein At1g59620
Sequence:
MAVSAFRGTRLPLFHHSQFPVARTVSGTSKKMIGARNFKGFVLTAQYSQTQDLFTSRLQSQIEKLPKLVEDIVQTSINTGPRGVTRLVQGVQAFVGVGGEWLNDLSKSTSASGGLPSELQLGLLSPLYLRKLFERMGATYIKLGQFIASAPTLFPPEYVKEFQNCFDKAPPVPFEEIRKILQEELGRPIESVYEYVDPTPIASASIAQVHGARLRGSQEDVVIKVLKPGIEDFLVADLNFIYVVSRIFEFLSPEFSRTSLVGIVKDIRESMLEEVDFNKEAQNIESFKRYLETMGLTGQATAPRVYKYCSSRRVLTMERLYGVPLTDLDSIRSLVSSPENSLITALNVWFGSLLACESFHADVHAGNLWLLRDGRIGFLDFGIVGRISPKTWAAMEVFLASIATEEYESMASALIQMGATNRDVDGKAFAKDLEKMFSSIQELDTEIVVATARGTNSDTTAVAANVVMDERQMNALFLDLVRVSESYGLKFPREFALLLKQLLYFDRYTRLLAPNLNMLQDQRISIASNKRTNGYKDSFN
Protein: [F-actin]-monooxygenase MICAL1 (EC 1.14.13.225) (EC 1.6.3.1) (Molecule interacting with CasL protein 1) (MICAL-1) (NEDD9-interacting protein with calponin homology and LIM domains) (Q8TDZ2)
Organism: Homo sapiens (Human)
Function: Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). Acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. Also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L; acts by antagonizing STK38 and STK38L activation by MST1/STK4. Involved in regulation of lamina-specific connectivity in the nervous system such as the development of lamina-restricted hippocampal connections. Through redox regulation of the actin cytoskeleton controls the intracellular distribution of secretory vesicles containing L1/neurofascin/NgCAM family proteins in neurons, thereby regulating their cell surface levels (By similarity). May act as Rab effector protein and play a role in vesicle trafficking.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32344433}. Cytoplasm, cytoskeleton. Endosome membrane {ECO:0000269|PubMed:32344433}. Midbody {ECO:0000269|PubMed:28230050}. Note=Accumulates transiently at the abscission site before abscission occurs. Colocalized with GRAF1/ARHGAP26 and GRAF2/ARHGAP10, RAB8A, RAB8B and RAB10 on endosomal tubules (PubMed:32344433). {ECO:0000269|PubMed:28230050, ECO:0000269|PubMed:32344433}.
Interaction partners:
- Enhancer of filamentation 1
- Ras-related protein Rab-10
- Plexin-A1
- Ras-related protein Rab-8A
- Plexin-A4
- Plexin-A3
- Ras-related protein Rab-35
- Plexin-A2
- Serine/threonine-protein kinase 38
Sequence:
MASPTSTNPAHAHFESFLQAQLCQDVLSSFQELCGALGLEPGGGLPQYHKIKDQLNYWSAKSLWTKLDKRAGQPVYQQGRACTSTKCLVVGAGPCGLRVAVELALLGARVVLVEKRTKFSRHNVLHLWPFTIHDLRALGAKKFYGRFCTGTLDHISIRQLQLLLLKVALLLGVEIHWGVTFTGLQPPPRKGSGWRAQLQPNPPAQLANYEFDVLISAAGGKFVPEGFKVREMRGKLAIGITANFVNGRTVEETQVPEISGVARIYNQSFFQSLLKATGIDLENIVYYKDDTHYFVMTAKKQCLLRLGVLRQDWPDTNRLLGSANVVPEALQRFTRAAADFATHGKLGKLEFAQDAHGQPDVSAFDFTSMMRAESSARVQEKHGARLLLGLVGDCLVEPFWPLGTGVARGFLAAFDAAWMVKRWAEGAESLEVLAERESLYQLLSQTSPENMHRNVAQYGLDPATRYPNLNLRAVTPNQVRDLYDVLAKEPVQRNNDKTDTGMPATGSAGTQEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQAVVAGSDPLGLIAYLSHFHSAFKSMAHSPGPVSQASPGTSSAVLFLSKLQRTLQRSRAKENAEDAGGKKLRLEMEAETPSTEVPPDPEPGVPLTPPSQHQEAGAGDLCALCGEHLYVLERLCVNGHFFHRSCFRCHTCEATLWPGGYEQHPGDGHFYCLQHLPQTDHKAEGSDRGPESPELPTPSENSMPPGLSTPTASQEGAGPVPDPSQPTRRQIRLSSPERQRLSSLNLTPDPEMEPPPKPPRSCSALARHALESSFVGWGLPVQSPQALVAMEKEEKESPFSSEEEEEDVPLDSDVEQALQTFAKTSGTMNNYPTWRRTLLRRAKEEEMKRFCKAQTIQRRLNEIEAALRELEAEGVKLELALRRQSSSPEQQKKLWVGQLLQLVDKKNSLVAEEAELMITVQELNLEEKQWQLDQELRGYMNREENLKTAADRQAEDQVLRKLVDLVNQRDALIRFQEERRLSELALGTGAQG
Protein: Ultra-long-chain fatty acid omega-hydroxylase (EC 1.14.14.177) (Cytochrome P450 4F22) (Q6NT55)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in epidermal ceramide biosynthesis. Hydroxylates the terminal carbon (omega-hydroxylation) of ultra-long-chain fatty acyls (C28-C36) prior to ceramide synthesis. Contributes to the synthesis of three classes of omega-hydroxy-ultra-long chain fatty acylceramides having sphingosine, 6-hydroxysphingosine and phytosphingosine bases, all major lipid components that underlie the permeability barrier of the stratum corneum. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:26056268}; Single-pass type I membrane protein {ECO:0000269|PubMed:26056268}. Microsome membrane {ECO:0000269|PubMed:26056268}; Single-pass type I membrane protein {ECO:0000269|PubMed:26056268}.
Interaction partners:
- Magnesium transporter NIPA4
- Glucosylceramide transporter ABCA12
- Protein-glutamine gamma-glutamyltransferase K
- Omega-hydroxyceramide transacylase
- Lipase member N
- Hydroperoxide isomerase ALOXE3
- Arachidonate 12-lipoxygenase, 12R-type
- Ceramide synthase 3
- Short-chain dehydrogenase/reductase family 9C member 7
Sequence:
MLPITDRLLHLLGLEKTAFRIYAVSTLLLFLLFFLFRLLLRFLRLCRSFYITCRRLRCFPQPPRRNWLLGHLGMYLPNEAGLQDEKKVLDNMHHVLLVWMGPVLPLLVLVHPDYIKPLLGASAAIAPKDDLFYGFLKPWLGDGLLLSKGDKWSRHRRLLTPAFHFDILKPYMKIFNQSADIMHAKWRHLAEGSAVSLDMFEHISLMTLDSLQKCVFSYNSNCQEKMSDYISAIIELSALSVRRQYRLHHYLDFIYYRSADGRRFRQACDMVHHFTTEVIQERRRALRQQGAEAWLKAKQGKTLDFIDVLLLARDEDGKELSDEDIRAEADTFMFEGHDTTSSGISWMLFNLAKYPEYQEKCREEIQEVMKGRELEELEWDDLTQLPFTTMCIKESLRQYPPVTLVSRQCTEDIKLPDGRIIPKGIICLVSIYGTHHNPTVWPDSKVYNPYRFDPDNPQQRSPLAYVPFSAGPRNCIGQSFAMAELRVVVALTLLRFRLSVDRTRKVRRKPELILRTENGLWLKVEPLPPRA
Protein: Candida glabrata strain CBS138 chromosome J complete sequence (Q6FNQ3)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MKFLTTAATLTAASILGSTALAAAMPDLKDCTTTAQGNHQHKRAVAVEYVYETVIVDDQGHTLNVPPVKNDAASPTQAPKQSTQTPAAAPSTSTLAPASSSSPSPAKKADSTTSTLAPSSSSSPSPSPSSSSSSSSSSQQSKPSSSTSSSSSYSGGIYGDLAAFSGPSEKFQDGVIPCSQFPAGQGVIPISWLGENGWSGVENSDTSTGGDCKEGSYCSYACQPGMSKTQWPSSQPADGRSIGGLLCKNGYLYRSNTNADYLCEWGVNSAEVESKLSQGVAICRTDYPGTENMVIPTFVQAGATLPLTVVNQDTYYQWQGMKTSAQYYVNNAGISVEDGCVWGNAGSGLGNWAPLNFGAGYTNGITYLSLIPNPNNKAPLNYNVKIVAADDSSVVNGECSYENGVYSGGADGCTVAVRSGKAKFVLY
Protein: Microprocessor complex subunit DGCR8 (DiGeorge syndrome critical region 8) (Q8WYQ5)
Organism: Homo sapiens (Human)
Function: Component of the microprocessor complex that acts as a RNA- and heme-binding protein that is involved in the initial step of microRNA (miRNA) biogenesis. Component of the microprocessor complex that is required to process primary miRNA transcripts (pri-miRNAs) to release precursor miRNA (pre-miRNA) in the nucleus. Within the microprocessor complex, DGCR8 function as a molecular anchor necessary for the recognition of pri-miRNA at dsRNA-ssRNA junction and directs DROSHA to cleave 11 bp away form the junction to release hairpin-shaped pre-miRNAs that are subsequently cut by the cytoplasmic DICER to generate mature miRNAs. The heme-bound DGCR8 dimer binds pri-miRNAs as a cooperative trimer (of dimers) and is active in triggering pri-miRNA cleavage, whereas the heme-free DGCR8 monomer binds pri-miRNAs as a dimer and is much less active. Both double-stranded and single-stranded regions of a pri-miRNA are required for its binding. Specifically recognizes and binds N6-methyladenosine (m6A)-containing pri-miRNAs, a modification required for pri-miRNAs processing. Involved in the silencing of embryonic stem cell self-renewal (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:16906129, ECO:0000269|PubMed:16963499, ECO:0000269|PubMed:17159994, ECO:0000269|PubMed:22118463, ECO:0000269|PubMed:34188037}. Nucleus, nucleolus {ECO:0000269|PubMed:17159994}. Note=Colocalizes with nucleolin and DROSHA in the nucleolus. Mostly detected in the nucleolus as electron-dense granular patches around the fibrillar center (FC) and granular component (GC). Also detected in the nucleoplasm as small foci adjacent to splicing speckles near the chromatin structure. Localized with DROSHA in GW bodies (GWBs), also known as P-bodies (PubMed:17159994).
Interaction partners:
- Ribonuclease 3
- Probable ATP-dependent RNA helicase DDX17
- Probable ATP-dependent RNA helicase DDX5
- Endoribonuclease Dicer
- Heterogeneous nuclear ribonucleoproteins A2/B1
- N
- N
- Protein argonaute-2
- Methyl-CpG-binding protein 2
- RISC-loading complex subunit TARBP2
Sequence:
METDESPSPLPCGPAGEAVMESRARPFQALPREQSPPPPLQTSSGAEVMDVGSGGDGQSELPAEDPFNFYGASLLSKGSFSKGRLLIDPNCSGHSPRTARHAPAVRKFSPDLKLLKDVKISVSFTESCRSKDRKVLYTGAERDVRAECGLLLSPVSGDVHACPFGGSVGDGVGIGGESADKKDEENELDQEKRVEYAVLDELEDFTDNLELDEEGAGGFTAKAIVQRDRVDEEALNFPYEDDFDNDVDALLEEGLCAPKKRRTEEKYGGDSDHPSDGETSVQPMMTKIKTVLKSRGRPPTEPLPDGWIMTFHNSGVPVYLHRESRVVTWSRPYFLGTGSIRKHDPPLSSIPCLHYKKMKDNEEREQSSDLTPSGDVSPVKPLSRSAELEFPLDEPDSMGADPGPPDEKDPLGAEAAPGALGQVKAKVEVCKDESVDLEEFRSYLEKRFDFEQVTVKKFRTWAERRQFNREMKRKQAESERPILPANQKLITLSVQDAPTKKEFVINPNGKSEVCILHEYMQRVLKVRPVYNFFECENPSEPFGASVTIDGVTYGSGTASSKKLAKNKAARATLEILIPDFVKQTSEEKPKDSEELEYFNHISIEDSRVYELTSKAGLLSPYQILHECLKRNHGMGDTSIKFEVVPGKNQKSEYVMACGKHTVRGWCKNKRVGKQLASQKILQLLHPHVKNWGSLLRMYGRESSKMVKQETSDKSVIELQQYAKKNKPNLHILSKLQEEMKRLAEEREETRKKPKMSIVASAQPGGEPLCTVDV