wanglab/gogpt-training-data huggingface dataset:
Protein: Prolyl 4-hydroxylase 5 (AtP4H5) (EC 1.14.11.2) (Q24JN5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the post-translational formation of 4-hydroxyproline in -Xaa-Pro-Gly- sequences in proline-rich peptide sequences of plant glycoproteins and other proteins. Hydroxyprolines are important constituent of many plant cell wall glycoproteins such as extensins, hydroxyproline-rich glycoproteins, lectins and arabinogalactan proteins. Possesses high affinity for leucine-rich repeat and proline-rich extensins of root cell walls that are essential for root hair development. Hydroxyprolines define the subsequent O-glycosylation sites by arabinosyltransferases which elongate the O-arabinosides on extensins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:21680836}; Single-pass type II membrane protein {ECO:0000305|PubMed:21680836}. Golgi apparatus membrane {ECO:0000305|PubMed:21680836}; Single-pass type II membrane protein {ECO:0000305|PubMed:21680836}. Note=Predominantly localized in the endoplasmic reticulum. {ECO:0000269|PubMed:21680836}.
Interaction partners:
- Pyrroline-5-carboxylate reductase
- Proline iminopeptidase
- Arabinosyltransferase RRA3
- Proline dehydrogenase 2, mitochondrial
- Proline dehydrogenase 1, mitochondrial
- Arabinosyltransferase XEG113
- Hydroxyproline O-arabinosyltransferase 3
- procollagen-proline 3-dioxygenase
- Arabinosyltransferase RRA1
- Hydroxyproline O-arabinosyltransferase 1
Sequence:
MASKSKQHLRYQPRKSVSRSTQAFTVLILLLVVILILLGLGILSLPNANRNSSKTNDLTNIVRKSETSSGDEEGNGERWVEVISWEPRAVVYHNFLTNEECEHLISLAKPSMVKSTVVDEKTGGSKDSRVRTSSGTFLRRGHDEVVEVIEKRISDFTFIPVENGEGLQVLHYQVGQKYEPHYDYFLDEFNTKNGGQRIATVLMYLSDVDDGGETVFPAARGNISAVPWWNELSKCGKEGLSVLPKKRDALLFWNMRPDASLDPSSLHGGCPVVKGNKWSSTKWFHVHEFKV
Protein: Asporin (M0R5F1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000256|ARBA:ARBA00004498, ECO:0000256|PIRNR:PIRNR002490}.
Interaction partners:
Sequence:
MPGWTCTRDSMKEYMMLLLLAVCSAKPFFSPSHTALKTMMLKDMEDTDDEDNDDDDDDNSLFPTKEPVNPFFPFDLFPTCPFGCQCYSRVVHCSDLGLTSVPSNIPFDTRMVDLQNNKIKEIKENDFKGLTSLYALILNNNKLTKIHPKTFLTTKKLRRLYLSHNQLSEIPLNLPRSLAELRIHDNKVKKIQKDTFKGMNALHVLEMSANPLDNNGIEPGAFEGVTVFHIRIAEAKLTSIPKGLPPTLLELHLDFNKISTVELEDFKRYKELQRLGLGNNKITDIENGTFANIPRVREIHLEHNKLKKIPSGLQELKYLQIIFLHNNSITKVGVNDFCPTVPKMKKSLYSAISLFNNPMKYWEIQPATFRCVVGRMSVQLGNVGK
Protein: adenine phosphoribosyltransferase (EC 2.4.2.7) (H3BQF1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MADSELQLVEQRIRSFPDFPTPGVVFRDISPVLKDPASFRAAIGLLARHLKATHGGRIDYIAGLDSRGFLFGPSLAQELGLGCVLIRKRGKLPGPTLWASYSLEYGKLCFSHTEPNYTQRENAVNSFPTRAVSCPPVPQGREPQDNTR
Protein: Cyclophilin 40, isoform A (Cyclophilin 40, isoform B) (Cyclophilin 40, isoform C (EC 5.2.1.8)) (Cyclophilin 40, isoform D) (GH06403p) (Q9VT21)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Heat shock protein 83
- LD43819p
- Cytosolic Prostaglandin E synthase
- FI23714p1
- Stress-induced-phosphoprotein 1
- LD23779p
- Heat shock protein 75 kDa, mitochondrial
- Nucleotide exchange factor Sil1
- T-complex protein 1 subunit gamma
- J domain-containing protein
Sequence:
MEERKLLRAVKSTNPLVYLDISIGKEDAGRMIIELRKDVVPKTAENFRALCTGECGIGTLGKPLHYKGTKFHKIKRVFVVQSGDVVKNDGSSGESIYGPVFDDENFELSHNEEGVVSMANYGKPNSNNSQFFISAAGCENLNGTNVVVGRVLRGLGIVAEMEQNCTDEGDPTAPIVIRDCGEIAHNEDWGIECNDETTDKLPAYPQDWPRKLDKFTGDGAVELLTGIRQSGNHFYQLGRYHEARAKYRKANRYYHYLSRQFGWQQLNPLKKHLVDEDLLKVDGFSVVNNINAAAVDLKVGNYTSAREVCNEAIRLDPKCSKAFYRRAQAQRGLRNYEEAINDLKTAHNLLPENKQILNELNSTKQLLAQYNRQQRNALKNLFA
Protein: Siroheme biosynthesis protein MET8 [Includes: Precorrin-2 dehydrogenase (EC 1.3.1.76); Sirohydrochlorin ferrochelatase (EC 4.99.1.4)] (P15807)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme.
Interaction partners:
- Uroporphyrinogen-III C-methyltransferase
- Sulfite reductase subunit beta
- Phosphoadenosine phosphosulfate reductase
- Adenylyl-sulfate kinase
- Porphobilinogen deaminase
- Sulfite reductase flavoprotein component
- Uroporphyrinogen-III synthase
- Homocysteine/cysteine synthase
- Sulfate adenylyltransferase
- 3'
Sequence:
MVKSLQLAHQLKDKKILLIGGGEVGLTRLYKLIPTGCKLTLVSPDLHKSIIPKFGKFIQNEDQPDYREDAKRFINPNWDPTKNEIYEYIRSDFKDEYLDLEDENDAWYIIMTCIPDHPESARIYHLCKERFGKQQLVNVADKPDLCDFYFGANLEIGDRLQILISTNGLSPRFGALVRDEIRNLFTQMGDLALEDAVVKLGELRRGIRLLAPDDKDVKYRMDWARRCTDLFGIQHCHNIDVKRLLDLFKVMFQEQNCSLQFPPRERLLSEYCSS
Protein: Geranyltranstransferase (Farnesyl-diphosphate synthase) (Q9PFJ6)
Organism: Xylella fastidiosa (strain 9a5c)
Interaction partners:
- Ditrans,polycis-undecaprenyl-diphosphate synthase
- 4-hydroxy-3-methylbut-2-enyl diphosphate reductase
- Octaprenyl diphosphate synthase
- Exodeoxyribonuclease 7 small subunit
- tRNA
Sequence:
MSEALFTRWRQRTDSYLERTLSIPTQAPQRLHAAMRYTVLSRGKRIRPLLVYAAGHLFHVDEPLLDVPAAAVELIHAYSLVHDDLPAMDDDLLRRGRPTVHIAFDEATAILTGDALQTLAFECLADAPSDTSLRIAWLQTLTHAAGVAGMCGGQAIDIDATGQSQTLKALEAMHALKSGTLMRAAVRMGALAGDPSAEDLHSLDTFAATLGLAFQVRDDILDIESSSEQLGKTAGKDAIQQKSTFPALLSVEGAKCYLQELAERLYTQLHPYGERAAPLTALARLAVERAH
Protein: Augmin complex subunit msd1 (Mitotic spindle density protein 1) (Q9W0G7)
Organism: Drosophila melanogaster (Fruit fly)
Function: As part of the augmin complex, plays a role in centrosome-independent generation of spindle microtubules. The complex is required for mitotic spindle assembly through its involvement in localizing gamma-tubulin to spindle microtubules. msd1 is required for microtubule nucleation from within the mitotic spindle and for localization of Grip71 to centrosomes and mitotic spindle.
Subcellular location: Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:19369198}.
Interaction partners:
- Augmin complex subunit msd5
- Augmin complex subunit wac
- Augmin complex subunit dgt2
- Augmin complex subunit dgt6
- Augmin complex subunit dgt4
- Augmin complex subunit dgt5
- Augmin complex subunit dgt3
- Meiotic 38, isoform C
- Mitotic spindle assembly checkpoint protein MAD2A
Sequence:
MSDAVDKMLAGMAANRQTMNRQLAKIDEIMERSNNTLLHIESNSKAFSQNVALSETQKMYNLRPEAEMTLSKILENFKLLMSSSDQREETYSALEGCLAYRHRVEHLGSSVRKLVALYDTVGQMKNSQEEQYASEDSP
Protein: Photosystem I chlorophyll a/b-binding protein 6, chloroplastic (LHCI type III LHCA6) (Q8LCQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The light-harvesting complex (LHC) functions as a light receptor, it captures and delivers excitation energy to photosystems with which it is closely associated. Seems involved in the function of the photosystem I in low light conditions, when other LHCA proteins are less abundant. Required, together with LHCA5, for the formation of a full-size NAD(P)H dehydrogenase-photosystem I supercomplex (NDH-PSI) that triggers cyclic and chlororespiratory electron transport in chloroplast thylakoids, especially under stress conditions (e.g. increased light intensity).
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000250|UniProtKB:Q9C639}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Photosystem I chlorophyll a/b-binding protein 5, chloroplastic
- Photosystem I reaction center subunit V, chloroplastic
- Photosystem I reaction center subunit psaK, chloroplastic
- Photosystem I reaction center subunit III, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A2
- Photosystem I reaction center subunit IV A, chloroplastic
- Photosystem I reaction center subunit IX
- Photosystem I reaction center subunit VI-2, chloroplastic
- Photosystem I P700 chlorophyll a apoprotein A1
- Photosynthetic NDH subunit of lumenal location 3, chloroplastic
Sequence:
MAFAIASALTSTLTLSTSRVQNPTQRRPHVASTSSTGGRLMRERLVVVRAGKEVSSVCEPLPPDRPLWFPGSSPPEWLDGSLPGDFGFDPLGLGSDPDTLKWFAQAELIHSRWAMLAVTGIIIPECLERLGFIENFSWYDAGSREYFADSTTLFVAQMVLMGWAEGRRWADLIKPGSVDIEPKYPHKVNPKPDVGYPGGLWFDFMMWGRGSPEPVMVLRTKEIKNGRLAMLAFLGFCFQATYTSQDPIENLMAHLADPGHCNVFSAFTSH
Protein: Uncharacterized protein, isoform D (E1JJN5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAFQLIKSALDGPPQQQQQQQLLRRHSNLGLPHQHAAGVVLLKYEHKLNSGSWEDTLDEPHHHHAHHSHHQQHLHQHHSHLSQRHQQQQQQQQQLQQTSFIGSPPSSASITTAQLHSAFSRRIAEQRERDQRDQRDQREAVGCTAATIAGGSFSANGGQAAVGVGVGSSSSCGSSSERDTKSPCRERDRNLERDRDRERDKNDDLGEEEVLTEEEQTSSSVSSLSAGNQRNSQLRSTFNKAKQHLSFDKWRTAATGSATGSASGPGSSATDSNNAASNMIMRRASACTMPSSGGGGGAGVGSSQREEATTPGESPGGRLSRWFSIRRGSSHQYDVGGRDGRHSTASSFDTPDSGSGNSPKNGSNAVAGTGGAGSQGVALDAASPQKLANLGASKMMPGVPESEDDEATANRFDVDLMMTPGSRANGTARTAHNRLIVPMLPPAPAGLSQQQLKRRHIVAAIVHSENSYVATLQRLVNDYKKPLEECSPPVLNPVKIATLFHCLPDILHSHKLFRISLAECVRNWDRDEKIGDCFVSAFGKPQLLEIYSGFINNFSAAMELAKMEEKRKSALADFFKVKQISAHDRLSFFGLMVKPVQRFPQFILFLQDLLKYTPQGHHDRMSLQLALSQLELLAELLNESKREAEQYQAFKEMLGHISGTFNARSLSLSSVSVSDSAGGHRPRYLLREDNVTHMEFNQAGFIVKCKQRRLLLLNDKVICVSVAPKQSHDFGATEKLTFKWMFPVNDVEIVDNSTSATLSRILTAGLNRGGSLKSNGSSGANGSPYANSTLPGHGGGVSGFSGFGDPHSSPAAQLTNGADNLCSEMSTLMYDYEVISRIQDLVSSLKGSYKELNANTTRNVLNLIQGSIQRKDEEMAWVDSCCLQLIGRHKSGKEETFTFQTQTPAVKKEWITELRLAQLALDPNNSPAWERGGSHPQPAHHHPHHHPLQHPHAGAGDPRQTQEQLQLQEAVQQKQSRKMPLFVKAMPVYKSQHQTEVRCGCYYSIANDTKQSGNARRRHKQLNYLWMCSSDGTSSHITVLAQHPQQAGNLREAGAFDLFETQVSALEFVKGLDQLKSRDEPASLLGDLVWLGTDSRKILIYSARNPEQEEQLGSYSVPGAVQRILYHFDAVYVALSGATVLIFRRGNDGVWQLRDPQTIRLGDTDLVVPSLLPINMCIYASCGNRVYVMNALNGEIQRSFEVQHGATQQVNLMAHSGIGLWISLKNSTMLCLYHTETFKHLQDINIASSVLRHDGKKEQPLNNSSVYVTALMACKGLLWVGTNVGIAVTIPLPRLEGVPIISGGINMSCHAHFGPITFLLPLIPKVYPAYKPPTVGAAPLVPSMGDDLQLPAIDADPKIQELDDGAVVLRRDLAKEEMSSSNPGADSTASSPRSSKLDKQNSLDQSFTAKIRASLANSPAFHRKRFRDDPNRMSKTLPRGLGAAAAGSGAGGASAAGSGTASGNTSQHGEHGICDVYGLYGKLIFVKEDYDAEEGNQGNLMDMMYEGMRRSDPELAAIPGKVCTLDRRLRMKASRPRSLDLSNWSVDSKSSSLYTSSGSEESMGIRHFGGRSVSRNSSSASHKTSGTGSDLGNISENGLMTTADIHHHQQQQQQLNSSAKPDEMSRLGAGNSGLDKPAAAVATLKRKQKQNSKQQQQQNADGPRTVITLMGGRGYWRQMWYNGAGGSPSHKNSSSGGGGGSGSGFSGQTMQSGNPSCSPLTANSNDAHIVVWEKKL
Protein: Probable ubiquitin-conjugating enzyme E2 24 (EC 2.3.2.23) (AtPHO2) (E2 ubiquitin-conjugating enzyme 24) (Ubiquitin carrier protein 24) (Ubiquitin-protein ligase 24) (Q8VY10)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E2 ubiquitin-protein ligase that mediates E1-dependent protein ubiquitination. Mediates PHO1 degradation through multivesicular body-mediated vacuolar proteolysis in response to inorganic phosphate (Pi) availability. Negatively regulates the protein abundance of PHF1 and PHT1s under Pi-sufficient conditions by facilitating the degradation of PHT1 proteins at the endomembrane. Functions cooperatively with NLA to regulate the abundance of the inorganic phosphate (Pi) transporters PHT1-1, PHT1-2 and PHT1-3 in different subcellular compartments. Regulates Pi homeostasis by mediating, cooperatively with NLA, polyubiquitination of PHT1-4 and its targeting for degradation.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:22634761, ECO:0000269|PubMed:24122829}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22634761, ECO:0000269|PubMed:24122829}.
Interaction partners:
- Inositol-3-phosphate synthase isozyme 1
- Phosphate transporter PHO1
- E3 ubiquitin-protein ligase NLA
- E3 SUMO-protein ligase SIZ1
- Protein PHOSPHATE STARVATION RESPONSE 1
- Probable gamma-glutamyl hydrolase 3
- Inorganic phosphate transporter 1-1
- Gamma-glutamyl hydrolase 2
- Gamma-glutamyl hydrolase 1
- Inorganic phosphate transporter 1-4
Sequence:
MEMSLTDSDWDSSSDSGSSEHEEVEFSYGGRAQNIFSNLEETIGKIDEFLSFERGFMYGDIVRSATEPSGQSGRVINIDMFVNLESTHGKIMKEVDTKRLQKLRSISLSDYVINGPWVGRVDKIVERVSVTLDDGTNYEVLVDGQDKLVAIPPNLLEDSQYSYYPGQRVQVKLAHAPRSTTWLCGTWRGTQVMGTVCTVEAGLVYVDWVASIVMEGDRNLTAPQALQNPESLTLLPCVSHASWQLGDWCILPGSSHCDIAERQTPNVAAYNLNECHKTFQKGFNRNMQNSGLDELFVITKTKMKVAVMWQDGSCSLGVDSQQLLPVGAVNAHDFWPEQFVVEKETCNSKKWGVVKAVNAKEQTVKVQWTIQVEKEATGCVDEVMEEIVSAYELLEHPDFGFCFSDVVVKLLPEGKFDPNADTIVATEAKHLLTESDYSGAYFLSSIGVVTGFKNGSVKVKWANGSTSKVAPCEIWKMERSEYSNSSTVSSEGSVQDLSQKISQSDEASSNHQETGLVKLYSVGESCNENIPECSSFFLPKAAIGFITNLASSLFGYQGSTSVISSHSRCNDSEDQSDSEVLVQETAESYDNSETNSGEVDMTTTMVNIPIEGKGINKTLDSTLLENSRNQVRFRQFDMVNDCSDHHFLSSDKGLAQSQVTKSWVKKVQQEWSNLEANLPNTIYVRVCEERMDLLRAALVGAPGTPYHDGLFFFDIMLPPQYPHEPPMVHYHSGGMRLNPNLYESGRVCLSLLNTWSGSGTEVWNAGSSSILQLLLSFQALVLNEKPYFNEAGYDKQLGRAEGEKNSVSYNENAFLITCKSMISMLRKPPKHFEMLVKDHFTHRAQHVLAACKAYMEGVPVGSSANLQGNSTTNSTGFKIMLSKLYPKLLEAFSEIGVDCVQEIGPES
Protein: RRM domain-containing protein (D5MCQ2)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNASSAPQQQQQQQQPQQGQAPQQQQQGPPQHQYQQQRPFHGRVQNHMRGSGPFGNSNGYGRYTAPRGDQQHHDSTPLSSVSSRRVPLPPTSQHRASSNFNTTPSSTNLYIRGLMPNTNDDLLREMCSKYGNIASTKAIMDKATNNCKGYGFVDFESPQAAAAAVDGLNTEGVQAQMAKLQQQEQDPTNLYIANLPLDFTEQMLETELNKFGMVISTRILRTPDNQSRGVGFARMDSKEKCEVIISALNGGRFDTMSKEGPALLIKQADTGRKSKHSMNNPEMLQRMQYPQVYQSYYGYHPAAVYQQHYDVNSLASQMGGMHVGGGNPQANGGGDMYGAHMYGQNAGGQGGQGVGQGGQGGNQQFYNPNNGRNKKPMNPQ
Protein: Alanine--glyoxylate aminotransferase (EC 2.6.1.44) (Q3LSM4)
Organism: Aedes aegypti (Yellowfever mosquito) (Culex aegypti)
Function: Catalyzes the pyridoxal 5'-phosphate-dependent transamination of alanine with glyoxylate as an amino group acceptor. Can also catalyze, although with much less efficiency, the transamination of serine, and histidine with glyoxylate and the and transamination of glycine with pyruvate as an amino group acceptor. Does not catalyze the transamination of both 3-hydroxykynurenine and L-kynurenine. May play a role in the detoxification of glyoxylate, a toxic plant metabolite from the pupae and adult diet (Probable).
Subcellular location: Peroxisome {ECO:0000250|UniProtKB:P21549}.
Interaction partners:
- malate synthase
- Serine hydroxymethyltransferase
- AAEL005819-PA
- Phosphoserine phosphatase
- Glyoxylate reductase/hydroxypyruvate reductase
- Glyoxylate reductase/hydroxypyruvate reductase
- Glyoxylate reductase/hydroxypyruvate reductase
- Aminomethyltransferase
- (S)-2-hydroxy-acid oxidase
- (S)-2-hydroxy-acid oxidase
Sequence:
MEYKVTPPAVLREPLVTPNKLLMGPGPSNAPQRVLDAMSRPILGHLHPETLKIMDDIKEGVRYLFQTNNIATFCLSASGHGGMEATLCNLLEDGDVILIGHTGHWGDRSADMATRYGADVRVVKSKVGQSLSLDEIRDALLIHKPSVLFLTQGDSSTGVLQGLEGVGALCHQHNCLLIVDTVASLGGAPMFMDRWEIDAMYTGSQKVLGAPPGITPVSFSHRAVERYKRRNTKVKVYYWDMSLVGDYWGCFGRPRIYHHTISSTLLYGLREAIAMACEEGLPALIARHEDCAKRLYRGLQDAGFELYADPKDRLSTVTTIKVPQGVDWLKAAQYAMKTYLVEISGGLGPTAGQVFRIGLMGQNATTERVDRVLQVFQEAVAAVKPDVQVKGKM
Protein: Breast carcinoma-amplified sequence 1 homolog (Novel amplified in breast cancer 1 homolog) (Q80YN3)
Organism: Mus musculus (Mouse)
Function: Required for myelination.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q3ZB98}.
Interaction partners:
Sequence:
MGNQMSVPLRPGDQEHDPGADTCKVTSDNECVQNGNPVVLSTRVIQHYEEVDLGISSSKDNVATSSPKTMEAQAVGDASGKNLGKEAKTKAPAARSHFFLTLSRPVPGRPGDQGTDSSAASGRFDVSPSAAPENKDPSEHGALPVAAAPGQAPDKTPGCPEAKQQTLPATGPLAPSPPESQAEAPAQDKDFGFLNRFFKLDKGRESAPVNSQPKEAKGSEDPEQATEAPAVPGNPHGVSAGEDIVDSEQRGQDVDTLSYSVPGDPEVPGTTKEDPQVVDTTENSSSIMSFFKTLVSPNKTETKKDPEDTKATKADSVCDGHAAGQKMSETQAKSKKKRLDSPRLGLSFRKLFRHKDTENSPTTSANLKSDKANFTPQETRGKTKATKSCSPPPPPPEPTSEGRDSGKEKAGPTSLPLGKLFWKKSVKEDTLSTGAEENAVCESPVETVRLEEVESSLQTVDLSEETQPEPTDVKVKEESKPRKTPLMAFLRQMSVRSSEGIPRSEESNVKDSSCQTSNSVEKTPSPPEPEPAGTAQKNKETSSSKDKKSVDKKSATENSKQKNGKQEVREPAPCVQPPTVEANAMQTGDKTPKKSEKRRQSLGGFLKGLGPKRMSDAQVQTDPVSIGPVGKSK
Protein: Carbazole 1,9a-dioxygenase, terminal oxygenase component CarAa (CARDO) (EC 1.14.12.22) (Q8G8B6)
Organism: Metapseudomonas resinovorans (Pseudomonas resinovorans)
Function: Part of the multicomponent carbazole 1,9a-dioxygenase (CARDO), that converts carbazole (CAR) into 2-aminobiphenyl-2,3-diol. Catalyzes the dioxygenation at the angular (C-9a) and adjacent (C-1) positions of carbazole to yield a highly unstable cis-hydrodiol intermediate which is spontaneously converted to 2-aminobiphenyl-2,3-diol. It is also able to attack the angular position adjacent of hetero atom of heterocyclic aromatic compounds such as polychlorinated dibenzo-p-dioxin (DD) and dibenzofuran (DBF). It was also shown that CARDO has the ability to metabolize biphenyl and polycyclic aromatic hydrocarbons, such as naphthalene and phenanthrene.
Interaction partners:
Sequence:
MANVDEAILKRVKGWAPYVDAKLGFRNHWYPVMFSKEIDEGEPKTLKLLGENLLVNRIDGKLYCLKDRCLHRGVQLSVKVECKTKSTITCWYHAWTYRWEDGVLCDILTNPTSAQIGRQKLKTYPVQEAKGCVFIYLGDGDPPPLARDTPPNFLDDDMEILGKNQIIKSNWRLAVENGFDPSHIYIHKDSILVKDNDLALPLGFAPGGDRKQQTRVVDDDVVGRKGVYDLIGEHGVPVFEGTIGGEVVREGAYGEKIVANDISIWLPGVLKVNPFPNPDMMQFEWYVPIDENTHYYFQTLGKPCANDEERKNYEQEFESKWKPMALEGFNNDDIWAREAMVDFYADDKGWVNEILFEVDEAIVAWRKLASEHNQGIQTQAHVSG
Protein: Aurora kinase (EC 2.7.11.1) (Q9VGF9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Inner centromere protein, isoform A
- Protein aurora borealis
- Deterin
- Transforming acidic coiled-coil protein, isoform K
- Cell division cycle protein 20 homolog
- Borealin
- Kinetochore protein NDC80
- BcDNA.LD24702
- Ubiquitin-conjugating enzyme E2 C
- Serine/threonine-protein kinase polo
Sequence:
MSHPSDHVLRPKENAPHRMPEKSAAVHNMQKNLLLGKKPNSENMAPASKPLPGSSGALIRKPGLGGSNSIASSEGNNFQKPMVPSVKKTTSEFAAPAPVAPIKKPESLSKQKPTAASSESSKELGAASSSAEKEKTKTETQPQKPKKTWELNNFDIGRLLGRGKFGNVYLAREKESQFVVALKVLFKRQIGESNVEHQVRREIEIQSHLRHPHILRLYAYFHDDVRIYLILEYAPQGTLFNALQAQPMKRFDERQSATYIQALCSALLYLHERDIIHRDIKPENLLLGHKGVLKIADFGWSVHEPNSMRMTLCGTVDYLPPEMVQGKPHTKNVDLWSLGVLCFELLVGHAPFYSKNYDETYKKILKVDYKLPEHISKAASHLISKLLVLNPQHRLPLDQVMVHPWILAHTQ
Protein: 7-dimethylallyltryptophan synthase (7-DMATS) (EC 2.5.1.80) (Tryptophan aminopeptidase) (EC 3.4.11.17) (Q4WYG3)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Catalyzes the prenylation of L-tryptophan at the C-7 position of the indole moiety. The enzyme is specific for dimethylallyl diphosphate (DMAPP) as prenyl donor. Accepts also D-tryptophan, typtophan-derivatives with modifications at the side chain or the indole ring, and linear and cyclic dipeptides such as H-L-Trp-L-Gly-OH or cyclo-L-Trp-L-Gly as substrates, however with lower efficiency. Also has tryptophan aminopeptidase activity towards linear peptides with a tryptophanyl moiety at the N-terminus. Dipeptides are better substrates than peptides with 3 or more amino acids. Enzymatic rate constants however are much higher for the prenyltransferase activity than for the aminopeptidase activity.
Interaction partners:
Sequence:
MSIGAEIDSLVPAPPGLNGTAAGYPAKTQKELSNGDFDAHDGLSLAQLTPYDVLTAALPLPAPASSTGFWWRETGPVMSKLLAKANYPLYTHYKYLMLYHTHILPLLGPRPPLENSTHPSPSNAPWRSFLTDDFTPLEPSWNVNGNSEAQSTIRLGIEPIGFEAGAAADPFNQAAVTQFMHSYEATEVGATLTLFEHFRNDMFVGPETYAALRAKIPEGEHTTQSFLAFDLDAGRVTTKAYFFPILMSLKTGQSTTKVVSDSILHLALKSEVWGVQTIAAMSVMEAWIGSYGGAAKTEMISVDCVNEADSRIKIYVRMPHTSLRKVKEAYCLGGRLTDENTKEGLKLLDELWRTVFGIDDEDAELPQNSHRTAGTIFNFELRPGKWFPEPKVYLPVRHYCESDMQIASRLQTFFGRLGWHNMEKDYCKHLEDLFPHHPLSSSTGTHTFLSFSYKKQKGVYMTMYYNLRVYST
Protein: Ubiquitin carboxyl-terminal hydrolase 2 (EC 3.4.19.12) (41 kDa ubiquitin-specific protease) (Deubiquitinating enzyme 2) (Ubiquitin thioesterase 2) (Ubiquitin-specific-processing protease 2) (O88623)
Organism: Mus musculus (Mouse)
Function: Hydrolase that deubiquitinates polyubiquitinated target proteins such as MDM2, MDM4 and CCND1 (By similarity). Isoform 1 and isoform 2 possess both ubiquitin-specific peptidase and isopeptidase activities (By similarity). Deubiquitinates MDM2 without reversing MDM2-mediated p53/TP53 ubiquitination and thus indirectly promotes p53/TP53 degradation and limits p53 activity (By similarity). Has no deubiquitinase activity against p53/TP53 (By similarity). Prevents MDM2-mediated degradation of MDM4 (By similarity). Plays a role in the G1/S cell-cycle progression in normal and cancer cells (By similarity). Plays a role in the regulation of myogenic differentiation of embryonic muscle cells (By similarity). Regulates the circadian clock by modulating its intrinsic circadian rhythm and its capacity to respond to external cues. Associates with clock proteins and deubiquitinates core clock component PER1 but does not affect its overall stability. Regulates the nucleocytoplasmic shuttling and nuclear retention of PER1 and its repressive role on the clock transcription factors CLOCK and BMAL1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14686789}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:14686789}. Note=Localizes in the spermatid head in late-elongating spermatids in the thin area between the outer acrosomal membrane and the plasma membrane. {ECO:0000250|UniProtKB:Q5U349}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000250|UniProtKB:Q5U349}. Membrane {ECO:0000269|PubMed:26756164}; Peripheral membrane protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:26756164}. Note=Predominantly expressed at membranes. {ECO:0000269|PubMed:26756164}.
Interaction partners:
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eS31 fusion protein
- Polyubiquitin-C
- E3 ubiquitin-protein ligase Mdm2
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin carboxyl-terminal hydrolase 14
- Ubiquitin carboxyl-terminal hydrolase 28
- Period circadian protein homolog 1
- Zinc finger-containing ubiquitin peptidase 1
- Period circadian protein homolog 2
Sequence:
MSQLSSTLKRYTESSRYTDAPYAKPGYGTYTPSSYGANLAASFLEKEKLGFKPVSPTSFLPRPRTYGPSSILDCDRGRPLLRSDIIGSSKRSESQTRGNERPSGSGLNGGSGFSYGVSSNSLSYLPMNARDQGVTLSQKKSNSQSDLARDFSSLRTSDGYRTSDGYRTSEGFRIDPGNLGRSPMLARTRKELCALQGLYQAASRSEYLTDYLENYGRKGSAPQVLTQAPPPSRVPEVLSPTYRPSGRYTLWEKSKGQASGPSRSSSPGRDTMNSKSAQGLAGLRNLGNTCFMNSILQCLSNTRELRDYCLQRLYMRDLGHTSSAHTALMEEFAKLIQTIWTSSPNDVVSPSEFKTQIQRYAPRFMGYNQQDAQEFLRFLLDGLHNEVNRVAARPKASPETLDHLPDEEKGRQMWRKYLEREDSRIGDLFVGQLKSSLTCTDCGYCSTVFDPFWDLSLPIAKRGYPEVTLMDCMRLFTKEDILDGDEKPTCCRCRARKRCIKKFSVQRFPKILVLHLKRFSESRIRTSKLTTFVNFPLRDLDLREFASENTNHAVYNLYAVSNHSGTTMGGHYTAYCRSPVTGEWHTFNDSSVTPMSSSQVRTSDAYLLFYELASPPSRM
Protein: Sporulation-specific protein (F4HZS8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ankyrin repeat family protein
Sequence:
MSRLAKWKLEKAKVKVVFRLQFHATHVPQAGWDKLFISFIPADSVKATAKTTKALVRNGTCKWGDPIYETTRLLQDTRTKQFDEKLYKIVVAMGTSRSSILGEAMINLAEYADALKPFAVILPLQGCDPGAILHVTIQLLTSKTGFREFEQQREISERGPSTTPDHSSPDESSRCRISPSDETLSHVDKTNIRGSFKEKFRDNSLVEETVGLNDLDSGLGFDVSSNTSGSLNAEKHDISSINEVDSLKSVVSGDLSGLAQSPQKEKDSLGWQHGWGSDYLGKNSDLGNAIEDNNKLKGFLEDMESSINEIKIEVSSLQCHADDIGSKAQDFSQILISEIGSGDHLVREVSVLKSECSKLKEEMERLRNVKSHVLFNSKDQDNVPHSLQLRWLQGLLVVEDNIREIQNKVCYGYHDRDLRLFLSDFESLLGVLQDFKTQIEQPISHFSTVPSEKIIMTDSKERGLSKAKHFVSGSEVDTDIYQPELDPLQYLGMPDLTSREPNSADSVSAMRDKILELVRGLDESKAERDSLTKKMDQMECYYESLVQELEETQRQLLVELQSLRTEHSTCLYSISGAKAEMETLRHDMNEQTLRFSEEKKTLDSFNEELDKRAMAAEAALKRARLNYSIAVNHLQKDLELLSSQVVSMFETNENLIKQAFPEPPQSFHECIQSTDDSISEKQDTRDVKLIQFQNEKKGMKERPLKGDIILLEDMKRSLHVQESLYQKVEEELYEMHSRNLYLEVFSNILRETFLEASVDIRIMKAKIDELGWQLELSTEAKEILKQRLDITLDEVCSLKEEKTTCIAKWNAVALQNQSLEANLQNITHENLILLQKIDELESVVLESKSWKTNYETCICEKKELAELMEKEAVEKAHYRTRLATVQAEFDAVRGKFDDLATANGNLQQNLSSLTDKLINTLGCYNEKLVSLPQWEGVDLDFESHDLTEQLDKFLCKICEKCFVLISENNGLMKEKSMTESYLRAAESDVMELKQMHENDVQCMVTKLEASTALLRRLQLETESVMDKMKVITEDEQNYESRHLDLLSRLDHFENEMHLLVSKNEGLGQEISELSSVAVEHGRTKLLVEELAEEKKRVLVSLQDKSQETLGLVRELENLKKTFDHELRLERNLRQELEIKMQDLTSEVIAKSSKLMSFDEQSSELVRLKQMVSDLELEKATHTHRLTRYETSLRSLTRDSSYISDLESQILEMMEISVAADIQIVFTRTEWETYADKLHKDHFEVLTAFNDSRNVGAQHMNANIKLLADLDSLKSELKIERNLRNNLDRRVEELTSELDEKHLLLENFDLQKSQVELLEKMVAELESEKSFQRLEYVRNAHRESSFIEELFQCLMAADVQLIFTKIQSDICINEFAEQLSCCSNSHLEFQKKYTDVESALNHCLVNETRYMDENNQLLINLEVLKSELESSMAKSRALADRNDEMSAELEEHATRDENAERSYSERSLCAPEVEQLKSLLFGYEEEIENLTVLKAEAEITVEILKDKLTGLCGKGASELETLKNRCSDLTQKLSEQILKTEEFKSMSNHLKELKDNAEAECNRAREKADYKAPLTPQQESLRIIFIKEQYDTKLQELQYQLTMSKKHGEEILMKLQDAIDENEARKKAESSQLKRSKELEGKILELEADRQSVIYDKREKTTAYDMMKAELDCSLLSLECCKEEKQKLEAILQQCKEQSLKMSKELESRRGLVQRCSSQKNIEMEENDRLNSEVSELADKNTIAVSSGDSVNNGQREVACIDPTVRIISPRSIIQGTIQSSSVNGNRDQLPSGEAMALDKREESLALINDKFRAETLRSSMDHLNDELERMKNENLLEPQDDNDSDTRFPGLEQELMQLRQAKEELQSIFPLSQENFSCGNALERVLALEIELAEALRGKKKSTTHFQSSFLKQHTDDEAIFQSFRDINNLIEEMLDTKGRYSSMETELREMHDRYSQLSLKFAEVEGERQKLMMTLKNVRASKKAMLLNRSSSATLGEH