wanglab/gogpt-training-data huggingface dataset:
Protein: Probable methylmalonyl-CoA mutase, mitochondrial (EC 5.4.99.2) (MethylmalonylCoA mutase homolog 1) (MCM) (Q23381)
Organism: Caenorhabditis elegans
Function: Involved, in man, in the degradation of several amino acids, odd-chain fatty acids and cholesterol via propionyl-CoA to the tricarboxylic acid cycle. MCM has different functions in other species (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250}.
Interaction partners:
- Methylmalonyl-CoA epimerase, mitochondrial
- Methylmalonic aciduria type A homolog, mitochondrial
- Succinate--CoA ligase [GDP-forming] subunit beta, mitochondrial
- Probable methionine synthase
- Corrinoid adenosyltransferase MMAB
- Succinate--CoA ligase subunit beta, mitochondrial
- Methylmalonic aciduria and homocystinuria type D homolog
- Succinate--CoA ligase subunit alpha, mitochondrial
- MMACHC-like protein)
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MYLQLLKPTLLRCSTRPSSSGAYTRSPIDQKWAAMAKKAMKGREADTLTWNTPEGIPIKPLYLRSDRDCDAQRSVELPGQFPFTRGPYPTMYTQRPWTIRQYAGFSTVEESNKFYKENIKAGQQGLSVAFDLATHRGYDSDNPRVFGDVGMAGVAVDSVEDMRQLFDGINLEKMSVSMTMNGAVVPVLAMYVVAAEEAGVSRKLLAGTIQNDILKEFMVRNTYIYPPEPSMRIIGDIFAYTSREMPKFNSISISGYHMQEAGADAVLEMAFTIADGIQYCETGLNAGLTIDAFAPRLSFFWGISMNFYMEIAKMRAARRLWANLIKERFSPKSDKSMMLRTHSQTSGWSLTEQDPYNNIIRTTIEAMASVFGGTQSLHTNSFDEALGLPTKFSARIARNTQIIIQEESGICNVADPWGGSYMMESLTDEIYEKALAVIKEIDELGGMAKAVASGMTKLKIEEAAAKKQARIDAGKDVIVGVNKYRLDHEQQVEVLKIDNAKVREEQCAKLNHIRATRDAEKAQKALDAITEGARGNGNLMELAIEAARARCTVGEISDAMEKVFNRHAAVNRLVSGAYKSEFGETSEMSQVLERVKSFADRDGRQPRIMVAKMGQDGHDRGAKVIATGFADLGFDVDVGPLFQTPLEAAQQAVDADVHVIGASSLAAGHLTLIPQLIGELKKLGRPDILVVAGGVIPPQDYKELYDAGVALVFGPGTRLPACANQILEKLEANLPEAPGKAASR
Protein: Probable Hsp90 co-chaperone cdc37 (Cell division cycle-related protein 37) (Hsp90 chaperone protein kinase-targeting subunit) (O02108)
Organism: Caenorhabditis elegans
Function: Co-chaperone that binds to numerous kinases and promotes their interaction with the Hsp90 complex, resulting in stabilization and promotion of their activity (By similarity). Inhibits daf-21/Hsp90 ATPase activity.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Heat shock protein 90
- Stress-induced-phosphoprotein 1
- Heat shock protein 70
- Serine/threonine-protein phosphatase 5
- Cyclin-dependent kinase 4 homolog
- Endoplasmin homolog
- Co-chaperone protein daf-41
- Histidine kinase/HSP90-like ATPase domain-containing protein
- Probable cyclin-dependent kinase 9
- Raf homolog serine/threonine-protein kinase
Sequence:
MPIDYSKWKDIEVSDDEDDTHPNIDTPSLFRWRHQARLERMAEKKMEQEKIDKEKGTTSKKMEELEKKLAAADVTDKSDIQKQIDEVKAQEEAWRKKEAELEEKERLEPWNVDTIGHEAFSTSRINKITEKKPQAPKTDEEDTHAMSTFFETHESLLEKMAVLKNGAKSTELFLAEHPHMASEYTANWLTIEALNAAIDFNEEKMKTMAEQCIIIQYLLELSKSLNAVATNTTVQKQFFKKFEAAEPVYMKHYQDEVKAFEDRLRTRAQTKRDAAMEEAEAEEKAERMKSAPGGIDPQEVFEQLPEEMRKCFEAHDIEALKGVAQKMDEEVFKYHFDRCIASGLWVPGKADDDDDDEEAAPAEEEPTTSS
Protein: Transcription factor bHLH154 (BHLH transcription factor beta) (bHLH beta) (Basic helix-loop-helix protein 154) (AtbHLH154) (bHLH 154) (bHLH transcription factor bHLH154) (Q7XJU1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- C2H2-like zinc finger protein
- AT5g54630/MRB17_13
- C2H2-like zinc finger protein
- High mobility group B protein 15
- Scarecrow-like protein 11
- Homeobox-leucine zipper protein HDG4
- Duplicated homeodomain-like superfamily protein
- Non-specific lipid-transfer protein 8
- Homeobox-leucine zipper protein HDG7
- Homeobox-leucine zipper protein HDG5
Sequence:
MEYSRDSAEMMMETKRNVYSLEDNKIKRHKSSDLSFSSKERKDKLAERISALQQLVSPYGKTDTASVLLEGMQYIQFLQEQVKVLSAPYLQATPSTTEEEVEEYSLRSKGLCLVPLEYTSEVAQTNGADIWAPVKTPTSSHAFNLSSSNSPFQ
Protein: High affinity nitrate transporter 2.7 (AtNRT2:7) (Q9LYK2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in high-affinity nitrate transport. Controls nitrate content in seeds.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:17540716}; Multi-pass membrane protein {ECO:0000269|PubMed:17540716}.
Interaction partners:
- Nitrate reductase 1
- Ferredoxin--nitrite reductase, chloroplastic
- Nitrate reductase 2
- Protein NRT1/ PTR FAMILY 2.12
- High-affinity nitrate transporter 3.1
- Protein NRT1/ PTR FAMILY 2.13
- Protein NRT1/ PTR FAMILY 6.2
- Protein NRT1/ PTR FAMILY 2.9
- Chloride channel protein CLC-a
- Protein NRT1/ PTR FAMILY 7.3
Sequence:
MEPSQRNTKPPSFSDSTIPVDSDGRATVFRPFSLSSPHSRAFHLAWLSLFSCFFSTFSIPPLVPVISSDLNLSASTVSAAGIASFAGSIFSRLAMGPLCDLIGPRTSSAILSFLTAPVILSASLVSSPTSFILVRFFVGFSLANFVANQYWMSSMFSGNVIGLANGVSAGWANVGAGISQLLMPLIYSTIAEFLPRAVAWRVSFVFPAIFQVTTAVLVLLYGQDTPHGNRKNSNQNKLTIPEEEEVLVVEEDERSSFVEILIGGLGNYRAWILALLYGYSYGVELTTDNVIAGYFYERFGVNLEAAGTIAASFGISNIASRPAGGMISDALGKRFGMRGRLWGLWIVQSVAGLLCVLLGRVNSLWGSILVMWVFSVFVQAASGLVFGVVPFVSTRSLGVVAGITGSGGTVGAVVTQFLLFSGDDVRKQRSISLMGLMTFVFALSVTSIYFPQWGGMCCGPSSSSEEEDISRGLLVEDEDEEGKVVSGSLRPVC
Protein: RE18364p (Q8SY09)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSDEDVALQKLAISSFDRMVLKNIQPLEYSNEAKHFMPWRIISTLLMTQPRAYLQERFAVLLERETIVTPRLVNVIISHLSTSMATDAWGLLLFLSSRITNNMDALIGIFNGLSSYNMKSNQFLALQLITGCLRNFSKPALNQLFQKLLNALRTGSIWLGIISSAVNLLNQIHHLSTSQSPTIASEMPYWQLSLLEDLVEGILSSAQNFQEEYARLQCLLGAYTELIVMVPQDVDNRIVSIVFKYLQECTKLCESEFDSDNERMTNWMIVIAGRLSLRDNHLANSASKLYITILTKNDRPQIINTTLIALNDLGKKHPSILESNFQAILSKLQSKFAMTRVRTFRCVKDVILSGNIKLKGPILISMLAALVDESAEVAREADAFFTRYKKLYNKMLFDHCLKECPFDLNDQAILRGVRTNGNYKSPLKGSQMAKKRRLLYNHIMSSMDENVLLLYFGQLKLLAEKTRDQAFINNPDALIVVQDMLFIMRRICYCTKGMGKEKNSRGEGDNIDEGEDASSEPATPPTRPEAGEATSRGRGRKADMSEEPLKQLERCLRFVEETHRNIVPVMSPELSHNFESFCRAMAMRFPNYIEFAQPAQFWRQFRSSAKAPRASRSKRRRMEEGEVESHEEHESESDSDSELPLDRHKTTPTASRLSQRKTSCDMLVTELIFQPPDW
Protein: Protein kinase, cAMP-dependent, regulatory, type II, beta (Q6DHZ2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSIEIPAGLTELLQGFTVEVLRHQPADLLEFALQHFTRLQQENERKGTARFCHEGRTWGDLGAAAGGGTPSKGVNFAEEPMQSDSEDGEEEEAAPADAGAFNAPVINRFTRRASVCAEAYNPDEEEDDAESRIIHPKTDDQRNRLQEACKDILLFKNLDPEQMSQVLDAMFEKLVKDGEHVIDQGDDGDNFYVIDRGTFDIYVKCDGVGRCVGNYDNRGSFGELALMYNTPRAATITATSPGALWGLDRVTFRRIIVKNNAKKRKMYESFIESLPFLKSLEFSERLKVVDVIGTKVYNDGEQIIAQGDSADSFFIVESGEVKITMKRKGKSEVEENGAVEIARCSRGQYFGELALVTNKPRAASAHAIGTVKCLAMDVQAFERLLGPCMEIMKRNIATYEEQLVALFGTNMDIVEPTA
Protein: Probable E3 ubiquitin-protein ligase IRF2BPL (EC 2.3.2.27) (Enhanced at puberty protein 1) (Interferon regulatory factor 2-binding protein-like) (Polyglutamine-containing protein) (Q5EIC4)
Organism: Rattus norvegicus (Rat)
Function: Probable E3 ubiquitin protein ligase involved in the proteasome-mediated ubiquitin-dependent degradation of target proteins. Through the degradation of CTNNB1, functions downstream of FOXF2 to negatively regulate the Wnt signaling pathway. Probably plays a role in the development of the central nervous system and in neuronal maintenance (By similarity). Also acts as a transcriptional regulator of genes controlling female reproductive function. May play a role in gene transcription by transactivating GNRH1 promoter and repressing PENK promoter.
Subcellular location: Nucleus {ECO:0000269|PubMed:17627301}.
Interaction partners:
Sequence:
MSAAQVSSSRRQSCYLCDLPRMPWAMIWDFSEPVCRGCVNYEGADRIEFVIETARQLKRAHGCFQDGRSPGPPPPVGVKTVALSAKEAAAAAAAAQQQQQQQQQQQQQQQQQPQQLNHVDGSTKPAVLPAPSGLERYGLSAAAAAAAAAAAAVEQRSRFEYPPPPVSLGSSSHAARLPNGLGGPNGFPKPAPEEGPPELNRQSPNSSSAATSVASRRGTHSGLVTGLPNPGGGGGPQLTVPPNLLPQTLLNGPASAAVLPPPHGLGGSRGPPTPAPPGAPGGPACLGGPPGVSATVSSAPSSTSSTVAEVGVGAAGKRPGSVSSTDQERELKEKQRNAEALAELSESLRNRAEEWANKPKMVRDTLLTLAGCTPYEVRFKKDHSLLGRVFAFDAVSKPGMDYELKLFIEYPTGSGNVYSSASGVAKQMYQDCMKDFGRGLSSGFKYLEYEKKHGSGDWRLLGDLLPEAVRFFKEGVPGADMLPQPYLDASCPMLPTALVSLSRAPSAPPGTGALPPAAPTGRGAAASLRKRKASPEPPDSAESALKLGEEQQRQQWMANQSEALKLTMSAGGFAAPGHAAGGPPPPPPPLGPHSNRTTPPESAPQNGPSPMAALMSVADTLGTAHSPKDGSSVHSTTASARRNSSSPVSPASVPGQRRLASRNGDLNLQVAPPPPSAHPGMDQVHPQNIPDSPMANSGPLCCTICHERLEDTHFVQCPSVPSHKFCFPCSRESIKAQGATGEVYCPSGEKCPLVGSNVPWAFMQGEIATILAGDVKVKKERDP
Protein: phosphoglucomutase (alpha-D-glucose-1,6-bisphosphate-dependent) (EC 5.4.2.2) (F4I6W4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFLLVTSCFLPDSGSSVKVSLFIFGTKRDPTKKKNEKRRATRVTFSFSLFISFPQTHCVKRLLFYHLQAYSIFFRFEMVSFKVSLVSTSPIDGQKPGTSGLRKKVKVFKQPNYLENFVQATFNALTTEKVKGATLVVSGDGRYYSEQAIQIIVKMAAANGVRRVWVGQNSLLSTPAVSAIIRERVGADGSKATGAFILTASHNPGGPTEDFGIKYNMENGGPAPESITDKIYENTKTIKEYPIAEDLPRVDISTIGITSFEGPEGKFDVEVFDSADDYVKLMKSIFDFESIKKLLSYPKFTFCYDALHGVAGAYAHRIFVEELGAPESSLLNCVPKEDFGGGHPDPNLTYAKELVARMGLSKTDDAGGEPPEFGAAADGDADRNMILGKRFFVTPSDSVAIIAANAVGAIPYFSSGLKGVARSMPTSAALDVVAKNLGLKFFEVPTGWKFFGNLMDAGMCSVCGEESFGTGSDHIREKDGIWAVLAWLSILAHKNKETLDGNAKLVTVEDIVRQHWATYGRHYYTRYDYENVDATAAKELMGLLVKLQSSLPEVNKIIKGIHPEVANVASADEFEYKDPVDGSVSKHQGIRYLFEDGSRLVFRLSGTGSEGATIRLYIEQYEKDASKIGRDSQDALGPLVDVALKLSKMQEFTGRSSPTVIT
Protein: E3 ubiquitin-protein ligase RNF4 (EC 2.3.2.27) (RING finger protein 4) (Small nuclear ring finger protein) (Protein SNURF) (P78317)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation. Catalyzes ubiquitination of sumoylated PARP1 in response to PARP1 trapping to chromatin, leading to PARP1 removal from chromatin by VCP/p97.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12885770}. Nucleus {ECO:0000269|PubMed:12885770}. Nucleus, PML body {ECO:0000269|PubMed:15707587, ECO:0000269|PubMed:20943951}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 D1
- Small ubiquitin-related modifier 2
- Ubiquitin-conjugating enzyme E2 N
- Polyubiquitin-C
- Small ubiquitin-related modifier 1
- Polyubiquitin-B
- Ubiquitin-ribosomal protein eL40 fusion protein
- Ubiquitin-ribosomal protein eS31 fusion protein
- Protein PML
- Ubiquitin-conjugating enzyme E2 variant 2
Sequence:
MSTRKRRGGAINSRQAQKRTREATSTPEISLEAEPIELVETAGDEIVDLTCESLEPVVVDLTHNDSVVIVDERRRPRRNARRLPQDHADSCVVSSDDEELSRDRDVYVTTHTPRNARDEGATGLRPSGTVSCPICMDGYSEIVQNGRLIVSTECGHVFCSQCLRDSLKNANTCPTCRKKINHKRYHPIYI
Protein: Mitochondrial ribosomal protein L2 (Q9VTF8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Large ribosomal subunit protein uL14
- Ribosomal protein
- Large ribosomal subunit protein uL16m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL20m
- Small ribosomal subunit protein uS12m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL22m
- Small ribosomal subunit protein uS2m
Sequence:
MQSVTRLLSTTLTIQTPFRTAPAFLQQLRGKTKVVEKPKPGAGQQFRRTVHFPEKYTVEPLKITHLAGRDPVSGRLVAKGIGGGIKQQYRWVKWVRDGPTEGAQEELVLEVLRDGCRTAKVALVAVGDELKYILATENMKAGDILKTSRFIPRIPVRPNEGDAYPLGALPVGTRIHCLEKNPGQMCHLIHAAGTFGTILRKFDEKVVVQLPSKREFAFQRTCMATVGRLSNPEHNKEHVGSAQRMREMGNRPRSGLWKRKEGKHGRKIRRLPPMTTISPPAPPKEEAIKLTLPL
Protein: Alpha-fetoprotein (Alpha-1-fetoprotein) (Alpha-fetoglobulin) (P02771)
Organism: Homo sapiens (Human)
Function: Binds copper, nickel, and fatty acids as well as, and bilirubin less well than, serum albumin. Only a small percentage (less than 2%) of the human AFP shows estrogen-binding properties.
Subcellular location: Secreted.
Interaction partners:
- Prothrombin
- Cell adhesion molecule CEACAM5
- Albumin
- Alpha-1-antitrypsin
- Glypican-3
- Alpha-2-HS-glycoprotein
- Apolipoprotein A-II
- Alanine aminotransferase 1
- Transthyretin
- Keratin, type I cytoskeletal 19
Sequence:
MKWVESIFLIFLLNFTESRTLHRNEYGIASILDSYQCTAEISLADLATIFFAQFVQEATYKEVSKMVKDALTAIEKPTGDEQSSGCLENQLPAFLEELCHEKEILEKYGHSDCCSQSEEGRHNCFLAHKKPTPASIPLFQVPEPVTSCEAYEEDRETFMNKFIYEIARRHPFLYAPTILLWAARYDKIIPSCCKAENAVECFQTKAATVTKELRESSLLNQHACAVMKNFGTRTFQAITVTKLSQKFTKVNFTEIQKLVLDVAHVHEHCCRGDVLDCLQDGEKIMSYICSQQDTLSNKITECCKLTTLERGQCIIHAENDEKPEGLSPNLNRFLGDRDFNQFSSGEKNIFLASFVHEYSRRHPQLAVSVILRVAKGYQELLEKCFQTENPLECQDKGEEELQKYIQESQALAKRSCGLFQKLGEYYLQNAFLVAYTKKAPQLTSSELMAITRKMAATAATCCQLSEDKLLACGEGAADIIIGHLCIRHEMTPVNPGVGQCCTSSYANRRPCFSSLVVDETYVPPAFSDDKFIFHKDLCQAQGVALQTMKQEFLINLVKQKPQITEEQLEAVIADFSGLLEKCCQGQEQEVCFAEEGQKLISKTRAALGV
Protein: L-ascorbate peroxidase 3 (AtAPx03) (EC 1.11.1.11) (Q42564)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a key role in hydrogen peroxide removal.
Subcellular location: Peroxisome membrane {ECO:0000269|PubMed:16873450, ECO:0000269|PubMed:20215589}; Single-pass membrane protein {ECO:0000269|PubMed:16873450}. Glyoxysome membrane {ECO:0000269|PubMed:16873450}; Single-pass membrane protein {ECO:0000269|PubMed:16873450}.
Interaction partners:
- Monodehydroascorbate reductase 3
- Glutathione S-transferase DHAR2
- Glutathione S-transferase DHAR1, mitochondrial
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- Glutathione reductase, chloroplastic
- Probable phospholipid hydroperoxide glutathione peroxidase 6, mitochondrial
- Probable glutathione peroxidase 5
- Phospholipid hydroperoxide glutathione peroxidase 1, chloroplastic
- Probable glutathione peroxidase 2
- Probable glutathione peroxidase 4
Sequence:
MAAPIVDAEYLKEITKARRELRSLIANKNCAPIMLRLAWHDAGTYDAQSKTGGPNGSIRNEEEHTHGANSGLKIALDLCEGVKAKHPKITYADLYQLAGVVAVEVTGGPDIVFVPGRKDSNVCPKEGRLPDAKQGFQHLRDVFYRMGLSDKDIVALSGGHTLGRAHPERSGFDGPWTQEPLKFDNSYFVELLKGESEGLLKLPTDKTLLEDPEFRRLVELYAKDEDAFFRDYAESHKKLSELGFNPNSSAGKAVADSTILAQSAFGVAVAAAVVAFGYFYEIRKRMK
Protein: Tripartite motif containing 4 (H7C0Q6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XDDQRPVCLVCRESQEHQTHAMAPIDEAFESYREKLLKSQRNLVAKMKKVMHLQDVEVKNATQWKDKIKSQRMRISTEFSKLHNFLVEEEDLFLQRLNKEEEETKKKLNENTLKLNQTIASLKKLILEVGEKSQAPTLELLQNPKEVLTRSEIQDVNYSLEAVKVKTVCQIPLMKEMLKRFQGIEKGDNVAEESDLSGRLHP
Protein: Lipid storage droplets surface-binding protein 1 (Q9VCI3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal deposition of neutral lipids in the oocyte.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12077142}. Lipid droplet {ECO:0000269|PubMed:12077142}. Note=Cytoplasmic and in lipid storage droplets of adipocytes of first instar larvae. Colocalizes with Lsd-2 on the surface of neutral lipid storage droplets in cells of fat bodies.
Interaction partners:
- Hormone-sensitive lipase, isoform A
Sequence:
MATATSGSGLHLEAIDRIGSIPLVESSVKRVETIYDKVKNNNRLFSWYFETAEATISAAYETIQPAVKLFEPSIQRLDNVMCKSLDILEQRIPLVYLPPEMMYWNTKEYMSDHLVRPVLKRADSVKQIGNAVLESPLTTYAAERIDGAFTVGDKFVDKYLVPIQTDQDQTDVKKLVSALNDNFSPIRQQLNRMFGHKSPQEDDNEAVPDERGAIKAIHHGQRFSRKLKRRLTQRTIAEARALKKQSKEAIHVLFYAAELIATDPKQAVQKAKELWVYLSADEPENQARPATLEQLIVLLTRESARRVVHLVNFSAHVAANIPRNLAHTTTEVAHHIIYINHRIITISRLDKVKTISKEEAESLFKRMLAFYGSLQGLTNAYLERVASFLSGRMEAEKVTGSDGGNSNHRSSRRRQDPNHYSATHNNINGVY
Protein: Selenocysteine insertion sequence-binding protein 2 (SECIS-binding protein 2) (Q96T21)
Organism: Homo sapiens (Human)
Function: Binds to the SECIS element in the 3'-UTR of some mRNAs encoding selenoproteins. Binding is stimulated by SELB.
Subcellular location: [Isoform 1]: Nucleus {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion {ECO:0000269|PubMed:19004874}.
Interaction partners:
- Selenocysteine-specific elongation factor
- Large ribosomal subunit protein eL30
- tRNA selenocysteine 1-associated protein 1
- Type II iodothyronine deiodinase
- Selenoprotein K
- L-seryl-tRNA
- Thioredoxin reductase-like selenoprotein T
- O-phosphoseryl-tRNA
- Selenoprotein N
- Small ribosomal subunit protein uS10
Sequence:
MASEGPREPESEGIKLSADVKPFVPRFAGLNVAWLESSEACVFPSSAATYYPFVQEPPVTEQKIYTEDMAFGASTFPPQYLSSEITLHPYAYSPYTLDSTQNVYSVPGSQYLYNQPSCYRGFQTVKHRNENTCPLPQEMKALFKKKTYDEKKTYDQQKFDSERADGTISSEIKSARGSHHLSIYAENSLKSDGYHKRTDRKSRIIAKNVSTSKPEFEFTTLDFPELQGAENNMSEIQKQPKWGPVHSVSTDISLLREVVKPAAVLSKGEIVVKNNPNESVTANAATNSPSCTRELSWTPMGYVVRQTLSTELSAAPKNVTSMINLKTIASSADPKNVSIPSSEALSSDPSYNKEKHIIHPTQKSKASQGSDLEQNEASRKNKKKKEKSTSKYEVLTVQEPPRIEDAEEFPNLAVASERRDRIETPKFQSKQQPQDNFKNNVKKSQLPVQLDLGGMLTALEKKQHSQHAKQSSKPVVVSVGAVPVLSKECASGERGRRMSQMKTPHNPLDSSAPLMKKGKQREIPKAKKPTSLKKIILKERQERKQRLQENAVSPAFTSDDTQDGESGGDDQFPEQAELSGPEGMDELISTPSVEDKSEEPPGTELQRDTEASHLAPNHTTFPKIHSRRFRDYCSQMLSKEVDACVTDLLKELVRFQDRMYQKDPVKAKTKRRLVLGLREVLKHLKLKKLKCVIISPNCEKIQSKGGLDDTLHTIIDYACEQNIPFVFALNRKALGRSLNKAVPVSVVGIFSYDGAQDQFHKMVELTVAARQAYKTMLENVQQELVGEPRPQAPPSLPTQGPSCPAEDGPPALKEKEEPHYIEIWKKHLEAYSGCTLELEESLEASTSQMMNLNL
Protein: Flavin-dependent halogenase otaD (EC 1.14.14.-) (Ochratoxin A biosynthesis cluster protein D) (A0A1R3RGJ2)
Organism: Aspergillus carbonarius (strain ITEM 5010)
Function: Flavin-dependent halogenase; part of the gene cluster that mediates the biosynthesis of ochratoxin A (OTA), a mycotoxin composed of a chlorinated type I polyketide dihydroisocoumarin moiety linked to L-phenylalanine, and demonstrated to have nephrotoxic, immunotoxic, genotoxic, neurotoxic, and teratogenic properties. OtaD chlorinates ochratoxin B (OTB) at the C-5 position to form OTA. The pathway begins with the highly reducing polyketide synthase otaA that catalyzes the formation of the isocoumarin group during the initial stages of biosynthesis, starting from one acetate and 4 malonate units, to originate the characteristic pentaketide skeleton 7-methylmellein (7-MM) of the OTA molecule. The newly identified cyclase otaY might be involved in the polyketide cyclization reaction during the initial steps of the OTA biosynthesis. 7-MM is then oxidized into 7-carboxymellein (also called ochratoxin beta) by the cytochrome P450 monooxygenase otaC. The NRPS encoded by the otaB gene is involved in the linking of phenylalanine to the dihydroisocoumarin ring. The reaction catalyzed by NRPS results in the production of ochratoxin B (OTB), which is the non-chlorinated analog of OTA and which subsequently serves as the substrate of the halogenase otaD for chlorination activity to form the final molecular structure of OTA, containing a chlorine atom in the C-5 position of the molecule (Probable).
Interaction partners:
Sequence:
MAIPQKATVLVIGGGPGGSYSASALAREGIDTVVLEADVFPRYHIGESLVASIRPFLKFIDLDDTFVNYGFVRKNGAAFKLNNQKEAYTDFILEAGADTFAWNVVRSESDDLMFKHAAKSGAQTFDGVRVTSIEFTDDDDDDDNNTNRPVSASWKAKDGRTGSIEFDYLVDASGRAGITSTKYLKNRTFNNYLKNVASWGYWEGATPYGMGTPVEGQPFFEALQDGSGWVWFIPLHNNTTSIGIVMNQELSTQKKKLSTTTSSRAFYLESLAGARGISRLLDPTTATLTSDIKHASDWSYNASAYGSPYLRIVGDAGAFIDPYFSSGVHLAVSGGLSAAVSIAASIRGDCPEEAAWKWHSQGVANRYGRFLLVVLGATKQIRAGDRPVLNGVGDEGFDEAFMVIRPVIQGIADVQGKVPVQDVYDAVTFSTNVVQPAAEGKRDPGWVEKARGALSHDEKEVGSVLNNLAKAYKTTDVCEGLMARLERGHLGLKLVSEV
Protein: Ly6/PLAUR domain-containing protein 2 (Q6UXB3)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Lymphocyte antigen 6K
- Ly-6/neurotoxin-like protein 1
- Lymphocyte antigen 6H
Sequence:
MRGTRLALLALVLAACGELAPALRCYVCPEPTGVSDCVTIATCTTNETMCKTTLYSREIVYPFQGDSTVTKSCASKCKPSDVDGIGQTLPVSCCNTELCNVDGAPALNSLHCGALTLLPLLSLRL
Protein: Chloride channel protein 2 (A0A098DN12)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00004554}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004554}. Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cell projection, dendritic spine membrane {ECO:0000256|ARBA:ARBA00004332}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004332}.
Interaction partners:
- Family with sequence similarity 131 member A.
- Uncharacterized protein.
Sequence:
MAVDGQEQRALQYEQTLMYGRYTQELGVYAREEAARLREDGRQRRSISERSPSLKLLEYEKGRCVKCRICAVHCQRFLMSRVGEDWIFLILLGLVMALVSFVMDFCIALLLQAQKWMYGGLDSNVVLQYLAWVTYPVVLISFSAGFTHIVAPQAAGSGIPEMKTILRGVVLKEYLTLKTFVAKVVGLTCALGSGLPLGKEGPFVHIASLCAALLCKFMSFFGGIYENESRNIEMLAAACAVGVGCCFAAPIGGVLFSIEVTSTFFAVRNYWRGFFAATFSAFIFRVLAVWNRDEETITALFKTRFRLDFPFDLQELPAFAVIGIASGFGGALFVYLNRLIVQFMRKQKTINKFLMKKRLLYPALVTLLISTLSFPPGFGQFMAGQLTQKETLVSFFDNRTWAKQGISEDFTFDTHLMAWKHPQANVFIILVIFIIMKFWMSALATTLPVPCGAFMPVFVIGAAFGRLVGESMAAWFPEGINTDGTIYPIVPGGYAVVGAAALSGAVTHTVSTAVIVFELTGQISHILPIMIAVILANAVAQSLQPSIYDSIIRIKKLPYLPELGWGHHEKYNIRVEDIMVRDVRYITLNSTYRDLQDILTIGNLKTVALVESADSMILLGSIERAQLQALLVQQVSRVRRQEVMRERAETERKRMSVASSPSSDDSSQKVNQEVRFQISTEESTFVPVRPISPKPLKPALKRTSVAEKNIEIPTSPHDSSMGLKNLLCARPQTDVMEESNNVELRQSKRVRISLLDDPDAEDDMTLGEIEEWEEQQLDEQVNFNSCKIDPAPFQLVERTSLHKTHTIFSLLGLDHAYVTSIGRLIGVVSLRELRKAIEGSMTVKGVKVRPPLASFRDSGTSGTSSESEATELHKLWDRHSSLSLPRDQQNHNTDNKTH
Protein: Secreted protein BARF1 (33 kDa early protein) (p33) (P03228)
Organism: Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4)
Function: Plays diverse functions in immunomodulation and oncogenicity, maybe by acting as a functional receptor for human CSF1. May inhibit interferon secretion from mononuclear cells. Exhibits oncogenic activity in vitro.
Subcellular location: Secreted {ECO:0000269|PubMed:18533018}. Note=Massively secreted in the serum of EBV-induced nasophyryngeal carcinoma patients.
Interaction partners:
Sequence:
MARFIAQLLLLASCVAAGQAVTAFLGERVTLTSYWRRVSLGPEIEVSWFKLGPGEEQVLIGRMHHDVIFIEWPFRGFFDIHRSANTFFLVVTAANISHDGNYLCRMKLGETEVTKQEHLSVVKPLTLSVHSERSQFPDFSVLTVTCTVNAFPHPHVQWLMPEGVEPAPTAANGGVMKEKDGSLSVAVDLSLPKPWHLPVTCVGKNDKEEAHGVYVSGYLSQ
Protein: Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma (AtB''gamma) (Serine/threonine protein phosphatase 2A regulatory subunit B''beta 2 isoform) (AtB''beta 2) (PP2A, B'' subunit, beta 2 isoform) (Q8VZQ4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable regulatory subunit of type 2A protein phosphatase.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15610358}. Nucleus {ECO:0000269|PubMed:15610358}.
Interaction partners:
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase PP2A-4 catalytic subunit
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' alpha isoform
- Serine/threonine-protein phosphatase PP2A-3 catalytic subunit
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' beta isoform
- Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' eta isoform
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' kappa isoform
- Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' epsilon isoform
- Serine/threonine protein phosphatase 2A 59 kDa regulatory subunit B' gamma isoform
Sequence:
MVDTVIPGDMACLDADLLQLQEMSSFVLNSKPGFTQKLFDQWLSLPEAQRQVGSLLKDAVAGAPINVTGSASGSNSATIPSMFPAGSAPPLSPRSCGSPRTTKQRAPSNLGSTLKVVNEPVKEPIPQFYFQNGRPPPSEIKEQCMFRINHFFYGHMDGLQIQEFKLVTREICKLPSFFSTSLFRKIDLNNTGFVTRDAFIDFWVNGNMLIMDTTTQIFKILKQKDQSFIVKDDFKPLLKELLATHPGLEFLQSTPEFQERYAETVTYRIFYYINRSGNGRITFRELKRGNLIDAMLHADEEEDINKVLRYFSYEHFYVIYCKFWELDTDHDFLIDKENLMRYGNHALTYRIVDRIFSQVARKFTNKVEGKMGYEDFVYFILAEEDKSSVPSLEYWFKCIDLDANGIITRNEMQFFYEEQLHRMECMAQEAVLFEDILCQMIDMIGPENESHITLHDLKGSKLSGNVFNILFNLNKFMAFETRDPFLIRQERENPTLTDWDRFAHREYIRLSMEEDVEDASNGSAEVWDESSLEAPF
Protein: Metallo-beta-lactamase type 2 (EC 3.5.2.6) (B2 metallo-beta-lactamase) (Beta-lactamase II) (Cephalosporinase) (Metallo-beta-lactamase type II) (Metallothioprotein beta-lactamase II) (Penicillinase) (Zinc-requiring beta-lactamase II) (P14488)
Organism: Bacillus cereus
Function: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Benzylpenicillin is a better substrate than cephalosporin C and ampicillin.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
Sequence:
MKNTLLKLGVCVSLLGITPFVSTISSVQAERTVEHKVIKNETGTISISQLNKNVWVHTELGYFSGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFKKRVTDVIITHAHADRIGGMKTLKERGIKAHSTALTAELAKKNGYEEPLGDLQSVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYQILAGGCLVKSASSKDLGNVADAYVNEWSTSIENVLKRYGNINLVVPGHGEVGDRGLLLHTLDLLK