wanglab/gogpt-training-data huggingface dataset:
Protein: CLIP domain-containing serine protease C9 (EC 3.4.21.-) [Cleaved into: CLIP domain-containing serine protease C9 subunit p12; CLIP domain-containing serine protease C9 subunit p30] (A0A1S4GMJ4)
Organism: Anopheles gambiae (African malaria mosquito)
Function: Probable serine protease which plays an essential role in the innate immune response against bacteria and protozoa infection by activating the melanization cascade. In the susceptible strain G3, appears to be dispensable for ookinete elimination which occurs by lysis.
Subcellular location: Secreted {ECO:0000269|PubMed:33045027}. Note=Secreted into the hemolymph (PubMed:33045027). Recruited by CLIPA8 to microbial surfaces where it is cleaved into the two chain active form (PubMed:33045027). {ECO:0000269|PubMed:33045027}.
Interaction partners:
Sequence:
MCILTLVERKHLKNMVHVRLLVMMHILIIYSTFGAVRRPINIRVLEGNSCDTPQVIGGKCMNISLCDPAFVHSIAYQEHTPVCQQNAFYRVICCQPFLDFCENSKQFQIMHGIEAEPGMFPHLARLGLKSEEDGIAWTCSANIISERFLLTAAHCNPVNIAGLGCAESMQCDQQNTVKSFISNPKYKTSFKYHDIALVELEQNIRFNKRVLPICPYISKTDLHESEDLVIAGWGATESHFQSPRLMFATVRTVLQNDCKDHYASLLKASPNKKLHQGITDEMYCAQGALVDNVTEYIDACSGDSGGPLQTKQNNNLYLIGVISTGFGCGSSSPGLYTRVASYFGWIKETVSATRDN
Protein: UDP-galactose transporter homolog 1 (Q8WZJ9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in specific transport of UDP-Gal from the cytosol to the Golgi lumen (By similarity). Involved in the maintenance of optimal conditions for the folding of secretory pathway proteins in the endoplasmic reticulum.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- UDP-galactose transporter
- Putative transporter C83.11
- Uncharacterized protein C12G12.12
- UDP-N-acetylglucosamine transporter yea4
- Uncharacterized transporter C22F8.04
- Large ribosomal subunit protein eL15B
- Protein bem46
- Large ribosomal subunit protein eL15A
- Periodic tryptophan protein 2 homolog
- GDP-mannose transporter
Sequence:
MAGFMRQLFVCMIGIYGSFLSWAVMQEKIITRPYDGERFSSPALLSLAQSFMTVLCGLLWNWFHGVSARGLLEPKFLGYFSSIAISASLSSYFGYASMFHLSYPTVILGKSCKLLPVIALHVFVYKRKFPPHKYLIVTMITAGVSIFSYFQNTSSKGKHAEHDSPIGLLLLFFNLLMDGITNTTQDKVFGKYKLSSVTMMIAVNLGIACLNGLYLISPFCNQQPLSFINRHPSILKDMLLFACTGSVGQLFIFFTLEKFGSITLVTITLTRKIFTMLLSVFHFHHTVSSIQWLGILLVFLGISLEAGLKILNNNSTAKKKAS
Protein: DNA polymerase lambda (Pol Lambda) (EC 2.7.7.7) (EC 4.2.99.-) (DNA polymerase kappa) (Q9QXE2)
Organism: Mus musculus (Mouse)
Function: DNA polymerase that functions in several pathways of DNA repair. Involved in base excision repair (BER) responsible for repair of lesions that give rise to abasic (AP) sites in DNA. Also contributes to DNA double-strand break repair by non-homologous end joining and homologous recombination. Has both template-dependent and template-independent (terminal transferase) DNA polymerase activities. Has also a 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q9UGP5}.
Interaction partners:
- DNA ligase 4
- X-ray repair cross-complementing protein 6
- DNA repair protein XRCC4
- X-ray repair cross-complementing protein 5
- DNA repair protein XRCC1
- Non-homologous end-joining factor 1
- DNA ligase 1
- DNA-dependent protein kinase catalytic subunit
- Terminal nucleotidyltransferase 4A
- Single-strand selective monofunctional uracil DNA glycosylase
Sequence:
MDPQGIVKAFPKRKKSHADLSSKALAKIPKREVGEARGWLSSLRAHIMPAGIGRARAELFEKQIIHHGGQVCSAQAPGVTHIVVDEDMDYERALRLLRLPQLPPGAQLVKSTWLSLCLQEGRLTDTEGFSLPMPKRSLDEPQPSKSGQDASAPGTQRDLPRTTLSLSPPHTRAVSPPPTAEKPSRTQAQLSSEDETSDGEGPQVSSADLQALITGHYPTPPEEDGGPDPAPEALDKWVCAQPSSQKATNYNLHITEKLEVLAKAYSVQGDKWRALGYAKAINALKSFHKPVSSYQEACSIPGIGKRMAEKVMEILESGHLRKLDHISDSVPVLELFSNIWGAGTKTAQMWYHQGFRNLEDLQSLGSLTAQQAIGLKHYDDFLDRMPREEAAEIEQTVRISAQAFNPGLLCVACGSYRRGKMTCGDVDVLITHPDGRSHRGIFSCLLDSLRQQGFLTDDLVSQEENGQQQKYLGVCRLPGPGKRHRRLDIIVVPYCEFACALLYFTGSAHFNRSMRALAKTKGMSLSEHALSAAVVRNSQGVKVGPGQVLPTPTEKDVFKHLGLPYREPAERDW
Protein: Ubiquitin-conjugating enzyme E2 (EC 6.3.2.19) (Q8IDP1)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MFNIMRPIILFNILIGYYFFIVINNVVGNLPKKNSYYNIPNYKVKNVSNIKNNKYNYFIIDTYNNMKRKNNSIYEHNFNNFNRKNKTYLFIDNKKRRRKFFYSKIEENKNLQGKELKPSRTVEKHIKTKYNLGNANYRIQKELNNFLKNPPINCTIDVHPSNIRIWIVQYVGLENTIYANEVYKIKIIFPDNYPLKPPIVYFLQKPPKHTHVYSNGDICLSVLGDDYNPSLSISGLILSIISMLSSAKEKKLPIDNYTHADAKPGSSQNNFLYHDDKC
Protein: INO80 complex subunit E (J3KNE2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNGPADGEVDYKKKYRNLKRKLKFLIYEHECFQEELRKAQRKLLKVSRDKSFLLDRLLQYENVDEDSSDSDATASSDNSETEGTPKLSDTPAPKRKRSPPLGGAPSPSSLSLPPSTGFPLQASGVPSPYLSSMAVGPPDCPVGGPLTFPGRGSGAGVGTTLTPLPPPKMPPPTILSTVPRQMFSDAGSGDDALDGDDDLVIDIPE
Protein: Phosphate-binding protein (B6EI64)
Organism: Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238))
Subcellular location: Periplasm {ECO:0000256|RuleBase:RU367119}. Secreted {ECO:0000256|RuleBase:RU367119}.
Interaction partners:
Sequence:
MKKSVIGALAILSSVVALPASAKETISAVGSSSVTPLMEVFSETYMKDHSNVYIEVQGPGSSAGIKAAKNGSADLGMSSRNLKASEKEATLKELVVAHDGIAVVVNPSNTLKGLTSEQVTAIYKGEVKNWKEVGGEDKPIVAITRDTASGTRGAFEDIMSLKKKISGMKVSAISQRAQVANGNGALKTMVASNPYAIGYISLGTVDNSVHALSIDNVVPSVADIKNGTYKVSRPFLVLYREGKPSVETQKFLDWMTDETAQSLVEKNGYISVN
Protein: RE53819p (Q9VT24)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Peptidase S1 domain-containing protein
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
- Aminopeptidase
Sequence:
MKLFLLTLSVALAVVAASPGFNRTSLLPQVTISEGAEGRIVNGYPAPEGKAPYIVGLLIRTDGSNSAAVGAGTIIASDWILTAAHCLTTDYVEIHYGSNWGWNGAFRQSVRRDNFISHPNWPAEGGRDIGLIRTPSVGFTDLINKVALPSFSEESDRFVDTWCVACGWGGMDNGNLADWLQCMDVQIISNSECEQSYGTVASTDMCTRRTDGKSSCGGDSGGPLVTHDNARLVGVITFGSVDCHSGPSGYTRVTDYLGWIRDNTGISY
Protein: Probable very-long-chain (3R)-3-hydroxyacyl-CoA dehydratase (EC 4.2.1.134) (3-hydroxyacyl-CoA dehydratase) (HACD) (O14346)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the third of the four reactions of the long-chain fatty acids elongation cycle. This endoplasmic reticulum-bound enzymatic process, allows the addition of two carbons to the chain of long- and very long-chain fatty acids/VLCFAs per cycle. This enzyme catalyzes the dehydration of the 3-hydroxyacyl-CoA intermediate into trans-2,3-enoyl-CoA, within each cycle of fatty acid elongation. Thereby, it participates in the production of VLCFAs of different chain lengths that are involved in multiple biological processes as precursors of membrane lipids and lipid mediators.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P40857}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P40857}.
Interaction partners:
- Putative enoyl reductase C646.07c
- Very-long-chain 3-oxoacyl-CoA reductase
- Putative fatty acid elongase 1
- Putative fatty acid elongase 2
- Probable acyl-CoA desaturase
- Suppressor of kinetochore protein 1
- Protein rot1
- Orotate phosphoribosyltransferase
Sequence:
MSKILKIQYLKLYNVISCFLWMSVLLRTGLIWGITKDTAVVFHETNTLVRWVQTLAIAEVFHSIFGLVSSSPLTTIIQVASRLYLVWGVCYPFSYVIEGSPIYLSMIIAWSITEIIRYAFYAFNLNGDIPAFLTWLRYNTFLILYPIGAGSEFLLVLKSRIAAQYVWSLNKLLWPILMSIYPPGLYIMYTHMLAQRRKISKRAAARRT
Protein: Phytochrome C (P14714)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the Pr form that absorbs maximally in the red region of the spectrum and the Pfr form that absorbs maximally in the far-red region. Photoconversion of Pr to Pfr induces an array of morphogenic responses, whereas reconversion of Pfr to Pr cancels the induction of those responses. Pfr controls the expression of a number of nuclear genes including those encoding the small subunit of ribulose-bisphosphate carboxylase, chlorophyll A/B binding protein, protochlorophyllide reductase, rRNA, etc. It also controls the expression of its own gene(s) in a negative feedback fashion.
Interaction partners:
- Phytochrome B
- Cryptochrome-2
- Cryptochrome-1
- Transcription factor PIF3
- E3 ubiquitin-protein ligase COP1
- Protein GIGANTEA
- Protein EARLY FLOWERING 3
- Phototropin-2
- Phototropin-1
- Cryptochrome DASH, chloroplastic/mitochondrial
Sequence:
MSSNTSRSCSTRSRQNSRVSSQVLVDAKLHGNFEESERLFDYSASINLNMPSSSCEIPSSAVSTYLQKIQRGMLIQPFGCLIVVDEKNLKVIAFSENTQEMLGLIPHTVPSMEQREALTIGTDVKSLFLSPGCSALEKAVDFGEISILNPITLHCRSSSKPFYAILHRIEEGLVIDLEPVSPDEVPVTAAGALRSYKLAAKSISRLQALPSGNMLLLCDALVKEVSELTGYDRVMVYKFHEDGHGEVIAECCREDMEPYLGLHYSATDIPQASRFLFMRNKVRMICDCSAVPVKVVQDKSLSQPISLSGSTLRAPHGCHAQYMSNMGSVASLVMSVTINGSDSDEMNRDLQTGRHLWGLVVCHHASPRFVPFPLRYACEFLTQVFGVQINKEAESAVLLKEKRILQTQSVLCDMLFRNAPIGIVTQSPNIMDLVKCDGAALYYRDNLWSLGVTPTETQIRDLIDWVLKSHGGNTGFTTESLMESGYPDASVLGESICGMAAVYISEKDFLFWFRSSTAKQIKWGGARHDPNDRDGKRMHPRSSFKAFMEIVRWKSVPWDDMEMDAINSLQLIIKGSLQEEHSKTVVDVPLVDNRVQKVDELCVIVNEMVRLIDTAAVPIFAVDASGVINGWNSKAAEVTGLAVEQAIGKPVSDLVEDDSVETVKNMLALALEGSEERGAEIRIRAFGPKRKSSPVELVVNTCCSRDMTNNVLGVCFIGQDVTGQKTLTENYSRVKGDYARIMWSPSTLIPPIFITNENGVCSEWNNAMQKLSGIKREEVVNKILLGEVFTTDDYGCCLKDHDTLTKLRIGFNAVISGQKNIEKLLFGFYHRDGSFIEALLSANKRTDIEGKVTGVLCFLQVPSPELQYALQVQQISEHAIACALNKLAYLRHEVKDPEKAISFLQDLLHSSGLSEDQKRLLRTSVLCREQLAKVISDSDIEGIEEGYVELDCSEFGLQESLEAVVKQVMELSIERKVQISCDYPQEVSSMRLYGDNLRLQQILSETLLSSIRFTPALRGLCVSFKVIARIEAIGKRMKRVELEFRIIHPAPGLPEDLVREMFQPLRKGTSREGLGLHITQKLVKLMERGTLRYLRESEMSAFVILTEFPLI
Protein: Stromal interaction molecule 2 (A0A8I6AK33)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
MGHLALNTGTQWNLLPLLTKQDPCMSLSPPCFTEEDRFSLEALQTIHKQMDDDKDGGIEVDESDEFIREDMKYKDATNKHSHLHREDKHITVEDLWKQWKTSEVHNWTLEDTLQWLIEFVELPQYEKNFRDNNVKGTTLPRIAVHETSFMISQLKISDRSHRQKLQLKALDVVLFGPLTRPPHNWMKDFILTISIVIGVGGCWFAYTQNKTSKEHVAKMMKDLESLQTAEQSLMDLQERLEKAQEENRTVAVEKQNLERKMMDEINYAKEEACRLRELREGAECELSRRQYAEQELEQVRMALKKAEKEFELRSSWSVPDALQKWLQLTHEVEVQYYNIKRQNAEMQLAIAKDEAEKIKKKRSTVFGTLHVAHSSSLDEVDHKILEAKKALSELTTCLRERLFRWQQIEKICGFQIAHNSGLPSLTSSLYSDHSWVVMPRVSIPPYPIAGGVDDLDEDTPPIVSQFPGTVAKPAGSLARSSSLCRSRRSIVPSSPQSQRAQLPAHAPLAAHPRHPHHPQHSLPSPDPDILSVSSCPALYRNEEEEEAIYFTAEKQWEVPDTASECDSLNSSIGRKQSPPSSLEIYQTLSSRKISRDELSLEDSSRGDSPVTADVSRGSPECVGLTETKSMIFSPASRVYNGILEKSCSMHQLSSGIPVPNPRHTSCSLAGSDSKPVQEASSVSRVGSIPHDLCHNGEKSKKPSKIKSLFKKKSK
Protein: Protein kinase C delta (C9J9P1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAPFLRIAFNSYELGSLQAEDEANQPFCAVKMKEALSTERGKTLVQKKPTMYPEWKSTFDAHIYEGRVIQIVLMRAAEEPVSEVTVGVSVLAERCKKNNGKAEFWLDLQPQAKVLMSVQYFLEDV
Protein: Poly(rC) binding protein 4 (C9J0A4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSGSDGGLEEEPELSITLTLRMLMHGKEVGSIIGKKGETVKRIREQSSARITISEGSCPERITTITGSTAAVFHAVSMIAFKLDEDLCAAPANGGNVSRPPVTLRLVIPASQCGSLIGKAGTKIKEIRETTGAQVQVAGDLLPNSTERAVTVSGVPDAIILCVRQICAVILESPPKGATIPYHPSLSLGTVLLSANQGFSVQGQYGAVTPAEVTKLQQLSSHAVPFATPSVVPGLDPGTQTSSQEFLVPNDLIGCVIGRQGSKISEIRQMSGAHIKIGNQAEGAGERHVTITGSPVSIALAQYLITAWAAAGLGGLHCQDGSS
Protein: Multifunctional methyltransferase subunit TRM112-like protein (tRNA methyltransferase 112 homolog) (Q9UI30)
Organism: Homo sapiens (Human)
Function: Acts as an activator of both rRNA/tRNA and protein methyltransferases. Together with methyltransferase BUD23, methylates the N(7) position of a guanine in 18S rRNA. The heterodimer with N6AMT1/HEMK2 catalyzes N5-methylation of ETF1 on 'Gln-185', using S-adenosyl L-methionine as methyl donor. The heterodimer with N6AMT1/HEMK2 also monomethylates 'Lys-12' of histone H4 (H4K12me1). The heterodimer with ALKBH8 catalyzes the methylation of 5-carboxymethyl uridine to 5-methylcarboxymethyl uridine at the wobble position of the anticodon loop in target tRNA species. Together with methyltransferase THUMPD3, catalyzes the formation of N(2)-methylguanosine at position 6 in a broad range of tRNA substrates and at position 7 of tRNA(Trp). Involved in the pre-rRNA processing steps leading to small-subunit rRNA production. Together with methyltransferase METTL5, specifically methylates the 6th position of adenine in position 1832 of 18S rRNA.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:25851604}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:25851604}. Note=Localizes to a polarized perinuclear structure, overlapping partially with the Golgi and lysosomes (PubMed:25851604). {ECO:0000269|PubMed:25851604}.
Interaction partners:
- Methyltransferase HEMK2
- 18S rRNA
- tRNA
- rRNA N
- tRNA
- Probable tRNA methyltransferase 9B
- tRNA wybutosine-synthesizing protein 2 homolog
- Dimethyladenosine transferase
- Bystin
- MTRF1L release factor glutamine methyltransferase
Sequence:
MKLLTHNLLSSHVRGVGSRGFPLRLQATEVRICPVEFNPNFVARMIPKVEWSAFLEAADNLRLIQVPKGPVEGYEENEEFLRTMHHLLLEVEVIEGTLQCPESGRMFPISRGIPNMLLSEEETES
Protein: Protein FMP16, mitochondrial (Found in mitochondrial proteome protein 16) (Q12497)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}.
Interaction partners:
- Meiotic sister chromatid recombination protein 1
- 6-phosphogluconolactonase 4
- Uncharacterized protein YNL195C
- Reticulon-like protein 2
- Heat shock protein 26
- Protein SIP18
- Transaldolase NQM1
- Catalase T
- Carboxypeptidase Y inhibitor
- Mitochondrial outer membrane protein OM45
Sequence:
MLRTTFLRTPRQLMRKSPRASFSIVTRAAFPHLKNNQDEAEKKEQGLFDSNKKRLDTLEHGKNPDYKQPGMEDLKKKGDDARIEQNRPDDGVY
Protein: Cytochrome P450 monooxygenase stcB (EC 1.14.-.-) (Cytochrome P450 62) (Sterigmatocystin biosynthesis cluster protein B) (Q12608)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Cytochrome P450 monooxygenase; part of the gene cluster that mediates the biosynthesis of sterigmatocystin (ST), a polyketide-derived furanocoumarin which is part of the most toxic and carcinogenic compounds among the known mycotoxins. The first step in the biosynthesis of sterigmatocystin is the production of hexanoate by the fatty acid synthase (FAS) units stcJ and stcK. The polyketide backbone is assembled by the non-reducing polyketide synthase stcA by condensation of the starter hexanoyl-CoA and 7 malonyl-CoA extender units followed by cyclization and release of norsolorinic acid (By similarity). Norsolorinic acid is the first stable intermediate in the biosynthesis of sterigmatocystin and is converted into averantin (AVN) by the ketoreductase stcE which reduces the hexanoate ketone to an alcohol (Probable). Averantin is then oxidized into 5'-hydroxyaverantin (HAVN) by the cytochrome P450 monooxygenase stcF. 5'-hydroxyaverantin is further converted to 5'-oxyaverantin (OAVN) by the 5'-hydroxyaverantin dehydrogenase stcG. The next step is the conversion of OAVN into averufin (AVF) which is catalyzed by a yet to be identified enzyme. The cytochrome P450 monoxygenase stcB and the flavin-binding monooxygenase stcW are both required for the conversion of averufin to 1-hydroxyversicolorone. The esterase stcI probably catalyzes the formation of versiconal hemiacetal acetate from 1-hydroxyversicolorone. The oxydoreductase stcN then probably catalyzes the biosynthetic step from versiconal to versicolorin B (VERB). The next step is performed by the versicolorin B desaturase stcL to produce versicolorin A (VERA). The ketoreductase stcU and the cytochrome P450 monooxygenase stcS are involved in the conversion of versicolorin A to demethylsterigmatocystin. The Baeyer-Villiger oxidas stcQ and the reductase stcR might be involved in the biosynthetic step from versicolorin A to demethylsterigmatocystin. The final step in the biosynthesis of sterigmatocystin is the methylation of demethylsterigmatocystin catalyzed by the methyltransferase stcP.
Interaction partners:
Sequence:
MISQICNEVIGLVPKKEEPGWLSVTGHPGAVYCENSISSGPEATGADVSQAIRIAYFTPLKHIPGPWYASLTGLRLSWSVFANNRIHYVHSLHQKYGPIVRIGPQEIDVADPVAGREIHRMGSGFMKAPFYELLSPGPVDNIFNFRDPKLHAARRKLYARGFTLQSLRNEWEPKVRDIIKLTVEKIKCDAVKGEAEIMGWWTLMANEIVCQLTFGGGAGIVAKGVKEPFVLMLERRMGDLAHLLKHFAPPGYYLGRALAWFIPPLQDIFYSQERMFAAGGDVVSRAREAKKAQAEPRNLFNKALEAGNLTDTDIITDAGALLLAGSDPTAISLTFLLWCVLSRPEVQKQVEAEVATLEGELTDEACERLPILNAVIDESLRLYGAAPGCMPRSPPSGGVTIGGYFIPDDTIVATQNWSLQRNPSIWDDADTFDHTRWLSNSRITDQAKLAFNPFGYGARQCLGIHLGRMEMRLAAAMFFRECVGARLGRSVTDESMHVVDSFIAGVPRDRRCAITLT
Protein: Nuclear cap-binding protein complex subunit 1 (80 kDa nuclear cap-binding protein) (CBP80) (NCBP 80 kDa subunit) (Glycolysis regulation protein 3) (Protein SUT1) (Suppressor of TOP1 protein) (P34160)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the CBC complex, which binds co-transcriptionally to the 5'-cap of pre-mRNAs and is involved in maturation, export and degradation of nuclear mRNAs. The CBC complex is required for efficient pre-mRNA splicing through efficient commitment complex and spliceosome formation. Together with NPL3, the CBC complex is required for export of mRNAs out of the nucleus. The CBC complex is also involved in nuclear mRNA degradation, probably by directing the mRNAs to the sites of degradation. Affects replication of the positive-strand RNA virus BMV.
Subcellular location: Nucleus {ECO:0000269|PubMed:10733586, ECO:0000269|PubMed:10823828, ECO:0000269|PubMed:8858145}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:10823828}. Note=Predominantly nuclear, is able to exit the nucleus in an RNA-dependent manner. {ECO:0000269|PubMed:10823828}.
Interaction partners:
- U1 small nuclear ribonucleoprotein A
- Small nuclear ribonucleoprotein-associated protein B
- Protein NAM8
- Nuclear cap-binding protein subunit 2
- Small nuclear ribonucleoprotein Sm D2
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein Sm D3
- U1 small nuclear ribonucleoprotein C
- U1 small nuclear ribonucleoprotein 70 kDa homolog
- 66 kDa U4/U6.U5 small nuclear ribonucleoprotein component
Sequence:
MFNRKRRGDFDEDENYRDFRPRMPKRQRIPPVVQLCKEMMPDIRTIGESVKAFEDDIKFLSEAIMNEYGHEDYFNNALLSTLNAVVVEQPQKQAAIALLTMVVNSKNNVAGKSIINYFFEELQKWCKQTYNDEFKSTSNETGPWNKIKLILRFLSILSPMFLVDELINIYKSLFELSIELNNLDPGNRVPLSEAIYTNTLLNIPYLFFFNRNNDGLRTKVEELLAYVEQNYLVKTTDINLLREYNGEPPYEMVELVRVVLPNVKKALINNLEQLNELFPDWNHLLTPQTGDEGFNDALTLPSVDDLKSFVRLNKNFGSVDSMWKTPRYAFHVYLPNSAGNFETVVPISTYAGQLFNDIIIDLVESLEFNRKEVARQVITLDLFFKAGIFTEPGESIAQLIATYEENPLAPTFKIEDLAIETILGLIFKLPSVSQPFAYFYTLLVDICQNSPKAIAPVFGRAFRFFYSHLDSLDFELKLRYLDWFSIQMSNFNFSWKWNEWEDDSIKFGKYFYNPKVNFAKNLIQKELRLTSNFSEVEDSLPQEFTKYLDTSYIPRDQLINYYQSLFTGYTVEEDSVRKNDLYFRQEGVPMENTVRKILDYTHKANNSREVTELESILGELKNEYGSIISDFNRFVIILLVQAVTDSGSRSLSHANKYINDLKEDLKTIFAKIELDIETKEYIIIEAVLTFWNANPQTGFLVADAFKYAGLLTSRTIFTFIFNETGLKNNGLIEATAIEAVFRNLSQQISEENESGNNFEFVFERLCTIANSTIDLLDVNADEDIEIPKVNGEMDIDDIEDDKLDLKWKYFTVIGFIKSILRRYSHEYRELADKFIANIDNAIPHESTRRTISNWIQETKEV
Protein: Dephospho-CoA kinase (EC 2.7.1.24) (Dephosphocoenzyme A kinase) (P9WPA3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A. Can also use dATP, with lower efficiency, but cannot use GTP, dGTP or CTP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00376}.
Interaction partners:
- Phosphopantetheine adenylyltransferase
- Coenzyme A biosynthesis bifunctional protein CoaBC
- DNA polymerase I
- Holo-[acyl-carrier-protein] synthase
- Small ribosomal subunit protein bS1
- Endonuclease
- Ribonuclease HII
- Riboflavin biosynthesis protein
- GTP cyclohydrolase 1
- Glutamine-dependent NAD
Sequence:
MLRIGLTGGIGAGKSLLSTTFSQCGGIVVDGDVLAREVVQPGTEGLASLVDAFGRDILLADGALDRQALAAKAFRDDESRGVLNGIVHPLVARRRSEIIAAVSGDAVVVEDIPLLVESGMAPLFPLVVVVHADVELRVRRLVEQRGMAEADARARIAAQASDQQRRAVADVWLDNSGSPEDLVRRARDVWNTRVQPFAHNLAQRQIARAPARLVPADPSWPDQARRIVNRLKIACGHKALRVDHIGSTAVSGFPDFLAKDVIDIQVTVESLDVADELAEPLLAAGYPRLEHITQDTEKTDARSTVGRYDHTDSAALWHKRVHASADPGRPTNVHLRVHGWPNQQFALLFVDWLAANPGAREDYLTVKCDADRRADGELARYVTAKEPWFLDAYQRAWEWADAVHWRP
Protein: GDNF family receptor alpha-3 (GDNF receptor alpha-3) (GDNFR-alpha-3) (GFR-alpha-3) (O35118)
Organism: Mus musculus (Mouse)
Function: Receptor for the glial cell line-derived neurotrophic factor, artemin. Mediates the artemin-induced autophosphorylation and activation of the RET receptor tyrosine kinase (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O60609}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:O60609}.
Interaction partners:
- Artemin
- Proto-oncogene tyrosine-protein kinase receptor Ret
- Neurturin
- Persephin
- Glial cell line-derived neurotrophic factor
- GDNF family receptor alpha-1
Sequence:
MGLSWSPRPPLLMILLLVLSLWLPLGAGNSLATENRFVNSCTQARKKCEANPACKAAYQHLGSCTSSLSRPLPLEESAMSADCLEAAEQLRNSSLIDCRCHRRMKHQATCLDIYWTVHPARSLGDYELDVSPYEDTVTSKPWKMNLSKLNMLKPDSDLCLKFAMLCTLHDKCDRLRKAYGEACSGIRCQRHLCLAQLRSFFEKAAESHAQGLLLCPCAPEDAGCGERRRNTIAPSCALPSVTPNCLDLRSFCRADPLCRSRLMDFQTHCHPMDILGTCATEQSRCLRAYLGLIGTAMTPNFISKVNTTVALSCTCRGSGNLQDECEQLERSFSQNPCLVEAIAAKMRFHRQLFSQDWADSTFSVVQQQNSNPALRLQPRLPILSFSILPLILLQTLW
Protein: ABC multidrug transporter C (E9RBG1)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Function: Pleiotropic ABC efflux transporter that shows a strong substrate specificity for the azole class of drugs such as lotrimazole (CLT), fluconazole (FLC), itraconazole (ITC), ketoconazole (KTC), posaconazole (POS), tebuconazole (TEBZ), and voriconazole (VRC) (Probable). Is also able to transport rhodamine 6G (R-6G), a known substrate for many ABC transporters. Required for normal pathogenesis in a Galleria mellonella (greater wax moth) infection model.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24123268}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- ABC-transporter-regulating transcription factor
- Sterol 14-alpha demethylase cyp51A
Sequence:
MSLLGTINPNINPERTVAGRGTQEEEGEIARVEHNHHNNAASVSTDETVLERSKEIGDEDVAVEEVTRLARQLTRQSTRFSTSGNVENPFLETKEDSTLNPLSPNFKAKNWMKNLLALSSRDPERYPKRVAGVAFKNLSVHGYGSPTDYQKDVFNSVLEVGTLVRRIMGTGKQKIQILRDFDGLVKSGEMLVVLGRPGSGCSTFLKTISGEMNGIYMDEKSYLNYQGISSKQMRKQFRGEAIYTAETDVHFPQLTVGDTLKFAALARAPRNRLPGVSREQYAVHMRDVVMAMLGLTHTMNTRVGNDFVRGVSGGERKRVSIAEATLSGSPLQCWDNSTRGLDSANALEFCKTLNLMTKYAGATVAVAIYQASQSAYDVFDKVTVLYEGRQIYFGRTDEAKEFFTNMGFECPERQTTADFLTSLTSPAERVVKPGFEGKVPQTPDEFVRAWKSSEAYAKLMREIEEYDREFPIGGESLNQFIESRRAMQAKNQRVKSPYTISVWQQIELCMIRGFQRLKGDSSLTMSQLIGNFIMALVIGSVFYNLPDDTSSFYARGALLFFAVLLNAFSSALEILTLYAQRPIVEKQARYAMYHPFAEAIASMLCDMPYKITNAIIFNLTLYFMTNLRREPGAFFVFLLFSFVTTLTMSMLFRTMAASSRTLSQALVPAAILILGLVIYTGFTIPTRNMLGWSRWMNYIDPIAYGFESLMVNEFHNRQFLCPDSAFVPSSGAYDSQPLAYRVCSTVGSVSGSRYVQGDDYLNQSFQYYKSHQWRNLGIMFGFMFFFMFTYLTATEYISESKSKGEVLLFRRGHAQPTGSHDVEKSPEVSSAAKTDEASSKEATGAIQRQEAIFQWKDVCYDIKIKGEPRRILDHVDGWVKPGTCTALMGVSGAGKTTLLDVLATRVTMGVVSGEMLVDGRPRDQSFQRKTGYVQQQDLHLHTTTVREALRFSALLRQPAHVPRQEKIDYVEEVIKLLGMESYADAVVGVPGEGLNVEQRKRLTIGVELAAKPQLLLFLDEPTSGLDSQTSWSILDLIDTLTKHGQAILCTIHQPSAMLFQRFDRLLFLAKGGKTVYFGEIGEKSSTLASYFERNGAPKLPPDANPAEWMLEVIGAAPGSHSDIDWPAVWRDSPERRAVHEHLDELKRTLSQKPIDPSKADPGSYDEFAAPFTIQLWECLLRVFSQYWRTPVYIYSKTALCVLTALYIGFSFFNAQNSAQGLQNQMFSIFMLMTIFGNLVQQIMPNFCTQRSLYEVRERPSKTYSWKAFMAANIIVELPWNTLMAFLIFVCWYYPIGLYRNAEPTDSVHERGALMFLLIWSFLLFTSTFAHMMIAGIELAETGGNLANLLFSLCLIFCGVLAPPQSLPGFWIFMYRVSPFTYLVSAMLSTGVSGTNAVCEPVEFLHFDPPSNMTCKDYMADYISTRGGYLENPSATSDCTFCTISSTDTFLSAVSSHYSDAWRNFGIMWAYIIFNIFAAVFIYWLARVPKGKRTKGST
Protein: Cyclin-dependent kinase 9 (EC 2.7.11.22, EC 2.7.11.23) (GH21935p) (Positive transcription elongation factor b small subunit) (O17432)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cyclin-T
- Cyclin-K
- Transcription elongation factor SPT5
- Cyclin-H
- ENL/AF9-related, isoform B
- Transcription elongation factor SPT4
- Hexamethylene bisacetamide inducible, isoform B
- AF4/FMR2 family member lilli
- RNA polymerase II elongation factor Ell
- Mediator of RNA polymerase II transcription subunit 1
Sequence:
MAHMSHMLQQPSGSTPSNVGSSSSRTMSLMEKQKYIEDYDFPYCDESNKYEKVAKIGQGTFGEVFKAREKKGNKKFVAMKKVLMDNEKEGFPITALREIRILQLLKHENVVNLIEICRTKATATNGYRSTFYLVFDFCEHDLAGLLSNMNVKFSLGEIKKVMQQLLNGLYYIHSNKILHRDMKAANVLITKHGILKLADFGLARAFSIPKNESKNRYTNRVVTLWYRPPELLLGDRNYGPPVDMWGAGCIMAEMWTRSPIMQGNTEQQQLTFISQLCGSFTPDVWPGVEELELYKSIELPKNQKRRVKERLRPYVKDQTGCDLLDKLLTLDPKKRIDADTALNHDFFWTDPMPSDLSKMLSQHLQSMFEYLAQPRRSNQMRNYHQQLTTMNQKPQDNSMIDRVW