wanglab/gogpt-training-data huggingface dataset:
Protein: Chromatin assembly factor 1 subunit FAS1 (CAF-1 subunit FAS1) (CAF-1 p150 homolog) (Protein FASCIATA 1) (Q9SXY0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the chromatin assembly factor complex (CAF-1) involved in chromatin assembly following DNA replication and DNA repair. Assembles histone octamers onto replicating DNA in vitro. Required for several aspects of development, including seedling growth and leaf hair differentiation. Plays a critical role in the organization of shoot apical meristem (SAM) and root apical meristem (RAM) during postembryonic development by facilitating stable maintenance of gene expression states. Seems not required to maintain transcriptional repression of heterochromatic genes. Involved in heterologous recombination. May repress endocycle.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Histone-binding protein MSI1
- Chromatin assembly factor 1 subunit FAS2
- Histone chaperone ASF1B
- Probable histone chaperone ASF1A
- Chromo domain-containing protein LHP1
- DNA polymerase alpha catalytic subunit
- DNA replication licensing factor MCM3
- DNA replication licensing factor MCM5
- DNA replication licensing factor MCM4
- Proliferating cellular nuclear antigen 1
Sequence:
MDEVSTVNENENRKTMIEPKKLNKRKREPTAIENLTSEEKESQISSLNLEMKGLFDYFREVMDKSKRTDLFSGFSECSSLNSMVALLMEEMSLPLSKLVDEIYLKLKEKTESVTMVAVKSAVVSVGQRVSYGVLNVDADVLEDDSESCLWCWETRDLKIMPSSVRGVLKLRRTCRKKIHERITAVSAMLAALQREETEKLWRSDLSKAAEKLGKILSEVDIRSFMDNMMQKNSSEMAEKDSKREEKLLLKQLEKNRCEAEKEKKRMERQVLKEKLQQEKEQKLLQKAIVDENNKEKEETESRKRIKKQQDESEKEQKRREKEQAELKKQLQVQKQASIMERFLKKSKDSSLTQPKLPSSEVTAQELSCTKHENEIGKVVQAIDNAFSTTCEATVDDIRREHFASWRQLGHLLSSSKKHWGMRRQPKSELFPKLKLSTNSGVTSDGEPNMEKQGDGCEENNFDGRQCKPSSSNRKKSRRVKQLLQFDKSCRPGFYGIWPSQSQVVKPRRPLQKDPELDYEVDSDEEWEEEEAGESLSDCEKDEDESLEEGCSKADDEDDSEDDFMVPDGYLSEDEGVQVDRMDIDPSEQDANTTSSKQDQESPEFCALLQQQKHLQNLTDHALKKTQPLIICNLTHEKVSLLAAKDLEGTQKVEQICLRALMVRQFPWSSLIEISINDIQDEDQEASKFSCSQSTPPSNSKAKIIPDSDLLTVVSTIQSCSQGINRVVETLQQKFPDVPKTKLRQKVREISDFEDSRWQVKKEVLTKLGLSPSPDKGGKRLPKTISTFFSKRCLPPSTKPQPAVEDAAERLENENA
Protein: Neuronal PAS domain-containing protein 4-like (Protein cloche) (P0DOC7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Transcription factor specifically expressed in endothelial and hematopoietic precursor cells that acts as a key regulator of the endothelial differentiation cascade. Acts as an early-response transcription factor that regulates the expression of early regulators of endothelial and haematopoietic differentiation, such as etv2 and tal1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}.
Interaction partners:
- ETS variant transcription factor 2
- Vascular endothelial growth factor receptor kdr-like
- Lysocardiolipin acyltransferase 1
- Fli-1 protein
- T-cell acute lymphocytic leukemia protein 1 homolog
- GATA-binding protein 1a.
- Aryl hydrocarbon receptor nuclear translocator.
- Zinc finger-like gene 2a
- Aryl hydrocarbon receptor nuclear translocator 2
Sequence:
MSCGDSGIRRILRASKRFRSTKGASKARRDQMNSEIRNLRALLPISPEHRLSYLHSMSITCTYIRKSVELRGVCEESTVFSAVNGCVPQDCALQDCALQECVLQECVLQECVLQECVLQALPGFIVAFTTDGKLLYVSENVHEYLGLSMVDVLQSDSFFDMLDRSDVEAVRSVLADASPSGERWVVCRMLVSKAMRLRSSCCPLLVRIRLRDGVCVSLCRPTADRLPARNADFHTHHSADMRLASASSSVLFHLGFSADELIGRSWYELLHPDDLRHAADRHAAILAAATADAEMLIRVQCKDLSWVWMYTHASATAERDAISCSNYMISEAEAVYLQQRLSSSSSSSSSSSSSSASPQCSSVSDSSDAHSAHTLFCTPPYSPTSSQCSDFLSEGYGSLEALVDSAFCSPPYPPLFPNPCCTPTVCPPDTALDPARLCPPDSALVPAALCPPDAALDPTQLCPPGAALDPTLLCPPGAALDPTQLCLPDGALVPAVFCPPNGALVPARLCPSDAALVPAALGRPDAALVPVCRPLQVCECPLDGAVPLEDLSMFPLPQGGGSRLMPPEASPTTHTHFSYDAAQQAGIGTLAMQIHTLICSFDAYSAARHTHSHHTSCWAPEPLLDEGIIDSILRELDSTHTDAHTLI
Protein: ATP-dependent zinc metalloprotease FtsH (EC 3.4.24.-) (Q9WZ49)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01458}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01458}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_01458}.
Interaction partners:
- ftsH protease activity modulator HflC
- ftsH protease activity modulator HflK
- Conserved hypothetical protein
- Large ribosomal subunit protein uL3
- tRNA
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL27
- ATP-dependent Clp protease ATP-binding subunit ClpX
- Small ribosomal subunit protein uS11
Sequence:
MNRSNIWNLLFTILIIVTLFWLARFFYVENSPVSKLSYTSFVQMVEDERSVVSEVVIRDDGVLRVYTKDGRVYEVDAPWAVNDSQLIEKLVSKGIKVSGERSGSSSFWINVLGTLIPTILFIVVWLFIMRSLSGRNNQAFTFTKSRATMYKPSGNKRVTFKDVGGAEEAIEELKEVVEFLKDPSKFNRIGARMPKGILLVGPPGTGKTLLARAVAGEANVPFFHISGSDFVELFVGVGAARVRDLFAQAKAHAPCIVFIDEIDAVGRHRGAGLGGGHDEREQTLNQLLVEMDGFDSKEGIIVMAATNRPDILDPALLRPGRFDKKIVVDPPDMLGRKKILEIHTRNKPLAEDVNLEIIAKRTPGFVGADLENLVNEAALLAAREGRDKITMKDFEEAIDRVIAGPARKSKLISPKEKRIIAYHEAGHAVVSTVVPNGEPVHRISIIPRGYKALGYTLHLPEEDKYLVSRNELLDKLTALLGGRAAEEVVFGDVTSGAANDIERATEIARNMVCQLGMSEELGPLAWGKEEQEVFLGKEITRLRNYSEEVASKIDEEVKKIVTNCYERAKEIIRKYRKQLDNIVEILLEKETIEGDELRRILSEEFEKVVE
Protein: L-amino-acid oxidase BmooLAAO-I (LAO) (EC 1.4.3.2) (Q6TGQ8)
Organism: Bothrops moojeni (Lance-headed viper) (Caissaca)
Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the toxicity of the venom. Shows very high activity on L-Met, and L-Leu, high activity on L-Ile, L-Phe and L-Tyr and moderate activity on L-His, L-Val and L-Ala. Exhibits diverse biological activities, such as edema, apoptosis of tumor cell lines, antibacterial activities against both Gram-positive and Gram-negative bacteria, as well as induction of platelet aggregation. Effects of snake L-amino oxidases on platelets are controversial, since they either induce aggregation or inhibit agonist-induced aggregation. These different effects are probably due to different experimental conditions. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage. It may also induce hemolysis. Has parasiticidal activities against and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production.
Subcellular location: Secreted {ECO:0000269|PubMed:11162565}.
Interaction partners:
Sequence:
MNVFFTFSLLFLAALGSCADDRNPLEECFRETDYEEFLEIAKNGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIRKFDLQLNEFSQENENAWYFIKNIRKRVGEVNKDPGVLEYPVKPSEVGKSAGQLYEESLQKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVHLNARVIKIQQDVKEVTVTYQTSEKETLSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAICRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPVDRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNSAS
Protein: Mitochondrial inner membrane protease subunit 1 (EC 3.4.21.-) (O74800)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the removal of transit peptides required for the targeting of proteins from the mitochondrial matrix, across the inner membrane, into the inter-membrane space.
Subcellular location: Mitochondrion inner membrane {ECO:0000305|PubMed:16823372}.
Interaction partners:
- Nitrogen permease regulator 2 homolog
- Uncharacterized WD repeat-containing protein C4F8.11
- Uncharacterized RWD, RING finger and WD repeat-containing protein C11E3.05
- Vacuolar membrane-associated protein iml1
- Mitochondrial inner membrane protease subunit 2
- Signal peptidase complex subunit 2
- Signal peptidase complex subunit 1
- Signal peptidase complex subunit 3
Sequence:
MAGMFRIPIAVVQIAAFVHQIHEYLFQVQMTSGPSMMPTLNSGGEFVLLDKLHGRFARSCSVGDVVVSAKPSDSKQHVCKRIIGMPGDTIYVDPTSSNKKITIPLGHVWLAGDNIAHSLDSRNYGPVPMGLIKAKVIARVWPHPHWMSNILNDIDVE
Protein: Glucocorticoid receptor (Nuclear receptor subfamily 3 group C member 1) (Q1XHK0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000256|ARBA:ARBA00004300}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|ARBA:ARBA00004186}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}. Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma, coactivator 1 alpha.
- Prostaglandin E synthase 3
- Heat shock protein HSP 90-alpha 1
- Corticotropin-releasing hormone b.
- Stress-induced-phosphoprotein 1
- Nuclear receptor coactivator 2
- Peptidylprolyl isomerase.
- Nuclear receptor coactivator 1.
- Heat shock protein HSP 90-beta
- Protein c-Fos
Sequence:
MDQGGLENGKKRDERLNTLDYNKRATEGILPRRIQSTMSVAPTSMVPQAGPMMQPVSGDIPNGLSNSPTLEEHTSSVSSIFGDDSELKLLGKEQRALQQQTLVPFTLGDSLSGLEASIADLNNPSPSMDSLIGGVDPNLFPLKTEDFSPMIKGDMDLDQDSFGHIGKDVDVGNHKLFSDNTLDLLQDFELDGSPSDFYVADDAFLSTIGEDALLSELPTNLDRDSKAAVSGSNTLNGTASSSLSTANTSILPNIKVEKDSIIQLCTPGVIKQENTGASYCQGGLHSTPINICGVTTSSGQSFLFGNSSPTAVVGLQKDQKPDFNMYTPLTSSGDGWSRSQGFGNVSGMQQRASLCFSKNFSSSPYSRPEDSTATSSAGGKTGTHKICLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRFRKCLMAGMNLEARKSKSKARQAGKVIQQQSIPERNLPPLPEARALVPKPMPQLVPTMLSLLKAIEPDTLYAGYDSTIPDTSVRLMTTLNRLGGRQVISAVKWAKALPGFRNLHLDDQMTLLQCSWLFIMSFGLGWRSYQHCNGNMLCFAPDLVINEERMKLPYMSDQCEQMLKISNEFVRLQVSTEEYLCMKVLLLLNTVPKDGLKSQSVFDELRMSYIKELGKAIVKREENSSQNWQRFYQLTKLLDSMHDLVGGLLNFCFYTFVNKSLSVEFPEMLAEIISNQLPKFKDGSVKPLLFHQK
Protein: Cyclin-dependent kinase 16 (EC 2.7.11.22) (Cell division protein kinase 16) (PCTAIRE-motif protein kinase 1) (Serine/threonine-protein kinase PCTAIRE-1) (Q63686)
Organism: Rattus norvegicus (Rat)
Function: Protein kinase that plays a role in vesicle-mediated transport processes and exocytosis. Can phosphorylate CCNY at 'Ser-336' (in vitro) Plays a role in the regulation of insulin secretion in response to changes in blood glucose levels. Regulates GH1 release by brain neurons. Required for normal spermatogenesis. Regulates neuron differentiation and dendrite development (By similarity). Phosphorylates NSF, and thereby regulates NSF oligomerization.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q00536}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:16461345}. Cell membrane {ECO:0000250|UniProtKB:Q00536}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q00536}; Cytoplasmic side {ECO:0000250|UniProtKB:Q00536}. Synapse, synaptosome {ECO:0000269|PubMed:16461345}. Note=Colocalizes with insulin in pancreas islets. Recruited to the cell membrane by CCNY. {ECO:0000250|UniProtKB:Q00536}.
Interaction partners:
- Cyclin Y
- Cyclin Y-like 1
Sequence:
MDRMKKIKRQLSMTLRGGRGIDKTNGVPEQIGLDESGGGGGSDLGEAPTRVAPGELRSIRGPLSSAPEIVHEDMKMGSDGESDQASATSSDEVQSPVRVRMRNHPPRKISTEDINKRLSLPADIRLPEGYLEKLTLNSPIFDKPLSRRLRRVSLSEIGFGKLETYIKLDKLGEGTYATVYKGKSKLTDNLVALKEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYLDKDLKQYLDDCGNVINMHNVKLFLFQLLRGLAYCHRQKVLHRDLKPQNLLINERGELKLADFGLARAKSIPTKTYSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMATGRPLFPGSTVEEQLHFIFRILGTPTEDTWPGILSNEEFRTYNYPKYRAEALLSHAPRLDSDGADLLTKLLQFEGRNRISAEDAMKHPFFLSLGERIHKLPDTTSIFALKEVQLQKEANIRSTSMPDSGRPAFRVVDTEF
Protein: Aryl hydrocarbon receptor type 1 (Q8QGQ3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLALKKTLTNHESVSLEIMSSSNIYASRKRRKPVQKSVKQPLTCVKSNPSKRHRDRMNEVLASLAREIPFPQEIVSTLDKLTILRLSVSYLRAKSHFKITLNSKSSSQQANNTKQAQELPEGEFLLQAINGFLLVVTSSGTVFYVSSNIEDYLGFHQSDVIHQSVYELIHTEDRHEFQRQLHWALYPGFTPDSRQLVQASPDASRTCYSPEQLSLENSTCLERNFICRLRCLLDSTSGFLAVNFQGRLKFLYGQNESTADGKRIPPQLALFALACPLQPPSILEIRTKNLMFKTKYKLDFTPIACDTNWNFVLGYTEAELCNSGSGYQFIHAADMMYCAEGHMRMMRTGETGLTVFRLLTKQNRWVWVQSNGKLVYKNGQPDCIITSHRVITAEEGEENLRNRAMMLPFSFTTGDAVLCAMNCPTSSDPAPSDGNTQPKTTRTVNPDSLLVSLLKQPKSIYLSPGDERSVLVQSLGNKDLDGIYSINSQESVSVSGSCPFKQESVFSSERDDSCEILNFMGSLGISLEDLKFLQQKDLFINIDLDSHNDMADLSDDILSHVQQSLKLKMDCTVSKNTQGNIKEQELIRNPAQTIIPNDSCDTITLLSQEQQMTFITDKTEPKIQLAQIQPYTPQKGIPYLQIDPHEHQDTRPQSYNGTGITLPKSSHSTISQHLQFSNLPPFHEQVCEALRSPQVCGTMAEVIDSDIQQVSPLFPPELQPSGCFYLKRPILDPKLCTSSSQQLSSSQTTEGEPVKFTTQDLEDLINDMNGVGERNNYSGLDRGMDIRSSLDQQAYIGTVRNKLFI
Protein: Vacuolar protein sorting-associated protein 33B (r-vps33b) (Q63616)
Organism: Rattus norvegicus (Rat)
Function: May play a role in vesicle-mediated protein trafficking to lysosomal compartments and in membrane docking/fusion reactions of late endosomes/lysosomes. Mediates phagolysosomal fusion in macrophages. Proposed to be involved in endosomal maturation implicating VIPAS39. In epithelial cells, the VPS33B:VIPAS39 complex may play a role in the apical recycling pathway and in the maintenance of the apical-basolateral polarity. Seems to be involved in the sorting of specific cargos from the trans-Golgi network to alpha-granule-destined multivesicular bodies (MVBs) promoting MVBs maturation in megakaryocytes (By similarity).
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q9H267}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H267}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H267}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H267}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H267}; Cytoplasmic side {ECO:0000250|UniProtKB:Q9H267}. Early endosome {ECO:0000250|UniProtKB:Q9H267}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250|UniProtKB:Q9H267}. Recycling endosome {ECO:0000250|UniProtKB:Q9H267}. Note=Colocalizes in clusters with VIPAS39 at cytoplasmic organelles. Colocalizes with RAB11A and VIPAS39 on recycling endosomes. Colocalizes with AP-3, clathrin, Rab5 and Rab7b. {ECO:0000250|UniProtKB:Q9H267}.
Interaction partners:
- Vacuolar protein sorting-associated protein 11 homolog
- VPS39 subunit of HOPS complex
- Vacuolar protein sorting-associated protein 18 homolog
- Spermatogenesis-defective protein 39 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- VPS8 subunit of CORVET complex
- Vacuolar protein sorting-associated protein 41 homolog
- Transforming growth factor, beta receptor associated protein 1
- Vesicle-associated membrane protein 8
- CCZ1 homolog, vacuolar protein trafficking and biogenesis associated
Sequence:
MAFPHRLDAPELPDFSMLKRLARDQLIYLLEQLPGKKDLFIEADLMSPLDRIANVSILKQHEVDKLYKVENKLTLSSNEQLCFLVRPRIKTMRYIANLVNADKLAGRVRKYKIILSPQKFYACEMVLEEEGVYGDVSCDEWAFSLLPLDVDLLSMELPEFFRDYFLEGDQRWINTVAQALHLLSTLYGPFPNCYGIGRCTKMSYDLWRKLEEEEDSETKGRRPEIGHIFLLDRDVDFVTALCSQVVYEGLVDDTFRIKCGSVDFGPEVTSSDKSLKVLLNAEDKVFSEIRNEHFSNVFGFLSQKARNLQAQYDRRRGMDIKQMKNFVSQELKGLKQEHRLLSLHIGACESIMKKKTKQDFQELIKTEHALLEGFNIRESTSYIEEHIDRQVSPIESLRLMCLLSITENGLIPKDYRSLKTQYLQSYGPEHLLTFSNLRRAGLLTEQASGDTLTAVENKVSKLVTDKAAGKITDAFSSLAKRSNFRAISKKLNLIPRVDGEYDLKVPRDMAYVFSGAYVPLSCRIIEQVLDRRSWQGLDEVVRLLNCSDFAFTDMAKEDKASSESLRLILVVFLGGCTFSEISALRFLGREKGYRFIFLTTAVTNSARLMEAMSEVKS
Protein: E3 ubiquitin-protein ligase RFI2 (EC 2.3.2.27) (Protein RED AND FAR-RED INSENSITIVE 2) (O82239)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates phytochrome (phyA and phyB)-controlled seedling deetiolation responses such as hypocotyl elongation in response to red and far-red light. Required for light-induced expression of LHCB3 and CHALCONE SYNTHASE (CHS). Regulates negatively CONSTANS (CO) and FLOWERING LOCUS T (FT) expression and photoperiodic flowering.
Subcellular location: Nucleus {ECO:0000269|PubMed:16384903}.
Interaction partners:
- At3g29270
- E3 ubiquitin-protein ligase RMA
- Homeobox protein ATH1
- Probable E3 ubiquitin-protein ligase WAVH2
- SBP family protein
- AT-hook motif nuclear-localized protein 18
- E3 ubiquitin-protein ligase APD1
- Transmembrane protein
- AP2-like ethylene-responsive transcription factor TOE2
- CHY-type/CTCHY-type/RING-type Zinc finger protein
Sequence:
MAGAKDSGCDDDLRIAGGCDPGKRGNPEDSSSPVEVSCSICLESVLDDGTRSKAKLQCGHQFHLDCIGSAFNMKGAMQCPNCRNVEKGQWLYANGSTRPFPEFSMEDWIPEEDLYGLSYPEMQYRVHWCPFGELSQAAASFEELEPATTTYHTEFHGHHAAAVNHSYLAYVGPGPAATPRTSDNNSTDDHPWNSHSNDHFHQLPVAPQYHHHSPSFSLPAAHVVDGEVDSSAARGLPYAHPFLFSHRSNQRSSPAINSYQGSSTQMREQHHAYNHQRQQHHANGPTLASPLISMTRRGLPPPPPPPPMPDQNVGFFIYPGGHHEPETDQIHAWERDWFPHFPVPSNHRTIPSLWHRHF
Protein: 3-ketosteroid-9-alpha-monooxygenase, oxygenase component (3-ketosteroid-9-alpha-hydroxylase, oxygenase component) (KSH) (Androsta-1,4-diene-3,17-dione 9-alpha-hydroxylase) (EC 1.14.15.30) (Rieske-type oxygenase) (RO) (A0R4R3)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Involved in the degradation of cholesterol. Catalyzes the introduction of a 9a-hydroxyl moiety into 1,4-androstadiene-3,17-dione (ADD) to yield the 9alpha-hydroxy-1,4-androstadiene-3,17-dione (9OHADD) intermediate which spontaneously form 3-hydroxy-9,10-seconandrost-1,3,5(10)-triene-9,17-dione (HSA) via the meta-cleavage of ring B with concomitant aromatization of ring A.
Interaction partners:
- 3-ketosteroid-9-alpha-monooxygenase, ferredoxin reductase component
- 3-oxosteroid 1-dehydrogenase
- Uncharacterized protein
- Oxidoreductase, NAD/FAD-binding
- 3-ketosteroid-delta-1-dehydrogenase
- 3-oxosteroid 1-dehydrogenase
- 3-ketosteroid dehydrogenase
- HTH-type transcriptional repressor KstR
- Biphenyl-2,3-diol 1,2-dioxygenase
- Rieske-type oxygenase
Sequence:
MATETVGIREIDTGALPDRYARGWHCLGPVKNFSDGKPHSVNIFGTKLVVFADSKGELNVLDAYCRHMGGDLSKGTVKGDEVACPFHDWRWGGDGKCKLVPYAKRTPRLARTRSWHTDVRGGLLFVWHDHEGNPPQPEVRIPEIPEWHSGEWTDWKWNSMLIEGSNCREIIDNVTDMAHFFYIHFGLPTYFKNVFEGHIASQYLHNVGRPDVNDLGTAYGEAKLDSEASYFGPSFMINWLHNTYGEFKAESILINCHYPVTQDSFVLQWGVIVEKPKGLDDATTEKLADAFTEGVSKGFLQDVEIWKHKTRIDNPLLVEEDGAVYQMRRWYQQFYVDVADITPDMTDRFEMEVDTTAAVEKWNIEVQENLKAQAEAEKAEQSS
Protein: AP-2 complex subunit alpha (A0A8I6A5N8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane, coated pit {ECO:0000256|ARBA:ARBA00004277}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004277}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004277}.
Interaction partners:
Sequence:
MRDRPLGSHGRQTAPKPAPALCSSWATGKRRGGRKLITLPLVAGGCLWPCVPCSLSTGKSKEAEIKRINKELANIRSKFKGDKALDGYSKKKYVCKLLFIFLLGHDIDFGHMEAVNLLSSNKYTEKQIGYLFISVLVNSNSELIRLINNAIKNDLASRNPTFMCLALHCIANVGSREMGEAFAADIPRILVAGDSMDSVKQSAALCLLRLYKASPDLVPMGEWTARVVHLLNDQHMGVVTAAVSLITCLCKKNPDDFKTCVSLAVSRLSRIVSSASTDLQDYTYYFVPAPWLSVKLLRLLQCYPPPEDAAVKGRLVECLETVLNKAQEPPKSKKVQHSNAKNAILFETISLIIHYDSEPNLLVRACNQLGQFLQHRETNLRYLALESMCTLASSEFSHEAVKTHIDTVINALKTERDVSVRQRAADLLYAMCDRSNAKQIVSEMLRYLETADYAIREEIVLKVAILAEKYAVDYSWYVDTILNLIRIAGDYVSEEVWYRVLQIVTNRDDVQGYAAKTVFEALQAPACHENMVKVGGYILGEFGNLIAGDPRSSPPVQFSLLHSKFHLCSVATRALLLSTYIKFINLFPETKATIQGVLRAGSQLRNADVELQQRAVEYLTLSSVASTDVLATVLEEMPPFPERESSILAKLKRKKGPGAASALDDSRRDTSSNDINGGVEPTPSNVSTPSPSADLLGLRAAPPPAAPPAPVGGNLLVDVFSDGPTAQPSLGPTPEEAFLRFVCKNSGVLFENQLLQIGVKSEFRQNLGRMYLFYGNKTSVQFQSFLPTVVHPGDLQTHILCSCTKRVAAQVDGGAQVQQVLNIECLRDFLTPPLLSVRFRYGGTAQSLTLKLPVTINKFFQPTEMAAQDFFQRWKQLSLPLQEAQKIFKANHPMDAEVTKAKLLGFGSALLDNVDPNPENFVGAGIIQTKALQVGCLLRLEPNAQAQMYRLTLRTSKEPVSRHLCELLAQQF
Protein: IP02289p (Odorant binding protein d) (Odorant-binding protein 56f) (Q7KE32)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Odorant binding protein b
- Odorant binding protein c
- GEO08953p1
- Uncharacterized protein
- IP02285p
- Odorant-binding protein 56g
- Serpin 28F
- Uncharacterized protein
- Accessory gland protein Acp29AB
- IP20609p
Sequence:
MKVFLLFIFISAIWLQAFCMKSSEKIKACLKRQLGYTITENTKFDAKEDSLQSKCFYHCLLEVKGVIANDAISSEQPRKVLEKKYGITDTDELEKAEEKCHSIKASGKCELGYEILKCYQSITKH
Protein: Nucleoporin NUP192 (Nuclear pore protein NUP192) (G0S4T0)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. NUP192 is located to the NPC core at the nuclear membrane and is essential for de novo assembly of NPCs.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000250|UniProtKB:P47054}. Note=Cytoplasmic and nucleoplasmic side of the nuclear pore complex in the nuclear envelope (symmetric distribution). {ECO:0000250|UniProtKB:P47054}.
Interaction partners:
- Nucleoporin NUP170
- Nucleoporin NIC96
- Nucleoporin NUP152
- Nucleoporin NUP49
- Nucleoporin NUP57
- Nucleoporin NUP84
- Nucleoporin NUP159
- Nucleoporin SEH1
- Nucleoporin NUP133
- Nucleoporin NUP188
Sequence:
MTDLRKLEALQALHAELVAVRQHRFEGLQVLETLLEEQTDAFKALIAKPARDTKDREALGKEPKKLKIGEEEYSLNEDFVNDCLKLADELDLNEKESARILIDCDAEGDVETQSRPLWECGVIRFHQERKYLLDCMRLILEIAADEDIDAGLQESFGVAAEDKIFGIPPPWERNKENQPTQVKKFIPRCMEAMKGVRSMLQCMADKANARNMLQQASLVRPLDNQETLDFSRLSLVEQHECLASILHAAVQRHHATIADFQDFIKILRKWDKYDHFLIHLIPVLAAYITEFGSPEGMGDLQQARRLNDFICKGGDEDSWALPVLGAAVRAWWIAEHNGFYLDDTVQDLRGINLDEEDEQRTKQFLDALKEGAFDFILSVAADCKAQEWQDPSQLGARQWLQRKIPSLPSEPFPFSHFLQHSLMVHLEGFVDATISNLPDVLRKLRTEEDEQRQLRPNHEQDMDLERFLIIISYAYEGRPDAAMSFWEDPDSNLAGFLQWASRRASTPLVSAFCEMLRCLADNEECATAAHNFLLDEGHQASGKMKRSQSLTWSQIFKELEYFTTKVCSERPNPPQASMHRPGRPGADPAEIEPESALMLECYLRLIAKLATESEIARKRLIMDEDFNLVDTILKLSVGVIPHRLRACIFYVLKALMIRKTHEELDAMWRWVEAWMTNPFSSLPGSQGAPQRISFLGQTPGPQECMEMMFREFGTGFEQSNAFIQLLTTLLVPPEGLNSLNDSVPFPEWLGSSIRTLGIEPYVDFVFDVFANRTKDISDPSQLRILRLSCLDFVMVCLVTFNEDLIVLGHESNISIDDAMAATNLATYVRLHPFSRVMEWLFNEKVITSLINTIHQDPISLGSASPDSPLVVSILRAIQVMIKALELQETYLHLVRPEVLRYQGEAGVRRKPVANAAYSAFEDGILSHLSLVVDLGKYCNLGHAELTLACLKLLEKISTSSRILSAWSPDSGRLGHRNKAIVQLERNGEGETISASLSASIMATLDPALAASGENYRVKLAILDFLYACLRATPDQPTIAHQLLGFHCELSKLGIEPKGPFDMQKSLFHSLLNVLITLTVSEEEQGMRGYLVTLKYRVLRILQLLWKSPLSASLVMDELRATNFLFHMLLREVQIQPQLPWDGQLVTGCEFLLSDASLAYIDYLASRAAIFEYIGKELCSVSQNRIPSIKRQIFDALNGQIFVDEEAPLTIPSIFDFFDFINTDYKWEEIPSPHFTYLKDLDLGPCILEHKYAGVHYDIRKAQEILALKRKEYEHSQLATPEFLETVELEEKVLIEWLTVRNRANLLLTARLNLLQAWANLLLVMIESNDFKSTPKMAFLLQALQAILPTLEAFSSLKSDEAFELARVAKVLLWKLDFSQDSDAGLDREQFTVGNLIGDKLFQLFQLCLSAISQCSGTPELRSLYYSICYRYLTAVVDNDATVAATPASSTIGPTRSVTNARARTLKAITLYGDRLLNVICDDAYGSDTTCQTAAMILLNALVHTSRASSAAGVSPADVDCPIIDALNRLNFIGVLVDSLKEILNEWLAPSSTFDPSLSTNASPSLPIPASPSQQYTSAKLALLLQLCQTRQGAKYVLQANLFRALEQSGVFAADPELVEVDSESGVPRVVALERHYALLVALARVVGAAVTARGAHNIVQGRKFLTQHRGLVVHVLKKNAGIGGGVVGNSLASSINGGSTATMTRRDEILAQQALEERIEELAEAFMLLITATGFLEYESEQVPSEQPRAHTTFFH
Protein: Acyl-CoA-binding protein (ACBP) (Diazepam-binding inhibitor) (DBI) (Endozepine) (EP) (P07108)
Organism: Homo sapiens (Human)
Function: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as a neuropeptide to modulate the action of the GABA receptor.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:17953517, ECO:0000269|PubMed:21698759}. Golgi apparatus {ECO:0000269|PubMed:17953517, ECO:0000269|PubMed:21698759}. Note=Golgi localization is dependent on ligand binding (PubMed:17953517). {ECO:0000269|PubMed:17953517}.
Interaction partners:
- Translocator protein
- Peroxisomal biogenesis factor 3
- Apolipoprotein A-V
- Apolipoprotein E
- Platelet-activating factor acetylhydrolase
- Golgi resident protein GCP60
- Cholecystokinin
- Sterol carrier protein 2
- Apolipoprotein A-I
- Apolipoprotein B-100
Sequence:
MSQAEFEKAAEEVRHLKTKPSDEEMLFIYGHYKQATVGDINTERPGMLDFTGKAKWDAWNELKGTSKEDAMKAYINKVEELKKKYGI