wanglab/gogpt-training-data huggingface dataset:
Protein: Simjang, isoform A (Simjang, isoform B) (Q0E8G1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MAKMEVDDVVDLSLGSGRDPALTITPAPPPAALSNRDLRALTANNAGLTITPSASPATNNGTTSNSSNTNSNSSSTTTTTNNNNNSSSNTNSSSANNNNNNNSINASDGVTGATSGSIGGGQDENKVQRRVLRPRTEPKSYAEAPDIVLLPARTNGRQQNGNIDSETDDEEMPPYVPIKELSHAELKEREKSLRKLRQDLRNEETKLMLLKKLKQSQQVMKENLVVTPTSVSPNNPLSAIPAALTSKGSLSVTPTSAVPLPAHSKGSRSSLSGSGGPAVSISATNSRTGSSSSAAAAASAIAAAAMSGQHRSGSNSILPPPRSSLPAGATLAAGTTITPATSSSHRSSNLPPRTNLPNLTITPSVTITPTSAPPSSLKPRNVPGTISNSVSITPALPLSQSHQNQHNDQKNDRSTPREDAQTPAQRQAAAKMALRKQLEKTLLQIPPPKPPPPEMHFIPNPSNTDFVYLLGLETVVDYLTVNKKANAVAAPFRCAQCKIDFTPVWKWEKQTNKDPKVICEQCVTSNVKKALKAEHTNRLKQAFVKALQQEQEIEQRLASQSSPSPVDNHGSSGGGNSLSVSAVSSNSSSSHMQREREQLQASHASAAAALVNLPPSVTVIPTKCQTPTPATPRPTPPPPQSQATPPPSSGGSRSSRAAATAAAAAIAAQQAGILSPGPSPAHHHEPTTSSRSSRNDRLDHHHQSQQQQQRDQRERDQQQRDQQSQQQAQNYDKYSAATLAAAAHLSALGGMGGLNINSLASLGNLGNLGNLSQLGNLAALGGLGNFGGASTGSANPAAGLSGSSPAATAAAMQAFQQQLFRALGQGLGGNPQHMMQFAPLLYSYQMAMAQAAQVAAFNNNNKKSSSSSGSAKNSSSSNSMAEVQRAAELQRQYLLEMIPPQQQSGASGSRQNNWKA
Protein: C-1-tetrahydrofolate synthase, cytoplasmic (C1-THF synthase) [Cleaved into: C-1-tetrahydrofolate synthase, cytoplasmic, N-terminally processed] [Includes: Methylenetetrahydrofolate dehydrogenase (EC 1.5.1.5); Methenyltetrahydrofolate cyclohydrolase (EC 3.5.4.9); Formyltetrahydrofolate synthetase (EC 6.3.4.3)] (Q922D8)
Organism: Mus musculus (Mouse)
Function: Trifunctional enzyme that catalyzes the interconversion of three forms of one-carbon-substituted tetrahydrofolate: (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate, 5,10-methenyltetrahydrofolate and (6S)-10-formyltetrahydrofolate. These derivatives of tetrahydrofolate are differentially required in nucleotide and amino acid biosynthesis, (6S)-10-formyltetrahydrofolate being required for purine biosynthesis while (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate is used for serine and methionine biosynthesis for instance.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:15611115}.
Interaction partners:
- Trifunctional purine biosynthetic protein adenosine-3
- Bifunctional purine biosynthesis protein ATIC
- Serine hydroxymethyltransferase, mitochondrial
- Serine hydroxymethyltransferase, cytosolic
- Methylenetetrahydrofolate reductase
- Methionine synthase
- Dihydrofolate reductase
- Thymidylate synthase
- Mitochondrial 10-formyltetrahydrofolate dehydrogenase
- Formimidoyltransferase-cyclodeaminase
Sequence:
MAPAGILNGKLVSAQIRDRLKNQVTRMQEQVPGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYVISLNEDASVHGFIVQLPLDSENSINTEAVINAIAPEKDVDGLTSVSAGKLARGDLNDCFIPCTPKGCLELIKEAGVQIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDDTKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRFLQKFKPGKWTIQYNKLNLKTPVPSDIAISRSCKPKLIGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLRQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLVPSVNGIRKFSDIQIRRLRRLGIEKTDPTTLTDDEINRFARLDIDPETITWQRVLDTNDRFLRKITIGQSPTEKGHTRTAQFDISVASEIMAVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMHGGGPTVTAGLPLPKAYTEEDLDLVEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSREHGAFDAVKCTHWAEGGQGALALAQAVQRASQAPSSFQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAEIYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
Protein: Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit beta (GMP-PDE beta) (EC 3.1.4.35) (P23440)
Organism: Mus musculus (Mouse)
Function: Rod-specific cGMP phosphodiesterase that catalyzes the hydrolysis of 3',5'-cyclic GMP (By similarity). Necessary for the formation of a functional phosphodiesterase holoenzyme. Involved in retinal circadian rhythm photoentrainment via modulation of UVA and orange light-induced phase-shift of the retina clock. May participate in processes of transmission and amplification of the visual signal (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P35913}; Lipid-anchor {ECO:0000250|UniProtKB:P35913}. Cell projection, cilium, photoreceptor outer segment {ECO:0000250|UniProtKB:P35913}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Guanine nucleotide-binding protein G
- Rod cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanylate kinase
- Rhodopsin
- Hypoxanthine-guanine phosphoribosyltransferase
- Peripherin-2
Sequence:
MSLSEEQVRSFLDGNPTFAHQYFGKKLSPENVAGACEDGWLADCGSLRELCQVEESAALFELVQDMQESVNMERVVFKILRRLCTILHADRCSLFMYRQRNGIAELATRLFSVQPDSLLEDCLVPPDSEIVFPLDIGIVGHVAQTKKMINVQDVAECPHFSSFADELTDYVTKNILSTPIMNGKDVVAVIMAVNKLDGPCFTSEDEDVFTKYLNFATLNLKIYHLSYLHNCETRRGQVLLWSANKVFEELTDIERQFHKAFYTVRAYLNCERYSVGLLDMTKEKEFFDVWPVLMGEAQPYSGPRTPDGREIVFYKVIDYILHGKEDIKVIPTPPADHWALASGLPTYVAESGFICNIMNASADEMFNFQEGPLDDSGWVIKNVLSMPIVNKKEEIVGVATFYNRKDGKPFDDQDEVLMESLTQFLGWSVLNTDTYDKMNKLENRKDIAQDMVLYHVRCDKDEIQEILPTRDRLGKEPADCEEDELGKILKEELPGPTKFDIYEFHFSDLECTELELVKCGIQMYYELGVVRKFQIPQEVLVRFLFSVSKAYRRITYHNWRHGFNVAQTMFTLLMTGKLKSYYTDLEAFAMVTAGLCHDIDHRGTNNLYQMKSQNPLAKLHGSSILERHHLEFGKFLLAEESLNIYQNLNRRQHEHVIHLMDIAIIATDLALYFKKRTMFQKIVDESKNYEDKKSWVEYLSLETTRKEIVMAMMMTACDLSAITKPWEVQSKVALLVAAEFWEQGDLERTVLDQQPIPMMDRNKAAELPKLQVGFIDFVCTFVYKEFSRFHEEILPMFDRLQNNRKEWKALADEYEAKVKALEEEKKKEEDRVAAKKVGTEVCNGGPAPKSSTCCIL
Protein: Probable prolyl 4-hydroxylase 4 (AtP4H4) (EC 1.14.11.2) (Q8LAN3)
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.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:F4JAU3}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:F4JAU3}.
Interaction partners:
- Pyrroline-5-carboxylate reductase
- Proline iminopeptidase
- Proline dehydrogenase 2, mitochondrial
- Proline dehydrogenase 1, mitochondrial
- procollagen-proline 3-dioxygenase
Sequence:
MARRGLLISFFAIFSVLLQSSTSLISSSSVFVNPSKVKQVSSKPRAFVYEGFLTELECDHMVSLAKASLKRSAVADNDSGESKFSEVRTSSGTFISKGKDPIVSGIEDKISTWTFLPKENGEDIQVLRYEHGQKYDAHFDYFHDKVNIVRGGHRMATILMYLSNVTKGGETVFPDAEIPSRRVLSENKEDLSDCAKRGIAVKPRKGDALLFFNLHPDAIPDPLSLHGGCPVIEGEKWSATKWIHVDSFDRIVTPSGNCTDMNESCERWAVLGECTKNPEYMVGTTELPGYCRRSCKAC
Protein: Malonyl CoA-acyl carrier protein transacylase (EC 2.3.1.39) (O54437)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MSASLAFVFPGQGSQSLGMLAELGAQQALVRDTFAEASEALGYDLWALVQNGPEERLNQTDKTQPAILTVSIALWRLWLAEGGARPAFVAGHSLGEYSALVAAESLAFADAVKLVERRGQLMQQAVPAGQGGMAAILGLEDADVLAACAEAAQGEVVSAVNFNAPGQVVIAGAAAAVERAIEACKARGAKRAVALPVSVPSHCELMRPAAEQFAASVESLQWQAPKISLVQNVSAAVPADLDTLRRDLLAQLYSPVRWVESIQLLAEKGVTELVECGPGKVLAGLNRRCAKGINTHGLDGVEAFAATRAALA
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 6 (Q9LHI0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Accessory subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I), that is believed to be not involved in catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Matrix side {ECO:0000250}.
Interaction partners:
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- NADH dehydrogenase 1 beta subcomplex subunit 10-B
- NADH dehydrogenase iron-sulfur protein 8-A, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase iron-sulfur protein 8-B, mitochondrial
- NADH dehydrogenase iron-sulfur protein 3
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase iron-sulfur protein 6
- Cytochrome b-c1 complex subunit 9, mitochondrial
- NADH dehydrogenase iron-sulfur protein 2
Sequence:
MAAPFALRKIGVPPNSANLTEARRRVFDFFRAACRSIPTIMDIYNLQDVVAPSQLRYAISAQIRNNAHITDPKVIDLLIFKGMEELTDIVDHAKQRHHIIGQYVVGEGLVQNTGNKDQGKTDFLKNFYTSNYF
Protein: Elongation factor 1-alpha 1 (EF-1-alpha-1) (EC 3.6.5.-) (Elongation factor Tu) (EF-Tu) (Eukaryotic elongation factor 1 A-1) (eEF1A-1) (P68105)
Organism: Oryctolagus cuniculus (Rabbit)
Function: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. Plays a role in the positive regulation of IFNG transcription in T-helper 1 cells as part of an IFNG promoter-binding complex with TXK and PARP1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P68104}. Nucleus {ECO:0000250|UniProtKB:P68104}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P68104}. Cell membrane {ECO:0000250|UniProtKB:P68104}. Note=Colocalizes with DLC1 at actin-rich regions in the cell periphery. Translocates together with ZPR1 from the cytoplasm to the nucleus and nucleolus after treatment with mitogens. Localization at the cell membrane depends on EEF1A1 phosphorylation status and the presence of PPP1R16B. {ECO:0000250|UniProtKB:P68104}.
Interaction partners:
- Elongation factor 1-gamma
- Elongation factor 1-gamma
- Elongation factor 1-beta
- GTP-binding nuclear protein Ran
- GTP-binding nuclear protein Ran
- Poly
- 3'-phosphoadenosine 5'-phosphosulfate synthase 2
- Bifunctional 3'-phosphoadenosine 5'-phosphosulfate synthase 1
- protein-tyrosine-phosphatase
- Valine--tRNA ligase
Sequence:
MGKEKTHINIVVIGHVDSGKSTTTGHLIYKCGGIDKRTIEKFEKEAAEMGKGSFKYAWVLDKLKAERERGITIDISLWKFETSKYYVTIIDAPGHRDFIKNMITGTSQADCAVLIVAAGVGEFEAGISKNGQTREHALLAYTLGVKQLIVGVNKMDSTEPPYSQKRYEEIVKEVSTYIKKIGYNPDTVAFVPISGWNGDNMLEPSANMPWFKGWKVTRKDGNASGTTLLEALDCILPPTRPTDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFAPVNVTTEVKSVEMHHEALSEALPGDNVGFNVKNVSVKDVRRGNVAGDSKNDPPMEAAGFTAQVIILNHPGQISAGYAPVLDCHTAHIACKFAELKEKIDRRSGKKLEDGPKFLKSGDAAIVDMVPGKPMCVESFSDYPPLGRFAVRDMRQTVAVGVIKAVDKKAAGAGKVTKSAQKAQKAK
Protein: Matrix protein (H2DMX1)
Organism: Avian paramyxovirus 1 (NDV) (Avian orthoavulavirus 1)
Subcellular location: Virion {ECO:0000256|ARBA:ARBA00004328}.
Interaction partners:
Sequence:
MDSSRTIGLYFDSALPSSSLLAFPIILQDTGDGKKQITPQYRIQRLDSWTDSKEDSVFITTYGFIFQVGNEEATVGVINDNPRHELLSSAMLCLGSVPNNGDLVELARACLTMVVTCKKSATNTERIVFSVVQAPRVLQNCMVVSNRYSSVNAVKHVKAPEMIPGSGALEYEVIFVSLTVVPRRDVYRIPTAVLKVSGSSLYNLALNVTIDVDVDPKSPLVKSLSKSDSGYYANLFLHIGLMSTVDKRGKKVTFDKIEEKIRRLNLSVGLSDVLGPSVLVKARGARTKLLAPFFSSSGTACYPIANASPQVAKILWSQTAHLRSVKVIIQAGTQRAVAVTADHEVTSTKIERRHAIAKYNPFRK
Protein: 43 kDa receptor-associated protein of the synapse (Rapsyn protein) (Receptor-associated protein of the synapse, 43kD) (Q8QGW4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Muscle, skeletal receptor tyrosine-protein kinase isoform 3 precursor
- Docking protein 7.
- Agrin
- Acetylcholine receptor subunit delta
- Acetylcholinesterase collagenic tail peptide isoform X2 of asymmetric acetylcholinesterase)
- Acetylcholine receptor subunit epsilon precursor
- Cholinergic receptor, nicotinic, beta 1
- Neuralized E3 ubiquitin protein ligase 1Ab.
- Acetylcholine receptor subunit gamma precursor
- Acetylcholine receptor subunit alpha
Sequence:
MGQDQTKQQIEKGLKLYQSNDTEKALYVWMKVLRKTSDPGGKFRVLGCLITAHSEMGKYKEMLQFSLAQINTAREMEDPDYLTEGYLNLARSNEKLCDFQKTVSYCETCLNMQGTTVSLQLNGQVCLSMGNAYLGLSVFQKALVSYEKALRYAHNNDDKMLECRVCCSLGNFYIQLKDFEKALFFPCKAAELVNDYGKGWSLKYRAMSQYHMSVAYKKLMRLPDAMECCEESMKIALQHGDRPLQALCLLNFADIHRCQKDVDKAFPRYESSMCIMSEIGNRLGQASIYVGVGKCWILQKEYDKALDSLQRANDLAEAIGNKLCILKVHSLCEGIYRCKEQQEELREQVVKFLQCVEELELYCGMCGESIGEKNQQLQALPCSHIFHLKCLQTNGTKGCPKCHRSSVKLGFV
Protein: Arabinosyltransferase RRA1 (EC 2.4.2.-) (Protein REDUCED RESIDUAL ARABINOSE 1) (Q9C9Q6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in the arabinosylation of cell wall components. Involved in the arabinosylation of extensin proteins in root hair cells. Extensins are structural glycoproteins present in cell walls and its arabinosylation is important for root hair cell development.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:21680836}; Single-pass type II membrane protein {ECO:0000305|PubMed:21680836}.
Interaction partners:
- Arabinosyltransferase XEG113
- Hydroxyproline O-arabinosyltransferase 1
- Hydroxyproline O-arabinosyltransferase 3
- Hydroxyproline O-arabinosyltransferase 2
- Arabinosyltransferase RRA2
- Arabinosyltransferase RRA3
- Peptidyl serine alpha-galactosyltransferase
- Prolyl 4-hydroxylase 5
- Alpha-L-arabinofuranosidase 1
- Prolyl 4-hydroxylase 2
Sequence:
MAVRKEKVQPFRECGIAIAVLVGIFIGCVCTILIPNDFVNFRSSKVASASCESPERVKMFKAEFAIISEKNGELRKQVSDLTEKVRLAEQKEVIKAGPFGTVTGLQTNPTVAPDESANPRLAKLLEKVAVNKEIIVVLANNNVKPMLEVQIASVKRVGIQNYLVVPLDDSLESFCKSNEVAYYKRDPDNAIDVVGKSRRSSDVSGLKFRVLREFLQLGYGVLLSDVDIVFLQNPFGHLYRDSDVESMSDGHDNNTAYGFNDVFDDPTMTRSRTVYTNRIWVFNSGFFYLRPTLPSIELLDRVTDTLSKSGGWDQAVFNQHLFYPSHPGYTGLYASKRVMDVYEFMNSRVLFKTVRKDEEMKKLKPVIIHMNYHSDKLERMQAAVEFYVNGKQDALDRFRDGS
Protein: Melanin-concentrating hormone receptor 1 (MCH receptor 1) (MCH-R1) (MCHR-1) (G-protein coupled receptor 24) (MCH-1R) (MCH1R) (MCHR) (SLC-1) (Somatostatin receptor-like protein) (Q8JZL2)
Organism: Mus musculus (Mouse)
Function: Receptor for melanin-concentrating hormone, coupled to both G proteins that inhibit adenylyl cyclase and G proteins that activate phosphoinositide hydrolysis.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q99705}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Pro-MCH
- BBSome complex member BBS1
- BBSome complex member BBS2
- Pro-neuropeptide Y
- BBSome complex member BBS4
- Pro-opiomelanocortin
- Somatostatin receptor type 3
- Hypocretin neuropeptide precursor
- BBSome complex member BBS7
- Tubby-related protein 3
Sequence:
MDLQASLLSTGPNASNISDGQDNFTLAGPPPRTRSVSYINIIMPSVFGTICLLGIVGNSTVIFAVVKKSKLHWCSNVPDIFIINLSVVDLLFLLGMPFMIHQLMGNGVWHFGETMCTLITAMDANSQFTSTYILTAMAIDRYLATVHPISSTKFRKPSMATLVICLLWALSFISITPVWLYARLIPFPGGAVGCGIRLPNPDTDLYWFTLYQFFLAFALPFVVITAAYVKILQRMTSSVAPASQRSIRLRTKRVTRTAIAICLVFFVCWAPYYVLQLTQLSISRPTLTFVYLYNAAISLGYANSCLNPFVYIVLCETFRKRLVLSVKPAAQGQLRTVSNAQTADEERTESKGT
Protein: Nicotinamidase (EC 3.5.1.19) (Nicotinamide deamidase) (NAMase) (P53184)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the deamidation of nicotinamide, an early step in the NAD(+) salvage pathway. Positively regulates SIR2-mediated silencing and longevity by preventing the accumulation of intracellular nicotinamide, an inhibitor of SIR2, during times of stress. Acts also on nicotinyl hydroxamate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12736687}. Nucleus {ECO:0000269|PubMed:12736687}. Peroxisome {ECO:0000269|PubMed:12736687, ECO:0000269|PubMed:14562095}. Note=Concentrates in peroxisomes (PubMed:12736687). {ECO:0000269|PubMed:12736687}.
Interaction partners:
- Nicotinate phosphoribosyltransferase
- NAD-dependent histone deacetylase SIR2
- Uridine nucleosidase
- NAD-dependent protein deacetylase HST2
- NAD-dependent histone deacetylase HST4
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- NAD-dependent histone deacetylase HST3
- Glutamine-dependent NAD
- Purine nucleoside phosphorylase
Sequence:
MKTLIVVDMQNDFISPLGSLTVPKGEELINPISDLMQDADRDWHRIVVTRDWHPSRHISFAKNHKDKEPYSTYTYHSPRPGDDSTQEGILWPVHCVKNTWGSQLVDQIMDQVVTKHIKIVDKGFLTDREYYSAFHDIWNFHKTDMNKYLEKHHTDEVYIVGVALEYCVKATAISAAELGYKTTVLLDYTRPISDDPEVINKVKEELKAHNINVVDK
Protein: Probable cytochrome c-type biogenesis protein NrfE (P32710)
Organism: Escherichia coli (strain K12)
Function: May be required for the biogenesis of c-type cytochromes. Possible subunit of a heme lyase.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305|PubMed:15919996}.
Interaction partners:
- Formate-dependent nitrite reductase complex subunit NrfF
- Formate-dependent nitrite reductase complex subunit NrfG
- Cytochrome c-type protein NrfB
- Protein NrfC
- Protein NrfD
- Thiol:disulfide interchange protein DsbE
- Cytochrome c-552
- Cytochrome c-type biogenesis protein CcmH
- Cytochrome c-type biogenesis protein CcmE
- Heme exporter protein C
Sequence:
MLTPLTAFAGVRLRWPAMMRLTCIGILAQFALLLLAFGVLTYCFLISDFSVIYVAQHSYSLLSWELKLAAVWGGHEGSLLLWVLLLSAWSALFAWHYRQQTDPLFPLTLAVLSLMLAALLLFVVLWSDPFVRIFPPAIEGRDLNPMLQHPGLIFHPPLLYLGYGGLMVAASVALASLLRGEFDGACARICWRWALPGWSALTAGIILGSWWAYCELGWGGWWFWDPVENASLLPWLSATALLHSLSLTRQRGIFCHWSLLLAIVTLMLSLLGTLIVRSGILVSVHAFALDNVRAVPLFSLFALISLASLALYGWRARDGGPAVHFSGLSREMLILATLLLFCAVLLIVLVGTLYPMIYGLLGWGRLSVGAPYFNRATLPFGLLMLVVIVLATFVSGKRVQLPALVAHAGVLLFAAGVVVSSVSRQEISLNLQPGQQVTLAGYTFRFECLDLQAKGNYTSEKAIVALFDHQQRIGELTPERRFYEARRQQMMEPSIRWNGIHDWYAVMGEKTGPDRYAFRLYVQSGVRWIWGGGLLMIAGALLSGWRGKKRDE
Protein: Aromatase (EC 1.14.14.14) (CYPXIX) (Cytochrome P-450AROM) (Cytochrome P450 19A1) (Estrogen synthase) (P11511)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase that catalyzes the conversion of C19 androgens, androst-4-ene-3,17-dione (androstenedione) and testosterone to the C18 estrogens, estrone and estradiol, respectively. Catalyzes three successive oxidations of C19 androgens: two conventional oxidations at C19 yielding 19-hydroxy and 19-oxo/19-aldehyde derivatives, followed by a third oxidative aromatization step that involves C1-beta hydrogen abstraction combined with cleavage of the C10-C19 bond to yield a phenolic A ring and formic acid. Alternatively, the third oxidative reaction yields a 19-norsteroid and formic acid. Converts dihydrotestosterone to delta1,10-dehydro 19-nordihydrotestosterone and may play a role in homeostasis of this potent androgen. Also displays 2-hydroxylase activity toward estrone. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:2973313}; Multi-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000269|PubMed:2973313}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 17-beta-hydroxysteroid dehydrogenase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- 17-beta-hydroxysteroid dehydrogenase type 3
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 17-beta-hydroxysteroid dehydrogenase type 2
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- Sulfotransferase 1E1
Sequence:
MVLEMLNPIHYNITSIVPEAMPAATMPVLLLTGLFLLVWNYEGTSSIPGPGYCMGIGPLISHGRFLWMGIGSACNYYNRVYGEFMRVWISGEETLIISKSSSMFHIMKHNHYSSRFGSKLGLQCIGMHEKGIIFNNNPELWKTTRPFFMKALSGPGLVRMVTVCAESLKTHLDRLEEVTNESGYVDVLTLLRRVMLDTSNTLFLRIPLDESAIVVKIQGYFDAWQALLIKPDIFFKISWLYKKYEKSVKDLKDAIEVLIAEKRRRISTEEKLEECMDFATELILAEKRGDLTRENVNQCILEMLIAAPDTMSVSLFFMLFLIAKHPNVEEAIIKEIQTVIGERDIKIDDIQKLKVMENFIYESMRYQPVVDLVMRKALEDDVIDGYPVKKGTNIILNIGRMHRLEFFPKPNEFTLENFAKNVPYRYFQPFGFGPRGCAGKYIAMVMMKAILVTLLRRFHVKTLQGQCVESIQKIHDLSLHPDETKNMLEMIFTPRNSDRCLEH
Protein: Erythritol/L-threitol dehydrogenase (EC 1.1.1.-) (A0QXD8)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Catalyzes the NAD-dependent reversible oxidation of erythritol and L-threitol. Involved in the degradation pathways of erythritol and L-threitol, that allow M.smegmatis to grow on these compounds as the sole carbon source.
Interaction partners:
- Erythritol/L-threitol-binding protein
- D-erythrulose kinase
- D-erythrulose-4-phosphate isomerase 1
- Transcriptional regulator
- Transporter
- ABC transporter, permease protein
- Trehalose import ATP-binding protein SugC
- Trehalose import ATP-binding protein SugC
Sequence:
MSNQVPEKMQAVVCHGPHDYRLEEVAVPQRKPGEALIRVEAVGICASDLKCYHGAAKFWGDENRPAWAETMVIPGHEFVGRVVELDDEAAQRWGIAVGDRVVSEQIVPCWECLFCKRGQYHMCQPHDLYGFKRRTPGAMASYMVYPAEALVHKVSPDIPAQHAAFAEPLSCSLHAVERAQITFEDTVVVAGCGPIGLGMIAGAKAKSPMRVIALDMAPDKLKLAEKCGADLTINIAEQDAEKIIKDLTGGYGADVYIEGTGHTSAVPQGLNLLRKLGRYVEYGVFGSDVTVDWSIISDDKELDVLGAHLGPYCWPAAIKMIESGALPMDEICTHQFPLTEFQKGLDLVASGKESVKVSLIPA
Protein: Transcription factor MYC4 (AtMYC4) (Basic helix-loop-helix protein 4) (AtbHLH4) (bHLH 4) (Transcription factor EN 37) (bHLH transcription factor bHLH004) (O49687)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor involved in jasmonic acid (JA) gene regulation. With MYC2 and MYC3, controls additively subsets of JA-dependent responses. Can form complexes with all known glucosinolate-related MYBs to regulate glucosinolate biosynthesis. Binds to the G-box (5'-CACGTG-3') of promoters. Activates multiple TIFY/JAZ promoters.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:21321051, ECO:0000269|PubMed:21335373}.
Interaction partners:
- Transcription factor MYB24
- Protein TIFY 7
- Transcription factor MYB21
- Protein TIFY 10A
- Protein TIFY 3B
- Protein TIFY 9
- Protein TIFY 5A
- Protein TIFY 6B
- Protein TIFY 11B
- Protein TIFY 5B
Sequence:
MSPTNVQVTDYHLNQSKTDTTNLWSTDDDASVMEAFIGGGSDHSSLFPPLPPPPLPQVNEDNLQQRLQALIEGANENWTYAVFWQSSHGFAGEDNNNNNTVLLGWGDGYYKGEEEKSRKKKSNPASAAEQEHRKRVIRELNSLISGGVGGGDEAGDEEVTDTEWFFLVSMTQSFVKGTGLPGQAFSNSDTIWLSGSNALAGSSCERARQGQIYGLQTMVCVATENGVVELGSSEIIHQSSDLVDKVDTFFNFNNGGGEFGSWAFNLNPDQGENDPGLWISEPNGVDSGLVAAPVMNNGGNDSTSNSDSQPISKLCNGSSVENPNPKVLKSCEMVNFKNGIENGQEEDSSNKKRSPVSNNEEGMLSFTSVLPCDSNHSDLEASVAKEAESNRVVVEPEKKPRKRGRKPANGREEPLNHVEAERQRREKLNQRFYSLRAVVPNVSKMDKASLLGDAISYISELKSKLQKAESDKEELQKQIDVMNKEAGNAKSSVKDRKCLNQESSVLIEMEVDVKIIGWDAMIRIQCSKRNHPGAKFMEALKELDLEVNHASLSVVNDLMIQQATVKMGNQFFTQDQLKVALTEKVGECP
Protein: Calsyntenin-3 (Q8R553)
Organism: Rattus norvegicus (Rat)
Function: May modulate calcium-mediated postsynaptic signals. Complex formation with APBA2 and APP, stabilizes APP metabolism and enhances APBA2-mediated suppression of beta-APP40 secretion, due to the retardation of intracellular APP maturation.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, dendrite {ECO:0000250|UniProtKB:Q99JH7}. Note=Most prominent in the postsynaptic specializations of asymmetric (type I) synapses with both axodendritic and axospinous localization. {ECO:0000250|UniProtKB:Q99JH7}.; SUBCELLULAR LOCATION: [Isoform CLSTN3beta]: Lipid droplet {ECO:0000250|UniProtKB:Q99JH7}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q99JH7}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to endoplasmic reticulum-lipid droplet contact sites through the partitioning of its N-terminal hydrophobic hairpins onto lipid droplets while its C-terminal transmembrane domain remains anchored in the endoplasmic reticulum. {ECO:0000250|UniProtKB:Q99JH7}.
Interaction partners:
- Leucine-rich repeat transmembrane neuronal protein 1
- Neurexin-3
- Neurexin-2
- Neurexin-1
Sequence:
MTLLLVSLLLASLLQISSGNKANKHKPWIEAEYQGIVMENDNTVLLNPPLFALDKDAPLRYAGEICGFRLHGSGVPFKAVILDKATGEGLIRAKEPVDCEAQKEHTFTTQAYDCVDGPDGANTKKSHKATVHVRVNDVNEFAPVFVERLYRAAVTEGKLYDRILRVEAIDGDCSPQYSQICYYEILTPNTPFLIDNDGNIENTEKLQYSGEKLYKFTVTAYDCGKKRAADDAEVEIQVKPTCKPSWQGWNKRIEYAPGAGSLALFPGIRLETCDEPLWNIQATIELQTSHVAKGCDRDNYSERALRKLCGAATGEVDLLPMPGPNANWTAGLSVHYSQDSSLIYWFNGTQAVQVPLGGPAGLGSGPQDGLSDHFTLSFWMKHSVTPSKGKKEEETIVCNTIQNEDGYSHYSLTVHGCRIAFLYWPLLESARPVKFLWKLEQVCDDEWHHYALNLEFPTVTLYTDGISFDPALIHDNGLIHPPRREPALMIGACWSEEKNKEKEKGGENSTDTTSGDPLPIHHYFHGYLAGFSVRSGRLESREVIECLYACREGLDYRDFESLGKGMKVHVNPSQSLLTLEGDDVETFNHALQHVAYMNTLRFATPGVRPLRLTTAVKCFSEESCVSIPEVEGYVVVLQPDAPQILLSGTAHFARPAVDFEGPEGVPLFPDLQITCSISHQVEAKADESWQGTVTDTRMSDEIVHNLDGCEISLVGDDLDPERESLLLDMASLQQRGLELTNRSAYLTIAGVETITVYEEILRQARYQLRHGAALYARKFRLSCSEMNGRYSSNEFIVEVNVLHSMNRVAHPSHVLSSQQFLHRGHQPPPEMAGHSLASSHRNSMVPSAATLIIVVCVGFLVLMVILGLVRIHSLHRRVSGTGGPSGASADPKDPDLFWDDSALTIIVNPMESYQNQQTGVAGVAGGQQEEEDSSDSEAADSPSSDERRIIESPPHRY