wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha-maltose-1-phosphate synthase (M1P synthase) (EC 2.4.1.342) (ADP-alpha-D-glucose:alpha-D-glucose-1-phosphate 4-alpha-D-glucosyltransferase) (M1P-producing glucosyltransferase) (P9WMZ1)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of the maltose-1-phosphate (M1P) building block required for alpha-glucan production by the key enzyme GlgE. Catalyzes the formation of an alpha-1,4 linkage between glucose from ADP-glucose and glucose 1-phosphate (G1P) to yield maltose-1-phosphate (M1P). Also able to catalyze the elongation of the non-reducing ends of glycogen, maltodextrin and maltoheptaose using ADP-glucose as sugar donor, however the rate of the reaction appears to be too low to be physiologically relevant. GlgM is also able to use UDP-glucose as sugar donor with G1P, however, it is less efficient than with ADP-glucose. UDP-glucose is not used as sugar donor when glycogen is used as acceptor.
Interaction partners:
- Glucose-1-phosphate adenylyltransferase
- Alpha-1,4-glucan:maltose-1-phosphate maltosyltransferase
- 1,4-alpha-glucan branching enzyme GlgB
- Maltokinase
- UTP--glucose-1-phosphate uridylyltransferase
- Glycogen phosphorylase
- Malto-oligosyltrehalose trehalohydrolase
- 4-alpha-glucanotransferase
- Probable phosphoglucomutase PgmA
- Probable 1,4-alpha-glucan branching enzyme Rv3031
Sequence:
MRVAMLTREYPPEVYGGAGVHVTELVAYLRRLCAVDVHCMGAPRPGAFAYRPDPRLGSANAALSTLSADLVMANAASAATVVHSHTWYTALAGHLAAILYDIPHVLTAHSLEPLRPWKKEQLGGGYQVSTWVEQTAVLAANAVIAVSSAMRNDMLRVYPSLDPNLVHVIRNGIDTETWYPAGPARTGSVLAELGVDPNRPMAVFVGRITRQKGVVHLVTAAHRFRSDVQLVLCAGAADTPEVADEVRVAVAELARNRTGVFWIQDRLTIGQLREILSAATVFVCPSVYEPLGIVNLEAMACATAVVASDVGGIPEVVADGITGSLVHYDADDATGYQARLAEAVNALVADPATAERYGHAGRQRCIQEFSWAYIAEQTLDIYRKVCA
Protein: Presenilin-like protein At2g29900 (Q9SIK7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Nicastrin
- Probable gamma-secretase subunit PEN-2
- Gamma-secretase subunit APH1-like
- Signal peptide peptidase
- At5g11810
- Leucine-rich repeat
- Pentatricopeptide repeat-containing protein At5g64320
- Pentatricopeptide repeat-containing protein At4g38010
- Protein NSP-INTERACTING KINASE 1
Sequence:
MDRNQRPRSILDSLGEELIAILTPVSICMFTVVLLVCILNSDPSSSSASFSSIATAAYSESDSDSSWDKFVGALLNSVVFVAAITVATFVLVLLFYLRCVKFLKFYMGFSAFIVLGNLGGEILVLLIDRFRFPIDSITFLILLFNFSVVGVFAVFMSKFSILITQGYLVWIGVLVAYFFTLLPEWTTWVLLVALALYDIAAVLLPVGPLRLLVEMAISRDEDIPALVYEARPVIRNDSRSVQRRVWREQRSSQNNANRNEVRVVESAEVEEEHVGSSERAEISVPLIDRRPEQAENSETFLEGIGLGSSGAIKLGLGDFIFYSVLVGRAAMYDLMTVYACYLAIIAGLGITLMLLSVYQKALPALPVSIMLGVVFYFLARLLLEVFVVQCSSNLVMF
Protein: SMAD family member 3 (H3BP09)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MELCEFAFNMKKDEVCVNPYHYQRVETPVLPPVLVPRHTEIPAEFPPLDDYSHSIPENTNFPAGIEPQSNIPETPPPGYLSEDGETSDHQMNHSMDAGSPNLSPNPMSPAHNNL
Protein: Active breakpoint cluster region-related protein (Q5SSL4)
Organism: Mus musculus (Mouse)
Function: Protein with a unique structure having two opposing regulatory activities toward small GTP-binding proteins. The C-terminus is a GTPase-activating protein domain which stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP hydrolysis of RAC1 or CDC42, leading to down-regulation of the active GTP-bound form. The central Dbl homology (DH) domain functions as guanine nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-bound to the GTP-bound form (By similarity). Functions as an important negative regulator of neuronal RAC1 activity. Regulates macrophage functions such as CSF-1 directed motility and phagocytosis through the modulation of RAC1 activity.
Subcellular location: Cell projection, dendritic spine {ECO:0000269|PubMed:20962234}. Cell projection, axon {ECO:0000269|PubMed:20962234}. Synapse {ECO:0000250|UniProtKB:A0A0G2JTR4}.
Interaction partners:
Sequence:
MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPPEGSETMPYIDESPTMSPQLSARSQGGGDSVSPTPPEGLAPGVEAGKGLEMRKLVLSGFLASEEIYINQLEALLLPMKPLKATATTSQPVLTIQQIETIFYKIQDIYEIHKEFYDNLCPKVQQWDSQVTMGHLFQKLASQLGVYKAFVDNYKVALETAEKCSQSNNQFQKISEELKVKGPKDSKDSHTSVTMEALLYKPIDRVTRSTLVLHDLLKHTPVDHPDYPLLQDALRISQNFLSSINEDIDPRRTAVTTPKGETRQLVKDGFLVEMSESSRKLRHVFLFTDVLLCAKLKKTSAGKHQQYDCKWYIPLADLVFPSPEESEASPQVHPFPDHELEDMKTKISALKSEIQKEKANKGQSRAIERLKKKMFENEFLLLLNSPTIPFRIHNRNGKSYLFLLSSDYERSEWREAIQKLQKKDLQAFVLSSVELQVLTGSCFKLRTVHNIPVTSNKDDDESPGLYGFLHVIVHSAKGFKQSANLYCTLEVDSFGYFVSKAKTRVFRDTTEPKWDEEFEIELEGSQSLRILCYEKCYDKTKVNKDNNEIVDKIMGKGQIQLDPQTVESKNWHTDVIEMNGIKVEFSMKFTSRDMSLKRTPSKKQTGVFGVKISVVTKRERSKVPYIVRQCIEEVEKRGIEEVGIYRISGVATDIQALKAVFDANNKDILLMLSDMDINAIAGTLKLYFRELPEPLLTDRLYPAFMEGIALSDPAAKENCMMHLLRSLPDPNLITFLFLLEHLKRVAEKEPINKMSLHNLATVFGPTLLRPSEVESKAHLTSAADIWSHDVMAQVQVLLYYLQHPPISFAELKRNTLYFSTDV
Protein: Serine endoprotease DegS (EC 3.4.21.107) (Site-1 protease DegS) (S1P protease DegS) (Site-1-type intramembrane protease) (P0AEE3)
Organism: Escherichia coli (strain K12)
Function: A site-1 protease (S1P) that cleaves the peptide bond between 'Val-148' and 'Ser-149' in RseA. Part of a regulated intramembrane proteolysis (RIP) cascade. When heat shock or other environmental stresses disrupt protein folding in the periplasm, DegS senses the accumulation of unassembled outer membrane porins (OMP) and then initiates RseA (anti sigma-E factor) degradation by cleaving its periplasmic domain, making it a substrate for subsequent cleavage by RseP. This cascade ultimately leads to the sigma-E-driven expression of a variety of factors dealing with folding stress in the periplasm and OMP assembly. Required for basal and stress-induced degradation of RseA.
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:11442831}; Single-pass membrane protein {ECO:0000305|PubMed:11442831}. Note=It is unclear how this protein is anchored to the inner membrane, programs predict a signal sequence, but replacing the N-terminal 26 residues with a known signal sequence gives a protein unable to fully complement a disruption mutant. {ECO:0000269|PubMed:11442831}.
Interaction partners:
- Anti-sigma-E factor RseA
- Regulator of sigma-E protease RseP
- Sigma-E factor regulatory protein RseB
- ECF RNA polymerase sigma-E factor
- Lon protease
Sequence:
MFVKLLRSVAIGLIVGAILLVAMPSLRSLNPLSTPQFDSTDETPASYNLAVRRAAPAVVNVYNRGLNTNSHNQLEIRTLGSGVIMDQRGYIITNKHVINDADQIIVALQDGRVFEALLVGSDSLTDLAVLKINATGGLPTIPINARRVPHIGDVVLAIGNPYNLGQTITQGIISATGRIGLNPTGRQNFLQTDASINHGNSGGALVNSLGELMGINTLSFDKSNDGETPEGIGFAIPFQLATKIMDKLIRDGRVIRGYIGIGGREIAPLHAQGGGIDQLQGIVVNEVSPDGPAANAGIQVNDLIISVDNKPAISALETMDQVAEIRPGSVIPVVVMRDDKQLTLQVTIQEYPATN
Protein: Marneral synthase (AtMRN1) (EC 5.4.99.53) (Pentacyclic triterpene synthase 5) (AtPEN5) (Q9FJV8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Converts oxidosqualene to marneral.
Interaction partners:
- Squalene epoxidase 1
- Squalene epoxidase 4
- Squalene epoxidase 5
- Squalene epoxidase 2, mitochondrial
- Squalene epoxidase 3
- Squalene epoxidase 6
- Cytochrome P450 71A16
- Cytochrome P450 705A12
- Cytochrome P450 708A2
- Cytochrome P450 705A5
Sequence:
MWRLRIGAEARQDPHLFTTNNFAGRQIWEFDANGGSPEELAEVEEARLNFANNKSRFKASPDLFWRRQFLREKKFEQKIPRVRIEDAEKITYEDAKTALRRGVLYYAACQANDGHWPSEVSGSMFLDAPFVICLYITGHLEKIFTLEHVKELLRYMYNTQNEDGGWGLDVESHSVMFCTVLNYICLRILGVEPDHDGQKSACARARKWILDHGGATYAPMVAKAWLSVLGVYDWSGCKPLPPEIWMLPSFSPINGGTLWIYIRDLLMGMSYLYGKKFVATPTALILQLREELYPQPYSKIIWSKARNRCAKEDLLYPKSFGQDLFWEGVHMLSENIINRWPLNKFVRQRALRTTMELVHYHDETTHYITGACVAKPFHMLACWVEDPDGDYFKKHLARVPDFIWIAEDGLKFQLMGMQSWNAALSLQVMLAANMDDEIRSTLIKGYDFLKQSQISENPQGDHLKMFRDITKGGWTFQDREQGLPISDGTAESIECCIHFHRMPSEFIGEKMDVEKLYDAVNFLIYLQSDNGGMPVWEPAPGKKWLEWLSPVEHVENTVVEQEYLECTGSVIAGLVCFKKEFPDHRPKEIEKLIKKGLKYIEDLQMPDGSWYGNWGVCFTYGTLFAVRGLAAAGKTFGNSEAIRRAVQFILNTQNAEGGWGESALSCPNKKYIPSKGNVTNVVNTGQAMMVLLIGGQMERDPSPVHRAAKVLINSQLDIGDFPQQERRGIYMNMLLHYPTYRNMFSLWALALYTNALRLLVS
Protein: Nuclear protein MDM1 (Q8TC05)
Organism: Homo sapiens (Human)
Function: Microtubule-binding protein that negatively regulates centriole duplication. Binds to and stabilizes microtubules.
Subcellular location: Nucleus {ECO:0000269|PubMed:26337392}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:26337392}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:26337392}. Note=Localizes to the centriole lumen. {ECO:0000269|PubMed:26337392}.
Interaction partners:
Sequence:
MPVRFKGLSEYQRNFLWKKSYLSESCNSSVGRKYPWAGLRSDQLGITKEPSFISKRRVPYHDPQISKSLEWNGAISESNVVASPEPEAPETPKSQEAEQKDVTQERVHSLEASRVPKRTRSHSADSRAEGASDVENNEGVTNHTPVNENVELEHSTKVLSENVDNGLDRLLRKKAGLTVVPSYNALRNSEYQRQFVWKTSKETAPAFAANQVFHNKSQFVPPFKGNSVIHETEYKRNFKGLSPVKEPKLRNDLRENRNLETVSPERKSNKIDDRLKLEAEMELKDLHQPKRKLTPWKHQRLGKVNSEYRAKFLSPAQYLYKAGAWTHVKGNMPNQVKELREKAEFYRKRVQGTHFSRDHLNQILSDSNCCWDVSSTTSSEGTVSSNIRALDLAGDPTSHKTLQKCPSTEPEEKGNIVEEQPQKNTTEKLGVSAPTIPVRRRLAWDTENTSEDVQKQPGEKEEEDDNEEEGDRKTGKQAFMGEQEKLDVREKSKADKMKEGSDSSVSSEKGGRLPTPKLRELGGIQRTHHDLTTPAVGGAVLVSPSKMKPPAPEQRKRMTSQDCLETSKNDFTKKESRAVSLLTSPAAGIKTVDPLPLREDSEDNIHKFAEATLPVSKIPKYPTNPPGQLPSPPHVPSYWHPSRRIQGSLRDPEFQHNVGKARMNNLQLPQHEAFNDEDEDRLSEISARSAASSLRAFQTLARAKKRKENFWGKT
Protein: (-)-alpha-pinene synthase 1, chloroplastic (EC 4.2.3.119) ((-)-beta-phellandrene synthase (-)alpha/betapin1, chloroplastic) (EC 4.2.3.52) ((-)-beta-pinene synthase 1, chloroplastic) (EC 4.2.3.120) (Terpene synthase (-)alpha/betapin1) (PbTPS-(-)alpha/betapin1) (R9QMW1)
Organism: Pinus banksiana (Jack pine) (Pinus divaricata)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products included in conifer oleoresin secretions and volatile emissions; these compounds contribute to biotic and abiotic stress defense against herbivores and pathogens. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) to (-)-alpha-pinene and (-)-beta-pinene, and, to a lower extent, to (-)-beta-phellandrene.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MDLISVLPSASKSCVCLHKPLSSSTHKLKPFCKTIRILGMPRRWKFAGPSMSLSTVASDDDIQRRTGGYHSNLWNDDVIQFLSTPYGELAYRERAERLIDEVRDIFSSMSLEDGEFSDLIQRLWMVDNVERLGIDRHFKNEIKSALDYVYSYWSEKGIGCGTKSIITNLNSTALGFRTLRLHGYPVSADVLKHFRNQIGQFVSCPSETEEDIRSMVNLYRASLIAFPGEEVMEEAERFSEKYLKETLQKIPDCSLSREIGDVLEHGWHTNLPRLEARNYIDVFGQDTKNMESNRKTEKLLELAKLEFNIFQSIQETELESLLRWWNDSGSPQITFTRHRHVEYYTLASCIAFEPQHSGFRLGFAKACHIITVLDDMYDLFGTVDELKLFTAAIKRWDPSATDCLPQYMKGIYMMVYNTVNEMSAEAQKAQGRDTLNYARQAWEDCLDSYMQEAKWIATGFLPTFEEYLENGKVSSAHRVSALQPMLTMDIPFPPHILKEVDFPSNLNDLACAMLRLRGDTRCYQADRARGEETSCISCYMKDNPGATEEDALNRLNVMISGVIKELNWELLKPDSGVPISSKKINFDITRAFHYGYKYRDGYSVSSVETKSFVMRTLLEPVPL
Protein: Histidine--tRNA ligase, mitochondrial (EC 6.1.1.21) (Histidyl-tRNA synthetase) (HisRS) (O43011)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the aminoacylation of histidyl-tRNA in both the cytoplasm and the mitochondrion.
Subcellular location: Mitochondrion {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable threonine--tRNA ligase, mitochondrial
- Threonine--tRNA ligase, cytoplasmic
- Putative glycine--tRNA ligase
- Lysine--tRNA ligase, cytoplasmic
- Lysine--tRNA ligase, mitochondrial
- Valine--tRNA ligase
- Uncharacterized ABC transporter ATP-binding protein C29A3.09c
- Putative leucine--tRNA ligase, cytoplasmic
- eIF-2-alpha kinase activator gcn1
- Valine--tRNA ligase, mitochondrial
Sequence:
MFVFTKNLFTTKFSSSLLNWRFLRTMADSLVDINERITSQGNLVRSLKSQGASKEDIDKEVAKLLQLKNLKLGGSEVSGKKKDTSFTLKTPKGTKDWCDKDVVLREHIFSTVTEIFKRHGGVTLDTPVFELKEILSGKYGEDSKLIYDLKDQGGELCSLRYDLTVPFARWLAMNPKVTSIKRFHIAKVYRRDQPAMTKGRMREFYQCDFDIAGNYDPMIPDSEALKVLVEALDALEVGNYTIKLNHRKILDGIFTVCGVPDDKIRTISSAVDKLDKLPWEDVRREMVVEKGLKEEVADKIKEYVLLKGDRSLLDKLEADSLLSSNSSAVAAFNDMRLLFDYLEAFGVLDRFSFDMSLARGLDYYTGIIYEAVTEASAPKIKSSAEKKKSADPEADRSNDDSIGVGSIAAGGRYDNLVGMFAAKKNAKIPCVGISLGLERIFSILRSKIPDEDIRANDVDVFVMAFGGGKEWTGFLKERMSVCKDLWANGIKAEFLYKVKPKPRQQFDAADKFDVPFAVILGQDEFAKGSVRIKQMGLKENSDEGQLVPREEMVSVLKKLLKYD
Protein: Aspartyl/asparaginyl beta-hydroxylase (EC 1.14.11.16) (Aspartate beta-hydroxylase) (ASP beta-hydroxylase) (Peptide-aspartate beta-dioxygenase) (Q28056)
Organism: Bos taurus (Bovine)
Function: Specifically hydroxylates an Asp or Asn residue in certain epidermal growth factor-like (EGF) domains of a number of proteins.
Subcellular location: Endoplasmic reticulum membrane; Single-pass type II membrane protein {ECO:0000303|PubMed:1378441}.
Interaction partners:
- Calsequestrin
- Calsequestrin
- Ryanodine receptor 2
- Triadin
- Ryanodine receptor 1.
- Coagulation factor X
Sequence:
MAPRKNAKGGGGNSSSSSSGSPTGCTSGGSSSPGARRETKQGGLKNGRKGGLSGSSFFTWFMVIALLGVWTSVAVVWFDLVDYEEVLAKAKDFRYNLSEVLQGKLGIYDADGDGDFDVDDAKVLLGLKEKPAPKPTVPPEEADMYPWLEDQVLESPGRQNIEDEVYEQVQSLDETVYSEPGENLPQEPEGPAEELQPDDHVFVGSDADDRYEPMGTGAVHEETEDSYHIEETASPAYSQDMEDMMYEQENPDSSEPVVVDDAERTYQETDDVTYRDYDEQDHAVDNSNTILEEPHMPPAEEQQEVPPETNKKADEPGKKGKVKKKKPKLLNKFDKTIKAELDAAEKLRKRGKIEEAVNAFEELVRKYPQSPGARYGKAQCEDDLAEKRRSNEILRRAIETYQEAASLPDAPTDLVKLSLKRRSDRQQFLGHMRGSLLTLQKLVQLFPDDTALKNDLGVGYLLIGDNDSAKKVYEEVLSVTPNDGFAKVHYGFILKAQNKIAESIPYLKEGIESGDPGTDDGRFYFHLGDAMQRVGNKEAYRWYELGHQRGHFASVWQRSLYNVQGLKAQPWWTPKETGYTELVKSLERNWKLIRDEGLAAMDRTHGLFLPEDENLREKGDWSQFTLWQQGRKNENACKGAPKTCSLLDKFPETTGCRRGQIKYSIMHPGTHVWPHTGPTNCRLRMHLGLVIPKEGCKIRCANETRTWEEGKVLIFDDSFEHEVWQDAASFRLIFIVDVWHPELTPHQRRSLPAI
Protein: Natural killer cell protein group 2-A2 (Q9WVJ8)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MSNERVTYAELKVAKNSRNQHRKPRGPRSSISVIEQEIIYSDFSFQNPSQEHPWICRNCPCKDTEAKAQINSSMTRTHRDINYTLSSAQPCPHCPKEWISYSHNCYFIGMERKSWNDSLVSCISKNCSLLYIDSEEEQDFLQSLSLISWTGILRKGRGQPWVWKEDSIFKPMIAEILHDECNCAMMSASGLTADNCTTLHPYLCKCKFPI
Protein: Zinc finger protein 8 (Zinc finger protein HF.18) (P17098)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. May modulate BMP and TGF-beta signal transduction, through its interaction with SMAD proteins.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDPEDEGVAGVMSVGPPAARLQEPVTFRDVAVDFTQEEWGQLDPTQRILYRDVMLETFGHLLSIGPELPKPEVISQLEQGTELWVAERGTTQGCHPAWEPRSESQASRKEEGLPEEEPSHVTGREGFPTDAPYPTTLGKDRECQSQSLALKEQNNLKQLEFGLKEAPVQDQGYKTLRLRENCVLSSSPNPFPEISRGEYLYTYDSQITDSEHNSSLVSQQTGSPGKQPGENSDCHRDSSQAIPITELTKSQVQDKPYKCTDCGKSFNHNAHLTVHKRIHTGERPYMCKECGKAFSQNSSLVQHERIHTGDKPYKCAECGKSFCHSTHLTVHRRIHTGEKPYECQDCGRAFNQNSSLGRHKRTHTGEKPYTCSVCGKSFSRTTCLFLHLRTHTEERPYECNHCGKGFRHSSSLAQHQRKHAGEKPFECRQRLIFEQTPALTKHEWTEALGCDPPLSQDERTHRSDRPFKCNQCGKCFIQSSHLIRHQITHTREEQPHGRSRRREQSSSRNSHLVQHQHPNSRKSSAGGAKAGQPESRALALFDIQKIMQEKNPVHVIGVEEPSVGASMLFDIREST
Protein: Gap junction beta-7 protein (Connexin-25) (Cx25) (Q6PEY0)
Organism: Homo sapiens (Human)
Function: One gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell junction, gap junction {ECO:0000250}.
Interaction partners:
- Gap junction epsilon-1 protein
Sequence:
MSWMFLRDLLSGVNKYSTGTGWIWLAVVFVFRLLVYMVAAEHVWKDEQKEFECNSRQPGCKNVCFDDFFPISQVRLWALQLIMVSTPSLLVVLHVAYHEGREKRHRKKLYVSPGTMDGGLWYAYLISLIVKTGFEIGFLVLFYKLYDGFSVPYLIKCDLKPCPNTVDCFISKPTEKTIFILFLVITSCLCIVLNFIELSFLVLKCFIKCCLQKYLKKPQVLSV
Protein: Homoserine O-acetyltransferase (HAT) (EC 2.3.1.31) (Homoserine O-trans-acetylase) (Homoserine transacetylase) (HTA) (P45131)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine. Utilizes a ping-pong kinetic mechanism in which the acetyl group of acetyl-CoA is initially transferred to the enzyme to form an acetyl-enzyme intermediate before subsequent transfer to homoserine to form the final product, O-acetylhomoserine.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00296}.
Interaction partners:
- Bifunctional aspartokinase/homoserine dehydrogenase
- 5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase
- Tryptophan biosynthesis protein TrpCF
- Cysteine synthase
Sequence:
MSVQNVVLFDTQPLTLMLGGKLSHINVAYQTYGTLNAEKNNAVLICHALTGDAEPYFDDGRDGWWQNFMGAGLALDTDRYFFISSNVLGGCKGTTGPSSINPQTGKPYGSQFPNIVVQDIVKVQKALLDHLGISHLKAIIGGSFGGMQANQWAIDYPDFMDNIVNLCSSIYFSAEAIGFNHVMRQAVINDPNFNGGDYYEGTPPDQGLSIARMLGMLTYRTDLQLAKAFGRATKSDGSFWGDYFQVESYLSYQGKKFLERFDANSYLHLLRALDMYDPSLGYDNVKEALSRIKARYTLVSVTTDQLFKPIDLYKSKQLLEQSGVDLHFYEFPSDYGHDAFLVDYDQFEKRIRDGLAGN
Protein: Bypass of stop codon protein 2 (Q05611)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Lipid droplet {ECO:0000269|PubMed:14562095}. Membrane {ECO:0000269|PubMed:14562095}; Single-pass membrane protein {ECO:0000269|PubMed:14562095}. Note=Punctate lipid particles.
Interaction partners:
- Increased recombination centers protein 23
Sequence:
MFFFPKLRKLIGSTVIDHDTKNSSGKEEIMSNSRLALVIINHAFDKVLSLTWHCGILSEIRSGLMLMFGIFQLMCSLGVIVLLLPIIILDAIDLFLYMCRLLDYGCKLFHYNRSSLPVADGKEKTSGPISGKEEIVIDEEIINMLNESSESLINHTTAGLEYDISSGSVNKSRRLNSTSTVTFVKQNKLVNERREDAYYEEEDDDFLSNPNYDKISLIEKSFTSRFEVACEQKAA
Protein: Formimidoyltransferase-cyclodeaminase (Formiminotransferase-cyclodeaminase) (FTCD) (LCHC1) [Includes: Glutamate formimidoyltransferase (EC 2.1.2.5) (Glutamate formiminotransferase) (Glutamate formyltransferase); Formimidoyltetrahydrofolate cyclodeaminase (EC 4.3.1.4) (Formiminotetrahydrofolate cyclodeaminase)] (O95954)
Organism: Homo sapiens (Human)
Function: Folate-dependent enzyme, that displays both transferase and deaminase activity. Serves to channel one-carbon units from formiminoglutamate to the folate pool.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9YH58}. Golgi apparatus {ECO:0000250|UniProtKB:Q9YH58}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16534631}. Note=More abundantly located around the mother centriole. {ECO:0000269|PubMed:16534631}.
Interaction partners:
- C-1-tetrahydrofolate synthase, cytoplasmic
- Trifunctional purine biosynthetic protein adenosine-3
- Monofunctional C1-tetrahydrofolate synthase, mitochondrial
- 5-formyltetrahydrofolate cyclo-ligase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase
- Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial
- Dynein axonemal light chain 1
- Probable imidazolonepropionase
- Bifunctional purine biosynthesis protein ATIC
- Serine hydroxymethyltransferase, mitochondrial
Sequence:
MSQLVECVPNFSEGKNQEVIDAISGAITQTPGCVLLDVDAGPSTNRTVYTFVGPPECVVEGALNAARVASRLIDMSRHQGEHPRMGALDVCPFIPVRGVSVDECVLCAQAFGQRLAEELDVPVYLYGEAARMDSRRTLPAIRAGEYEALPKKLQQADWAPDFGPSSFVPSWGATATGARKFLIAFNINLLGTKEQAHRIALNLREQGRGKDQPGRLKKVQGIGWYLDEKNLAQVSTNLLDFEVTALHTVYEETCREAQELSLPVVGSQLVGLVPLKALLDAAAFYCEKENLFILEEEQRIRLVVSRLGLDSLCPFSPKERIIEYLVPERGPERGLGSKSLRAFVGEVGARSAAPGGGSVAAAAAAMGAALGSMVGLMTYGRRQFQSLDTTMRRLIPPFREASAKLTTLVDADAEAFTAYLEAMRLPKNTPEEKDRRTAALQEGLRRAVSVPLTLAETVASLWPALQELARCGNLACRSDLQVAAKALEMGVFGAYFNVLINLRDITDEAFKDQIHHRVSSLLQEAKTQAALVLDCLETRQE
Protein: Nucleoprotein (Nucleocapsid protein) (NC) (Protein N) (P15130)
Organism: Human coronavirus 229E (HCoV-229E)
Function: Packages the positive strand viral genome RNA into a helical ribonucleocapsid (RNP) and plays a fundamental role during virion assembly through its interactions with the viral genome and membrane protein M. Plays an important role in enhancing the efficiency of subgenomic viral RNA transcription as well as viral replication.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04095}. Host endoplasmic reticulum-Golgi intermediate compartment {ECO:0000255|HAMAP-Rule:MF_04095}. Host Golgi apparatus {ECO:0000255|HAMAP-Rule:MF_04095}. Note=Located inside the virion, complexed with the viral RNA. Probably associates with ER-derived membranes where it participates in viral RNA synthesis and virus budding. {ECO:0000255|HAMAP-Rule:MF_04095}.
Interaction partners:
Sequence:
MATVKWADASEPQRGRQGRIPYSLYSPLLVDSEQPWKVIPRNLVPINKKDKNKLIGYWNVQKRFRTRKGKRVDLSPKLHFYYLGTGPHKDAKFRERVEGVVWVAVDGAKTEPTGYGVRRKNSEPEIPHFNQKLPNGVTVVEEPDSRAPSRSQSRSQSRGRGESKPQSRNPSSDRNHNSQDDIMKAVAAALKSLGFDKPQEKDKKSAKTGTPKPSRNQSPASSQTSAKSLARSQSSETKEQKHEMQKPRWKRQPNDDVTSNVTQCFGPRDLDHNFGSAGVVANGVKAKGYPQFAELVPSTAAMLFDSHIVSKESGNTVVLTFTTRVTVPKDHPHLGKFLEELNAFTREMQQHPLLNPSALEFNPSQTSPATAEPVRDEVSIETDIIDEVN
Protein: Transcription factor sox-3 (Q20201)
Organism: Caenorhabditis elegans
Function: Probable transcription factor. Involved in the terminal differentiation of some neuronal cell types. Dispensable for neuronal fate commitment during embryogenesis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267}.
Interaction partners:
- Transcription initiation factor TFIID subunit 8
- Paired domain-containing protein
- Putative iroquois-class homeodomain protein irx-1
Sequence:
MTDLSCLYPSLLCTEAAKTSYDEDTTSVSSGLSPPGSPVDLQNSLDHVKRPMNAFMVWSRGQRRKMAQDNPKMHNSEISKRLGAEWKQLSEQEKRPFIDEAKRLRALHMKEHPDYKYRPRRKPKSSNLKQQPRLNIAMPTIPPQSLFNYSTAFDSLKTHDLSQYYSSFFQSPVLSGSTYAPYNMMAAYARQAAAVAAASQVSASTTPTAPAT
Protein: Peroxisome proliferator-activated receptor gamma (PPAR-gamma) (Nuclear receptor subfamily 1 group C member 3) (E9PFX5)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU364110}. Nucleus {ECO:0000256|RuleBase:RU364110}.
Interaction partners:
Sequence:
MVDTEMPFWPTNFGISSVDLSVMEDHSHSFDIKPFTTVDFSSISTPHYEDIPFTRTDPVVADYKYDLKLQEYQSAIKVEPASPPYYSEKTQLYNKPHEEPSNSLMAIECRVCGDKASGFHYGVHACEGCKGFFRRTIRLKLIYDRCDLNCRIHKKSRNKCQYCRFQKCLAVGMSHNAIRFGRMPQAEKEKLLAEISSDIDQLNPESADLRALAKHLYDSYIKSFPLTKAKARAILTGKTTDKSTAQVC
Protein: Probable beta-D-xylosidase 7 (AtBXL7) (EC 3.2.1.-) (Q9SGZ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted, extracellular space, extracellular matrix {ECO:0000250}.
Interaction partners:
- At3g14430
- Uncharacterized protein At2g41810
- Probable E3 ubiquitin-protein ligase RHY1A
- Histone-lysine N-methyltransferase SETD1B-like protein
- Berberine bridge enzyme-like 11
Sequence:
MAKQLLLLLLLFIVHGVESAPPPHSCDPSNPTTKLYQFCRTDLPIGKRARDLVSRLTIDEKISQLVNTAPGIPRLGVPAYEWWSEALHGVAYAGPGIRFNGTVKAATSFPQVILTAASFDSYEWFRIAQVIGKEARGVYNAGQANGMTFWAPNINIFRDPRWGRGQETPGEDPMMTGTYAVAYVRGLQGDSFDGRKTLSNHLQASACCKHFTAYDLDRWKGITRYVFNAQVSLADLAETYQPPFKKCIEEGRASGIMCAYNRVNGIPSCADPNLLTRTARGQWAFRGYITSDCDAVSIIYDAQGYAKSPEDAVADVLKAGMDVNCGSYLQKHTKSALQQKKVSETDIDRALLNLFSVRIRLGLFNGDPTKLPYGNISPNEVCSPAHQALALDAARNGIVLLKNNLKLLPFSKRSVSSLAVIGPNAHVVKTLLGNYAGPPCKTVTPLDALRSYVKNAVYHQGCDSVACSNAAIDQAVAIAKNADHVVLIMGLDQTQEKEDFDRVDLSLPGKQQELITSVANAAKKPVVLVLICGGPVDISFAANNNKIGSIIWAGYPGEAGGIAISEIIFGDHNPGGRLPVTWYPQSFVNIQMTDMRMRSATGYPGRTYKFYKGPKVYEFGHGLSYSAYSYRFKTLAETNLYLNQSKAQTNSDSVRYTLVSEMGKEGCDVAKTKVTVEVENQGEMAGKHPVLMFARHERGGEDGKRAEKQLVGFKSIVLSNGEKAEMEFEIGLCEHLSRANEFGVMVLEEGKYFLTVGDSELPLIVNV
Protein: Ubiquitin carboxyl-terminal hydrolase (EC 3.4.19.12) (Q5ZJE0)
Organism: Gallus gallus (Chicken)
Interaction partners:
Sequence:
MPGVLPSDGSAPPRGSPSRKNRLSLKLFQKKEAKRALDFTEPPENEQKGAELRGAEIDQVVPAAQPPSLVSCEKKDNMLPFVGLNNLGNTCYLNSVLQVLYFCPGFKTGVKHLYNIISKKKESLKDEGELKAEKGNCKEDPLASYELICSLHSLILSVEQLQASFLLNPEKYTDELATQPRRLLNTLRELNPMYEGYLQHDAQEVLQCILGNIQETCQLLKKEELNKLPLEEPKAKVEEKINPNSESNGTGNSAEEEEENAPGSHVGEVAEDKLPKGNGKRKSDAEGGNAKKKSKVSKEQIAAEENQRQTRSKRKATGEKLENQSDAIAKCSTENESAKPTQKKSRLKLNWLKSSCKQPSILSKFYSLGRLSTNLGSKDPEYDDCELEESSAKCENGNDIKEEDCHEPASPVESHTEKGTEKEPKNEGTELAVFELVEKLFQGQLVLRTRCLECECFTERREDFQDISVPVQEDELSKTEESSEISPEPKTEMKTLKWAISQFASVERIVGEDKYFCENCHHYTEAERSLLFDKMPEVITIHLKCFAASGLEFDCYGGLSKINTPLLTPLKLSLEEWSTKPTNDTYGLFAVVMHSGITISSGHYTASVKITDLNSLELDKGNFITAQMCETIKPEPLNEEEARTAAEDYDDGEVSFRVNGNAQPGKVLNKKNMEAVGLLGGQKSKSDCDLYSKPASSEKVLNIVTENRNPESAPANGSVECSTERGDQNGVAFSGLENKALYVLQSLKEYEGKWLLFDDSEVKVTEEKDFLNSLSPTSSSTSTPYLLFYKKIVE