wanglab/gogpt-training-data huggingface dataset:
Protein: DNA polymerase gamma (EC 2.7.7.7) (Mitochondrial DNA polymerase catalytic subunit) (Q12704)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in the replication of mitochondrial DNA.
Subcellular location: Mitochondrion.
Interaction partners:
- Putative glycine--tRNA ligase
- Single-stranded DNA-binding protein rim1, mitochondrial
- Triosephosphate isomerase
- DNA-directed RNA polymerase, mitochondrial
- Probable peptide methionine sulfoxide reductase
- ATP-dependent DNA helicase pfh1
- DNA primase small subunit
Sequence:
MFYKACPSTLTCSKWIHSIIKTKKFLYCRHYSSKSFIDNAPLRINPVGVQYLSPALQNQVFPQQNTQISQLHLDLAKFHLAKHQLLNKETIKLPSFNFRLPPLQGKTISEHFYNIGLEFAEPHLSKAIKFSKIDTPVQPKTWKRQPGWTKYAKDGSISCVPYPDSDCMVFDVEVLYKVSPFAVVATAVSEDAWYCWLSPWLLGKSENDRQLIPSNPKGALFVGHNVSFDRQRIREEYNIKSSRNVFLDTMSLHVATHGMCSRQKPTWFKARKAYIRSQSTETSEDDDSSSFDDDYQNYLKQEPWLAHSSVNSLKDVAKFHCNITLDKSKRDDFASLEKEPILQKLNELITYCAHDTYSTHQVFKKVFPQFLEVCPHPATFSAMLSLGSVFLPVNHSWTRYINGVEEQYQQMIQLVDQKLSQYAEKAKDLINTKDTVLKDPWLRQLDWTPCNLYRKLKKATQEVPVVPKWYKKAYCKTEKRAVITAKSRLAPILLRLKWKKHPLAWSDTYGWVFSVERTSKDEIEMLLDQGLVPCSREEDTKLDYNNYIFFKVPHKDGPEARCGSPLSKSYQRYFEEGILQSDYEVAKKALEMSASCSYWSSARDRIRSQMVVWDKDAELGVPSSVDGFGIILPCIIPMGTVTRRAVENTWLTASNSKKNRLGSELKAMIRAPDGYTFVGADVDSEELWIVALMGDSQFRLHGATALGMMTLEGKKSEGTDLHSKTAAILGVSRDSAKVFNYGRLYGAGLKHTTLLLMQMNPTLKTAEAKELAKKLYASTKGVKSKMSKRLQEMGLPKLTFWSQGTESFVFNKLEAMAQLPSPRTPVLDAGITQALSSKNLSKNSFMTSRVNWAIQSSAVDYLHLLLVSMNHLIKKYYLEARLSLTVHDEVRYLSSDKDKYRVAFALQVANLWTRAFFCQRLGINELPQSVAFFSSVDIDHVLRKDVKMDCVTPSNKVPIPPGEELTIESVLEKLEQSGQSLEPLEQIQCFVDVKATTSAEITEEDKKNIAYLKAQAFY
Protein: Delta-theraphotoxin-Hm1b (Delta-TRTX-Hm1b) (P0DOC5)
Organism: Heteroscodra maculata (Togo starburst tarantula) (Togo starburst baboon spider)
Function: Gating-modifier toxin that potently and selectively acts on Nav1.1/SCN1A and Nav1.3/SCN3A. It enhances hNav1.1/SCN1A currents and delays fast inactivation of the channel (EC(50)=11.6 nM), leading to a sustained current. Similar effects are observed at Nav1.3/SCN3A (EC(50)=11.8 nM), but with less sustained currents. When tested on Nav1.2/SCN2A, the native toxin decreases the peak current by 50% at saturating concentration, whereas the recombinant toxin only shows a weak decrease of peak current. The native toxin specifically activates the voltage-gated sodium channel Nav1.1/SCN1A in somatosensory neurons to elicit acute pain and mechanical allodynia. When tested on Nav1.1/SCN1A, the toxin induces a hyperpolarising shift of the voltage-dependence of steady-state activation, and induces a depolarizing shift in the voltage dependence of inactivation. In addition, it does not modify the recovery from fast inactivation in Nav1.1/SCN1A. The toxin hydrophobic face probably interacts with the domain IV voltage-sensor of Nav1.1/SCN1A and Nav1.3/SCN3A and may trap the voltage-sensing S4 helix in a partially activated state. In vivo, intracerebroventricular injection into mice elicits convulsions, spasms, tremors and rapid death (By similarity). When injected into mouse hindpaw, the toxin elicits an immediate and robust response to pain. However, intraplantar injection of toxin does not cause neurogenic inflammation or alter sensitivity to heat, indicative of a modality-specific effect on mechanosensitive neurons.
Subcellular location: Secreted {ECO:0000269|PubMed:27281198}.
Interaction partners:
Sequence:
ECRYLFGGCKTTADCCKHLGCRTDLYYCAWDGTF
Protein: RAD51/dmc1 protein, putative (Q38E34)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA repair protein RAD51 homolog
- DNA repair protein, putative
- HORMA domain-containing protein
- BRCA2 OB1 domain-containing protein
- Mnd1 HTH domain-containing protein
- DNA 3'-5' helicase
- Proliferating cell nuclear antigen
- Exonuclease, putative
- non-specific serine/threonine protein kinase
- Endo/exonuclease Mre11
Sequence:
MQHVGTRSGKSEAKDAAVSTDNSTHEDAAHTIMEIDRLTEQGVAAADVAKLRQAGIFTVTGIHMQCRKDLVLIKGLSDAKVDKIIEAARKLSDCGFSVGTAYLQQRGRVTRVTTGSTALDQLLGGGIESMSITEAFGEFRTGKTQIAHTLCVTCQLPISMGGGNGKAIYVDTEATFRPERIKPIAERFGLDVEAVLGNILVARAYTHEHQMHLLSMVAAKMVEDQFSLLVVDSVTALFRVDFSGRGELAERQQKLAKMLSNMIKLAEEYNVAVYITNQVVADPGGASMFVADPKKPIGGHILAHASTTRLSLRKGRGDQRVCKIYDSPSLPEVECVFSISEQGIVDARE
Protein: Nardilysin (EC 3.4.24.61) (N-arginine dibasic convertase) (NRD convertase) (NRD-C) (Nardilysin convertase) (Q8BHG1)
Organism: Mus musculus (Mouse)
Function: Cleaves peptide substrates on the N-terminus of arginine residues in dibasic pairs. Is a critical activator of BACE1- and ADAM17-mediated pro-neuregulin ectodomain shedding, involved in the positive regulation of axonal maturation and myelination. Required for proper functioning of 2-oxoglutarate dehydrogenase (OGDH).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:O43847}. Cell projection, dendrite {ECO:0000269|PubMed:19935654}.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Probable helicase senataxin
- Tripeptidyl-peptidase 2
- Thimet oligopeptidase
Sequence:
MLRRVAVAAVCVTGRKLRCEAGRELTALGRIEARGLCEESSKPFPTLTMPGRNKAKSTCSCPDLQPNGQDLGESGRLARLGADESEEEGRSFSNVGDPEIIKSPSDPKQYRYIKLQNGLQALLISDLSNVEGKTGNATDEEEEEEEEEEEEDDDDDDDDDDDDEDSGAEIQDDDEEGFDDEEEFDDDDDDEHDDDDLENEENELEELEERVEARKKTTEKQSAAALCVGVGSFADPDDLPGLAHFLEHMVFMGSLKYPDENGFDAFLKKHGGSDNASTDCERTVFQFDVQRKYFKEALDRWAQFFIHPLMIRDAIDREVEAVDSEYQLARPSDANRKEMLFGSLARPGHPMGKFFWGNAETLKHEPKKNNIDTHARLREFWMRYYSAHYMTLVVQSKETLDTLEKWVTEIFSQIPNNGLPKPNFSHLTDPFDTPAFNKLYRVVPIRKIHALTITWALPPQQQHYRVKPLHYISWLVGHEGKGSILSYLRKKCWALALFGGNGETGFEQNSTYSVFSISITLTDEGYEHFYEVAHTVFQYLKMLQKLGPEKRVFEEIQKIEDNEFHYQEQTDPVEYVENMCENMQLYPRQDFLTGDQLLFEYKPEVIAEALNQLVPQKANLVLLSGANEGRCDLKEKWFGTQYSIEDIENSWTELWKSNFDLNPDLHLPAENKYIATDFTLKAFDCPETEYPAKIVNTAQGCLWYKKDNKFKIPKAYIRFHLISPLIQKSAANVVLFDIFVNILTHNLAEPAYEADVAQLEYKLVAGEHGLIIRVKGFNHKLPLLFQLIIDYLTEFSSTPAVFTMITEQLKKTYFNILIKPETLAKDVRLLILEYSRWSMIDKYQALMDGLSLDSLLNFVKDFKSQLFVEGLVQGNVTSTESMDFLKYVVDKLNFAPLEREMPVQFQVVELPSGHHLCKVRALNKGDANSEVTVYYQSGTRSLREYTLMELLVMHMEEPCFDFLRTKQTLGYHVYPTCRNTSGILGFSVTVGTQATKYNSETVDKKIEEFLSSFEEKIENLTEDAFNTQVTALIKLKECEDTHLGEEVDRNWNEVVTQQYLFDRLAHEIEALKSFSKSDLVSWFKAHRGPGSKMLSVHVVGYGKYELEEDGAPFGEDSNSREGMQLTYLPPSPVLAESTTPITDIRAFTATLSLFPYHKIVK
Protein: Serotonin N-acetyltransferase (Serotonin acetylase) (EC 2.3.1.87) (Aralkylamine N-acetyltransferase) (AA-NAT) (Q16613)
Organism: Homo sapiens (Human)
Function: Controls the night/day rhythm of melatonin production in the pineal gland. Catalyzes the N-acetylation of serotonin into N-acetylserotonin, the penultimate step in the synthesis of melatonin.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11313340}.
Interaction partners:
- Acetylserotonin O-methyltransferase
- 14-3-3 protein zeta/delta
- Aromatic-L-amino-acid decarboxylase
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Indoleamine 2,3-dioxygenase 2
- Indoleamine 2,3-dioxygenase 1
- Indolethylamine N-methyltransferase
- Melanopsin
- Glycine N-acyltransferase-like protein 1
Sequence:
MSTQSTHPLKPEAPRLPPGIPESPSCQRRHTLPASEFRCLTPEDAVSAFEIEREAFISVLGVCPLYLDEIRHFLTLCPELSLGWFEEGCLVAFIIGSLWDKERLMQESLTLHRSGGHIAHLHVLAVHRAFRQQGRGPILLWRYLHHLGSQPAVRRAALMCEDALVPFYERFSFHAVGPCAITVGSLTFMELHCSLRGHPFLRRNSGC
Protein: Carboxysome shell protein CcmP (Carbon dioxide concentrating mechanism protein CcmP) (Q31QW7)
Organism: Synechococcus elongatus (strain ATCC 33912 / PCC 7942 / FACHB-805) (Anacystis nidulans R2)
Function: Probably part of the carboxysome shell, a polyhedral inclusion where RuBisCO (ribulose bisphosphate carboxylase, rbcL-rbcS) is sequestered. It is thought that this protein controls transport of RuBisCO reactants in and out of the carboxysome; residual densities in the 4 X-ray structures suggest that differing compounds bind in interior pockets, depending on the open or closed state of the pore.
Subcellular location: Carboxysome {ECO:0000269|PubMed:23572529}. Note=This cyanobacterium makes beta-type carboxysomes. {ECO:0000269|PubMed:23572529}.
Interaction partners:
- Carboxysome shell protein CcmK4
- Carboxysome shell protein CcmK3
- Carboxysome shell protein CcmK2
- Carboxysome assembly protein CcmO
- Carboxysome shell vertex protein CcmL
- Pentapeptide repeat
- Carboxysome assembly protein CcmN
- RuBisCO chaperone RbcX
Sequence:
MGVELRSYVYLDNLQRQHASYIGTVATGFLTLPGDASVWIEISPGIEINRMMDIALKAAVVRPGVQFIERLYGLMEVHASNQGEVREAGRAVLSALGLTERDRLKPKIVSSQIIRNIDAHQAQLINRQRRGQMLLAGETLYVLEVQPAAYAALAANEAEKAALINILQVSAIGSFGRLFLGGEERDIIAGSRAAVAALENLSGREHPGDRSRE
Protein: Protocadherin beta-13 (PCDH-beta-13) (Q9Y5F0)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MEASGKLICRQRQVLFSFLLLGLSLAGAAEPRSYSVVEETEGSSFVTNLAKDLGLEQREFSRRGVRVVSRGNKLHLQLNQETADLLLNEKLDREDLCGHTEPCVLRFQVLLESPFEFFQAELQVIDINDHSPVFLDKQMLVKVSESSPPGTTFPLKNAEDLDVGQNNIENYIISPNSYFRVLTRKRSDGRKYPELVLDKALDREEEAELRLTLTALDGGSPPRSGTAQVYIEVLDVNDNAPEFEQPFYRVQISEDSPVGFLVVKVSATDVDTGVNGEISYSLFQASEEIGKTFKINPLTGEIELKKQLDFEKLQSYEVNIEARDAGTFSGKCTVLIQVIDVNDHAPEVTMSAFTSPIPENAPETVVALFSVSDLDSGENGKISCSIQEDLPFLLKSAENFYTLLTERPLDRESRAEYNITITVTDLGTPMLITQLNMTVLIADVNDNAPAFTQTSYTLFVRENNSPALHIRSVSATDRDSGTNAQVTYSLLPPQDPHLPLTSLVSINADNGHLFALRSLDYEALQGFQFRVGASDHGSPALSSEALVRVVVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATELGLFGVWAHNGEVRTARLLSERDAAKHRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLPLPEAAPTQAQADLLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCLVPEGPLPGHLVDMSGTRTLSQSYQYEVCLAGGSGTNEFKFLKPIIPNFPPQCPGKEIQGNSTFPNNFGFNIQ
Protein: UBX domain-containing protein (Q38CY2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Ubiquitin fusion degradation protein, putative
- MPN domain-containing protein
- Guanine nucleotide-binding protein subunit beta-like protein
- Ubiquitin fusion degradation protein 2, putative
- UBX domain-containing protein
- Cell division cycle protein, putative
- ATPase, putative
- Valosin-containing protein homolog, putative
- AAA ATPase, putative
- AAA ATPase, putative
Sequence:
MPDVAEHIKRQCGLQSTVVSGRFKDALDEAQCRPAYLLIYLHCPTHEDTPAFLSEVLPNPPLRELIESRFVLYAASVMEPEGYRLSLEFEATTFPFLAVTLRRETVLTVKGLCCARDLVKYFQAMFDRFDGVLAEEIHLRHEREERMRARTDDERHIAEMQAVDRKRIEEFEKKKRDKVMRLLLESEEMRRKLEEEEEECDRRQHEEMFIQTRSDIARTEAEMRLAPEPPADADVSTTTFISFRSLSGKQSKRRFYLSDRLSNLREYGKTLEDYDGCNFQLVVGHPPRALETESDKTIGDEPTLFPRAVVMMRRL
Protein: Probable mitochondrial Rho GTPase gemA (Miro) (EC 3.6.5.-) (Q55G45)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Mitochondrial GTPase involved in mitochondrial trafficking. Probably involved in control of anterograde transport of mitochondria and their subcellular distribution (By similarity).
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}.
Interaction partners:
- Translocase of outer mitochondrial membrane
- SMP-LTD domain-containing protein
- Rac guanine nucleotide exchange factor B
- Uncharacterized protein
- Mitofilin
- Uncharacterized protein
- Kinesin-related protein 5
- Uncharacterized transmembrane protein DDB_G0283573
- Bacterial surface antigen
- Glutathione S-transferase domain-containing protein
Sequence:
MKNNIKVILIGDEQVGKSTIINSFISESFSEITQKTLPEVTIPAEFNNEICSTRIIDTFDDGKNLKNQMNMEIRTADAIVIVYSVDRFDTFMSIRMKWIPLINQLRGSNKSPIIIVGNKLDLVDDKHENNKVQIEETIQYFRSTYSNTIQWLECSAKTMENLPELLYASQTSVFFPERILYNREENKMTEGCERALKRIFKLCDHDNDGSLSEEEINYFQTKCGHETMTSEEIQNIQQFVLSKIPDGVNSNGFTEKGFLYMNLLFLLRGPCQHTWTSLRSFNYDDDLVLLESYVHPTLQVPPNHNTILSSMGNEFFKSLFEKYDSDSDGVLSSFDLVSLFSTTPKIPWEIGFEKHFNTDKDSNLTLSGFLSLWNLQTYENYKVTLEYLAYFGSQTENNNIDMISILNSRELDIKSNQFTRNIVNCYVFGAEAVGKTTFLNTFIGKSFSTLYNATNGNDNFKVCGHLLKNKYLILSEYVGEKIPTAELKSKCDLVCLLYDCNSEQSFKFIENIYNQLKQQQLNIPIVFIRTKNNNNNNNNNNNNNNNNNNNNLNNNNNNINNNNNNNNNNTTTTNANVSTSKIIDSFFKSHKNYSPKDFSISRSNSIYHEMMETIVNSSFNDNSNGSNGSNNSNILTYLVIAAGVAGVGLLLSKYLAKK
Protein: Tubulin alpha-1B chain (EC 3.6.5.-) (Alpha-tubulin 2) (Tubulin alpha-2 chain) [Cleaved into: Detyrosinated tubulin alpha-1B chain] (Q6P9V9)
Organism: Rattus norvegicus (Rat)
Function: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers are in GDP-bound state, owing to GTPase activity of alpha-tubulin.
Subcellular location: Cytoplasm, cytoskeleton.
Interaction partners:
- Tubulin alpha-1A chain
- Tubulin beta-5 chain
- Tubulin beta-3 chain
- Small vasohibin-binding protein
- Tubulin beta-4B chain
- Tubulin beta-2A chain
- Tubulin beta-2B chain
- Microtubule-associated protein tau
- Tubulin beta chain
- Tubulin beta chain
Sequence:
MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTGLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVAEITNACFEPANQMVKCDPRHGKYMACCLLYRGDVVPKDVNAAIATIKTKRSIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY
Protein: Peroxisomal protein 2 (O74758)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probably involved in peroxisome formation or maintenance as well as in amino acid metabolism.
Subcellular location: Peroxisome matrix {ECO:0000250|UniProtKB:P47148}. Cytoplasm, cytosol {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
Sequence:
MTHNTMLQRFNGLLEPTHLYIVSVVAYSACNRPDKISGIAKEAMEHVGPSIYPKLREALVKSSPLVGFPRTINSLREMTTNIPPPFPDEFARAADADIDTGKRGKIYFEKTYGKVTQRVLRSMQSSSLDLANIALDYAYGKVLSFNEVVSPLETSLMIIAALVPQDVNPQLRGHLKGALNHGATKEQVMSARNIALEISKECGIQFKGDIETL
Protein: Deoxyuridine 5'-triphosphate nucleotidohydrolase, mitochondrial (dUTPase) (EC 3.6.1.23) (dUTP pyrophosphatase) (Q54BW5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: This enzyme is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:31910901}.
Interaction partners:
- Flavin-dependent thymidylate synthase
- Thymidine kinase 1
- Thymidylate kinase
- dCTP deaminase
- dCTP deaminase
- Nucleoside diphosphate kinase, cytosolic
- Probable nucleoside diphosphate kinase DDB_G0292928
- Nucleoside diphosphate kinase, mitochondrial
- Ribonucleoside-diphosphate reductase large subunit
- Inosine triphosphate pyrophosphatase
Sequence:
MPIEQKYFSLFSNLFKRLTTNNNNNNYLKMAPPNFETFKVKKLSDKAIIPQRGSKGAAGYDLSSAHELVVPAHGKALAMTDLQIAIPDGTYGRIAPRSGLAWKNFIDCGAGVIDSDYRGNVGVVLFNHSDVDFKVAVGDRVAQLIFERIVTPEPLEVDEIDETQRGAGGFGSTGVKVQN
Protein: Paired immunoglobulin-like type 2 receptor alpha (Cell surface receptor FDF03) (Inhibitory receptor PILR-alpha) (Q2YFS3)
Organism: Mus musculus (Mouse)
Function: Paired receptors consist of highly related activating and inhibitory receptors and are widely involved in the regulation of the immune system. Receptor for CD99 and PIANP.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- Paired immunoglobulin-like type 2 receptor beta
- Tyrosine-protein phosphatase non-receptor type 11
- Paired immunoglobulin-like type 2 receptor beta-2
- Nectin-1
Sequence:
MALLISLPGGTPAMAQILLLLSSACLHAGNSERSNRKNGFGVNQPESCSGVQGGSIDIPFSFYFPWKLAKDPQMSIAWRWKDFHGEFIYNSSLPFIHEHFKGRLILNWTQGQTSGVLRILNLKESDQTRYFGRVFLQTTEGIQFWQSIPGTQLNVTNATCTPTTLPSTTAATSAHTQNDITEVKSANIGGLDLQTTVGLATAAAVFLVGVLGLIVFLWWKRRRQGQKTKAEIPAREPLETSEKHESVGHEGQCMDPKENPKDNNIVYASISLSSPTSPGTAPNLPVHGNPQEETVYSIVKAK
Protein: Diacylglycerol O-acyltransferase 3 (AtDGAT3) (EC 2.3.1.20) (Q9C5W0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in triacylglycerol (TAG) biosynthesis. Catalyzes the acylation of the sn-3 hydroxy group of sn-1,2-diacylglycerol using acyl-CoA. May preferentially use linolenoyl-CoA as substrate and to a lesser extent linoleoyl-CoA. May contribute to the active recycling of linoleate and linolenate into TAG when seed oil breakdown is blocked.
Interaction partners:
- Phospholipid:diacylglycerol acyltransferase 1
- Diacylglycerol O-acyltransferase 1
- Diacylglycerol O-acyltransferase 2
- Putative phospholipid:diacylglycerol acyltransferase 2
- Triacylglycerol lipase SDP1
- Phosphatidate phosphatase PAH1
- Phosphatidate phosphatase PAH2
- Wax ester synthase/diacylglycerol acyltransferase 1
- Sulfoquinovosyl transferase SQD2
- Monogalactosyldiacylglycerol synthase 1, chloroplastic
Sequence:
MEVSGVVLRQIPCVSSGSVAGLRLVSEFSGNTRTVGFRTRRFRGIVCNNEFADKGHVNYYIEPTRCGEEKEKVKVMEKEKKALKKKAKVLKSLSKNLDMFSSIGFGLDPEAGLVGEIQTKTISEATEILVKQLEQLKAEEKILKKQRKEEKAKAKAMKKMTEMDSESSSSSESSDSDCDKGKVVDMSSLRNKAKPVLEPLQPEATVATLPRIQEDAISCKNTSEALQIALQTSTIFPSMANPGQTLKTVEAVSVVGLPLNRVEVCMGGKCKRSGGALLLDEFQRAMTGFEGSAVACKCMGKCRDGPNVRVVKETDAVMTDSVRTPSKTLCVGVGLQDVETIVTSFFDEECSREGLGSVSY
Protein: E3 ubiquitin-protein ligase SMURF2 (hSMURF2) (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase SMURF2) (SMAD ubiquitination regulatory factor 2) (SMAD-specific E3 ubiquitin-protein ligase 2) (Q9HAU4)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling. In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1. Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation. SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation. Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation.
Subcellular location: Nucleus {ECO:0000269|PubMed:12717440}. Cytoplasm {ECO:0000269|PubMed:12717440}. Cell membrane {ECO:0000269|PubMed:12717440}. Membrane raft {ECO:0000269|PubMed:12717440}. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts.
Interaction partners:
- Mothers against decapentaplegic homolog 7
- TGF-beta receptor type-1
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 6
- Mothers against decapentaplegic homolog 3
- Polyubiquitin-C
- Ubiquitin-ribosomal protein eS31 fusion protein
- E3 ubiquitin-protein ligase SMURF1
- Ubiquitin carboxyl-terminal hydrolase 15
- RING finger protein 11
Sequence:
MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPISGTNGATCGQSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNNRTTQFTDPRLSANLHLVLNRQNQLKDQQQQQVVSLCPDDTECLTVPRYKRDLVQKLKILRQELSQQQPQAGHCRIEVSREEIFEESYRQVMKMRPKDLWKRLMIKFRGEEGLDYGGVAREWLYLLSHEMLNPYYGLFQYSRDDIYTLQINPDSAVNPEHLSYFHFVGRIMGMAVFHGHYIDGGFTLPFYKQLLGKSITLDDMELVDPDLHNSLVWILENDITGVLDHTFCVEHNAYGEIIQHELKPNGKSIPVNEENKKEYVRLYVNWRFLRGIEAQFLALQKGFNEVIPQHLLKTFDEKELELIICGLGKIDVNDWKVNTRLKHCTPDSNIVKWFWKAVEFFDEERRARLLQFVTGSSRVPLQGFKALQGAAGPRLFTIHQIDACTNNLPKAHTCFNRIDIPPYESYEKLYEKLLTAIEETCGFAVE
Protein: Histone transcription regulator 3 (P47171)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: HIR1, HIR2 and HIR3 are repressors of histone gene transcription. They are required for the periodic repression of three of the four histone gene loci during cell cycle as well as for autogenous regulation of the HTA1-HTB1 locus by H2A and H2B. Also has a role in nucleosome assembly.
Subcellular location: Nucleus {ECO:0000269|PubMed:9671488}. Chromosome {ECO:0000269|PubMed:19683497}. Note=Localizes to the promoter region of histones HTA1-HTB1. {ECO:0000269|PubMed:19683497}.
Interaction partners:
- Protein HIR2
- Histone promoter control protein 2
- Protein HIR1
- Histone chaperone ASF1
- Chromatin assembly factor 1 subunit B
- Histone chaperone RTT106
- Histone H3
- Histone-binding protein MSI1
- Protein SPT10
- Histone H2A.1
Sequence:
MSMFNALNSNIEGEQYEAEEHSRELQIEQSFNILQDALIDLKNKDFEKSDSKFQELFQIDVVKPDRWGMYRNSSPTLDNLRYLCYRNRGMYYHLYLENNYERLNSQELVNCILKAVENLVESIQHSDADFAVTDLLARIFKSFNSVKLERLISEYEFTKQENLSLLLGRHRKFLLNDLTLMMNNYVELTNKLLVPNLSDNTIFERYHLEKYKDIKPEPLAFGPILSRISEMKKQDEEIMKKLDVFNVTLNEESWDEVAKALKNLLPSVKTSSLIGRNMDPYNEIEEPIEAVKFELSEAINNTPSLDRESERQEEEQDNESVRADDKSGNLAPSDIQTNEEARPNKRTDEHIDSTKPLQRSSKRFKEREQENSKELVMDVHKRFFGEFNTLLSYIHILPFCDFDTFASKFIIGSSDKQPEKFIPYTDLYECLKSWSSRYTDIFNQNDYLSSGSNENEELFQLNALLKSNAFDDKESFPRYLNDLDSDHIRSFISEVNAGNLHFHQVRLKLLFKLLGTYDEGNGRRLIIDYLWESQLLKIVLWFVFGIESNIFALINKNKRQCKYLALSIYELLVNHLGNIVEEITNKRIQGHKSADLKSQRNKVEKRIRSWHTLLEQIADEKDKELYVHFQWTHYCFLQYTCDIVDSRLSETLTSLENTIKDSDSSLDIAYPNYRHIPALNLNTVQSQKRKIRIIQNITVEDISEDTNSDTHSENHLETLEKVLLHILHPSTNHSNIDEEMVSFIFNSPFLLKIRLWGVLFSSYVKKSSIQDVQRIYFHVLDFMKGALTSPVYKESNPHGRHQMLLTVLTAIGYLSSQLTAILNSNRWESSDFVLEDYMFEKLLQTFFFFYTVLFYESSAVNDVSNKSFFKRASKSSGKMKDIMIDLATLILYYYDLQAKLRTPAEQGIETTELIWSLHTLFGHFHFCDASNGKFLDLAEKLLCQFINNDSFLQLKQILWCRYHYAIASDNFSPDLHDTKAVEMEKIHSLPLGTYLIKLQYQNKNPYLSSSKTTLKQIMDNIIEKIGDPSTLDNHIISRNSFLLNEYLSRPITADLLKHTFSGATSLYLTSPNDELQQGMTAGLFYVSSLQSLGLYKMRKKSMQARPSELDSIIRMLKNDIIYNTNRFESWILLGKCYSYIVEDDLIWTSDKITVPEKKDVIALTQRKAILCYLMAISIYYSKLDRTIDDKKIILEALDDLGSMLISGYYNPMNKLCFSWKSSAENTMRLSETGEVVMEKTKKITTISDFNIEQSIFLCFNRACSLSGDIKSQDDVFVLNWSSFYNLAKFFFKTDGGNNCKLVAKYITQGCQIAYESSPAKDPIIEPHYLLVNACYKWVKRGVIGVNEALTLLSKDNQFFQEQEEFWVNDEGLAWDYQEKFFFDKIIRLLRHLLSVDKKKWQHRPRYRIARILFDDLGDVNGALEEMDSLISAKSINKNLVNIWKPDFERPGKHFIYTYQYLVLYLDLLFAIKDFNTTGLVIKKLRRFGSGTVNVNELLERAINVYTQSAKIKLQLQDKSYVEQILPTLNYQEFLKISEQLNQVFDQGKYPEEISSGLKLAFQLKKGHSGIAFDSVCLGIYFEYLYFPLARQDQSLTDVNDENNPALPSSGSVTSKSTPDPTSKPSAIKKRVTKKEVFDRVRLLVDKIT
Protein: Cell division cycle protein 27 homolog (Q9VS37)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Anaphase-promoting complex subunit 4
- Anaphase-promoting complex subunit 10
- Anaphase-promoting complex subunit 13
- Shattered
- Anaphase-promoting complex subunit 5
- Cell division cycle 16
- Anaphase-promoting complex subunit 2
- Anaphase promoting complex subunit 7, isoform A
- Cyclosome subunit 8
- Cell division cycle protein 20 homolog
Sequence:
MMIQEPVQAAIWHCLNYYDFKDAVFLSERLCSEVESDETIFLLATSYFRSNQVHQAYWLLKEKARRSPQCRFLQAKCAYELKKYAEAESALISTGFADAKNCDELQRDFGDLACFAYQLMAQICMRTERNKLAVSALRRALKLNPFMWHAFADLCLLGQDTDAAAIFQIHSTDVFNTCQGSSVNANAMVLFGAEQQGQQHQERQSLITNLSNVSNYILTTPVDQQQQQINQNQNQHHNSNMVTPINNNNNNNNLNSSISMLRGGLVQNSSMLAMLEDTPMGAPQDPAGQYQQNQQLYDMSSGTPFRKQFKYLSAISPPTPSFGIMPLTSPCTGNDGSFIGNHTPVMNISYSPMPQMLVEVNQEPKMMGKKLKTHVGGLINRKEGSLNKPAVFTQAGNITPRTPNNNNVGNNGNMNVPPNPNAAVRRSSRLFSNSYSVKENNKSPNIANKFVQPRSPPRKAKSRMTKICLNNELIEDKSHHLSEKRKEKVETITSSGANNNSGGRSAAEEAKVLLNNSLNNAQTMAHQLMGLKKQSADGLMALLRGLAEAYQLLSNFQCKAAIKQLETTIPKHHLNSSWVQSLIGLARYEMREYEAAVAIFETIHKTEPCRLDYMEIYSSSLWHLQREVELSALAQDLINQDKTSPVTWCVSGNCFSLQKEHETAIKFFKRAVQVDPDFVYSYTLLGHELVLTEEFDKAMDYFRAAVVRDPRHYNAWYGIGTIYSKQEKYELAEIHYVKALKINPQNSVILVHIGAMQFYMKKKDLSLQTLNTAATLDPKNPLTRFHRGSIYFSLGKYQEALRELEELKEVVPKESVVFYLIGKIHKTLGNMDLALMHFSWATDLDPKGANNQIKDAFDSMAHPSCCPANTTALDVDLEPTSERSDDSTQAQQDGSYDSDY