wanglab/gogpt-training-data huggingface dataset:
Protein: Arylamine N-acetyltransferase (EC 2.3.1.5) (Arylhydroxamate N,O-acetyltransferase) (N-hydroxyarylamine O-acetyltransferase) (EC 2.3.1.118) (P77567)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the acetyl-CoA-dependent N-acetylation of aromatic amines, and, probably, the O-acetylation of N-hydroxyarylamines. In vitro, catalyzes the N-acetylation of various arylamines such as aminobenzoic acid, aminophenol, aminotoluene, phenetidine, anisidine, aniline, isoniazid and 2-amino-fluorene. N-hydroxyarylamine O-acetyltransferase activity has not been assayed directly, however, NhoA activity is required for the mutagenicity of nitroaromatic compounds, suggesting that it also has O-acetyltransferase activity (Probable).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q00267}.
Interaction partners:
- NAD-dependent protein deacylase
Sequence:
MTPILNHYFARINWSGAAAVNIDTLRALHLKHNCTIPFENLDVLLPREIQLDNQSPEEKLVIARRGGYCFEQNGVFERVLRELGFNVRSLLGRVVLSNPPALPPRTHRLLLVELEEEKWIADVGFGGQTLTAPIRLVSDLVQTTPHGEYRLLQEGDDWVLQFNHHQHWQSMYRFDLCEQQQSDYVMGNFWSAHWPQSHFRHHLLMCRHLPDGGKLTLTNFHFTHYENGHAVEQRNLPDVASLYAVMQEQFGLGVDDAKHGFTVDELALVMAAFDTHPEAGK
Protein: MAG2-interacting protein 2 (Q9FIN7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for proper maturation of seed storage proteins. Forms a complex with MAG2, ZW10/MIP1 and MIP3 on the endoplasmic reticulum that may be responsible for efficient transport of seed storage proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:24118572}; Peripheral membrane protein {ECO:0000305|PubMed:24118572}.
Interaction partners:
- RINT1-like protein MAG2
- Centromere/kinetochore protein zw10 homolog
- RINT1-like protein MAG2L
- Syntaxin-81
- At3g24315
- Sec1 family domain-containing protein MIP3
- Homeobox protein LUMINIDEPENDENS
- At3g55600
- Membrane fusion protein Use1
- Gamma-soluble NSF attachment protein
Sequence:
MESPGRKVLYEIRHHASLPYVPRYPPLPQADGTNSKGGLRSLVSIKGVSQLKEKWSEYWNPKKTNKPVSLFISPRGELVAVTSGNHVTILRKDDDYRKPCGNFTSSISGSFTSGVWSEKHDVLGLVDDSETLFFIRANGEEISQVTKRNLKVSAPVLGLMEDDSDLQPSCLCSFSILTSDGRIHHVEISREPSASAFSKHASNSVSKQFPNHVFCFDYHPDLSFLLIVGSVAGISSSGSSGSSCISLWRKCQNLGLELLSTTKFDGVYCENKDDQLAYPKTLISPQGSHVASLDSNGCVHIFQLDKARLTLSCCPSEDSSDSLKPDKSLQSWKESLRNVVDFTWWSDHALAILKRSGNISIFDISRCVIVQEDATIYSMPVVERVQKYEGHIFLLESSTQEAKSALANVDRDASEFHHTSEHSMLWRLISFTEKTIPEMYKILVEKCQYQEALDFSDSHGLDRDEVFKSRWLKSEKGVSDVSTILSKIKDKAFVLSECLDRIGPTEDSMKALLAHGLYLTNHYVFAKSEDQESQQLWEFRLARLRLLQFSERLDTYLGISMGRYSVQDYRKFRSNPINQAAISLAESGRIGALNLLFKRHPYSLVSFMLQILAAIPETVPVETYAHLLPGKSPPTSMAVREEDWVECEKMVKFINNLPENGKNDSLIQTEPIVRRCLGYNWPSSEELAAWYKSRARDIDSTTGLLDNCICLIDIACRKGISELEQFHEDLSYLHQIIYSDEIGGEICFSLSLAGWEHLSDYEKFKIMLEGVKADTVVRRLHEKAIPFMQKRFLGTNNQNVESFLVKWLKEMAAKSDMDLCSKVIDEGCIDLYTVCFFKDDVEAVDCALQCLYLCKVTDKWNVMATMLSKLPKINDKAGEDIQRRLKRAEGHIEAGRLLEFYQVPKPINYFLEVHLDEKGVKQILRLMLSKFVRRQPGRSDNDWACMWRDLRQLQEKAFYFLDLEFVLTEFCRGLLKAGKFSLARNYLKGTGSVALPSEKAESLVINAAKEYFFSAPSLASEEIWKARECLNIFSSSRTVKAEDDIIDAVTVRLPKLGVSLLPVQFKQVKDPMEIIKMAITGDPEAYLHGEELIEVAKLLGLNSSEDISSVKEAIAREAAIAGDMQLAFDLCLVLTKEGHGPIWDLGAAIARSPALEHMDISSRKQLLGFALGHCDDESISELLHAWKDFDLQGQCETLGMLSESNSPEFQKMDGVSCLTDFPQMLDGLSSDQQLDLDRAKDSISCVAKDMPVDDSVDLESLLKENGKLFSFAASHLPWLLKLGRNRKLDKSLVLDSIPGKQFVSIKATALITILSWLAKNGFAPKDELIAMITDSIIEHPVTKEEDVIGCSFLLNLVDASNAVEVIEKQLRIRGNYQEIRSIMSLGMIYSLLHDSGVECTAPIQRRELLQKNFERKQTESLADDMSKIDKLQSTFWKEWKHKLEEKMHDADRSRMLERIIPGVETERFLSHDIEYIKVAVFSLIESVKSEKKLILKDVLKLADTYGLKQSEVILRYLSSILCSEIWTNEDITAEILQVKEEILTFASDTIETISTIVYPAASGLNKQRLAYIYSLLSECYCHLAESKEASLLVQPNSSFAGLSNWYNVLKQECSRVSFIKDLDFKNISELGGLNFDSFNNEVHAHINEMNLEALAKMVETLSGLSMENSSKGLISCQDVYKQYIMNLLDTLESRRDLDFGSAESFQGFLGQLEKTYDHCRVYVRILEPLQAVEILKRHFTLVLPPNGSYMHIPDSSTWQECLILLINFWIRLADEMQEVKSSNPSLVENLTLSPECISSCFTLLIKLVMYDSLSPSQAWAAILVYLRSGLVGDCATEIFNFCRAMVFSGCGFGPISDVFSDMSSRYPTALQDLPHLYLSVLEPILQDLVSGAPETQNLYRLLSSLSNLEGNLEELKRVRLVVWKQLVIFSENLELPSQVRVYSLELMQFISGKNIKGSSSELQSNVMPWDGSAELLSSMQKTEAALNQALPDQADGSSRLTNTLVALKSSQVAVAAISPGLEISPEDLSTVETSVSCFSKLSAAVTTASQAEALLAILEGWEELFEAKNAELLPSNEATDQGNDWGDDDWNDGWETLQESEPVEKVKKECVVSAHPLHSCWLDIFRKYIALSMPENVLQLIDGSLQKPEEVIIEETEAESLTGILARTDPFLALKISLLLPYKQIRSQCLSVVEEQLKQEGIPELSSQSHHEVLLLVIYSGTLSTIISNACYGSVFSFLCYLIGKLSREFQEERITQADNRESNASSESRFISCFGQLMFPCFVSGLVKADQQILAGFLVTKFMHSNPSLSLINVAEASLRRYLDKQLESLEHLEDSFAESSDFETLKNTVSSLRGTSKEVIRSALASLSNCTNSR
Protein: Inner membrane protein YijD (P0AF40)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- HTH-type transcriptional repressor FabR
- Inner membrane protein YqcE
- Uncharacterized protein YhfL
- Uric acid transporter UacT
Sequence:
MKQANQDRGTLLLALVAGLSINGTFAALFSSIVPFSVFPIISLVLTVYCLHQRYLNRTMPVGLPGLAAACFILGVLLYSTVVRAEYPDIGSNFFPAVLSVIMVFWIGAKMRNRKQEVAE
Protein: Homeobox protein unc-4 homolog (Homeobox protein Uncx4.1) (A6NJT0)
Organism: Homo sapiens (Human)
Function: Transcription factor involved in somitogenesis and neurogenesis. Required for the maintenance and differentiation of particular elements of the axial skeleton. May act upstream of PAX9. Plays a role in controlling the development of connections of hypothalamic neurons to pituitary elements, allowing central neurons to reach the peripheral blood circulation and to deliver hormones for control of peripheral functions (By similarity).
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MMDGRLLEHPHAQFGGSLGGVVGFPYPLGHHHVYELAGHQLQSAAAAASVPFSIDGLLGGSCAAAASVVNPTPLLPAACGVGGDGQPFKLSDSGDPDKESPGCKRRRTRTNFTGWQLEELEKAFNESHYPDVFMREALALRLDLVESRVQVWFQNRRAKWRKKENTKKGPGRPAHNSHPTTCSGEPMDPEEIARKELEKMEKKKRKHEKKLLKSQGRHLHSPGGLSLHSAPSSDSDSGGGGLSPEPPEPPPPAAKGPGAHASGAAGTAPAPPGEPPAPGTCDPAFYPSQRSGAGPQPRPGRPADKDAASCGPGAAVAAVERGAAGLPKASPFSVESLLSDSPPRRKAASNAAAAAAAGLDFAPGLPCAPRTLIGKGHFLLYPITQPLGFLVPQAALKGGAGLEPAPKDAPPAPAVPPAPPAQASFGAFSGPGGAPDSAFARRSPDAVASPGAPAPAPAPFRDLASAAATEGGGGDCADAGTAGPAPPPPAPSPRPGPRPPSPAEEPATCGVPEPGAAAGPSPPEGEELDMD
Protein: piRNA biogenesis protein EXD1 (Exonuclease 3'-5' domain-containing protein 1) (Exonuclease 3'-5' domain-like-containing protein 1) (Inactive exonuclease EXD1) (mExd1) (Q8CDF7)
Organism: Mus musculus (Mouse)
Function: RNA-binding component of the PET complex, a multiprotein complex required for the processing of piRNAs during spermatogenesis. The piRNA metabolic process mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and governs the methylation and subsequent repression of transposable elements, preventing their mobilization, which is essential for the germline integrity. The PET complex is required during the secondary piRNAs metabolic process for the PIWIL2 slicing-triggered loading of PIWIL4 piRNAs. In the PET complex, EXD1 probably acts as an RNA adapter. EXD1 is an inactive exonuclease (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:H9IUR0}. Note=Component of the meiotic nuage, also named P granule, a germ-cell-specific organelle required to repress transposon activity during meiosis. {ECO:0000250|UniProtKB:H9IUR0}.
Interaction partners:
- Putative ATP-dependent RNA helicase TDRD12
- Piwi-like protein 2
- Protein bicaudal D homolog 1
- Exonuclease 3'-5' domain-containing protein 2
- Protein bicaudal D homolog 2
- Inactive peptidyl-prolyl cis-trans isomerase FKBP6
Sequence:
MDPSSDYHFLNQILWRRVKLTLVSGIFEGVLQHVDPNKIVVLKNVRNAESGRSVPGVKVFFGHEILNVELMDEAEGASGEKASAVSINTERAGMEKVKNEDVNVCEPASPAPEVPTSSLLSDLKYCPSEEEEVTYTVIDQFQQKFGAAMLHIKKQSVLSVAAEGANVCRHGKLCWLQVATNSRVYLFDIFLLGSRAFNNGLQMILEDKRILKVIHDCRWLSDCLSHQYGIMLNNVFDTQVADVLQFSMETGGFLPNCISTLQESLIRHLKVAPRYLFFLEERQKRIQENPEIWLTRPLPPSLLKILALETTYLLPLRLVLLDEVMSDLTTLVDGYLNTYREGSADRLAGTEPACMELPAELLQLQDFQKQRRERAVKEYRVNARGLLIRTPLHPKEPTACTAGKEERVQGFLFYKTDGGDQVPRFLCPKSHEDEKFLDKESKQTTAKSQIVPPRKEGEAHKDSKNKPGCWESAGPEDPRAQKAHALPPTWASQSQFSLKEEIEQLTVVGNKGALTSPKEGALVSPSLLQETWEAPTDTFHLPEKAEVSTLPPCPALEKTDSWISPSLNLF
Protein: T. brucei spp.-specific protein (D6XF60)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVRSDTFLGGRGSRVPSTGFNSQCAKTHAYQRGADGGFMGRKIYCQPVPLYCCSLLFMQWYPVTLMDASFLVTAITKQKKLEKIGLHSDHHHDFSHMAHMRLIFPRHVIFPVNELN
Protein: Rlf protein (Q922U7)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
TTQCHSKKDECSSETDLESSCEETESKISGISSPIGSHREEGEEKEGRGSRRTVAKGNLCYILNKYHKPFHCIHKTCNSSFTNLKGLIRHYRTVHQYNKEQLCLEKDKARTKRELVKCKKLFACKYKDCNKRFLCSKALAKHCSDSHNLDHIEESKVLSETESAARFSCNQPQCPAVFYSFSKLKHHLLEQHNIEGEIHSDYEIHCTLNGCGQIFSHRSNYFQHVYYRHKDYYDNLFSSQKVANERLLRSEKVCQTTQAQGLTQTQGQTQGQTQGQEQQAAKRPFNTKAKKCGLLKDKKAPITFKTRAEAIHMCVEHSEHTQYPCMVQGCLSVVKLESSIVRHYKRTHQMNSAYLEQQLENLVVCVKYGTKIKDEPPSEVEPCVKKEESTSCESVHTENGAPGDSSVPLPNTDSTCPAEQDGGQKGCSERNPVFDTHSLLYRGTLKCNHSSETTSLEQCNIAQSSPCKIESPIPNPSGTESGTYFTDFQLPLPRIKEEPGQHSSGQENTVKNATQVPKENIRKHSQPRSFDLKTYKPMGFESSFLKFIQESEEKDDDFDDWEPSEHLTLNNSSHPSSDLTGNVVADTIVNESAPQVDIPHSSSDPPVSENLTAVPPLVVAEATAVPSLENLRVVLDKALTDCGELALKQLHYLRPVVVLERSKFSTPILDLFPTKKTDELCVGSS
Protein: CBK1 kinase activator protein MOB2 (Q5ABC6)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Functions as an activator subunit for the CBK1 protein kinase. Part of the regulation of ACE2 activity and cellular morphogenesis (RAM) signaling network. The RAM network is critically required for hyphal growth as well as normal vegetative growth, and for polarization of lipid rafts and the actin cytoskeleton. It play an essential role in biofilm formation. The RAM network also plays a role in serum- and antifungal azoles-induced activation of ergosterol biosynthesis genes, especially those involved in the late steps of ergosterol biosynthesis.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=localizes to sites of polarized growth in both yeast and hyphal cells. {ECO:0000269|PubMed:21593210}.
Interaction partners:
- Serine/threonine-protein kinase CBK1
- Hym1p
- non-specific serine/threonine protein kinase
- Sog2p
- Cell wall transcription factor ACE2
- Cell cycle protein kinase DBF2
- Tyrosine-protein phosphatase CDC14
- Protein phosphatase PP2A regulatory subunit B
- Cyclin-dependent kinase 1
- Cas4p
Sequence:
MSFLNTIRGLGRGSKKNKKDLEPSNNAIYSHSNLSGNGLRRTQSPTKFSPSKLSSKGAQGSAAYTSSPTKRSRTGQSLQHQDSQSSLQYQQQSGSVSPSKRSSIQTTKSTTVNADPPLFLCEPYVKTALVKGSFKTIVQLPKYVDYCEWLALNIFELFNHLNRFYGVIQEYATPEAYPTMNAGPNTNYLWVNSSGQAVNLPACQYIEYVITWVTNKLNDQSVFPTKNGGAFPPNFIKDCKNISRQMFRIFAHIYHNHFDKIIHLSLEAHWNSFFAHFISFVKEFNLIDRTEMEPLLPLIENFEQQGKITQASK
Protein: Beta-hexosaminidase (EC 3.2.1.52) (Q2URY6)
Organism: Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold)
Interaction partners:
- Glycoside hydrolase family 3 domain protein
- N-acetyltransferase domain-containing protein
- Probable alpha-galactosidase A
- Probable alpha-galactosidase B
- Probable alpha-galactosidase D
- Arylsulfatase
- alpha-galactosidase
- Probable alpha-galactosidase C
- beta-N-acetylhexosaminidase
- beta-N-acetylhexosaminidase
Sequence:
MRISQICTVLSTVTSAVAVGVNPLPAPREISWGSSGPKSIAGELQLRTDSDSADGIVADAWNRAWETIVALRWVPAATEAPISSFEPFPTPTAGASKKSKRASNSLQYVNVQVKDIEADLQHGVDESYTLDVEEDSDTITINAETVWGALHAFTTLQQLVISDGHGGLIIEEPVNIKDSPLYPYRGIMLDTGRNFVSLPKIFEQLEGMSLSKLNVLHWHIDDAQSWPIWVDVYPEMVKDAYSPHEIYSRNDVRNIVNYARARGIRVIPEIDMPSHSSSGWKQVDPEMVTCTDSWWSNDDWPLHTAVEPNPGQLDIIYNKTYEVVGNVYKELSDIFPDHWFHVGGDEIQPNCFNFSTHVTKWFAEDPSRTYHDLAQYWVDHAVPIFQNYSQERRLVMWEDIALSADNAHDVPKNIVMQSWNNGLEYISNLTARGYDVIVSSSDFLYLDCGHGGFVTNDPRYNVMANPDANTPNFNYGGNGGSWCAPYKTWQRIYDYDFTLNLTETQAKHIIGATAPLWGEQVDDINVSSMFWPRAAALAELVWSGNRDANGNKRTTEMTQRILNFREYLVANGVQAQALVPKYCLQHPHACDLYRNQAAIQ
Protein: DNA topoisomerase 2-beta (EC 5.6.2.2) (DNA topoisomerase II, beta isozyme) (O42131)
Organism: Gallus gallus (Chicken)
Function: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand. Plays a role in B-cell differentiation.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q02880}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q02880}. Nucleus {ECO:0000269|PubMed:11453553}.
Interaction partners:
- DNA topoisomerase I
- DNA topoisomerase
- DNA topoisomerase
- DNA topoisomerase I
- BTB/POZ domain-containing protein KCTD9
- Structural maintenance of chromosomes protein 2
- Structural maintenance of chromosomes protein 6
- Proliferating cell nuclear antigen
- Condensin complex subunit 2
- Cyclin-dependent kinase 1
Sequence:
MAKSGGGGGGGGGGGGGGGGSGGLTCVTLFDNQINASKKEESESVNKNDTSKKMSVERVYQKKTQLEHILLRPDTYIGSVEPLTQLMWVYDEDVGMNCREVTFVPGLYKIFDEILVNAADNKQRDKNMTCIKISIDPESNIISIWNNGKGIPVVEHKVEKVYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETACKEYKHSFKQTWMNNMMKTSEPKIKHFEGDDYTCITFQPDLSKFKMENLDKDIVSLMTRRAYDLAGSCKGVKVMLNGKKLPVNGFRSYVDLYVKDKLDETGVALKVIHEVVNERWDVCLTLSEKGFQQISFVNSIATTKGGRHVDYVVDQVVGKLIEVVKKKNKAGVSVKPFQVKNHIWVFVNCLIENPSFDSQTKENMTLQPKSFGSKCQLSEKFFKAASNCGIIESILNWVKFKAQTQLNKKCSSVKHSKIKGIPKLDDANDAGGKHSLDCTLILTEGDSAKSLAVSGLGVIGRDRYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKSYEDPESLKSLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLKHGFLEEFITPIVKASKNKQELSFYSIPEFDEWKKHMENHKAWKIKYYKGLGTSTAKEAKEYFADMERHRILFRYAGPEDDAAITLAFSKKKIDDRKEWLTNFMEDRRQRRLHGLPEQFLYGTATKHLTYNDFINKELILFSNSDNERSIPSLVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSAYHHGEQALMMTIVNLAQNFVGSNNVNLLQPIGQFGTRLHGGKDAASPRYIFTMLSPLARLLFPSVDDNLLKFLYDDNQRVEPEWYIPIIPMVLVNGAEGIGTGWACKLPNYDTREIVNNVRRMLDGLDPHPMLPNYKNFRGTIQELGQNQYVVSGEIFVVDRNTVEITELPVRTWTQVYKEQVLEPMLNGTEKTPALISDYKEYHTDTTVKFVVKMTEEKLAQAEAAGLHKVFKLQTSLTCNSMVLFDHMGCLKKYETVQDILKEFFDLRLHYYSLRKEWLVGMLGAESTKLNNQARFILEKIQGKITIENRSKRDLIQMLVQRGYESDPVKAWKEAQEKAAEEEDPQNANDDASSASGSTSGPDFNYILNMSLWSLTKEKVEELIKHRDSKERELNDLKRKSASDLWKEDLAAFVEELEKVEAQEREDVLAGMVGKPIKGKVGKPKMKKLQLEETMPSPFGRRIVPQITSAMKADASRKLLKKKKGDADSVAIKMEFDEEFGGVQAEGGGDDTVNTAASGTKTPKLKREKKEPGTRVRRAPSSTKSSAKKVKKRNPWSDDESKSESDLEESEPVIIPRDSLLRRAAADRAKYTFDFSKEEDDAHDDDDANNNNDLDELKVKASPVINDREDEFVPSDSVEKDEYDFSPVKSKPSPEKMSQEKKNQDFGNIFSFPSYSQKTDDDTTKLDSDEEDSTPVFSSPFAPKQTEKMLSKTVAAKKAKVDVPPKPKRAPKAKKMETVNSDSDSEFGIPKKTAAPKGKGRGAKKRKTSGSENEGEYNPGKKAPKSTPCKKSKKAAFDQDSDVEIFQSGFASETAPKPRTGRARKEVKYFAESDEDDDFDMFN
Protein: Acetolactate synthase small subunit 1, chloroplastic (ALS-interacting protein 1) (Acetohydroxyacid synthase small subunit 1) (Q93YZ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Regulatory subunit of acetohydroxy-acid synthase. Involved in the feed-back inhibition by branched-chain amino acids. Contains 2 repeats, each of them being able to activate partially the catalytic subunit. The enzyme reconstituted with the first repeat is inhibited by leucine, but not by valine or isoleucine and the enzyme reconstituted with the second repeat is not inhibited by any branched-chain amino acid. In vitro, inhibited by valine and leucine, but not isoleucine. Involved in valine and leucine homeostasis. Required for reproductive development and sodium homeostasis. May play a role under prolonged flooding or oxygen deficiency.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:28388946}. Peroxisome {ECO:0000269|PubMed:28388946}.
Interaction partners:
- Acetolactate synthase, chloroplastic
- 2-hydroxyacyl-CoA lyase
- Threonine dehydratase biosynthetic, chloroplastic
- Ketol-acid reductoisomerase, chloroplastic
- 3-isopropylmalate dehydrogenase 2, chloroplastic
- 3-isopropylmalate dehydrogenase 3, chloroplastic
- 2-isopropylmalate synthase 1, chloroplastic
- 2-isopropylmalate synthase 2, chloroplastic
- Dihydroxy-acid dehydratase, chloroplastic
- Hydroxymethylglutaryl-CoA lyase, mitochondrial
Sequence:
MAAISVSSSPSIRCLRSACSDSSPALVSSTRVSFPAKISYLSGISSHRGDEMGKRMEGFVRSVDGKISDASFSEASSATPKSKVRKHTISVFVGDESGMINRIAGVFARRGYNIESLAVGLNRDKALFTIVVCGTERVLQQVIEQLQKLVNVLKVEDISSEPQVERELMLVKVNAHPESRAEIMWLVDTFRARVVDIAEHALTIEVTGDPGKMIAVERNLKKFQIREIVRTGKIALRREKMGATAPFWRFSAASYPDLKEQAPVSVLRSSKKGAIVPQKETSAGGDVYPVEPFFDPKVHRILDAHWGLLTDEDTSGLRSHTLSLLVNDIPGVLNIVTGVFARRGYNIQSLAVGHAETKGISRITTVIPATDESVSKLVQQLYKLVDVHEVHDLTHLPFSERELMLIKIAVNAAARRDVLDIASIFRAKAVDVSDHTITLQLTGDLDKMVALQRLLEPYGICEVARTGRVALARESGVDSKYLRGYSFPLTG
Protein: Angiopoietin-related protein 3 (Angiopoietin-like protein 3) [Cleaved into: ANGPTL3(17-224)] (Q9R182)
Organism: Mus musculus (Mouse)
Function: Acts in part as a hepatokine that is involved in regulation of lipid and glucose metabolism. Proposed to play a role in the trafficking of energy substrates to either storage or oxidative tissues in response to food intake. Has a stimulatory effect on plasma triglycerides (TG), which is achieved by suppressing plasma TG clearance via inhibition of LPL activity; the function seems to be specific for the feeding conditions. The inhibition of LPL activity appears to be an indirect mechanism involving recruitment of proprotein convertases PCSK6 and FURIN to LPL leading to cleavage and dissociation of LPL from the cell surface; the function does not require ANGPTL3 proteolytic cleavage but seems to be mediated by the N-terminal domain, and is not inhibited by GPIHBP1. Can inhibit endothelial lipase, causing increased plasma levels of high density lipoprotein (HDL) cholesterol and phospholipids; the cleaved N-terminal domain is more efficient than the uncleaved proprotein. Can bind to adipocytes to activate lipolysis, releasing free fatty acids and glycerol (By similarity). Suppresses LPL specifically in oxidative tissues which is required to route very low density lipoprotein (VLDL)-TG to white adipose tissue (WAT) for storage in response to food; the function may involve cooperation with circulating, liver-derived ANGPTL8 and ANGPTL4 expression in WAT. Contributes to lower plasma levels of low density lipoprotein (LDL)-cholesterol by a mechanism that is independent of the canonical pathway implicating APOE and LDLR. May stimulate hypothalamic LPL activity.
Subcellular location: Secreted {ECO:0000269|PubMed:23918928}. Cell projection, lamellipodium {ECO:0000269|PubMed:25710887}. Note=Colocalized with HSPG2 and activated ITGB3 on podocytes. {ECO:0000269|PubMed:20424482, ECO:0000269|PubMed:25710887}.
Interaction partners:
- Lipoprotein lipase
- Angiopoietin-like protein 8
- Angiopoietin-related protein 4
- Apolipoprotein A-V
- Glycosylphosphatidylinositol-anchored high density lipoprotein-binding protein 1
- Apolipoprotein C-III
- Apolipoprotein B-100
- Endothelial lipase
- Proprotein convertase subtilisin/kexin type 9
- Apolipoprotein A-I
Sequence:
MHTIKLFLFVVPLVIASRVDPDLSSFDSAPSEPKSRFAMLDDVKILANGLLQLGHGLKDFVHKTKGQINDIFQKLNIFDQSFYDLSLRTNEIKEEEKELRRTTSTLQVKNEEVKNMSVELNSKLESLLEEKTALQHKVRALEEQLTNLILSPAGAQEHPEVTSLKSFVEQQDNSIRELLQSVEEQYKQLSQQHMQIKEIEKQLRKTGIQEPSENSLSSKSRAPRTTPPLQLNETENTEQDDLPADCSAVYNRGEHTSGVYTIKPRNSQGFNVYCDTQSGSPWTLIQHRKDGSQDFNETWENYEKGFGRLDGEFWLGLEKIYAIVQQSNYILRLELQDWKDSKHYVEYSFHLGSHETNYTLHVAEIAGNIPGALPEHTDLMFSTWNHRAKGQLYCPESYSGGWWWNDICGENNLNGKYNKPRTKSRPERRRGIYWRPQSRKLYAIKSSKMMLQPTT
Protein: ATP-dependent RNA helicase, putative (Q582D6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- PRP8 protein homologue
- Spliceosomal U5 snRNP-specific protein, putative
- Small nuclear ribonucleoprotein E
- Small nuclear ribonucleoprotein Sm D2
- Sm protein G
- Small nuclear ribonucleoprotein SmD1
- Sm protein B
- U5 small nuclear ribonucleoprotein component, putative
- PRP1 splicing factor N-terminal domain-containing protein
- Small nuclear ribonucleoprotein, putative
Sequence:
MMAAITRYSPHSERTRVHYERFLRDIRRWLPPGLDDSIGEVAEETLSIVCRAGSGGFSGSGAATQLQNVRKQLETLFDSPLSAETLNEVLQYGRLIDDFVSTEDEPGAHTNNVVAEDGLSDLLLMQEGKGQRKPSDMSSSDSDGDTQKADYGKGRDLMKFAADVDSINDGFDDQNDDDDANCTNAIRVTFEEVACNPNYIRDSLRRLFPTQTIEECDLQAERVLQYCGKRSVDQLTLETQLTAFLGGYDDEAVTDWIATVAASRWDIVYGMSFASKQTQKEKSLVMDAVKEHARTDRVVERLYQSITGKELDNKPHSGERGNDADGSKPLRRVDLQAYAFKDERTPHQYTHAVVPQGTKRAVFETHDEVILPPTASATENLPCTPLAVFPEWARPAFPGVTQLNPMQSKIFECAFRSDENMLVCAPTGAGKTNVAMMAILRAISNNMSRTGLVNLRELKVVYVAPMKALVQEVVRTFSARLEPLGLAVIELTGDSGANQAQVGGAQLIVTTPEKWDVVTRKSVELGVASLLKLLIIDEVHLLHNERGPVLEAIVARTLLQQQHRCEAGIRLVGLSATLPNFHDVASFLQVDRQRGLFVFDSSYRPIPLQQTFCAVKKVRGTNQAAVMNLVVYDKVLEAATEGAQSLVFVHSRKDTDYTALYIVRRVVDDKRTHYFVRPGSDSEQVLREAVSDPSNSLRPSIQQMLPFGFAVHHAGMSREERSLVESLFAGGHVRVLVCTSTLAWGVNLPAHQVIIKGTRVFNAAKGETELLNALDVLQMFGRAGRVGFGSTLGRAAVITSAEDLQYYLSVLNNQLPIESQMMRRVVDMLNAEVVLGHITNLDEGVRWLQRTYLYIRMRRAPEIYGARASSNDPLLLRHLGNIVHTAADDLRRSQMVEYDSNTHRIATTSLGRIASHYYLTTTSMATYLTYLCNTMHDVDLFRLFSMSKEFSHIIVRPEEQSQLQYLLENAPIAVRESRYTPLAKINVLLQCYISNMNLQGLPLMSEMSYVKDSAQRILRALYEISLVREYGRTAQQMLQLYLMTVHQQWAVQSPARQLRHTVPPKVFASFIHALESRRVSWEEVRSWSLEDLVEKLSDERRAEAAYACIRRVPHFIVEAAVRPLTRRMLYVDVDITPDFMFDETVHTGTSGELVITVEHTNGRILHCERINLRAAALRGCETVSSPTIVVPVVDPKPTHYFVRCHSMNWLGVESSVAISLMNVLLPDIAPPLLEVHHRPPSVRSEDERDVSTAMQPYGMEAAASKVFPFTEFFQIQHDLVAPIMENRGESFFVAFPPGSGKTAVAEIFILKFLLECAHSRSANGVSSPVGGGNEEENNDGGESILRTEQKLLYLTATEACAMRRYNEWRYKFGEELNQRVAKLEPYGEELAIKAEKVRGATIIISCGSSFAPLLRHGAMDFLSAITHVIVDHVHLLRAPEGRWMEECVARLQSKPYIVNRGQGPARLLALSYPLISCTEVSRWMKVPTARQYNYGNSYRQLRVRLEAVEQFSARSRYAAATISVLKLLQNDRYAVSPCVIFVPTAQDAEELARRIVLRCRDFVPTDACEDVEDRQLALLLASGVAYMHRGSSLLDELNITEKVERPARHPKTDEPLPLYLVCSFEAAWRLPAALFATAFVCAAERIGNVCEEDKESEVGDFATDCSVSELLQMTSRALNEAVVYCRAARRWVWSRLLNDPLPIESHLRYPEDFRDTINTAVAQGRARDMPDVLRILQSHYFLHHLRTNLHFYGVPSKEDIPAYASEFARSVIASLQRTGCVTSSSNSASSTGCDGDELTALQPTPRGVAAMRHGISIESLEAIDEAVSANSRCGDSVTRMWRVIASCCVELTPQHVGDAARIVDIAELSALHVVARAFPHTYDVQYLDMDFSKGWTKVHLLVLAHCARMFVLPVSCDDGGVEAERGEIDALHPFASRSSLAVEPQLLLQIPHSVAERLLEDLNVLLPVVLDLVRGVSEIFDGRTQWRHARCLMRLLSQIERRVWGFENPIMVVPCVQETPALQRLLLSEDPNCVSYSLERLQELCDAGVKASKEWCDLAKRLCEEVPVVSDTAASEALVRRLRSEVAAVPRVVSLSSRGTIELTKGGQAFVIRVTGRVLCACSTVGGSLGPWWIACVVRHSGREHVTERLMALRTVAAVVEPTTRDTQGGNTRDKDATGKDLTTPPPLLSAWSIEETLSFPLHAVDGEDLDTITMVAIVISARYRADAEVDVTFAAG
Protein: Restriction of telomere capping protein 3 (P38804)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May play a role in RNA metabolism, rRNA-processing, and in a process influencing telomere capping.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Ribosome maturation protein SDO1
- Eukaryotic translation initiation factor 6
- Meiotic sister chromatid recombination protein 1
- 6-phosphogluconolactonase 4
- Carboxypeptidase Y inhibitor
- 12 kDa heat shock protein
- Phosphoglucomutase 2
- Catalase T
- ATPase-stabilizing factor 15 kDa protein
- Aldehyde dehydrogenase [NAD
Sequence:
MSTVTKYFYKGENTDLIVFAASEELVDEYLKNPSIGKLSEVVELFEVFTPQDGRGAEGELGAASKAQVENEFGKGKKIEEVIDLILRNGKPNSTTSSLKTKGGNAGTKAYN
Protein: Interleukin-4 receptor subunit alpha (IL-4 receptor subunit alpha) (IL-4R subunit alpha) (IL-4R-alpha) (IL-4RA) (CD antigen CD124) (Q63257)
Organism: Rattus norvegicus (Rat)
Function: Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell types, can signal through activation of insulin receptor substrates, IRS1/IRS2 (By similarity).
Subcellular location: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
Interaction partners:
- Interleukin-13
- Interleukin-4
- Tyrosine-protein kinase
- Interleukin-13 receptor subunit alpha-1
- Interleukin-13 receptor subunit alpha-2
- Interleukin 2 receptor, gamma, isoform CRA_a.
- Signal transducer and activator of transcription
- Tyrosine-protein kinase JAK3
- Tyrosine-protein kinase JAK2
- Interleukin-10
Sequence:
MGWLCTKFLSSVSCLILLWVTGSGGIKVLGDPTCFSDYIRTSTCEWQLDSTVDCSSQLLLDYRLLFEFSENLTCTPKNSADTVCVCQMAIEEPIQADTYWLELWSERGQLWQGSFKPSDNVKPPAPDNLTLHTNVSNALLLMWSNPYPSNNFLHKGLICMVNISREDNPAEFKVYNVTYTEPKLSFPVNTLTSGVRYRARVRVLSQSFPGIWSEWSPSITWYNHFQLPLLQRLPLGVSISCICILLFCLTCYFSIIKIKKIWWDQIPTPARSPLAAIIIQDTKVSLWEKQTRSQESTKSRHWKTCLTKLLPCLLEHRVKKERESPKAAKTKPLQSPEKAGWYPAEVSRTVLWPENVHVSVVRCMELFEAPVQNVEEEEDEMVKGDLSMSPENSGGGFQESQADIMARLTENLFSDLLGAENGGVGQSSMAESSSLLPSESGQASTSWACFPTGPSETTCQVTGQQPPHPDPERATGTACTQVPLVISDNPAYRSFSDFSSPAPNPGELASEQKQAGHLEEGDLLSPVDPHSSGPPMQQAESWEQILHMSVLQHGTAGSTPAPTSGYQEFVQAVKQGASQDAGVPGVGPSGDTGYKAFSSLLSSSGVCTDTAAAGTDSGCGGYKPFQNPVPNQSPNSMPLFTFGLDMELPPSPLNSAPPNSTPECLGLELGLKGGTWLKAPPPSEQVPKPFGDDLGLGIVYSSLTCHLCGHLKQHHSQEEDGQIHVVASPGCGCCYDEKSPSLGNLSGTLESCPGEMSQEANLTLAPRTPSNLSGVGKGPGHSPVPSQTTEVPVGTLGVTVS