wanglab/gogpt-training-data huggingface dataset:
Protein: Outer envelope pore protein 24A, chloroplastic (Chloroplastic outer envelope pore protein of 24 kDa A) (Q1H5C9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: High-conductance voltage-dependent solute channel with a slight selectivity for cations transporting triosephosphates, dicarboxylic acids, ATP, inorganic phosphate (Pi), sugars, and positively or negatively charged amino acids.
Subcellular location: Plastid, etioplast membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Plastid, chloroplast outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Present in non-green root plastids. {ECO:0000250}.
Interaction partners:
- Protein TIC 20-v, chloroplastic
- Mitochondrial import receptor subunit TOM20-2
- Chloroplast envelope quinone oxidoreductase homolog
- Outer envelope pore protein 24B, chloroplastic
- Putative pumilio homolog 7, chloroplastic
- Protein TIC 20-II, chloroplastic
- Outer envelope pore protein 21B, chloroplastic
Sequence:
MMKASFKGKFDVDKSGSVASLTFNAGNAKLRATMTDASFVAGPSFNGLSLAVEKPGFFIIDYNVPKKDVRFQFMNTIRIAEKPLNLTYIHMRGDNRTIVDGSFVIDPANKLSANYMVGTKNCKLKYTYVHGGIATFEPCYDVAKNMWDFAISHKLYGGDNLKATYQTSSKMLGLEWSNNSKSTGSFKVCASMNLAEELKPPKLTAETTWNLEL
Protein: Histone H3-like centromeric protein A (Centromere autoantigen A) (Centromere protein A) (CENP-A) (P49450)
Organism: Homo sapiens (Human)
Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapped around the nucleosome and gives rise to protruding DNA ends that are less well-ordered and rigid compared to nucleosomes containing histone H3. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:14667408, ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:9024683}. Chromosome, centromere {ECO:0000269|PubMed:11756469, ECO:0000269|PubMed:15282608, ECO:0000269|PubMed:15475964, ECO:0000269|PubMed:15702419, ECO:0000269|PubMed:17651496, ECO:0000269|PubMed:18072184, ECO:0000269|PubMed:19114591, ECO:0000269|PubMed:20739937, ECO:0000269|PubMed:21743476, ECO:0000269|PubMed:23818633, ECO:0000269|PubMed:25556658, ECO:0000269|PubMed:27499292, ECO:0000269|PubMed:7962047, ECO:0000269|PubMed:9024683}. Note=Localizes exclusively to sites of kinetochore assembly in centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constriction but encompassing only one third of the constriction width and height (PubMed:19114591). Phosphorylation at Ser-68 during early mitosis abolishes association with chromatin and centromeres and results in dispersed nuclear location (PubMed:25556658). {ECO:0000269|PubMed:19114591, ECO:0000269|PubMed:25556658}.
Interaction partners:
- Centromere protein N
- Centromere protein I
- Centromere protein C
- Holliday junction recognition protein
- Centromere protein M
- Centromere protein H
- Histone H4
- Histone H2A type 2-A
- Centromere protein U
- Centromere protein T
Sequence:
MGPRRRSRKPEAPRRRSPSPTPTPGPSRRGPSLGASSHQHSRRRQGWLKEIRKLQKSTHLLIRKLPFSRLAREICVKFTRGVDFNWQAQALLALQEAAEAFLVHLFEDAYLLTLHAGRVTLFPKDVQLARRIRGLEEGLG
Protein: Trinucleotide repeat containing adaptor 6A (A0A0G2JZJ3)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Protein argonaute-2
- Protein argonaute-1
- Protein argonaute-3
- Endoribonuclease Dicer
- RISC-loading complex subunit TARBP2
- Protein argonaute-4
- Probable ATP-dependent RNA helicase DDX6
- CCR4-NOT transcription complex subunit 1
- Decapping mRNA 2
- Exportin-5
Sequence:
VPEQIKPSVSQPQPANSDNGTSTATSTNNNAKRATASNQQPPPPQQQPQQQQQQQQQQQEQQQQQQQQQQQQQQPQALPRYPREVPPRFRHQEHKQLLKRGQHFPVIAANLGSAVKVLNSQSESSAVTNQQPQNNGEVQNSKSQSDINHNTSGSHYENCQRGPVSSTSDCSTSCKNAVNDLLEKEAWPSAPGSDPELASECIDADSASNSESERNITVMASGNTGGEKDGLRNSTGLGPQSKFVVGSSSNNVGHGSSTGPWGFPHGAIISTCQVSVDAPESKPESSNSRMNAWGTVSSSSNGGLNPSTLNSASNHGAWPVLENNGLALKGPVGSGNSGINIQCSTIGQMPNNQSINSKVSGSSTHGTWGSLQETCEPEVSGSQKVSFSGQPQNITTETTGPNNTTNFMTSSLPNSGSVQNNELPTSNPGAWRVSTMNHPQIQAPSVLNGTSLSHLSNGESKTGGSYGTTWGAYGSNYSGDKCAGPNGQANGDTVNATLMQPGINGPMGTNFQVSTNKGGGVWEPGTVNSQSSPWGSGNGANSGGSRRGWGSPAQNTGTSLSSVEWNKLPSNQHSNDSANGNGSKKLTNGWKSTEEDDQGSGTSQTNEQNSVWAKAGGTVESDGSAESTGRLEEKVTGESQSRDRRKIDQHTLLQSIVNRTDLDPRVLSNSGWGQTPIKQNTAWDTETSPRGERKTDNGTEAWGSSATQTFNSGACTDKTSPNSNDTSSVSGWGDPKPTLRWGDSKGSNCQGGWEDDSAATGMIKSNQWGHCKEDKSAWNDSQKNKQGWGDGQKSSQGWSVSASDNWGESSRSNHWGEANKKSSSGGSDSDRSISGWNELGKTSSFTWGNNINPNNSSGWDESSKPNSSQGWGDPPKCNQSLGWGDSSKPVSSPDWNKQQDIVGSWGIPPATSKPPGTGWLGGPIPAPAKEEEPTGWEEPSPESIRRKMEIDDGTSAWGDPSKYNYKNVNMWNKNIPEGSSRSDQQAQMHRLLPAASAISSKETSSGSGWGEPWAEPSTPATTVDNGTSAWGKPIDSGPSWGEPITAASSASTWGSNSVGPQSLSKSGPKSMQDGWCGEDTPLPGSRPTGWEEEEDVEIGMWNSSSSQELNSSLNWPPYTKKMSSKGIFSTLLFTKGMMKGGNKQEDAWINPFVKQFSNISFSRDSPEENVQSNKMDLSGGMLQDKRMEIDKHSLNIGDYNRAVGKGPGSRPQISKESSMERNPYFDKDGIVADESQNMQFMSSQSMKLPPSNNALPNQALGSIAGLGTQNLNSVRQNGNPSMFGVGNTAAQPRGMQQPPAQPLSSSQPNLRAQVPPPLLSPQVPVSLLKYAPNNGGLNPLFGPQQVAMLNQLSQLNQLSQISQLQRLLAQQQRAQSQRSVPSANRQQQDQQGRPLSVQQQMMQQSRQLDPSLLVKQQTPPSQQPLHQPAMKSFLDNVMPHTTPELQKGPSPVNAFSSFPIGLNSNLNVNMDMNSIKEPQSRLRKWTTVDSMSVNTSLDQNSSKHGAISSGFRLEESPFVPYDFMNSSTSPASPPGSIGDGWPRAKSPNGSSSVNWPPEFRPGEPWKGYPNIDPETDPYVTPGSVINSLSINTVREVDHLRDRNSGSSSSLNTTLPSTSAWSSIRASNYNVPLSSTAQSTSARNSDSKLTWSPGSVTNTSLAHELWKVPLPPKNITAPSRPPPGLTGQKPPLSTWDNSPLRVGGGWGNSDARYTPGSSWGESSSGRITNWLVLKNLTPQIDGSTLRTLCMQHGPLITFHLNLPHGNALVRYSSKEEVVKAQKSLHMCVLGNTTILAEFASEEEISRFFAQSQSLTPSPGWQSLGSSQSRLGSLDCSHSFSSRTDLNHWNGAGLSGTNCGDLHGTSLWGTPHYSTSLWGPPSSSDPRGISSPSPINAFLSVDHLAFIFIFFLFFCFFVFFFFFKTVLG
Protein: Phosphate system positive regulatory protein PHO4 (P07270)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcriptional activator that regulates the expression of repressible phosphatase under phosphate starvation conditions. Binds to the upstream activating sequence (UAS) of several phosphatase encoding PHO genes. Inhibited by the cyclin-CDK PHO80-PHO85 under high-phosphate conditions.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:8539622}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:8539622}. Note=Predominantly cytoplasmic under high-phosphate conditions and localized to the nucleus upon phosphate starvation.
Interaction partners:
- PHO85 cyclin PHO80
- Cyclin-dependent protein kinase PHO85
- Importin subunit beta-3
- Phosphate system positive regulatory protein PHO81
- Regulatory protein PHO2
- Inorganic phosphate transporter PHO84
- Inorganic phosphate transporter PHO87
- Low-affinity phosphate transporter PHO90
- Phosphate permease PHO89
- Centromere-binding protein 1
Sequence:
MGRTTSEGIHGFVDDLEPKSSILDKVGDFITVNTKRHDGREDFNEQNDELNSQENHNSSENGNENENEQDSLALDDLDRAFELVEGMDMDWMMPSHAHHSPATTATIKPRLLYSPLIHTQSAVPVTISPNLVATATSTTSANKVTKNKSNSSPYLNKRRGKPGPDSATSLFELPDSVIPTPKPKPKPKQYPKVILPSNSTRRVSPVTAKTSSSAEGVVVASESPVIAPHGSSHSRSLSKRRSSGALVDDDKRESHKHAEQARRNRLAVALHELASLIPAEWKQQNVSAAPSKATTVEAACRYIRHLQQNVST
Protein: Trafficking regulator of GLUT4 1 (Brain endothelial cell-derived protein 1) (BEC-1) (Dispanin subfamily B member 1) (DSPB1) (Tumor suppressor candidate 5 homolog) (Q2MHH0)
Organism: Rattus norvegicus (Rat)
Function: Regulates insulin-mediated adipose tissue glucose uptake and transport by modulation of SLC2A4 recycling. Not required for SLC2A4 membrane fusion upon an initial stimulus, but rather is necessary for proper protein recycling during prolonged insulin stimulation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q8C838}; Single-pass membrane protein {ECO:0000305}. Endomembrane system {ECO:0000269|PubMed:26240143}; Single-pass membrane protein {ECO:0000305}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:26240143}. Note=Shifts from low-density microsome vesicles to the cell membrane upon insulin stimulation. {ECO:0000250|UniProtKB:Q8C838}.
Interaction partners:
Sequence:
MANPVQPQLQDPGSTSPLDLPEMEKLLTKVENKDDQALNLSKSLSGALDLEQNGHSLPFKVISEGHRQPSLSGSPSRASSRRASSVVTTSYAQDQEAPKDYLVLAIASCFCPVWPLNLIPLIFSIMSRSSVQQGDLDGARRLGRLARLLSITFIILGIVIIIVAVTVNFTVPK
Protein: U6 snRNA-associated Sm-like protein LSm4 (Glycine-rich protein) (GRP) (Q9Y4Z0)
Organism: Homo sapiens (Human)
Function: Plays role in pre-mRNA splicing as component of the U4/U6-U5 tri-snRNP complex that is involved in spliceosome assembly, and as component of the precatalytic spliceosome (spliceosome B complex). The heptameric LSM2-8 complex binds specifically to the 3'-terminal U-tract of U6 snRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:10523320, ECO:0000269|PubMed:26912367, ECO:0000269|PubMed:28781166}.
Interaction partners:
- U6 snRNA-associated Sm-like protein LSm2
- U6 snRNA-associated Sm-like protein LSm8
- Small nuclear ribonucleoprotein Sm D2
- U4/U6 small nuclear ribonucleoprotein Prp3
- U6 snRNA-associated Sm-like protein LSm7
- U6 snRNA-associated Sm-like protein LSm6
- Protein PAT1 homolog 1
- U6 snRNA-associated Sm-like protein LSm1
- U6 snRNA-associated Sm-like protein LSm5
- Pre-mRNA-processing factor 6
Sequence:
MLPLSLLKTAQNHPMLVELKNGETYNGHLVSCDNWMNINLREVICTSRDGDKFWRMPECYIRGSTIKYLRIPDEIIDMVKEEVVAKGRGRGGLQQQKQQKGRGMGGAGRGVFGGRGRGGIPGTGRGQPEKKPGRQAGKQ
Protein: Protein LIAT1 (Ligand of ATE1 protein) (Q6ZQX7)
Organism: Homo sapiens (Human)
Function: May be involved in ATE1-mediated N-terminal arginylation.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:33443146}. Cytoplasm {ECO:0000269|PubMed:33443146}. Note=Shuttles between the cytoplasm and nucleoplasm, a significant portion localizes to the nucleolus. {ECO:0000269|PubMed:33443146}.
Interaction partners:
- Keratin, type II cytoskeletal 7
- Homeobox protein CDX-2
- Keratin, type I cytoskeletal 19
- Keratin, type II cytoskeletal 5
- Napsin-A
- Synaptophysin
- Prolactin-inducible protein
- Keratin, type I cytoskeletal 18
- Paired box protein Pax-8
- Cell adhesion molecule CEACAM5
Sequence:
METRGPGLAVRAESRRLVGIGPRAPPGRVGLQPSGRLDRRGGAGTMGYKDNDGEEEEREGGAAGPRGSRLPPITGGASELAKRKVKKKKRKKKTKGSGKGDDKHQSQSLKSQPLSSSFHDILSPCKERGPKPEHRQSKVEKKHLPSDSSTVSLPDFAEIENLANRINESLRWDGILADPEAEKERIRIYKLNRRKRYRCLALKGFHPDPEALKGFHPDPDALKGFHPDPEALKGFHPDPEALKGFHPDPEALKGFHPDPEALKGIHPDPEALKGIHPDPEALKGFHPDPEALKGFHPDPEALKGFHTDPEALKGFHIDPEALKGFHPDPKALKGFHPDPKALKGFHTDPEALKGFHPDPKALKGFHPDPEALKGFHPDPEALKGFHPDPEALKGFHTDPNAEEAPENLPYLSDKDGSSSHRQPTSKAECPNLCFEGNLTPKLLHSDLAPTLLE
Protein: CheY (O51615)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
- CheC-like family protein
- Chemotaxis protein CheA
- Lipoprotein, putative
- Purine-binding chemotaxis protein
- Flagellar motor switch protein FliN
- Chemotaxis protein CheA
- Flagellar motor switch protein FliM
- Chemotaxis response regulator
- Methyl-accepting chemotaxis protein
- CheY
Sequence:
MIQKTTIAADSSSKPRGINYDTGIPFNVLIVDDSVFTVKQLTQIFTSEGFNIIDTAADGEEAVIKYKNHYPNIDIVTLDITMPKMDGITCLSNIMEFDKNARVIMISALGKEQLVKDCLIKGAKTFIVKPLDRAKVLQRVMSVFVK
Protein: Mannitol-1-phosphatase (M1Pase) (EC 3.1.3.22) (O43980)
Organism: Eimeria tenella (Coccidian parasite)
Function: Key enzyme for mannitol biosynthesis.
Interaction partners:
Sequence:
MAETEWTPEALSGRYEEIKSCIPQQLEAYARFLREAAPEDLRRWQQIAQDLKLELNLENGRIKYKKEFKPLELPVDICYIRHGKTQGNTEPRVFQGQVDYANNQLTQQGQQQAAAAATKLEAMAAAKEFIPDLLLSSPLLRAVHTAQPFVDANPKPLFRVLPELAEMAFGEWDNRKVAELEKDDPAHLFYLQQNAVIKAKGPHRICCQLWQSPEWLEGKKELPAENFLECLDRQRKALIKVGEIAKELCGPSCGERKPRVAVYGHSMAGAAVSVLLGFGKEDQLGFLGFDGNYIMPNATPTILIPNAKP
Protein: Cytochrome b-c1 complex subunit 7 (A0A8I6AL93)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004443}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004443}; Matrix side {ECO:0000256|ARBA:ARBA00004443}.
Interaction partners:
Sequence:
VAASSKWLDGFRKWYYNAAGFNKLGLMRDDTMHETEDVKEAIRRLPENLYNDRMFRIKRALDLSMRHQILPKDQWTKYEEDKFYLEPYLKEVIRERKEREEWAKK
Protein: Mitogen-activated protein kinase 4 (MAP kinase 4) (MAPK 4) (EC 2.7.11.24) (Extracellular signal-regulated kinase 4) (ERK-4) (MAP kinase isoform p63) (p63-MAPK) (P31152)
Organism: Homo sapiens (Human)
Function: Atypical MAPK protein. Phosphorylates microtubule-associated protein 2 (MAP2) and MAPKAPK5. The precise role of the complex formed with MAPKAPK5 is still unclear, but the complex follows a complex set of phosphorylation events: upon interaction with atypical MAPKAPK5, ERK4/MAPK4 is phosphorylated at Ser-186 and then mediates phosphorylation and activation of MAPKAPK5, which in turn phosphorylates ERK4/MAPK4. May promote entry in the cell cycle (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Translocates to the cytoplasm following interaction with MAPKAPK5. {ECO:0000250}.
Interaction partners:
- MAP kinase-activated protein kinase 5
- Mitogen-activated protein kinase 6
- Insulin-like growth factor 2 mRNA-binding protein 1
- Exportin-1
Sequence:
MAEKGDCIASVYGYDLGGRFVDFQPLGFGVNGLVLSAVDSRACRKVAVKKIALSDARSMKHALREIKIIRRLDHDNIVKVYEVLGPKGTDLQGELFKFSVAYIVQEYMETDLARLLEQGTLAEEHAKLFMYQLLRGLKYIHSANVLHRDLKPANIFISTEDLVLKIGDFGLARIVDQHYSHKGYLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCILAEMLTGRMLFAGAHELEQMQLILETIPVIREEDKDELLRVMPSFVSSTWEVKRPLRKLLPEVNSEAIDFLEKILTFNPMDRLTAEMGLQHPYMSPYSCPEDEPTSQHPFRIEDEIDDIVLMAANQSQLSNWDTCSSRYPVSLSSDLEWRPDRCQDASEVQRDPRAGSAPLAEDVQVDPRKDSHSSSERFLEQSHSSMERAFEADYGRSCDYKVGSPSYLDKLLWRDNKPHHYSEPKLILDLSHWKQAAGAPPTATGLADTGAREDEPASLFLEIAQWVKSTQGGPEHASPPADDPERRLSASPPGRPAPVDGGASPQFDLDVFISRALKLCTKPEDLPDNKLGDLNGACIPEHPGDLVQTEAFSKERW
Protein: Tripartite motif-containing protein 5 (EC 2.3.2.27) (RING finger protein 88) (RING-type E3 ubiquitin transferase TRIM5) (Q9C035)
Organism: Homo sapiens (Human)
Function: Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by N-tropic murine leukemia virus (N-MLV), equine infectious anemia virus (EIAV), simian immunodeficiency virus of macaques (SIVmac), feline immunodeficiency virus (FIV), and bovine immunodeficiency virus (BIV). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2. Also plays a role in autophagy by acting as a selective autophagy receptor which recognizes and targets HIV-1 capsid protein p24 for autophagic destruction.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25127057}. Nucleus {ECO:0000250|UniProtKB:Q0PF16}. Note=Predominantly localizes in cytoplasmic bodies (PubMed:12878161, PubMed:20357094). Localization may be influenced by the coexpression of other TRIM proteins, hence partial nuclear localization is observed in the presence of TRIM22 or TRIM27 (By similarity). In cytoplasmic bodies, colocalizes with proteasomal subunits and SQSTM1 (By similarity). {ECO:0000250|UniProtKB:Q0PF16, ECO:0000269|PubMed:12878161, ECO:0000269|PubMed:20357094, ECO:0000269|PubMed:25127057}.
Interaction partners:
- Ubiquitin-conjugating enzyme E2 N
- BTB/POZ domain-containing protein 2
- T-cell receptor-associated transmembrane adapter 1
- DNA dC->dU-editing enzyme APOBEC-3G
- BTB/POZ domain-containing protein 1
- Peptidyl-prolyl cis-trans isomerase A
- Deoxynucleoside triphosphate triphosphohydrolase SAMHD1
- Bone marrow stromal antigen 2
- Gamma-butyrobetaine dioxygenase
- Ubiquitin-conjugating enzyme E2 D2
Sequence:
MASGILVNVKEEVTCPICLELLTQPLSLDCGHSFCQACLTANHKKSMLDKGESSCPVCRISYQPENIRPNRHVANIVEKLREVKLSPEGQKVDHCARHGEKLLLFCQEDGKVICWLCERSQEHRGHHTFLTEEVAREYQVKLQAALEMLRQKQQEAEELEADIREEKASWKTQIQYDKTNVLADFEQLRDILDWEESNELQNLEKEEEDILKSLTNSETEMVQQTQSLRELISDLEHRLQGSVMELLQGVDGVIKRTENVTLKKPETFPKNQRRVFRAPDLKGMLEVFRELTDVRRYWVDVTVAPNNISCAVISEDKRQVSSPKPQIIYGARGTRYQTFVNFNYCTGILGSQSITSGKHYWEVDVSKKTAWILGVCAGFQPDAMCNIEKNENYQPKYGYWVIGLEEGVKCSAFQDSSFHTPSVPFIVPLSVIICPDRVGVFLDYEACTVSFFNITNHGFLIYKFSHCSFSQPVFPYLNPRKCGVPMTLCSPSS
Protein: UDP-sugar-dependent glycosyltransferase 52 (EC 2.4.1.173) (Sterol 3-beta-glucosyltransferase) (UDP-glycosyltransferase 52) (Q54IL5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Involved in the biosynthesis of sterol glucoside. Can use different sterols such as cholesterol, sitosterol, and ergosterol as sugar acceptors.
Interaction partners:
- Serine palmitoyltransferase 1
- Serine palmitoyltransferase 2
Sequence:
MDEFTSDSLTTSRLLRQISHSDSLSSVGSSSNRSNSNYENKINNGIINDFDSTNANDGISNNSNNSNNNNNSSSILKIHQSPQSILSTEQQHQIQQYQQYHQQQIYESGYVPPHVYIFDPDYKSNNDEEDKEKRSLIELNKSTDLSNIKTTTTTTTTTTPPPLMIPENEEENKQLRQEILNELSKSESFTKIKEPGEIYGFCECSLLYNHLTCANLVITSNYLIFLPQQQVDSDYVLENYLYKKGDFFWKKYWFVLTPDSISWYKSSILKETHYPNGTILLSKIVTVDKLDPEETGKPFCLQIMTNTSIHLIQLDTEPQLEHWYHEINRMQKNLNVTIPIGDIVSITMESNAALFFDSLCLTLKKGENCLVTPSSSSNEVYSLLIKLWNRNRGVTVVEPEKQQRLLEFQKTFKLSQGVNLLIETPCVFYQDEEFSYEGVLYATTEGTLYFSSLDSVLIIPESDIYAITIDRKSDNRDALKVYTTDYDVLFFDSIDDIETFFNVISTSLARSNPKIFFSTVGQIPPIDEPKHDEKEHKSTYQTISSGIRSWKIPIPSLPNFSIPIPKSIPIPLFRSKSSSHLDPQNSQQQQQQQQQSSSLQLDDNNNNIVIPHTSNPTTIIPSTSSSSAIPPPPSSTSSTSSTTHEKTIIIQKNSSINSTFHDIFPLLPLDETVIMFQNCSLYYYSYDSNVEGIVYITKSYIAFNPSPLDKQQQQQQQQQQQQPNSSSITSTTYDRDLDTDSDTDSESDFDYPKQSQHDNSVVMVNNNQYKVKEVLMKKALIPIEDIVSVTKERFLLFFNQCVKIITLDHKWIFGSLNNINSFYNLILETWKQIPKTLLDSSSSSSSSSSSSLLSSSPNNNNSDLNINGNSEGSIFTPLESIKIKNKLGLPADEVLITWFNCTNFKGAQLKYGFLYISNNNICFRSKFGFQKRTIVIPLSQVIEIKKYSAFIPNGIKITTASHHEFQFASFIHRNRVYQILYETWLKANNKKSNSSNSLSSSPTITSPLAISPSIASPSITPPSSTPPSSTTPSSTTPTITSPTIHSTLPSTVVYNDIQEIIDGENNSNNNNNNNNTNNTNKSNSFIGNVEEDVDKIKRSIKSLPILKIHSAQQQQQQQPKTTTTTTSTTTTNLISPRLLTPLTITQSPGFSSLVNSPILPVKPLRITILTIGSRGDIQPFIALSLGLKEYGHNVTLATHELYRDLISKEFGLNYQPLGGDPRELMDLCVRNGIFTPKFIKEALSRFRSFIDDLLLTCWKAVQNSNTQVLIATPGCFAGPHIGEVLQIPFFNAFTMPFTRTRTYPNPFAPFASHQMGGVFNLATHVMMEKVLWQPISGQINQWRTETLKIPPWNSSVSINETYRMPYLYCFSKYLVPKPPDWSGEIAITGYWTLKNQANSDSPPDDLIQFLNEESSTENDDIPIYIGFGSIVIDNPTALSLLLIEAIKLSGKRAIISQGWGGLSIDEHNNNNNNNNNNNNGENSDSNKSSLQSNRIYLLKKPVDHSWLFEKVSLVISHGGAGTVAASLLAAKPTIVVPFFGDQFFWGERIKQTGIGTSIPFDILTAKSLSSHIISILNEPSVRAKVNKMSHLLKREDGVKTAIDFIHRYLPFSFIPPREIPFSSAPNSCMGCKQPFTLLHVMKARVHCHCCGKIFCESCTSHKCPIKKYRINTPVRVCDKCFNDLQSNPSSNSFILND
Protein: Uncharacterized protein (Q389X0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- NLE domain-containing protein
Sequence:
MDLDNVVLDDDVLLGDGVAASVPPPLLVSAPVLDLAMHPTLPLFVAGLVTGDVEIHEYCGAETRHRPTSQQYFTDMDTTHAFSPYNIRMHPRGGVTSMEFTEDGKYLVSVSSDRTISVFDCVTEKMALHIAAKESDTSAGAPAKAKVKETKERETKAKNKVGQNDNLVKSKKKKNPHKFGISAVNVCDANTIATGDDDGMIVLWDMRKRKAAHHYHEHGDYVSQMVYFSDIEELVSSSGDTCLGVFDMRAGKIRDYSEKRKDELNCFAFVNNTASNRNTFIPSIICGTPKGCLPVWKFGSWRRPYDMMDRHPAECESIISFNNPDSPFNHNIILTGACDGLVRVLEMYPVRRNLCQLSARDFTYSHQSALGCGGSSNSYANTAVRRQRGNQGISRMRLSFDSSLLAVCGTDNIIDFVDVAFLSNEKELNKLRSQTEQRHLEVLKEVEEERNKEAEEDSDSGSDGSSSAEGVVSVEDTVGKKRGRDAEKTELESNVGRGDGVDEEEADVEVKTERQKRRERVAAAKWLKVEKKKKVNFTFEKRRRRVHGFFGDLNS
Protein: Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR6 (EC 3.1.3.95) (Myotubularin-related protein 6) (Phosphatidylinositol-3-phosphate phosphatase) (G5ED68)
Organism: Caenorhabditis elegans
Function: May dephosphorylate phosphatidylinositol-3-phosphate (PI3P). In association with mtm-9, plays a role in endosome trafficking probably by regulating phosphatidylinositol-3-phosphate levels. Regulates fluid phase endocytosis in coelomocytes. Controls the endosomal localization of sorting nexin snx-3 and the levels of sorting receptor mig-14. By regulating the retrograde transport of mig-14, may be involved in the secretion of Wnt ligands such as egl-20. Regulates posterior migration of QL neuroblast descendants and the anterior migration of QR neuroblast descendants and HSN neurons during larval development. Involved in the formation of correct synapse number in DA9 motor neurons probably in part by regulating the secretion of Wnt ligand egl-20.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14565969}. Membrane {ECO:0000269|PubMed:14565969}; Peripheral membrane protein {ECO:0000269|PubMed:14565969}. Apical cell membrane {ECO:0000269|PubMed:12788949}; Peripheral membrane protein {ECO:0000269|PubMed:12788949}.
Interaction partners:
- Myotubularin-related protein 9
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- SAC domain-containing protein
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol 3-kinase piki-1
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase mtm-1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta egl-8
- 1-phosphatidylinositol 4-kinase
- Phosphoinositide 3-kinase adapter subunit
Sequence:
MRFEDIGISKVDKVCLVDRLGCQENLVGTVHVTTTHIIFRAENGSKELWLATGLISSVEKGTLTAAGCMLVIRCKHFQVITLLISRDKSCQDLYETLQRAAKPVSVNVTELLAFENREPVEDVRGWRRLDWNSEMTRQGITKSQWTESNINEGYTICDTYPNKLWFPTAASTSVLLGSCKFRSRGRLPVLTYFHQQTEAALCRCAQPLTGFSARCVEDEKLMELVGKANTNSDNLFLVDTRPRVNAMVNKVQGKGFEDERNYSNMRFHFFDIENIHVMRASQARLLDAVTKCRDVTEYWKTLEASGWLKHVRSVVECSLFLAESISRGTSCVVHCSDGWDRTSQVVALCQLLLDPYYRTIHGFQVLIEKDWLGFGHKFDDRCGHVGALNDEAGKEVSPIFTQWLDCIWQIMQQKPRAFQFNERYLIEMHEHVYSCQFGTFIGNCDKDRRDLNLSKRTKSLWTWMDARHDDYMNPFYSPTAHVALLDLDTRAARFTVWTAMYNRFDNGLQPRERLEDLTMAAMEHVGVLESHVAQLRTRLAELKTQQNQQITSTNTPTNMVDSGMSSATDDLKNLSLSHPLDPLSSTLPILERATSQESGVMDSSLYYPDEALTKYSLKWQPLRGADRCSNPACRGEFSSTIERRIHCHLCGMIFCRRCLKVSADERERVCDKCKTD
Protein: C2 domain-containing protein (Q7Z1P8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MLWVILSWGLVAVLCYFALNHLGSTGEAAHTSSTFGSSVSGNGVANGGTHTSSGEWSNEIVSWLYSNFHKVPAPMDAWIKSLNEAAKKVTSPTKCEVLFEGFGDHSDVLQPPKISNVRVEHGPRDHLTVRSNVHLPCVKLRLVSSQRTPERMIVSNYDVSIVDLRGEVECRMACIANQLYLMGCFSGRPEMDIELRNTDPNAQYQVSIPMVEESIRRCLLSAVTNINLSEEMPEERNTFADTFSRTIYNPPTHSPSGTMRNSYNNYDTNLHVDAYGTQSSHRSNSPSGDVPEMFKKLNESHLISPSYNTNSIPNKMRIKVIKASRLGREVSQPFVNVEMDEPAQKYSTTKGINANPFWEETFDFDLTPATEEILFEIYEGNDKLHMNDDEGFLGLAIVNFEEIRRSGETVHSLKLQGRPYRKDAISGEITVQFDFFYDPNLLTSGKLTDTVKVTNPNGSEFRETLTTHRRPIYDPHDNFDGHEPIVPSKTTTVTVKTVSQTLKEKPTIQSVHGSLENAVDPATQKILDRQFKNHNDPKTRELEAKLQSVAQSMSASSTLDRPSKNGNNGQYYRDQTAPPEFHEELDVRQSRDKSKKAPTEKRDRSFFGELKDRLSGRRGRSQKRSKSVDVENNQLLEEAVSLPPSRDPSRTRYAVSSNDKYRETHSVGGRSGESTKSLYQHSTLILELDQDKQAKYFLIPPAMLNEPAASRLMRKGKKLHIYNDHTFVAVKVKGGATCNVCQQRIRSSFSKQAYQCRDCKMVCHKTCHYKTDAFCTQSNVSKLQIAKDVDWAHFLSHYQLEEFISSEGL
Protein: Mycinamicin IV hydroxylase/epoxidase (EC 1.14.-.-) (Cytochrome P450 MycG) (Multifunctional P450 enzyme) (Mycinamicin biosynthesis protein G) (Q59523)
Organism: Micromonospora griseorubida
Function: Involved in the biosynthesis of mycinamicin, a 16-membered macrolide antibiotic. Catalyzes consecutive hydroxylation (at C14) and epoxidation (at C12-C13) reactions with mycinamicin IV as initial substrate, leading to mycinamicin II. These reactions require prior dimethylation of 6-deoxyallose to mycinose for effective conversion by the dual function MycG enzyme.
Interaction partners:
Sequence:
MTSAEPRAYPFNDVHGLTLAGRYGELQETEPVSRVRPPYGEEAWLVTRYEDVRAVLGDGRFVRGPSMTRDEPRTRPEMVKGGLLSMDPPEHSRLRRLVVKAFTARRAESLRPRAREIAHELVDQMAATGQPADLVAMFARQLPVRVICELLGVPSADHDRFTRWSGAFLSTAEVTAEEMQEAAEQAYAYMGDLIDRRRKEPTDDLVSALVQARDQQDSLSEQELLDLAIGLLVAGYESTTTQIADFVYLLMTRPELRRQLLDRPELIPSAVEELTRWVPLGVGTAFPRYAVEDVTLRGVTIRAGEPVLASTGAANRDQAQFPDADRIDVDRTPNQHLGFGHGVHHCLGAPLARVELQVALEVLLQRLPGIRLGIPETQLRWSEGMLLRGPLELPVVW