wanglab/gogpt-training-data huggingface dataset:
Protein: Small ribosomal subunit protein mS38 (Mitochondrial mRNA-processing protein COX24) (P32344)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the mitochondrial ribosome (mitoribosome), a dedicated translation machinery responsible for the synthesis of mitochondrial genome-encoded proteins, including at least some of the essential transmembrane subunits of the mitochondrial respiratory chain. The mitoribosomes are attached to the mitochondrial inner membrane and translation products are cotranslationally integrated into the membrane. mS38 is also involved in the splicing of the COX1 mRNA.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14562095}. Mitochondrion inner membrane {ECO:0000269|PubMed:16339141}; Peripheral membrane protein {ECO:0000269|PubMed:16339141}; Matrix side {ECO:0000269|PubMed:16339141}. Note=Mitoribosomes are tethered to the mitochondrial inner membrane and spatially aligned with the membrane insertion machinery through two distinct membrane contact sites, formed by the 21S rRNA expansion segment 96-ES1 and the inner membrane protein MBA1. {ECO:0000269|PubMed:25609543}.
Interaction partners:
- Small ribosomal subunit protein mS47
- Small ribosomal subunit protein mS37
- Small ribosomal subunit protein mS45
- Small ribosomal subunit protein mS46
- Small ribosomal subunit protein mS33
- Small ribosomal subunit protein bS6m
- Small ribosomal subunit protein mS26
- Small ribosomal subunit protein uS3m
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein uS10m
Sequence:
MLGRALRPGWLGITRTVVKKPSCGSYFNRTFQTAINTTMPPMQEGMLSTMMMMTATATRITGTVSEPLNGSNIVMQLDSVMRKRKKKMKKHKLRKRRKREKAERRKLSQGR
Protein: AT4g30600/F17I23_60 (Signal recognition particle receptor alpha subunit family protein) (Signal recognition particle receptor-like protein) (Q9M0A0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004397}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004397}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004397}.
Interaction partners:
- Signal recognition particle receptor subunit beta
- Signal recognition particle receptor subunit beta
- Signal recognition particle subunit SRP68
- Signal recognition particle subunit SRP72
- Signal recognition particle subunit SRP72
- Signal recognition particle 9 kDa protein
- Large ribosomal subunit protein uL23y
- Signal recognition particle 14 kDa protein
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL18z
Sequence:
MLEQLLIFTRGGLILWTCKEIGNALKGSPIDTLIRSCLLEERSGAVSFNYDAPGAAYTLKWTFHNDLGLVFVAVYQRILHLLYVDDLLSMVKQSFSEVYDPKRMAYDDFDETFRQLRIEAEARAEELRKTKQVGKPVTSVKKQGQVSKPGLEGGNKRVSSEGGSKKDDGDGGNKAKVSTLTNGHSNGNHQMEDDSQETNDLANGKENTSSNVAVDLSKLQKLRSKGVRGRGGVRKTDSIGNKSSKVAEPAKKATKKNRVWDDAAPKQSKLDFTDSIDENGNNDHVDIVAADQGESMMDKEEVFSSDSESEDDDEPGSDEKPAQAKKKGWFSSVFQSITGKANLERTDLGPALKALKERLMTKNVAEEIAEKLCESVEASLEGKKLSSFTRISSTVQAAMEDALVRILTPRRSIDILRDVHAAKEQRKPYVVVFVGVNGVGKSTNLAKVAYWLQQHKVSVMMAACDTFRSGAVEQLRTHARRLQIPIFEKGYEKDPAVVAKEAIQEATRNGSDVVLVDTAGRMQDNEPLMRALSKLINLNQPDLVLFVGEALVGNDAVDQLSKFNQKLSDLSTSGNPRLIDGILLTKFDTIDDKVGAALSMVYISGSPVMFVGCGQSYTDLKKLNVKAIVKTLLK
Protein: CASP-like protein 4D1 (AtCASPL4D1) (Q8GWD5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000269|PubMed:24920445}; Multi-pass membrane protein {ECO:0000269|PubMed:24920445}.
Interaction partners:
- Transcription factor CAULIFLOWER
Sequence:
MAPPPPAPPSVTLRTVLLLLRVLTAAFLLITVVLISTNTVTLEISSTSIKLPFNDVYAYRYMLSAAVIGLVYAVVQLFLTISQFATGKTHPLTYQFDFYGDKVISYLLATGSAAGFGVSKDLKDTYIALIEFDSTDPVDKFFSKGYASASLLLFAFVSLAVLSVFSSLALSKRPVPVS
Protein: Cytotoxic and regulatory T-cell molecule (Class-I MHC-restricted T-cell-associated molecule) (CD antigen CD355) (O95727)
Organism: Homo sapiens (Human)
Function: Mediates heterophilic cell-cell adhesion which regulates the activation, differentiation and tissue retention of various T-cell subsets (By similarity). Interaction with CADM1 promotes natural killer (NK) cell cytotoxicity and IFNG/interferon-gamma secretion by CD8+ T-cells in vitro as well as NK cell-mediated rejection of tumors expressing CADM1 in vivo. Regulates CD8+ T-cell proliferation in response to T-cell receptor (TCR) activation (By similarity). Appears to be dispensable for CD8+ T-cell-mediated cytotoxicity (By similarity). Interaction with SCRIB promotes the late phase of cellular polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG, IL17 and IL22 production (By similarity). By interacting with CADM1 on CD8+ dendritic cells, regulates the retention of activated CD8+ T-cells within the draining lymph node (By similarity). Required for the intestinal retention of intraepithelial CD4+ CD8+ T-cells and, to a lesser extent, intraepithelial and lamina propria CD8+ T-cells and CD4+ T-cells (By similarity). Interaction with CADM1 promotes the adhesion to gut-associated CD103+ dendritic cells, which may facilitate the expression of gut-homing and adhesion molecules on T-cells and the conversion of CD4+ T-cells into CD4+ CD8+ T-cells (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q149L7}; Single-pass type I membrane protein {ECO:0000255}. Note=In a subset of CD4+ T-cells, colocalizes with SCRIB at the immunological synapse during the late phase of T-cell activation. {ECO:0000250|UniProtKB:Q149L7}.
Interaction partners:
- Cell adhesion molecule 1
- Nectin-2
- T-cell surface glycoprotein CD8 alpha chain
- Nectin-1
- Protein scribble homolog
Sequence:
MWWRVLSLLAWFPLQEASLTNHTETITVEEGQTLTLKCVTSLRKNSSLQWLTPSGFTIFLNEYPALKNSKYQLLHHSANQLSITVPNVTLQDEGVYKCLHYSDSVSTKEVKVIVLATPFKPILEASVIRKQNGEEHVVLMCSTMRSKPPPQITWLLGNSMEVSGGTLHEFETDGKKCNTTSTLIIHTYGKNSTVDCIIRHRGLQGRKLVAPFRFEDLVTDEETASDALERNSLSSQDPQQPTSTVSVTEDSSTSEIDKEEKEQTTQDPDLTTEANPQYLGLARKKSGILLLTLVSFLIFILFIIVQLFIMKLRKAHVIWKKENEVSEHTLESYRSRSNNEETSSEEKNGQSSHPMRCMNYITKLYSEAKTKRKENVQHSKLEEKHIQVPESIV
Protein: Nucleoporin nup61 (Nuclear pore protein nup61) (Q9USL4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope. May play a role in mitotic spindle formation and/or function.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:15116432, ECO:0000269|PubMed:16823372}.
Interaction partners:
- Nucleoporin nup184
- Nucleoporin nup40
- Uncharacterized WD repeat-containing protein C4F10.18
- Armadillo repeat protein involved in nucleocytoplasmic transport Syo2
- Uncharacterized protein ely5
- Nucleoporin nup85
- Nucleoporin nup107
Sequence:
MSKRGADHQLTKDQDDSDDDRHGPVEVPKEASADVMATRKIAKPKSRKRPTSGVSSPGIFANLAAKPVSLPASTTQFTFGKPAVTANNDSDIHLKKRGLNKSFIDAVIKSVDNNPFGNLSPLFDEYRQHFSSIEKKPAEEQPTSNAVVSEVNPQQQKSQDSSSFVTEKPASSEKEDKEKPLVPPGAPRFGFSAPALGSSFQFNSSAFTPKGSFGEKSATEAEAKEKETSSNQTATGTAATTTNQFSFNTAANPFAFAKKENEESKPLTPVFSFSTTMASADASKETKQTHETKDSKSEESKPSNNEKSENAVEPAKGNTMSFSWTPDKPIKFDTPEKKFTFTNPLSSKKLPASSDVKPPSAAAVGFSFGTTTNPFSFAAPKSSFPTSSTPASVGAEKSEETSNGNKSEQEEKENGNDETRSNDSLVSGKGKGEENEDSVFETRAKIYRFDATSKSYSDIGIGPLKINVDRDTGSARILARVEGSGKLLLNVRLCQDFEYSLAGKKDVKVPAASTDGKSIEMYLIRVKEPSTAEKLLAELNEKKVSKSEN
Protein: Dual specificity mitogen-activated protein kinase kinase mek-2 (MAP kinase kinase mek-2) (EC 2.7.12.2) (Q10664)
Organism: Caenorhabditis elegans
Function: Functions in the let-60 Ras signaling pathway; acts downstream of lin-45 raf kinase, but before the sur-1/mpk-1 gene product in controlling vulval cell differentiation. Required for progression of developing oocytes through the pachytene stage. Plays a role in responses to M.nematophilum-mediated bacterial infection by promoting tail swelling and preventing constipation. Involved in fluid homeostasis. Positively regulates lifespan upstream of mpk-1.
Interaction partners:
- Mitogen-activated protein kinase mpk-1
- Raf homolog serine/threonine-protein kinase
- Ras protein let-60
- Kinase suppressor of Ras A
- Kinase suppressor of Ras B
- Late endosomal/lysosomal adaptor and MAPK and MTOR activator 5
- Sex muscle abnormal protein 5
- Cyclin-dependent kinase 1
- mitogen-activated protein kinase kinase
- non-specific serine/threonine protein kinase
Sequence:
MSSGKRRNPLGLSLPPTVNEQSESGEATAEEATATVPLEEQLKKLGLTEPQTQRLSEFLQVKEGIKELSEDMLQTEGELGHGNGGVVNKCVHRKTGVIMARKLVHLEIKPSVRQQIVKELAVLHKCNSPFIVGFYGAFVDNNDISICMEYMDGLSLDIVLKKVGRLPEKFVGRISVAVVRGLTYLKDEIKILHRDVKPSNMLVNSNGEIKLCDFGVSGMLIDSMANSFVGTRSYMAPERLTGSHYTISSDIWSFGLSLVELLIGRYPVPAPSQAEYATMFNVAENEIELADSLEEPNYHPPSNPASMAIFEMLDYIVNGPPPTLPKRFFTDEVIGFVSKCLRKLPSERATLKSLTADVFFTQYADHDDQGEFAVFVKGTINLPKLNP
Protein: Ras-related protein Rab-3C (EC 3.6.5.2) (P62824)
Organism: Rattus norvegicus (Rat)
Function: Protein transport. Probably involved in vesicular traffic (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Regulating synaptic membrane exocytosis protein 2
Sequence:
MRHEAPMQMASAQDARFGQKDSSDQNFDYMFKLLIIGNSSVGKTSFLFRYADDSFTSAFVSTVGIDFKVKTVFKNEKRIKLQIWDTAGQERYRTITTAYYRGAMGFILMYDITNEESFNAVQDWSTQIKTYSWDNAQVILAGNKCDMEDERVVSTERGQRLGEQLGFEFFETSAKDNINVKQTFERLVDIICDKMSESLETDPAITAAKQSTRLKETPPPPQPNCGC
Protein: Calcium-binding and coiled-coil domain-containing protein 1 (Calphoglin) (Coiled-coil coactivator protein) (Sarcoma antigen NY-SAR-3) (Q9P1Z2)
Organism: Homo sapiens (Human)
Function: Functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). Recruited to promoters through its contact with the N-terminal basic helix-loop-helix-Per-Arnt-Sim (PAS) domain of transcription factors or coactivators, such as NCOA2. During ER-activation acts synergistically in combination with other NCOA2-binding proteins, such as EP300, CREBBP and CARM1. Involved in the transcriptional activation of target genes in the Wnt/CTNNB1 pathway. Functions as a secondary coactivator in LEF1-mediated transcriptional activation via its interaction with CTNNB1. Coactivator function for nuclear receptors and LEF1/CTNNB1 involves differential utilization of two different activation regions (By similarity). In association with CCAR1 enhances GATA1- and MED1-mediated transcriptional activation from the gamma-globin promoter during erythroid differentiation of K562 erythroleukemia cells.
Subcellular location: Cytoplasm. Nucleus. Note=Shuttles between nucleus and cytoplasm. {ECO:0000250}.
Interaction partners:
- GABA type A receptor associated protein like 1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- Gamma-aminobutyric acid receptor-associated protein
Sequence:
MEESPLSRAPSRGGVNFLNVARTYIPNTKVECHYTLPPGTMPSASDWIGIFKVEAACVRDYHTFVWSSVPESTTDGSPIHTSVQFQASYLPKPGAQLYQFRYVNRQGQVCGQSPPFQFREPRPMDELVTLEEADGGSDILLVVPKATVLQNQLDESQQERNDLMQLKLQLEGQVTELRSRVQELERALATARQEHTELMEQYKGISRSHGEITEERDILSRQQGDHVARILELEDDIQTISEKVLTKEVELDRLRDTVKALTREQEKLLGQLKEVQADKEQSEAELQVAQQENHHLNLDLKEAKSWQEEQSAQAQRLKDKVAQMKDTLGQAQQRVAELEPLKEQLRGAQELAASSQQKATLLGEELASAAAARDRTIAELHRSRLEVAEVNGRLAELGLHLKEEKCQWSKERAGLLQSVEAEKDKILKLSAEILRLEKAVQEERTQNQVFKTELAREKDSSLVQLSESKRELTELRSALRVLQKEKEQLQEEKQELLEYMRKLEARLEKVADEKWNEDATTEDEEAAVGLSCPAALTDSEDESPEDMRLPPYGLCERGDPGSSPAGPREASPLVVISQPAPISPHLSGPAEDSSSDSEAEDEKSVLMAAVQSGGEEANLLLPELGSAFYDMASGFTVGTLSETSTGGPATPTWKECPICKERFPAESDKDALEDHMDGHFFFSTQDPFTFE
Protein: Calreticulin-2 (Q38858)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Molecular calcium-binding chaperone promoting folding, oligomeric assembly and quality control in the ER via the calreticulin/calnexin cycle. This lectin may interact transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER (By similarity).
Subcellular location: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-ProRule:PRU10138}.
Interaction partners:
- Endoplasmin homolog
- Calnexin homolog 1
- UDP-glucose:glycoprotein glucosyltransferase
- Calnexin homolog 2
- Heat shock 70 kDa protein BIP3
- Calreticulin-1
- Heat shock 70 kDa protein BIP2
- Heat shock 70 kDa protein BIP1
- Calreticulin-3
- Protein disulfide isomerase-like 1-3
Sequence:
MAKMIPSLVSLILIGLVAIASAAVIFEERFDDGWENRWVKSEWKKDDNTAGEWKHTAGNWSGDANDKGIQTSEDYRFYAISAEFPEFSNKDKTLVFQFSVKHEQKLDCGGGYMKLLSGDVDQKKFGGDTPYSIMFGPDICGYSTKKVHAILTYNEANHLIKKDVPCETDQLTHVYTFILRPDATYSILIDNVEKQTGSLYSDWDLLPPKKIKDPSAKKPEDWDEQEYISDPEDKKPDGYDDIPKEIPDTDSKKPEDWDDEEDGEWTAPTIPNPEYMGEWKPKQIKNPNYKGKWEAPLIDNPDFKDDPELYVFPKLKYVGLELWQVKSGSLFDNVLICDDPDYAKKLADETWGKLKDAEKAAFDEAEKKNEEEESKDAPAESDAEDEPEDDEGGDDSDSESKAEETKSVDSEETSEKDATAHDEL
Protein: Munster protein (Q9U5X2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
HEPQSSNSLDNELKASYGTGAMSPSRLSPNIFLNLNIDHLGLERGGSGLSMEWSTYPPQTQAQTHPQMDSDNQLQQHPPQQHASDPIHAGSSSHHQQQQQQHQQEQHNPQLHPGLEFAASLSLDMTDGSSAYDEMKFLSVDVDQFTIDSFKADCILSMEQSQMQAYGGHSQLVGSSNELCLDGIGMFSFGMEEGEPKSPPSLLVLDKSLPSLSIGVEGIADLVEQLHHHQHEGGPVGGGVITGDVM
Protein: Gallinacin-7 (Gal 7) (Beta-defensin 7) (Gallinacin-5) (Gal-5) (Q6QLR2)
Organism: Gallus gallus (Chicken)
Function: Has bactericidal activity.
Subcellular location: Secreted. Cytoplasmic granule {ECO:0000250}.
Interaction partners:
- Gallinacin-2
- Gallinacin-1
- Gallinacin-5
- Gallinacin-4
- Gallinacin-14
- Gallinacin-9
- Gallinacin-3
- Gallinacin-8
- Gallinacin-10
- Gallinacin-12
Sequence:
MRILYLLLSVLFVVLQGVAGQPFIPRPIDTCRLRNGICFPGICRRPYYWIGTCNNGIGSCCARGWRS
Protein: DCN1-like protein 5 (DCNL5) (DCUN1 domain-containing protein 5) (Defective in cullin neddylation protein 1-like protein 5) (Squamous cell carcinoma-related oncogene 5) (Q9CXV9)
Organism: Mus musculus (Mouse)
Function: Contributes to the neddylation of all cullins by transferring NEDD8 from N-terminally acetylated NEDD8-conjugating E2s enzyme to different cullin C-terminal domain-RBX complexes which is necessary for the activation of cullin-RING E3 ubiquitin ligases (CRLs). May play a role in DNA damage response and may participate in cell proliferation and anchorage-independent cell growth.
Subcellular location: Nucleus {ECO:0000269|PubMed:29958295}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q9BTE7}. Note=Subcellular localization is independent of the interaction with cullins. {ECO:0000250|UniProtKB:Q9BTE7}.
Interaction partners:
- NEDD8-conjugating enzyme Ubc12
- NEDD8-conjugating enzyme UBE2F
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin-like protein NEDD8
- Cullin-3
- Cullin-2
- Cullin-associated NEDD8-dissociated protein 1
- NEDD8-activating enzyme E1 regulatory subunit
- E3 ubiquitin-protein ligase RBX1
Sequence:
MPVKKKRKAPGVAAAVAEDAGLKKCKIPSYCRSQPPARLISGEEDFSRKKCLAWFYEYAGPDEVVGPEGMEKFCEDIGVEPENIIMLVLAWKLEAESMGFFTKEEWLKGMTSLQCDCTEKLQSRFDFLRSQLNDISSFKNIYRYAFDFARDKDQRSLDIDTAKSMLALLLGRTWPLFSVFYQYLEQSKYRVMNKDQWYNVLEFSRTVHADLSNYDEDGAWPVLLDEFVEWQKIRQTS
Protein: Proteasome subunit beta (Q9VJJ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU004203}. Nucleus {ECO:0000256|RuleBase:RU004203}.
Interaction partners:
- Proteasome subunit beta type-4
- Proteasome subunit beta
- Proteasome subunit alpha type-5
- Proteasome subunit alpha type-2
- Proteasome subunit alpha type-3
- Proteasome subunit alpha type-4
- Proteasome subunit beta
- Proteasome subunit beta type-3
- Proteasome subunit beta type-1
- Proteasome subunit alpha type-7-1
Sequence:
METLLGIKGPDFVMLAADTTHARSIIVMKEDQNKIHKVSDSLLISTVGESGDTEQFTEFISKNIALYKMRNGYDLSPRESAHFTRKNLAEYLRSRTPYQVFMFVAGYDPNAGPELTFIDYLANALPVNYAGHGYGAIFASSIYDRYWHPNITQAEAYDVFKKCIAEIQKRLVVNLKNFTVAVVDKDGVRDLEPISAASLAA
Protein: Endonuclease V (hEndoV) (EC 3.1.26.-) (Inosine-specific endoribonuclease) (Q8N8Q3)
Organism: Homo sapiens (Human)
Function: Endoribonuclease that specifically cleaves inosine-containing RNAs: cleaves RNA at the second phosphodiester bond 3' to inosine. Active against both single-stranded and double-stranded RNAs. Has strong preference for single-stranded RNAs (ssRNAs) toward double-stranded RNAs (dsRNAs). Cleaves mRNAs and tRNAs containing inosine. Also able to cleave structure-specific dsRNA substrates containing the specific sites 5'-IIUI-3' and 5'-UIUU-3'. Inosine is present in a number of RNAs following editing; the function of inosine-specific endoribonuclease is still unclear: it could either play a regulatory role in edited RNAs, or be involved in antiviral response by removing the hyperedited long viral dsRNA genome that has undergone A-to-I editing (Probable). Binds branched DNA structures.
Subcellular location: [Isoform 1]: Cytoplasm {ECO:0000269|PubMed:23912718, ECO:0000269|PubMed:31703097}. Nucleus, nucleolus {ECO:0000269|PubMed:23139746, ECO:0000269|PubMed:31703097}. Cytoplasm, Stress granule {ECO:0000269|PubMed:27573237}. Note=Relocalizes to cytoplasmic stress granules upon cellular stress where it colocalizes with PABPC1. {ECO:0000269|PubMed:27573237}.; SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm {ECO:0000269|PubMed:31703097}. Nucleus, nucleolus {ECO:0000269|PubMed:31703097}. Cytoplasm, Stress granule {ECO:0000269|PubMed:31703097}. Note=Relocalizes to cytoplasmic stress granules upon cellular stress. {ECO:0000269|PubMed:31703097}.; SUBCELLULAR LOCATION: [Isoform 7]: Cytoplasm {ECO:0000269|PubMed:31703097}. Nucleus, nucleolus {ECO:0000269|PubMed:31703097}. Cytoplasm, Stress granule {ECO:0000269|PubMed:31703097}. Note=Relocalizes to cytoplasmic stress granules upon cellular stress. {ECO:0000269|PubMed:31703097}.
Interaction partners:
- Protoporphyrinogen oxidase
- Oxygen-dependent coproporphyrinogen-III oxidase, mitochondrial
- Uroporphyrinogen-III synthase
- Ferrochelatase, mitochondrial
- Molybdenum cofactor biosynthesis protein 1
- Porphobilinogen deaminase
Sequence:
MALEAAGGPPEETLSLWKREQARLKAHVVDRDTEAWQRDPAFSGLQRVGGVDVSFVKGDSVRACASLVVLSFPELEVVYEESRMVSLTAPYVSGFLAFREVPFLLELVQQLREKEPGLMPQVLLVDGNGVLHHRGFGVACHLGVLTDLPCVGVAKKLLQVDGLENNALHKEKIRLLQTRGDSFPLLGDSGTVLGMALRSHDRSTRPLYISVGHRMSLEAAVRLTCCCCRFRIPEPVRQADICSREHIRKSLGLPGPPTPRSPKAQRPVACPKGDSGESSALC
Protein: Phosphoribosylglycinamide formyltransferase, chloroplastic (EC 2.1.2.2) (5'-phosphoribosylglycinamide transformylase) (GAR transformylase) (GART) (P52422)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Probable phosphoribosylformylglycinamidine synthase, chloroplastic/mitochondrial
- Phosphoribosylamine--glycine ligase, chloroplastic
- AICARFT/IMPCHase bienzyme family protein
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- Formate--tetrahydrofolate ligase
- Serine hydroxymethyltransferase 1, mitochondrial
- Serine hydroxymethyltransferase 5
- Serine hydroxymethyltransferase 4
- Serine hydroxymethyltransferase 3, chloroplastic
Sequence:
MESRVLFSSQFNFPVNSPFKTRETSIAPLTPSRNVLSFSFRSPAERCAMRIVPLVKAASSTPQIVAEVDGSSHEPRRKKLAVFVSGGGSNFRKIHEGCSDGSVNGDVVLLVTNKKDCGGAEYARSNGIPVLVFPKAKREPSDGLSPSELVDVLRKYGVDFVLLAGYLKLIPVELVQAFPKRILNIHPALLPAFGGKGLYGIKVHKAVLESGARYSGPTIHFVNEEYDTGRILAQSAVRVIANDTPEELAKRVLHEEHKLYVEVVGAICEERIKWREDGVPLIQNKQNPDEYY
Protein: GEO07322p1 (MIP15436p) (Pherokine 3, isoform A) (Pherokine 3, isoform B) (Pherokine 3, isoform C) (Putative chemosensory protein CSP2) (RE09339p) (Q9W0X2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- CLIP domain-containing serine protease
- CLIP domain-containing serine protease
Sequence:
MKASLALVFCVCVGLAAAAPEKTYTNKYDSVNVDEVLGNNRVLGNYLKCLMDKGPCTAEGRELKRLLPDALHSDCSKCTEVQRKNSQKVINYLRANKAGEWKLLLNKYDPQGIYRAKHEGH
Protein: ADP-sugar pyrophosphatase (EC 3.6.1.13) (8-oxo-dGDP phosphatase) (EC 3.6.1.58) (Nuclear ATP-synthesis protein NUDIX5) (EC 2.7.7.96) (Nucleoside diphosphate-linked moiety X motif 5) (Nudix motif 5) (hNUDT5) (YSA1H) (Q9UKK9)
Organism: Homo sapiens (Human)
Function: Enzyme that can either act as an ADP-sugar pyrophosphatase in absence of diphosphate or catalyze the synthesis of ATP in presence of diphosphate. In absence of diphosphate, hydrolyzes with similar activities various modified nucleoside diphosphates such as ADP-ribose, ADP-mannose, ADP-glucose, 8-oxo-GDP and 8-oxo-dGDP. Can also hydrolyze other nucleotide sugars with low activity. In presence of diphosphate, mediates the synthesis of ATP in the nucleus by catalyzing the conversion of ADP-ribose to ATP and ribose 5-phosphate. Nuclear ATP synthesis takes place when dephosphorylated at Thr-45. Nuclear ATP generation is required for extensive chromatin remodeling events that are energy-consuming. Does not play a role in U8 snoRNA decapping activity (By similarity). Binds U8 snoRNA (By similarity).
Subcellular location: Nucleus {ECO:0000305|PubMed:27257257}.
Interaction partners:
- ADP-ribose pyrophosphatase, mitochondrial
- Phosphopentomutase
- Ribose-phosphate pyrophosphokinase 1
- Ribose-phosphate pyrophosphokinase 2
- Ribose-phosphate pyrophosphokinase 3
- Manganese-dependent ADP-ribose/CDP-alcohol diphosphatase
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Nucleotide triphosphate diphosphatase NUDT15
- Pyrroline-5-carboxylate reductase 2
- 8-oxo-dGDP phosphatase NUDT18
Sequence:
MESQEPTESSQNGKQYIISEELISEGKWVKLEKTTYMDPTGKTRTWESVKRTTRKEQTADGVAVIPVLQRTLHYECIVLVKQFRPPMGGYCIEFPAGLIDDGETPEAAALRELEEETGYKGDIAECSPAVCMDPGLSNCTIHIVTVTINGDDAENARPKPKPGDGEFVEVISLPKNDLLQRLDALVAEEHLTVDARVYSYALALKHANAKPFEVPFLKF
Protein: Prolyl 3,4-dihydroxylase TPA1 (EC 1.14.11.-) (Termination and polyadenylation protein 1) (uS12 prolyl 3,4-dihydroxylase) (P40032)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Prolyl 3,4-dihydroxylase that catalyzes 3,4-dihydroxylation of 'Pro-64' of small ribosomal subunit uS12 (RPS23A and RPS23B), thereby regulating protein translation termination efficiency. Part of a messenger ribonucleoprotein (mRNP) complex at the 3'-UTR of mRNAs. It associates specifically with components of the translation termination complex and is involved in both translation termination and in regulation of normal mRNA decay through translation termination-coupled poly(A) shortening.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Enhancer of translation termination 1
- Polyadenylate-binding protein, cytoplasmic and nuclear
- Eukaryotic peptide chain release factor GTP-binding subunit
- Elongation factor Tu, mitochondrial
- Eukaryotic peptide chain release factor subunit 1
- Elongation factor 3A
- tRNA
Sequence:
MKRKTAEVKGEKERNSKQISLEEDKIKGMFNPKIWDKTFQDGLKKEIEDSQPYNWGTIHELVNDDLLRAVRKEIETEIHFTKKETDIYRVNQSGDLANLSGLDWDDLSRLPNLFKLRQILYSKQYRDFFGYVTKAGKLSGSKTDMSINTYTKGCHLLTHDDVIGSRRISFILYLPDPDRKWKSHYGGGLRLFPSILPNVPHSDPSAKLVPQFNQIAFFKVLPGFSFHDVEEVKVDKHRLSIQGWYHIPQVGEEGYIPGEEEAWVRNNTSTLAQIESNVLEDFEFPKDERNILSFHEVKHFEKMLKGDAGAKTDNTPKESMTSVISDSVKLSEAEFTYLSQYISPEHLSSKGIEKLQKQFVENSSLQIESFLNDDKSELLKKVIKQKELEQECPYHSKDVKAPWKTAIPPHKARYLYIDGKEYRNFQTEADILEALNNNDLPNFQFTKDAIKIISDASGNSRENNFDAELALIDLAVFHKSTIFKKYLALLTSLCPVSEQILIRRFRPGMDFTLATKCRFNELLKSNPDIIDAVLEGTLCLTPSAGWESGELGGYELYMMDDDEDNKQYLKEDVEDASVYRADDSGDSVLINDPPAWNTFNLVLRDESVLEFVKYVSWSAKSSRWDVKMKWDVKSCDEDGQEDEA