wanglab/gogpt-training-data huggingface dataset:
Protein: La-related protein 7 (La ribonucleoprotein domain family member 7) (Q05CL8)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that specifically binds distinct small nuclear RNA (snRNAs) and regulates their processing and function. Specifically binds the 7SK snRNA (7SK RNA) and acts as a core component of the 7SK ribonucleoprotein (RNP) complex, thereby acting as a negative regulator of transcription elongation by RNA polymerase II (By similarity). The 7SK RNP complex sequesters the positive transcription elongation factor b (P-TEFb) in a large inactive 7SK RNP complex preventing RNA polymerase II phosphorylation and subsequent transcriptional elongation (By similarity). The 7SK RNP complex also promotes snRNA gene transcription by RNA polymerase II via interaction with the little elongation complex (LEC) (By similarity). LARP7 specifically binds to the highly conserved 3'-terminal U-rich stretch of 7SK RNA; on stimulation, remains associated with 7SK RNA, whereas P-TEFb is released from the complex (By similarity). LARP7 also acts as a regulator of mRNA splicing fidelity by promoting U6 snRNA processing. Specifically binds U6 snRNAs and associates with a subset of box C/D RNP complexes: promotes U6 snRNA 2'-O-methylation by facilitating U6 snRNA loading into box C/D RNP complexes. U6 snRNA 2'-O-methylation is required for mRNA splicing fidelity. Binds U6 snRNAs with a 5'-CAGGG-3' sequence motif (By similarity). U6 snRNA processing is required for spermatogenesis.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:32017896}.
Interaction partners:
- 7SK snRNA methylphosphate capping enzyme
- Protein HEXIM1
- Protein HEXIM2
- Cyclin-dependent kinase 9
- Cyclin-T1
- Cell growth-regulating nucleolar protein
- U3 small nucleolar ribonucleoprotein protein MPP10
- Cyclin-T2
- Bromodomain-containing protein 4
- La-related protein 4B
Sequence:
METENQKTMEESTKRKEEKKKRSRVKQVLADIAKQVDFWFGDANLHKDKFLREQIEKSRDGYVDISLLVSFNKMKKLTTDGKLIARALKSSSVVELDLEGTRIRRKKPLGERPKDEEERTVYVELLPKNVTHSWIERVFGKCGNVVYISIPHYKSTGDPKGFAFVEFETKEQAAKAIEFLNNPPEEAPRKPGIFPKTVKNKPIPSLRVAEEKKKKKKKKGRIKKEESVQAKESAVDSSSSGVCKATKRPRTASEGSEAETPEAPKQPAKKKKKRDKVEASSLPEARAGKRERCSAEDEDCLPPRPKAKKRAQKDGVGQAASEVSKESRDLEFCSTEEEKETDRKGDSLSKVKRKHKKKHKERHKMGEEVIPLRVLSKTEWMDLKKEYLALQKASMASLKKTISQIKLESEMETDCKAPTAGSGQECSTQEKVSAQGPQFVTGVIVKIVSGEPLPGRKQVKDILATISEVVYIDLLEGDTECHARFKTPEDAQAVMNAQTEIRKKHSWNLEVLSGDHEQRYWQKILVDRQAKLNQPREKKRGTEKLITKAEKIRLAKTQQASQHIRFSEYD
Protein: Polyadenylate-binding protein-interacting protein 8 (PABP-interacting protein 8) (Poly(A)-binding protein-interacting protein 8) (PAM2-containing protein CID8) (Protein CTC-INTERACTING DOMAIN 8) (Q9C8M0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Polyadenylate-binding protein-interacting protein 7
- Polyadenylate-binding protein-interacting protein 5
- Polyadenylate-binding protein-interacting protein 6
- Splicing factor, CC1-like protein
- Polyadenylate-binding protein-interacting protein 2
- At4g35785 family protein)
- Polyadenylate-binding protein-interacting protein 4
- Polyadenylate-binding protein-interacting protein 3
- U11/U12 small nuclear ribonucleoprotein 35 kDa protein
- THO complex subunit 4A
Sequence:
MAAITEMATDSNDVINDGGTGDGIEKSTDSKPEIESDDLKPKSKPEYDQMKKLVAMFKKLNPEAKEFFPSYKRNTNQSDDFVIAIKPSGEDNKKVAINRRRRNNYNQGRRVRLPGRASKAQREDSIRRTVYVSDIDQSVTEEGLAGLFSSCGQVVDCRICGDPNSVLRFAFVEFSDDQGARSALSLGGTMIGYYPVRVLPSKTAILPVNPTFLPRSEDEREMCSRTIYCTNVDKNATEDDVNTFFQSACGEVTRLRLLGDQVHSTRIAFVEFAMAESAVAALNCSGIVLGSQPIRVSPSKTPVRSRITRSPSPN
Protein: Syntaxin-8 (Syntaxin-like protein 3I35) (O88983)
Organism: Mus musculus (Mouse)
Function: Vesicle trafficking protein that functions in the early secretory pathway, possibly by mediating retrograde transport from cis-Golgi membranes to the ER.
Subcellular location: Membrane {ECO:0000250}; Single-pass type IV membrane protein {ECO:0000250}. Note=Preferentially associated with the early endosome. To a lesser extent, also present in late endosome, the plasma membrane and coated pits (By similarity). {ECO:0000250}.
Interaction partners:
- Vesicle-associated membrane protein 8
- Vesicle transport through interaction with t-SNAREs homolog 1B
- Syntaxin-7
- Vesicle-associated membrane protein 7
- Vesicle transport through interaction with t-SNAREs homolog 1A
- Syntaxin-16
- Synaptobrevin homolog YKT6
- Syntaxin-12
- Syntaxin-5
- Vesicle-associated membrane protein 4
Sequence:
MAPDPWFSTYDSTCQIAQEIAEKIQERNQCERRGEKTPKLTLTIRTLLKNLKVKIDLLKDLLLRAVSTRQITQLEGDRRQNLLDDLVTRERLLLASFKNEGAEPDLIRSSLMSEEAKRGTPNPWLCEEPEETRGLGFDEIRQQQQKIIQEQDAGLDALSSIISRQKQMGQEIGNELDEQNEIIDDLANLVENTDEKLRTEARRVTLVDRKSTSCGMIMVILLLLVAIVVVAVWPTN
Protein: Probable folylpolyglutamate synthase (EC 6.3.2.17) (Folylpoly-gamma-glutamate synthetase) (FPGS) (Tetrahydrofolylpolyglutamate synthase) (Tetrahydrofolate synthase) (P36001)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Conversion of folates to polyglutamate derivatives.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14576278}.
Interaction partners:
- Folic acid synthesis protein FOL1
- Dihydrofolate reductase
- Dihydrofolate synthetase
- Folylpolyglutamate synthase
- C-1-tetrahydrofolate synthase, cytoplasmic
- C-1-tetrahydrofolate synthase, mitochondrial
- Thymidylate synthase
- GTP cyclohydrolase 1
- Aminodeoxychorismate synthase
- Methylenetetrahydrofolate dehydrogenase [NAD
Sequence:
MDDISGRQTLPRINRLLEHVGNPQDSLSILHIAGTNGKETVSKFLTSILQHPGQQRQRVLIGRYTTSSLLNAKEEDISINNEAISLIEYSRIEKELIEADSSLKLQCNNLELLTSVALVYFAKKNCQWCIIETGLAGKQDPGSIIAGQSRVCCAITNVGISDEAFLCKFLSQITESSTNKAIFLLDGSNDEFVRNTITKRCHDVGCPLEITDPSLRDYNVHTDTWGTLEVRLPYSEEEYQIFNLRVAIAVLDFLSKEKKVCISKDQLSQGLISVDWPRSLHRLDYCYESTSGKKIALLLDNANNAKAARNLACHLRTTYGDTPLTFVIAITTGKKVSPLLDPLIRPQDYVIVTRFGSVVGMPWIQSLEPVNLLAFIKNRYTRNVNMQPDLQSVWTFLETSGLKTIVPVIVCGSLYICKELLRLHNCHLPV
Protein: Protein tyrosine phosphatase CRYP-2 (Q98945)
Organism: Gallus gallus (Chicken)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MLPQFAIAGHASEPGGGRRGAAARGRGAEEPQPPPPGRSRGRGRRAPRCPTAAGGARGGPGARSCLLWLFVLLKNAEPFQVTVQEDNCIVVSLEASDVVSSSSVYVVKIAGESKNYFFQFEEFNSTLPAPVIFNAKYHGLYYIVTLLVVNSNMVSKSARSITVLTKPLPVSSVSIYDYKPSPETGVLFEIQYPEKYNVFTRVNISYWEGKDYRTMLYKDFFKGKTVFNHWLPGICYSNITFQLVSEATFNKSTLVEYSGVRHEPKQHRTVPYPPRNISVQIVPINRNNWEEHSGNFAEESFMGQQEIISKEKLSRFPSDPPEIPVVNTTAAWPDYRSNSTEYETTSQPYWWSNEAESSEGEEEFVNAVPRDYGASEANASGKLTAEPAPFLPVQMVLTWLPPKPPTAFDGFHINIEREENSTELLTVSEDTHKFVAELKEPGKYKLSVTTFSSSGSCEVRGSQSAKTLSFYISPTGEWIEELTEKPQHVTVTVLSSTTALTSWTASHESGSNGTIVSVVSLTCQKQKESQRLEKHYCTEVNSSSSLIENLVPGAQYQVVVYLRKGPLVGPPSDPVTFSIVPTGIKDLTLYPLGPTAVVLSWNRPFLGVFRKYVVEMFYFNPSTMTSEWTTYYEIAATISLTASVRIANLLPAWYYNFRVTMVTWGDPELSCCDSSTISFITAPVAPEITSIEYYNHLLYVTWTYGGDGTDLSHSRMLHWMVIAEGKKKIKKSVTRSVMTAVLSLPPGDIYNLSVTACTERGSNTSLPQLVKLEPAPPKSLFAVNKTQTSVTLLWVEEGVADFFEVYCQQAGSNQEVKVQEPVTVSSHVVTISSLTPATSYNCSVTTFSHNSPSVPTYIAVSTMVTEMNPNIVVISVLAILSILLIGLLLVTLVVLRRKHLQMARECGAGTFVNFASLERDGKLPYNWRRSVFAFLTLLPSCLWTDYLLAFYINPWSKNGLKKRKLTNPVQLDDFDGYIKDMAKDSDYKFSLQFEELKLIGLDIPHFAADLPMNRCKNRYTNILPYDFSRVRLVSMNEEEGSDYINANYIPGYNSPQEYIATQGPLPETRNDFWKMVLQQKSQIIVMLTQCNEKRRVKCDHYWPFTEDPIAYGDITVEMLSEEEHTDWVYRNFRISYADEVQDVMHFNYTAWPDHGVPTANAAESILQFVQMVRQKSVKSKGPMIIHCSAGVGRTGTFIALDWLLQHIRDHEFVDILGLVSDMRSYRMSMVQTEEQYIFIHQCVQLMWQKKKQQFCISDVIYENVSKS
Protein: Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)] (P04578)
Organism: Human immunodeficiency virus type 1 group M subtype B (isolate HXB2) (HIV-1)
Function: Oligomerizes in the host endoplasmic reticulum into predominantly trimers. In a second time, gp160 transits in the host Golgi, where glycosylation is completed. The precursor is then proteolytically cleaved in the trans-Golgi and thereby activated by cellular furin or furin-like proteases to produce gp120 and gp41.
Subcellular location: [Surface protein gp120]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=The surface protein is not anchored to the viral envelope, but associates with the extravirion surface through its binding to TM. It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.; SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_04083}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04083}. Note=It is probably concentrated at the site of budding and incorporated into the virions possibly by contacts between the cytoplasmic tail of Env and the N-terminus of Gag. {ECO:0000255|HAMAP-Rule:MF_04083}.
Interaction partners:
Sequence:
MRVKEKYQHLWRWGWRWGTMLLGMLMICSATEKLWVTVYYGVPVWKEATTTLFCASDAKAYDTEVHNVWATHACVPTDPNPQEVVLVNVTENFNMWKNDMVEQMHEDIISLWDQSLKPCVKLTPLCVSLKCTDLKNDTNTNSSSGRMIMEKGEIKNCSFNISTSIRGKVQKEYAFFYKLDIIPIDNDTTSYKLTSCNTSVITQACPKVSFEPIPIHYCAPAGFAILKCNNKTFNGTGPCTNVSTVQCTHGIRPVVSTQLLLNGSLAEEEVVIRSVNFTDNAKTIIVQLNTSVEINCTRPNNNTRKRIRIQRGPGRAFVTIGKIGNMRQAHCNISRAKWNNTLKQIASKLREQFGNNKTIIFKQSSGGDPEIVTHSFNCGGEFFYCNSTQLFNSTWFNSTWSTEGSNNTEGSDTITLPCRIKQIINMWQKVGKAMYAPPISGQIRCSSNITGLLLTRDGGNSNNESEIFRPGGGDMRDNWRSELYKYKVVKIEPLGVAPTKAKRRVVQREKRAVGIGALFLGFLGAAGSTMGAASMTLTVQARQLLSGIVQQQNNLLRAIEAQQHLLQLTVWGIKQLQARILAVERYLKDQQLLGIWGCSGKLICTTAVPWNASWSNKSLEQIWNHTTWMEWDREINNYTSLIHSLIEESQNQQEKNEQELLELDKWASLWNWFNITNWLWYIKLFIMIVGGLVGLRIVFAVLSIVNRVRQGYSPLSFQTHLPTPRGPDRPEGIEEEGGERDRDRSIRLVNGSLALIWDDLRSLCLFSYHRLRDLLLIVTRIVELLGRRGWEALKYWWNLLQYWSQELKNSAVSLLNATAIAVAEGTDRVIEVVQGACRAIRHIPRRIRQGLERILL
Protein: N-myc-interactor (Nmi) (N-myc and STAT interactor) (O35309)
Organism: Mus musculus (Mouse)
Function: Acts as a signaling pathway regulator involved in innate immune system response. In response to interleukin 2/IL2 and interferon IFN-gamma/IFNG, interacts with signal transducer and activator of transcription/STAT which activate the transcription of downstream genes involved in a multitude of signals for development and homeostasis (By similarity). Enhances the recruitment of CBP/p300 coactivators to STAT1 and STAT5, resulting in increased STAT1- and STAT5-dependent transcription (By similarity). In response to interferon IFN-alpha, associates in a complex with transcriptional regulator IFI35 to regulate immune response; the complex formation prevents proteasome-mediated degradation of IFI35 (By similarity). In complex with IFI35, negatively regulates nuclear factor NF-kappa-B signaling by inhibiting the nuclear translocation, activation and transcription of NF-kappa-B subunit p65/RELA, resulting in the inhibition of endothelial cell proliferation, migration and re-endothelialization of injured arteries (By similarity). Negatively regulates virus-triggered type I interferon/IFN production by inducing proteosome-dependent degradation of IRF7, a transcriptional regulator of type I IFN, thereby interfering with cellular antiviral responses. Beside its role as an intracellular signaling pathway regulator, also functions extracellularly as damage-associated molecular patterns (DAMPs) to promote inflammation, when actively released by macrophage to the extracellular space during cell injury or pathogen invasion (By similarity). Macrophage-secreted NMI activates NF-kappa-B signaling in adjacent macrophages through Toll-like receptor 4/TLR4 binding and activation, thereby inducing NF-kappa-B translocation from the cytoplasm into the nucleus which promotes the release of pro-inflammatory cytokines (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q13287}. Nucleus {ECO:0000250|UniProtKB:Q13287}. Secreted {ECO:0000250|UniProtKB:Q13287}. Note=Cytoplasmic NMI localizes in punctate granular structures. Nuclear localization increased following IFN-alpha treatment. Extracelullar following secretion by macrophage. {ECO:0000250|UniProtKB:Q13287}.
Interaction partners:
- Interferon-induced 35 kDa protein homolog
- N-myc proto-oncogene protein
- Signal transducer and activator of transcription 2
- Histone acetyltransferase KAT5
- Signal transducer and activator of transcription 1
- Myc proto-oncogene protein
Sequence:
MDADKDNIKQACDERSAEMDDMRGEQSMGLVHEIMSENKELDEEIKKLEAELQSDAREFQIKENVPEKKLKLTSVESPKDGCHFSNSSCSFQVSSQILYELQEGQALITFEKEEVAQNVISMGNHVVQMEGTPVKVSAHPVPLNTGVRFQVHVDISKMKINVTGIPDELSEEQTRDKLELSFCKSRNGGGEVESVDYDRKSRSAVITFVETGVVDKILKKKTYPLYMNQKCHSVAVSPCIERCLEKYQVFSAVSKKTVLLTGLEGIPVDEETGEDLLNIHFQRKNNGGGEVEVVKCSLDQSFAAYFKEEARETI
Protein: Cyclops (Nodal-related 2 precursor) (Znr-1) (P87358)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MHALGVARLACYCQLLLLGVFGKHTRYRHNNYNSLRNMSHRMHLPTYMMHLYRHYKMNQTRIPAESLEHEHADTIRSIMSKNVLNNDNHYVAIFDLSPVLSERQIQAAELRIRVPRDLHPDGLTLELQHQQGAPCPRHQPCPKSQSLGLLPEESLLSVTQHWRVYNVTNLLLHWPRPRTSPRSRVKTKRPAAAPGGKEIHSGPRRPAAAPGGQELQRRPRRPAVAPEEQELPSRPRRPAVAPGAQELQSGPQRPAAAPGGQKIQNRPRRPSAAPKGQEVQSRPSRPATAPRGQELQSAPQRPVVAPGGREIHSRPWLPAATPGGQEIQNGTQKHRAMLLLFSEQQDGASLLHTAGASKFLFSRNKKEVKRGRALRSRRGRRGPPVRSPELQRTPLHKSTTCRRVDMHVDFNQIGWGSWIVFPKKYNAYRCEGACPNPLGEELRPTNHAYMQSLLKYHHPSRVPASCCAPTRTSALSMLYYENGEMILRHHEDMQVEECGCL
Protein: Mitogen-activated protein kinase (EC 2.7.11.24) (Q8TG19)
Organism: Gibberella zeae (Wheat head blight fungus) (Fusarium graminearum)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGDLQGRKVFKVFNQDFVVDERYTVTKELGQGAYGIVCAAVNNQTNEGVAIKKVTNVFSKKILAKRALREIKLLQHFRGHRNITCLYDMDIPRPDNFNETYLYEELMECDLAAIIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLARGFSVDPEENAGYMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGGRPFFKGRDYVDQLNQILHILGTPNEETLSRIGSPRAQEYVRNLPFMPKKPFPSLFPQANPDALDLLDKMLAFDPSSRISVEQALEHPYLQIWHDASDEPDCPTTFNFDFEVVEDVGQMRGMILDEVQRFRQNVRTVPGQSGGGLQGQGVPVPLPQGNGQWTAEDPRPQEYAGHGNTGLEQDLQGGLDASRR
Protein: Oligosaccharide 4-alpha-D-glucosyltransferase (EC 2.4.1.161) (Alpha-glucosidase 31B) (CJAgd31B) (B3PEE6)
Organism: Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Function: Alpha-transglucosylase that specifically transfers single glucosyl units from alpha(1->4)-glucans to the non-reducing terminal 4-OH of glucose and alpha(1->4)- and alpha(1->6)-linked glucosyl residues. Acts on amylose, amylopectin, glycogen and maltooligosaccharides, with the highest activity with maltotriose as a donor, and also accepts maltose. Does not act as a hydrolase: weak hydrolysis activity is only observed on the disaccharide maltose.
Interaction partners:
- 4-alpha-glucanotransferase
Sequence:
MFRRIAGFSPIFLMLFGSSLPTMGNPVKREIHPDAVFYKEHKLRNDGLVITTNQGNIRLQFKSEAAIEVLYRADSKQLPSFALAQPESAIKAQLTETENHLQFSGGTLTARIQKRPFAISYYRDSELLLAEESGFQVNTDKINFRFYLSPGEKILGGGQRILGMDRRGQRFPLYNRAHYGYSDHSGQMYFGLPAIMSSKQYILVFDNSASGAMDIGKTESDILQLEAKSGRSAYILVAGNSYPSLIENFTQVTGRQPLPPRWALGSFASRFGYRSEAETRATVQKYKTEDFPLDTIVLDLYWFGKDIKGHMGNLDWDKENFPTPLDMMADFKQQGVKTVLITEPFVLTSSKRWDDAVKAKALAKDPQGQPKAFELYFGNGGIIDVFSKEGSRWFSSIYKDLSKQGVAGWWGDLGEPEMHPEDTQHAIGDADTVHNAYGHRWAEMLYQQQLDQFPELRPFIMMRAGFVGSQRYGMIPWTGDVSRTWGGLASQVELALQMSLLGFGYIHSDLGGFADGETLDKEMYIRWLQYGVFQPVYRPHGQDHIPSEPVFQDEETKAILRPLVKLRYRMLPYIYTAAYQNTLTGMPLMRPLFFSDEKNPALIDNKTSYFWGDSLLVTPITQAGVESVSIPAPKGVWFDFWKDTRYQTDGAPLTLPTDLHTIPVLVKAGAFMPYVPAVSTTEDYRSDSLEIHYYADASVPLAQGEIFEDDGKDPNSIKRNQFDLLTLQATHTDNQLHFQLARTGKGYRGMPERRATTLVIHNASDQYQHLDINGKTIAIAQADCASTPALACYDQERRQLQLVFTWGREALNLRLH
Protein: Nucleolar complex-associated protein 3 (AtNOC3) (F4IDJ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be required for synthesis of 60S ribosomal subunits and the transport of pre-ribosomes from the nucleoplasm to the cytoplasm (By similarity). Also required for initiation of DNA replication.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768}. Nucleus, nucleolus {ECO:0000269|PubMed:30338215}. Nucleus, nucleoplasm {ECO:0000269|PubMed:30338215}. Note=Also observed in nucleoplasmic bodies. {ECO:0000269|PubMed:30338215}.
Interaction partners:
- Ribosome biogenesis protein BOP1 homolog
- Nucleolar complex-associated protein 2
- Protein REBELOTE
- Ribosome biogenesis protein WDR12 homolog
- AT5g04600/T32M21_200
- Protein MAK16 homolog
- Protein SLOW WALKER 2
- Pescadillo homolog
- Probable rRNA-processing protein EBP2 homolog
- 60S ribosome subunit biogenesis protein NIP7 homolog
Sequence:
MGKNRRKQKVIPPPLLPPDVAEEDIEFSDEDLKYVKENTDYAQFVSQIDTAAINKQCGGRVMTVEDKYEEERSKRKTLQEEKGNGEILVDPVDVLPVKTLDGKLHYRTESKKSKLAEAETDEAEKDVLEDEHVLNKSQRREKAKKSKREAKKHEKDLPDEILQEEEETPQAAVLAEVKEELSAEESFENKKNKIAELGMLLLSDPEANIKTLKDMLDICKDQNTKIVKLALLSLLAVFKDIIPGYRIRLPTEKELEMKISKEVKKTRFYESTLLKAYKSYLQKLIIFEKQSVYNQIANRCLCTLLEAVPHFNYRDNLLIAVVRNISSPDEVVRRLCCSTIRYLFSNEGKHGGELTVQAVRLIADHVKAHNCQLHPNAIEVFMSIRFDEDIGKPNKEDEHNKKYKKNNKRKTQEEQNQVQENERKKSKKDMMSKIRDEVSADHRGVTYEPDAKERRKMQTETLSAVFETYFRILRNTMYTIGERTEEIPTSNPGAFGSHPLLAPCLDGLAKFTQQLDLDYMGDLMNYLKKLASSSSSVSNNTKQKNSKLLTVSERLRCCLVAFKVMRSNLNALNVDLQDFFVQLYNLILEYRPGRDSGVILAESLKIMLCDDRHQDMQKAAAFVKRLATFALCFGCAESMSALVTLKTLLQKNVKCRNLLENDAGGGSVSGSIAKYQPYATDPNLSGALATVLWELSLLSKHYHPAISTMATTVSNMNTSQSQTFLSAVTPQQAFADFSLVKESFEPKNESRKLNNKRKRESLPEEAKNVPEIDMVKLSKKLKENFTILRDIKEDERVRMELLQSEEKKPLKKQNNVVKKKLKNPKSKKQI
Protein: Sorting nexin-7 (Q9UNH6)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of endocytosis and in several stages of intracellular trafficking. Together with SNX4, involved in autophagosome assembly by regulating trafficking and recycling of phospholipid scramblase ATG9A.
Subcellular location: Early endosome membrane {ECO:0000269|PubMed:32513819}; Peripheral membrane protein {ECO:0000250|UniProtKB:O95219}; Cytoplasmic side {ECO:0000250|UniProtKB:O95219}.
Interaction partners:
- Sorting nexin-4
- Biogenesis of lysosome-related organelles complex 1 subunit 2
- Sorting nexin-6
- Sorting nexin-32
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 29
Sequence:
MDMNSFSPMMPTSPLSMINQIKFEDEPDLKDLFITVDEPESHVTTIETFITYRIITKTSRGEFDSSEFEVRRRYQDFLWLKGKLEEAHPTLIIPPLPEKFIVKGMVERFNDDFIETRRKALHKFLNRIADHPTLTFNEDFKIFLTAQAWELSSHKKQGPGLLSRMGQTVRAVASSMRGVKNRPEEFMEMNNFIELFSQKINLIDKISQRIYKEEREYFDEMKEYGPIHILWSASEEDLVDTLKDVASCIDRCCKATEKRMSGLSEALLPVVHEYVLYSEMLMGVMKRRDQIQAELDSKVEVLTYKKADTDLLPEEIGKLEDKVECANNALKADWERWKQNMQNDIKLAFTDMAEENIHYYEQCLATWESFLTSQTNLHLEEASEDKP
Protein: Histone H2B type 1-N (Histone H2B.d) (H2B/d) (Q99877)
Organism: Homo sapiens (Human)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus. Chromosome.
Interaction partners:
- Histone H2A type 1-C
- Histone H4
- Histone H3.2
- Histone H3-like centromeric protein A
- Histone H2A type 1-D
- Histone H2A.J
- Centromere protein N
- Histone H2B type 1-O
- Histone H3.1t
- Histone H2A
Sequence:
MPEPSKSAPAPKKGSKKAVTKAQKKDGKKRKRSRKESYSVYVYKVLKQVHPDTGISSKAMGIMNSFVNDIFERIAGEASRLAHYNKRSTITSREIQTAVRLLLPGELAKHAVSEGTKAVTKYTSSK
Protein: Transcription activator, putative (Q585S8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- FYR C-terminal domain-containing protein
- Histone H3 variant
- Histone H3, putative
- Histone H2A
- Transcription factor CBF/NF-Y/archaeal histone domain-containing protein
- Histone H4
- Histone H4
- NOT1
- Histone H2A
- Transcription factor CBF/NF-Y/archaeal histone domain-containing protein
Sequence:
MEAPAGRSIRQRQDLQTTSSVDRHVKDLSAIELYEQILLGCIRAGDDPNAAVKIEHFEGYVEPTFDLLHGAHVVAHQRQRLSDIYHEREHIIGTLRASPEHQQRNAFDRLLLETEYWTGLREWNETTRSGSGDTTRGRLRRRLEATVGGKGGSEGMESEMLHLTESPSYIRGKLRPYQIEGVNWLLGLYSRCINGILADEMGLGKTLQTISTLAYLKFSHGLPGPHLVVCPKSVMGNWYREVRQWCPALSVLKFHCSSNIRPQLVRAHLMPCGNIKYDIIVTTFEMVLEEHGAFRKIPWQYLIVDEAHKLKNEEGRAHVTLGSINANYRLIITGTPLQNNLKELWALLHFLTPRLFDDSKSFDSWFDTASGQEDSEALSNMHQILAPLMIRRLKSEVSTGIPPKKEIYVSCRLSKVQRRWYMQVLAKDAEVLNKGSGGSSAFLTNTLMSLRKVINHPYMMDGGEEGPPFITDERIVKYSGKMLLLDKLLHRLRRDEKEGHKVLIFSQFTSMLDILEDYCSMRGFKVCRIDGSTSGYDRDSQMAAFNAPKSDYFIFLLSTRAGGLGINLQAANNVIIYDSDWNPQMDLQAQDRAHRIGQKRVVRVYRFVTDGTVEERIYHRALKKLYLDAMVVQQGRASGGGNGNNLSREELLSMIKFGAEEIFKAKDEDITEADIDCLFDDDRKSRELNDAVRQQVQMSLASFKLGADETNIYDFEGVSFREGVESRLLHITLSDPVSQDELHKQCSQFGDVIKVVLHTNLKEALASFRTTAGAMDAKDGLPYKCEFASKEARRVVPKEIITEYYNTEEKLGRGHRQREPVQFYTEEEVETIQKQKKGPPLKLPRAPQFKSHQLFNMKRLLELHATEVSLMVRNWERGINGTGNGTSGTGNGGADENTDHVKDAGNEVVGAEEKRNKDEGNNETTKVEERDDVKETSKQEGNGEVETGVEEETLTAVEREERERLMKEGFPDWTINEYRTLVGVITSGSVDISDYPAITAAVNARRCNKTVEEVRKYLTALLERGSQYIKNFARVEERIQRMQERRKAQEDELRAAKWKVESYEDPETQLTFKGRCNDDFDRKLFLMAYDVGFARQNWETFIRRMPESRFDVWLQSRDSGYCERRLRGLKAAVKREWQPPNDEDTEVVGRRRRLERKFPE
Protein: Gamma-L-glutamyl-butirosin B gamma-glutamyl cyclotransferase (EC 4.3.2.6) (Butirosin biosynthesis protein G) (Q4H4F0)
Organism: Niallia circulans (Bacillus circulans)
Function: Cyclotransferase that catalyzes the last step in the biosynthesis of the aminoglycoside antibiotic butirosin B. Cleaves the amide bond via transamidation using the alpha-amine of the terminal gamma-L-glutamate of the side chain, releasing it as the cyclic 5-oxoproline.
Interaction partners:
Sequence:
MISWTKAFTKPLKGRIFMPNLFVYGTLREGENNHKYMKEATLLSRKASIAGSLVDTGNGYPGLLLENQLVAGEWYEVSEETLKRIDELEEYFGPGDTRNLFDRIECQVNESGGTHLGWTYVYNRDDYLETRFSDWKQYRLQHASGIEEKQDVPHSL
Protein: Cytochrome P450 98A8 (EC 1.14.-.-) (p-coumarate 3-hydroxylase) (Q9CA61)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts redundantly with CYP98A9 as tricoumaroylspermidine meta-hydroxylase. Catalyzes also the meta-hydroxylation of the three triferuloylspermidine phenolic rings. Unable to use 5-O-(4-coumaroyl) D-quinate or 5-O-(4-coumaroyl) shikimate as substrates.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Tapetum-specific methyltransferase 1
- Cytochrome P450 98A9
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- Probable caffeoyl-CoA O-methyltransferase At4g26220
- Cinnamoyl-CoA reductase 1
- Cinnamoyl-CoA reductase 2
- Shikimate O-hydroxycinnamoyltransferase
- Phenylalanine ammonia-lyase 4
- Phenylalanine ammonia-lyase 3
- Phenylalanine ammonia-lyase 2
Sequence:
MIIYLISLLPIIVATLMLYQRWWRSNIPPGPKPKFLLGNLHQMKPLWTHSFSEWSETYGPIISVWIGSQLTVVVSSSDLARQVLRDKDHQLSNRHRIARMTQTGTDLVWSDYSPHYVKLRKLCTLELFSLKSIENFRSLREMEARSMVVSILKDLMSNSGDDQERKPVIVRKYLAAVVLNTISRLMIGKEFGSEEGKEFKAIVEKEHLLSGSGTILDHVWWLKWVSSWFFSDKEFLAHKDRRTKWFRGAIMVEEDIEIEDHRGFVRKLLVLKEQKELSEETVGGLVWNMLTAGADTTAVVIEWAMAEMIKCPTVQEKAQQELDSVVGSERLMTESDIPILPYLQCVVKEALRLHPSTPLMLPHKASETVWVGGYKVPKGATVYVNVQAIGRDPANWINPYEFRPERFLQEETDVKGRDFRVLPFGSGRRMCPAAQLSMNLMTLVMGNLLHCFSWSSPVPGERIDMSENPGLLCNMRTPLQALALPRAAARAIPLPLD