wanglab/gogpt-training-data huggingface dataset:
Protein: Dual specificity protein kinase CLK2 (EC 2.7.12.1) (CDC-like kinase 2) (P49760)
Organism: Homo sapiens (Human)
Function: Dual specificity kinase acting on both serine/threonine and tyrosine-containing substrates. Phosphorylates serine- and arginine-rich (SR) proteins of the spliceosomal complex. May be a constituent of a network of regulatory mechanisms that enable SR proteins to control RNA splicing and can cause redistribution of SR proteins from speckles to a diffuse nucleoplasmic distribution. Acts as a suppressor of hepatic gluconeogenesis and glucose output by repressing PPARGC1A transcriptional activity on gluconeogenic genes via its phosphorylation. Phosphorylates PPP2R5B thereby stimulating the assembly of PP2A phosphatase with the PPP2R5B-AKT1 complex leading to dephosphorylation of AKT1. Phosphorylates: PTPN1, SRSF1 and SRSF3. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Phosphorylates PAGE4 at several serine and threonine residues and this phosphorylation attenuates the ability of PAGE4 to potentiate the transcriptional activator activity of JUN.
Subcellular location: Nucleus {ECO:0000269|PubMed:28289210}.; SUBCELLULAR LOCATION: [Isoform 1]: Nucleus {ECO:0000269|PubMed:9637771}. Nucleus speckle {ECO:0000269|PubMed:9637771}. Note=Inhibition of phosphorylation at Ser-142 results in accumulation in the nuclear speckle. {ECO:0000250|UniProtKB:O35491}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus speckle {ECO:0000269|PubMed:9637771}. Note=Co-localizes with serine- and arginine-rich (SR) proteins in the nuclear speckles. {ECO:0000269|PubMed:9637771}.
Interaction partners:
- Arginine/serine-rich protein 1
- Dual specificity protein kinase CLK3
- Bcl-2-associated transcription factor 1
- Dual specificity protein kinase CLK1
- E3 ubiquitin-protein ligase RBBP6
- Smad nuclear-interacting protein 1
- Platelet-activating factor acetylhydrolase IB subunit alpha1
- Apoptotic chromatin condensation inducer in the nucleus
- Serine/arginine-rich splicing factor 12
- Serine/arginine-rich splicing factor 8
Sequence:
MPHPRRYHSSERGSRGSYREHYRSRKHKRRRSRSWSSSSDRTRRRRREDSYHVRSRSSYDDRSSDRRVYDRRYCGSYRRNDYSRDRGDAYYDTDYRHSYEYQRENSSYRSQRSSRRKHRRRRRRSRTFSRSSSQHSSRRAKSVEDDAEGHLIYHVGDWLQERYEIVSTLGEGTFGRVVQCVDHRRGGARVALKIIKNVEKYKEAARLEINVLEKINEKDPDNKNLCVQMFDWFDYHGHMCISFELLGLSTFDFLKDNNYLPYPIHQVRHMAFQLCQAVKFLHDNKLTHTDLKPENILFVNSDYELTYNLEKKRDERSVKSTAVRVVDFGSATFDHEHHSTIVSTRHYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTHDNREHLAMMERILGPIPSRMIRKTRKQKYFYRGRLDWDENTSAGRYVRENCKPLRRYLTSEAEEHHQLFDLIESMLEYEPAKRLTLGEALQHPFFARLRAEPPNKLWDSSRDISR
Protein: Rho GTPase-activating protein 28 (Rho-type GTPase-activating protein 28) (Q8BN58)
Organism: Mus musculus (Mouse)
Function: GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.
Interaction partners:
Sequence:
MEVEDSGGVVLTAYHSHARSQPQGAEPRCASRASHPLSRKSIPRCRRINRMLSNESLHPPSFSRSNSQASVDSSASMEEFLREIESIKESSVGASQEQPPTAAAAAAEVKPVDEGELEAEWLQDVGLSTLISGNEEEDGKALLSTLTRTQAAAVKKRYNTYTQTLRKKNKQPVRDVRDIFGVSESPPSDSCEHATQLDGTKEEKDLPGVTKTSRPLPDDASLSSTTLSNGAQDEEGGFVALQSGSVSILEAIPDIAVHTNGSADAEQSVQSTLSDDDYHGKNVPAEAEELSFEVSYSEMVTEMPDRNKWKKSDIKKEDYVLTKFIIQKTRFGLTETGDLSVEDMKKIRHLSLIELTAFFDAFGIQLKRNKTERVRGRDNGIFGVPLTVLLDNDRKKDPAVKVPLVLQKFFQKVEESGLESEGIFRLSGCTAKVKQYREELDARFNADKFKWDKMCHREAAVMLKAFFRELPTSLFPVEYIPAFISLMERGPDIKVQFQALHLMVMALPDANRDTAQALMAFFNKVIANESKNRMNLWNISTVMAPNLFFSRSKHSDCEELLLANTATHIIRLMLKYQKILWKVPSFLITQVRRMNEATMLLKKQLPSMKKLLRRKTLDREVSILKTSKVPQKSPSSRRMSDVPEGVIRVHAPLLSKVSMAIQLNSQTKAKDILAKFQYENSHGSSEHIKMQNQRLYEVGGNIGQHCLDPDAYILDVYHINPHAEWVIKP
Protein: Vacuolar protein sorting-associated protein 29 (hVPS29) (PEP11 homolog) (Vesicle protein sorting 29) (Q9UBQ0)
Organism: Homo sapiens (Human)
Function: Acts as component of the retromer cargo-selective complex (CSC). The CSC is believed to be the core functional component of retromer or respective retromer complex variants acting to prevent missorting of selected transmembrane cargo proteins into the lysosomal degradation pathway. The recruitment of the CSC to the endosomal membrane involves RAB7A and SNX3. The SNX-BAR retromer mediates retrograde transport of cargo proteins from endosomes to the trans-Golgi network (TGN) and is involved in endosome-to-plasma membrane transport for cargo protein recycling. The SNX3-retromer mediates the retrograde endosome-to-TGN transport of WLS distinct from the SNX-BAR retromer pathway. The SNX27-retromer is believed to be involved in endosome-to-plasma membrane trafficking and recycling of a broad spectrum of cargo proteins. The CSC seems to act as recruitment hub for other proteins, such as the WASH complex and TBC1D5. Required to regulate transcytosis of the polymeric immunoglobulin receptor (pIgR-pIgA). Acts also as component of the retriever complex. The retriever complex is a heterotrimeric complex related to retromer cargo-selective complex (CSC) and essential for retromer-independent retrieval and recycling of numerous cargos such as integrin alpha-5/beta-1 (ITGA5:ITGB1). In the endosomes, retriever complex drives the retrieval and recycling of NxxY-motif-containing cargo proteins by coupling to SNX17, a cargo essential for the homeostatic maintenance of numerous cell surface proteins associated with processes that include cell migration, cell adhesion, nutrient supply and cell signaling. The recruitment of the retriever complex to the endosomal membrane involves CCC and WASH complexes. Involved in GLUT1 endosome-to-plasma membrane trafficking; the function is dependent of association with ANKRD27.
Subcellular location: Cytoplasm. Membrane; Peripheral membrane protein. Endosome membrane {ECO:0000250|UniProtKB:Q9QZ88}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9QZ88}. Early endosome {ECO:0000305}. Late endosome {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 26C
- Vacuolar protein sorting-associated protein 35
- Sorting nexin-1
- TBC1 domain family member 5
- Vacuolar protein sorting-associated protein 26A
- Vacuolar protein sorting-associated protein 26B
- Sorting nexin-2
- VPS35 endosomal protein-sorting factor-like
- Sorting nexin-5
- Sorting nexin-6
Sequence:
MLVLVLGDLHIPHRCNSLPAKFKKLLVPGKIQHILCTGNLCTKESYDYLKTLAGDVHIVRGDFDENLNYPEQKVVTVGQFKIGLIHGHQVIPWGDMASLALLQRQFDVDILISGHTHKFEAFEHENKFYINPGSATGAYNALETNIIPSFVLMDIQASTVVTYVYQLIGDDVKVERIEYKKP
Protein: Lymphocyte antigen 86 (E7F6I2)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MKTYFNMLLFLILGLVQMDRAHSQDPQWPLHTICNSNKLTVTYRSCDPLQDVGVSFLPCPNKLTDPTTVRIAFILRQSITEFYSSIKLFLNGLHVWGVDEPLCLPQFPRFTFCGSRRGEMITFEMLIKSKVDLPLKGDFNLMVHGINQDGFQIACVNATLSFW
Protein: Four domain-type voltage-gated ion channel alpha-1 subunit (Ion transport domain-containing protein) (G5EG32)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLTRRKSSIDGTKTERNRRRGESIGGAFTDMINIEPTSIINKSTELLHERFLRDMVRVACLLSMISLCLHTPETIKMWPPLNYIILANDVIVTLIFIGEAAVTINQNGLFDNQNSYLRDRWYQFEFFLLINHILSCVIHIYELCSIWFPALNFVYYPWLGALRSARPFIFLRFIRSIVRFKLPKNRIKLIIKRSSQQIQNVTIFFMFFVFSYAIMGVQLFGRLNYHCVVNGTDPNNVTIADLAIPDTMCSQKGAGGYECPGNMVCMRLQLKPQEEGFYGQFSDFASSLFTVYLAASQEGWVYVLYDCLDSLPSFLAFFYFVTLIFFLAWLVKNVFIAVITETFAEIRVQFSEMWQTREATTDHVYTQKLEKDEDGWKLVEVDKYNRAHSNNSLFLHTIVTSTAFQTVMQLLILANAIFHATFVFYHDESDQIRKIWYYYVEVGFTILFNTEVIIKIYAFGWKAYIARGQHKFDCILCVGSSLNAIWVLYETNIFTYFQVFRIARLIKASPMLEDFVYKIFGPGKKLGGLVIFTGILLIVTSAISLQLFCYVPKLNKFTNFAVAFMSMFQIITQEGWTDVVIEILRACNEQAVPFVAIYFVAYHLLVTLFVLSLFVAVILDNLEMDEELKKVKQLKAREQDTIKTTLPMRLRIFNRFPTAPTMVTMKKVSSEFPLPKIRDSFTRQFADEFVETSDDTIQEIGFKVRSMLSGRGPSKETRITTTIRHVGQLSNKTILTSMLTESNRNRALFSESNQHLASLTRSNTSSKHGKSGALSTNSRSRTRGLASLKGKHMVEGFKENGDLRPEDTARKVEKHGEIDFKALQMKRAHAEITRNRIEEEMRENHPMFDRPLFLVGRESSLRRMCQLIAHSRHSYDQNDGQHRKHSNKYKQFHDFLAIMTYMDWTMVLVTTLSCCSMLWESPWPTTGENLIFNNFYLQIAEYIFVLVMSFELIVKCIANGLFFTPKALVTDVGDILTIFIYITSLMFLIWMPNHIEINSWAQLLMVCRAMRPLRVYALIPHIRRVVVELCRGFREILLVTILLVVLMFIFASFGVQLVGGKLASCNDPMITSRENCTGLYDVKLFVTRMEVYGKNDNLMHPSIIVPRVWTNPRNFNFDHIGNAMLALFETLSYKGWNVVRDVLYLRHGAWAVLFIHIYVFIGCMIGLTLFVGVVVANYTENRGTALLTVDQRRWHDLKARLKMAQPLHVPPKPPESAKLRCYLYDLTTSRWFKQLFAVLVVVNSFTLVIPWNVSEEQDRKTFLLCLTVISAICNILFTLECLLKMIAFTLSGFWQSRRNRIDFIITILGINWIVFHFLFQLPAYFAGGITEWKRLTYTYGYLVVILRFFTIAGRKSTLKMLMLTVVMSMVRSSFIIAAMFLLVLFYANAGVVLFGMVKYGQAVGKHVNFRNGREALVVLFRSVTGEDWNDIMHDCMRAPPFCNWHPGLSYWQTDCGNYVGAIVYFCSFYLIITYIVLNLLVAIIMENFSLFYSSEEDALLSYADIRNFQLVWNMVDIEQKRSIPVRRVKFLLRLLKGRLEVNDESDGLLFKHMCHEMERLHNGDDVSFHDVLNMLSYRSVDIRKSLQLEELLQREELEYIIEEEVAKHTIRAWLENCLKNIKAKQNNTLGKMSSIGSTFAFPQSQEVLTKGVVLTEASPEEDSLQGDKGSGKKKAQRGNSITEIVAEAQKKSVKRATDKISERRGTLRQMQMGTYDELEEVEEDEDTDGEIRRSSFEYSGVDMIQMSHEKQLEDVKTWWTLCD
Protein: UPF0321 protein PJ695.01c (Q9URW1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Uncharacterized protein C29B12.08
Sequence:
MLLLLYICCLFLKFILANVDLTFVEYAKLPSKYAELLANATNQQGVMLFSTGDIRIGAYNYLVNNVTEINNDTDAYLCQLLTGQYTTDCYIFDTNSDDKPETFNSSIHLLNSDLDPK
Protein: Fish-lips, isoform C (Fish-lips, isoform D) (RE58108p) (Q5U1A7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MPDHTRVTATTRSRPWLCGAIPVLLLLLLTLVILPPETTAFCPSKCQCLGGEANSRALCVDAALEDVPIQLNPETKYINLTVNRIRTLEFSLPFYMKLEILDLSQNIIETLGSKNFEYQSELRTLNLSRNLVSSLHKHAFKGLTNLLLLDLSFNRIETVHPTALSDLASLVELDLTNNNIVSLEDNCFKGMNTLEVLVFRNNRLLDVPASNLWHLHALKSLDMSLNLVEFVRNDSFEGLKELLALSVQGNVMSELDLSAFEGLISLKHLDLSDNNLTMVPTQQLSKLSNLTYLNLGGNRFSQLPAVAFLNLFHLRELHLSRLDFLQRIDSRAFVDNTHLQTLHLNNNPQLSDIPMRLFQGNPNILEVYMQSNSLQTLYSAQFPVDQLQKLYLGDNPLQCNCSLLWLWRLVTGNFEGVDPGMEHAAGGAVAALAKEADDEELADEATAVASTDDGVAALAAYIAEQHIVNALHTTEPSAYELATSSSNRNSGILRMDRQQIGCDIWRDKVRTRRKLLTMSEGEITCPAHIVTVVCAVITCLLVAMIGISVLYYLRFVKRRRKLLHERGPMRTSKSIINVHDRILQGHNPGGLGLGMSMTLGGGNHVNGLGMTLNYPHHAQTLQAHHHYHQAMPLQSHGGNGNHEYQQTTLPQLDKLELERYLAAQTIANEYRALKPWELPVKEADDEPEHLYERFDHYEYPDTHTMSKLKQAASLNHSNSSAGPSPVPPSSGKPHVVYV
Protein: beta-N-acetylhexosaminidase (EC 3.2.1.52) (Q8MSS9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MKSTRTALGVALLLALVSQLAAHSSDDLVYGYECRSGYCQKVELSEENYVKAISLPVCRLFCGSSIGTLWPKPTGTVRLDTLMRQVDISFIDFNFNGIARQQKLWRAVEDRFMNMLEAQIPDRKVLARGGYRMSVNINTPDEPTPARLTLDTDESYTLDIDTDASGHVLANITASNFFGARHGLETLAQLIVYDDIRREVQVTANATINDAPVYKWRGLLLDTSRNYYSVKSIKRTLEGMALVKLNTFHWHITDSHSFPLEVKKRPELHKLGAYSQRQVYTRRDVAEVVEYGRVRGIRVMPEFDAPAHVGEGWQHKNMTACFNAQPWKSLCVEPPCGQLDPTVNEMYDVLEDIYGTMFDQFNPDIFHMGGDEVSTSCWNSSQPIQQWMKKQGWGLETADFMRLWGHFQTEALGRVDKVANGTHTPIILWTSGLTEEPFIDEYLNPERYIIQIWTTGVDPKVKKILERGYKIIVSNYDALYLDCGGAGWVTDGNNWCSPYIGWQKVYDNSLKSIAGDYEHHVLGAEGAIWSEQIDEHTLDNRFWPRASALAERLWSNPAEGWRQAESRLLLHRQRLVDNGLGAEAMQPQWCLQNEHECPIDAYDAQV
Protein: RNA-binding protein OPG065 (RNA-binding protein E3) (p25) (P21605)
Organism: Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR))
Function: RNA-binding protein that plays a role in the inhibition of multiple cellular antiviral responses activated by double-stranded RNA (dsRNA), such as inhibition of PKR activation, necroptosis, and IFN-mediated antiviral activities. Recognizes and binds Z-RNA structures via its Z-binding domain and dsRNA via its DRBM domain: RNA-binding activity is required to escape host ZBP1-dependent necroptosis. Mechanistically, the Z-binding domain binds Z-RNAs that are produced during vaccinia virus infection, thereby competing with Z-RNA detection by host ZBP1, suppressing ZBP1-dependent necroptosis. Acts as a key inhibitor of the interferon response by blocking the phosphorylation and subsequent activation of IRF3 and IRF7 kinases that are required for interferon-alpha gene expression. Inhibits NF-kappa-B activation and the ubiquitin-like protein ISG15, which is an early antiviral protein. The binding with host ISG15 subsequently blocks host ISGylation.
Interaction partners:
Sequence:
MSKIYIDERSNAEIVCEAIKTIGIEGATAAQLTRQLNMEKREVNKALYDLQRSAMVYSSDDIPPRWFMTTEADKPDADAMADVIIDDVSREKSMREDHKSFDDVIPAKKIIDWKGANPVTVINEYCQITRRDWSFRIESVGPSNSPTFYACVDIDGRVFDKADGKSKRDAKNNAAKLAVDKLLGYVIIRF
Protein: Pheromone receptor transcription factor (GRM/PRTF protein) (P11746)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription factor required for the efficient replication of minichromosomes and the transcriptional regulation of early cell cycle genes. Activates transcription of ECB-dependent genes during the G1/M phase. Genes that contain a ECB (early cell box) element in their transcription regulatory region are transcribed only during G1/M phases. Interacts with the alpha-2 repressor or with the alpha-1 activator thereby regulating the expression of mating-type-specific genes. With ARG80, ARG81 and ARG82, coordinates the expression of arginine anabolic and catabolic genes in response to arginine.
Subcellular location: Nucleus.
Interaction partners:
- Fork head protein homolog 2
- Homeobox protein YOX1
- Protein STE12
- Silenced mating-type protein ALPHA2
- Inositol polyphosphate multikinase
- Arginine metabolism regulation protein II
- Homeobox protein YHP1
- Nuclear division defective protein 1
- Regulatory protein SWI4
- Fork head protein homolog 1
Sequence:
MSDIEEGTPTNNGQQKERRKIEIKFIENKTRRHVTFSKRKHGIMKKAFELSVLTGTQVLLLVVSETGLVYTFSTPKFEPIVTQQEGRNLIQACLNAPDDEEEDEEEDGDDDDDDDDDGNDMQRQQPQQQQPQQQQQVLNAHANSLGHLNQDQVPAGALKQEVKSQLLGGANPNQNSMIQQQQHHTQNSQPQQQQQQQPQQQMSQQQMSQHPRPQQGIPHPQQSQPQQQQQQQQQLQQQQQQQQQQPLTGIHQPHQQAFANAASPYLNAEQNAAYQQYFQEPQQGQY
Protein: LD45843p (Q9VVV6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSDQCAAFVDGASITYGTGNELESGSGSSAACKPTLREFNVRLEVPLAAEERLGLTGDVKALGEWQLSRSVALESLDELNWQATVALQSCRQLEYRYFVYVEDLSGYKQIRRWETHFKPRSLGPCTELQCSQLDVFGITSDNSDLKPQVHRGWLNHEAILQLKFNGEKMFQVHDIETFDPQHVQLKIVPVEKTAGLHVEYSKQEYGKSQLELQPTFGVPYTKGDIVIFHITLPLERMMEQHFRLECYSMSNELLGSATLVTSDLTGSEGVLHLPIKSAKNADETLARLRLPYVAVQPYRYSPLDFKNTYAHYWPKSWPNLDVGHRGNGKSYIADAPAERENTIASFLSAHEHHADMIELDVHLTADGVPVIYHDFGLRTAPPGKQISRPDQLEYVLIKDINYELLKRLRIFSVIAGQVREYPSHNAEPRMEHRIFPTLVEVLEKLPKSLGIDVEIKWPQRRQGGGSEAEQTIDKNFFADKVIHQVIQKGCGRPIIFSSFDADMCTMLRFKQNVFPVMFLTQGETKKWQPFLDLRTRTFIAAVNNAQAFELAGTAPHAEDFLGENASEMLRKAKDLGQIAVIWGDDCNSKERVQYFTRIGATATCYDRSDLFMPEGKREAFFKSPALMAEFAAQCRI
Protein: Heat shock 70 kDa protein 7, chloroplastic (Chloroplast heat shock protein 70-2) (cpHsc70-2) (Heat shock protein 70-7) (AtHsp70-7) (Q9LTX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts redundantly with HSP70-6 in the thermotolerance of germinating seeds. Plays an important role in the protein precursor import into chloroplasts.
Subcellular location: Plastid, chloroplast stroma {ECO:0000269|PubMed:18997426, ECO:0000269|PubMed:20506024}.
Interaction partners:
- Heat shock protein 90-5, chloroplastic
- AT4g39960/T5J17_130
- Chaperone protein dnaJ 20, chloroplastic
- 20 kDa chaperonin, chloroplastic
- Heat shock protein 90-6, mitochondrial
- Chaperonin 60 subunit beta 2, chloroplastic
- Heat shock protein 90-1
- Chaperonin 60 subunit alpha 1, chloroplastic
- Chaperonin 60 subunit beta 1, chloroplastic
- Mitochondrial import inner membrane translocase subunit TIM44-2
Sequence:
MASSAAQIHILGGIGFPTSSSSSSTKNLDNKTNSIPRSVFFGNRTSPFTTPTSAFLRMGRRNNNASRYTVGPVRVVNEKVVGIDLGTTNSAVAAMEGGKPTIVTNAEGQRTTPSVVAYTKSKDRLVGQIAKRQAVVNPENTFFSVKRFIGRRMNEVAEESKQVSYRVIKDENGNVKLDCPAIGKQFAAEEISAQVLRKLVDDASRFLNDKVTKAVITVPAYFNDSQRTATKDAGRIAGLEVLRIINEPTAASLAYGFERKSNETILVFDLGGGTFDVSVLEVGDGVFEVLSTSGDTHLGGDDFDKRVVDWLASTFKKDEGIDLLKDKQALQRLTEAAEKAKIELSSLTQTNMSLPFITATADGPKHIETTLTRGKFEELCSDLLDRVRTPVENSLRDAKLSFKDIDEVILVGGSTRIPAVQDLVRKLTGKEPNVSVNPDEVVALGAAVQAGVLSGDVSDIVLLDVTPLSLGLETLGGVMTKIIPRNTTLPTSKSEVFSTAADGQTSVEINVLQGEREFVRDNKSIGSFRLDGIPPAPRGVPQIEVKFDIDANGILSVSASDKGTGKKQDITITGASTLPKDEVDTMVQEAERFAKEDKEKRDAIDTKNQADSVVYQTEKQLKELGEKIPGPVKEKVEAKLQELKEKIASGSTQEIKDTMAALNQEVMQIGQSLYNQPQPGGADSPPGGEASSSSDTSSSAKGGDNGGDVIDADFTDSN
Protein: Protein panoramix (Protein silencio) (Q9W2H9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acts via the piwi-interacting RNA (piRNA) pathway which 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 transposons. Required for transcriptional silencing of transposons targeted by piwi and confers its effects by interacting with nascent RNA transcripts. Likely to be recruited to nascent transcripts cotranscriptionally by piwi and to recruit additional factors involved in transcriptional silencing. In the ovaries, forms a complex with nxf2, piwi and Nxt1 which acts as effectors of cotranscriptional transposon silencing. The interaction with nxf2 stabilizes the nuclear protein complex.
Subcellular location: Nucleus {ECO:0000269|PubMed:23665231, ECO:0000269|PubMed:31219034, ECO:0000269|PubMed:31368590, ECO:0000269|PubMed:31384064}. Note=Nuclear localization depends on interaction with nxf2. {ECO:0000269|PubMed:31219034}.
Interaction partners:
- Protein piwi
- Nuclear RNA export factor 2
- NTF2-related export protein
- Small ovary, isoform A
- Dynein light chain 1, cytoplasmic
- Dynein light chain 2, cytoplasmic
- Histone-lysine N-methyltransferase eggless
- Gametocyte-specific factor 1 homolog
- Protein aubergine
- BcDNA.LD26050
Sequence:
MEAPMKLEVKVENYVECGINEDEATPLREGTGETPPHAFACGVPMSGSGWCSDPEDGNLVHHSATPTSDEHLQPSLDTIEPKMEPKIKEDADNAMLDSLLADPFENNSPATLQTPADVKPNAMLDSVEQGSRSCELLPSEFSKRENLDDMDLFSLKAAKTLVPDEQQSFPQNDTPIDDPEAADLIAQKREILKMLEMTAENRKVKHKKKKHKKERSHRSNKHQEESRKRNHSNSSSDEGADDKNQFDCDYRGHKKYKNRRGSASSQNESSKERKLRDTELDYVPVRPDEHFIRPIKFSNLIERRPPQVEFNTVNLSKADKRSLAVARAELVLEQIQQKANKEEPPEFHMVDTICKLPVNESFRNQDCFENPSPICNNMNVVYKFNSTPGTRIDLSKWGLETVPEATKRLLRLLGIDVARLKELQSTVKPSQRILKLKKEQLEQGLAPTEEQETATLYKNAATQTERRTATRDAGTQVRLESKLNGAFWQNPHFDPMNLTQHQSNVMLALQEIYQTLPSATMAVKLSRALAPALAIIKGRQP
Protein: Transcription factor SOX-9 (P48434)
Organism: Gallus gallus (Chicken)
Function: Transcription factor that plays a key role in chondrocytes differentiation and skeletal development. Specifically binds the 5'-ACAAAG-3' DNA motif present in enhancers and super-enhancers and promotes expression of genes important for chondrogenesis, including COL2A1. Plays a central role in successive steps of chondrocyte differentiation. Absolutely required for precartilaginous condensation, the first step in chondrogenesis during which skeletal progenitors differentiate into prechondrocytes (By similarity). Together with SOX5 and SOX6, required for overt chondrogenesis when condensed prechondrocytes differentiate into early stage chondrocytes, the second step in chondrogenesis (By similarity). Later, required to direct hypertrophic maturation and block osteoblast differentiation of growth plate chondrocytes: maintains chondrocyte columnar proliferation, delays prehypertrophy and then prevents osteoblastic differentiation of chondrocytes (By similarity). Also required for chondrocyte hypertrophy, both indirectly, by keeping the lineage fate of chondrocytes, and directly, by remaining present in upper hypertrophic cells (By similarity). Low lipid levels are the main nutritional determinant for chondrogenic commitment of skeletal progenitor cells: when lipids levels are low, FOXO transcription factors promote expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation (By similarity). In addition to cartilage development, also acts as a regulator of proliferation and differentiation in epithelial stem/progenitor cells (By similarity). In response to bone morphogenetic protein stimulus, phosphorylation is induced and then sumoylation, allowing cooperation with SNAI2 to trigger neural crest delamination.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:23382206}.
Interaction partners:
- Runt-related transcription factor
- Aggrecan core protein
- Collagen alpha-1
- Indian hedgehog protein
- Forkhead box protein L2
- Uncharacterized protein.
- TGF_BETA_2 domain-containing protein.
- Forkhead box protein D3
- Collagen alpha-1
- Bone morphogenetic protein 4
Sequence:
MNLLDPFMKMTEEQDKCISDAPSPTMSDDSAGSPCPSGSGSDTENTRPQENTFPKGDPDLKKESDEDKFPVCIREAVSQVLKGYDWTLVPMPVRVNGSSKNKPHVKRPMNAFMVWAQAARRKLADQYPHLHNAELSKTLGKLWRLLNESEKRPFVEEAERLRVQHKKDHPDYKYQPRRRKSVKNGQSEQEEGSEQTHISPNAIFKALQADSPQSSSSISEVHSPGEHSGQSQGPPTPPTTPKTDAQQPGKQDLKREGRPLAEGGRQPPHIDFRDVDIGELSSDVISNIETFDVNEFDQYLPPNGHPGVPATHGQVTTYSGTYGISSSASSPAGAGHAWMAKQQPQPPQPPAQPPAQHTLPALSGEQGPAQQRPHIKTEQLSPSHYSEQQQHSPQQQQQQQQQLGYGSFNLQHYGSSYPPITRSQYDYTEHQNSGSYYSHAAGQSGGLYSTFTYMNPTQRPMYTPIADTSGVPSIPQTHSPQHWEQPVYTQLTRP
Protein: Spindlin-2B (Spindlin-like protein 2B) (SPIN-2) (SPIN-2B) (Q9BPZ2)
Organism: Homo sapiens (Human)
Function: Involved in the regulation of cell cycle progression, this activity is related to the inhibition of apoptosis following the removal of essential growth factors. Exhibits H3K4me3-binding activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:12145692}.
Interaction partners:
- Spindlin interactor and repressor of chromatin-binding protein
- Spindlin-1
- Threonylcarbamoyl-AMP synthase
- CGG triplet repeat-binding protein 1
Sequence:
MKTPNAQEAEGQQTRAAAGRATGSANMTKKKVSQKKQRGRPSSQPRRNIVGCRISHGWKEGDEPITQWKGTVLDQVPINPSLYLVKYDGIDCVYGLELHRDERVLSLKILSDRVASSHISDANLANTIIGKAVEHMFEGEHGSKDEWRGMVLAQAPIMKAWFYITYEKDPVLYMYQLLDDYKEGDLRIMPESSESPPTEREPGGVVDGLIGKHVEYTKEDGSKRIGMVIHQVEAKPSVYFIKFDDDFHIYVYDLVKKS
Protein: Sphingosine kinase B (SK B) (SPK B) (EC 2.7.1.91) (Q6B516)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Catalyzes the phosphorylation of sphingosine to form sphingosine-1-phosphate (S1P), which probably acts intracellularly as a second messenger perhaps by promoting cell proliferation.
Interaction partners:
- Sphingosine-1-phosphate lyase
- sphinganine-1-phosphate aldolase
- Neutral ceramidase B
- sphingolipid 4-desaturase
- Probable sphingosine-1-phosphate phosphatase
- Neutral ceramidase A
- 3-ketodihydrosphingosine reductase
- Putative alkaline ceramidase dcd3B
- Putative alkaline ceramidase dcd3A
- Sphingosine kinase A
Sequence:
MENNNNEPAETVQEKGPKLKNDIDLNDQFKDEKEKKEEISSSSIENKNNNNNNTSTNNVIPNESNNNISNNNVISNENNNTNNNTDNNTDNNNNNNNNNNNNNEPVTSFTVNNKSLIEKEPTLFEFNQEQQIKYKNKSINSLIIKRSGIVIKISQKKSTIIYQDSIIACSELPDNFDTATTTTTTTTTLPIKVTLFTCVLKKKQLTIDKEQRKRKSYTFQFKSNQDSLNFYSNIQSTFLNSLPRGNPKNRKIRILINPKSGKKESHNIFKEVEQLFKDSGIKMKLTVTMEPEHAKKIGFKSNIYKYDTVVFISGDGLLHEFINGLLSREDYEDAKKIPLALIPAGTGNGLANSIGLQDPMSAALAILRGFTKPLDVCIVQQPTVTTIPVVDNNTVTTTTTTTSPTSASPTITSANNNNNNNNNNNNNNNNNNNNNNNNNNSNITKWCSILSLTWGLVSDVDIESEKYRSLGDLRLIIGAAVRILNLRIYRGKVYFLPAIPLDKSQMQSIPKCSFDCNICDSSNSVKVIEDLVCNDNDNNNKNKNEEQNEINSTTSNNNNNNNTTTTSTSSSTSTSTSTSSLTATTTTAKSTNSLSSSPRSDINMSSNSISKSLDIGTIPSCKVTHNSNLLNESSDSLLSKGWKCIEGEFIGVVASTVSHLASDFISSPNAHLSDGLIDLIFINNRSKLSKASLLSILTDSATGDHLKSDLIEHHKVKALILEPSIQKHGIVAIDGERIPYAKTSMENIRGCLNLICRSYH
Protein: Threonine--tRNA ligase, mitochondrial 1 (EC 6.1.1.3) (AtSYT1) (Threonyl-tRNA synthetase) (ThrRS) (O04630)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:10583378}. Cytoplasm, cytosol {ECO:0000269|PubMed:10583378}.
Interaction partners:
- Leucine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase, mitochondrial 1
- Valine--tRNA ligase, chloroplastic/mitochondrial 2
- Leucine--tRNA ligase, chloroplastic/mitochondrial
- Methionine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, chloroplastic/mitochondrial
- Cysteine--tRNA ligase 2, cytoplasmic
- Cysteine--tRNA ligase 1, cytoplasmic
- Lysine--tRNA ligase, cytoplasmic
Sequence:
MLLRLTARSIRRFTTSSSSLPLLSSSSFCTVPTMAANHPKDEAYLSAVIPKRIKLFEQIQANQLENLKSLPHDPIKVTLPDGNVKEGKKWETTPMDIAAQISKGLANSALISAVDDVLWDMNRPLEGDCKLELFKFDSDKGRDTLWHSSAHILGQALEQEYGCQLCIGPCTTRGEGFYYDGFYGELGLSDNHFPSIEAGAAKAAKEAQPFERIEVTKDQALEMFSENNFKVELINGLPADMTITVYRCGPLVDLCRGPHIPNTSFVKAFKCLRASSAYWKGDKDRESLQRVYGISYPDQKQLKKYLQFLEEAKKYDHRLLGQKQELFFSHQLSPGSYFFLPLGTRVYNRLMDFIKNQYWHRGYTEVITPNMYNMELWQTSGHADNYKDNMFTFNIEKQEFGLKPMNCPGHCLIFQHRVRSYRELPMRLADFGVLHRNEASGALSGLTRVRRFQQDDAHIFCTTEQVKGEVQGVLEFIDYVYKVFGFTYELKLSTRPEKYLGDLETWDKAEADLKEAIEAFGKPLVLNEGDGAFYGPKIDITVSDAMNRKFQCATLQLDFQLPIRFNLEYAAEDEAKKSRPVMIHRAVLGSVERMFAILLEHYKGKWPFWISPRQAIVCPISEKSQQYAEKVQKQIKDAGFYVDADLTDRKIDKKVREAQLAQYNYILVVGETEAATGQVSVRVRDNAAHSVKSIEDLLEEFKAKTAEFV