wanglab/gogpt-training-data huggingface dataset:
Protein: Protein pid-3 (piRNA biogenesis and chromosome segregation protein 1) (piRNA-induced silencing defective protein 3) (O76616)
Organism: Caenorhabditis elegans
Function: Component of the pid-1 and tost-1 variants of the PETISCO complexes, which have roles in the biogenesis of a class of 21 nucleotide PIWI-interacting RNAs (piRNAs) that possess a uracil residue at the 5'-end (also called 21U-RNAs) and embryogenesis, respectively. Within the pid-1 variant of the PETISCO complex may stabilize 21U-RNA precursor molecules. Promotes the biogenesis of 21U-RNAs. Required for chromosome segregation and cell division in early embryos.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:31147388}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:31147388}. Nucleus {ECO:0000269|PubMed:31216475}. Note=Dispersedly distributes throughout the cytoplasm in early embryos (PubMed:31147388). During early embryogenesis, localizes to the nucleus at prophase of cell division, and remains in the cytosol at interphase in 2- and 4-cell embryos (PubMed:31216475). Localizes to puncta in the perinuclear region in the germline syncytium (PubMed:31147388). {ECO:0000269|PubMed:31147388, ECO:0000269|PubMed:31216475}.
Interaction partners:
- Embryonic developmental protein tofu-6
- Enhancer of rudimentary homolog 2
- Protein tost-1
- Eukaryotic translation initiation factor 4E-3
- Protein pid-1
- Enhancer of rudimentary homolog
- Schlafen-like protein 1
- K Homology domain-containing protein
- Schlafen-like protein 2
- RRM domain-containing protein
Sequence:
MVAHQKADFKSKWAMVVTVNNLNDKKRADLREFSEWFIETLRLEGAFIGHYFNYEAAPVTIVETLPGNFDSCTNAYQKIHKEHPQVVLVVHILPQSQSNEYEWMKVLASRYGFVRQGLLYDNCANRFQNVETDQNSVFRNMCQWIYRSGTAIVRNEGNACGILHGKDPKPTFDKVLFNSEDIKDSVFKVLHAEEEPRGADQENMLKISGYPGMLNTFGIAQLLTPYRVNGITITGAQSAVVALENKFQVYQAVQDFNGKKLDRNHKLQVSSLVVSSPAVPLEWPSLKKSKKLVEQVGKPIRLSKVSS
Protein: Histone H3.3A (H3.A) (C0HL66)
Organism: Drosophila melanogaster (Fruit fly)
Function: Variant histone H3 which replaces conventional H3 in a wide range of nucleosomes in active genes and is specifically enriched in modifications associated with active chromatin. Constitutes the predominant form of histone H3 in non-dividing cells and is incorporated into chromatin independently of DNA synthesis. Deposited at sites of nucleosomal displacement throughout transcribed genes, suggesting that it represents an epigenetic imprint of transcriptionally active chromatin. 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 {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H2A
- Heterochromatin protein 1
- Polycomb group protein Pc
- Histone H4
- Chromatin assembly factor 1 p55 subunit
- TBP-associated factor 3
- Histone H2A.v
- Histone-lysine N-methyltransferase SETD1
- Histone chaperone asf1
- Chromo domain-containing protein rhino
Sequence:
MARTKQTARKSTGGKAPRKQLATKAARKSAPSTGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSAAIGALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA
Protein: Uncharacterized membrane protein YNL019C (P53975)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cell membrane; Single-pass membrane protein.
Interaction partners:
- Uncharacterized protein YNL034W
- Uncharacterized protein YNL162W-A
- Uncharacterized protein YNL018C
- Uncharacterized membrane protein YFL051C
- Uncharacterized transporter YNL095C
- Uncharacterized membrane protein YFL067W
Sequence:
MLYSRESRTTVLFLALVTSLTVLCHSVDVTTVFTTSTITEITTVTAAPQPQNKAETALNTATNIIQTMQFLFNCAPFKWKGPLKITSCALNFIVLLLTAWGYLLKYLQENKLNSDADMEKMVGLGFGEMVGRIFGKGVGKAFTKMDITQKLVYPFEGSNRQKCLLMTVGENSIVPFHDLSTEICFDQYTLDSLSHHNHGSISILDAGSVSALGFADISSKMPSVSELYTLFGDYTIEVLGGITKLASTLNREDWQGERNGFAVLSRDRPNQTLLSVHMYSSSLL
Protein: [Citrate [pro-3S]-lyase] ligase (EC 6.2.1.22) (Acetate:SH-citrate lyase ligase) (Citrate lyase synthetase) (P77390)
Organism: Escherichia coli (strain K12)
Function: Acetylation of prosthetic group (2-(5''-phosphoribosyl)-3'-dephosphocoenzyme-A) of the gamma subunit of citrate lyase.
Interaction partners:
- Citrate lyase subunit beta
- 2-
- Citrate lyase acyl carrier protein
- Citrate lyase alpha chain
- Apo-citrate lyase phosphoribosyl-dephospho-CoA transferase
- Sensor histidine kinase DpiB
- Transcriptional regulatory protein DpiA
- Citrate/succinate antiporter
Sequence:
MFGNDIFTRVKRSENKKMAEIAQFLHENDLSVDTTVEVFITVTRDEKLIACGGIAGNIIKCVAISESVRGEGLALTLATELINLAYERHSTHLFIYTKTEYEALFRQCGFSTLTSVPGVMVLMENSATRLKRYAESLKKFRHPGNKIGCIVMNANPFTNGHRYLIQQAAAQCDWLHLFLVKEDSSRFPYEDRLDLVLKGTADIPRLTVHRGSEYIISRATFPCYFIKEQSVINHCYTEIDLKIFRQYLAPALGVTHRFVGTEPFCRVTAQYNQDMRYWLETPTISAPPIELVEIERLRYQEMPISASRVRQLLAKNDLTAIAPLVPAVTLHYLQNLLEHSRQDAAARQKTPA
Protein: Stage IV sporulation protein FB (EC 3.4.24.-) (P26937)
Organism: Bacillus subtilis (strain 168)
Function: Implicated in the coupling of mother cell to forespore gene expression. Required for spore formation. Processes the pro-sigma K factor.
Subcellular location: Forespore outer membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Stage IV sporulation protein FA
- Sigma-K factor-processing regulatory protein BofA
- SpoIVB peptidase
- Stage II sporulation protein M
- Stage II sporulation protein P
- Stage III sporulation protein AH
- Carboxy-terminal processing protease CtpB
- Stage II sporulation protein Q
- Stage III sporulation protein AA
- Stage III sporulation protein AG
Sequence:
MNKWLDLILKIHVHPFLWIIAALGLLTGHMKALLCLLLIVLIHELGHAALAVFFSWRIKRVFLLPFGGTVEVEEHGNRPLKEEFAVIIAGPLQHIWLQFAAWMLAEVSVIHQHTFELFTFYNLSILFVNLLPIWPLDGGKLLFLLFSKQLPFQKAHRLNLKTSLCFCLLLGCWVLFVIPLQISAWVLFVFLAVSLFEEYRQRHYIHVRFLLERYYGKNRELEKLLPLTVKAEDKVYHVMAEFKRGCKHPIIIEKSGQKLSQLDENEVLHAYFADKRTNSSMEELLLPY
Protein: Protein DESIGUAL 2 (O81898)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved, partially redundantly with VCC/DEAL1 and DEAL3, to ensure bilateral symmetry development and early leaf margin patterning, probably via the regulation of auxin and CUC2 distribution.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9ZV57}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- At1g52910
- Protein MODIFYING WALL LIGNIN-1
- Protein MODIFYING WALL LIGNIN-2
- At4g27438
Sequence:
MARNVGFFICILILAMDVSAGILGIEAEIAQNKVKHLKMWIFECRDPSYTAFKYGLAACILLVLAHVTANFLGGCLCVASRQDLEKSSANKQLAVASLIFTWIILAIAFSMLIVGTMANSRSRKNCGISHHRVLSIGGILCFVHGLFAVAYYISATASTREQTSAGHA
Protein: Potassium channel subfamily K member (Q5TZ59)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Potassium channel, subfamily K, member 9
- Bicaudal C homolog 2.
- ATPase 13A3.
- Eukaryotic translation initiation factor 2 alpha kinase 4.
Sequence:
MKRQNIRTLVLIICTFTYLLVGAAVFDALESKMEITQKKILDDRKRELMDKYNLSKVNFDELERVVLQLKPHKAGVQWRFAGSFYFAITVITTIGYGHAAPSTDGGKVFCMFYALLGIPLTLVMFQSLGERINTFVKYLLHRLKKCLGLRHTEVSMANMVCIGLISCMSTLCVGAAAFSRYEDWSFFHAYYYCFITLTTIGFGDYVALQKDNALQTNPQYVAFSFMYILTGLTVIGAFLNLVVLRFMTMNAEDERRDAEQRTLLSRNRQSGGAGTNHCISDPPSSSTAGHGGGSGKGLCNVYAEVLHFQSMCSCLWYKSQEKMRYSIPMIISHDLSTSDTYMEHSETSDVLHSNGCVCSALQEHSAASSVYTGLLSPAHYQRLSKRRSSI
Protein: Transcription factor GATA-6 (GATA-binding factor 6) (Q92908)
Organism: Homo sapiens (Human)
Function: Transcriptional activator. Regulates SEMA3C and PLXNA2. Involved in gene regulation specifically in the gastric epithelium. May regulate genes that protect epithelial cells from bacterial infection. Involved in bone morphogenetic protein (BMP)-mediated cardiac-specific gene expression (By similarity). Binds to BMP response element (BMPRE) DNA sequences within cardiac activating regions (By similarity). In human skin, controls several physiological processes contributing to homeostasis of the upper pilosebaceous unit. Triggers ductal and sebaceous differentiation as well as limits cell proliferation and lipid production to prevent hyperseborrhoea. Mediates the effects of retinoic acid on sebocyte proliferation, differentiation and lipid production. Also contributes to immune regulation of sebocytes and antimicrobial responses by modulating the expression of anti-inflammatory genes such as IL10 and pro-inflammatory genes such as IL6, TLR2, TLR4, and IFNG. Activates TGFB1 signaling which controls the interfollicular epidermis fate.
Subcellular location: Nucleus {ECO:0000269|PubMed:19666519, ECO:0000269|PubMed:27756709}.
Interaction partners:
- LIM and cysteine-rich domains protein 1
- Zinc finger protein ZFPM2
- Lysyl oxidase homolog 2
- Homeobox protein CDX-2
- Hepatocyte nuclear factor 3-alpha
- Homeobox protein Nkx-2.1
- Homeobox protein Nkx-2.5
- Hepatocyte nuclear factor 3-beta
- Transcription factor SOX-17
- Homeobox protein NANOG
Sequence:
MALTDGGWCLPKRFGAAGADASDSRAFPAREPSTPPSPISSSSSSCSRGGERGPGGASNCGTPQLDTEAAAGPPARSLLLSSYASHPFGAPHGPSAPGVAGPGGNLSSWEDLLLFTDLDQAATASKLLWSSRGAKLSPFAPEQPEEMYQTLAALSSQGPAAYDGAPGGFVHSAAAAAAAAAAASSPVYVPTTRVGSMLPGLPYHLQGSGSGPANHAGGAGAHPGWPQASADSPPYGSGGGAAGGGAAGPGGAGSAAAHVSARFPYSPSPPMANGAAREPGGYAAAGSGGAGGVSGGGSSLAAMGGREPQYSSLSAARPLNGTYHHHHHHHHHHPSPYSPYVGAPLTPAWPAGPFETPVLHSLQSRAGAPLPVPRGPSADLLEDLSESRECVNCGSIQTPLWRRDGTGHYLCNACGLYSKMNGLSRPLIKPQKRVPSSRRLGLSCANCHTTTTTLWRRNAEGEPVCNACGLYMKLHGVPRPLAMKKEGIQTRKRKPKNINKSKTCSGNSNNSIPMTPTSTSSNSDDCSKNTSPTTQPTASGAGAPVMTGAGESTNPENSELKYSGQDGLYIGVSLASPAEVTSSVRPDSWCALALA
Protein: Corrinoid adenosyltransferase MMAB (EC 2.5.1.-) (ATP:co(I)rrinoid adenosyltransferase MMAB) (Methylmalonic aciduria type B homolog) (Q9D273)
Organism: Mus musculus (Mouse)
Function: Converts cob(I)alamin to adenosylcobalamin (adenosylcob(III)alamin), a coenzyme for methylmalonyl-CoA mutase, therefore participates in the final step of the vitamin B12 conversion. Generates adenosylcobalamin (AdoCbl) and directly delivers the cofactor to MUT in a transfer that is stimulated by ATP-binding to MMAB and gated by MMAA.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q96EY8}.
Interaction partners:
- Cobalamin trafficking protein CblD
- Mevalonate kinase
- Methylmalonic aciduria type A homolog, mitochondrial
- Cyanocobalamin reductase / alkylcobalamin dealkylase
- Methylmalonyl-CoA mutase, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
Sequence:
MAVWLFGGRLGLRGRLSACRLLCPRFQSRGPQGGEDGDRLQPSSTAAKIPKIYTKTGDKGFSSTFTGERRPKDDQVFEAVGTTDELSSAIGFAMELVTEKGHMFAEELQKIQCMLQDVGSALATPRSSAREAHLKHTAFQEGPVLELERWIDKYSSQLPPLKAFILPSGGKSSSALHFCRAVCRRAERRVVPLVQMGETDANVAKFLNRLSDYLFTVARYAAMKEGSQEKIYKKHDV
Protein: Protein phosphatase 1 regulatory subunit 17 (G substrate) (Q9Z2E4)
Organism: Mus musculus (Mouse)
Function: Inhibits phosphatase activities of protein phosphatase 1 (PP1) and protein phosphatase 2A (PP2A) complexes.
Interaction partners:
- cGMP-dependent protein kinase 1
- cGMP-dependent protein kinase 2
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
Sequence:
MSTEMMTTEPVPPLELSDDILGKLDPQCSPSDDLSDQFIKDCDLKKKPRKGKNVQATLNVESDQKKPRRKDTPAVHIPPFIPGVISEHLIKRYDVQERIPKAKSGPALHNSDMEQKRPRRKDTPALHMPPFVAGLTLLRDESAGVILEDEEMDGDKLAI
Protein: C2H2-type zinc finger family protein (Q9LZD5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Ac-like transposase
- HAT family dimerization domain-containing protein
- Probable histone H2A.2
- Defensin-like protein 11
- AGAMOUS-like 57
- Probable transcription factor At4g00130
- Probable protein phosphatase 2C 49
- Duplicated homeodomain-like superfamily protein
- Protein FAR1-RELATED SEQUENCE 6
Sequence:
MTSVLEESGDHARLVLLIKGKRTKRQRSASPLMMNAAAVSSVCSGERSSVEVREEEAAGEVEFQGATDEDEDMANCLILLSQGHQAKSSDDHLSMQRMGFFSNKKPVASLGLGLDGVYQCKTCDKSFHSFQALGGHRASHKKPKLGASVFKCVEKKTASASTVETVEAGAVGSFLSLQVTSSDGSKKPEKTHECSICKAEFSSGQALGGHMRRHRGLTINANATSAIKTAISSSSHHHHEESIRPKNFLQLDLNLPAPEDERCCEKPKFAFASKDQILLFTAASNSLIDCHH
Protein: Death-associated protein kinase 2 (DAP kinase 2) (EC 2.7.11.1) (DAP-kinase-related protein 1) (DRP-1) (Q8VDF3)
Organism: Mus musculus (Mouse)
Function: Calcium/calmodulin-dependent serine/threonine kinase involved in multiple cellular signaling pathways that trigger cell survival, apoptosis, and autophagy. Capable of regulating both type I apoptotic and type II autophagic cell death signals. The former involves caspase activation, chromatin and mitochondrial condensation while the latter involves caspase-independent cell death in conjunction with accumulation of mature autophagic vesicles, plasma membrane blebs, and nuclear condensation without DNA degradation. Mediator of anoikis and a suppressor of beta-catenin-dependent anchorage-independent growth of malignant epithelial cells. May play a role in granulocytic maturation (By similarity). Regulates granulocytes motility by controlling cell spreading and polarization.
Subcellular location: Cytoplasm {ECO:0000250}. Cytoplasmic vesicle, autophagosome lumen {ECO:0000250}.
Interaction partners:
- Beclin-1
- Mitogen-activated protein kinase 3
- Mitogen-activated protein kinase 1
- Death-associated protein kinase 1
- Death-associated protein kinase 3
Sequence:
MVQASMRSPNMETFKQQKVEDFYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRASRRGVCREEIEREVSILRQVLHPNIITLHDVYENRTDVVLILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEEFFSQTSELAKDFIRKLLVKETRKRLTIQEALRHPWITPVDTQQAMVRRESVVNLENFKKQYVRRRWKLSFSIVSLCNHLTRSLMKKVHLRTSEDLRNCESDTEENIARRKALHPRRRSSTS
Protein: T-cell immunoglobulin and mucin domain-containing protein 2 (TIMD-2) (T-cell immunoglobulin mucin receptor 2) (TIM-2) (T-cell membrane protein 2) (Q8R183)
Organism: Mus musculus (Mouse)
Function: Cell surface glycoprotein that participates in iron homeostasis in the liver, the kidney, the retina and oligodendrocytes by acting as a receptor of H-ferritin. Mechanistically, mediates iron-containing ferritin uptake via an endocytic pathway, trafficking to endosomes and subsequently to lysosomes. Plays also an important role in the regulation of Th2 immunity. Receptor for SEMA4A involved in the regulation of T-cell function, enhancing T-cell activation.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17363299, ECO:0000269|PubMed:21886823}; Single-pass type I membrane protein {ECO:0000269|PubMed:17363299}.
Interaction partners:
- Semaphorin-4A
- Ferritin heavy chain
- B-cell differentiation antigen CD72
Sequence:
MNQIQVFISGLILLLPGAVESHTAVQGLAGHPVTLPCIYSTHLGGIVPMCWGLGECRHSYCIRSLIWTNGYTVTHQRNSLYQLKGNISEGNVSLTIENTVVGDGGPYCCVVEIPGAFHFVDYMLEVKPEISTSPPTRPTATGRPTTISTRSTHVPTSTRVSTSTSPTPAHTETYKPEATTFYPDQTTAEVTETLPDTPADWHNTVTSSDDPWDDNTEVIPPQKPQKNLNKGFYVGISIAALLILMLLSTMVITRYVVMKRKSESLSFVAFPISKIGASPKKVVERTRCEDQVYIIEDTPYPEEES
Protein: Acetate/butyrate--CoA ligase AAE7, peroxisomal (EC 6.2.1.1) (EC 6.2.1.2) (AMP-binding protein 7) (AtAMPBP7) (Acetyl-CoA synthetase) (Acyl-activating enzyme 7) (Butyryl-CoA synthetase) (Protein ACETATE NON-UTILIZING 1) (Q8VZF1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Peroxisomal acetate/butyrate--CoA ligase that is probably involved in the activation of exogenous acetate for entry into the glyoxylate cycle. May play a role to prevent carbon loss from peroxisomes during lipid mobilization. In vitro, is active with both acetate and butyrate.
Subcellular location: Peroxisome {ECO:0000269|PubMed:15533942}.
Interaction partners:
- Malate synthase
- Acetyl-coenzyme A synthetase, chloroplastic/glyoxysomal
- Citrate synthase 3, peroxisomal
- Aldehyde dehydrogenase family 3 member H1
- Aldehyde dehydrogenase family 2 member B4, mitochondrial
- Citrate synthase 2, peroxisomal
- Citrate synthase 4, mitochondrial
- Citrate synthase 5, mitochondrial
- Citrate synthase 1, peroxisomal
- Acetyl-CoA acetyltransferase 1
Sequence:
MAATKWRDIDDLPKIPANYTALTPLWFLDRAAVVHPTRKSVIHGSREYTWRQTYDRCRRLASALADRSIGPGSTVAIIAPNIPAMYEAHFGVPMCGAVLNCVNIRLNAPTVAFLLSHSQSSVIMVDQEFFTLAEDSLRLMEEKAGSSFKRPLLIVIGDHTCAPESLNRALSKGAIEYEDFLATGDPNYPWQPPADEWQSIALGYTSGTTASPKGVVLHHRGAYIMALSNPLIWGMQDGAVYLWTLPMFHCNGWCFPWSLAVLSGTSICLRQVTAKEVYSMIAKYKVTHFCAAPVVLNAIVNAPKEDTILPLPHTVHVMTAGAAPPPSVLFSMNQKGFRVAHTYGLSETYGPSTVCAWKPEWDSLPPETQAKLNARQGVRYTGMEQLDVIDTQTGKPVPADGKTAGEIVFRGNMVMKGYLKNPEANKETFAGGWFHSGDIAVKHPDNYIEIKDRSKDVIISGGENISSVEVENVVYHHPAVLEASVVARPDERWQESPCAFVTLKSDYEKHDQNKLAQDIMKFCREKLPAYWVPKSVVFGPLPKTATGKIQKHILRTKAKEMGPVPRSRL
Protein: Proteasome subunit beta type-4 (26 kDa prosomal protein) (HsBPROS26) (PROS-26) (Macropain beta chain) (Multicatalytic endopeptidase complex beta chain) (Proteasome beta chain) (Proteasome chain 3) (HsN3) (Proteasome subunit beta-7) (beta-7) (P28070)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). SMAD1/OAZ1/PSMB4 complex mediates the degradation of the CREBBP/EP300 repressor SNIP1.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Nucleus {ECO:0000269|PubMed:12181345, ECO:0000269|PubMed:34711951}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000269|PubMed:34711951}.
Interaction partners:
- Proteasome subunit beta type-10
- Proteasome subunit alpha type-7
- 26S proteasome regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 4
- Proteasome subunit alpha type-2
- 26S proteasome regulatory subunit 6B
- 26S proteasome non-ATPase regulatory subunit 11
- Proteasome subunit alpha type-1
- Proteasome subunit beta type-6
- 26S proteasome non-ATPase regulatory subunit 6
Sequence:
MEAFLGSRSGLWAGGPAPGQFYRIPSTPDSFMDPASALYRGPITRTQNPMVTGTSVLGVKFEGGVVIAADMLGSYGSLARFRNISRIMRVNNSTMLGASGDYADFQYLKQVLGQMVIDEELLGDGHSYSPRAIHSWLTRAMYSRRSKMNPLWNTMVIGGYADGESFLGYVDMLGVAYEAPSLATGYGAYLAQPLLREVLEKQPVLSQTEARDLVERCMRVLYYRDARSYNRFQIATVTEKGVEIEGPLSTETNWDIAHMISGFE
Protein: Exonuclease domain-containing protein (Q580Z1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Pab1p-dependent poly
- Proliferating cell nuclear antigen
Sequence:
MGRRKCSASTVKRPGGPDATTGSNEGAREAPVEGVMNAAGEPNTSEAQPLQSQEGEKDGEKGVAAAITEHFSTVEIYFQPAAEKRRGGCFYPRDIGTLLLWSVPSPVPLVEGPRVIFVKNRSKLRDVVVLYVNGWTHDEMLLGATAAPAIQNTANGAQGNKSSLKGKNGKRPREGNDEKGATQRNTVERQCSESIGRAMLCPIRQQQCWARPECGVQFAPMIVQEGNSRVERDIFWRGGKPATPVGGQHSQEGEQQSNGARAAATKGENRSSGTDSSAPRGVGALFNRALTIANGTSNTSSAQSDDKLPTPLESLKVLSSPPGGGPSLWDDRDLLLKYALSLERDKATLEALGFAVGVPDHDEPSTWESFDAVGSAADANCADKTKNSLPNVFALDCEMVLVKNNVSALARVTLVDVRASSVVVDTLVKPDEEVVDYVTRFSGIDSGMLEGVTTTLKDCQQKLKRYVTKDAFLVGHSLENDLRACKMLPNCWLLDTAHLFPHPSGLPCKNSLRYLALRYLKKSIQQGSHDSEIDACTSAELVYLKMQHGPDFGLHTRVNVLKLMEEVSVTGEASDERQGGPPTVNSPISVELNLFDDACVLSDIVPNNRGKGGVAVNAVPVRHDGDAVRKAVRCLEKRRNAPKDAGDDVAVSYALTWVQLTQTVVPKNAEVANEETPSWEELQRERVDETNRHVMQVVQAAPHNSLIVVVVAGSSNDTNKSKKCGEDAASAPAGGAAPRGACFAFVKDDNAVGPLAAWLNKGLTDNGDGAKDETNASDGLRSIPACEQQ
Protein: Calcium-dependent secretion activator (G3MU01)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MKSINEWLTERLQQSLSATQYISLSTIVKKVYQDFSLQGIDEERLNSKTYQSISRRLQLEESNSHIQEAAINGSAQGSVFPTSLGNATAAVSNMSSMVEGAGAKMFSLFK
Protein: Splicing factor 3B subunit 4 (Spliceosome-associated protein 49) (Q09442)
Organism: Caenorhabditis elegans
Function: Subunit of the splicing factor SF3B required for 'A' complex assembly formed by the stable binding of U2 snRNP to the branchpoint sequence (BPS) in pre-mRNA. Sequence independent binding of SF3A/SF3B complex upstream of the branch site is essential, it may anchor U2 snRNP to the pre-mRNA. May also be involved in the assembly of the 'E' complex. SF3B4 has been found in complex 'B' and 'C' as well. Belongs also to the minor U12-dependent spliceosome, which is involved in the splicing of rare class of nuclear pre-mRNA intron (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- PSP proline-rich domain-containing protein
- Splicing factor 3B subunit 3
- PHD finger-like domain-containing protein 5A
- Splicing factor 3B subunit 1 domain-containing protein
- Probable U2 small nuclear ribonucleoprotein A'
- Splicing factor 3A subunit 2
- Pre-RNA processing 21
- Splicing factor 3B subunit 6-like protein
- Matrin-type domain-containing protein
- RRM domain-containing protein
Sequence:
MSAGPIVERNQDATIYVGGLDEKVSESILWELMVQAGPVVSVNMPKDRVTANHQGFGFVEFMGEEDADYAIKILNMIKLYGKPIKVNKASAHEKNMDVGANIFVGNLDPEVDEKLLYDTFSAFGVILQVPKIMRDVDSGTSKGFAFINFASFEASDTALEAMNGQFLCNRAITVSYAFKRDSKGERHGTAAERMLAAQNPLFPKDRPHQVFSDVPLGVPANTPLAMPGVHAAIAAHATGRPGYQPPPLMGMAQSGYQGQYPPVPPPPPSVTPMPPPMPPTPGMTPRPPPPPSSGMWPPPPPPPPGRTPGPPGMPGMPPPPPPSRFGPPGMGGMPPPPPPGMRYPGGMPPPPPPRYPSAGPGMYPPPPPSRPPAPPSGHGMIPPPPPPS
Protein: Growth arrest-specific protein 6 (GAS-6) (AXL receptor tyrosine kinase ligand) (Q61592)
Organism: Mus musculus (Mouse)
Function: Ligand for tyrosine-protein kinase receptors AXL, TYRO3 and MER whose signaling is implicated in cell growth and survival, cell adhesion and cell migration. GAS6/AXL signaling plays a role in various processes such as endothelial cell survival during acidification by preventing apoptosis, optimal cytokine signaling during human natural killer cell development, hepatic regeneration, gonadotropin-releasing hormone neuron survival and migration, platelet activation, or regulation of thrombotic responses.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Tyrosine-protein kinase Mer
- Tyrosine-protein kinase receptor UFO
- Tyrosine-protein kinase receptor TYRO3
- Lactadherin
- Tubby-related protein 1
- Vitamin K-dependent protein S
- T-cell immunoglobulin and mucin domain-containing protein 4
- Glucocorticoid receptor
- Furin
- Galectin-3
Sequence:
MPPPPGPAAALGTALLLLLLASESSHTVLLRAREAAQFLRPRQRRAYQVFEEAKQGHLERECVEEVCSKEEAREVFENDPETEYFYPRYQECMRKYGRPEEKNPDFAKCVQNLPDQCTPNPCDKKGTHICQDLMGNFFCVCTDGWGGRLCDKDVNECVQKNGGCSQVCHNKPGSFQCACHSGFSLASDGQTCQDIDECTDSDTCGDARCKNLPGSYSCLCDEGYTYSSKEKTCQDVDECQQDRCEQTCVNSPGSYTCHCDGRGGLKLSPDMDTCEDILPCVPFSMAKSVKSLYLGRMFSGTPVIRLRFKRLQPTRLLAEFDFRTFDPEGVLFFAGGRSDSTWIVLGLRAGRLELQLRYNGVGRITSSGPTINHGMWQTISVEELERNLVIKVNKDAVMKIAVAGELFQLERGLYHLNLTVGGIPFKESELVQPINPRLDGCMRSWNWLNGEDSAIQETVKANTKMQCFSVTERGSFFPGNGFATYRLNYTRTSLDVGTETTWEVKVVARIRPATDTGVLLALVGDDDVVPISVALVDYHSTKKLKKQLVVLAVEDVALALMEIKVCDSQEHTVTVSLREGEATLEVDGTKGQSEVSTAQLQERLDTLKTHLQGSVHTYVGGLPEVSVISAPVTAFYRGCMTLEVNGKILDLDTASYKHSDITSHSCPPVEHATP