wanglab/gogpt-training-data huggingface dataset:
Protein: Cholesterol 22-monohydroxylase CYP90B51 (EC 1.14.14.-) (Cytochrome P450 CYP90B51) (PpCYP90B51) (A0A517FNC6)
Organism: Trigonella foenum-graecum (Fenugreek)
Function: Canonical brassinosteroid (BR)-biosynthetic enzyme capable of converting cholesterol to 22S-hydroxycholesterol via sterol-C22 hydroxylation.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSDSDITFYCLSSILSVLLIFIFILIKRKQAKPKLNLPPGKMGWPFLGETIGYLKPYSATTLGEFMDQHIARYGKIYKSKLFGEPAIVSADAGLNRFILQNEGKLFECSYPRSIGGILGKWSMLVLVGDMHRDMRLISLNFLSHARLRTHLLKEVEKHTRLVISSWKENSTFAAQDEAKKFTFNLMAEHIMSLQPGKIETEKLKKEYVTFMKGVVSAPLNFPGTAYWKALKSRGTILKFIEGKMEERIKRMKEGNENLEEDDLLNWVLKHSNLSTEQILDLILSLLFAGHETSSVSIALAIYFLPGCPQAILQLREEHKEIARAKKQAGETELTWEDYKKMEFTHCVVNETLRLGNVVRFLHRKALKDVRYKGYDIPCGWKVLPVIAAVHLDPLLFDQPQHFNPWRWQNNGNCPNFSGASSNSNNIFLPFGGGPRLCAGSELAKLEMAVFIHHLILNYHWELTDNNDQAFAYPFVDFPKGLQIRVQSHSLI
Protein: CUB and zona pellucida-like domain-containing protein 1 (CUB and ZP domain-containing protein 1) (Integral membrane-associated protein 1) (P70412)
Organism: Mus musculus (Mouse)
Function: Localized to zymogen granules, where it functions in trypsinogen activation. May indirectly regulate cell motility, cell-cell and cell/extracellular matrix interactions (By similarity).
Subcellular location: Zymogen granule membrane {ECO:0000269|PubMed:12401800}; Single-pass type I membrane protein {ECO:0000269|PubMed:12401800}.
Interaction partners:
Sequence:
MEVTGRLFIWAILAVSCGAQLNSTEAEGKSRCTASLGGANLGETHKALVLQLSANENCTWTIERPENRSIRIIFSYIKLDPGSRCETENIKVFDGSSTSGPLLGKACSRNDFVPVFESSSNSMTFQIVTGLTKFPRSVFIFYYFFSAATVIPNCGGDLRALEGSFSSPNYPKPHPELAYCVWHIQVGKGYKIQLKFTDLLLEMDENCKFDFIAVYDGPSTTAGLLKQLCGRGKPTLESSSDAMTVVLSTDYANSYKGFSASYTSIYIHDVNTTSLSCVSDKMRVIISKSYLPALNYNESNLQLNDPTCRPNVSNVIEFSIPLHECGTVKKIEDHAISYTNRITFIESPVSAVITRQKLLQIVVTCEMEYNSTVEIMYITEDDIIQNQSVLGKYNTSLALYESDSFENLVQESPYYVDLNQTLFVQATLHTSDPSLVVFLDTCRASPTSDFASPTYDLISSGCCQDETCKVYPLFGHYGRFQFNAFKFLKHLNSVYLKCKILICDNNDQTSRCNQGCVPRRKRDIPSYKWKTDSVIGPIRLKRDRSASRDSGLLPQIHEAEISNQPLSRLYLFSFMVLALNVVIVAITTVKHFLNRWMDHRYQKLQVY
Protein: Receptor protein-tyrosine kinase (EC 2.7.10.1) (G3V6K6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- SHC-transforming protein 1
- Growth factor receptor-bound protein 2
- Protransforming growth factor alpha
- Proepiregulin
- Amphiregulin
- Probetacellulin
- Proto-oncogene tyrosine-protein kinase Src
- Tyrosine-protein phosphatase non-receptor type 11
- Focal adhesion kinase 1
Sequence:
MRPSGTARTKLLLLLAALCAAGGALEEKKVCQGTSNRLTQLGTFEDHFLSLQRMFNNCEVVLGNLEITYVQRNYDLSFKTIQEVAGYVLIALNTVERIPLENLQIIRGNALYENTYALAVLSNYGTNKTGLRELPMRNLQEILIGAVRFSNNPILCNMETIQWRDIVQDVFLSNMSMDVQRHLTGCPKCDPSCPNGSCWGRGEENCQKLTKIICAQQCSRRCRGRSPSDCCHNQCAAGCTGPRESDCLVCHRFRDEATCKDTCPPLMLYNPTTYQMDVNPEGKYSFGATCVKKCPRNYVVTDHGSCVRACGPDYYEVEEDGVSKCKKCDGPCRKVCNGIGIGEFKDTLSINATNIKHFKYCTAISGDLHILPVAFKGDSFTRTPPLDPRELEILKTVKEITGFLLIQAWPENWTDLHAFENLEIIRGRTKQHGQFSLAVVGLNITSLGLRSLKEISDGDVIISGNRNLCYANTINWKKLFGTPNQKTKIMNNRAEKDCKATNHVCNPLCSSEGCWGPEPTDCVSCQNVSRGRECVDKCNILEGEPREFVENSECIQCHPECLPQTMNITCTGRGPDNCIKCAHYVDGPHCVKTCPSGIMGENNTLVWKFADANNVCHLCHANCTYGCAGPGLKGCQQPEGPKIPSIATGIVGGLLFIVVVALGIGLFMRRRHIVRKRTLRRLLQERELVEPLTPSGEAPNQAHLRILKETEFKKIKVLGSGAFGTVYKGLWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQLMPYGCLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESILHRIYTHQSDVWSYGVTVWELMTFGSKPYDGIPASEISSILEKGERLPQPPICTIDVYMIMVKCWMIDADSRPKFRELILEFSKMARDPQRYLVIQGDERMHLPSPTDSNFYRALMEEEDMEDVVDADEYLIPQQGFFNSPSTSRTPLLSSLSANSNSSAVACINRNGSCRVKEDAFLQRYSSDPTSVLTEDNIDDTFLPVPEYINQSVPKRPAGSVQNPVYHNQPLHPAPGRDLHYQNPHSNAVSNPEYLNTAQPTCLSSGFDSSALWIQKGSHQMSLDNPDYQQDFFPKEAKPNGIFKGPTAENAEYLRVAPPSSEFIGA
Protein: E3 ubiquitin-protein ligase mib1 (EC 2.3.2.27) (Protein mind bomb) (RING-type E3 ubiquitin transferase mib1) (Q804S5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: E3 ubiquitin-protein ligase that mediates ubiquitination of Delta receptors, which act as ligands of Notch proteins. Positively regulates the Delta-mediated Notch signaling by ubiquitinating the intracellular domain of Delta, leading to endocytosis of Delta receptors. It thereby participates in many processes regulated by the Notch signaling pathway, such as midline cell fate specification prior to germ layer formation, patterning of sensory cell differentiation in the ear, neurogenesis of the hindbrain and commitment to a secretory fate in the intestine. Essential for early embryonic development.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. Cytoplasm. Cell membrane. Note=Localizes to the plasma membrane.
Interaction partners:
- Delta-like protein D
- Erythrocyte membrane protein band 4.1-like 5.
- Delta-like protein C
- Delta-like protein A
- Mindbomb E3 ubiquitin protein ligase 2.
- Protein jagged-1a
- Delta-like protein
- Sorting nexin
Sequence:
MTTGRNNRVMMEGVGARVIRGPDWKWGKQDGGEGHVGTVRSFESPEEVVVVWDNGTAANYRCSGAYDVRILDSAPTGIKHDGTMCDTCRQQPIIGIRWKCAECTNYDLCTTCYHGDKHHLRHRFYRITTPGSERVLLESRRKSKKITARGIFAGGRVVRGVDWQWEDQDGGNGRRGKVTEIQDWSAASPHSAAYVLWDNGAKNLYRVGFEGMSDLKCVQDAKGGTFYRDHCPVLGEQNGNRNPGGLQIGDLVNIDLDLEIVQSLQHGHGGWTDGMFETLTTTGTVCGIDEDHDIVVQYPSGNRWTFNPAVLTKANVVRSGEVAAGAEGGSSQFMVGDLVQICYDIDRIKLLQRGHGEWAEAMLPTLGKVGRVQQIYSDSDLKVEVCGTSWTYNPAAVTKVAPAGSAVTNASGERLSQLLKKLFETQESGDINEELVKAAANGDLAKVEDILKRPDVDVNGQCAGHTAMQAASQNGHVDVLKLLLKHSVDLEAEDKDGDRAVHHASFGDEGSVIEVLHRGGADLNARNKRRQTPLHIAVNKGHLQVVKTLLDFGCHPSLQDSEGDTPLHDAISKKRDDMLSVLLEAGADVTITNNNGFNALHHAALRGNPSAMRVLLSKLPRPWIVDEKKDDGYTALHLAALNNHVEVAELLVHQGNANLDVQNVNQQTALHLAVERQHTQIVRLLVRAEAKLDVQDKDGDTPLHEALRHHTLSQLRQLQDMQDVSKVEPWEPSKNTLIMGLGTQGAEKKSAASIACFLAANGADLTIRNKKGQSPLDLCPDPSLCKALAKCHKEKTSGQVGSRSPSLNSNNETLEECMVCSDMKRDTLFGPCGHIATCSLCSPRVKKCLICKEQVQSRTKIEECVVCSDKKAAVLFQPCGHMCACENCASLMKKCVQCRAVVERRTPFVLCCGGKGMEDATDDEDLTGGSNSMAGGSQDLLQPNNLALSWSSGNIPALQRDKDNTNVNADVQKLQQQLQDIKEQTMCPVCLDRLKNMIFMCGHGTCQLCGDRMSECPICRKAIERRILLY
Protein: Threonine synthase 1, chloroplastic (EC 4.2.3.1) (Protein METHIONINE OVER-ACCUMULATOR 2) (Q9S7B5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the gamma-elimination of phosphate from L-phosphohomoserine and the beta-addition of water to produce L-threonine.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- Threonine dehydratase biosynthetic, chloroplastic
- Homoserine kinase
- Probable low-specificity L-threonine aldolase 2
- Low-specificity L-threonine aldolase 1
- Phosphoserine aminotransferase 1, chloroplastic
- Phosphoserine aminotransferase 2, chloroplastic
- Threonine synthase 2, chloroplastic
- Cystathionine gamma-synthase 1, chloroplastic
- Probable cystathionine gamma-synthase 2
- Diaminopimelate decarboxylase 2, chloroplastic
Sequence:
MASSCLFNASVSSLNPKQDPIRRHRSTSLLRHRPVVISCTADGNNIKAPIETAVKPPHRTEDNIRDEARRNRSNAVNPFSAKYVPFNAAPGSTESYSLDEIVYRSRSGGLLDVEHDMEALKRFDGAYWRDLFDSRVGKSTWPYGSGVWSKKEWVLPEIDDDDIVSAFEGNSNLFWAERFGKQFLGMNDLWVKHCGISHTGSFKDLGMTVLVSQVNRLRKMKRPVVGVGCASTGDTSAALSAYCASAGIPSIVFLPANKISMAQLVQPIANGAFVLSIDTDFDGCMKLIREITAELPIYLANSLNSLRLEGQKTAAIEILQQFDWQVPDWVIVPGGNLGNIYAFYKGFKMCQELGLVDRIPRMVCAQAANANPLYLHYKSGWKDFKPMTASTTFASAIQIGDPVSIDRAVYALKKCNGIVEEATEEELMDAMAQADSTGMFICPHTGVALTALFKLRNQGVIAPTDRTVVVSTAHGLKFTQSKIDYHSNAIPDMACRFSNPPVDVKADFGAVMDVLKSYLGSNTLTS
Protein: DNA N6-methyl methyltransferase (EC 2.1.1.72) (DNA N6 adenine methyltransferase 1) (Q09956)
Organism: Caenorhabditis elegans
Function: Methylates DNA on the 6th position of adenine (N(6)-methyladenosine). N(6)-methyladenosine (m6A) DNA is involved in epigenetic transgenerational inheritance.
Interaction partners:
- DNA N6-methyl adenine demethylase
- Lysine-specific histone demethylase 1
- Putative ammonium transporter 3
- Putative ammonium transporter 2
- U6 small nuclear RNA
Sequence:
MDTEFAILDEEKYYDSVFKELNLKTRSELYEISSKFMPDSQFEAIKRRGISNRKRKIKETSENSNRMEQMALKIKNVGTELKIFKKKSILDNNLKSRKAAETALNVSIPSASASSEQIIEFQKSESLSNLMSNGMINNWVRCSGDKPGIIENSDGTKFYIPPKSTFHVGDVKDIEQYSRAHDLLFDLIIADPPWFSKSVKRKRTYQMDEEVLDCLDIPVILTHDALIAFWITNRIGIEEEMIERFDKWGMEVVATWKLLKITTQGDPVYDFDNQKHKVPFESLMLAKKKDSMRKFELPENFVFASVPMSVHSHKPPLLDLLRHFGIEFTEPLELFARSLLPSTHSVGYEPFLLQSEHVFTRNISL
Protein: Endomucin (Endomucin-2) (Gastric cancer antigen Ga34) (Mucin-14) (MUC-14) (Q9ULC0)
Organism: Homo sapiens (Human)
Function: Endothelial sialomucin, also called endomucin or mucin-like sialoglycoprotein, which interferes with the assembly of focal adhesion complexes and inhibits interaction between cells and the extracellular matrix.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type I membrane protein. Membrane; Single-pass type I membrane protein. Note=Consistently localized to the plasma membrane and less abundantly to Golgi-like perinuclear stacks.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000305}.
Interaction partners:
- tRNA N6-adenosine threonylcarbamoyltransferase
- Platelet endothelial cell adhesion molecule
- Mucin-1
- Cadherin-5
- Adhesion G protein-coupled receptor L4
- L-selectin
- Hematopoietic progenitor cell antigen CD34
- Angiopoietin-1 receptor
- Lymphatic vessel endothelial hyaluronic acid receptor 1
- Podocalyxin
Sequence:
MELLQVTILFLLPSICSSNSTGVLEAANNSLVVTTTKPSITTPNTESLQKNVVTPTTGTTPKGTITNELLKMSLMSTATFLTSKDEGLKATTTDVRKNDSIISNVTVTSVTLPNAVSTLQSSKPKTETQSSIKTTEIPGSVLQPDASPSKTGTLTSIPVTIPENTSQSQVIGTEGGKNASTSATSRSYSSIILPVVIALIVITLSVFVLVGLYRMCWKADPGTPENGNDQPQSDKESVKLLTVKTISHESGEHSAQGKTKN
Protein: Response regulator 6 (Q9FRY9)
Organism: Zea mays (Maize)
Interaction partners:
Sequence:
MPSQSTHTSSSLSSSTAPILPCSSAAALFRSVMAAVATETPFHVLAVDDSLPDRKLIERLLKTSSFQVTTVDSGSKALQFLGLHDQDSTVPPVHTHQLDVAANQDVAVNLIITDYCMPGMTGYDLLKKIKESSSLRDIPVVIMSSENIPSRINRCLEEGADEFFLKPVRLSDMNKLKPHILKSRCNQEQHQQSDSHSGERRNPTISSSDSINNRKRKGAGTEEILPQLANRSRHS
Protein: Cytochrome c oxidase subunit 4, mitochondrial (Cytochrome c oxidase polypeptide IV) (P04037)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of COX2 and heme A of COX1 to the active site in COX1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:30598554}.
Interaction partners:
- Cytochrome b-c1 complex subunit 10, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 8, mitochondrial
- Cytochrome b
- Respiratory supercomplex factor 2, mitochondrial
- Cytochrome c oxidase subunit 7, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome c oxidase subunit 13, mitochondrial
- Cytochrome c oxidase subunit 3
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
Sequence:
MLSLRQSIRFFKPATRTLCSSRYLLQQKPVVKTAQNLAEVNGPETLIGPGAKEGTVPTDLDQETGLARLELLGKLEGIDVFDTKPLDSSRKGTMKDPIIIESYDDYRYVGCTGSPAGSHTIMWLKPTVNEVARCWECGSVYKLNPVGVPNDDHHH
Protein: TPR repeat-containing protein (Q54T23)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNIEELEIFKDYQLLSLLNIGSHVLKDTYKNRNKTQFTNKSYLKQLEVAQIQNINKNGIWQIASTSELLLSSNNNNNNNNNNNNNNNNNNNNNNNNNNKNNKNKSTLPSAQQLIIENKAIEIIKLIDRNKNIEILNNSNKGYFTKERVRQIINGGNKEFDENQEFTKKLINESNELFKNRKFKESLEYYNSKLILCKNIDIDNNNNNDNNDDGGDYGDESKLFKIKSFGYLGSSRCDYEIYKELTESKNSIDNEIVTLEYKDLISLDKLKYSLSYDPFNSECYYEIAFLLCKNNNSFYNLALNHLEIAILLLSTNDSINNEKYKQLQSTILEKSLKQEKEKKEKEKQEKEMDNFELKAIEYVKSNPIPLEFQSIINSNDIDKIYELSLKLSDYNNINTNDGNDSLNKVYNYKLSMDLLYNGSLLKPLETYNEIEKKRFYSTFTNILLEIGYRYFNGCGYLDADNVCALYYFGLVTKQFTLFNSNCFHLTTLAFMFSFPNRNIPKPILDTIILPMLLKGSSVGNLKCQKLYCLLTGKDLNKTFKTIGNSESIEEIQSKRMNEKIQNDDRYDFEIKQYEYNSIKRLNKGSKKQINRLIKTLDLKNQFLSLFENYINDNNIEKLTQANKILIEALKLEYHSIRIPLTKENLIINSLIKFIDNSTTNNNNNNNNKVNEDDIKNARLVLLCLTIRKPISNFNQFINDSIKQFPNELEFIFYRAMNFRLNNDPKSAQLHFNSIIESCNSGDGELDYPLKYLYYKGVNRFYCGSISESDCNGIIQIFKSYIDKSIKEEFTYKVPELSYFISLIYIMNNDLEQSKEWFKKAINFEKSQLPCFIDQDYEIKKMVDSKLNPIKNK
Protein: Dynein light chain 2, cytoplasmic (Dynein light chain LC8-type 2) (Q78P75)
Organism: Rattus norvegicus (Rat)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12097491}.
Interaction partners:
- Dynein light chain Tctex-type 3
- Cytoplasmic dynein 1 intermediate chain 1
- Cytoplasmic dynein 2 light intermediate chain 1
- Cytoplasmic dynein 1 heavy chain 1
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 1 light intermediate chain 2
- Cytoplasmic dynein 1 light intermediate chain 1
- Dynein light chain roadblock-type 1
- Dynein light chain roadblock
- Dynein light chain Tctex-type 1
Sequence:
MSDRKAVIKNADMSEDMQQDAVDCATQAMEKYNIEKDIAAYIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
Protein: Glutamine-rich 1 (HCG2002013, isoform CRA_c) (cDNA FLJ77780) (A1L3Z9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MNNSLENTISFEEYIRVKARSVPQHRMKEFLDSLASKGPEALQEFQQTATTTMVYQQGGNCIYTDSTEVAGSLLELACPVTTSVQPQTQQEQQIQVQQPQQVQVQVQVQQSPQQVSAQLSPQLTVHQPTEQPIQVQVQIQGQAPQSAAPSIQTPSLQSPSPSQLQAAQIQVQHVQAAQQIQAAEIPEEHIPHQQIQAQLVAGQSLAGGQQIQIQTVGALSPPPSQQGSPREGERRVGTASVLQPVKKRKVDMPITVSYAISGQPVATVLAIPQGQQQSYVSLRPDLLTVDSAHLYSATGTITSPTGETWTIPVYSAQPRGDPQQQSITHIAIPQEAYNAVHVSGSPTALAAVKLEDDKEKMVGTTSVVKNSHEEVVQTLANSLFPAQFMNGNIHIPVAVQAVAGTYQNTAQTVHIWDPQQQPQQQTPQEQTPPPQQQQQQLQVTCSAQTVQVAEVEPQSQPQPSPELLLPNSLKPEEGLEVWKNWAQTKNAELEKDAQNRLAPIGRRQLLRFQEDLISSAVAELNYGLCLMTREARNGEGEPYDPDVLYYIFLCIQKYLFENGRVDDIFSDLYYVRFTEWLHEVLKDVQPRVTPLGYVLPSHVTEEMLWECKQLGAHSPSTLLTTLMFFNTKYFLLKTVDQHMKLAFSKVLRQTKKNPSNPKDKSTSIRYLKALGIHQTGQKVTDDMYAEQTENPENPLRCPIKLYDFYLFKCPQSVKGRNDTFYLTPEPVVAPNSPIWYSVQPISREQMGQMLTRILVIREIQEAIAVANASTMH
Protein: Proteasome subunit alpha type-1 (30 kDa prosomal protein) (PROS-30) (Macropain subunit C2) (Multicatalytic endopeptidase complex subunit C2) (Proteasome component C2) (Proteasome nu chain) (Proteasome subunit alpha-6) (alpha-6) (P25786)
Organism: Homo sapiens (Human)
Function: 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).
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-2
- 26S proteasome non-ATPase regulatory subunit 1
- 26S proteasome regulatory subunit 4
- Proteasome subunit beta type-8
- Proteasome subunit beta type-9
- 26S proteasome non-ATPase regulatory subunit 14
- Proteasome subunit alpha type-3
- Proteasome maturation protein
- 26S proteasome regulatory subunit 10B
- Proteasome subunit beta type-3
Sequence:
MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHIFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMECNLNELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLEGLEERPQRKAQPAQPADEPAEKADEPMEH
Protein: Tumor necrosis factor receptor superfamily member 1A (Tumor necrosis factor receptor 1) (TNF-R1) (Tumor necrosis factor receptor type I) (TNF-RI) (TNFR-I) (p55) (p60) (CD antigen CD120a) (P25118)
Organism: Mus musculus (Mouse)
Function: Receptor for TNFSF2/TNF-alpha and homotrimeric TNFSF1/lymphotoxin-alpha. The adapter molecule FADD recruits caspase-8 to the activated receptor. The resulting death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation which initiates the subsequent cascade of caspases (aspartate-specific cysteine proteases) mediating apoptosis (By similarity).
Subcellular location: Cell membrane; Single-pass type I membrane protein. Golgi apparatus membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- FAS-associated death domain protein
- TNF receptor-associated factor 2
- Lymphotoxin-alpha
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- Receptor-interacting serine/threonine-protein kinase 1
- Tumor necrosis factor
- Baculoviral IAP repeat-containing protein 2
- Baculoviral IAP repeat-containing protein 3
- Tumor necrosis factor ligand superfamily member 6
Sequence:
MGLPTVPGLLLSLVLLALLMGIHPSGVTGLVPSLGDREKRDSLCPQGKYVHSKNNSICCTKCHKGTYLVSDCPSPGRDTVCRECEKGTFTASQNYLRQCLSCKTCRKEMSQVEISPCQADKDTVCGCKENQFQRYLSETHFQCVDCSPCFNGTVTIPCKETQNTVCNCHAGFFLRESECVPCSHCKKNEECMKLCLPPPLANVTNPQDSGTAVLLPLVILLGLCLLSFIFISLMCRYPRWRPEVYSIICRDPVPVKEEKAGKPLTPAPSPAFSPTSGFNPTLGFSTPGFSSPVSSTPISPIFGPSNWHFMPPVSEVVPTQGADPLLYESLCSVPAPTSVQKWEDSAHPQRPDNADLAILYAVVDGVPPARWKEFMRFMGLSEHEIERLEMQNGRCLREAQYSMLEAWRRRTPRHEDTLEVVGLVLSKMNLAGCLENILEALRNPAPSSTTRLPR
Protein: Apoptosis-inducing factor 3 (EC 1.-.-.-) (Apoptosis-inducing factor-like protein) (Q96NN9)
Organism: Homo sapiens (Human)
Function: Induces apoptosis through a caspase dependent pathway. Reduces mitochondrial membrane potential.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:15764604}. Note=Does not translocate to the nucleus upon induction of apoptosis.
Interaction partners:
- Leucine-zipper-like transcriptional regulator 1
Sequence:
MGGCFSKPKPVELKIEVVLPEKERGKEELSASGKGSPRAYQGNGTARHFHTEERLSTPHPYPSPQDCVEAAVCHVKDLENGQMREVELGWGKVLLVKDNGEFHALGHKCPHYGAPLVKGVLSRGRVRCPWHGACFNISTGDLEDFPGLDSLHKFQVKIEKEKVYVRASKQALQLQRRTKVMAKCISPSAGYSSSTNVLIVGAGAAGLVCAETLRQEGFSDRIVLCTLDRHLPYDRPKLSKSLDTQPEQLALRPKEFFRAYGIEVLTEAQVVTVDVRTKKVVFKDGFKLEYSKLLLAPGSSPKTLSCKGKEVENVFTIRTPEDANRVVRLARGRNVVVVGAGFLGMEVAAYLTEKAHSVSVVELEETPFRRFLGERVGRALMKMFENNRVKFYMQTEVSELRGQEGKLKEVVLKSSKVVRADVCVVGIGAVPATGFLRQSGIGLDSRGFIPVNKMMQTNVPGVFAAGDAVTFPLAWRNNRKVNIPHWQMAHAQGRVAAQNMLAQEAEMSTVPYLWTAMFGKSLRYAGYGEGFDDVIIQGDLEELKFVAFYTKGDEVIAVASMNYDPIVSKVAEVLASGRAIRKREVELFVLHSKTGDMSWLTGKGS
Protein: Putative short-chain type dehydrogenase/reductase Rv0148 (EC 1.1.1.-) (P96825)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- 3-hydroxyacyl-thioester dehydratase Y
- Enoyl-CoA hydratase ChsH3
- Possible quinone oxidoreductase
- 3-oxoacyl-[acyl-carrier-protein] reductase
- Aldehyde dehydrogenase
- Probable fatty acid synthase Fas
- Putative S-adenosyl-L-methionine-dependent methyltransferase Rv0146
Sequence:
MPGVQDRVIVVTGAGGGLGREYALTLAGEGASVVVNDLGGARDGTGAGSAMADEVVAEIRDKGGRAVANYDSVATEDGAANIIKTALDEFGAVHGVVSNAGILRDGTFHKMSFENWDAVLKVHLYGGYHVLRAAWPHFREQSYGRVVVATSTSGLFGNFGQTNYGAAKLGLVGLINTLALEGAKYNIHANALAPIAATRMTQDILPPEVLEKLTPEFVAPVVAYLCTEECADNASVYVVGGGKVQRVALFGNDGANFDKPPSVQDVAARWAEITDLSGAKIAGFKL
Protein: Peroxidase 9 (Atperox P9) (EC 1.11.1.7) (ATP18a) (Q96512)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Removal of H(2)O(2), oxidation of toxic reductants, biosynthesis and degradation of lignin, suberization, auxin catabolism, response to environmental stresses such as wounding, pathogen attack and oxidative stress. These functions might be dependent on each isozyme/isoform in each plant tissue.
Subcellular location: Secreted {ECO:0000255|PROSITE-ProRule:PRU00297}.
Interaction partners:
- At4g36190
- Cytochrome P450, family 705, subfamily A, polypeptide 13
- Transcription factor MYB36
- B3 domain-containing protein At4g34400
Sequence:
MAISKLIPTLVLFVLFSFDVSVAHPGLGFGWGSNSPIGGSFYSNLYPQFYQFSCPQADEIVMTVLEKAIAKEPRMAASLLRLHFHDCFVQGCDASILLDDSATIRSEKNAGPNKNSVRGFQVIDEIKAKLEQACPQTVSCADILALAARGSTILSGGPSWELPLGRRDSRTASLNGANTNIPAPNSTIQNLLTMFQRKGLNEEDLVSLSGGHTIGVARCTTFKQRLYNQNGNNQPDETLERSYYYGLRSICPPTGGDNNISPLDLASPARFDNTYFKLLLWGKGLLTSDEVLLTGNVGKTGALVKAYAEDERLFFQQFAKSMVNMGNIQPLTGFNGEIRKSCHVIN
Protein: procollagen-proline 4-dioxygenase (EC 1.14.11.2) (Q8IQS7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum lumen {ECO:0000256|ARBA:ARBA00004319}.
Interaction partners:
Sequence:
MRKYHSLLPVLLGFAVLNSFVGCVEDIEEKERYSSSTVGLLKLLKVEEKFTDNLLNQVDQLGEKFEALRMYLSSVGYELHRSLNEKVQYVSNPINAFSLLRRTHEDLPKWHEYFKEAIGEGNQSILVDLVKMVPNDVDMLSAMHGIQRIEKIYDLKIDDLAQGVLQGVQYNVQLTYRDLIAMGNSMYQQSDYQTAAKWYRIACKRELENPEQLFIQILGDPSEHLHRQYIKSLFKYGSTTSEPSKSIEEAFIMVQASQEELDNIMSDLNEPQNDVEVEKDLYQVKRSPSNCELGCRGLYRQKTNLVCRYKSTANTFLRLAPLKLEEISLDPFMAMYHEVLYDSEIRELKGQSMNMVNGYASQRNGTEIRDTVVRYDWWSNTSLVRERINQRIIDMTGFNFLKDEKLQIANYGLGTYFQPHFDYSSDGFETPNITTLGDRLASILFYASEVPQGGATVFPEINVTVFPQKGSMLYWFNLHDDGKPDIRSLHSVCPVLNGDRWTLTKWVPMFPQMFSFPCKS