wanglab/gogpt-training-data huggingface dataset:
Protein: Peroxisome biogenesis protein (Q5ACV4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
- Peroxin/Ferlin domain-containing protein
Sequence:
MSKVEASSGTNKNPVSTATSTVGESATATTETSTELRANFAEVTDPKLNAKPQSSPLLSSTPPSVSKALVNSYPYLIIINKLLSITTWTNDDYWVNVVIISLYALVVLYFENLVIWSGHLILVAILISYALLNNKIIKEANLHPTLDDVVQALTSTCVKADILLSPITSLSLTAYDIKRLIFTTLFLTPVYLVVTFLLIKPRTILLLTGVYLLTYHSSYSIVTRRILWKLKIVRLIFFYLTGLDLSETKNHSLFAAAFAKVSSSGTSSKSNKPVRFTYVIYENQRKWLGIGWTSNLLSYERTPWTDEFLNESSSIDSFKLPNAADDATNGDSNMQGATWRWVDKTWRLDLTNDGAITLSSSKRSKTTANPTNDEGFIYYDNTWKKPSTEDTFSKYTRRRRWIRTAELIFDNKQEEALESSENVKATGVSVQDATTTKKVKSLRFAEDESNVEESADTDKKND
Protein: BTB domain containing 2 (E9PY28)
Organism: Mus musculus (Mouse)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MAAGGSGRASCPPGVGAGAGSLGPSANAAAAPSNAAACAPVPPPPPSPPPGPGTDAQAVGDERDDAGPGALLREPVYNWQATKPTVQERFAFLFNNEVLCDVHFLVGKGLSSQRVPAHRFVLAVGSAVFDAMFNGGMATTSTEIELPDVEPAAFLALLKFLYSDEVQIGPETVMTTLYTAKKYAVPALEAHCVEFLKKHLRADNAFMLLTQARLFDEPQLASLCLESIDKNTADAIAAEGFTDIDLDTLVAVLERDTLGIREVRLFNAVVRWSEAECQRQQLQVTPENKRKVLGKALSLIRFPLMTIEEFAAGPAQSGILVDREVVSLFLHFTVNPKPRVEFIDRPRCCLRGKECSINRFQQVESRWGYSGTSDRIRFSVNKRIFVVGFGLYGSIHGPTDYQVNIQIIHTDSNTVLGQNDTGFSCDGSASTFRVMFKEPVEVLPNVNYTACATLKGPDSHYGTKGLRKVTHESPTTGAKTCFTFCYAAGNNNGTSVEDGQIPEVIFYT
Protein: Metaxin-like protein C409.19c (Q9UUA5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in transport of proteins into the mitochondrion.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. Mitochondrion outer membrane {ECO:0000250}.
Interaction partners:
- SAM50-like protein SPAC17C9.06
- Mitochondrial distribution and morphology protein 10
- Probable mitochondrial import receptor subunit tom40
- Metaxin-1
- Mitochondrial import receptor subunit tom22
- Mitochondrial import receptor subunit tom7
- Mitochondrial import receptor subunit tom20
- Mitochondrial distribution and morphology protein 12
- Probable mitochondrial import receptor subunit tom70
- Mitochondrial import protein 1
Sequence:
MLQLFIYSPGLGQPTMDPGCLAALIYCALAVPKDEIEILRTANSGMSPTHKLPALWDGHVWIGSLKNILIYLKQKGYNLDNFDAKQLANVMAFTSLLEGSVNDLWLLEAFVNEENFVEAIRPAWSKALKFPHNYLTPNALQRQAKERLAQTLGIRDEEVSYEASRMPISHKWTNATRHRQALLRTQARRIRISSLARQVYGSLESLISDSKFIFGEKPTSLDCLFYAYLSFHAFTNELPQATLRPCLQFNSPKLYAYLKSLRETWFSDDSNILSPLSIKVQPENLLTIARLAWNNVTAKANDTRKSITKFSVPPERKLLWARNGFFIFASAFSFVWFVISNGIVVIETEDDEASFEEVDDAKESIQEKEIDETTESKATHDSSETSSSKELPKEEEKESSSFDLQPLSAQDLLFSGFAEDEIMDEEFGYDDDDDEEFDLDDLDDLEEEIV
Protein: leucine--tRNA ligase (EC 6.1.1.4) (Leucyl-tRNA synthetase) (A0A1D8PQ56)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- serine--tRNA ligase
- Methionine--tRNA ligase, mitochondrial
- leucine--tRNA ligase
- arginine--tRNA ligase
- glutamine--tRNA ligase
- isoleucine--tRNA ligase
- threonine--tRNA ligase
- methionine--tRNA ligase
- Serine--tRNA ligase, cytoplasmic
- Isoleucine--tRNA ligase, cytoplasmic
Sequence:
MFPYPSGVLHIGHLRVYTISDVVARYKRSKGFNVIHPMGWDAFGLPAENAAVERNINPSEWTETNIAKMKNQMETFLADFDWQREVNTSSPEYYKWTQKIFLMLFERGLAYRKAAEINWDPVDNTVLANEQVDAEGRSWRSGAIVEKRNLEQWFIGITKYAKELNRDLKNLPDWPEKVKTMQKNWIGESNGVEINIPVNFPGLEHVTVFTSRPDTLFSMQFVALALNHPIVEAAAREDQELAAFIESAKSIDDPTSKAGYMLKNIKASIPIDVDNNIKKSFDIPVFTAPYVLGNYGHGAVMGCPGHDERDFDFWKLNGPRGVPAIQIITPKKQNAKDDYPYTLKKGTLEDSSVLTHGLNDIGEYKGKTIEKATQMITDCLKSHSLGDYTTQFKIRDWLISRQRYWGAPIPIVHCHDCGPVAVPDKDLPVMLPGVKGKNFGKGNPLGNIEEFVNCKCPSCGKDARRETDTMDTFMDSSWYFFRYLDSKNENLPIGPEASKQMPVDLYVGGVEHAILHLLYSRFIAKFLSDCGLWDGEPHHKEPFKKLVTQGMVHGKTFSDPITGKFLIPDELDFTDPANPLIKTTGKTPVVTFEKMSKSKHNGADPGEFIERYGADVIRAHLLFSAPVSDTLNWQEEQISGTDRWLRRVIQLGDSITEIPKDQFKTEASGSSQTFQNVTLNKVHYDSIEFNSQELELYNTIQGYVQSIASSIEVKFSLNTIVSDLMKMTNTISEAIKTTNTYNQDLIFDSYQKLLICMSPVTPATAEECWERFALNQGKPAPKSIFYEKFPTDVPIESNLTMYNIFINGKHRGTMEAPKSFAKESETEIVKQISGAEKFNDLITGPVKKVIAKPSMISIVFK
Protein: Tripartite motif-containing protein 5 (EC 2.3.2.27) (RING-type E3 ubiquitin transferase TRIM5) (TRIM5alpha) (Q5C8U4)
Organism: Chlorocebus pygerythrus (Vervet monkey) (Cercopithecus pygerythrus)
Function: Capsid-specific restriction factor that prevents infection from non-host-adapted retroviruses. Blocks viral replication early in the life cycle, after viral entry but before reverse transcription. In addition to acting as a capsid-specific restriction factor, also acts as a pattern recognition receptor that activates innate immune signaling in response to the retroviral capsid lattice. Binding to the viral capsid triggers its E3 ubiquitin ligase activity, and in concert with the heterodimeric ubiquitin conjugating enzyme complex UBE2V1-UBE2N (also known as UBC13-UEV1A complex) generates 'Lys-63'-linked polyubiquitin chains, which in turn are catalysts in the autophosphorylation of the MAP3K7/TAK1 complex (includes TAK1, TAB2, and TAB3). Activation of the MAP3K7/TAK1 complex by autophosphorylation results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes, thereby leading to an innate immune response in the infected cell. Restricts infection by human immunodeficiency virus type 1 (HIV-1) and N-tropic murine leukemia virus (N-MLV). Plays a role in regulating autophagy through activation of autophagy regulator BECN1 by causing its dissociation from its inhibitors BCL2 and TAB2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q0PF16}. Nucleus {ECO:0000250|UniProtKB:Q0PF16}. Note=Predominantly localizes in cytoplasmic bodies. Localization may be influenced by the coexpression of other TRIM proteins, hence partial nuclear localization is observed in the presence of TRIM22 or TRIM27. In cytoplasmic bodies, colocalizes with proteasomal subunits and SQSTM1. {ECO:0000250|UniProtKB:Q0PF16}.
Interaction partners:
Sequence:
MASGILVNVKEEVTCPICLELLTEPLSLPCGHSLCQACITANHKESMLYKEEERSCPVCRISYQPENIQPNRHVANIVEKLREVKLSPEEGQKVDHCARHGEKLLLFCQEDSKVICWLCERSQEHRGHHTFLMEEVAQEYHVKLQTALEMLRQKQQEAEKLEADIREEKASWKIQIDYDKTNVSADFEQLREILDWEESNELQNLEKEEEDILKSLTKSETEMVQQTQYMRELISDLEHRLQGSMMELLQGVDGIIKRVENMTLKKPKTFHKNQRRVFRAPDLKGMLDMFRELTDVRRYWVDVTLAPNNISHAVIAEDKRQVSYRNPQIMYQSPGSLFGSLTNFSYCTGVPGSQSITSGKLTNFNYCTGVLGSQSITSGKHYWEVDVSKKSAWILGVCAGFQPDATYNIEQNENYQPKYGYWVIGLQEGDKYSVFQDGSSHTPFAPFIVPLSVIICPDRVGVFVDYEACTVSFFNITNHGFLIYKFSQCSFSKPVFPYLNPRKCTVPMTLCSPSS
Protein: Protein cramped (O76906)
Organism: Drosophila melanogaster (Fruit fly)
Function: Polycomb group (Pc-G) genes are needed to maintain expression patterns of the homeotic selector genes of the Antennapedia (Antp-C) and Bithorax (Bx-C) complexes, and hence for the maintenance of segmental determination. Can act as a modifier of position effect variegation (PEV).
Subcellular location: Nucleus {ECO:0000269|PubMed:9310333}. Note=During S-phase in early embryogenesis. Colocalizes with PCNA in polytene nuclei during embryogenesis.
Interaction partners:
- Acyl-CoA-binding protein homolog
Sequence:
MEELSKQPPPPPLTQPPPPSSSVSIEEPLPNGKGGGAVVVNSIAKLPEEELLGSVTMHNCPGTRASARVIQKMKQDQTRPMTPPPSEREPNKKEEKAAQKTPSQLKTGSGKTTWTNVERNCFFDALNEFGKDFEAVANCINAKLKRRNANSDYSFKTKDQVRQHYYQTHHKICKYVRFSEELKKPAQELYTLINYGEMRRKLQFLTEKHFMKLKQLVYQGQITVRCKGKNIRIKTPSCKALRRLNQLDDSLEDIRLPSKVEVLVTPANMEAFGRVQSLAQNPRGRIIVPLHKKLISFIKTFEYKWRSANQRLHEEKSAYFSSSLPSAASNNNNNNNETEPLQPSVASLDPSMCFQPRPGVAIHRPLLSITAYLSSISICLTAYEERMGFKVRSETLGNLAGMSVAANKRLRTESGSEKRSPETKKPKSSASPPLEKSLDDGPLEGNLMKMENSSGDELGEEIHEFLGDILEAMQHPQAATIPALSATTGDTTNVAVALETSHDPVQQAYPANADLSNAMATSVLQTSCAAAPAPSTPVTGSLAAPSVARSKRKEAKEAAAAAQARNFKPLLSDDILKRIRKGWTQANAADITIGDLYVVFGQDSKLELEYYWCEVDSSTAMASSILTINTVTPSSSSVGTQTGSAASNANQTGASSNCYVSASSNSSTSSTSLPYNPNDCDSVERVRAVTTSSVSNKLKHLLLVANLSERVRKRQCNCGHTCDRKRDLMTKAQQLAEATATGGVGGMVEGNFRTPMLPVRRPISNIDPVRQLSALTRQKISRQVLVQRRLLPPTSAGDRPYDLLSVRQLHSGLFEPIDRVDGTSSAGISTSGSKPDCSMNAMTASQDQEPGDQGALEFLNDEATQVSARDMPNLDICVATNRTDVSSSLNEAAQDGSTTQSFFQGSMSPMHLLRDSTSNARWLEDNINDFSLTSLLGHLDEIDATRDILDPSSSMSVISESSVDFRHKFQEIAALLQQQEKD
Protein: Catenin alpha (P35220)
Organism: Drosophila melanogaster (Fruit fly)
Function: Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}. Cell junction, adherens junction {ECO:0000269|PubMed:25653389}. Cell membrane {ECO:0000269|PubMed:25653389}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell junction. Note=Found only at cell-cell boundaries.
Interaction partners:
- Armadillo segment polarity protein
- DE-cadherin
- Adherens junction protein p120
- Vinculin
- Rhea, isoform B
- FI11703p
- Ankyrin, isoform B
- Eukaryotic translation initiation factor 4G1, isoform B
- LIM domain-containing protein jub
- Atf6, isoform C
Sequence:
MLKPDKMGTLTDFGQIALKWDPKNLEIRTMSVEKTLEPLVLQVTTLVNTKGPSKKKKGKSKRASALVAAVEKATENFIQKGEQIAYENPDITQEMLTAVDEVKKTGDAMSIAAREFSEDPCSSLKRGNMVRAARNLLSAVTRLLILADMVDVHLLLKSLHIVEDDLNKLKNASSQDELMDNMRQFGRNAGELIKQAAKRQQELKDPQLRDDLAAARAMLKKHSTMLLTASKVYVRHPELDLAKVNRDFILKQVCDAVNTISDVAQGKSSQPTDIYSGAGELAAALDDFDEGIVMDPMTYSEKRSRQLLEERLESIISAAALMADADCTRDERRERIVAECNAVRQALQDLLSEYMSNMSQKDNSPGLSRAIDQMCRKTRDLRRQLRKAVVDHVSDSFLETTTPLLDLIEAAKSGNEKKVREKSEIFTKHAEKLVEVANLVCSMSNNEDGVKMVRYAAAQIESLCPQVINAASILTVRPNSKVAQENMTTYRQAWEVQVRILTEAVDDITTIDDFLAVSENHILEDVNKCVMALQVGDARDLRATAGAIQGRSSRVCNVVEAEMDNYEPCIYTKRVLEAVKVLRDQVMMKFDQRVGAAVGALSNNSNKDVDENDFIDASRLVYDGVREIRRAVLMNRSSEDLDTDTEFEPVEDLTLETRSRSSAHTGDQTVDEYPDISGICTAREAMRKMTEEDKQKIAQQVELFRREKLTFDSEVAKWDDTGNDIIFLAKHMCMIMMEMTDFTRGRGPLKTTMDVINAAKKISEAGTKLDKLTREIAEQCPESSTKKDLLAYLQRIALYCHQIQITSKVKADVQNISGELIVSGLDSATSLIQAAKNLMNAVVLTVKYSYVASTKYTRQGTVSSPIVVWKMKAPEKKPLVRPEKPEEVRAKVRKGSQKKVQNPIHALSEFQSPADAV
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-5 (Q80SZ7)
Organism: Mus musculus (Mouse)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Pituitary adenylate cyclase-activating polypeptide type I receptor
- Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
- 5-hydroxytryptamine receptor 7
- C-X-C chemokine receptor type 4
- Melatonin receptor type 1B
- C-C chemokine receptor type 5
Sequence:
MSGSSSVAAMKKVVQQLRLEAGLNRVKVSQAAADLKQFCLQNAQHDPLLTGVSSSTNPFRPQKVCSFL
Protein: 26S proteasome regulatory subunit 4 homolog (Tat-binding protein alpha) (DdTBPalpha) (Q55BV5)
Organism: Dictyostelium discoideum (Social amoeba)
Function: The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex (By similarity). Plays an important role in regulating both growth and multicellular development.
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 6A homolog
- 26S proteasome non-ATPase regulatory subunit 13
- 26S proteasome non-ATPase regulatory subunit 7
- 26S proteasome non-ATPase regulatory subunit 11
- 26S proteasome regulatory subunit 7
- 26S proteasome regulatory subunit 6B homolog
- 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 3
Sequence:
MGNNQSQGQGDKGEKKDQPKYQPPPPPTQFGKKKKRRGAETSTKLPVITPHSKCKLKQLKLERIKDYLLMEQEFLQNYDLNQPKVDENSKEQADEKIIEELRGDPLTVGNLEEIIDDNHAIVSSTVGPEHYVRIMSFVDKSKLYLGATVLLNNKTLSVVGVIDGEVDPMVNVMKVEKAPTESYSDIGGLEAQVQEMKEAIELPLTHPELYEEIGIKPPKGVILYGEPGTGKTLLAKAVANQTSATFLRVVGSELIQKYLGDGPKLVRELFRVADECAPSIVFIDEIDAVGTKRYDSQSGGEREIQRTMLELLNQLDGFDARTDVKVIMATNRIETLDPALIRPGRIDRKIEFPLPDIKTKRKIFEIHTAKMNLSEDVNLEEFVMSKDDLSGADIKAICTESGLLALRERRMRVTHTDFKKAKEKVLYRKTAGAPEGLYM
Protein: Bis(5'-adenosyl)-triphosphatase (EC 3.6.1.29) (AP3A hydrolase) (AP3Aase) (Adenosine 5'-monophosphoramidase FHIT) (EC 3.9.1.-) (Adenylylsulfatase) (EC 3.6.2.1) (Adenylylsulfate-ammonia adenylyltransferase) (EC 2.7.7.51) (Diadenosine 5',5'''-P1,P3-triphosphate hydrolase) (Dinucleosidetriphosphatase) (Fragile histidine triad protein) (P49789)
Organism: Homo sapiens (Human)
Function: Possesses dinucleoside triphosphate hydrolase activity. Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Exhibits adenylylsulfatase activity, hydrolyzing adenosine 5'-phosphosulfate to yield AMP and sulfate. Exhibits adenosine 5'-monophosphoramidase activity, hydrolyzing purine nucleotide phosphoramidates with a single phosphate group such as adenosine 5'monophosphoramidate (AMP-NH2) to yield AMP and NH2. Exhibits adenylylsulfate-ammonia adenylyltransferase, catalyzing the ammonolysis of adenosine 5'-phosphosulfate resulting in the formation of adenosine 5'-phosphoramidate. Also catalyzes the ammonolysis of adenosine 5-phosphorofluoridate and diadenosine triphosphate. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15007172, ECO:0000269|PubMed:15313915}. Mitochondrion {ECO:0000269|PubMed:19622739}. Nucleus {ECO:0000269|PubMed:15313915}.
Interaction partners:
- WW domain-containing oxidoreductase
- Bis
- Deaminated glutathione amidase
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Bis
- Catenin beta-1
- Adenosine 5'-monophosphoramidase HINT1
- Ras association domain-containing protein 1
- Receptor-type tyrosine-protein phosphatase gamma
- Omega-amidase NIT2
Sequence:
MSFRFGQHLIKPSVVFLKTELSFALVNRKPVVPGHVLVCPLRPVERFHDLRPDEVADLFQTTQRVGTVVEKHFHGTSLTFSMQDGPEAGQTVKHVHVHVLPRKAGDFHRNDSIYEELQKHDKEDFPASWRSEEEMAAEAAALRVYFQ
Protein: small monomeric GTPase (EC 3.6.5.2) (Q7ZX67)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004523}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004523}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004523}.
Interaction partners:
- E3 ubiquitin-protein ligase AMFR
- Intersectin-2 isoform X1
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Intersectin-1
- Uncharacterized protein.
Sequence:
MREYKVVVLGSGGVGKSALTVQFVTGTFIEKYDPTIEDFYRKEIEVDSSPSVLEILDTAGTEQFASMRDLYIKNGQGFILVYSLVNQQSFQDIKPMRDQIIRVKRYEKVPVILVGNKVDLESEREVSSNEGRALAEDWGCPFMETSAKSKTMVDELFAEIVRQMNYAAQPDKDDPCCSACNIQ
Protein: Protein zyg-11 homolog B (Q9C0D3)
Organism: Homo sapiens (Human)
Function: Serves as substrate adapter subunit in the E3 ubiquitin ligase complex ZYG11B-CUL2-Elongin BC. Acts redudantly with ZER1 to target substrates bearing N-terminal glycine degrons for proteasomal degradation. Involved in the clearance of proteolytic fragments generated by caspase cleavage during apoptosis since N-terminal glycine degrons are strongly enriched at caspase cleavage sites. Also important in the quality control of protein N-myristoylation in which N-terminal glycine degrons are conditionally exposed after a failure of N-myristoylation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36933219}.
Interaction partners:
- Cullin-2
- Elongin-B
- E3 ubiquitin-protein ligase RBX1
- Protein zer-1 homolog
- Elongin-C
- Kelch domain-containing protein 2
- Protein fem-1 homolog B
- Kelch domain-containing protein 3
- Kelch domain-containing protein 10
- Protein fem-1 homolog C
Sequence:
MPEDQAGAAMEEASPYSLLDICLNFLTTHLEKFCSARQDGTLCLQEPGVFPQEVADRLLRTMAFHGLLNDGTVGIFRGNQMRLKRACIRKAKISAVAFRKAFCHHKLVELDATGVNADITITDIISGLGSNKWIQQNLQCLVLNSLTLSLEDPYERCFSRLSGLRALSITNVLFYNEDLAEVASLPRLESLDISNTSITDITALLACKDRLKSLTMHHLKCLKMTTTQILDVVRELKHLNHLDISDDKQFTSDIALRLLEQKDILPNLVSLDVSGRKHVTDKAVEAFIQQRPSMQFVGLLATDAGYSEFLTGEGHLKVSGEANETQIAEALKRYSERAFFVREALFHLFSLTHVMEKTKPEILKLVVTGMRNHPMNLPVQLAASACVFNLTKQDLAAGMPVRLLADVTHLLLKAMEHFPNHQQLQKNCLLSLCSDRILQDVPFNRFEAAKLVMQWLCNHEDQNMQRMAVAIISILAAKLSTEQTAQLGTELFIVRQLLQIVKQKTNQNSVDTTLKFTLSALWNLTDESPTTCRHFIENQGLELFMRVLESFPTESSIQQKVLGLLNNIAEVQELHSELMWKDFIDHISSLLHSVEVEVSYFAAGIIAHLISRGEQAWTLSRSQRNSLLDDLHSAILKWPTPECEMVAYRSFNPFFPLLGCFTTPGVQLWAVWAMQHVCSKNPSRYCSMLIEEGGLQHLYNIKDHEHTDPHVQQIAVAILDSLEKHIVRHGRPPPCKKQPQARLN
Protein: 6-phosphogluconolactonase (C8VLZ3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
Sequence:
MISFLRTLTFGLTLSSALAKSTSSTLYATHYSTSSIYTLTLKQSNNTYSLAEASSLKTCGRYPSWITLDASTKTLYCSDEYGWRNAGGTVNGSLTTVNVGEDGSLSEEAVTGTAPGSGVHNIVYEGDGGEKYLAIAHYSGAAVSTYALPLENDADPLQVFEFELDTPGEVPDRQEAPHPHQTFLDPTGSFVLVPDLGADLIRVFAIDKSNGELNACPSLNYTLGGGPRHGVFRTASDSELRIRGRAPGPETVLYVTGELNGEVEAFAVSYPKSGCLSFEQIDTEIPYPSDLPDGASLSEIRLVEDDLYVSVRLDSAFGGDDSLARLSLRQDGKVEFEEISTSGGVLPRTFAINKAGDLVAVGNQLSSTVTIVERDPETGALGEVVAELLVGEPGEPNNLEGLSSIIWNE
Protein: NACHT, LRR and PYD domains-containing protein 1a allele 5 (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1a, C-terminus (Nlrp1a-CT); NACHT, LRR and PYD domains-containing protein 1a, N-terminus (Nlrp1a-NT)] (D9I2G4)
Organism: Rattus norvegicus (Rat)
Function: Acts as the sensor component of the Nlrp1a inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis (By similarity). Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation (By similarity). Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, such as Val-boroPro inhibitor, and mediates the formation of the inflammasome polymeric complex. In response to pathogen-associated signals, the N-terminal part of Nlrp1a is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1a, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome directly recruits pro-caspase-1 (proCASP1) independently of PYCARD/ASC and promotes caspase-1 (CASP1) activation, which subsequently cleaves and activates inflammatory cytokines IL1B and IL18 and gasdermin-D (GSDMD), leading to pyroptosis (By similarity). In the absence of GSDMD expression, the Nlrp1a inflammasome is able to recruit and activate CASP8, leading to activation of gasdermin-E (GSDME) (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9C000}. Cytoplasm {ECO:0000250|UniProtKB:Q9C000}. Nucleus {ECO:0000250|UniProtKB:Q9C000}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1a, C-terminus]: Inflammasome {ECO:0000250|UniProtKB:Q9C000}.
Interaction partners:
Sequence:
MGESQSKQESNTRVAQHGSQQDVDPTFQTKRALERERSSPQVEQSFLGQLQSLLGWSSTSKDVPLSQLIREMDHESRRHSHQSKKKLDRSEHISEGTIPEIYEKRKETISHTQSMEQKYLFQNFTKLLLLQKCCPGGSEKLVRESWHPCVPEEGGHMIEIQDLFDPNLDTEKKPQLVIIEGAAGIGKSTLARQVKRAWEEGQLYRDRFQHVFFFSCRELAQCKQLSLAELIAQGQEVLTAPTRQILSRPEKLLFILDGIDEPAWVLEDQNPELCVHWSQAQPVHTLLGSLLGKSILPEASLMLTARTTALQKLIPSLGQPHRVEVLGFSEFERKDYFYKYFAKERNTIIDFNLIGSIPVLLTLCEVPWVCWLLCTCLEKQMQQGEVLSLTSQTTTALCLKYLSLTIPGQHLSTQLRTLCSLAAEGICQRRTLFSKSDLCKQGLAEDAIATFLKIGVLQRQPSSLSYSFAHLCLQEFFAAMSYILEDSEEARGDMGNDRTVETLVERYGRQNLFEAPTVRFLLGLLNTREMREMENIFACKFPWKTKLKLLRSIVGEPFCQPCHLGLFHCLYENQEEELLTETMLCFPLTASGPNHMEATVFQTNVKRLVIQTDMELMVVTFCITFSHVRSLRLKGKGQQEYKLTAPAMVLYRWTPISEASWKVLFSNLKCTRNLEELDLSGNPLSYSAVRSLCTALRQPGCRLKTLWLVDCGLTSRCCSFLASMLSAHSRLAELDLRLNDLGDNGVRQLCEGLRNPACNLSILRLDQASLSEQVITELRALETKNPKLFISSTWMSHMTMPTENTDGEESLTSSKQQQQQSGDKHMEPLGTDDDFWGPSGPVSTEVVDRERNLYRVRLPMAGSYHCPSTGLHFVVTRAVTIEIGFCAWSQFLHETPLQHSHMVAGPLFDIKAEHGAVTAVCLPHFVSLQEGKVDSSLFHVAHFQDHGMVLETPARVEPHFAVLENPSFSPMGVLLRMIPAVGHFIPITSITLIYYRLYLEDITFHLYLVPNDCTIRKAIDEEELKFQFVRINKPPPVDALYVGSRYIVSSSKEVEILPKELELCYRSPRESQLFSEIYVGNIGSGINLQLTDKKYMNLIWEALLKPGDLRPALPRMASAPKDAPALLHFVDQHREQLVARVTSVDPLLDKLHGLVLSEEDYETVRAEATNQDKMRKLFRGSRSWSWDCKDHFYQALKETHPHLIMDLLEKSGGVSVRL
Protein: Endogenous retrovirus group K3 member 1 (HCG2043597, isoform CRA_b) (LOC113386 protein) (Q96A10)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSQRNLNAKTEQGPTGVTMTSNPITWGQIKKTTQEAEKLLERQGQAKTPDSMFLAMLAVVSCASIGSGEPPTGN
Protein: Chitinase-like protein (Q0WNC2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Transcription factor EMB1444
- Putative defensin-like protein 40
- Protein DOWNY MILDEW RESISTANCE 6
Sequence:
MKSLCFISTAPLIRSPPFLDLSPTSLNRFTLKIPASLYVSHPTRCSISNPSSSEELLNSNGGMSRASISVFGGTSLNNLKMQVGSPISLHSINPLAKLSLSDQAFLLLAFIVCTTSVAFTSLVITAIPTLVAMGRAATSFAKLADTARKELPSTLAAVRLSGMEISDLTLELSDLSQDITDGINKSAKAVQAAEAGIKQIGTLAQQQTLSMIEERANLPEISLQPVVAGAAEKTSHAIGSATKRLMNIITGGNKDED