wanglab/gogpt-training-data huggingface dataset:
Protein: GH26833p (Lipophorin receptor 2, isoform F) (Q7YTZ6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
Interaction partners:
Sequence:
MGPICRILGCSFLLLIAGLVPHHASRVVGLESTCSQEQFRCGNGKCIPRRWVCDRENDCADGSDESTSQCRGLCSSLMFMCKNGEQCIHREFMCDGDQDCRDGSDELECGNRTCRSDEFTCGNGRCIQNRFKCDDDDDCGDGSDEKNCGEKAKCGSNFFACKSGPCIPNQWVCDGDSDCRNGEDEMQNCTVSLLNFCQAGEFQCSDRITCLHKSWVCDGEADCPDGEDESQSNCLKVSCRPDQFQCNDQSCIAGHLTCNGKRDCADGSDEIMCDISATPRTCNATTEFDCGGGLCIPNAKVCNRRKDCPNGEDEPAGKCGINECSSKNGGCMHQCVNLEVGYRCECHDGYKLGADQHTCVDIDECETPGICSQVCVNEIGAFKCECEAGYMRLLKNHTRCKASEGHASLLLARRHDIRKIALDRPEMTSIVNSTKAATALDFVFRTGMIFWSDVATQSIYKAPIDEGNDRTVVLTKSSVTSDGLAVDWIYNHVYFTDTHKCTIELTNFEGSMGKVLVKDSLDIPRSIALDPIEGWMYWSDWGASPRIERAGMDGTHRTAIITYDVKWPNGITLDLVQKRLYWVDGKLNTISSSNYDGSQRHQVLYSGEYLRHPFSITTFEDYVYWTDWDKQAVFKANKFNGMDVEPVTATHMLEHPMVVHVYHPYRQPDGVNHCQSVNGHCSHLCLPAPRINERSPRISCACPTGLKLMPDGLMCVEDLGIPTVRPTAPMHRTIEQSSNSTTKLPQDGYSETPVETKTGNNRTDTSNQVHKSDAESENDYVEIALHVIASLAGTALVASVIYVVYRRCTRAVNSMNFENPVYHKTTEDHFSLEKNGTPHIYAAANDEEAVNPLFKSGTECV
Protein: CCT-beta (O97247)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- T-complex protein 1 subunit gamma
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit epsilon
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit alpha
- T-complex protein 1 subunit eta
- T-complex protein 1 subunit delta
- Phosducin-like protein 1, putative
- Cell division cycle protein 20 homolog, putative
- Serine/threonine-protein phosphatase
Sequence:
MMNSVMPDVLKEGAQEDKGEIARLQYFVGAIAVGDLVKSTLGPRGLDKILTPLNIEGTRSHQHTVTNDGATILKSVWLDNPVSKILVDVSMQQDNKCGDGTTGVVVLAAEMLRNAEILVENKIHPQIICDGFRMALASAREALLDSCFCHDVDSELFKEDMLKIARTTLSSKLLTHEKEHFAELAVNAILRIKDNLNLDLIQIIKKTGGTIKDSYLEEGFILEKRIGINQPKSLSNCKIMVANTPMDTDKIKIYGTKVNVHSFEDVQDLENEERLKMKNKVENIISHGCNVFINRQLIYNYPEQIFRENNVMTIEHSDFDGMERLANCLDAEIASTFEKDLNIKLGYCDKIEEIIIGEDKLVRFSGCKKNGACTIILRGASTHILEESERSLHDALAVLAETMKDNRVVLGAGCVEMLMSNAVDNLARTVEGKKSLAIEAYAKALRQIPTYILDNGGFDSSEIVSKIRAQHTKGNKYAGIDIEKGDVGNIMELGIYESYNSKLSQITSATEAVEMILRVDDIIKCAPRKRSGM
Protein: Girdin homolog (Coiled-coil domain-containing protein grdn-1) (F3Y5P4)
Organism: Caenorhabditis elegans
Function: Scaffolding protein that plays a role in ciliogenesis, cilium positioning and dendrite anchoring in sensory amphid neurons including AWB, AWA, AWC, ADL and ASI, the phasmid neurons PHA and PHB and the gas sensing neurons AQR, PQR, URX and BAG. Its role in cilium positioning may be through regulation of the localization of cell adhesion proteins such as the apical junction protein ajm-1, and the ciliary scaffolding protein Rootletin/che-10. Plays a more prominent role in regulating dendrite morphogenesis in AQR than in PQR neurons. Regulates localization of hmr-1 to the distal AQR dendrite. During embryonic elongation, required for the anchoring of URX and BAG dendrites to the presumptive nose.
Subcellular location: [Isoform a]: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:27623382, ECO:0000269|PubMed:33460640}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:27623382, ECO:0000269|PubMed:33460640}. Note=Enriched at the proximal ends of centrioles (PubMed:27623382). Localizes to the cilium basal body in AQR and PQR sensory neurons (PubMed:33460640). Localizes to the cilium basal body in the outgrowing AQR dendrite (PubMed:33460640). Localizes to puncta near dendrite contacts in the nose (PubMed:31988188). {ECO:0000269|PubMed:27623382, ECO:0000269|PubMed:31988188, ECO:0000269|PubMed:33460640}.
Interaction partners:
- Serpentine receptor class r-10
- Neuroglian
- GAS
- Fas-binding factor 1 C-terminal domain-containing protein
- Rootletin
Sequence:
MKEKHENWSHPLAFWLCDCAAIIPNPATQNFAKNDFLDGLLMLNLMKFINPHFSENEKNGQSLYEELLNQISQFYEKNLDQVIVCKMPEISILESSGEIDEITFEELKKLLLLLLGCAIQSDHKKVFVDRITGFDQTIQAELAACIQKLTESDEIVQNLEDFERRKMKETDEVGGGGGSIEDVDSDDMESSTTSSSNGEIAIKQQDQSFLMSRSTSPTSELRHQTLQIANLQHEMRQMRTQAENRDEECQKLELDNEEKAQKIKILENERLKLVDFKKKWKSVNDDLQEANCKIEKLQNLVGIEKKYREARDGKELYKSKYDIVVKKNLEMEETITTLEKNLKTLQMEMKEKFGVEDNLQRMRNTIDDLEAEISKKNLEIEDFLDEKHRMDREIKELKEIVHQMEVPSTTTTPRIMDSLADQLENAKQDEFEMMKAEIRKLRAQTEGATPETTIIQCNQDLDTLRSQLSTEQHQTAQLHLEIQKMQVEKEQIDGNMERIGIELEEMSAQVENLNLERDEAVKQLLEARRKFGEFQMGQSRDLEEKWSKEVEKSNKISKKCEILEEKLQESDFLLAKSRDEAKKLQFELDEALEETSHVTRSLSSEKNTLKAKLLELQDQVEAQTLELLNQKNCGKRLEDRDQMISNLHNLKNELENDLKTCQTQLELESKKLQRLREDLVLEKSRRADLIGRIHSLCTTLSLNGANFEKINNDDELIDNIDDIMMNALVAVKRERDDLRIQGNQQIQELHDLKRDIEKLRRSESESLNESDDRVRELTRENMHTKEQVFMLQEKLRELNLELSTKNDEIDMVKASIEELNRNSTASCTSNAEIARLQVSIRNSQIQEDLVKQENTKLRDELQEMQKMSKKRSQNLDELENMHKTLLVDHSRLQQLHNLLTRDYDEAKKESMELRQKVQNIPRQQAVFMNANIRELEAKLSEEISRREQLEKEHKMCRIHCENLRRDITELVQTRDELSLELRRAHDTCHNKNNQIDELKKQLNQKISEVNKLSSKIEALSQLNRTYNEENRNLSRQLEILLTQNKELLQRALHDKDQYHLEMKDFQDQLSALRRHKEKLEDKIMDQYRTMENKKSTPERKQPLVKRAAKALINRRRATSNGGSTTEDSSVYSADERSSPPLAGTNEDVDHLPPTCSSSDDHDVISPDFSAKNPLLRSRNDFMGGSVRSPRRYGNDHDGHIYTSPFLPPRVPIRNSPMTSSLRSRPPPPPYNRSPAHKIEQNSSFFEPIAHSTPNSSILEERRVVGEGEKRELVRDKEERIDKTLSYYENVNLPQNPPDLPENSDLKPNESTIWHEYGCV
Protein: Embryonic ectoderm development (A0A8I6AJ96)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MLEDDAVSIESGTNTERPDTPTNTPNAPGRKSWGKGKWKSKKCKYSFKCVNSLKEDHNQPLFGVQFNWHSKEGDPLVFATVGSNRVTLYECHSQGEIRLLQSYVDADADENFYTCAWTYDSNTSHPLLAVAGSRGIIRIINPITMQCIKHYVGHGNAINELKFHPRDPNLLLSVNHALRLWNIQTDTLVAIFGGVEGHRDEVLSADYDLLGEKIMSCGMDHSLKLWRINSKRMMNAIKESYDYNPNKTNRPFISQKIHFPDFSTRDIHRNYVDCVRWLGDLILSKSCENAIVCWKPGKMEDDIDKIKPSESNVTILGRFDYSQCDIWYMRFSMDFWQKMLALGNQVGKLYVWDLEVEDPHKAKCTTLTHHKCGAAIRQTSFSRDSSILIAVCDDASIWRWDRLR
Protein: FAS-associated factor 2 (UBX domain-containing protein 8) (Q3TDN2)
Organism: Mus musculus (Mouse)
Function: Plays an important role in endoplasmic reticulum-associated degradation (ERAD) that mediates ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. By controlling the steady-state expression of the IGF1R receptor, indirectly regulates the insulin-like growth factor receptor signaling pathway. Involved in inhibition of lipid droplet degradation by binding to phospholipase PNPL2 and inhibiting its activity by promoting dissociation of PNPL2 from its endogenous activator, ABHD5 which inhibits the rate of triacylglycerol hydrolysis.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q96CS3}. Lipid droplet {ECO:0000250|UniProtKB:Q96CS3}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q96CS3}.
Interaction partners:
- Transitional endoplasmic reticulum ATPase
- Ubiquitin recognition factor in ER-associated degradation protein 1
- Nuclear protein localization protein 4 homolog
- UBX domain-containing protein 7
- UBX domain-containing protein 1
- Ubiquitin-associated domain-containing protein 2
- Lipid droplet-regulating VLDL assembly factor AUP1
- Derlin-2
- Large proline-rich protein BAG6
- E3 ubiquitin-protein ligase AMFR
Sequence:
MAAPEEQDLTQEQTEKLLQFQDLTGIESMEQCRLALEQHNWNMEAAVQDRLNEQEGVPSVFNPPPARPLQVNTADHRIYSYVVSRPQPRGLLGWGYYLIMLPFRFTYYTILDIFRFALRFIRPDPRSRVTDPVGDIVSFMHSFEEKYGRAHPVFYQGTYSQALNDAKRELRFLLVYLHGDDHQDSDEFCRNALCAPEVISLINSRMLFWACSTNKPEGYRVSQALRENTYPFLAMIMLKDRRMTVVGRLEGLIQPDDLINQLTFIMDANQTYLVSERLEREERNQTQVLRQQQDEAYLASLRADQEKERKKREEKERKRRKEEEVQQQKLAEERRRQNLQEEKERKLECLPPEPSPDDPESVKIIFKLPNDSRVERRFHFSQSLTVIHDFLFSLKESPEKFQIEANFPRRVLPCVPSEEWPNPPTLQEAGLSHTEVLFVQDLTDE
Protein: Zinc finger protein 354C (Kidney, ischemia, and developmentally-regulated protein 3) (hKID3) (Q86Y25)
Organism: Homo sapiens (Human)
Function: May function as a transcription repressor. Binds to 5'-CCACA-3' core sequence. Suppresses osteogenic effects of RUNX2. May be involved in osteoblastic differentiation (By similarity). Plays a role in postnatal myogenesis, may be involved in the regulation of satellite cells self-renewal (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:15555547, ECO:0000269|PubMed:33154469}. Nucleus membrane {ECO:0000269|PubMed:33154469}. Cytoplasm {ECO:0000269|PubMed:33154469}.
Interaction partners:
- Transcription intermediary factor 1-beta
- Protein deacetylase HDAC6
Sequence:
MAVDLLSAQEPVTFRDVAVFFSQDEWLHLDSAQRALYREVMLENYSSLVSLGIPFSMPKLIHQLQQGEDPCMVEREVPSDTRLGFKTWLETEALPHRQDIFIEETSQGMVKKESIKDGHWDINFEEAVEFESEIEEEQEKKPLRQMIDSHEKTISEDGNHTSLELGKSLFTNTALVTQQSVPIERIPNMYYTFGKDFKQNFDLMKCFQIYPGGKPHICNECGKSFKQNLHLIEHQRIHTGEKPYKCNECEKTFSHRSSLLSHQRIHTGEKPYKCNECEKAFSNSSTLIKHLRVHTGEKPYRCRECGKAFSQCSTLTVHQRIHTGEKLYKCGECEKAFNCRAKLHRHQRIHTGEKPYKCSECGKGYSQFTSLAEHQRFHTGEQLYTCLECGRTFTRIVTLIEHQRIHTGQKPYQCNECEKAFNQYSSFNEHRKIHTGEKLYTCEECGKAFGCKSNLYRHQRIHTGEKPYQCNQCGKAFSQYSFLTEHERIHTGEKLYKCMECGKAYSYRSNLCRHKKVHTKEKLYKWKEYGKPFICSSSLTQYQRFFKGDKAYEV
Protein: D-glycero-alpha-D-manno-heptose 1-phosphate guanylyltransferase (EC 2.7.7.71) (D-alpha-D-heptose 1-phosphate guanylyltransferase) (Q0P8J1)
Organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Function: Catalyzes the GDP transfer from GTP to D-glycero-alpha-D-manno-heptose 1-phosphate, yielding GDP-D-alpha-D-heptose. Is able to use ATP, CTP or UTP as substrate in the presence of pyrophosphatase, but at a significantly slower rate. Can also form GDP-alpha-D-mannose from alpha-D-mannose 1-phosphate and GTP.
Interaction partners:
- D-glycero-alpha-D-manno-heptose 7-phosphate kinase
- Selenocysteine-specific elongation factor
- dTDP-4-dehydrorhamnose 3,5-epimerase
- D-glycero-alpha-D-manno-heptose-1,7-bisphosphate 7-phosphatase
- GDP-D-glycero-alpha-D-manno-heptose dehydrogenase
- Sugar transferase
- Phosphoheptose isomerase 2
- GDP-L-fucose synthase
- Capsular polysaccharide heptosyltransferase
- Methyltransferase FkbM domain-containing protein
Sequence:
MQAIILCGGLGTRLKSIIKDIPKPMAPINDKPFLEFIFEYLKKQGIKEVILAVSYKYEVIKEYFKDEFLGIKIKYSIEKEPLGTGGAIKETLKFVKNEAYVLNGDTFFDIDLSKLKLNESKICLALKQMNDFDRYGTVNVDEQDLVISFEEKVFKKQGLINGGIYLLTKDIFNDFALQEKFSFEEFLQENYKKLKARACIFDDYFIDIGVPEDYYHFLINN
Protein: G protein-activated inward rectifier potassium channel 2 (GIRK-2) (BIR1) (Inward rectifier K(+) channel Kir3.2) (KATP-2) (Potassium channel, inwardly rectifying subfamily J member 6) (P48051)
Organism: Homo sapiens (Human)
Function: This potassium channel may be involved in the regulation of insulin secretion by glucose and/or neurotransmitters acting through G-protein-coupled receptors. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- G protein-activated inward rectifier potassium channel 1
- G protein-activated inward rectifier potassium channel 3
- Inner centromere protein
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid type B receptor subunit 1
- Borealin
- G protein-activated inward rectifier potassium channel 4
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit gamma
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MAKLTESMTNVLEGDSMDQDVESPVAIHQPKLPKQARDDLPRHISRDRTKRKIQRYVRKDGKCNVHHGNVRETYRYLTDIFTTLVDLKWRFNLLIFVMVYTVTWLFFGMIWWLIAYIRGDMDHIEDPSWTPCVTNLNGFVSAFLFSIETETTIGYGYRVITDKCPEGIILLLIQSVLGSIVNAFMVGCMFVKISQPKKRAETLVFSTHAVISMRDGKLCLMFRVGDLRNSHIVEASIRAKLIKSKQTSEGEFIPLNQTDINVGYYTGDDRLFLVSPLIISHEINQQSPFWEISKAQLPKEELEIVVILEGMVEATGMTCQARSSYITSEILWGYRFTPVLTLEDGFYEVDYNSFHETYETSTPSLSAKELAELASRAELPLSWSVSSKLNQHAELETEEEEKNLEEQTERNGDVANLENESKV
Protein: Malate dehydrogenase (EC 1.1.1.37) (A0A5K1VW95)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLKDVIATDKEDVAFKDLDVAILVGSMPRREGMERKDLLKANVKIFKSQGAALDKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKAQIALKLGVTANDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFVTTVQQRGAAVIKARKLSSAMSAAKAICDHVRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKELTEEKESAFEFLSSAXLDNDVTKCFKAEESKCRL
Protein: E3 SUMO-protein ligase PIAS4 (EC 2.3.2.27) (PIASy) (Protein inhibitor of activated STAT protein 4) (Protein inhibitor of activated STAT protein gamma) (PIAS-gamma) (Q9JM05)
Organism: Mus musculus (Mouse)
Function: Functions as an E3-type small ubiquitin-like modifier (SUMO) ligase, stabilizing the interaction between UBE2I and the substrate, and as a SUMO-tethering factor. Mediates sumoylation of CEBPA, PARK7, HERC2, MYB, TCF4 and RNF168. Plays a crucial role as a transcriptional coregulation in various cellular pathways, including the STAT pathway, the p53/TP53 pathway, the Wnt pathway and the steroid hormone signaling pathway. Involved in gene silencing. In Wnt signaling, represses LEF1 and enhances TCF4 transcriptional activities through promoting their sumoylations. Enhances the sumoylation of MTA1 and may participate in its paralog-selective sumoylation (By similarity). Binds to AT-rich DNA sequences, known as matrix or scaffold attachment regions (MARs/SARs). Catalyzes conjugation of SUMO2 to KAT5 in response to DNA damage, facilitating repair of DNA double-strand breaks (DSBs) via homologous recombination (HR) (By similarity). Mediates sumoylation of PARP1 in response to PARP1 trapping to chromatin (By similarity).
Subcellular location: Nucleus, PML body {ECO:0000269|PubMed:11731474, ECO:0000269|PubMed:16816390}. Note=Colocalizes with SUMO1 and TCF7L2/TCF4 and LEF1 in a subset of PML (promyelocytic leukemia) nuclear bodies. Accumulates in the cytoplasm upon treatment with UVB and TNF-alpha. {ECO:0000250|UniProtKB:Q8N2W9}.
Interaction partners:
- Small ubiquitin-related modifier 1
- Small ubiquitin-related modifier 3
- Small ubiquitin-related modifier 2
- Serine-protein kinase ATM
- Cellular tumor antigen p53
- SUMO-conjugating enzyme UBC9
- NF-kappa-B essential modulator
- Protein kinase C zeta type
- E3 ubiquitin-protein ligase RNF168
- Signal transducer and activator of transcription 3
Sequence:
MAAELVEAKNMVMSFRVSDLQMLLGFVGRSKSGLKHELVTRALQLVQFDCSPELFKKIKELYETRYAKKSAEPGPQAPRPLDPLALHSMPRTPLSGPTVDYPVLYGKYLNGLGRLPTKTLKPEVRLVKLPFFNMLDELLKPTELVPQSAEKLQESPCIFALTPRQVEMIRNSRELQPGVKAVQVVLRICYSDTSCPQEDQYPPNIAVKVNHSYCSVPGYYPSNKPGVEPKRPCRPINLTHLMYLSSATNRITVTWGNYGKSYSVALYLVRQLTSSDLLQRLKTIGVKHPELCKALVKEKLRLDPDSEIATTGVRVSLICPLVKMRLSVPCRAETCAHLQCFDAVFYLQMNEKKPTWMCPVCDKPAAYDQLIIDGLLSKILSECEGADEIEFLAEGSWRPIRAEKEPSCSPQGPILVLGTSDANGLAPASSTPGIGSGLSGPGSAGSGAGAAGSLENGKTGADVVDLTLDSSSSSEDEDEDEDDDEDEDEGPRPKRRCPFQKGLVPAC
Protein: MADS domain protein (Q6EUV6)
Organism: Gerbera hybrida (Daisy)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGRGRVELKRIENKINRQVTFSKRRNGLLKKAYELSVLCDAEVGLIIFSSRDKLYEFGSVGVMKTLERYQRCCFNPQDNNNERETQSWYQEVSKLKAKFESLQRTQRHLLGEDLGPLSVKELHNLEKQLEGALTQARQRKTQIMVEQMEELRRKERELGDMNKHLKIKVSHELSTFDAEGQGYRAQLPCPWNSGTNNTFTMHPSQSNPMDCQQEPILQIGYNQFMHGEGSSVQRNMVGENGIHGWVL
Protein: Cathepsin D (EC 3.4.23.5) (Q8AWD9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Lysosome {ECO:0000256|ARBA:ARBA00004371}.
Interaction partners:
- Lysosomal-associated membrane protein 1b
- Cathepsin B
- Cathepsin S, ortholog 2, tandem duplicate 2
- Napsin A aspartic peptidase
- Cathepsin S, ortholog 1
- Cathepsin S, b.1
- Cathepsin Bb
- Cathepsin La
- Cystein proteinase inhibitor protein salarin
- Cystein proteinase inhibitor protein salarin
Sequence:
MRIAFLLLVVAFFCTSDAIVRIPLKKFRTLRRTLSDSGRSLEELVSSSNSLKYNLGFPASNDPTPETLKNYLDAQYYGEIGLGTPVQTFTVVFDTGSSNLWVPSVHCSLTDIACLLHHKYNGGKSSTYVKNGTQFAIQYGSGSLSGYLSQDTCTIGDIAVEKQIFGEAIKQPGVAFIAAKFDGILGMAYPRIAVDGVPPVFDMMMSQKKVEKNVFSFYLNRNPDTQPGGELLLGGTDPKYYTGDFNYVDISRQAYWQIHMDGMSIGSGLSLCKGGCEAIVDTGTSLITGPAAEVKALQKAIGAIPLMQGEYMVDCKKVPTLPTISFSLGGKVYSLTGEQYILKESQGGHDICLSGFMGLDIPPPAGPLWILGDVFIGQYYTVFDRENNRVGFAKAKSV
Protein: Uncharacterized protein (Q587G7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Transmembrane protein
- Thioredoxin domain-containing protein
- Mitochondrial fission process protein 1
- MICOS complex subunit MIC10
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Rhodanese domain-containing protein
Sequence:
MTVATAPTPPDLSKPPADKLEIHTQTTGNDGGSSSGAAKEVFVTPEEVERQVKLGLLLVQLGAAKENQIFGPRGLMTPPRDLLVINRYEDSKEARRPFKWYDPISWFLSGPKPSPMFWSPSPFRNEEQERAVTTSPTAASGTAAATQTPEIGPATSLAPAVKKIRAIPPVDMRPLGDDVHLEAAVRLDREKLLKDEETLHKMLNGVEDTRHAYLVPAQELQCEDEVLAVVQCYEKHVSAIQAASGSGMSNSGKILSEGAALELPVIADVLQCGPVVSLLRRCAEGVVGAYSQKDVAVQL
Protein: Interferon-inducible protein AIM2 (Interferon-inducible protein 210) (Ifi-210) (Interferon-inducible protein p210) (Q91VJ1)
Organism: Mus musculus (Mouse)
Function: Involved in innate immune response by recognizing cytosolic double-stranded DNA and inducing caspase-1-activating inflammasome formation in macrophages. Upon binding to DNA is thought to undergo oligomerization and to associate with PYCARD initiating the recruitment of caspase-1 precursor and processing of interleukin-1 beta and interleukin-18. Detects cytosolic dsDNA of viral and bacterial origin in a non-sequence-specific manner. Also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection. Can also trigger PYCARD-dependent, caspase-1-independent cell death that involves caspase-8.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19158679, ECO:0000269|PubMed:22555457}. Inflammasome {ECO:0000269|PubMed:19158679, ECO:0000269|PubMed:27846608}. Nucleus {ECO:0000269|PubMed:27846608}. Note=Activated inflammasomes can aggregate in the cytosol as speck-like particles (PubMed:19158679). Activated inflammasomes can also aggregate in the nucleus in response to DNA damage: AIM2 is recruited to double-strand DNA breaks and mediates activation of the AIM2 inflammasome (PubMed:27846608). {ECO:0000269|PubMed:19158679, ECO:0000269|PubMed:27846608}.
Interaction partners:
- Caspase-1
- Pyrin
- NACHT, LRR and PYD domains-containing protein 1a
- NLR family CARD domain-containing protein 4
- NACHT, LRR and PYD domains-containing protein 6
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 3
- Baculoviral IAP repeat-containing protein 1a
- NACHT, LRR and PYD domains-containing protein 1b allele 2
- Gasdermin-D
Sequence:
MESEYREMLLLTGLDHITEEELKRFKYFALTEFQIARSTLDVADRTELADHLIQSAGAASAVTKAINIFQKLNYMHIANALEEKKKEAERKLMTNTKKRGTQKVENRSQAENCSAASATRSDNDFKEQAATEVCPQAKPQKKQMVAEQEAIREDLQKDPLVVTVLKAINPFECETQEGRQEIFHATVATETDFFFVKVLNAQFKDKFIPKRTIKISNYLWHSNFMEVTSSSVVVDVESNHEVPNNVVKRARETPRISKLKIQPCGTIVNGLFKVQKITEEKDRVLYGIHDKTGTMEVLVLGNPSKTKCEEGDKIRLTFFEVSKNGVKIQLKSGPCSFFKVIKAAKPKTDMKSVE
Protein: Inactive tyrosine-protein kinase PEAK1 (Pseudopodium-enriched atypical kinase 1) (X1WGC5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSACNTFTEHVWKPGECKNCFKPKSLHRPPESASECKTNINAKLTNSQRSTSSSRAGQVRPPVAKKPTIAVKPTMMLPCSPPGLDSEGNVPRLAEGPQVTKSSPFTVWNHNSLNSLRPAGTNNNQGEDLVGQTEAYSAISLQPTSSNNNGLTDVLKEIAGLGSSPSTSRNDFFGRICSSYRRSLERGLPAASCLHAGSSGRGAMKRVSLSDSTEVISTEGGRFCYPEFSSDGDDEEEDSDEDDDGEHDSWDESDEELLAMGIRMRGQPRFANFRAATLSPVPFALVKKWNTVPLRNRSLQRFCAVDYDDSYDEILNGYPSVDSNGAPALLSYTSDHQGSGFLSTSESTTSPESLASLPEETCTESSRDTDDHRNGLPFPPNKETSSRGPSSPKSNETHKAVLAIRLEEQDDSQREGGALPQALPGQPITISFSPTEEQAKPYRVVNLEKAPICKPYTVVDVSASMATKDNTHLSEITPKSSVTVDPCPVSPISPQSPRSPMSPVTSPSISLSPLMPQSPIGSSSGLSGFRTKPGSIRYQEVWTSCTSPRQKIPKVDLTSGSADPRLINHKSAPTSPTAAFGSARTVPTKSPNLSEIKFNSYNNAGMPPFPIIIRDEPAYARSSKKAVKVPIVINPSAYDNLAVYKSFLGLNGELPHSKPGAGERVASHTYEEIGSSESSQPSPSEQKPPPISADLTATGELRTTTVNDGKYRTTTGVAFHAGIQSTNPAFLAHSSLDRIRNPSSEQPPEGSKDCQLASSGSSGQREKASAVLSQIVSSIQPPVSPPESPAGQSKTCSAEELYSLPPDASRDTTVNRPKSLHCSAEPHKETPHKLLPKSQSASAAVPPTSPKSETSAPFPPVRSSSSPYHSSNLLQRHFNWTRPAGAKSTDGETSPGAEGRRSSDGNKPKRWISFKSFFRRRKDEDEQKEKMEREKEKGKLLGLDGTVITVLPPPPLQRQQWFSESKTDDPLQKPTIIFTYKSESATGGEEAELRVEEHKESVTAEGGASSLSTPPKSRASLLISKVMNQLPVQETEISSATSLPAKLELSPLREPPASCPPPASPTSNSSRQADPEEEGIAHTISRSPESNSCRATYTNLGQSRANMIPVKHPRHPKASDDTLTSDPEVSELTNKSTPPPLPKKLVPRAQIDSSAAGKELAPRPKGEARPGGTSLSVANPLYDLESTWDTASQSSSLSSEARHHDESGDSLECPVGGRSLSCLTSSTSMQGCDRRGYRSTESLTARTRGPGRLTKGQKQMPYRGMESWEEVVGRIRGLHTDTLRKLATRCEDRFMAGQKDHLRFGTDSWSHFRLTAGKPCCEAGDAVYYTASFAKEPLMNYAVKICRGVVKETQQQFFHSLAVRQSIAVHFNIQQDCGHFLADVPARLLPWEQKEDKDERGGTEGGEDEKEDAAGPGGKLCSCVVVITREVPFQTVADFVREGVERHARNPELYERQVCLLLLQLCAGLEHMKPYHVTHCDLRLENLLLVHCQPGNPWNLELLEPNNNAASGSSTAAASACPARLIISNFSQAKLKNVVLEPASFRDHSRLAPELLTATQYRKCDEFQTGILIYEMLHRPNPFEDSPELKEREYCSSDLPQLPLRSLYSNGLQQLATLLLNPNPSERIQMADARACLQCLLWGPREDLFNSLNPGAGTVQRHTVLQNWLDLKRTLMMIKFAERSLESGCGVSLEDWLCCQYLAFSTTESLSRVIKILQQPQGVLI
Protein: Dipeptidyl-peptidase 7 (DPP7) (EC 3.4.14.-) (A6L2J8)
Organism: Phocaeicola vulgatus (strain ATCC 8482 / DSM 1447 / JCM 5826 / CCUG 4940 / NBRC 14291 / NCTC 11154) (Bacteroides vulgatus)
Function: Catalyzes the removal of dipeptides from the N-terminus of oligopeptides. Most potently cleaves the synthetic substrate Met-Leu-methylcoumaryl-7-amide (Met-Leu-MCA), followed by Leu-Arg-MCA, while this enzyme does not hydrolyze Gly-Arg-, Gly-Gly-, Lys-Lys-, or Gly-Pro-MCA.
Interaction partners:
- Dipeptidyl-peptidase
- Dipeptidyl peptidase IV
- DUF4369 domain-containing protein
Sequence:
MKKFKLLLLALMCVAFLPSKADEGMWLLQLMQEQHLADRMKAQGLLLEADDIYNPNRVSLKDAVGIFGGGCTGEIISPDGLILTNHHCGYGAIQQHSSVEHDYLTDGFWAKSRKEELPTPGLKFKFVERIVDVTDKVNNKVKSGEVKEEETFEYDFLKKLADEELKASDLNGKAGISAQALPFYAGNKFYLIYLKTYSDVRMVAAPPSSIGKFGGETDNWMWPRHTCDFSVFRIYADANGEPAEYNENNVPLKAKKHLAISLKGINEGDYAMIMGFPGSTNRYLTQSEVKQRMHSTNEPRIRIRGVRQDVLKKEMAASDKVRIQYASKYAGSSNYWKNSIGMNKAIIDNKVLETKAEQEAKFAAFAKAKGNTDYEKVVSEIDAAIEKSNPILYNYTCFREVFQGGIEFGTPYLILDKLKDAIKNKDKEAINKNIETLKKVYADIHNKDYDHEVDRKVAKALLPLYAEMVPADALPAFYTTIQKDFKGNYDAYVDHCYDNSIFSNEANFNKFIKKPTVKAIEKDPMTAYVRAKYDLMDKLGNELAESMKGMDLLHKTYVRGLCEMYSPEPKAPDANFTIRLTYGNVKSYNPKDGVHYKYYTTLKGVMEKEDPTNPEFVVPAKLKELYEAKDFGRYALPNGDMPACFLTTNDITGGNSGSPVINGNGELIGAAFDGNWESLSGDINFDNNLQRCIAVDIRYVLFIIDKLGGCKHLIDEMTIVE