wanglab/gogpt-training-data huggingface dataset:
Protein: Pyrin (Q9JJ25)
Organism: Rattus norvegicus (Rat)
Function: Involved in the regulation of innate immunity and the inflammatory response in response to IFNG/IFN-gamma. Organizes autophagic machinery by serving as a platform for the assembly of ULK1, Beclin 1/BECN1, ATG16L1, and ATG8 family members and recognizes specific autophagy targets, thus coordinating target recognition with assembly of the autophagic apparatus and initiation of autophagy. Acts as an autophagy receptor for the degradation of several inflammasome components, including CASP1, NLRP1 and NLRP3, hence preventing excessive IL1B- and IL18-mediated inflammation. However, it can also have a positive effect in the inflammatory pathway, acting as an innate immune sensor that triggers PYCARD/ASC specks formation, caspase-1 activation, and IL1B and IL18 production (By similarity). Together with AIM2, also acts as a mediator of pyroptosis, necroptosis and apoptosis (PANoptosis), an integral part of host defense against pathogens, in response to bacterial infection (By similarity). It is required for PSTPIP1-induced PYCARD/ASC oligomerization and inflammasome formation. Recruits PSTPIP1 to inflammasomes, and is required for PSTPIP1 oligomerization (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:O15553}. Cell projection, ruffle {ECO:0000250|UniProtKB:O15553}. Cell projection, lamellipodium {ECO:0000250|UniProtKB:O15553}. Cytoplasm {ECO:0000250|UniProtKB:O15553}. Cytoplasmic vesicle, autophagosome {ECO:0000250|UniProtKB:O15553}. Nucleus {ECO:0000250|UniProtKB:O15553}. Note=Associated with microtubules and with the filamentous actin of perinuclear filaments and peripheral lamellar ruffles. In pre-apoptotic cells, colocalizes with PYCARD/ASC in large specks (pyroptosomes). In migrating monocytes, strongly polarized at the leading edge of the cell where it colocalizes with polymerizing actin and PYCARD/ASC (By similarity). {ECO:0000250|UniProtKB:O15553}.
Interaction partners:
- NLR family CARD domain-containing protein 4
- NLR family, pyrin domain-containing 1A.
- Caspase-1
- Absent in melanoma 2
- Proline-serine-threonine phosphatase-interacting protein 1
- NACHT, LRR and PYD domains-containing protein 3
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 6
- NLR family, apoptosis inhibitory protein 6
- Interleukin-18
Sequence:
MANTRVDHLLNTLEELLPYELEKFKFKLHTTSLEKGHSRIPLSLVKMARPIKLTRLLLTYYGEEYAVRLTLQILRATNQRQLAEELHKATGPEHLTEENGVGGSVQSSAENKDKGVKGSDVPGEDEAQQNDDESDILPPIQAEVGKGPQKKSLAKRKDQRGPESLDSQTKPGARSAAPLYRRTLVTQSPGDKENRAGAQPQECQLCREAARSTAMSQGGERSRRLKCICLQERSDPGVLKLPLTQKKENPQIQKLFRLKRKQEMAVSFVREATLNGRTTGTLEKGVGIPEHSMMLDEETSRNMSSKISLTREKRCTASWTENGNGGPETPETLGETVSSILCDSCSPKVLLSLGEKLAQTPEDPASLGQAASKGRSRDKVACPLCHTQGELPAKACVQSSCSCSVAPGDPKASGRHSICFQCQSSRAGKSCEAQSPQFLPQCPRHMKQVQLLFCEDHREPICLICRLSQEHQGHRVRPIEEAALQYKEQIRKQLERLREMRGYVEEHKLPADKKAEDFLKQTETQKQRISCPLEKLFQFLEQQEQLFVTWLQELVQTIGKVRETYYTQVSLLDKLIGELEAKQDQPEWELMQDIGATLHRAETMTASELLGIPPGVKEKLHLLYQKSKSAEKNMQRFSEMLGSEMAFSASDVATREGCRPSTTKAQALIPTVHLKCDGAHTQDFDVILCAELEAGGSEPQDYLHPSSAQDTPELHEIHSQNNKRKFKSFLKWKPSFSRTDRCLRTCW
Protein: Small ribosomal subunit protein uS14m (28S ribosomal protein S14, mitochondrial) (MRP-S14) (S14mt) (O60783)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25838379}.
Interaction partners:
- Small ribosomal subunit protein uS10m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS15m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein bS16m
Sequence:
MAAFMLGSLLRTFKQMVPSSASGQVRSHYVDWRMWRDVKRRKMAYEYADERLRINSLRKNTILPKILQDVADEEIAALPRDSCPVRIRNRCVMTSRPRGVKRRWRLSRIVFRHLADHGQLSGIQRATW
Protein: Growth factor receptor-bound protein 2 (Adapter protein GRB2) (SH2/SH3 adapter GRB2) (Q07883)
Organism: Gallus gallus (Chicken)
Function: Adapter protein that provides a critical link between cell surface growth factor receptors and the Ras signaling pathway.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. Golgi apparatus {ECO:0000250}.
Interaction partners:
- SHC-transforming protein 1
- SOS Ras/Rho guanine nucleotide exchange factor 2
- SOS Ras/Rac guanine nucleotide exchange factor 1
- GRB2 associated binding protein 1.
- Uncharacterized protein.
- Focal adhesion kinase 1
- SH2 domain-containing protein.
- Epidermal growth factor receptor
- Insulin receptor substrate 1.
- Fibroblast growth factor receptor substrate 2
Sequence:
MEAIAKYDFKATADDELSFKRGDILKVLNEECDQNWYKAELNGKGGFIPKNYIEMKPHPWFFGKIPRAKAEEMLGKQRHDGAFLIRESESAPGDFSLSVKFGNDVQQFKVLRDGAGKYLLWVVKFNSLNELVDYHRSTSVSRNQQIFLRDIEQVPQQPTYVQALFDFDPQEEGELGFRRGDFIQVLDNSDPNWWKGACHGQTGMFPRNYVTPVNRNI
Protein: Ceroid-lipofuscinosis neuronal protein 5 homolog (Protein CLN5) (Q553W9)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Battenin
- Cathepsin D
- Cysteine proteinase 1
- Tripeptidyl-peptidase 1
- Palmitoyl-protein thioesterase 1
- Cathepsin B
Sequence:
MKRTIIILLFVSLFVTFVLSQIPDNDPELCQQRIQREDCPQTPVPWGTFNDNDEIEVYYMQAPVFEAVFGNFFGKLGGYHSAIGFYDLTTGLNYTAEYDAFFEVGNGTLPNIINVDGKDELLWCNAGILCTVPYINETYWDKNIYSTASKTYMGTINGTQLNQYIEWMQQYNISNPVYQTWDVWNNYGQDLFVPSTTCDDFTQQSIEHLGSIGINYNCSTVFKRDYINLFTEKPQPIDFTEHYDDIFKFYEAVLEIKEGSIAQIIERILSIIGLKKYIYVQGEYYLLELNYPFMNAKYDYITLPGCPANGIDYENGNFIHLN
Protein: Odorant receptor 88a (Q9VFN2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Odorant receptor which mediates acceptance or avoidance behavior, depending on its substrates. The odorant receptor repertoire encodes a large collection of odor stimuli that vary widely in identity, intensity, and duration. May form a complex with Orco to form odorant-sensing units, providing sensitive and prolonged odorant signaling and calcium permeability.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Odorant receptor 67d
- Odorant receptor 65a
- Odorant receptor 47b
- Odorant receptor 47a
- Odorant receptor 56a
- Odorant receptor 23a
- Odorant receptor 43a
- Odorant receptor 85a
- Odorant receptor 7a
- Odorant receptor 98a
Sequence:
MKPTEIKKPYRMEEFLRPQMFQEVAQMVHFQWRRNPVDNSMVNASMVPFCLSAFLNVLFFGCNGWDIIGHFWLGHPANQNPPVLSITIYFSIRGLMLYLKRKEIVEFVNDLDRECPRDLVSQLDMQMDETYRNFWQRYRFIRIYSHLGGPMFCVVPLALFLLTHEGKDTPVAQHEQLLGGWLPCGVRKDPNFYLLVWSFDLMCTTCGVSFFVTFDNLFNVMQGHLVMHLGHLARQFSAIDPRQSLTDEKRFFVDLRLLVQRQQLLNGLCRKYNDIFKVAFLVSNFVGAGSLCFYLFMLSETSDVLIIAQYILPTLVLVGFTFEICLRGTQLEKASEGLESSLRSQEWYLGSRRYRKFYLLWTQYCQRTQQLGAFGLIQVNMVHFTEIMQLAYRLFTFLKSH
Protein: Exosome complex protein C1739.07 (O74469)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for exosome-dependent processing of pre-rRNA and small nucleolar RNA (snRNA) precursors. Involved in processing of 35S pre-rRNA at the A0, A1 and A2 sites (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Exosome complex exonuclease dis3
- Exosome complex component rrp43
- Exosome complex component rrp4
- Exosome complex component rrp45
- Exosome complex component rrp46
- Exosome complex component csl4
- Exosome complex component rrp40
- Exosome complex component rrp42
- Exosome complex component ski6
- Exosome complex component mtr3
Sequence:
MDPEYSELFERLNKQLDNVEDVLKPLKDAESIFELAEGKSELEQAKLYITMSYAINSTLYSFYKLNGIDASERPVMQELQRVKNYISKIQQAEKNVNPKTEAVNTSNAAISSSSSNRPKVAKDAATRIIKHHT
Protein: 6-phosphogluconolactonase-like protein 2 (Suppressor of LOS1) (P37262)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in regulation of tRNA subcellular distribution.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15454531}.
Interaction partners:
- Glucose-6-phosphate 1-dehydrogenase
- Probable gluconokinase
- 6-phosphogluconate dehydrogenase, decarboxylating 2
- 6-phosphogluconate dehydrogenase, decarboxylating 1
- Exportin-T
- 6-phosphogluconolactonase-like protein 1
- Bifunctional purine biosynthesis protein ADE16
Sequence:
MTTTVPKIFAFHEFSDVAEAVADHVVHAQDGALAPKNERKHSVPNISMNALDMTREASCKSTASAAEGKSGSSGSGSGSSKPKKEKRFKIALSGGSLIEVLHEGLLKRDDVRWGDWDIYFADERLVPFSSNESNYGCAKRKILDLIDTAKYGTPKVYHIDESLIDDPQECADNYEKVLIRGFAGRDSVKLPMFDLFLLGCAPDGHIASLFPNFQDNLREKLAWVVPVENAPSGPSTRISLTIPVICHSHRVTFVVEGATKAPIIKTIMERPEKGLPSSIVNEGAAGRVSWFVDDDALTDVLVTKKKYKFHQGLSI
Protein: Thioredoxin (H9ZYJ2)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MVKQIESKTAFQEALDAAGDKLVVVDFSATWCGPCKMIKPFFHSLSEKYSNVIFLEVDVDDCQDVASECEVKCMPTFQFFKKGQKVGEFSGANKEKLEATINELV
Protein: Homeobox A9 (A8MVF3)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MATTGALGNYYVDSFLLGADAADELSVGRYAPGTLGQPPRQAATLAEHPDFSPCSFQSKATVFGASWNPVHAAGANAVPAAVYHHHHHHPYVHPQAPVAAAAPDGS
Protein: Enolase (EC 4.2.1.11) (2-phospho-D-glycerate hydro-lyase) (2-phosphoglycerate dehydratase) (C1G9X3)
Organism: Paracoccidioides brasiliensis (strain Pb18)
Interaction partners:
- Fructose-bisphosphate aldolase
- Pyruvate kinase
- Phosphoglycerate kinase
- 2,3-bisphosphoglycerate-independent phosphoglycerate mutase
- Glucose-6-phosphate isomerase
- Glyceraldehyde-3-phosphate dehydrogenase
- Triosephosphate isomerase
- Fructose-bisphosphate aldolase
- transketolase
- Triosephosphate isomerase
Sequence:
MAITKIHARSVYDSRGNPTVEVDVVTETGLHRAIVPSGASTGQHEACELRDGDKSKWLGKGVLNAVKNVNSIIGPAIIKENIDVKDQSKVDEFLNKLDGTPNKSKLGANAILGVSLAIAKAGAAEKGVPLYAHVSDLAGTKKPYVLPVPFQNVLNGGSHAGGRLAFQEFMIVPTAAPSFSEALRQGSEVYHKLKALAKKKYGQSAGNVGDEGGVAPDIQTPEEALDLITEAIEQAGYTGQVKIALDIASSEFYKADEKKYDLDFKNPDSDKSKWLTYEQLADLYKKLASKYAIVSIEDPFAEDDWEAWSYYFKTCDLQVVADDLTVTNPIRIKKAIELKSCNALLLKVNQIGTLTESIQAAKDSYAAGWGVMVSHRSGETEDVTIADVVVGLRAGQIKTGAPARSERLAKLNQILRIEEELGSNAVYAGDKFRAAINM
Protein: Serine/threonine-protein kinase zyg-8 (EC 2.7.11.1) (Doublecortin-like and CAM kinase-like protein) (Q95QC4)
Organism: Caenorhabditis elegans
Function: Plays a role in spindle positioning during asymmetric division of one-cell stage embryos. Affects spindle position by promoting microtubule assembly during anaphase. Plays a role in regulating thermotaxis responses in AFD thermosensory neurons.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:11702948}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:11702948, ECO:0000269|PubMed:39226307}. Note=Enriched at microtubule asters throughout the cell cycle and is present on the spindle during mitosis. {ECO:0000269|PubMed:11702948}.
Interaction partners:
- Exchange factor for Arf-6
- Tubulin beta-1 chain
- Tubulin beta-2 chain
- Tubulin beta-4 chain
- Tubulin beta chain
- Tubulin beta chain
- Tubulin beta chain
- Tubulin alpha-3 chain
- Tubulin alpha chain
- Patronin
Sequence:
MPQTSAWQLNDTTARPPPPPPPPGSEAGGSDGASMNGANTLPRVSKRVSAAGKTSNIPRFKRPHLPHSTRPLSAVLTSSSSPVVHRKISPSSSAPSTSSAHRRFSHLPQQHFHHHIHHNQTAVISEETLTTPRASTLNLNQTSVFPTAISQGSMPNSGTNTAEASMTSSVCAMETEGTNGDELAESRDMVSEMQRRCRIGPSGYPHLLKAKRLRFYRNGDQYFKGIQYALQSDRVKSMQPLMEDLMKTVICDSTALPHGIRHIFTIDGAQRITSVDQFEDGGGYVCSSTDAFKPVDYSRAAEPSWRLTLANRYNRHLETKKLALSVVEPCHENTDFVFPRIIKVIRNGVKPRRISRHLLNKKTARSFDQVLRDLTFVVKLDSGAIRKLFTLSGRPVLSLQDFFRDDDVFVAYGGNEKMAADDLLVASEEHKSVGSGTSSNMRRTSRRSTMPNRNESLRHDRSGSVIPDQDQQRLPPLLDEKFQLVRLIGDGNTAVVYEVIDKTNNDDRKAMKVIARENVIGKEHLIEMELAILQKIDHTFIVQLYDHWFVDDSYYLSLELIEMGDLFEHLRIVRRVPERDAVRMMTCLGQALEYIHELGIVHRDVKLENLLIVKDEFGELGVKLADFGLAAEMPKDFGVLSTICGTPTYVAPEVLNKTGYGCKVDIWAAGVILYAILVGFPPFQSSDGSEQDLFSAIMSGEFSFPSPSWDDVSWSVRHLIMCLIHTDPFHRYSAGELLNDEWMVNLGDVDPEYEEWAHRFVQSKMHVEEEQETPYEYYTSRRTSMDELSESAAVEFSYSCES
Protein: Mediator of RNA polymerase II transcription subunit 27 (Cofactor required for Sp1 transcriptional activation subunit 8) (Mediator complex subunit 27) (A0A8I6AJL8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MADVLSVGVNLEAFSQAISAIQALRSSVSRVFDCLKDGMRNKETLEGREKAFIAHFQDNLHSVNRDLNELERLSNLVGKPSENHPLHNSGLLSLDPVQDKTPLYSQLLQAYKWSNKLQYHAGLASGLLNQQSLKRSANQMGVSAKRRPKAQPTTLVLPPQYVDDVISRIDRMFPEMSIHLSRPNGTSAVLLVTLGKVLKVIVVMRSLFIDRTIVKGYNESVYTEDGKLDIWSKSSYQVFQKVTDHATTALLHYQLPQMPDVVVRSFMETPFVSTLPWLPGSCLLL
Protein: P-type phospholipid transporter (EC 7.6.2.1) (Q9JK64)
Organism: Rattus norvegicus (Rat)
Subcellular location: Apical cell membrane {ECO:0000256|ARBA:ARBA00004221}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MELEEDLNGRADKNFSKMGKKSKKEKKEKKPAVSVLTMFRYAGWLDRFYMLLGTLAAIIHGIALPLMMLVFGDMTDSFANVGNNRSMSFYNATDIYAKLEDEMTTYAYYYTGIGAGVLIVAYIQVSLWCLAAGRQIHKIRQKFFHAIMNQEIGWFDVHDVGELNTRLTDDVSKINEGIGDKIGMFFQAMATFFGGFIIGFTRGWKLTLVILAISPVLGLSAGIWAKILSSFTDKELQAYAKAGAVAEEVLAAIRTVIAFGGQKKELERYNNNLEEAKRLGIKKAITANISMGAAFLLIYASYALAFWYGTSLVISKEYTIGQVLTVFFSVLIGAFSVGQASPNIEAFANARGAAYEVFSIIDNKPSIDSFSKSGHKPDNIQGNLEFKNIHFSYPSRKDVQILKGLNLKVKSGQTVALVGNSGCGKSTTVQLLQRLYDPIEGEVSIDGQDIRTINVRYLREIIGVVSQEPVLFATTIAENIRYGRENVTMDEIEKAVKEANAYDFIMKLPHKFDTLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEAVVQAALDKAREGRTTIVIAHRLSTVRNADVIAGFDGGVIVEQGNHDELMREKGIYFKLVMTQTAGNEIELGNEACESKDGIDNVDMSSKDSGSSLIRRRSTRKSIRGPHDQDGELSTKEALDDDVPPASFWRILKLNSTEWPYFVVGVFCAIINGGLQPAFSIIFSKVVGVFTKNDTPEIQRQNSNLFSLLFLILGIISFITFFLQGFTFGKAGEILTKRLRYMVFKSMLRQDISWFDDPKNTTGALTTRLANDAAQVKGATGSRLAVITQNIANLGTGIIISLIYGWQLTLLLLAIVPIIAIAGVVEMKMLSGQALKDKKELEGSGKIATEAIENFRTVVSLTREQKFETMYAQSLQIPYRNALKKAHVFGITFSFTQAMMYFSYAACFRFGAYLVARELMTFENVLLVFSAIVFGAMAVGQVSSFAPDYAKAKVSASHIIRIIEKIPEIDSYSTEGLKPNMLEGNVKFNGVMFNYPTRPNIPVLQGLSLEVKKGQTLALVGSSGCGKSTVVQLLERFYDPMAGTVFLDGKEIKQLNVQWLRAHLGIVSQEPILFDCSIAENIAYGDNSRVVSHEEIVKAAKEANIHQFIDSLPEKYNTRVGDKGTQLSGGQKQRIAIARALVRQPHILLLDEATSALDTESEKVVQEALDKAREGRTCIVIAHRLSTIQNADLIVVIQNGQVKEHGTHQQLLAQKGIYFSMVSVQAGAKRS
Protein: Ectoine dioxygenase (EC 1.14.11.55) (Ectoine hydroxylase) (Q1GNW5)
Organism: Sphingopyxis alaskensis (strain DSM 13593 / LMG 18877 / RB2256) (Sphingomonas alaskensis)
Function: Involved in the biosynthesis of 5-hydroxyectoine, called compatible solute, which helps organisms to survive extreme osmotic stress by acting as a highly soluble organic osmolyte. Catalyzes the 2-oxoglutarate-dependent selective hydroxylation of L-ectoine to yield (4S,5S)-5-hydroxyectoine.
Interaction partners:
- L-ectoine synthase
- Diaminobutyrate--2-oxoglutarate transaminase
- L-2,4-diaminobutyric acid acetyltransferase
- aspartate kinase
- General substrate transporter
- Major facilitator superfamily MFS_1
Sequence:
MQDLYPSRQRADAEMRPRLDPVVHSEWTNDAPISARQAAAFDRDGYIVLEDIFSADEVAFLQKAAGNLLADPAALDADTIVTEPQSNEIRSIFEIHAQSPVMARLAADARLADVARFLLGDEVYIHQSRLNYKPGFKGREFYWHSDFETWHVEDGMPRMRALSMSVLLAENTPHNGPLMVIPGSHRTYLTCVGETPDDHYLSSLKKQEYGVPDEESLAELAHRHGIVAPTGKPGTVILFDCNLMHGSNGNITPFPRANAFLVYNAVSNRLEKPFGVEKPRPWFLARRGEPAALRVERGPLVETVPA
Protein: Serine hydroxymethyltransferase 2, mitochondrial (AtSHMT2) (EC 2.1.2.1) (Glycine hydroxymethyltransferase 2) (Serine methylase 2) (Q94C74)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions outside the photorespiratory pathway in catalyzing the interconversion of serine and glycine with the conversion of tetrahydrofolate (THF) into 5,10-methylene-THF.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Formate--tetrahydrofolate ligase
- Phosphoserine phosphatase, chloroplastic
- Glycine dehydrogenase
- Glycine dehydrogenase
- Bifunctional dihydrofolate reductase-thymidylate synthase 1
- Bifunctional dihydrofolate reductase-thymidylate synthase 2
- AICARFT/IMPCHase bienzyme family protein
- Formyltetrahydrofolate deformylase 1, mitochondrial
- Aminomethyltransferase, mitochondrial
- Methylenetetrahydrofolate reductase 1
Sequence:
MALALRRLSSSVKKPISLLSSNGGSLRFMSSLSTAAMAESEKSRSSWIKQLNASLDEIDPEVADIIELEKARQWKGFELIPSENFTSLSVMQAVGSVMTNKYSEGYPGARYYGGNEYIDMAETLCQKRALEAFQLDPSKWGVNVQSLSGSPANFQVYTALLKPHERIMALDLPHGGHLSHGYQTDTKKISAVSIFFETMPYRLDENTGYIDYDQLEKSAVLFRPKLIVAGASAYARLYDYARIRKVCNKQKAVMLADMAHISGLVAAGVIPSPFEYADVVTTTTHKSLRGPRGAMIFFRKGLKEINKQGKEVMYDYEDRINQAVFPGLQGGPHNHTITGLAVALKQARTPEYKAYQDQVLRNCSKFAETLLAKGYDLVSGGTDNHLVLVNLKNKGIDGSRVEKVLELVHIAANKNTVPGDVSAMVPGGIRMGTPALTSRGFIEEDFAKVAEYFDLAVKIALKIKAESQGTKLKDFVATMQSNEKLQSEMSKLREMVEEYAKQFPTIGFEKETMRYKE
Protein: Octanoyltransferase LIP2, mitochondrial (EC 2.3.1.181) (Lipoate biosynthesis protein) (Lipoate-protein ligase) (Lipoyl ligase) (Lipoyl/octanoyl transferase) (Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase) (Q9SXP7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate (By similarity). Together with LIP1 is essential for mitochondrial protein lipoylation during seed development. Required for the lipoylation of mitochondrial 2-oxoglutarate dehydrogenase component E2 proteins in leaves and roots.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:24872381}.
Interaction partners:
- Lipoyl synthase, mitochondrial
- Lipoyl synthase, chloroplastic
- Octanoyltransferase LIP2p, chloroplastic
- Octanoyltransferase LIP2p2, chloroplastic
- 3-oxoacyl-[acyl-carrier-protein] synthase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase I, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, mitochondrial
- 3-oxoacyl-[acyl-carrier-protein] synthase II, chloroplastic
- Enoyl-[acyl-carrier-protein] reductase, chloroplastic
- Palmitoyl-acyl carrier protein thioesterase, chloroplastic
Sequence:
MRSPRTLEVWKLGTVNYLKSLKLQEKLVSERKAHQIPDTLLSLQHPPTYTLGKRRTDHNLLIPESELTKIGAELHYTQRGGDITFHGPHQAILYPIISLRSIGFGARNYVETLERSMIEFASIYGVKARAGNKCETGVWVGDRKIGAIGVRISSGITSHGLALNIDPDMKYFEHIVPCGIADKEVTSLRRETDTLLPSEEVIHEQLVSCLAKAFSYDDVVWKEDPSLILDTQDKE
Protein: Zinc finger protein ZIC 2 (Zinc finger protein of the cerebellum 2) (O95409)
Organism: Homo sapiens (Human)
Function: Acts as a transcriptional activator or repressor. Plays important roles in the early stage of organogenesis of the CNS. Activates the transcription of the serotonin transporter SERT in uncrossed ipsilateral retinal ganglion cells (iRGCs) to refine eye-specific projections in primary visual targets. Its transcriptional activity is repressed by MDFIC. Involved in the formation of the ipsilateral retinal projection at the optic chiasm midline. Drives the expression of EPHB1 on ipsilaterally projecting growth cones. Binds to the minimal GLI-consensus sequence 5'-TGGGTGGTC-3'. Associates to the basal SERT promoter region from ventrotemporal retinal segments of retinal embryos.
Subcellular location: Nucleus. Cytoplasm {ECO:0000250}. Note=Localizes in the cytoplasm in presence of MDFIC overexpression. Both phosphorylated and unphosphorylated forms are localized in the nucleus (By similarity). {ECO:0000250}.
Interaction partners:
- Homeobox protein SIX3
- Protein dispatched homolog 1
- Sonic hedgehog protein
- Ephrin type-B receptor 1
- Hepatocyte nuclear factor 3-beta
- Insulin gene enhancer protein ISL-2
- Growth arrest-specific protein 1
- Zinc finger protein ZIC 5
Sequence:
MLLDAGPQFPAIGVGSFARHHHHSAAAAAAAAAEMQDRELSLAAAQNGFVDSAAAHMGAFKLNPGAHELSPGQSSAFTSQGPGAYPGSAAAAAAAAALGPHAAHVGSYSGPPFNSTRDFLFRSRGFGDSAPGGGQHGLFGPGAGGLHHAHSDAQGHLLFPGLPEQHGPHGSQNVLNGQMRLGLPGEVFGRSEQYRQVASPRTDPYSAAQLHNQYGPMNMNMGMNMAAAAAHHHHHHHHHPGAFFRYMRQQCIKQELICKWIDPEQLSNPKKSCNKTFSTMHELVTHVSVEHVGGPEQSNHVCFWEECPREGKPFKAKYKLVNHIRVHTGEKPFPCPFPGCGKVFARSENLKIHKRTHTGEKPFQCEFEGCDRRFANSSDRKKHMHVHTSDKPYLCKMCDKSYTHPSSLRKHMKVHESSPQGSESSPAASSGYESSTPPGLVSPSAEPQSSSNLSPAAAAAAAAAAAAAAAVSAVHRGGGSGSGGAGGGSGGGSGSGGGGGGAGGGGGGSSGGGSGTAGGHSGLSSNFNEWYV
Protein: Kappa-actitoxin-Bcs3b (Kappa-AITX-Bcs3b) (Potassium channel toxin BcsTx2) (BcsTx2) (C0HJC3)
Organism: Bunodosoma caissarum (Sea anemone)
Function: Inhibits voltage-gated potassium channels (IC(50)=14.42 nM for rKCNA1/Kv1.1, IC(50)=80.4 nM for rKCNA2/Kv1.2, IC(50)=7.76 nM for rKCNA6/Kv1.6, IC(50)=13.12 nM for hKCNA3/Kv1.3, and IC(50)=49.14 nM for insect Shaker IR). Binds the Shaker IR channels in a voltage-independent manner.
Subcellular location: Secreted {ECO:0000269|PubMed:23466933}. Nematocyst {ECO:0000269|PubMed:23466933}.
Interaction partners:
Sequence:
ACKDGFPTATCQHAKLVGNCKNSQKYRANCAKTCGPC
Protein: Peroxiredoxin-6 (EC 1.11.1.27) (1-Cys peroxiredoxin) (1-Cys PRX) (24 kDa protein) (Acidic calcium-independent phospholipase A2) (aiPLA2) (EC 3.1.1.4) (Antioxidant protein 2) (Glutathione-dependent peroxiredoxin) (Liver 2D page spot 40) (Lysophosphatidylcholine acyltransferase 5) (LPC acyltransferase 5) (LPCAT-5) (Lyso-PC acyltransferase 5) (EC 2.3.1.23) (Non-selenium glutathione peroxidase) (NSGPx) (Red blood cells page spot 12) (P30041)
Organism: Homo sapiens (Human)
Function: Thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively. Can reduce H(2)O(2) and short chain organic, fatty acid, and phospholipid hydroperoxides. Also has phospholipase activity, can therefore either reduce the oxidized sn-2 fatty acyl group of phospholipids (peroxidase activity) or hydrolyze the sn-2 ester bond of phospholipids (phospholipase activity). These activities are dependent on binding to phospholipids at acidic pH and to oxidized phospholipds at cytosolic pH. Plays a role in cell protection against oxidative stress by detoxifying peroxides and in phospholipid homeostasis. Exhibits acyl-CoA-dependent lysophospholipid acyltransferase which mediates the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC). Shows a clear preference for LPC as the lysophospholipid and for palmitoyl CoA as the fatty acyl substrate.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16186110, ECO:0000269|PubMed:19188445, ECO:0000269|PubMed:9497358}. Lysosome {ECO:0000250|UniProtKB:O35244}. Note=Also found in lung secretory organelles (lamellar bodies). {ECO:0000250|UniProtKB:O35244}.
Interaction partners:
- Phospholipid hydroperoxide glutathione peroxidase GPX4
- Glutathione S-transferase P
- Probable glutathione peroxidase 8
- Glutathione peroxidase 7
- Glutathione peroxidase 2
- Epididymal secretory glutathione peroxidase
- Glutathione peroxidase 3
- Glutathione peroxidase 6
- Glutathione reductase, mitochondrial
- Glutathione S-transferase omega-1
Sequence:
MPGGLLLGDVAPNFEANTTVGRIRFHDFLGDSWGILFSHPRDFTPVCTTELGRAAKLAPEFAKRNVKLIALSIDSVEDHLAWSKDINAYNCEEPTEKLPFPIIDDRNRELAILLGMLDPAEKDEKGMPVTARVVFVFGPDKKLKLSILYPATTGRNFDEILRVVISLQLTAEKRVATPVDWKDGDSVMVLPTIPEEEAKKLFPKGVFTKELPSGKKYLRYTPQP
Protein: Metacaspase-2 (EC 3.4.22.-) (TbMCA2) [Cleaved into: Large subunit p20; Small subunit p10] (Q585F3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: Cysteine protease that cleaves specifically after arginine or lysine residues.
Subcellular location: Recycling endosome {ECO:0000250|UniProtKB:Q8T8E7}.
Interaction partners:
Sequence:
MCSLITQLCDAGQLADYVGLGWLNAVSSQPYLVQALGLQPPPRRVDVDAAFRDAKGLHGHQPWVATPLPGQTVRALFIGINYYGTSAALSGCCNDVKQMLATLQKKGLPINEAVILVDEDNFPGRTDQPTRDNIVRYMAWLVKDAKPGDVLFFHYSGHGTQCKSRGDSDEKYDQCIAPVDFQKSGCIVDDDIHKLLFSRLPEKVRLTAVFDCCHSGSIMDLPFTYVCSGGEQASGTPHMKRIREGNDVLGDVMMISGCADEQTSADVKNTATFGTGSTGAGGAATQCITCMLMNNQSLSYGKLLIETRDMLKRKGFKQVPQLSASKAIDLDQTFSLTEMFSVDRSIQ