wanglab/gogpt-training-data huggingface dataset:
Protein: ESAT-6-like protein EsxH (10 kDa antigen CFP7) (CFP-7) (Low molecular weight protein antigen 7) (Protein TB10.4) (P9WNK3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: EsxH, in complex with EsxG, disrupts ESCRT function and impairs host phagosome maturation, thereby promoting intracellular bacterial growth. The complex acts by interacting, via EsxH, with the host hepatocyte growth factor-regulated tyrosine kinase substrate (HGS/HRS), a component of the ESCRT machinery.
Subcellular location: Secreted {ECO:0000269|PubMed:24204276}. Note=Secreted via the ESX-3 / type VII secretion system (T7SS). {ECO:0000305|PubMed:21730061, ECO:0000305|PubMed:24204276}.
Interaction partners:
- ESAT-6-like protein EsxG
- ESX-3 secretion-associated protein EspG3
- ESAT-6-like protein EsxB
- 6 kDa early secretory antigenic target
- PPE family protein PPE4
- ESAT-6-like protein EsxS
- Diacylglycerol acyltransferase/mycolyltransferase Ag85B
- ESX-3 secretion system protein EccD3
- Diacylglycerol acyltransferase/mycolyltransferase Ag85A
- PE family immunomodulator PE5
Sequence:
MSQIMYNYPAMLGHAGDMAGYAGTLQSLGAEIAVEQAALQSAWQGDTGITYQAWQAQWNQAMEDLVRAYHAMSSTHEANTMAMMARDTAEAAKWGG
Protein: Protein no-on-transient A (Puff-specific protein Bj6) (Q04047)
Organism: Drosophila melanogaster (Fruit fly)
Function: Required for normal vision and courtship behavior in Drosophila.
Interaction partners:
- Phosphatidylinositol glycan anchor biosynthesis class Q, isoform B
- LD31543p
- Heterogeneous nuclear ribonucleoprotein 87F
- Zinc finger protein on ecdysone puffs
Sequence:
MESAGKQDNNATQQLPQRQQRGNQQANKNLGKHNAQKQNDSADGGPAEKKQRFGGPNAQNQNQNQNQNGGVTGGGGAVGGPNQNKNFGNNKGGFVGNRNRNNNRAGNQNRTFPGNNNPNQKPNNETSKADGPNALAKNNEPATAAAGQNQANQNANKGQNQRQGQNQNQNQVHGQGNQGGPGNQGGAGNQGGQGNQGGAGNQGNGQGFRGRNAGNNQGGGFSGGPQNQQRDNRNRSGPRPGGGAGGAMNSTNMGGGGGGGGGGGPRGGEDFFITQRLRSISGPTFELEPVEVPTETKFSGRNRLYVGNLTNDITDDELREMFKPYGEISEIFSNLDKNFTFLKVDYHPNAEKAKRALDGSMRKGRQLRVRFAPNATILRVSNLTPFVSNELLYKSFEIFGPIERASITVDDRGKHMGEGIVEFAKKSSASACLRMCNEKCFFLTASLRPCLVDPMEVNDDTDGLPEKAFNKKMPDFNQERSIGPRFADPNSFEHEYGSRWKQLHNLFKTKQDALKRELKMEEDKLEAQMEYARYEQETELLRQELRKREVDNERKKLEWEMREKQAEEMRKREEETMRRHQTEMQSHMNRQEEDMLRRQQETLFMKAQQLNSLLDQQEGFGGGGGGNNSTFDNFAGNSNSPFEVFRGNNNNNSTMIGNNAAPNTQDSFAFEFGVNNMNQGGNQRGNNGGGNNVPWGRRRF
Protein: Transcription elongation factor 1 (P36053)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Transcription elongation factor implicated in the maintenance of proper chromatin structure in actively transcribed regions.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Transcription elongation factor SPT5
- Transcription elongation factor SPT4
- DNA-directed RNA polymerase II subunit RPB1
- Cell division control protein 73
- DNA-directed RNA polymerase II subunit RPB2
- DNA-directed RNA polymerase II subunit RPB3
- FACT complex subunit POB3
- RNA polymerase-associated protein LEO1
- FACT complex subunit SPT16
- DNA-directed RNA polymerase II subunit RPB4
Sequence:
MGKRKKSTRKPTKRLVQKLDTKFNCLFCNHEKSVSCTLDKKNSIGTLSCKICGQSFQTRINSLSQPVDVYSDWFDAVEEVNSGRGSDTDDGDEGSDSDYESDSEQDAKTQNDGEIDSDEEEVDSDEERIGQVKRGRGALVDSDDE
Protein: Guanylate-binding protein 7 (EC 3.6.1.-) (EC 3.6.5.-) (GTP-binding protein 7) (GBP-7) (Guanine nucleotide-binding protein 7) (Guanylate-binding protein 4-like) (Q91Z40)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes GTP to GMP in two consecutive cleavage reactions and predominantly uses GTP and not GDP or GMP as the substrate. Confers protection to several pathogens, including the bacterial pathogens Listeria monocytogenes and Mycobacterium bovis BCG as well as the protozoan pathogen Toxoplasma gondii. Promotes IFN-gamma-mediated host defense against bacterial infections by regulating oxidative responses and bacteriolytic peptide generation. May help to assemble NADPH oxidase on phagosomal membranes by acting as a bridging protein between NADPH oxidase cytosolic subunits NCF2-NCF4 and the membrane subunits CYBA-CYBB. Participates along with GBP1 in trafficking monoubiquinated protein cargo to autolysosomes for generating ubiquitin-derived antimicrobial peptides. Required for disruption of the parasitophorous vacuole formed following T.gondii infection and subsequent killing of the parasite. Facilitates influenza A virus replication by inhibiting the activation of NF-kappaB and JAK-STAT signaling pathways and the expression of type I, type III interferons and pro-inflammatory cytokines (By similarity).
Subcellular location: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:18025219, ECO:0000269|PubMed:21551061, ECO:0000269|PubMed:31689351, ECO:0000269|PubMed:31964735}.
Interaction partners:
- Interferon-inducible GTPase 1
- Immunity-related GTPase family M protein 3
- Guanylate-binding protein 3
- Immunity-related GTPase family M protein 1
- Interferon-induced protein 44
- Cysteine protease ATG4B
- Immunity-related GTPase family M protein 2
- Neutrophil cytosol factor 2
- E3 ISG15--protein ligase Herc6
- GTP-binding protein
Sequence:
MASGPNMEAPVCLVENENEELRVNSKAINILERITQPVVVVAIVGLYRTGKSYLMNRLAGQNHGFNLGTTVRSETKGIWMWCVPHPSKPKFTLVLLDTEGLGDVEKGDPKNDSWIFALAVLLSSTFVYNSMSTINHQALEQLHYVTELTERIRAKSTSRSEEVDDSDEFVSFFPDFIWTVRDFVLELKLEGRVITADEYLENALKLIPGMSIKAQKANLPRECIRHFFPRRKCFVFDRPTKDKELLVHVEEMPEDQLDHSFQVQSKEFCSYIFSNSKAKTLKEGIVVNGNRLATLVTTYVDAINSGDVPCLENAVTTLAQRENSIAVQKAADHYSEQMAQRMRLPTDTLQELLTVHTACEKEAIAVFMEHSFKDENQQFQKNLVVTIEEKKEDFLRQNEAASLSHCQAELDKLSESLRESISRGVFSVPGGHRLYLEARKKVEQDYERVPRKGVKANHVLQSFLQSQISIEDSIMQSDKALTDGQKAMEAERAQKEAAEKEQELLRQKQKELQQVMEAQERSYKENVAQLHEKMETERKNILREQEVKLEHKLKIQKDMLNEGFKRKCEAMDLEISQLQKEIQLNKEKNSSLGAKILDGFGDVLISVVPGSGKYFGLGLKILSSQMNQTQNSDKVRKL
Protein: Brefeldin A-inhibited guanine nucleotide-exchange protein 4 (BIG4) (ARF guanine-nucleotide exchange factor BIG4) (F4JN05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Activates the ARF proteins by exchanging bound GDP for free GTP. Plays a role in vesicular protein sorting (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Soluble and partially membrane-bound. {ECO:0000250}.
Interaction partners:
- ADP-ribosylation factor
- ADP-ribosylation factor 2-B
- ADP-ribosylation factor 1
- Coatomer subunit gamma
- V-type proton ATPase subunit a1
- Rop guanine nucleotide exchange factor 11
- Floral homeotic protein APETALA 1
Sequence:
MSTSQTLGGATRCGRIIGPSLDKIIKNAAWRKHTYLVSSCKSVLDKLESLPDDFHDPSSVVSGLAASDADSVLQPFLLSLETAYSKVVEPSLDCAFKLFSLSILRGEIQSSKQDSILFKLVNAVSKVGAIAEEPIQLAVLRVLLAAVRSPCILIRGDCLLHVVKTCYNIYLGGLSGTTQICAKSVLAQMMLVIFTRSEEDSLDVSVKTIYVNELLTFTDKSVNEGSSVYFCQGFVNEVMAAGQGSPLPPPDVIQILLQNPETETVMTPDSPSFRGYVANGEGDSETGDMSKVRQDAFLLFKNLCKLSMRFSSKENNDDQIMVRGKTLSLELLKVIIDNGGSVWRTNESFINAVKQYLCLSLLKNSAVSIMSIFQLQCAIFMSLLSKLRSVLKAEIGIFFPMIVLRVLENVLQPSYLQKMTVLNLLDKMSQDPQLMVDIFVNYDCDVESSNILERIVNGLLKTALGPPTGSSTTLSPAQDSTFRNDSVKCLVNLAKAMGNWMDQQLKVNETVWPKGSQVYASMDSNASQISELEGTISDCDSQPDTSNPEAYDASMLEQRRAYKIELQKGISLFNRKPSKGVEFLISTKKIGSSPEEVASFLMKTAGLNGTVIGDYLGERDELPLKVMHAYVDSFNFEKKDFVEAIRFFLRGFRLPGEAQKIDRIMEKFAEHYWKCNPGSFTSADTAYVLAYSVIMLNTDAHNNMVKDKMTKADFVRNNRGIDDGKDLPEEYLGSLYDRVVKEEIRMNSDTLAPQNKQVNGLNKLLGLDGILNLVSWMQPDEKPHGANGRLIRDIQEQFQAKPEKSESVYHTVTDISILRFILEVSWGPMLAAFSVTIDQSDDRLATSLCLQGFRYAVHVTAVMGMQTQRDAFVTSMAKFTNLHCAADMKQKNVDAVKAIITIAIEDGNHLHGSWEHILTCLSRIEHLQLLGEVSPSEKRYVPTKKAEVDDKKALGFPNLKKRGSFQNPSVMAVVRGGSYDSTSLVKSVPKLVTPEQIKSFIANLNLLDQIGNFELNHVYANSQRLNSEAIVSFVKALCKVSMSELQSPTDPRVFSLTKLVETAHYNMNRIRLVWSRIWNVLSDFFVSVGLSENLSVAIFVMDSLRQLSMKFLEREELANYHFQHEFLRPFVVVMQKSSSAEIRELIVRCVSQMVLSRVSNVKSGWKNVFTVFTTAALDERKNIVLLAFETIEKIVRDHFHCIIETEITVYADCIRCLITFTNSKFEGDIGFNTIEFLRFCALKLEEGGLVLNEKLKNNTISALKEDFSDTQSFTDLDEQVSYWIPLLTGLCKQVSDPRPAIRKRSIEVLFHILMDHGHLFTRPFWTGIFSSIILPVFNNIRSKTDMLFEESVDSPSSASLDTEETTWDVETSTLALQLLVDLLVKFFRSVRSQLPSVVSIIVGFIKSPFQGSTGSGISVLLHLADGLARSASEDEWREIFLALKEAASLTFAGFMKVLRTMDDIEDVETLSGQSVNIGDLDDDSLHIMSYVVSRTKKHIDVLSQIVEVVSDLYRRNQFSLSASHVDILADIFSCIASHAQQLNTDTVLRRKFKRACSVQNLTEPQLLNFENEAYKSYMMFLQDMVTCNPNVSKELDLESRLVTECAKIVKIYLKCTDPQQQEQQQRKPVLWVLPMESDRVEEATARTSLLVSSLEALCSLEAESLKKHVSSFFPLLVDLVRTEHCSPQVPYVLSNVLKSCIGPILA
Protein: Bearded (GEO11750p1) (RT02933p) (O16528)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Enhancer of split m4 protein
- Protein neuralized
- BARBU
- Enhancer of split mgamma protein
- Achaete-scute complex protein T3
- Enhancer of split mdelta protein
- Brother of bearded A
- Enhancer of split m5 protein
- Brother of Bearded protein A
- GEO09613p1
Sequence:
MAYETLMNTTIYTTTPVCQKKTYTPAKAMKKIFKVACKIFKASGHQQLKNHSMPKELPLPTSEEELQNSQNEQLEAELVQL
Protein: Dihydropyrimidinase (DHP) (DHPase) (EC 3.5.2.2) (Dihydropyrimidine amidohydrolase) (Hydantoinase) (Q63150)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the second step of the reductive pyrimidine degradation, the reversible hydrolytic ring opening of dihydropyrimidines. Can catalyze the ring opening of 5,6-dihydrouracil to N-carbamyl-alanine and of 5,6-dihydrothymine to N-carbamyl-amino isobutyrate.
Interaction partners:
- Dihydropyrimidine dehydrogenase [NADP
- Beta-ureidopropionase
- Uridine monophosphate synthetase, isoform CRA_a.
- Dihydroorotate dehydrogenase
- Carbamoyl-phosphate synthase, mitochondrial
Sequence:
MAPQERLLIRGGRVVNDDFSQVADVLVEDGVVRALGRDLLPPGDTSRGLRILDAAGKLVLPGGIDTHTHMQFPFMGSQSVDDFHQGTKAALAGGTTMIIDFAIPQKGSSLIEAFETWRNWADPKVCCDYSLHVAVTWWSDKVKEEMKTLAQDKGVNSFKMFMAYKDLYMVQDQQMYAAFSQCKEIGAIAQVHAENGDLIAEGAKKMLALGITGPEGHELCRPEAVEAEATLRAITIASAVNCPLYIVHVMSKSAAKVIADAKREGKVVYGEPIAAGLGTDGTQYWNKEWRHAAHHVMGPPLRPDPSTPGFLMNLLANGDLTTTGSDNCTFNTCQKALGKDDFTKIPNGVNGVEDRMSVIWEKGVHSGKMDENRFVAVTSTNAAKIFNLYPKKGRIAVGSDADIVIWDPEATRTISAKTHHQAVNFNIFEGMVCHGVPLVTISRGRVVYEAGVFDVTAGHGKFIPRQPFAEFIYKRVKQRDQTCTPIPVKRAPYKGEVITLKPRETKEDDTAGTRMQGHS
Protein: Ret finger protein-like 3 (O75679)
Organism: Homo sapiens (Human)
Function: (Microbial infection) Stimulates the activity of Human Immunodeficiency Virus 1/HIV-1 pre-integration complex.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25107902}. Nucleus {ECO:0000269|PubMed:25107902}. Note=A higher concentration of RFPL3 is observed in the cytoplasm compared to the nucleus. {ECO:0000269|PubMed:25107902}.
Interaction partners:
- Ret finger protein-like 2
Sequence:
MKRLSLVTTNRLSPQGNFLPLCTFPLAVDMAALFQEASSCPVCSDYLEKPMSLECGCTVCLKCINSLQKEPHGEDLLCCCCSMVSQRNKIRPNRQLERLVSHIKELEPKLKKILQMNPRMRKFQVDMTLDADTANNFLLISDDLRSVRSGLITQNRQDLAERFDVSVCILGSPRFTCGRHYWEVDVGTSTEWDLGVCRESVHCKGKIQLTTELGFWTVSLRDGSRLSASTVPLTFLLVDRKLQRVGIFLDMGMQNVSFFDAESGSHVYTFRSVSAEEPLRPFLAPSIPPNGDQGVLSICPLMNSGTTDAPVRPGEAK
Protein: Uricase (EC 1.7.3.3) (Urate oxidase) (O74409)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin.
Subcellular location: Peroxisome {ECO:0000250}. Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable 5-hydroxyisourate hydrolase
- Probable allantoicase
- Alpha-ketoglutarate-dependent xanthine dioxygenase xan1
- Ureidoglycolate lyase
- Urease
- Inosine-5'-monophosphate dehydrogenase
- Probable guanine deaminase
- Adenine phosphoribosyltransferase
- Putative purine permease C1399.01c
- Uncharacterized deaminase C1683.02
Sequence:
MSETTYVKQCAYGKTLVRFMKKDICPKTKTHTVYEMDVQSLLTGELEESYTKADNSIVVPTDTQKNTIYVFAKNNDVSVPEVFAAKLAKHFVDKYKHIHGAALDITITPWTRMEVQGKPHSHSFIRNPGETRKTHVVFSEGKGFDVVSSLKDVLVLKSTGSGFTNFHKCEFTTLPEVTDRIFSTSIDCNYTFKHFDTFEELAGFDFNSIYEKVKEITLETFALDDSESVQATMYKMADTIINTYPAINEVYYALPNKHYFEINLAPFNIDNLGSNCSLYQPQAYPSGYITCTVARK
Protein: Inactive dipeptidyl peptidase 10 (Dipeptidyl peptidase X) (DPP X) (Q6NXK7)
Organism: Mus musculus (Mouse)
Function: Promotes cell surface expression of the potassium channel KCND2. Modulates the activity and gating characteristics of the potassium channel KCND2. Has no dipeptidyl aminopeptidase activity (Probable).
Subcellular location: Cell membrane {ECO:0000269|PubMed:22311982}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- A-type voltage-gated potassium channel KCND2
- A-type voltage-gated potassium channel KCND3
- IgLON family member 5
- Voltage-gated potassium channel KCNC1
- Potassium voltage-gated channel subfamily A member 4
- Leucine-rich glioma-inactivated protein 1
- Calsenilin
- A-type potassium channel modulatory protein KCNIP1
- Contactin-associated protein-like 2
- Zinc finger protein 11
Sequence:
MKQEQQPTPGARATQSQPADQELGSNSPPQRNWKGIAIALLVILVVCSLITMSVILLTPDELTNSSETRLSLEELLGKGFGLHNPEPRWINDTVVVYKTNNGHVMKLNTESNASTLLLDNSTFVTFKASRHSLSPDLKYVLLAYDVKQIFHYSFTASYLIYNIHTGEVWELNPPEVEDSVLQYAAWGVQGQQLIYIFENNIYYQPDIKSSSLRLTSSGKEGIIFNGIADWLYEEELLHSHIAHWWSPDGERLAFLMINDSLVPNMIIPRFTGALYPKAKQYPYPKAGQANPSVKLYVVNLYGPTHTLELMPPDIFKSREYYITMVKWVSNTRTVVRWLNRPQNISILTLCESTTGACSRKYEMTSDTWLSKQNEEPVFSRDGSKFFMTVPVKQGGRGEFHHIAMFLVQSKSEQITVRHLTSGNWEVIRILAYDETTQKIYFLSTESSPQGRQLYSASTEGLLNRDCISCNFMKEDCTYFDASFSPMNQHFLLFCEGPKVPVVSLHITDNPSRYFLLENNSVMKETIQKKKLAKRETRILHIDDYELPLQLSFPKDFMEKNQYALLLIMDEEPGGQMVTDKFHVDWDSVLIDTDNVIVARFDGRGSGFQGLKVLQEIHRRIGSVEAKDQVAAVKYLLKQPYIDSKRLSIFGKGYGGYIASMILKSDEKFFKCGAVVAPISDMKLYASAFSERYLGMPSKEESTYQASSVLHNIHGLKEENLLIIHGTADTKVHFQHSAELIKHLIKAGVNYTLQVYPDEGYHISDKSKHHFYSTILRFFSDCLKEEVSVLPQEPEEDE
Protein: Vid27p (A0A1D8PP94)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- tRNA
Sequence:
MNFIKKFIGTTTTDEVASIPSGKLYLTRSKQSPKGAIECLYNDAFASIKKTTSPYYYQLCITKVYQEGEADFNRFDDSEEEYDGEESAPTNDTRRQSKDEWIFPIADELKIHVCEKEDGSRAIAWKDVNGDLGDKFEFVIDEEVRGSEVEAFGMTIYKCLFENKYQTSYAKVNDPNQLKEFIYNPKGELLTFDELKDLNDLEEYETDEYEDCETLPIDAPKGETKYASTDVDLHLYDTRTGTFILHLAKPDFELKLIDLGNWEYTLYIHGETTRINTTLSKNMNPTFNYQHLSFIFNDYTVDEGGINACSWLVKFPDYNDMSKFQTVFLGLMYETLNRRKWGETEEHDYFVDAFSRVSIGDAKDLESEEEEESEEENEGDGPVKWETEKNEKNSSLTVGYAKDRSYVVRGDKIGVFSEDDAGQLNFQTAIINVADLKGKHFSPEKMLLHQQDQYMIISNPQFDDKALYKMDLTRGKIVEEWEVSKDVPVKSYAPTSKFAQLTDEQTLTGISSNGLFTIDPRLSGTKLVNDKTYKAYKTTNNQFQTLATTDKGYIALGSGKGDIRLFDRLGANAKTALPSLGDPIIGIDVSKDGRWLLATCKTYLLLIDNKISDGQKNAGKLGFTNYFDKDKKPTPRRLALKPEHEAYMVRENGGKQLSFTPAYFNTGRDSKETTIVTSLGKYVVTWSMGKVLLDKENPYLVKRYTQNVIADNFKFGSNNEVIMALQDDVSMVSRRSLANPKNVFK
Protein: Ribonucleotide reductase catalytic subunit M1 (E9PL69)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCSLENRDECLMCGS
Protein: Apoptosis regulator Bcl-2 (O02718)
Organism: Bos taurus (Bovine)
Function: Suppresses apoptosis in a variety of cell systems including factor-dependent lymphohematopoietic and neural cells. Regulates cell death by controlling the mitochondrial membrane permeability. Appears to function in a feedback loop system with caspases. Inhibits caspase activity either by preventing the release of cytochrome c from the mitochondria and/or by binding to the apoptosis-activating factor (APAF-1). Also acts as an inhibitor of autophagy: interacts with BECN1 and AMBRA1 during non-starvation conditions and inhibits their autophagy function. May attenuate inflammation by impairing NLRP1-inflammasome activation, hence CASP1 activation and IL1B release.
Subcellular location: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P10415}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P10417}.
Interaction partners:
- Beclin-1
- BCL2/adenovirus E1B 19 kDa protein-interacting protein 3
- Cellular tumor antigen p53
- Beclin 2
- BCL2 binding component 3
- BH3-interacting domain death agonist
- Cytochrome c
- Cytochrome c 2
- Bcl-2 homologous antagonist/killer
- BCL2 associated agonist of cell death
Sequence:
MAHAGGTGYDNREIVMKYIHYKLSQRGYEWDAGDAGAAPPGAAPAPGILSSQPGRTPAPSRTSPPPPPAAAAGPAPSPVPPVVHLTLRQAGDDFSRRYRRDFAEMSSQLHLTPFTARERFATVVEELFRDGVNWGRIVAFFEFGGVMCVESVNREMSPLVDSIALWMTEYLNRHLHTWIQDNGGWDAFVELYGPSMRPLFDFSWLSLKALLSLALVGACITLGAYLGHK
Protein: 14-3-3-like protein GF14-D (G-box factor 14-3-3 homolog D) (Q2R2W2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Is associated with a DNA binding complex that binds to the G box, a well-characterized cis-acting DNA regulatory element found in plant genes.
Interaction partners:
- HECT-type E3 ubiquitin transferase
- Os03g0311300 protein
- Arsenate reductase 2.1
- F-box domain containing protein
- Os12g0463700 protein
- F-box domain containing protein, expressed
- Arsenate reductase 2.2
- Serine/threonine-protein phosphatase PP2A-3 catalytic subunit
- Os05g0483801 protein
- Serine/threonine-protein phosphatase PP2A-1 catalytic subunit
Sequence:
MSPAEPTREESVYKAKLAEQAERYEEMVEYMERVARAAGGASGGEELTVEERNLLSVAYKNVIGARRASWRIISSIEQKEEGRGNDAHAATIRSYRGKIEAELARICDGILALLDSHLVPSAGAAESKVFYLKMKGDYHRYLAEFKSGDERKQAAESTMNAYKAAQDIALADLAPTHPIRLGLALNFSVFYYEILNSPDRACNLAKQAFDEAISELDSLGEESYKDSTLIMQLLRDNLTLWTSDANDDGGDEIKEAAAPKEPGDQ
Protein: Costars domain-containing protein (B3WFX8)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MEQNVATQSKDDVYSKDFTQKKMDKSSSEYGRPKPGTLTEQRAKKAAAHVHREMLTLCEVVEDYGKQEKEGDPIRITFGRLFTIYVNISDKVVGTLLRARKHKMIDFEGEMLFQKRDDHVIITLLLSGAQLKEAIRAHAAANPKE
Protein: L-tyrosine decarboxylase (A8MQJ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MFKPQHMYDREFGTGNGYSNGNGYTNGNGHTNGNGNYNGNGHVNGNGKANGAKVVKMKPMDSELLREQGHIMVDFIADYYKNLQDSPQDFPVLSQVQPGYLRDMLPDSAPERPESLKELLDDVSKKIMPGITHWQSPSYFAYYASSTSVAGFLGEMLNAGLSVVGFTWLTSPAATELEIIVLDWLAKLLQLPDHFLSTGNGGGVIQGTGCEAVLVVVLAARDRILKKVGKTLLPQLVVYGSDQTHSSFRKACLIGGIHEENIRLLKTDSSTNYGMPPESLEEAISHDLAKGFIPFFICATVGTTSSAAVDPLVPLGNIAKKYGIWLHVDAAYAGNACICPEYRKFIDGIENADSFNMNAHKWLFANQTCSPLWVKDRYSLIDALKTNPEYLEFKVKVSKKDTVVNYKDWQISLSRRFRSLKLWMVLRLYGSENLRNFIRDHVNLAKHFEDYVAQDPSFEVVTTRYFSLVCFRLAPVDGDEDQCNERNRELLAAVNSTGKIFISHTALSGKFVLRFAVGAPLTEEKHVTEAWQIIQKHASKFTRNDHY
Protein: CDP-diacylglycerol--inositol 3-phosphatidyltransferase (EC 2.7.8.11) (Phosphatidylinositol synthase) (PI synthase) (PtdIns synthase) (P70500)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the biosynthesis of phosphatidylinositol (PtdIns) as well as PtdIns:inositol exchange reaction. May thus act to reduce an excessive cellular PtdIns content. The exchange activity is due to the reverse reaction of PtdIns synthase and is dependent on CMP, which is tightly bound to the enzyme.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:3032971}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:3032971}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Phosphatidate cytidylyltransferase 1
- Phosphatidylinositol 4-kinase beta
- Phosphatidate cytidylyltransferase 2
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphatidylinositol 4-kinase alpha
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol 4-kinase type 2-alpha
- Cardiolipin synthase
- Inositol monophosphatase 2
Sequence:
MPEENIFLFVPNLIGYARIVFAIISFYFMPCCPFTASSFYLLSGLLDAFDGHAARALNQGTRFGAMLDMLTDRCATMCLLVNLALLYPRATLLFQLSMSLDVASHWLHLHSSVVRGSESHKMIDLSGNPVLRIYYTSRPALFTLCAGNELFYCLLYLFNFSEGPLVGSVGLFRMGLWITAPIALLKSIISVIHLVTAARNMAALDAADRAKKK
Protein: Serum amyloid P-component (SAP) (9.5S alpha-1-glycoprotein) [Cleaved into: Serum amyloid P-component(1-203)] (P02743)
Organism: Homo sapiens (Human)
Function: Can interact with DNA and histones and may scavenge nuclear material released from damaged circulating cells. May also function as a calcium-dependent lectin.
Subcellular location: Secreted.
Interaction partners:
- Low affinity immunoglobulin gamma Fc region receptor II-a
- Transthyretin
- Apolipoprotein E
- Serum amyloid A-1 protein
- C-reactive protein
- Fibronectin
- Ceramide transfer protein
- Amyloid-beta precursor protein
- Apolipoprotein A-I
- Serum amyloid A-2 protein
Sequence:
MNKPLLWISVLTSLLEAFAHTDLSGKVFVFPRESVTDHVNLITPLEKPLQNFTLCFRAYSDLSRAYSLFSYNTQGRDNELLVYKERVGEYSLYIGRHKVTSKVIEKFPAPVHICVSWESSSGIAEFWINGTPLVKKGLRQGYFVEAQPKIVLGQEQDSYGGKFDRSQSFVGEIGDLYMWDSVLPPENILSAYQGTPLPANILDWQALNYEIRGYVIIKPLVWV
Protein: AT11025p (Farinelli) (Q9VSD3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004211}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004211}.
Interaction partners:
- Oxysterol-binding protein
- Steroidogenic acute regulatory protein-like
- GEO12122p1
- Cytochrome c oxidase subunit 4
- Phosphatidylinositol 4-kinase alpha
Sequence:
MSDNTESKLALDPCDVIVFEGPFNRSVSRKLVIKNTSKTQRMAFKMKTTTPKLFYVRPNIGVLGPEQKVSVDIFMQPILQEQIKKRHKFLLLAAEVTGDISDVQEFWKMQNPNETRETKIKCELVPSKEDDFRQAGGSAVISTDNKDGEVHFDAQEVSEPMAKLLKQVSMLEDEHMALTDQIDGLRDQAIGRTFFYMAAIVIIILSAVAGAYYGKTRL
Protein: Lethal(2)neighbour of tid protein (NOT45) (NOT56) (Q27333)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Alpha-1,2-mannosyltransferase Alg9
- Dol-P-Man:Man
- Dolichol-phosphate mannosyltransferase subunit 1
- Probable dolichyl pyrophosphate Man9GlcNAc2 alpha-1,3-glucosyltransferase
- Dolichyl-phosphate beta-glucosyltransferase
- Insulin receptor substrate 53 kDa, isoform A
- GDP-Man:Man
- Dolichol phosphate-mannose biosynthesis regulatory protein
- GPI mannosyltransferase 1
- Dolichol-phosphate mannosyltransferase subunit 3
Sequence:
MAPPKAASHRPAVRRKKSGTLVDSILDKYLNVRFFKYLLLEPAALPIVGLFVLLAELVINVVVIQRVPYTEIDWVAYMQECEGFLNGTTNYSLLRGDTGPLVYPAAFVYIYSALYYVTSHGTNVRLAQYIFAGIYLLQLALVLRLYSKSRKVPPYVLVLSAFTSYRIHSIYVLRLFNDPVAVLLLYAALNLFLDRRWTLGSTFFSLAVGVKMNILLFAPALLLFYLANLGLLRTILQLAVCGVIQLLLGAPFLLTHPVEYLRGSFDLGRIFEHKWTVNYRFLSRDVFENRTFHVSLLGLHLLLLLAFAKPIWTFFQSYVRLRRIEDQLQPQITQQNLQLKAQKRPKKVEKDKDKDQKKFTTEQQSFLKAFEKSLQKASGGKATPAPAQAEPERYGIHFDRCTQLALLPFFLCNLVGVACSRSLHYQFYVWYFHSLPYLAWSTPYSLGVRCLILGLIEYCWNTYPSTNFSSAALHFTHIILLAGVAKQLIQTMRINNAAKREQQEQQKKLQ