wanglab/gogpt-training-data huggingface dataset:
Protein: Myb domain-containing protein (Q54VX6)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Transcriptional regulator
- Probable transcription-associated protein 1
- Transcription initiation factor TFIID subunit 9
- DUF1325 family protein
- Transcription initiation factor TFIID subunit 12
- Ubiquitin carboxyl-terminal hydrolase
- TATA-binding protein-associated-factor
- Transcription and mRNA export factor ENY2
- histone acetyltransferase
- UBP-type zinc finger-containing protein
Sequence:
MTSTINKEEPTTLVNKKRRKEHVDDDDDNDDDIEMQNVSNDNINNTDDENNNVNTNGNNTNKTNNNNNNNNNNNNNNNEEDDDEEDLLITKRRNSRSTTMSNNSSNKSTPSKKKRIKKSYDNDKDFVGDDEEEDDNDDEDDDGDVVISNNNNNNNNNNTNNNNNNNNGNGNGNNNTNNSFEEDDDEEDDDEEDEEEEEEGMKISKSKRQTQIIPPTQSEVDDLVNKSFNSVDDDEEDNEEDDKTKNTTTTTATNTTNVPTTTTTTTTTSNNTTLPTTTTTTTTNNTTKPNVKIEQPKTQQPPQPQPINKPTQSNTITTNTNTSTNTNTATNTNSNTATATTTSPTSMTKQTRKSTNSPTNSNGNNNNNNNNNNFIEEQVNEGLYHCDYCQKDISGVVRIRCSVCTDFDLCLECFSVGVEITPHRNFHDYHVVDNMHFPMFTDDWGADEELLLLEAIELYGLGNWNEVSENVGAHSKSPLECKAHYFAHYLNSSTSPLPDTSKVLTTNENVHFKRAKTTVNGNYYNDYIIDNSDDDDNNNNNNNYNDNSNNTTPTKSFNSVNKSKKLNHRNSHGEEGPSGPVTDSVGYMKNRGHFEVEYDNEAELVVKDLTFEPDDSQADRDIKLNVLESYDQRLDERIRRRNFIVEKGLLDYRKVERKRYKDDKEILNSLKCFLQTVTKEEHESMINGLINEKNIKNRILQLQEYRENGIKTLADGQNFDEDKRKREVDKSMKRSKSELASYSLNSGLSSYNPNHNPFGHHYLGGSSSGLSGGSGGGGGGGGDPSFKTQKQLTKEKEDIYLGIGENRKHHSSKLKKNAKMELEGLPNADALSLKEKQICTTHKLLPQQYLIVKQALISESLKTQGVIKLSTAFKLIKLNQVKIHRLLEFFERNHWLKFNIDCETNTSNTTSNYK
Protein: Mating-type M-specific polypeptide Mi (P0CY15)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Mating type proteins are sequence specific DNA-binding proteins that act as master switches in yeast differentiation by controlling gene expression in a cell type-specific fashion. Required for meiosis, but plays no role in conjugation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Meiosis inducing protein mei3
- Mating-type M-specific polypeptide Mc
Sequence:
MSAEDLFTIQILCDQIELKLASIVINSNIKLQLKRKKKTQQL
Protein: NRR repressor homolog 1 (Q6L589)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Binds to and represses NPR1/NH1-mediated transcriptional activation of LG2 in vitro.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q5ZEF1}.
Interaction partners:
Sequence:
MEGVDVKAPRPGCGGDDGGAAAASLSARREEEEEGAVVGGEDEQVERFYALLANIRALRGMYSRYNGEEGAAGGDGDGASGRKRARRAEPPWRPAFRMEDFEFEEAAAGAGDDDAACSGRTTKKQRSGGGGHGAAVEKRRTEKEAAAAAAEDDDDEQEGGEVVEGKEEHRPGRRVEAHGPTDQ
Protein: Eukaryotic translation initiation factor 6 (eIF-6) (Q12522)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit to form the 80S initiation complex in the cytoplasm. Is also involved in ribosome biogenesis. Associates with pre-60S subunits in the nucleus and is involved in its nuclear export. Cytoplasmic release of TIF6 from 60S subunits and nuclear relocalization is promoted by the GTPase RIA1/EFL1 and by SDO1. Also required for pre-rRNA processing.
Subcellular location: Cytoplasm. Nucleus, nucleolus. Note=Shuttles between cytoplasm and nucleus/nucleolus.
Interaction partners:
- Ribosome biogenesis protein YTM1
- Ribosome biogenesis protein RLP24
- Nucleolar GTP-binding protein 1
- Large ribosomal subunit protein uL18
- 27S pre-rRNA
- 60S ribosome subunit biogenesis protein NIP7
- Ribosome production factor 1
- Nucleolar GTP-binding protein 2
- 60S ribosomal export protein NMD3
- Nuclear GTP-binding protein NUG1
Sequence:
MATRTQFENSNEIGVFSKLTNTYCLVAVGGSENFYSAFEAELGDAIPIVHTTIAGTRIIGRMTAGNRRGLLVPTQTTDQELQHLRNSLPDSVKIQRVEERLSALGNVICCNDYVALVHPDIDRETEELISDVLGVEVFRQTISGNILVGSYCSLSNQGGLVHPQTSVQDQEELSSLLQVPLVAGTVNRGSSVVGAGMVVNDYLAVTGLDTTAPELSVIESIFRLQDAQPESISGNLRDTLIETYS
Protein: Putative general negative regulator of transcription C16C9.04c (Q09818)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May negatively regulate the basal and activated transcription of many genes.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- General negative regulator of transcription subunit 1
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- Poly
- Cell differentiation protein rcd1
- General negative regulator of transcription subunit 3
- General negative regulator of transcription subunit 2
- Putative ATP-dependent RNA helicase ste13
- Deadenylation-dependent mRNA-decapping factor pdc2
- Serine/threonine-protein kinase srb10
- Histone acetyltransferase gcn5
Sequence:
MLKTQEIYSSEDEDDMCCPLCMEEIDISDKNFKPCQCGYRVCRFCWHHIKEDLNGRCPACRRLYTEENVQWRPVTAEEWKMDLHRKNERKKREKERKEVELSNRKHLANIRVVQKNLAYVNGLSPKVANEENINVLKGPEYFGQYGKIIKIAINKKAAANSANGHVGVYITYQRKEDAARAIAAIDGSVSDGRHLRASYGTTKYCTSYLRNQQCPNPSCMYLHEPGDEVDSYTKEDLASLQHTRPLSTKPNVVNGATHSPSPSLPFKTPLLPVTKTPLEEANSSPAAQNQHITTVDHVHPQVSMTPSLSTNNTATSVPAPYSSAASVNVVPGHATTILHHEESSALPPTAAWAKLSPSVLQERLRAAVNQQPLDALKSSSTQTSIPKIQKLKAAKLPSEEENTTKWLNKAINDLVSSLSKINFSTEGTEFDKKQIEMIQNLPPLFVFNARSVIDKEVVPEQEKSAENQPPTSLGINNGNPVMPPPGFQS
Protein: Autophagy-related protein 8 (Autophagy-related ubiquitin-like modifier ATG8) (P0C075)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Ubiquitin-like modifier involved in autophagosomes formation. With ATG4, mediates the delivery of the autophagosomes to the vacuole via the microtubule cytoskeleton. Required for selective autophagic degradation of the nucleus (nucleophagy) as well as for mitophagy which contributes to regulate mitochondrial quantity and quality by eliminating the mitochondria to a basal level to fulfill cellular energy requirements and preventing excess ROS production. Participates also in membrane fusion events that take place in the early secretory pathway. Also involved in endoplasmic reticulum-specific autophagic process and is essential for the survival of cells subjected to severe ER stress. The ATG8-PE conjugate mediates tethering between adjacent membranes and stimulates membrane hemifusion, leading to expansion of the autophagosomal membrane during autophagy.
Subcellular location: Cytoplasmic vesicle, autophagosome membrane {ECO:0000269|PubMed:31284951}; Lipid-anchor {ECO:0000305|PubMed:31284951}. Vacuole membrane {ECO:0000269|PubMed:31284951}; Lipid-anchor {ECO:0000305|PubMed:31284951}.
Interaction partners:
- Serine/threonine-protein kinase ATG1
- Autophagy-related protein 3
- Ubiquitin-like modifier-activating enzyme ATG7
- Cysteine protease ATG4
- ZZ-type domain-containing protein
- Putative lipase ATG15
- Ubiquitin-like protein ATG12
- Autophagy protein 5
- Oxidant-induced cell-cycle arrest protein 5
- Beclin 1
Sequence:
MRSQFKDEHPFEKRQAEAARIAQRFKDRVPVICEKVENSDIPEIDKRKYLVPVDLTVGQFVYVIRKRIKLPSEKAIFIFVNDILPPTAALISTIYEEHKDEDGFLYVLYSGENTFGEKLAIDISSLDFSDIPDYV
Protein: Antimicrobial peptide 5 (PGLa-like peptide) (XT-5) (P84385)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Has very strong antimicrobial activity against Gram-positive bacterium S.aureus, Gram-negative bacterium E.coli and yeast C.albicans. Has strong hemolytic activity against human red blood cells.
Subcellular location: Secreted {ECO:0000269|PubMed:11738090}.
Interaction partners:
Sequence:
GMATKAGTALGKVAKAVIGAAL
Protein: Col4a5 protein (Q80V57)
Organism: Mus musculus (Mouse)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MGPDGPPGPPGFPGPKGEPGFGLPGPPGPPGFPGFKGTPGPKGDRGFPGPSGPPGPPGEKGKPGQDGIPGPAGQKGEPGQPGFGIPGPPGLPGLSGQKGDGGSPGLPGNPGLPGSKGEPGFQGFPGMPGPPGPPGSPGQALEGPKGNPGPQGPPGRPGPPGFQGPPGTEGPRGPPGNGGIKGERGNPGPPGQPGLPGLKGDQGPPGLPGNPGRPGLNGMKGDPGLPGVPGFPGMKGPIGVPGSTGPDGEPGLTGPPGPPGLPGPSGQSIVIKGDPGPPGIPGQPGLKGLPGLPGPQGLPGPIGPPGDPGRNGLPGFDGAGGRKGDPGLPGQPGARGLDGPPGPDGLQGPPGPPGTTSVAHGFLITRHSQTTEAPQCPRGTVHIYEGFSLLYVQGNKRAHGQDLGTAGSCLRRFSTMPFMFCNINNVCNFASRNDYSYWLSTPEPMPMNMEPLKGQSIQPFISRCAVCEAPAVVIAVHSQTIQIPHCPQGWDSLWIGYSFMMHTSAGAEGSGQALASPGSCLEEFRSAPFIECHGRGTCNYYANSYSFWLATVDMSDMFNKPQSETLKAGDLRTRISRCQVCMKRT
Protein: GPI-anchored protein LLG1 (LORELEI-like-GPI-anchored protein 1) (Q9FKT1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of the FER-regulated Rho GTPase signaling complex. Acts as a chaperone and coreceptor for FER. Required for localization of FER to the plasma membrane.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26052747}; Lipid-anchor, GPI-anchor {ECO:0000255, ECO:0000269|PubMed:26052747}.
Interaction partners:
- Rapid alkalinization factor 23
- Protein RALF-like 1
- Receptor-like protein kinase ANXUR1
- Ferritin-4, chloroplastic
- Brefeldin A-inhibited guanine nucleotide-exchange protein 5
- Rac-like GTP-binding protein ARAC4
- Receptor-like protein kinase THESEUS 1
- Receptor-like protein kinase ANXUR2
- BRASSINOSTEROID INSENSITIVE 1-associated receptor kinase 1
- Serine/threonine-protein kinase RIPK
Sequence:
MELLSRALFFFLLLSVLSSFSSSSFISDGVFESQSLVLGRNLLQTKKTCPVNFEFMNYTIITSKCKGPKYPPKECCGAFKDFACPYTDQLNDLSSDCATTMFSYINLYGKYPPGLFANQCKEGKEGLECPAGSQLPPETSAEVNAATTSSSRLWLTVSAALLVFVKLF
Protein: Xenoxin-1 (Q09022)
Organism: Xenopus laevis (African clawed frog)
Function: Lacks alpha-neurotoxic activity, has apparently no antibacterial activity, nor anti-coagulant potency.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MRYAIVFFLVCVITLGEALKCVNLQANGIKMTQECAKEDTKCLTLRSLKKTLKFCASGRTCTTMKIMSLPGEQITCCEGNMCNA
Protein: Putrescine aminotransferase (PAT) (PATase) (EC 2.6.1.82) (Cadaverine transaminase) (Diamine transaminase) (EC 2.6.1.29) (Putrescine transaminase) (Putrescine--2-oxoglutaric acid transaminase) (Putrescine:2-OG aminotransferase) (P42588)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the aminotransferase reaction from putrescine to 2-oxoglutarate, leading to glutamate and 4-aminobutanal, which spontaneously cyclizes to form 1-pyrroline. This is the first step in one of two pathways for putrescine degradation, where putrescine is converted into 4-aminobutanoate (gamma-aminobutyrate or GABA) via 4-aminobutanal, which allows E.coli to grow on putrescine as the sole nitrogen source. Also functions as a cadaverine transaminase in a a L-lysine degradation pathway to succinate that proceeds via cadaverine, glutarate and L-2-hydroxyglutarate. Is also able to transaminate spermidine, in lower extent, but not ornithine. Alpha-ketobutyrate and pyruvate can also act as amino acceptors, although much less efficiently.
Interaction partners:
- Gamma-aminobutyraldehyde dehydrogenase
- Constitutive lysine decarboxylase
- Gamma-glutamylputrescine synthetase PuuA
- Spermidine N
- Constitutive ornithine decarboxylase
- Polyamine aminopropyltransferase
- Agmatinase
- Inducible lysine decarboxylase
- Inducible ornithine decarboxylase
- ATP-dependent Clp protease adapter protein ClpS
Sequence:
MNRLPSSASALACSAHALNLIEKRTLDHEEMKALNREVIEYFKEHVNPGFLEYRKSVTAGGDYGAVEWQAGSLNTLVDTQGQEFIDCLGGFGIFNVGHRNPVVVSAVQNQLAKQPLHSQELLDPLRAMLAKTLAALTPGKLKYSFFCNSGTESVEAALKLAKAYQSPRGKFTFIATSGAFHGKSLGALSATAKSTFRKPFMPLLPGFRHVPFGNIEAMRTALNECKKTGDDVAAVILEPIQGEGGVILPPPGYLTAVRKLCDEFGALMILDEVQTGMGRTGKMFACEHENVQPDILCLAKALGGGVMPIGATIATEEVFSVLFDNPFLHTTTFGGNPLACAAALATINVLLEQNLPAQAEQKGDMLLDGFRQLAREYPDLVQEARGKGMLMAIEFVDNEIGYNFASEMFRQRVLVAGTLNNAKTIRIEPPLTLTIEQCELVIKAARKALAAMRVSVEEA
Protein: DNA replication protein 17 (Gene product 17) (gp17) (Protein p17) (P03686)
Organism: Bacillus phage phi29 (Bacteriophage phi-29)
Function: Involved in the replication of viral DNA. It is required at the very beginning of the virus amplification, conditions in which a low number of viral DNA molecules enter the host cell, possibly to recruit the limiting amount of initiation factors at the replication origins. Once the infection process is established and the other replication proteins reach optimal concentration, it becomes dispensable. Optimizes the binding of protein p6 at the viral DNA ends, thus favoring the initiation of replication.
Interaction partners:
Sequence:
MNNYQLTINEVIDIINTNTEINKLVAKKENLFPTDLYDLDKQELIAIILNSDFALSSIKRVLLEVTVEELGTQDNDEDDELEDLDGEIDRVDYIDKDGIRFDVPRETSPHVDKSIVTFNDELLDEANKIAKSIQEHDFNDKAIEEAELKIFKNHLPSIYSMKKENK
Protein: Testis-expressed protein 47 (Q8TBZ9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSFSVHNQKGSKRPLPLEPLLFLQVPRSNYLHFQEEKQRLHLKKFLLDRMFLVAKIQANVERKDVADYYEQMFQSVLKHHLGEAVTGLLLIYPTSILHILESSSDTLYKVLLDYIGHVKDETVFFIQQMKIIVISHNIPMRLFMQWHVSVIKVPVMYLDDVTQSQSLKEVITDFLTQTHKLSLYLCQTMKVGTKGPGDNLHQVAPDLLLPEQIIKYLCKSEEFMDPATFINMYNRPIHITLDSEVVWPAPSRF
Protein: FMN reductase (NADPH) (EC 1.5.1.38) (FMN reductase) (Sulfate starvation-induced protein 4) (SSI4) (P80644)
Organism: Escherichia coli (strain K12)
Function: Catalyzes an NADPH-dependent reduction of FMN, but is also able to reduce FAD or riboflavin.
Interaction partners:
- Putative aliphatic sulfonates-binding protein
- Alkanesulfonate monooxygenase
- Putative aliphatic sulfonates transport permease protein SsuC
- Aliphatic sulfonates import ATP-binding protein SsuB
- Alpha-ketoglutarate-dependent taurine dioxygenase
- Phosphoadenosine 5'-phosphosulfate reductase
- Sulfite reductase hemoprotein beta-component
- Sulfite reductase flavoprotein alpha-component
- Bifunctional riboflavin kinase/FMN adenylyltransferase
- 5-amino-6-
Sequence:
MRVITLAGSPRFPSRSSSLLEYAREKLNGLDVEVYHWNLQNFAPEDLLYARFDSPALKTFTEQLQQADGLIVATPVYKAAYSGALKTLLDLLPERALQGKVVLPLATGGTVAHLLAVDYALKPVLSALKAQEILHGVFADDSQVIDYHHRPQFTPNLQTRLDTALETFWQALHRRDVQVPDLLSLRGNAHA
Protein: CTD nuclear envelope phosphatase 1 homolog (EC 3.1.3.16) (Serine/threonine-protein phosphatase dullard homolog) (Q9VRG7)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine/threonine protein phosphatase that may dephosphorylate and activate lipin-like phosphatases. Lipins are phosphatidate phosphatases that catalyze the conversion of phosphatidic acid to diacylglycerol and control the metabolism of fatty acids at different levels. May indirectly modulate the lipid composition of nuclear and/or endoplasmic reticulum membranes and be required for proper nuclear membrane morphology and/or dynamics. May also indirectly regulate the production of lipid droplets and triacylglycerol (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Nuclear envelope phosphatase-regulatory subunit 1 homolog
- Transmembrane protein 188
- phosphatidate phosphatase
- Transcription factor Dp
- Chromosomal protein D1
Sequence:
MISLLQMKFRALLLLLSKVWTCICFMFNRQVRAFIQYQPVKYELFPLSPVSRHRLSLVQRKTLVLDLDETLIHSHHNAMPRNTVKPGTPHDFTVKVTIDRNPVRFFVHKRPHVDYFLDVVSQWYDLVVFTASMEIYGAAVADKLDNGRNILRRRYYRQHCTPDYGSYTKDLSAICSDLNRIFIIDNSPGAYRCFPNNAIPIKSWFSDPMDTALLSLLPMLDALRFTNDVRSVLSRNLHLHRLW
Protein: Histidine N-acetyltransferase (EC 2.3.1.33) (I3J7Q8)
Organism: Oreochromis niloticus (Nile tilapia) (Tilapia nilotica)
Function: Enzyme responsible for the N-acetyl-histidine (NAH) synthesis, which is a major constituent of brain and lens of ectothermic vertebrates.
Interaction partners:
Sequence:
MKIDTSLNMPQLPEALSQAGLQFSVATEEDFDEIMAMSQDIYGGLDYLPTRYTSWLQDTNRTVILARKHGKVIALESVCVIDDGETMLVEGLRVAPQERGKGVAGVLLRFCAELVKSRYPEVKVCRLTRDDQLGPKDFEKYRIITKQGILLMRFRAEDLKLHLSEFGLEGDNESTLSTFCSSPPPVRLDHTAIQQLYLNSDLLHGVLPNATIIQDWQPFKLLPSNMAILLKKEIDWMVDDMSNPTVASLCTFPFRVPIGDDWYYLNIDMFGKDLALARQQFLYHLQRHTATLKGHVMCQMFLDPPLWKAMAEFCHNTLSVELVKEYTEQCVVECDLI
Protein: Large ribosomal subunit protein eL28 (60S ribosomal protein L28) (P41105)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:36517592}.
Interaction partners:
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein eS10
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein eL22
- Large ribosomal subunit protein eL19
Sequence:
MSAHLQWMVVRNCSSFLIKRNKQTYSTEPNNLKARNSFRYNGLIHRKTVGVEPAADGKGVVVVMKRRSGQRKPATSYVRTTINKNARATLSSIRHMIRKNKYRPDLRMAAIRRASAILRSQKPVVVKRKRTRPTKSS
Protein: DNA repair protein RecO (Recombination protein O) (P42095)
Organism: Bacillus subtilis (strain 168)
Function: Plays a role in DNA double-stranded break repair. It seems to be involved in an RecBC-independent recombinational process of DNA repair. It may act with RecF and RecR. Is recruited to repair centers, foci that are the site of double-strand break(s) after RecN and before RecF; may actively recruit RecF.
Subcellular location: Cytoplasm, nucleoid {ECO:0000269|PubMed:15186413, ECO:0000269|PubMed:21170359}. Note=Cytoplasmically located in untreated cells. Recruited to foci following treatment with DNA damaging agents; these foci are presumably the breaks themselves. They are almost always located within nucleoids (PubMed:15186413). Another study found it localizes in tight foci on the nucleoid with active replication forks; targeted via the 6 C-terminal residues of SSB (ssbA) (PubMed:21170359). {ECO:0000269|PubMed:15186413, ECO:0000269|PubMed:21170359}.
Interaction partners:
- Recombination protein RecR
- DNA replication and repair protein RecF
- Single-stranded-DNA-specific exonuclease RecJ
- Regulatory protein RecX
- Protein RecA
- Single-stranded DNA-binding protein A
- DNA repair protein RecN
- Probable ATP-dependent DNA helicase RecS
- Holliday junction resolvase RecU
- ATP-dependent DNA helicase RecG
Sequence:
MLTKCEGIVLRTNDYGETNKIVTLLTREHGKIGVMARGAKKPNSRLSAVSQPFLYGSFLMQKTSGLGTLQQGEMILSMRGIREDLFLTAYAAYVAELVDRGTEEKKPNPYLFEFILESLKQLNEGTDPDVITFIVQMKMLGVMGLYPELNHCVHCKSQDGTFHFSVRDNGFICHRCFEKDPYRIPIKPQTARLLRLFYYFDLSRLGNVSLKEETKAELKQVIDLYYEEYSGLYLKSKRFLDQMESMKHLMGENKS
Protein: FYN proto-oncogene, Src family tyrosine kinase (E5RFS5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MGCVQCKDKEATKLTEERDGSLNQSSGYRYGTDPTPQHYPSFGVTSIPNYNNFHAAGGQGLTVFGGVNSSSHTGTLRTRGGTGVTLFVALYDYEARTEDDLSFHKGEKFQILNSSEGDWWEARSLTTGETGYIPSNYVAPVDSIQAEEWYFGKLGRKDAERQLLSFGNPRGTFLIRESETTKGAYSLSIRDWDDMKGDHVKHYKIRKLDNGGYYITTRAQFETLQQLVQHYS
Protein: Apoptosis regulatory protein Siva (CD27-binding protein) (CD27BP) (O54926)
Organism: Mus musculus (Mouse)
Function: Induces CD27-mediated apoptosis. Inhibits BCL2L1 isoform Bcl-x(L) anti-apoptotic activity. Inhibits activation of NF-kappa-B and promotes T-cell receptor-mediated apoptosis (By similarity).
Subcellular location: Cytoplasm. Nucleus {ECO:0000250}. Note=In the nucleus, accumulates in dot-like structures. {ECO:0000250}.
Interaction partners:
- Bcl-2-like protein 1
- Apoptosis regulator Bcl-2
- CD27 antigen
Sequence:
MPKRSCPFADAAPLQLKVHVGLKELSHGVFAERYSREVFERTKQLLFQGARAYRDHISSEDCSVNHLQESLKSGVVGAPQPARGQMLIGPDGRLTRCQAQASEGGLPRTAPIACSSCMRSVDGKAVCSQCERALCGQCVYTCWGCGALACVLCGLADYADDGEKTLCTSCAMFEA
Protein: Acyl-protein thioesterase 1 (APT-1) (EC 3.1.2.-) (Lysophospholipase 1) (Lysophospholipase I) (LPL-I) (LysoPLA I) (Palmitoyl-protein hydrolase) (EC 3.1.2.22) (P97823)
Organism: Mus musculus (Mouse)
Function: Acts as a acyl-protein thioesterase hydrolyzing fatty acids from S-acylated cysteine residues in proteins such as trimeric G alpha proteins or HRAS (By similarity). Has depalmitoylating activity toward KCNMA1 (By similarity). Could also depalmitoylate ADRB2 (By similarity). Acts as a lysophospholipase hydrolyzing various lysophospholipids including lysophosphatidylcholine (lyso-PC), lysophosphatidylethanolamine (lyso-PE), lysophosphatidylinositol (lyso-PI) and lysophosphatidylserine (lyso-PS). Has much higher thioesterase activity than lysophospholipase activity (By similarity). Contributes to the production of lysophosphatidic acid (LPA) during blood coagulation by recognizing and cleaving plasma phospholipids to generate lysophospholipids which in turn act as substrates for ENPP2 to produce LPA (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O75608}. Cell membrane {ECO:0000250|UniProtKB:O75608}. Nucleus membrane {ECO:0000250|UniProtKB:O75608}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O75608}. Note=Shows predominantly a cytoplasmic localization with a weak expression in the cell membrane, nuclear membrane and endoplasmic reticulum. {ECO:0000250|UniProtKB:O75608}.
Interaction partners:
- Glycerophosphocholine phosphodiesterase GPCPD1
- Phospholipase B1, membrane-associated
- Lysosomal phospholipase A and acyltransferase
- Lysophospholipid acyltransferase 5
- Phosphatidylcholine-sterol acyltransferase
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Patatin-like phospholipase domain-containing protein 6
- Lysophospholipid acyltransferase LPCAT4
- Patatin-like phospholipase domain-containing protein 7
- Membrane-bound glycerophospholipid O-acyltransferase 1
Sequence:
MCGNNMSAPMPAVVPAARKATAAVIFLHGLGDTGHGWAEAFAGIKSPHIKYICPHAPVMPVTLNMNMAMPSWFDIVGLSPDSQEDESGIKQAAETVKALIDQEVKNGIPSNRIILGGFSQGGALSLYTALTTQQKLAGVTALSCWLPLRASFSQGPINSANRDISVLQCHGDCDPLVPLMFGSLTVERLKALINPANVTFKIYEGMMHSSCQQEMMDVKHFIDKLLPPID
Protein: C2H2-type zinc finger-containing protein (Q54ZS5)
Organism: Dictyostelium discoideum (Social amoeba)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 1
- DEAD/DEAH box helicase
- RNA helicase
- Initiation factor eIF-4 gamma middle domain-containing protein
- NKAP family protein
- Peptidyl-prolyl cis-trans isomerase cypE
- peptidylprolyl isomerase
- RING-type E3 ubiquitin transferase
- Pre-mRNA-splicing factor 18
Sequence:
MEQEEAVDEFGRPLRPNRDSSSDSDSDRDYDNRYRKRRDDSRERDYERYSPDRYSRRGDHSPERRRRSPSPYRGRGRGRDDWDGGNNNNNNNNNNNNNNNNNNNNNNNNISSSNNSNGYRGNRNGFPSSMVVDNNSNNNINNNNINNNNNNNNENNNNNTNGMTTSTSTSISSPSTIPSGSAKGLIGGPKRAQKRGDIFEGGYFRSYKQFLDYQDDSITPIEADKKYEEYKIEYSKRQSRVFFKEHQQEEWFKEKYDPFFLAKKRKEKVEKSKSFIQTFALNLNDENHKFSLESKDNIKEGDKLDLDGLDMHHHHHPHINNEDNSNNINNTSTTTNNTNNTTTITTTSATGEEVSESSSSSSSSSSSSSSSSSSSSSSTTTETEEKSNNNNTNNNNNSNTNNNNNNNISTSITSINKSNINDKEKSTLFIKAVSPTCTKEELLEVLNKVGNGEICVTKLTLSEPVRYKNFYRLGWVTFKNAELASKALKELNGHKMRDFDLYLNINKPSEDAERRFKITPNIASTENRITIDLEQSTTLMKLFDENKGITNNPINSFEKWDSLTNIERLDRTILYLRYVHFYCYYCSEEFSDECETTRKCGTIHLRRTQGEQTSIINNNNNINNNNTAIQSSSSSSSSSITTSTTATTTTKTTENNKEEQEEEQDKIKEDKEEEEDKIQEDKPEKVEEENQDKIKEDKPEKVDEDKEMEDDETTTKTTTTNNTTSATTTTTTTSMEIDNKQPKLTTESEMLWVTSLDNNTKNKINKIPTSEEQYTCKESIEKAAEEYIATNTIKIEEEKFKCSLCSKLFRGAEFVKKHINLKHPEDLQKESEAKGTEEQFFLNYFSDPRRITPLPPQSQNQNQMVFGGYGPSAPGGTGLGRGGHPPGTATQMLTPRTRFNPAIGQWETVVVPMIIPGMIPNQGMVQIMSPVFASPNNMRGRPGGANGTATGGGGGGSGNGGPIPPHMVGGPVPMRRSYGGPTGNLSPNSSSNGGGSGGRYGSGPPGMDGGPPQSMRYRPYPTQPSRHSTSSMDPRGIREYVDLDAPIDHVPEIDYRSALKEYQNKKSL
Protein: Olfactory receptor 7D4 (OR19-B) (Odorant receptor family subfamily D member 4RT) (Olfactory receptor OR19-7) (Q8NG98)
Organism: Homo sapiens (Human)
Function: Odorant receptor. Selectively activated by androstenone and the related odorous steroid androstadienone.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MEAENLTELSKFLLLGLSDDPELQPVLFGLFLSMYLVTVLGNLLIILAVSSDSHLHTPMYFFLSNLSFVDICFISTTVPKMLVSIQARSKDISYMGCLTQVYFLMMFAGMDTFLLAVMAYDRFVAICHPLHYTVIMNPCLCGLLVLASWFIIFWFSLVHILLMKRLTFSTGTEIPHFFCEPAQVLKVACSNTLLNNIVLYVATALLGVFPVAGILFSYSQIVSSLMGMSSTKGKYKAFSTCGSHLCVVSLFYGTGLGVYLSSAVTHSSQSSSTASVMYAMVTPMLNPFIYSLRNKDVKGALERLLSRADSCP