wanglab/gogpt-training-data huggingface dataset:
Protein: Exosome complex component RRP4 (Exosome component 2) (Ribosomal RNA-processing protein 4) (Q13868)
Organism: Homo sapiens (Human)
Function: Non-catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and promoter-upstream transcripts (PROMPTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The RNA exosome may be involved in Ig class switch recombination (CSR) and/or Ig variable region somatic hypermutation (SHM) by targeting AICDA deamination activity to transcribed dsDNA substrates. In the cytoplasm, the RNA exosome complex is involved in general mRNA turnover and specifically degrades inherently unstable mRNAs containing AU-rich elements (AREs) within their 3' untranslated regions, and in RNA surveillance pathways, preventing translation of aberrant mRNAs. It seems to be involved in degradation of histone mRNA. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. EXOSC2 as peripheral part of the Exo-9 complex stabilizes the hexameric ring of RNase PH-domain subunits through contacts with EXOSC4 and EXOSC7.
Subcellular location: Cytoplasm. Nucleus, nucleolus. Nucleus.
Interaction partners:
- Exosome complex exonuclease RRP44
- Exosome complex component RRP45
- Exosome complex component 10
- Exosome complex component CSL4
- Nuclear nucleic acid-binding protein C1D
- Exosome complex component RRP40
- DIS3-like exonuclease 1
- Exosome complex component RRP42
- Exosome complex component RRP41
- Exosome complex component RRP43
Sequence:
MAMEMRLPVARKPLSERLGRDTKKHLVVPGDTITTDTGFMRGHGTYMGEEKLIASVAGSVERVNKLICVKALKTRYIGEVGDIVVGRITEVQQKRWKVETNSRLDSVLLLSSMNLPGGELRRRSAEDELAMRGFLQEGDLISAEVQAVFSDGAVSLHTRSLKYGKLGQGVLVQVSPSLVKRQKTHFHDLPCGASVILGNNGFIWIYPTPEHKEEEAGGFIANLEPVSLADREVISRLRNCIISLVTQRMMLYDTSILYCYEASLPHQIKDILKPEIMEEIVMETRQRLLEQEG
Protein: FMRFamide-related peptides [Cleaved into: FMRFamide A; Corticotropin-releasing factor-like; AAMDRY-amide; DPKQDFMRF-amide; TPAEDFMRF-amide; SDNFMRF-amide; SPKQDFMRF-amide; PDNFMRF-amide; SAPQDFVRS-amide; MDSNFIRF-amide] (P10552)
Organism: Drosophila melanogaster (Fruit fly)
Function: In insects, FMRFamide and related peptides have modulatory actions at skeletal neuromuscular junctions, and peptides that are immunologically related to FMRFamide are released into the circulation from neurohemal organs.
Subcellular location: Secreted.
Interaction partners:
- Short neuropeptide F
- Neuropeptide-like 1
- Cardioactive peptide
- Eclosion hormone
- Protein dimmed
- Protein PDF
- Neuropeptide F
- Neuropeptide SIFamide
- Zinc finger protein squeeze
Sequence:
MGIALMFLLALYQMQSAIHSEIIDTPNYAGNSLQDADSEVSPSQDNDLVDALLGNDQTERAELEFRHPISVIGIDYSKNAVVLHFQKHGRKPRYKYDPELEAKRRSVQDNFMHFGKRQAEQLPPEGSYAGSDELEGMAKRAAMDRYGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRDPKQDFMRFGRTPAEDFMRFGRTPAEDFMRFGRSDNFMRFGRSPHEELRSPKQDFMRFGRPDNFMRFGRSAPQDFVRSGKMDSNFIRFGKSLKPAAPESKPVKSNQGNPGERSPVDKAMTELFKKQELQDQQVKNGAQATTTQDGSVEQDQFFGQ
Protein: Expression site-associated gene (ESAG) protein, putative (Q57YD6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
Sequence:
MRFWFVLLALLGKETRANYYERNALNATAANKVCELSTYLKGVAHRVNSGSAAVMKKLSDLKIKSAQLQLSVMRNSVPSSEKDCKDIRTLLKTVLKNEFTFQQELEEMRNASALAAAAAGLAAGRLEEWIFAFAQAARTTSQFCISVGGSRPAVHDKLQECFRGTIGPETLYKIEDSHVTKSAEKNLQLHEALSSISFSSLGAESIIERNEDRGCNLMRTATDGLLKGGSLSHSFTWGGGVMNFASSVEGKLNVKGGEYGDVTSYGAVRWTEDPNKVSIFGDVIRLFARFEEAKNAVMEKIKTTADELTKCIGHKEAELTNDQLHERQFKAIQNYLELL
Protein: ATP synthase, delta subunit, isoform A (ATP synthase, delta subunit, isoform B) (ATP synthase, delta subunit, isoform C) (RE24457p) (Q9W2X6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004273}.
Interaction partners:
- ATP synthase-coupling factor 6, mitochondrial
- Protein stunted
- ATP synthase subunit beta, mitochondrial
- ATPase protein 9
- ATP synthase subunit g
- ATP synthase F
- ATP synthase subunit O, mitochondrial
- Putative ATP synthase subunit f
- ATP synthase subunit alpha, mitochondrial
- ATP synthase subunit a
Sequence:
MSFVKNARLLAARGARLAQNRSYSDEMKLTFAAANKTFYDAAVVRQIDVPSFSGSFGILAKHVPTLAVLKPGVVQVVENDGKTLKFFVSSGSVTVNEDSSVQVLAEEAHNIEDIDANEARQLLAKYQSQLSSAGDDKAKAQAAIAVEVAEALVKAAE
Protein: Alpha-tubulin (O48873)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
GDVVPKDVNAAVASIKTKRTIQFVDWCPTGFKCGINYQPPTVVPGGDLAKVQRAVCMISNSTSVAEVFSRIDHKFDLMYAKRAFIHWYVGEGMEE
Protein: Probable serine/threonine-protein kinase PBL22 (EC 2.7.11.1) (PBS1-like protein 22) (Q9SFX0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in plant defense signaling.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O48814}; Lipid-anchor {ECO:0000250|UniProtKB:O48814}.
Interaction partners:
Sequence:
MRCFSCLNTQTNDMRINIDTLSDLTDYASVATKIDPRGTGSKSGILVNGKVNSPKPGGGARSFTFKELAAATKNFREGNIIGKGGFGSVYKGRLDSGQVVAIKQLNPDGHQGNQEFIVEVCMLSVFHHPNLVTLIGYCTSGAQRLLVYEYMPMGSLEDHLFDLEPDQTPLSWYTRMKIAVGAARGIEYLHCKISPSVIYRDLKSANILLDKEFSVKLSDFGLAKVGPVGNRTHVSTRVMGTYGYCAPEYAMSGRLTIKSDIYSFGVVLLELISGRKAIDLSKPNGEQYLVAWARPYLKDPKKFGLLVDPLLRGKFSKRCLNYAISITEMCLNDEANHRPKIGDVVVAFEYIASQSKSYEDRRTARKSTDSNRLRRETKQSY
Protein: E3 ubiquitin-protein ligase ARIH2 (ARI-2) (Protein ariadne-2 homolog) (EC 2.3.2.31) (Triad1 protein) (UbcM4-interacting protein 48) (Q9Z1K6)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 UBE2L3 (By similarity). Acts as an atypical E3 ubiquitin-protein ligase by working together with cullin-5-RING ubiquitin ligase complex (ECS complex, also named CRL5 complex) and initiating ubiquitination of ECS substrates: associates with ECS complex and specifically mediates addition of the first ubiquitin on ECS targets (By similarity). The initial ubiquitin is then elongated (By similarity). E3 ubiquitin-protein ligase activity is activated upon binding to neddylated form of the ECS complex. Mediates 'Lys-6', 'Lys-48'- and 'Lys-63'-linked polyubiquitination. May play a role in myelopoiesis (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O95376}. Cytoplasm {ECO:0000250|UniProtKB:O95376}.
Interaction partners:
- Cullin-5
- RING-box protein 2
- Elongin-B
- Elongin-C
- E3 ubiquitin-protein ligase RBX1
- Ubiquitin-like protein NEDD8
- RING-box protein 2
- Ubiquitin-conjugating enzyme E2 L3
- Ankyrin repeat domain-containing protein 9
- Kelch domain-containing protein 1
Sequence:
MSVDMNSQGSDSNEEDYDPNCEEEEEEEEDPGDIEDYYVGVASDVEQQGADAFDPEEYQFTCLTYKESEGALHEHMTSLASVLKVSHSVAKLILVNFHWQVSEILDRYRSNSAQLLVEARVQPNPSKHVPTAHPPHHCAVCMQFVRKENLLSLACQHQFCRSCWEQHCSVLVKDGVGVGISCMAQDCPLRTPEDFVFPLLPNEELRDKYRRYLFRDYVESHFQLQLCPGADCPMVIRVQEPRARRVQCNRCSEVFCFKCRQMYHAPTDCATIRKWLTKCADDSETANYISAHTKDCPKCNICIEKNGGCNHMQCSKCKHDFCWMCLGDWKTHGSEYYECSRYKENPDIVNQSQQAQAREALKKYLFYFERWENHNKSLQLEAQTYERIHEKIQERVMNNLGTWIDWQYLQNAAKLLAKCRYTLQYTYPYAYYMESGPRKKLFEYQQAQLEAEIENLSWKVERADSYDRGDLENQMHIAEQRRRTLLKDFHDT
Protein: DNA mismatch repair protein MSH3 (Mismatch-binding protein) (MBP) (MutS protein homolog 3) (P25336)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS beta, which binds to DNA mismatches thereby initiating DNA repair. MSH3 provides substrate-binding and substrate specificity to the complex. When bound, the MutS beta heterodimer bends the DNA helix and shields approximately 20 base pairs. Acts mainly to repair insertion-deletion loops (IDLs) from 2 to 13 nucleotides in size, but can also repair base-base and single insertion-deletion mismatches that occur during replication. After mismatch binding, forms a ternary complex with either the MutL alpha or MutL beta heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. MutS beta also has a role in regulation of heteroduplex formation during mitotic and meiotic recombination. MutS beta binds to DNA flap structures predicted to form during recombination, and is required for 3' non-homologous tail removal (NHTR). MutS beta-binding alters the DNA conformation of its substrate at the ds/ssDNA junction and may facilitate its recognition and/or cleavage by the downstream nucleotide excision repair (NER) RAD1-RAD10 endonuclease. ATP binding and hydrolysis play a pivotal role in MMR and NHTR.
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DNA mismatch repair protein MSH2
- DNA mismatch repair protein MLH1
- DNA mismatch repair protein PMS1
- DNA mismatch repair protein MSH6
- DNA mismatch repair protein MLH3
- DNA repair protein RAD10
- DNA repair protein RAD1
- Exodeoxyribonuclease 1
- DNA mismatch repair protein MLH2
- DNA mismatch repair protein MSH1, mitochondrial
Sequence:
MAGQPTISRFFKKAVKSELTHKQEQEVAVGNGAGSESICLDTDEEDNLSSVASTTVTNDSFPLKGSVSSKNSKNSEKTSGTSTTFNDIDFAKKLDRIMKRRSDENVEAEDDEEEGEEDFVKKKARKSPTAKLTPLDKQVKDLKMHHRDKVLVIRVGYKYKCFAEDAVTVSRILHIKLVPGKLTIDESNPQDCNHRQFAYCSFPDVRLNVHLERLVHHNLKVAVVEQAETSAIKKHDPGASKSSVFERKISNVFTKATFGVNSTFVLRGKRILGDTNSIWALSRDVHQGKVAKYSLISVNLNNGEVVYDEFEEPNLADEKLQIRIKYLQPIEVLVNTDDLPLHVAKFFKDISCPLIHKQEYDLEDHVVQAIKVMNEKIQLSPSLIRLVSKLYSHMVEYNNEQVMLIPSIYSPFASKIHMLLDPNSLQSLDIFTHDGGKGSLFWLLDHTRTSFGLRMLREWILKPLVDVHQIEERLDAIECITSEINNSIFFESLNQMLNHTPDLLRTLNRIMYGTTSRKEVYFYLKQITSFVDHFKMHQSYLSEHFKSSDGRIGKQSPLLFRLFSELNELLSTTQLPHFLTMINVSAVMEKNSDKQVMDFFNLNNYDCSEGIIKIQRESESVRSQLKEELAEIRKYLKRPYLNFRDEVDYLIEVKNSQIKDLPDDWIKVNNTKMVSRFTTPRTQKLTQKLEYYKDLLIRESELQYKEFLNKITAEYTELRKITLNLAQYDCILSLAATSCNVNYVRPTFVNGQQAIIAKNARNPIIESLDVHYVPNDIMMSPENGKINIITGPNMGGKSSYIRQVALLTIMAQIGSFVPAEEIRLSIFENVLTRIGAHDDIINGDSTFKVEMLDILHILKNCNKRSLLLLDEVGRGTGTHDGIAISYALIKYFSELSDCPLILFTTHFPMLGEIKSPLIRNYHMDYVEEQKTGEDWMSVIFLYKLKKGLTYNSYGMNVAKLARLDKDIINRAFSISEELRKESINEDALKLFSSLKRILKSDNITATDKLAKLLSLDIH
Protein: Receptor-type tyrosine-protein phosphatase alpha (Protein-tyrosine phosphatase alpha) (R-PTP-alpha) (EC 3.1.3.48) (Q03348)
Organism: Rattus norvegicus (Rat)
Function: Tyrosine protein phosphatase which is involved in integrin-mediated focal adhesion formation (By similarity). Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GTPase RAC1 and CDC42 (By similarity).
Subcellular location: Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P18052}. Note=Localizes to focal adhesion sites following integrin engagement. {ECO:0000250|UniProtKB:P18052}.
Interaction partners:
- Tyrosine-protein kinase Fyn
- Growth factor receptor-bound protein 2
- 6-pyruvoyl tetrahydrobiopterin synthase
- Proto-oncogene tyrosine-protein kinase Src
- Focal adhesion kinase 1
- Neural cell adhesion molecule 1
- RING finger protein 37
Sequence:
MDSWFILILFGSGLIHISANNTTTVSPSLGTTRLIKTSTTESAKEENKTSNSTSSVISLSVTPTFSPNLTLEPTYVTTVNSSHSDNGTKRAASTESGGTTISPNGTYGTWLTDNQFTDARTEPWEGNSSSAATTPETFPPADETPIIAVMVALSSLLVILFIIIVLYMLRFKKYKQAGSHSNSFRLSNGRTEDVEPQSVPLLARSPSTNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNLLPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEETVNDFWRMIWEQNTATIVMVTNLKERKECKCAQYWPDQGCWPYGNVRVSVEDVTVLVDYTVRKFCIQQVGDVTNRKPQRLITQFHFTSWPDFGVPFTPIGMLKFLKKVKACNPQYAGAIVVHCSAGVGRTGTFVVIDAMLDMMHSERKVDVYGFVSRIRAQRCQMVQTDMQYVFIYQALLEHYLYGDTELEVTSLDTHLQKIYNKIPGTSNNGLEEEFKKLTSIKIQNDKMRTGYLPANMKKNRVLQIIPYEFNRVIIPVKRGEENTDYVNASFIDPYRQKDSYIASQGPLLHTTEDFWRMIWEWKSCSIVMLTELEERGQEKCAQYWPSDGLVSYGDITVELKKEEECESYTVRDLLVTNTRENKSRQIRQFHFHGWPEVGIPSDGKGMINIIAAVQKQQQQSGNHPITVHCSAGAGRTGTFCALSTVLECVKAEGILDVFQTVKTLRLQRPHMVQILEQYEFCYKVVQEYIDAFSDYANFK
Protein: Galectin-3 (Gal-3) (35 kDa lectin) (Carbohydrate-binding protein 35) (CBP 35) (Galactose-specific lectin 3) (Galactoside-binding protein) (GALBP) (IgE-binding protein) (L-31) (Laminin-binding protein) (Lectin L-29) (Mac-2 antigen) (P17931)
Organism: Homo sapiens (Human)
Function: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis (By similarity). In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocytes macrophages, opsonization of apoptotic neutrophils, and activation of mast cells. Together with TRIM16, coordinates the recognition of membrane damage with mobilization of the core autophagy regulators ATG16L1 and BECN1 in response to damaged endomembranes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32272059}. Nucleus. Secreted {ECO:0000269|PubMed:32272059}. Note=Secreted by a non-classical secretory pathway and associates with the cell surface. Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059). {ECO:0000269|PubMed:32272059}.
Interaction partners:
- Galectin-3-binding protein
- Mucin-1
- C-type lectin domain family 7 member A
- Tripartite motif-containing protein 16
- Low affinity immunoglobulin gamma Fc region receptor II-b
- Lymphocyte activation gene 3 protein
- Fibronectin
- Elastin
- Receptor-type tyrosine-protein phosphatase C
- Platelet glycoprotein VI
Sequence:
MADNFSLHDALSGSGNPNPQGWPGAWGNQPAGAGGYPGASYPGAYPGQAPPGAYPGQAPPGAYPGAPGAYPGAPAPGVYPGPPSGPGAYPSSGQPSATGAYPATGPYGAPAGPLIVPYNLPLPGGVVPRMLITILGTVKPNANRIALDFQRGNDVAFHFNPRFNENNRRVIVCNTKLDNNWGREERQSVFPFESGKPFKIQVLVEPDHFKVAVNDAHLLQYNHRVKKLNEISKLGISGDIDLTSASYTMI
Protein: Chorismate synthase (Q56YR0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- S-adenosyl-L-methionine-dependent methyltransferases superfamily protein
- AT-hook motif nuclear-localized protein 20
- Protein REVEILLE 5
- Serrate RNA effector molecule
- Eukaryotic translation initiation factor 4E-1
- Eukaryotic translation initiation factor isoform 4E
- Probable glucomannan 4-beta-mannosyltransferase 15
Sequence:
MMSIANEQQFAMDQLVETNDDSEKKPRITYTRKFLISLSEKDVCKKLPNLPGEFDEALLLDFEDPSPERARISGDFSSHGFRRNDYSSSPPTRGELGTNSRGTHGRWEGRSGGWNDKDSDSQSDRDSGEPGRRSGMPSRRSWQAPEHDGLLGKGSFPKPSGFGAGTSAPRPQSNDSHQLSRTNEPYHPPRPYKAPPFTRRDARDSFNDETFGSSDSTSEDRAEEERKRRASFELLRKEHQKAFQERQKSNPDLRKNDFDFTELLGESKDDKGRPSRSDEVNHAPTIPGSSNTSLPSQSNAPRPLVPPGFASTILEKKQGEKPQTETSQYERSPLNSKGINVVNGTSVNNGGKPLGIKIGSSEMLIEGEDVRVSSTDANERAVNISSLLGISTDTVNKDKSFEKLSSISTPTEIQGYPIKSEKATMTLGKKKSLEHSDGPSILDKIFNTAINLNSGDSSNMNKKNVEKVEEIRSPQTINKSSKFAHLFLEEDNKPVEVLPSSEPPRGLLSLLQGADKLQTFDTKANPDLSTDFPFQGHATKRTDQLSSTSTTKSVTAVPPVLTCEDLEQSILSEVGDSYHPPPPPVDQDTSVPSVKMTKQRKTSVDDQASQHLLSLLQRSSDPKSQDTQLLSATERRPPPPSMKTTTPPPSVKSTTAGEADPGKSLTLENLFGSAFMNELQSIGEPVSGRAMVSDAPGVPLRSERSIGELSQRNQIRPDGPPGGVLALPEDGNLLAVGGHANPSKYMSFPGSHNQEPEVAFNISDKLAALNSGPRNERPTMGGQDGLFLHQHPQQYVTNPSSHLNGSGPVFHPFDSQHAHVKPQLDFMGPGSTMSQHHDPPPNHRFPPNMIHRPPFHHTPTSGHPEFDRLPPHMMQKMHMQDNLQHHHLMQGFPGSGPQPHHSPHVNNQMPGLIPELNPSQGFPFAHRQPNYGMPPPGSQVNRGEHPASLQTLLGIQQRMDPAKQIPAVGQAGGPNRQGSVGHELDLGFGYR
Protein: UDP-glycosyltransferase 71C5 (EC 2.4.1.-) (Q9FE68)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses low quercetin 3-O-glucosyltransferase activity in vitro.
Interaction partners:
- Probable sugar phosphate/phosphate translocator At1g53660
- Abscisic acid 8'-hydroxylase 1
- Glucan endo-1,3-beta-glucosidase, acidic isoform
Sequence:
MKTAELIFVPLPETGHLLSTIEFGKRLLNLDRRISMITILSMNLPYAPHADASLASLTASEPGIRIISLPEIHDPPPIKLLDTSSETYILDFIHKNIPCLRKTIQDLVSSSSSSGGGSSHVAGLILDFFCVGLIDIGREVNLPSYIFMTSNFGFLGVLQYLPERQRLTPSEFDESSGEEELHIPAFVNRVPAKVLPPGVFDKLSYGSLVKIGERLHEAKGILVNSFTQVEPYAAEHFSQGRDYPHVYPVGPVLNLTGRTNPGLASAQYKEMMKWLDEQPDSSVLFLCFGSMGVFPAPQITEIAHALELIGCRFIWAIRTNMAGDGDPQEPLPEGFVDRTMGRGIVCSWAPQVDILAHKATGGFVSHCGWNSVQESLWYGVPIATWPMYAEQQLNAFEMVKELGLAVEIRLDYVADGDRVTLEIVSADEIATAVRSLMDSDNPVRKKVIEKSSVARKAVGDGGSSTVATCNFIKDILGDHF
Protein: PDR1 up-regulated protein 1 (Q6FIN8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Mitochondrial protein that contributes to the enhanced virulence of C.glabrata strains that acquired azole resistance.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:21408004}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MSDSREIKKPWWFKKAKEWADEFYTRDQKLEDSDRRDLSKKYATISKASVVGAATGLSAGLGGPYAYRYYTTGALKGVKLPRTILLGVVSMVIMRNVAAKIAWDKELKKLDPSGELKQNYKSAHKTVDDVSLSDNSTSVQKKYGMMKFLKYRTAPRWAMYFEGTYQHPDRKFPNPDQMVQDLKGSRRAFPPFFSKADKFWHQIDRKDNDHT
Protein: Defensin alpha 5 (Defensin-5) (HD5(20-94)) [Cleaved into: HD5(23-94); HD5(29-94); HD5(56-94); HD5(63-94)] (Q01523)
Organism: Homo sapiens (Human)
Function: Host-defense peptide that maintains sterility in the urogenital system. Has antimicrobial activity against a wide range of bacteria, including Gram-negative E.coli, P.aeruginosa and S.typhimurium, and Gram-positive E.aerogenes, S.aureus, B.cereus, E.faecium and L.monocytogenes. Confers resistance to intestinal infection by S.typhimurium. Exhibits antimicrobial activity against enteric commensal bacteria such as B.adolescentis, L.acidophilus, B.breve, L.fermentum, B.longum and S.thermophilus. Binds to bacterial membranes and causes membrane disintegration. Induces the secretion of the chemokine IL-8 by intestinal epithelial cells. Binds to B.antracis lef/lethal factor, a major virulence factor from B.anthracis, and neutralizes its enzymatic activity.
Subcellular location: Secreted {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:9588893}. Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:9588893}. Note=Stored as propeptide HD5(20-94) in secretory granules of small intestinal Paneth cells and found in the ileum lumen as processed mature peptides, predominantly in the HD5(63-94) form (PubMed:12021776). Peptides HD5(20-94), HD5(23-94) and HD5(29-94) are found within tissues, HD5(20-94) being the predominant intracellular form. Peptides HD5(56-94) and HD5(63-94) are found in the extracellular milieu, HD5(63-94) being the most abundant form (PubMed:12021776). Secreted into the female genital tract lumen (PubMed:9588893). {ECO:0000269|PubMed:12021776, ECO:0000269|PubMed:9588893}.
Interaction partners:
- Defensin-6
- Angiotensin-converting enzyme 2
- Beta-defensin 1
- Regenerating islet-derived protein 3-alpha
- Defensin beta 4A
- Beta-defensin 103
- Lithostathine-1-beta
- Trypsin-2
- Trypsin-3
- Beta-defensin 105
Sequence:
MRTIAILAAILLVALQAQAESLQERADEATTQKQSGEDNQDLAISFAGNGLSALRTSGSQARATCYCRTGRCATRESLSGVCEISGRLYRLCCR
Protein: Uncharacterized protein YejG (P0AD21)
Organism: Escherichia coli (strain K12)
Interaction partners:
Sequence:
MTSLQLSIVHRLPQNYRWSAGFAGSKVEPIPQNGPCGDNSLVALKLLSPDGDNAWSVMYKLSQALSDIEVPCSVLECEGEPCLFVNRQDEFAATCRLKNFGVAIAEPFSNYNPF
Protein: RING-type E3 ubiquitin transferase (EC 2.3.2.27) (F4I570)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MIPWGGVTCCLSAAALYLLGRSSGRDAEVLETVTRVNQLKELAQLLELDSKILPFIVAVSGRVGSETPIKCEHSGIRGVIVEETAEQHFLKHNETGSWVQDSALMLSMSKEVPWFLDDGTSRVHVMGARGATGFALTVGSEVFEESGRSLVRGTLDYLQGLKMLGVKRIERVLPTGIPLTIVGEAVKDDIGEFRIQKPDRGPFYVSSKSLDQLISNLGKWSRLYKYASMGFTVLGVFLITKHVIDSVLERRRRRQLQKRVLDAAAKRAELESEGIHW
Protein: Nuclear receptor subfamily 1 group I member 3 (Constitutive androstane receptor) (E9PCF2)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MLPKRSRRTVSKSIGPTCPFAGSCEVSKTQRRHCPACRLQKCLDAGMRKDMILSAEALALRRAKQAQRRAQQTPVQLSKEQEELIRTLLGAHTRHMGTMFEQFVQFRPPAHLFIHHQPLPTLAPVLPLVTHFADINTFMVLQVIKFTKDLPVFRSLPIEDQISLLKGAAVEICHIVLNTTFCLQTQNFLCGPLRYTIEDGARVGFQVEFLELLFHFHGTLRKLQLQEPEYVLLAAMALFSPDRPGVTQRDEIDQLQEEMALTLQSYIKGQQRRPRDRYGGTLRAWRPHQGRKGLVKH
Protein: Inactive hydroxysteroid dehydrogenase-like protein 1 (Short chain dehydrogenase/reductase family 12C member 3) (Q3SXM5)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:19026618}.
Interaction partners:
- Formimidoyltransferase-cyclodeaminase
Sequence:
MAAVDSFYLLYREIARSCNCYMEALALVGAWYTARKSITVICDFYSLIRLHFIPRLGSRADLIKQYGRWAVVSGATDGIGKAYAEELASRGLNIILISRNEEKLQVVAKDIADTYKVETDIIVADFSSGREIYLPIREALKDKDVGILVNNVGVFYPYPQYFTQLSEDKLWDIINVNIAAASLMVHVVLPGMVERKKGAIVTISSGSCCKPTPQLAAFSASKAYLDHFSRALQYEYASKGIFVQSLIPFYVATSMTAPSNFLHRCSWLVPSPKVYAHHAVSTLGISKRTTGYWSHSIQFLFAQYMPEWLWVWGANILNRSLRKEALSCTA
Protein: Adenylate kinase 2 (EC 2.7.4.3) (ATP-AMP transphosphorylase) (ATP:AMP phosphotransferase) (Adenylate kinase cytosolic and mitochondrial) (Adenylate monophosphate kinase) (Q9U915)
Organism: Drosophila melanogaster (Fruit fly)
Function: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways.
Subcellular location: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03168}. Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03168}. Note=Predominantly mitochondrial. {ECO:0000255|HAMAP-Rule:MF_03168}.
Interaction partners:
- Adenylate kinase isoenzyme 6 homolog
- Adenine phosphoribosyltransferase
- AMP deaminase
- Adenosine kinase
- Adenosine kinase
- Adenosine kinase
- Adenylosuccinate lyase
- Adenylate kinase 1
- Ribonucleoside-diphosphate reductase large subunit
- Dual 3',5'-cyclic-AMP and -GMP phosphodiesterase 11
Sequence:
MAPNAAVPVERYEPENIGINAILLGPPGSGKGTQAPLLKEKFCVCHLSTGDMLRAEISSGSKLGAELKKVMDAGKLVSDDLVVDMIDSNLDKPECKNGFLLDGFPRTVVQAEKLDTLLDKRKTNLDAVIEFAIDDSLLVRRITGRLIHQASGRSYHEEFAPPKKPMTDDVTGEPLIRRSDDNAEALKKRLEAYHKQTKPLVDYYGLRGLHFKVDAAKKSSDVFSTIDSIFQRKRPAQIQL