wanglab/gogpt-training-data huggingface dataset:
Protein: ATP-dependent RNA helicase DHX15 (EC 3.6.4.13) (DEAH box protein 15) (O35286)
Organism: Mus musculus (Mouse)
Function: RNA helicase involved in mRNA processing and antiviral innate immunity. Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA (By similarity). In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns (By similarity). Plays a key role in antiviral innate immunity by promoting both MAVS-dependent signaling and NLRP6 inflammasome. Acts as an RNA virus sensor: recognizes and binds viral double stranded RNA (dsRNA) and activates the MAVS-dependent signaling to produce interferon-beta and interferon lambda-3 (IFNL3) (By similarity). Involved in intestinal antiviral innate immunity together with NLRP6: recognizes and binds viral dsRNA and promotes activation of the NLRP6 inflammasome in intestinal epithelial cells to restrict infection by enteric viruses. The NLRP6 inflammasome acts by promoting maturation and secretion of IL18 in the extracellular milieu. Also involved in antibacterial innate immunity by promoting Wnt-induced antimicrobial protein expression in Paneth cells.
Subcellular location: Nucleus {ECO:0000269|PubMed:9342318}. Nucleus, nucleolus {ECO:0000269|PubMed:9342318}.
Interaction partners:
- Tuftelin-interacting protein 11
- Pre-mRNA-processing factor 17
- U2 small nuclear ribonucleoprotein A'
- Splicing factor 45
- 116 kDa U5 small nuclear ribonucleoprotein component
- Something about silencing protein 10
- SURP and G-patch domain-containing protein 1
- Pre-mRNA-processing factor 19
- Pre-mRNA-processing-splicing factor 8
- PIN2/TERF1-interacting telomerase inhibitor 1
Sequence:
MSKRHRLDLGEDYPSGKKRAGTDGKDRERDRDREDRSKDRDRERDRGDREREREKEKEKELRASTNAMLISAGLPPLKASHSAHSTHSAHSTHSTHSAHSTHTGHTGHTSLPQCINPFTNLPHTPRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQIHMCEEEEGDLLLFLTGQEEIDEACKRIKREVDDLGPEVGDIKIIPLYSTLPPQQQQRIFEPPPPKKQNGAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTEMQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPPAPETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFVRPTEAKKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHESVQWCYDNFINYRSLMSADNVRQQLSRIMDRFNLPRRSTDFTSRDYYINIRKALVTGYFMQVAHLERTGHYLTVKDNQVVQLHPSTVLDHKPEWVLYNEFVLTTKNYIRTCTDIKPEWLVKIAPQYYDMSNFPQCEAKRQLDRIIAKLQSKEYSQY
Protein: Multiplexin, isoform I (E1JI51)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MAMVISTRAKLVITALILFFLLGIVLVTGSTKGWFNPNRYNGERVAARIQLRVAALNEPSTGDLQGIRGADFACYRQGRRAGLLGTFKAFLSSRVQNLDTIVRPADRDLPVVNTRGDVLFNSWKGIFNGQGGFFSQAPRIYSFSGKNVMTDSTWPMKMVWHGSLPNGERSMDTYCDAWHSGDHLKGSFASNLDGHKLLEQKRQSCDSKLIILCVEALSQDRKRKKREIGDGSSHGESESREFKTADEYAAHLENLLL
Protein: Sugar phosphatase YidA (EC 3.1.3.23) (P0A8Y5)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dephosphorylation of different sugar phosphates including erythrose-4-phosphate (Ery4P), ribose-5-phosphate (Ribu5P), fructose-1-phosphate (Fru1P), fructose-6-phosphate (Fru6P), glucose-6-P (Glu6P), and also imidodiphosphate (Imido-di-P) and acetyl phosphate (Acetyl-P). Selectively hydrolyzes alpha-D-glucose-1-phosphate (Glu1P) and has no activity with the beta form.
Interaction partners:
- 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
- 5'-3' exoribonuclease Rnm
- Uncharacterized protein YidB
- Uncharacterized protein YecA
- Proofreading thioesterase EntH
- Hexitol phosphatase B
- Hexitol phosphatase A
- Epimerase family protein YfcH
Sequence:
MAIKLIAIDMDGTLLLPDHTISPAVKNAIAAARARGVNVVLTTGRPYAGVHNYLKELHMEQPGDYCITYNGALVQKAADGSTVAQTALSYDDYRFLEKLSREVGSHFHALDRTTLYTANRDISYYTVHESFVATIPLVFCEAEKMDPNTQFLKVMMIDEPAILDQAIARIPQEVKEKYTVLKSAPYFLEILDKRVNKGTGVKSLADVLGIKPEEIMAIGDQENDIAMIEYAGVGVAMDNAIPSVKEVANFVTKSNLEDGVAFAIEKYVLN
Protein: Interleukin-11 receptor subunit alpha-1 (IL-11 receptor subunit alpha-1) (IL-11R subunit alpha-1) (IL-11R-alpha-1) (IL-11RA1) (Enhancer trap locus homolog 2) (Etl-2) (Novel cytokine receptor 1) (NR-1) (NR1) [Cleaved into: Soluble interleukin-11 receptor subunit alpha (sIL-11R) (sIL-11RA) (sIL11RA)] (Q64385)
Organism: Mus musculus (Mouse)
Function: Receptor for interleukin-11. The receptor systems for IL6, LIF, OSM, CNTF, IL11 and CT1 can utilize IL6ST for initiating signal transmission. The IL11/IL11RA/IL6ST complex may be involved in the control of proliferation and/or differentiation of skeletogenic progenitor or other mesenchymal cells. Essential for the normal development of craniofacial bones and teeth.
Subcellular location: [Interleukin-11 receptor subunit alpha-1]: Membrane {ECO:0000269|PubMed:26876177}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:Q14626}.; SUBCELLULAR LOCATION: [Soluble interleukin-11 receptor subunit alpha]: Secreted {ECO:0000269|PubMed:26876177}.
Interaction partners:
- Interleukin-11
- Interleukin-6 receptor subunit beta
- Interleukin-11 receptor subunit alpha-2
- Oncostatin-M
- Cardiotrophin-1
- Ciliary neurotrophic factor
- Interleukin-6
- Interferon gamma
- UDP-glucose 4-epimerase
- N-acetylgalactosamine kinase
Sequence:
MSSSCSGLTRVLVAVATALVSSSSPCPQAWGPPGVQYGQPGRPVMLCCPGVSAGTPVSWFRDGDSRLLQGPDSGLGHRLVLAQVDSPDEGTYVCQTLDGVSGGMVTLKLGFPPARPEVSCQAVDYENFSCTWSPGQVSGLPTRYLTSYRKKTLPGAESQRESPSTGPWPCPQDPLEASRCVVHGAEFWSEYRINVTEVNPLGASTCLLDVRLQSILRPDPPQGLRVESVPGYPRRLHASWTYPASWRRQPHFLLKFRLQYRPAQHPAWSTVEPIGLEEVITDAVAGLPHAVRVSARDFLDAGTWSAWSPEAWGTPSTGPLQDEIPDWSQGHGQQLEAVVAQEDSPAPARPSLQPDPRPLDHRDPLEQVAVLASLGIFSCLGLAVGALALGLWLRLRRSGKDGPQKPGLLAPMIPVEKLPGIPNLQRTPENFS
Protein: NF-kappa-B inhibitor epsilon (NF-kappa-BIE) (I-kappa-B-epsilon) (IkB-E) (IkB-epsilon) (IkappaBepsilon) (O00221)
Organism: Homo sapiens (Human)
Function: Inhibits NF-kappa-B by complexing with and trapping it in the cytoplasm. Inhibits DNA-binding of NF-kappa-B p50-p65 and p50-c-Rel complexes.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Proto-oncogene c-Rel
- Transcription factor p65
- Transcription factor RelB
- Nuclear factor NF-kappa-B p105 subunit
- NF-kappa-B inhibitor beta
- NF-kappa-B inhibitor alpha
- Inhibitor of nuclear factor kappa-B kinase subunit beta
- Inhibitor of nuclear factor kappa-B kinase subunit alpha
- NF-kappa-B essential modulator
- Serine/threonine-protein phosphatase 6 catalytic subunit
Sequence:
MNQRRSESRPGNHRLQAYAEPGKGDSGGAGPLSGSARRGRGGGGAIRVRRPCWSGGAGRGGGPAWAVRLPTVTAGWTWPALRTLSSLRAGPSEPHSPGRRPPRAGRPLCQADPQPGKAARRSLEPDPAQTGPRPARAAGMSEARKGPDEAEESQYDSGIESLRSLRSLPESTSAPASGPSDGSPQPCTHPPGPVKEPQEKEDADGERADSTYGSSSLTYTLSLLGGPEAEDPAPRLPLPHVGALSPQQLEALTYISEDGDTLVHLAVIHEAPAVLLCCLALLPQEVLDIQNNLYQTALHLAVHLDQPGAVRALVLKGASRALQDRHGDTALHVACQRQHLACARCLLEGRPEPGRGTSHSLDLQLQNWQGLACLHIATLQKNQPLMELLLRNGADIDVQEGTSGKTALHLAVETQERGLVQFLLQAGAQVDARMLNGCTPLHLAAGRGLMGISSTLCKAGADSLLRNVEDETPQDLTEESLVLLPFDDLKISGKLLLCTD
Protein: Tropomodulin-2 (Neuronal tropomodulin) (N-Tmod) (P70566)
Organism: Rattus norvegicus (Rat)
Function: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Beta-adducin
- Alpha-adducin
- Gamma-adducin
- Nebulin
- Tropomyosin alpha-1 chain
- Gelsolin
- Tropomyosin alpha-4 chain
- Tropomyosin beta chain
- Dematin actin binding protein
- Troponin T, slow skeletal muscle
Sequence:
MALPFQKGLEKYKNIDEDELLGKLSEEELKQLENVLDDLDPESATLPAGFRQKDQTQKAATGPFDREHLLMYLEKEALEQKDREDFVPFTGEKKGRVFIPKEKPVETRKEEKVTLDPELEEALASASDTELYDLAAVLGVHNLLNNPKFDEETTNGQGRKGPVRNVVKGEKAKPVFEEPPNPTNVEASLQQMKANDPSLQEVNLNNIKNIPIPTLKEFAKALETNTHVRKFSLAATRSNDPVALAFAEMLKVNKTLKSLNVESNFITGAGILALVEALRENDTLTEIKIDNQRQQLGTAVEMEIAQMLEENSRILKFGYQFTKQGPRTRVAAAITKNNDLVRKKRVEGDRR
Protein: Heat shock protein HSP70 (SSA subfamily protein 1) (P41797)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12761219, ECO:0000269|PubMed:16720580}. Secreted, cell wall {ECO:0000269|PubMed:12761219, ECO:0000269|PubMed:12782322, ECO:0000269|PubMed:16720580, ECO:0000269|PubMed:8757872}.
Interaction partners:
- Hsp90 cochaperone
- Heat shock protein 90 homolog
- Zuotin
- Chaperone ATPase
- Heat shock transcription factor
- Hsp70 chaperone Ssb
- Type I HSP40 co-chaperone
- Heat shock protein SSA2
- Heat shock protein 78
- Type II HSP40 co-chaperone
Sequence:
MSKAVGIDLGTTYSCVAHFANDRVEIIANDQGNRTTPSFVAFTDTERLIGDAAKNQAAMNPANTVFDAKRLIGRKFDDPEVINDAKHFPFKVIDKAGKPVIQVEYKGETKTFSPEEISSMVLTKMKEIAEGYLGSTVKDAVVTVPAYFNDSQRQATKDAGTIAGLNVLRIINEPTAAAIAYGLDKKGSRGEHNVLIFDLGGGTFDVSLLAIDEGIFEVKATAGDTHLGGEDFDNRLVNFFIQEFKRKNKKDISTNQRALRRLRTACERAKRTLSSSAQTSIEIDSLYEGIDFYTSITRARFEELCADLFRSTLDPVGKVLADAKIDKSQVEEIVLVGGSTRIPKIQKLVSDFFNGKELNKSINPDEAVAYGAAVQAAILTGDTSSKTQDILLLDVAPLSLGIETAGGIMTKLIPRNSTIPTKKSETFSTYADNQPGVLIQVFEGERAKTKDNNLLGKFELSGIPPAPRGVPQIEVTFDIDANGILNVSALEKGTGKTQKITITNDKGRLSKEEIDKMVSEAEKFKEEDEKEAARVQAKNQLESYAYSLKNTINDGEMKDKIGADDKEKLTKAIDETISWLDASQAASTEEYEDKRKELESVANPIISGAYGAAGGAPGGAGGFPGAGGFPGGAPGAGGPGGATGGESSGPTVEEVD
Protein: Proline-rich protein 35 (Uncharacterized protein RJD1) (P0CG20)
Organism: Homo sapiens (Human)
Interaction partners:
- NHL-repeat-containing protein 4
- Olfactory receptor 51A4
- Olfactory receptor 51L1
Sequence:
MSREAGSCRVGTGARARSRKPKKPHYIPRPWGKPYNYKCFQCPFTCLEKSHLYNHMKYSLCKDSLSLLLDSPDWACRRGSTTPRPHAPTPDRPGESDPGRQPQGARPTGAAPAPDLVVADIHSLHCGGGPKSRAKGSPGPPPPVARATRKGPGPSGLLPESWKPGMGGDPRGVGAGDMASAGPEGSVPCYPPPAPGEFPEAHSLHLSLLGVNYPLSPGLFSYLGPSLAAAAHVPFLASASPLLPPATAFPAVQPPQRPTPAPRLYYPLLLEHTLGLPAGKAALAKAPVSPRSPSGTPAPGLLKVPVPGLGPWPRVTPRDPGQEGELERAAQSDPRRRLSLGSRLELPKASPSLTRFCSRSSLPTGSSVMLWPEDGDPGGPETPGPEGPLPLQPRGPVPGSPEHVGEDLTRALGDYARVEQRLGQLGPAGGLAPRPLREQLGKIRLELLTIHQALEQAVRPPDAPLDLSVKRAPAKGPQALGEAWGRPELGPVLTGGTPEPPGMLGPAAPQPFSGHTTKCEADSSVPPPGLPLAAPDDPVIPGSGWGTCVATRSSQTPEAVCGLQSPQGAEV
Protein: Large ribosomal subunit protein mL64 (39S ribosomal protein L59, mitochondrial) (MRP-L59) (Growth arrest and DNA damage-inducible proteins-interacting protein 1) (Q9CR59)
Organism: Mus musculus (Mouse)
Function: Acts as a negative regulator of G1 to S cell cycle phase progression by inhibiting cyclin-dependent kinases. Inhibitory effects are additive with GADD45 proteins but occurs also in the absence of GADD45 proteins. Acts as a repressor of the orphan nuclear receptor NR4A1 by inhibiting AB domain-mediated transcriptional activity. May be involved in the hormone-mediated regulation of NR4A1 transcriptional activity. May play a role in mitochondrial protein synthesis.
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q8TAE8}. Nucleus {ECO:0000250|UniProtKB:Q8TAE8}. Note=Using N-terminally tagged constructs, has been found in the nucleus. C-terminally tagged constructs are targeted exclusively to mitochondria. This discrepancy may be explained by masking of a potential N-terminal mitochondrial targeting signal by the tag. {ECO:0000250|UniProtKB:Q8TAE8}.
Interaction partners:
- Large ribosomal subunit protein mL62
- Growth arrest and DNA damage-inducible protein GADD45 gamma
- Large ribosomal subunit protein bL28m
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein bL33m
- Large ribosomal subunit protein mL49
- Large ribosomal subunit protein mL51
- 39S ribosomal protein L40
- Large ribosomal subunit protein mL41
- Large ribosomal subunit protein uL15m
Sequence:
MAALAMRSGYLLRLSVALGPRSRSYRAPPPPRRRPGPHSPDPENLLTPRWQLTPRYVAKQFGRHGAISGVPPASLWPTPEQLRELEAEEQEWYPSLATMQESLRLQQQALEARRQAREQRIAECMAKMPQMIENWRKQKRERWEKIQADKERRARLQAEAQERLGYHVDPRSARFQELLQDLDKQQRKRLKEERQRQKKEARIAAMASAEAQDSAVSGEPSS
Protein: Uncharacterized protein (F4JVV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Protein disulfide-isomerase 5-1
- Receptor-like serine/threonine-protein kinase NCRK
- DNA-directed RNA polymerases II, IV and V subunit 11
- Thioredoxin Y2, chloroplastic
Sequence:
MVNYVLKITADLENLTNLQPSGGCDDSNFPYLFKLKCERCGEVTPKETCVTLNETFTPPGGRGTCHLVQKKANIGSDLCKFCGREGNVTMIPGKGRPLTLEDSEAGEHAPLMVFDCRGYEPIDFGFGGYWKAQAESGTKFDEIDLSSGEEFTEYDEKGECPVMISNFRASFSVTK
Protein: GM08734p (Q95S53)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDMVRQSLLQEGTNPNAVIANERSTPDELGIAMLRLNKLMHGLVDKFVETLKLSTTDKEAKWREEILETSKRRAKIERTEERKRKRKELKEQKAQTKNRLEWLEQNKVVDADVNGATAETPTLQVSKVNDQEIPQSFAKTENSPVLKVKKEKTPKTPAKKERNLQKKQAFDEQINPEITKLSSKKQNLNTIKENNAEPQLEGRPKNLSQNPSRKNQPESRSLSHD
Protein: Cytochrome P450 2A4 (EC 1.14.14.1) (CYPIIA4) (Cytochrome P450-15-alpha) (Cytochrome P450-IIA3.1) (Testosterone 15-alpha-hydroxylase) (P15392)
Organism: Mus musculus (Mouse)
Function: Highly active in the 15-alpha-hydroxylation of testosterone. Also active in the 15-alpha-hydroxylation of progesterone and androstenedione. Little or no activity on corticosterone, pregnenolone, dehydroepiandrosterone, estradiol or estriol.
Subcellular location: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein.
Interaction partners:
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450 4A14
- Cytochrome P450 3A25
- Cytochrome P450 4A10
- Cytochrome P450 3A11
- Cytochrome P450 3A41
- Cytochrome P450 4A12A
- Cytochrome P450 3A13
- Cytochrome P450 4A12B
Sequence:
MLTSGLLLVAAVAFLSVLVLMSVWKQRKLSGKLPPGPTPLPFVGNFLQLNTEQMYNSLMKISQRYGPVFTIYLGSRRIVVLCGQETVKEALVDQAEEFSGRGEQATFDWLFKGYGIAFSSGERAKQLRRFSITTLRDFGVGKRGIEERIQEEAGFLIDSFRKTNGAFIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSLQFTATSMGQVYEMFSSVMKHLPGPQQQAFKELQGLEDFITKKVEHNQRTLDPNSPRDFIDSFLIRMLEEKKNPNTEFYMKNLVLTTLNLFFAGTETVSTTLRYGFLLLMKYPDIEAKVHEEIDRVIGRNRQPKYEDRMKMPYTEAVIHEIQRFADLIPMGLARRVTKDTKFRDFLLPKGTEVFPMLGSVLKDPKFFSNPKDFNPKHFLDDKGQFKKSDAFVPFSIGKRYCFGEGLARMELFLFLTNIMQNFHFKSTQEPQDIDVSPRLVGFVTIPPTYTMSFLSR
Protein: MAPK phosphothreonine lyase (EC 4.2.3.-) (27.5 kDa virulence protein) (Secreted effector protein SpvC) (P0A2M9)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Secreted effector that irreversibly inactivates host MAP kinases by catalyzing the dephosphorylation of the phosphothreonine residue in the pT-X-pY motif in MAPK2/ERK2, MAPK3/ERK1, and p38, via a beta-elimination reaction leading to a dehydrobutyrine residue. Is also able to remove the phosphate group from phospho-JNK in vitro, but JNK may not be a substrate in vivo. Could help suppress localized pro-inflammatory responses at infection foci in the spleen and liver, and thereby facilitate bacterial growth.
Subcellular location: Secreted {ECO:0000269|PubMed:18284579}. Note=Can be secreted in vitro by either the SPI-1 or SPI-2 type III secretion systems (T3SS). Translocation of the protein into the cytosol of infected macrophages by intracellular bacteria is dependent on the SPI-2 T3SS. Translocated SpvC proteins appear to be distributed evenly in the cytoplasm of infected cells, and neither colocalize with the SCV membrane nor accumulate in the nucleus of infected cells.
Interaction partners:
Sequence:
MPINRPNLNLNIPPLNIVAAYDGAEIPSTNKHLKNNFNSLHNQMRKMPVSHFKEALDVPDYSGMRQSGFFAMSQGFQLNNHGYDVFIHARRESPQSQGKFAGDKFHISVLRDMVPQAFQALSGLLFSEDSPVDKWKVTDMEKVVQQARVSLGAQFTLYIKPDQENSQYSASFLHKTRQFIECLESRLSENGVISGQCPESDVHPENWKYLSYRNELRSGRDGGEMQRQALREEPFYRLMTE
Protein: Antigen-presenting glycoprotein CD1d2 (CD antigen CD1d.2) (P11610)
Organism: Mus musculus (Mouse)
Function: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P11609}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11609}. Endosome membrane {ECO:0000250|UniProtKB:P11609}. Lysosome membrane {ECO:0000250|UniProtKB:P11609}. Note=Subject to intracellular trafficking between the cell membrane, endosomes and lysosomes. {ECO:0000250|UniProtKB:P11609}.
Interaction partners:
Sequence:
MRYLPCLLLWAFLQVWGQSEVQQKNYTFRCLQTSSFANISWSRTDSLILLGDLQTHRWSNDSATISFTKPWSQGKLSNQQWEKLQHMFQVYRVSFTRDIQELVKMMSPKEDYPIEIQLSTGCEMYPGNASESFFHVAFQGKYAVRFRGTSWQRVLGAPSWLDLPIKVLNADQGTSATVQTLLNDTWPQFARGLLEAGKSDLEKQEKPVAWLSSVPSSAHGHLQLVCHVSGFYPKPVWVMWMRGDQEQQGTHRGDFLPNADETWYLQATLDVEAGEEAGLACRVKHSSLGGQDIILYWDARQAPVGLIVFIVLIMLVVVGAVVYYIWRRRSAYQDIR
Protein: Ribosomal RNA-processing protein 42 (Q29QQ9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- Exosome complex component RRP4
- FI01414p
- Exosome complex exonuclease RRP44
- FI07225p
- Exosome complex component 10 homolog
- FI06805p
- Csl4
- Exosome complex component RRP45
- Nuclear nucleic acid-binding protein C1D
- RNA helicase
Sequence:
MAYVALSEAEKTYILHGVEDDFRCDGRSRRDYRPMDLETGLVSNASGSARLRLANTDILVGVKTEIDVPNPLTPEFGKLEFFVDCSANATPEFEGRGGSDLAQELILSLQNAYESPLAFNYRTLCLIPGQQCWKLYIDILILECGGNLHDAVSLAAKAALFNTKLPRVTATMLDAGITDLIISDNPYDCTRIGIETVPLLVTVCKIGDYVLVDPSAEEEVCSTVSMVVSVSMRNGQAFLSGTHLTGGGAMHRDTMRNCLELGLAIGEHLDRLLTKMLNLEQQRVGLKRPQIVGFLK
Protein: F26K24.24 protein (TRAF-like superfamily protein) (Q9SF04)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Ubiquitin-ribosomal protein eL40y fusion protein
- Ubiquitin-ribosomal protein eL40z fusion protein
- Ubiquitin-ribosomal protein eS31x fusion protein
- Ubiquitin-ribosomal protein eS31y fusion protein
- Ubiquitin-ribosomal protein eS31z fusion protein
- E3 ubiquitin-protein ligase PRT1
- Protein NBR1 homolog
- Homogentisate solanesyltransferase, chloroplastic
- 2-methyl-6-phytyl-1,4-hydroquinone methyltransferase, chloroplastic
- E3 ubiquitin-protein ligase KEG
Sequence:
MDPPVSDLESIEDQKEGGPSFHCDLYDTQVVHKIAQVFLPGLATACVDNTTGDIFRSPGSVAADIRKEMIEYLTRRSETFVAEHIVLQGGSEIEASHDPFDIISDFIDDFATSKRNLFSRVSGWMLSERREDNIDDFAQEMEISGFWLTDHREGIAQTLLKNVDFKSSAHCEMKFQTEGELAEHAMNCGYRTMNCENEGCTAVFCANQMENHDSVCPFKIIPCEQNCSESIMRRDMDRHCITVCPMKLVNCPFHSVGCLSDVHQCEVQQHHLDNVSSHLMYILRSIYKEASLDDLKPRAEQIQQLSTRLSEARNARSLTNLVKEIDGKLGPLEIKPKIVTDSESDKPENTEKKALEEAEIKEKPETSNLKAVTLEQTAREAPEDKLVSKEVDAAMVKEAAKKVSEAEIADNVNEEGELKAQKLLEIGEFIKEGDNNSADDLSERTETKAPEVVVMDEAREEEDSVETKDTRTYETIRGLEIEANEMIDEETKKSTETKTEAPSRIVMDKEGDEETKKSTETETEAPSRIVMETEKDEETMNSRARASDEAEALSKSSQGFSTVQAETVPHMS
Protein: GH17679p (Olig family, isoform A) (Olig family, isoform B) (Olig family, isoform C) (Olig family, isoform D) (Q9VJC1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- GTX/Nkx6B-like homeodomain protein
Sequence:
MDPSNLAFGFPGLPNHGHMPIPPTANMLGGQHPAPTASPPQSVPGRRTPLGSVGLGGFYAQGMGMSQQPPTDENKPGPSAPEKPLSPTAAAIAAIAISGGTTTVAVSSGGASGSGSNSGKQKNRQGKTVRLNINARERRRMHDLNDALDELRSVIPYAHSPSVRKLSKIATLLLAKNYILMQQNALEELRRLLAYIQSTTGAAPLDLGAFPAAAKLQALLQGPHNEPPTSSS
Protein: Peptide transport system ATP-binding protein (E0SFZ8)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004417}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004417}.
Interaction partners:
- Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily
- Predicted antimicrobial peptide transporter subunit membrane component of ABC superfamily
- Peptide transport system ATP-binding protein
- Peptide transport periplasmic protein
Sequence:
MALLEIRNLTIEFLTPDGPVKAVDRVSISLTEGEIRGLVGESGSGKSLIAKAICGINKENWRITADRFRFDDVDMLQLTPHQRRKLVRHNMSMIFQEPQSCLDPSARVGRQLMQSIPGWTYKGRWWQRINWRKRRAIELLHRVGIKDHKDIMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEATTQAQIFRLLARLNQNNNTTILLISHDLQTMSKWADRINVLYCGQTVESAVSDELISAPHHPYTQALIRAMPDFGCSLPHKSRLNALPGAIPSLAHLPVGCRLGPRCPYSQKECMTAPPLIPVKTHWYACHFPLNMEES
Protein: Transcriptional regulatory protein RcsA (Q8GM83)
Organism: Klebsiella pneumoniae
Interaction partners:
Sequence:
MSTMIMDLCSYTRLGLTGYLTSRGIKKQEIVEVNNAADLQKHCTSCCPAVVFLNEDCFVHDDESNGIIRQIITQNPATLFVIFMSLANIHFDRYLRVRKNLLISSKSITPKDLDVILVNYLKYKNTSVGQLTLPTLSLSKTESNMLQMWMAGHGTSQISTQMNIKAKTVSSHKGNIKKKIQTHNKQVIYHIVRLTENITSGIQVNMR
Protein: Splicing factor, arginine/serine-rich 19 (SR-related C-terminal domain-associated factor 1) (SR-related and CTD-associated factor 1) (SR-related-CTD-associated factor) (SCAF) (Serine arginine-rich pre-mRNA splicing factor SR-A1) (SR-A1) (Q9H7N4)
Organism: Homo sapiens (Human)
Function: May function in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- ETS domain-containing transcription factor ERF
- RNA exonuclease 1 homolog
- Proline-rich protein 12
- Nucleus accumbens-associated protein 1
- Tyrosine-protein phosphatase non-receptor type 23
Sequence:
MEEEDESRGKTEESGEDRGDGPPDRDPTLSPSAFILRAIQQAVGSSLQGDLPNDKDGSRCHGLRWRRCRSPRSEPRSQESGGTDTATVLDMATDSFLAGLVSVLDPPDTWVPSRLDLRPGESEDMLELVAEVRIGDRDPIPLPVPSLLPRLRAWRTGKTVSPQSNSSRPTCARHLTLGTGDGGPAPPPAPSSASSSPSPSPSSSSPSPPPPPPPPAPPAPPAPRFDIYDPFHPTDEAYSPPPAPEQKYDPFEPTGSNPSSSAGTPSPEEEEEEEEEEEEEEEDEEEEEGLSQSISRISETLAGIYDDNSLSQDFPGDESPRPDAQPTQPTPAPGTPPQVDSTRADGAMRRRVFVVGTEAEACREGKVSVEVVTAGGAALPPPLLPPGDSEIEEGEIVQPEEEPRLALSLFRPGGRAARPTPAASATPTAQPLPQPPAPRAPEGDDFLSLHAESDGEGALQVDLGEPAPAPPAADSRWGGLDLRRKILTQRRERYRQRSPSPAPAPAPAAAAGPPTRKKSRRERKRSGEAKEAASSSSGTQPAPPAPASPWDSKKHRSRDRKPGSHASSSARRRSRSRSRSRSTRRRSRSTDRRRGGSRRSRSREKRRRRRRSASPPPATSSSSSSRRERHRGKHRDGGGSKKKKKRSRSRGEKRSGDGSEKAPAPAPPPSGSTSCGDRDSRRRGAVPPSIQDLTDHDLFAIKRTITVGRLDKSDPRGPSPAPASSPKREVLYDSEGLSGEERGGKSSQKDRRRSGAASSSSSSREKGSRRKALDGGDRDRDRDRDRDRDRSSKKARPPKESAPSSGPPPKPPVSSGSGSSSSSSSCSSRKVKLQSKVAVLIREGVSSTTPAKDAASAGLGSIGVKFSRDRESRSPFLKPDERAPTEMAKAAPGSTKPKKTKVKAKAGAKKTKGTKGKTKPSKTRKKVRSGGGSGGSGGQVSLKKSKADSCSQAAGTKGAEETSWSGEERAAKVPSTPPPKAAPPPPALTPDSQTVDSSCKTPEVSFLPEEATEEAGVRGGAEEEEEEEEEEEEEEEEEEQQPATTTATSTAAAAPSTAPSAGSTAGDSGAEDGPASRVSQLPTLPPPMPWNLPAGVDCTTSGVLALTALLFKMEEANLASRAKAQELIQATNQILSHRKPPSSLGMTPAPVPTSLGLPPGPSSYLLPGSLPLGGCGSTPPTPTGLAATSDKREGSSSSEGRGDTDKYLKKLHTQERAVEEVKLAIKPYYQKKDITKEEYKDILRKAVHKICHSKSGEINPVKVSNLVRAYVQRYRYFRKHGRKPGDPPGPPRPPKEPGPPDKGGPGLPLPPL
Protein: Protein-tyrosine-phosphatase (A0A1D8PFT4)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSQIVPEIYVPPLRFSMVQPSLYRGAYPREVNFKFLETLQLKTNISLTPNPITKETDPELYNFAKENQIQLIHLECAQSGKGKKRGVPLDYEIAIQGLEYIIHNQYQPVYVHCYNGGQVTSLMVACLRKLQFWSAISIFNEFINFTTNITVNDRSFVDGFHGEIHINHDDKVDWLWVGVSKHVVGHHPKFQFIDKNKSMSSI