wanglab/gogpt-training-data huggingface dataset:
Protein: Bifunctional protein PyrR [Includes: Pyrimidine operon regulatory protein; Uracil phosphoribosyltransferase (UPRTase) (EC 2.4.2.9)] (P65946)
Organism: Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Function: Regulates transcriptional attenuation of the pyrimidine nucleotide (pyr) operon by binding in a uridine-dependent manner to specific sites on pyr mRNA. This disrupts an antiterminator hairpin in the RNA and favors formation of a downstream transcription terminator, leading to a reduced expression of downstream genes.
Interaction partners:
Sequence:
MKTKEVVDELTVKRAITRITYEIIERNKDLNKIVLAGIKTRGVFIAHRIQERLKQLENLSVPVVELDTKPFRDDVKSGEDTSLVSVDVTDREVILVDDVLYTGRTIRAAIDNIVGHGRPARVSLAVLVDRGHRELPIRPDYVGKNIPTSRSEEIIVEMTELDDQDRVLITEEA
Protein: Guanine nucleotide-binding protein G(z) subunit alpha (G(x) alpha chain) (Gz-alpha) (P19086)
Organism: Homo sapiens (Human)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems.
Subcellular location: Membrane; Lipid-anchor.
Interaction partners:
- Regulator of G-protein signaling 20
- Corticotropin-releasing factor receptor 1
- Insulin-like growth factor 1 receptor
- Metabotropic glutamate receptor 1
- Regulator of G-protein signaling 19
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-4
Sequence:
MGCRQSSEEKEAARRSRRIDRHLRSESQRQRREIKLLLLGTSNSGKSTIVKQMKIIHSGGFNLEACKEYKPLIIYNAIDSLTRIIRALAALRIDFHNPDRAYDAVQLFALTGPAESKGEITPELLGVMRRLWADPGAQACFSRSSEYHLEDNAAYYLNDLERIAAADYIPTVEDILRSRDMTTGIVENKFTFKELTFKMVDVGGQRSERKKWIHCFEGVTAIIFCVELSGYDLKLYEDNQTSRMAESLRLFDSICNNNWFINTSLILFLNKKDLLAEKIRRIPLTICFPEYKGQNTYEEAAVYIQRQFEDLNRNKETKEIYSHFTCATDTSNIQFVFDAVTDVIIQNNLKYIGLC
Protein: Periplasmic chaperone Spy (Spheroplast protein Y) (P77754)
Organism: Escherichia coli (strain K12)
Function: An ATP-independent periplasmic chaperone, decreases protein aggregation and helps protein refolding. Binds substrate over a large region of its convex inner surface. Substrate protein folds while it is bound to chaperone. Increasing Spy flexibility increases its substrate affinity and overall chaperone activity (shown for 3 different substrates). Protects proteins in vitro against tannin inactivation; tannins have antimicrobial activity. Overexpression enhances the stability of otherwise unstable periplasmic proteins.
Subcellular location: Periplasm {ECO:0000269|PubMed:21317898, ECO:0000269|PubMed:9068658, ECO:0000269|PubMed:9694902}.
Interaction partners:
- Inner membrane protein YebE
- Multidrug resistance protein MdtA
- Multidrug resistance protein MdtB
- Probable L,D-transpeptidase YcfS
- Signal transduction histidine-protein kinase BaeS
- Multidrug resistance protein MdtC
- Probable aminoglycoside efflux pump
- Uncharacterized protein YhdV
- Transcriptional regulatory protein BaeR
- Sensor histidine kinase CpxA
Sequence:
MRKLTALFVASTLALGAANLAHAADTTTAAPADAKPMMHHKGKFGPHQDMMFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEEQRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLTERPAAKGKMPATAE
Protein: FAM91 N-terminal domain-containing protein (Q4GYA4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
Sequence:
MTANYHTAELHQALGAGVSYAELCFALQQRMSVAEYQEQAVLFGAMRYWSYRRLPNFVREDVSEEKYYVSMVQHLKARLQLFPYPHVEAVVRYTHETPLVYYTVMIAELLKKERSYDTLPNFTAVDVLNCIGIGRNEYLELTREVRSKVRWHVNRGFVKDHLPARLLSTMELTPFCRVLPVDGSAEPRKKSELTKEELLMHNHLLQCYKDQDSKDSSGETIVKNPENIRSKNGGSGGPEVKKVEGDFGRMGSQCGAVSAASASSPRTPLGAPPSAHSGASVAADGTPIVPSPKSADDAASIAHRCCYACELSRVELLGLYHKGLVCTILDVSIEDQIVVPPLEHFVMNRTSDDPIEVLLYKVLGTIDDRTSLRQLAKLLVLEEEDLCLAVQMCIRLRLAQPRTNRIPKDFEPFVERVHTSWSELVQPFLTEESSSPVAETESTDGFGVIVGDDINSGALADSLVESSWQPSIDTEGLDIAVHFDGDCIKNSSNEVNVQSIISNACGTEGQPAKRLVLLYDTSLLGFLMMTNLSTDPSFRQHVVTLFEMGKLSDETMGGFIEKLEQVQGARAECGLFGEAAQYVQNVLSLREVVKKLRQVVGPEGEQGLDMLKVESVNEQDPTTRYSLLARNYWAYFVASPVAQAPLIDVSIKGVYGSSVSLMPSPWMMLFLYEKVHMGPPSVLLPVGLPLFAWPPALQDSRKRCVAKLRLQPFMVNAEVTYAEVATSLILANEMTATAPLFVQRVVDVPLEIPAPSAMAAAAAEAAYEDGGLEGDVTCAMNGVVVESPFHMLLTVLVPFTASDDEAVELLCKAVQHKKPSVAALRFISNQTRNTTTFTPQVNDTNNTIISEEGVASDGGCDTPTADVEESDKVVTPRASASVMEETHPMMYVECFRSAVEALQLQDSLGHFNFHVSLYEVGNTSTDSGNAYLFRVDAAHIVDMGLGIALADQPCCELMVKHLEGLLSESRMEAHSKAMLQLSREMGNFLERHSTLTTTEREHMALQSAAIAGPLTQQHVRRLGEKGNSGAPFPNCVLLFDGERLSAIDDWDPLVELWQV
Protein: Protein YdeP (P77561)
Organism: Escherichia coli (strain K12)
Function: Probably involved in acid resistance.
Interaction partners:
- HTH-type transcriptional regulator YdeO
- Sulfur carrier protein FdhD
- Formyl-CoA:oxalate CoA-transferase
- Oxalyl-CoA decarboxylase
- Protein YfdX
- DNA-binding transcriptional activator EvgA
- Two-component-system connector protein SafA
- Uncharacterized protein YbfB
- Acetyl-CoA:oxalate CoA-transferase
Sequence:
MKKKIESYQGAAGGWGAVKSVANAVRKQMDIRQDVIAMFDMNKPEGFDCPGCAWPDPKHSASFDICENGAKAIAWEVTDKQVNASFFAENTVQSLLTWGDHELEAAGRLTQPLKYDAVSDCYKPLSWQQAFDEIGARLQSYSDPNQVEFYTSGRTSNEAAFLYQLFAREYGSNNFPDCSNMCHEPTSVGLAASIGVGKGTVLLEDFEKCDLVICIGHNPGTNHPRMLTSLRALVKRGAKMIAINPLQERGLERFTAPQNPFEMLTNSETQLASAYYNVRIGGDMALLKGMMRLLIERDDAASAAGRPSLLDDEFIQTHTVGFDELRRDVLNSEWKDIERISGLSQTQIAELADAYAAAERTIICYGMGITQHEHGTQNVQQLVNLLLMKGNIGKPGAGICPLRGHSNVQGDRTVGITEKPSAEFLARLGERYGFTPPHAPGHAAIASMQAICTGQARALICMGGNFALAMPDREASAVPLTQLDLAVHVATKLNRSHLLTARHSYILPVLGRSEIDMQKNGAQAVTVEDSMSMIHASRGVLKPAGVMLKSECAVVAGIAQAALPQSVVAWEYLVEDYDRIRNDIEAVLPEFADYNQRIRHPGGFHLINAAAERRWMTPSGKANFITSKGLLEDPSSAFNSKLVMATVRSHDQYNTTIYGMDDRYRGVFGQRDVVFMSAKQAKICRVKNGERVNLIALTPDGKRSSRRMDRLKVVIYPMADRSLVTYFPESNHMLTLDNHDPLSGIPGYKSIPVELEPSN
Protein: NAD-dependent epimerase/dehydratase domain-containing protein (Q22945)
Organism: Caenorhabditis elegans
Interaction partners:
- Aminotransferase class I/classII large domain-containing protein
- L-serine deaminase
- Uncharacterized protein R102.4
- Domain of unknown function DB domain-containing protein
- Serine racemase
- Mucin-5AC
- Ubiquitin-like domain-containing protein
- Transthyretin-like protein 15
- Fatty acid synthase
- Isovaleryl-CoA dehydrogenase, mitochondrial
Sequence:
MKNLRVFGRIHNARRNYSPLPVDPLLRFKTISQTQKAPRVLITGSLGQLGRGLNSVYKYMYGSECVVMSDIVRLPANATDVSDYNYLDILNQGSIEEIVVNKNIDTIVHFSALLSAVGETNVPLALQVNCRGVENILQVAAKHKLKVFIPSTIGAFGPTTPRENTPDLTVQCPTTIYGVSKVYAERLGEYFNHRFGVDFRSMRFPGIISATKPGGGTTDYAIQIFYDALQKGKHTCYLRPDTRLPMMYDTDCMASVIQLLAADSQSLKRRTYNVTGFSFTPEEIADAIRRVMPGFEIDYDICPTRQSIADSWPMSLDDSEARKDWGWNPEYGLDETVQVMFALLRREEDKPTKIVSTA
Protein: Serine and arginine rich splicing factor 7 (C9JAB2)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MSRYGRYGGETKVYVGNLGTGAGKGELERAFSYYGPLRTVWIARNPPGFAFVEFEDPRDAEDAVRGLDGKVICGSRVRVELSTGMPRRSRFDRPPARRPFDPNDRCYECGEKGHYAYDCHRYSRRRRSRSRSRSHSRSRGRRYSRSRSRSRGRRSRSASPRRSRSISLRRSRSASLRRSRSGSIKGSRSPSRSRSRSRSISRPRSSRSKSRSPSPKRSRSPSGSPRRSASPERMD
Protein: Protein indeterminate-domain 5, chloroplastic (ID1-like zinc finger protein 2) (Q9ZUL3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor acting as a positive regulator of the starch synthase SS4. Controls chloroplast development and starch granule formation. Binds DNA via its zinc fingers. Recognizes and binds to SCL3 promoter sequence 5'-AGACAA-3' to promotes its expression when in complex with RGA.
Subcellular location: Plastid, chloroplast {ECO:0000305|PubMed:16934950}.
Interaction partners:
- At1g70770
- Zinc finger CCCH domain-containing protein 52
Sequence:
MAASSSSAASFFGVRQDDQSHLLPPNSSAAAPPPPPPHHQAPLPPLEAPPQKKKRNQPRTPNSDAEVIALSPKTLMATNRFICEVCNKGFQREQNLQLHRRGHNLPWKLKQKSTKEVKRKVYLCPEPSCVHHDPSRALGDLTGIKKHYYRKHGEKKWKCDKCSKRYAVQSDWKAHSKTCGTKEYRCDCGTLFSRRDSFITHRAFCDALAQESARHPTSLTSLPSHHFPYGQNTNNSNNNASSMILGLSHMGAPQNLDHQPGDVLRLGSGGGGGGAASRSSSDLIAANASGYFMQEQNPSFHDQQDHHHHHQQGFLAGNNNIKQSPMSFQQNLMQFSHDNHNSAPSNVFNLSFLSGNNGVTSATSNPNAAAAAAVSSGNLMISNHYDGENAVGGGGEGSTGLFPNNLMSSADRISSGSVPSLFSSSMQSPNSAPHMSATALLQKAAQMGSTSSNNNNGSNTNNNNNASSILRSFGSGIYGENESNLQDLMNSFSNPGATGNVNGVDSPFGSYGGVNKGLSADKQSMTRDFLGVGQIVKSMSGSGGFQQQQQQQQQQQQQQQHGNSRERVGSSSDSADRSSMNVNTGGGPASTSPPYGIHHASF
Protein: Histone deacetylase-like amidohydrolase (HDAH) (EC 3.5.1.-) (Acetylated lysine deacetylase) (Histone deacetylase homolog PA3774) (Q9HXM1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Probable protein deacetylase that catalyzes deacetylation of acetylated lysine residues. In vitro, exhibits high activity against artificial HDAC (histone deacetylase) substrates containing acetylated and trifluoroacetylated lysine residues. Is not able to deacetylate acetylated polyamines.
Interaction partners:
- Bis
- Major facilitator superfamily
- Methionine aminopeptidase
- Methionine aminopeptidase
- Tryptophan 2-monooxygenase
- Uncharacterized protein
- Transporter
Sequence:
MTRRTAFFFDELCLWHAAGPHALTLPVGGWVQPPAAAGHAESPETKRRLKSLLDVSGLTARLQLRSAPPASDEDLLRVHPAHYLERFKALSDAGGGSLGQDAPIGPGSYEIARLSAGLAIAALDAVLAGEADNAYSLSRPPGHHCLPDQAMGFCFFANIAVAIEAAKARHGVERVAVLDWDVHHGNGTQAIYYRRDDVLSISLHQDGCFPPGYSGAEDIGEDRGRGFNLNVPLLPGGGHDAYMQAMQRIVLPALERFRPQLIVVASGFDANAVDPLARMQLHSDSFRAMTAMVRDAAERHAGGRLVVVHEGGYSEAYVPFCGLAVIEELSGVRSAVRDPLRDFIELQQPNAAFRDFQRQRLEELAAQFGLCPAQPLQAAR
Protein: CcsA (C5MRI8)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MLFATLEHILTHISFSTISIVITIHLITLLVRELGGLRDSSEKGMIATFFCITGFLVSRWASSGHFPLSNLYESLIFLSWALYILHMIPKIQNSKNDLSTITTPSTILTQGFATSGLLTEMHQSTILVPALQSQWLMMHVSMMLLSYATLLCGSLLSAALLMIRFRKNLDFFSKKKKNVLSKTFFFNEIEYFYAKRSALKSTFFPLFPNYYKYQLIERLDSWSYRVISLGFTLLT
Protein: Cutinase (EC 3.1.1.74) (KrCUT) (A6WFI5)
Organism: Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216)
Function: Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle. Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters). Can depolymerize synthetic polyesters such as poly(epsilon-caprolactone) (PCL) and poly(1,3-propylene adipate) (PPA). Exhibits some activity on poly(lactic acid) (PLA). Can bind but not hydrolyze poly(hydroxybutyrate) (PHB).
Subcellular location: Secreted {ECO:0000305|PubMed:34705546}.
Interaction partners:
- Protein tyrosine/serine phosphatase
- Sulphate transporter
Sequence:
MLRARPSHRLASAAAVVAATGAALLAGSSPAAAATCSDVDVVFARGTGETPGLGVVGGPFVRSLTGELSDRTVTSHAVDYAASSSQASAGPGATAMSAHVREVAAACPSTRFVLGGYSQGATVTDIALGIRTGTTTGTPVPAELAGRVAAVVVFGNPLGLSGRTIATASSTYGPKSKDYCNSSDSVCGSAPKTGTGGHLSYASNGSTTDGARFAAGLVRAAGTPTTPTPTPTPTPVPTTCVRDSTRDHVAADRAVSLYGRAYARGSRDSLGATSSYNVVSLQQVEGGWRLVTAC
Protein: Chaperonin CPN60-like 1, mitochondrial (HSP60-like 1) (Q8L7B5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Heat shock 70 kDa protein 10, mitochondrial
- Heat shock 70 kDa protein 9, mitochondrial
- 20 kDa chaperonin, chloroplastic
- T-complex protein 1 subunit alpha
- U-box domain-containing protein 5
- HSP20-like chaperones superfamily protein
- Protein groES
- T-complex protein 1 subunit theta
- Endoplasmin homolog
- ATP binding protein
Sequence:
MYRLVSNVASKARIARKCTSQIGSRLNSTRNYAAKDIRFGVEARALMLRGVEDLADAVKVTMGPKGRNVIIEQSWGAPKVTKDGVTVAKSIEFKDRIKNVGASLVKQVANATNDVAGDGTTCATVLTRAIFTEGCKSVAAGMNAMDLRRGIKLAVDTVVTNLQSRARMISTSEEIAQVGTISANGDREIGELIAKAMETVGKEGVITIQDGKTLFNELEVVEGMKIDRGYISPYFITNPKTQKCELEDPLILIHEKKISNINAMVKVLELALKKQRPLLIVAEDVESDALATLILNKLRANIKVCAVKAPGFGENRKANLHDLAALTGAQVITEELGMNLDNIDLSMFGNCKKVTVSKDDTVVLDGAGDKQAIGERCEQIRSMVEASTSDYDKEKLQERLAKLSGGVAVLKIGGASETEVSEKKDRVTDALNATKAAVEEGIVPGGGVALLYASKELEKLSTANFDQKIGVQIIQNALKTPVYTIASNAGVEGAVVVGKLLEQDNPDLGYDAAKGEYVDMIKAGIIDPLKVIRTALVDAASVSSLLTTTEAVVTEIPTKEVASPGMGGGGMGGMGGMGGMGGMGF
Protein: 2-oxoglutarate dehydrogenase, mitochondrial (OGDH) (EC 1.2.4.2) (2-oxoglutarate dehydrogenase complex component E1) (OGDC-E1) (OGDHC subunit E1) (Alpha-ketoglutarate dehydrogenase complex subunit E1) (alpha-KGDHC subunit E1) (P20967)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components: 2-oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:25165143}. Mitochondrion matrix. Mitochondrion matrix, mitochondrion nucleoid.
Interaction partners:
- Dihydrolipoyl dehydrogenase, mitochondrial
- Succinate--CoA ligase subunit alpha, mitochondrial
- Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Succinate--CoA ligase subunit beta, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Isocitrate dehydrogenase, mitochondrial
- Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial
- Isocitrate dehydrogenase cytoplasmic
- Isocitrate dehydrogenase
Sequence:
MLRFVSSQTCRYSSRGLLKTSLLKNASTVKIVGRGLATTGTDNFLSTSNATYIDEMYQAWQKDPSSVHVSWDAYFKNMSNPKIPATKAFQAPPSISNFPQGTEAAPLGTAMTGSVDENVSIHLKVQLLCRAYQVRGHLKAHIDPLGISFGSNKNNPVPPELTLDYYGFSKHDLDKEINLGPGILPRFARDGKSKMSLKEIVDHLEKLYCSSYGVQYTHIPSKQKCDWLRERIEIPEPYQYTVDQKRQILDRLTWATSFESFLSTKFPNDKRFGLEGLESVVPGIKTLVDRSVELGVEDIVLGMAHRGRLNVLSNVVRKPNESIFSEFKGSSARDDIEGSGDVKYHLGMNYQRPTTSGKYVNLSLVANPSHLESQDPVVLGRTRALLHAKNDLKEKTKALGVLLHGDAAFAGQGVVYETMGFLTLPEYSTGGTIHVITNNQIGFTTDPRFARSTPYPSDLAKAIDAPIFHVNANDVEAVTFIFNLAAEWRHKFHTDAIIDVVGWRKHGHNETDQPSFTQPLMYKKIAKQKSVIDVYTEKLISEGTFSKKDIDEHKKWVWNLFEDAFEKAKDYVPSQREWLTAAWEGFKSPKELATEILPHEPTNVPESTLKELGKVLSSWPEGFEVHKNLKRILKNRGKSIETGEGIDWATGEALAFGTLVLDGQNVRVSGEDVERGTFSQRHAVLHDQQSEAIYTPLSTLNNEKADFTIANSSLSEYGVMGFEYGYSLTSPDYLVMWEAQFGDFANTAQVIIDQFIAGGEQKWKQRSGLVLSLPHGYDGQGPEHSSGRLERFLQLANEDPRYFPSEEKLQRQHQDCNFQVVYPTTPANLFHILRRQQHRQFRKPLALFFSKQLLRHPLARSSLSEFTEGGFQWIIEDIEHGKSIGTKEETKRLVLLSGQVYTALHKRRESLGDKTTAFLKIEQLHPFPFAQLRDSLNSYPNLEEIVWCQEEPLNMGSWAYTEPRLHTTLKETDKYKDFKVRYCGRNPSGAVAAGSKSLHLAEEDAFLKDVFQQS
Protein: Esculentin-2SN1 (E7EKI0)
Organism: Sylvirana spinulosa (Fine-spined frog) (Hylarana spinulosa)
Function: Antimicrobial peptide. Active against some Gram-negative and a variety of Gram-positive bacterial strains. Not active against fungi. Shows very weak hemolytic activity against human erythrocytes.
Subcellular location: Secreted {ECO:0000269|PubMed:24055160}.
Interaction partners:
Sequence:
MFTMKKSLLFLFFLGTISLSLCEQERGADEDDGGEEVKRGIFSLFKAGAKFFGKNLLKEAGKAGAEHLACKAANQC
Protein: NFAT activation molecule 1 (Calcineurin/NFAT-activating ITAM-containing protein) (NFAT-activating protein with ITAM motif 1) (Q8NET5)
Organism: Homo sapiens (Human)
Function: May function in immune system as a receptor which activates via the calcineurin/NFAT-signaling pathway the downstream cytokine gene promoters. Activates the transcription of IL-13 and TNF-alpha promoters. May be involved in the regulation of B-cell, but not T-cell, development. Overexpression activates downstream effectors without ligand binding or antibody cross-linking.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Partially recruited to lipid rafts upon BCR stimulation. {ECO:0000250}.
Interaction partners:
- Leucine-rich repeat-containing protein 25
Sequence:
MENQPVRWRALPGLPRPPGLPAAPWLLLGVLLLPGTLRLAGGQSVTHTGLPIMASLANTAISFSCRITYPYTPQFKVFTVSYFHEDLQGQRSPKKPTNCHPGLGTENQSHTLDCQVTLVLPGASATGTYYCSVHWPHSTVRGSGTFILVRDAGYREPPQSPQKLLLFGFTGLLSVLSVVGTALLLWNKKRMRGPGKDPTRKCPDPRSASSPKQHPSESVYTALQRRETEVYACIENEDGSSPTAKQSPLSQERPHRFEDDGELNLVYENL
Protein: Cytokine-like nuclear factor N-PAC (NPAC) (3-hydroxyisobutyrate dehydrogenase-like protein) (Glyoxylate reductase 1 homolog) (Nuclear protein NP60) (Nuclear protein of 60 kDa) (Nucleosome-destabilizing factor) (hNDF) (Putative oxidoreductase GLYR1) (Q49A26)
Organism: Homo sapiens (Human)
Function: Cytokine-like nuclear factor with chromatin gene reader activity involved in chromatin modification and regulation of gene expression. Acts as a nucleosome-destabilizing factor that is recruited to genes during transcriptional activation. Recognizes and binds histone H3 without a preference for specific epigenetic markers and also binds DNA. Interacts with KDM1B and promotes its histone demethylase activity by facilitating the capture of H3 tails, they form a multifunctional enzyme complex that modifies transcribed chromatin and facilitates Pol II transcription through nucleosomes. Stimulates the acetylation of 'Lys-56' of nucleosomal histone H3 (H3K56ac) by EP300. With GATA4, co-binds a defined set of heart development genes and coregulates their expression during cardiomyocyte differentiation. Regulates p38 MAP kinase activity by mediating stress activation of MAPK14/p38alpha and specifically regulating MAPK14 signaling. Indirectly promotes phosphorylation of MAPK14 and activation of ATF2. The phosphorylation of MAPK14 requires upstream activity of MAP2K4 and MAP2K6.
Subcellular location: Nucleus {ECO:0000269|PubMed:16352664}. Chromosome {ECO:0000269|PubMed:29759984, ECO:0000269|PubMed:30970244}. Note=Found in actively RNAPolII-transcribed gene bodies. {ECO:0000269|PubMed:30970244, ECO:0000269|PubMed:31408337}.
Interaction partners:
- AOF1 protein
- Histone H2A type 1-C
- Histone H2B type 1-O
- Histone H2B type 1-J
- Histone H3.1
- Lysine-specific histone demethylase 1A FAD-dependent demethylase 1A)
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Histone H3.3
- Histone H3.3C
Sequence:
MAAVSLRLGDLVWGKLGRYPPWPGKIVNPPKDLKKPRGKKCFFVKFFGTEDHAWIKVEQLKPYHAHKEEMIKINKGKRFQQAVDAVEEFLRRAKGKDQTSSHNSSDDKNRRNSSEERSRPNSGDEKRKLSLSEGKVKKNMGEGKKRVSSGSSERGSKSPLKRAQEQSPRKRGRPPKDEKDLTIPESSTVKGMMAGPMAAFKWQPTASEPVKDADPHFHHFLLSQTEKPAVCYQAITKKLKICEEETGSTSIQAADSTAVNGSITPTDKKIGFLGLGLMGSGIVSNLLKMGHTVTVWNRTAEKCDLFIQEGARLGRTPAEVVSTCDITFACVSDPKAAKDLVLGPSGVLQGIRPGKCYVDMSTVDADTVTELAQVIVSRGGRFLEAPVSGNQQLSNDGMLVILAAGDRGLYEDCSSCFQAMGKTSFFLGEVGNAAKMMLIVNMVQGSFMATIAEGLTLAQVTGQSQQTLLDILNQGQLASIFLDQKCQNILQGNFKPDFYLKYIQKDLRLAIALGDAVNHPTPMAAAANEVYKRAKALDQSDNDMSAVYRAYIH
Protein: Yip1-interacting factor 1, isoform C (Q8IMR4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004653}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004653}.
Interaction partners:
- Protein YIPF
- PRA1 family protein
- Syntaxin-5
- Protein YIPF
Sequence:
MNYNPNPGMRNRKWENSSAAGRPRPPKRVSDVNAMGPSAPMMGGGATFMAPPTGPGILDPNMYGAPAPAPVNSYGFDPNLGQPSQHIQQPPQQQPGYGYGAPPPQQAAGPPTYGIGAPQPVAPPTGQYPQFAMFQQPIVQDMAMQYGQKLADQGKQIMENQFEKWVPVAKLKYYFAVDNAYVGRKLRLLFFPYMHKDWSLRYDQEHPVQPRYDVNAPDLYLPTMGYITYVIVAGLLLGMQKRFSPEQLGIQASSAMAYSIFELVIYSLALYVMNVKTSLKTLDLLAFTGYKYVNIVVCLMVSTLFFKSGYYIALAYTSFSFGFFMLRTLRTKLLQDNSPAAPSGAINYDPYGNPQQFDYSGGKKRKLYFLFMIVAGQALFAFLLSKHLYLPEAEVLTVPKTF
Protein: Protein ORANGE, chloroplastic (BoOr) (DnaJ-like cysteine-rich domain-containing protein Or) (A2T1U1)
Organism: Brassica oleracea var. botrytis (Cauliflower)
Function: Involved in chromoplast differentiation. Is associated with a cellular process that triggers the differentiation of pro-plastids or other non-colored plastids into chromoplasts for carotenoid accumulation. Associated with carotenoid accumulation in de-etiolated cotyledons. Controls leaf petiole elongation by suppressing the expression of ERF1 genes.
Subcellular location: Plastid, chloroplast membrane {ECO:0000305}. Plastid {ECO:0000269|PubMed:17172359}. Nucleus {ECO:0000269|PubMed:21175633}. Note=Targeted to non-green plastids. {ECO:0000269|PubMed:17172359}.
Interaction partners:
Sequence:
MSCLGRILSVSYPPDPYGSRLSVSKLSSPGRNRRLRWRFTALDSDSSSLDSDSSDKFAAGFCIIEGPETVQDFAKMQLQEIQDNIRSRRNKIFLHMEEVRRLRIQQRIRNTELGIIDEEQEHELPNFPSFIPFLPPLTAANLRVYYATCFSLIAGIILFGGLLAPTLELKLGIGGTSYKDFIQSLHLPMQLSQVDPIVASFSGGAVGVISALMVVEVNNVKQQEHKRCKYCLGTGYLACARCSSTGSLIISEPVSAIAGGNHSVSTSKTERCSNCSGAGKVMCPTCLCTGMAMASEHDPRIDPFL
Protein: GP63 (Peptidase M8, leishmanolysin family protein) (Q6TU47)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Aspartate--tRNA ligase, mitochondrial
Sequence:
MQKIIYLSIVLLVVSLFLISIGFSSPTLFNNNNNNNNNENENNKLLNNNVNKEINNIINKGYQKMVDGLKLKSQFHYNEDKYMKRAMEKQQHNPLGYKCQHDSIVQKRINKLKLKSADDNNNGENLKTKTVTEKLVKDAKALEASATTVSATTASQPIRFQFDTSYITGTKDKYACHNVGDVISVGFSSGATKPCEPDGSVEVCLYTCTEADIQTTQLQNFYKNNIIETIKEVFQSRLLVRNPQNSFTFNPAATDGTCDYGVPIPDSYYTDGIENTDIYVWVTSRPTSSNNTIAYAFACDYDTTNNILGRPRAASINFNPIYFSPFIGAENSISFNEYVRVGIHEMTHALGFSSSFFDSFVKPNTADVIRDGTGAAENFKFSGKTPSGESYSVTKSAIYSDHVVNFAKQHYGCNDLKHQELEDFGGSGTAGSHWEARTAGEEYMLGFVSPVMPITDLSFNLLLDSGWYEIVTNSSEPLIWGKGLGCDFVQKPCSTSTWNYQGYFCTENGASSCTGTRMGKGVCRIVTGQNEWLPQYQHLDNPKLVGYNLAADGCPFYSVQDNNVYCFDTSKQSTANSQVFEEYCENCRCFEFKDGNDGSIQQSCWEQRCGSNGLQIKINNNWVDCPDSQTIVSSGVTVVCPTGYTICGGDPKPVIVTGSSGIKILPYFILISSLIILIYLLI
Protein: Esculentin-1SEb (P85054)
Organism: Lithobates sevosus (Dusky gopher frog) (Rana sevosa)
Function: Mast cell degranulating peptide. Causes histamine release from rat peritoneal mast cells in vitro. Has antibacterial activity against the Gram-negative bacterium E.coli K12 and Gram-positive bacterium M.luteus NCT C2665.
Subcellular location: Secreted {ECO:0000269|PubMed:16386333}.
Interaction partners:
Sequence:
GLFSKFNKKKIKSGLFKIIKTAGKEAGLEALRTGIDVIGCKIKGEC
Protein: Lrp3 protein (Q52KH0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MTRLEAEFVRREAPPSYGQLIAQGLIPPVEDFPVYSASQASVLQNLRTAMRRQMRRHASRRGPSRRRLGRLWNRLFHRPRAPRGQIPLLTAARTSQTVLGDGLLQAAPGPVPEPPAPNTDTGSPREAGDGPPSGSGHAPEVGPSVPPPPLNLRDPEYRPEDKERKACVEPLEDSPAPVDTPPEPCLAQDPHPQTPTASGTQDPHSAEPLGVCRSPPPPCSPILEASDDEALLVC
Protein: Brix domain-containing protein C4F8.04 (O14180)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Ribosome biogenesis protein nsa1
- Protein mak16
- Probable rRNA-processing protein ebp2
- Uncharacterized RNA-binding protein C1827.05c
- Ribosome biogenesis protein brx1
- Ribosomal RNA-processing protein 1 homolog
- 60S ribosome subunit biogenesis protein nip7
- Ribosome biogenesis protein ytm1
- Pescadillo homolog
- Ribosome biogenesis protein erb1
Sequence:
MGKIKNKIVRQQQYMKALHQKNKDKLERRKERAKEEEKDPEKKRLRLSENIPATIESKRVYDETIIEDKPDEELQAELKDDEFSAYFSEERKVPKLLVTTSKRASRKCYDFASELLDCFPNAEFRKRTGDIEVHEIAEAAAKRGYTDLLVLNEDRKKTNALTLVHLPNGPSFYFTLSNLQTAKEISNHGRSTGHIPELIINNFSTRLGMTVARAFQSLFIQTPQIQGRQVVTIHCQRDFLFFRRHRYAFREKSNMPDGIGTGLQELGPRFTMRLRMVQKGVWDRKEGEVFFESNAGEESDRRKFWL
Protein: Pre-mRNA-processing factor 39 (PRP39 homolog) (Q86UA1)
Organism: Homo sapiens (Human)
Function: Involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- U1 small nuclear ribonucleoprotein C
- Cell division cycle 5-like protein
- Small nuclear ribonucleoprotein-associated protein N
- tRNA selenocysteine 1-associated protein 1
- RNA-binding protein 25
- Splicing factor 3B subunit 1
- U1 small nuclear ribonucleoprotein 70 kDa
- Small nuclear ribonucleoprotein Sm D1
- Small nuclear ribonucleoprotein F
- U2 small nuclear ribonucleoprotein A'
Sequence:
MQNSHMDEYRNSSNGSTGNSSEVVVEHPTDFSTEIMNVTEMEQSPDDSPNVNASTEETEMASAVDLPVTLTETEANFPPEYEKFWKTVENNPQDFTGWVYLLQYVEQENHLMAARKAFDRFFIHYPYCYGYWKKYADLEKRHDNIKPSDEVYRRGLQAIPLSVDLWIHYINFLKETLDPGDPETNNTIRGTFEHAVLAAGTDFRSDRLWEMYINWENEQGNLREVTAIYDRILGIPTQLYSHHFQRFKEHVQNNLPRDLLTGEQFIQLRRELASVNGHSGDDGPPGDDLPSGIEDITDPAKLITEIENMRHRIIEIHQEMFNYNEHEVSKRWTFEEGIKRPYFHVKPLEKAQLKNWKEYLEFEIENGTHERVVVLFERCVISCALYEEFWIKYAKYMENHSIEGVRHVFSRACTIHLPKKPMVHMLWAAFEEQQGNINEARNILKTFEECVLGLAMVRLRRVSLERRHGNLEEAEHLLQDAIKNAKSNNESSFYAVKLARHLFKIQKNLPKSRKVLLEAIERDKENTKLYLNLLEMEYSGDLKQNEENILNCFDKAVHGSLPIKMRITFSQRKVEFLEDFGSDVNKLLNAYDEHQTLLKEQDSLKRKAENGSEEPEEKKAHTEDTTSSSTQMIDGDLQANQAVYNYSAWYQYNYQNPWNYGQYYPPPPT