wanglab/gogpt-training-data huggingface dataset:
Protein: Actin-related protein 2/3 complex subunit 1A (Actin-related protein C1) (Actin-related protein C1A) (Arp2/3 complex 41 kDa subunit) (p41-ARC) (O80856)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 2A
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 4
- Actin-related protein 2/3 complex subunit 2B
- Actin-related protein 3
- Actin-related protein 2
- Actin-related protein 2/3 complex subunit 5A
- Actin-related protein 2/3 complex subunit 5B
- Uncharacterized protein
- At4g14145
Sequence:
MAVVDVHRFAESITCHAWSPDLSMVALCPNNTEVHIYKSLSQDHWERLHVLQKHDQIVSGIDWSSKSNKIVTVSHDRNSYVWSLEGAEWVPTLVILRLNRAALCVQWSPKENKFAVGSGAKTVCICYYEQENNWWVSKLIRKRHESSVTSVAWHPNNVLLATTSTDGKCRVFSTFIKGVDTKDSKAGSPAETKFGEQILQLDLSYSWAFGVKWSPSGNTLAYVGHSSMIYFVDDVGPSPLAQSVAFRDLPLRDVLFISEKMVIGVGYDSNPMVFASDDTGIWSFIRYIGEKKAASSNSSYSSQFSEAFGKFYGSQSKSTTANDASESRGGVHDNCINSIVSLSKAGSPKVMRFSTSGLDGKVAIWDLENMEQELGNQF
Protein: Putative aldehyde dehydrogenase-like protein C9E9.09c (EC 1.2.1.-) (O14293)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable acetyl-coenzyme A synthetase
- Alcohol dehydrogenase
- Probable pyruvate decarboxylase Pdc101
- Putative pyruvate decarboxylase C13A11.06
- Probable pyruvate decarboxylase C186.09
- Alcohol dehydrogenase 4
- Putative pyruvate decarboxylase C3G9.11c
- Probable S-
- 4-aminobutyrate aminotransferase
- Putative S-
Sequence:
MSTKLVDHVEITVPTGKTYIQPVGLFINNQHVDSVHGGRVKVYSPSTEKLICEVADADEEDVDIAVKVARAAFQTDAPWRKFSSAQRGRCLSRLADCIEQNLEYLASIETLDNGKSITLARGDVQAAADCFRYYGGWADKDYGQTIETDIKRFAYTRHEPIGVCGQIIPWNFPFLMCAWKIAPAVACGNTIILKTAELTPLSALCLTKFVPECGFPPGVINVLSGDGRRCGNAISSHMDIDKVAFTGSTGVGRMVMRAAASSNLKKVTLELGGKSPNIVFNDADLDSAAVWTNYGIFYNSGQVCCAGSRVYVQEDVYDEFIKRMVAKAKTLKVGDPFAEDTFQGAQVSKQQYERIVSYIESGIAHGAKLEIGGKRHGNLGYFVEPTILSNVTEDMAVGKEEIFGPVLAVIKFKTIEEAIRRGNNSTYGLAAGVHTNNITNAIKVSNALEAGTVWVNCYNLLHHQIPFGGYKESGIGRELGSYGLTNYTQTKAVHINLGMDSPI
Protein: CCAAT-binding factor domain-containing protein (Q386U7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Nucleolar complex protein 2
- rRNA biogenesis protein, putative
- RNA-binding protein, putative
- ATP-dependent DEAD/H RNA helicase, putative
- Ribosome production factor 2 homolog
- Nucleolar protein, putative
- Nucleolar GTP-binding protein 1
- Pescadillo homolog
- Peter pan protein, putative
- CCAAT-binding factor domain-containing protein
Sequence:
MTREEEVLDLGKRWYERPLPLRVCSLKEVANDTTTKEEMDAMFSEARDILNQATNRGHSDKGRWYNTQFISRGTTSDKIASAAVKLSDTDFMFFLEGFNLLFDTARTDTHHYEAALKALAVIWTKLMPRRPLKRFFSQFFATLPANPADRKVVLVYWYLEDYLKRTYAQFLSLAEAMLKDRLQQRREAWLDVVGKLICNVAESRHVAMALMVDKLGDPAARVAHNAYHHLLALLRDSSIHQGVLFVELEKVIFMKNCPKSTMKYATNVMNQFVYNKDERKLALKAIQTYLSIFRQLAISGSVDLSVTTATIVGLRRAFPYAGTDVASLEEHLNALFVIANTGNFTQRVTTMSLLQLVALGKSATEEFRNRWYRALYKLLLISPKQVSHSAHITGFFSMLHKAVRLDTNDDRIAAFIHRLLQRALFFHESMICAILLLVGDVLQAHPRLRSVILGSRRPPVVPAEERYDVKHREPQYARAKNECLYTLGVLARHSHPSVVQLAVMLLFGEEIIFDSHPLDELTLINFLQMFVDAKAHTQHGIDSDVAAAEAVGKAGSSVFRRATHRANLPSASDPFFINSSVQQVDVSALFLHRYAVQRQRFIDGLSRVRSTWGDASGEADVALRVSDVDASLFGPSGVLGDPAVSKKKNKRAKKKKERLKEKLKEGAVLDECVEAIGSEEVEGGEDNFFDMEGSEGDLEWGSGDEGVMMDDDEDGDDGNERDDDGVGLALSRRENADVDDGEDLAEMLEAHRNVASKKRRREEAWLERVTSAAGTKGPNRRSFVSRRR
Protein: Trafficking protein particle complex subunit 3 (BET3 homolog) (O55013)
Organism: Mus musculus (Mouse)
Function: May play a role in vesicular transport from endoplasmic reticulum to Golgi.
Subcellular location: Golgi apparatus, cis-Golgi network {ECO:0000250}. Endoplasmic reticulum {ECO:0000250}.
Interaction partners:
- Trafficking protein particle complex subunit 5
- Trafficking protein particle complex subunit 2
- Trafficking protein particle complex subunit 4
- Trafficking protein particle complex subunit 6A
- Trafficking protein particle complex subunit 1
- Trafficking protein particle complex subunit 6B
- Trafficking protein particle complex 8
- Trafficking protein particle complex subunit 2-like protein
- Trafficking protein particle complex subunit 10
- Trafficking protein particle complex subunit 9
Sequence:
MSRQANRGTESKKMSSELFTLTYGALVTQLCKDYENDEDVNKQLDRMGYNIGVRLIEDFLARSNVGRCHDFRETADVIAKVAFKMYLGITPSITNWSPAGDEFSLILENNPLVDFVELPDNHSALIYSNLLCGVLRGALEMVQMAVEAKFVQDTLKGDGVTEIRMRFIRRIEDNLPAGEE
Protein: Transcriptional repressor p66-beta (GATA zinc finger domain-containing protein 2B) (p66/p68) (Q8WXI9)
Organism: Homo sapiens (Human)
Function: Transcriptional repressor. Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin. Enhances MBD2-mediated repression. Efficient repression requires the presence of GATAD2A. Targets MBD3 to discrete loci in the nucleus. May play a role in synapse development.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:11756549, ECO:0000269|PubMed:12183469, ECO:0000269|PubMed:16415179}. Nucleus {ECO:0000269|PubMed:27732854, ECO:0000269|PubMed:28977666, ECO:0000269|PubMed:33283408}. Chromosome {ECO:0000269|PubMed:27732854}. Note=Speckled nuclear localization requires both CR1 and CR2 regions (PubMed:16415179). Localizes to sites of DNA damage (PubMed:27732854). {ECO:0000269|PubMed:16415179, ECO:0000269|PubMed:27732854}.
Interaction partners:
- Histone-binding protein RBBP7
- Histone-binding protein RBBP4
- Histone deacetylase 1
- Chromodomain-helicase-DNA-binding protein 4
- Metastasis-associated protein MTA2
- Histone deacetylase 2
- Metastasis-associated protein MTA1
- Chromodomain-helicase-DNA-binding protein 3
- Metastasis-associated protein MTA3
- Transcriptional repressor p66-alpha
Sequence:
MDRMTEDALRLNLLKRSLDPADERDDVLAKRLKMEGHEAMERLKMLALLKRKDLANLEVPHELPTKQDGSGVKGYEEKLNGNLRPHGDNRTAGRPGKENINDEPVDMSARRSEPERGRLTPSPDIIVLSDNEASSPRSSSRMEERLKAANLEMFKGKGIEERQQLIKQLRDELRLEEARLVLLKKLRQSQLQKENVVQKTPVVQNAASIVQPSPAHVGQQGLSKLPSRPGAQGVEPQNLRTLQGHSVIRSATNTTLPHMLMSQRVIAPNPAQLQGQRGPPKPGLVRTTTPNMNPAINYQPQSSSSVPCQRTTSSAIYMNLASHIQPGTVNRVSSPLPSPSAMTDAANSQAAAKLALRKQLEKTLLEIPPPKPPAPLLHFLPSAANSEFIYMVGLEEVVQSVIDSQGKSCASLLRVEPFVCAQCRTDFTPHWKQEKNGKILCEQCMTSNQKKALKAEHTNRLKNAFVKALQQEQEIEQRLQQQAALSPTTAPAVSSVSKQETIMRHHTLRQAPQPQSSLQRGIPTSARSMLSNFAQAPQLSVPGGLLGMPGVNIAYLNTGIGGHKGPSLADRQREYLLDMIPPRSISQSISGQK
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (EC 3.1.4.11) (PLC-154) (Phosphoinositide phospholipase C-beta-1) (Phospholipase C-I) (PLC-I) (Phospholipase C-beta-1) (PLC-beta-1) (P10687)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein-coupled receptors. Regulates the function of the endothelial barrier.
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}. Cytoplasm {ECO:0000269|PubMed:8454637}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-11
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Guanine nucleotide-binding protein subunit alpha-15
- Guanine nucleotide-binding protein subunit alpha
- Protein kinase C beta type
- Guanine nucleotide-binding protein G
- Calmodulin-1
- Protein kinase C gamma type
Sequence:
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKAPKDPKLRELLDVGNIGHLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPDVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNSSLAKKGQMSVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFETSKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPSLACLRIAAYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLMLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETSSEAPSETRTTPAENGVNHTATLAPKPPSQAPHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTELIKEHTTKYNEIQNDYLRRRAALEKSAKKDSKKKSEPSSPDHGSSAIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKPKLQMELEQEYQDKFKRLPLEILEFVQEAMKGKVSEDSNHGSAPPSLASDPAKVNLKSPSSEEVQGENAGREFDTPL
Protein: glycerol kinase (EC 2.7.1.30) (Q961K9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTEGKNLPHSSADVPFRSKELRKQSLIQHTGLVGVIDEGTKTIGFSIYTTPDFKEIAAHRVELSVITPQDGWYEQDPLEMMASINKCAEEAIKQLPEQGFSASDIVTVGITNQRETTIVWDAVTGKPLYNALLWKDIRTSTTVEQIVAKVQDPNHFRSSTGLPISTYFSALKIRWLRDNVPEVRQAIRERRCKAGTVDSWIVWNLTNGALHITDVTNASRTLLMNLETQAWDPVLLKTFGIREEMLPTIHSCSEIFGKITSERSPLRGMTLSGIMGNQQASLLGQMCVKPGQTKNTYRSGCFLLCNTGDKPVFSRHGLLTTVAYKLGPQAPTIYAIEGAVSVAGHALSWLQNKVRILPDSRDAEKYAEMVPTSGDVYFVPAFTGLYAPYWRQNARGIIIGLTQFTRKNHIVRAALESICFQTRDILECMHQECGYEINKLHADGKLTTNNLLMQLQADTIGMPVFRSQLMDSTAFGAAMCAAQADGVNLCQFEPEKRYYENVHYDTFLATTTYVERKERYGKWKRAVERSLGWVIKQKKTREYTEENYRMLSSLPASIFLISSFAMLVHSLAASGQ
Protein: GID complex subunit 7 (Glucose-induced degradation protein 7) (Q9UT85)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GID complex subunit 1
- GID complex subunit 8
- GID complex substrate-recognition subunit 4
- E3 ubiquitin-protein ligase gid2
- Protein yippee-like PJ691.02
- GID complex substrate-recognition subunit 10
- GID complex subunit 9
- SPRY domain-containing protein C285.10c
- GID complex subunit 5
Sequence:
MALDEKFQLEVIHLLLQFLNDYGYDESLKALEKETGLVSETEDVKRLKQAVLQGDWITAEAAFSIMQLRDESKRKEAQFLLQKQRCLELARSGAICEAIYVLQNFESTDFNKEKERLVSIILESNNKSNNELITKNGYGNTRLDLLNQLSEYISPEILLPKRRLEHLLQQAKDYQVSSQVYHNVLKNFSFLSDYKADPSELPTKEYHVFHDHSDEVWQISYSHNGRYLASASKDKTAIIFDVVNLKRVFRLIGHIDTVAYIRWSPDDRYLLSCSCDKSVILWDAFTGEKLRDYKHGFSVSCCCWLPDGLSFITGSPDCHITHWSLNGEILYKWEDVNIYDMALTSDGTKLYIVGFEQLINAEDKHIAIYSVETRECIKKISLQSKVTSICLSKDSKYALTNLEPHTTFLWDLEENRIVRQYMGHKLGNFLIGSCFGGKDDTFVLSGSEDDKIRIWHRESGKLLATLSGHVKCVNYVAYNPVDPYQFASAGDDNTVRIWSNKDNPRRQ
Protein: Adenosine 5'-phosphosulfate reductase (APS reductase) (EC 1.8.4.10) (5'-adenylylsulfate reductase) (Thioredoxin-dependent 5'-adenylylsulfate reductase) (O05927)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000305}.
Interaction partners:
- Sulfite reductase
- Adenylyl-sulfate kinase
- Bifunctional enzyme CysN/CysC
- Sulfate adenylyltransferase subunit 2
- Sulfate/thiosulfate import ATP-binding protein CysA
- Probable sulfite or nitrite reductase
- 3'
- Sulfate transport system permease protein CysW
- Probable oxidoreductase
- Siroheme synthase
Sequence:
MLPFATIPATERNSAAQHQDPSPMSQPFDLPALASSLADKSPQDILKAAFEHFGDELWISFSGAEDVVLVDMAWKLNRNVKVFSLDTGRLHPETYRFIDQVREHYGIAIDVLSPDPRLLEPLVKEKGLFSFYRDGHGECCGIRKIEPLKRKLAGVRAWATGQRRDQSPGTRSQVAVLEIDGAFSTPEKPLYKFNPLSSMTSEEVWGYIRMLELPYNSLHERGYISIGCEPCTRPVLPNQHEREGRWWWEEATHKECGLHAGNLISKA
Protein: RRM domain-containing protein (D5MCQ7)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MNASSAPQQQQQQQQPQQGQAPQQQQQGPPQHQYQQQRPFHGRVQNHMRGSGPFGNSNGYGRYTAPRGDQQHHDSTPLSSTNLYIRGLMPNTNDDLLREMCSKYGNIASTKAIMDKATNNCKGYGFVDFESPQAAAAAVDGLNTEGVQAQMAKLQQQEQDPTNLYIANLPLDFTEQMLETELNKFGMVISTRILRTPDNQSRGVGFARMDSKEKCEVIISALNGGRFDTMSKEGPALLIKQADTGRKSKHSMNNPEMLQRMQYPQVYQSYYGYHPAAVYQQHYDVNSLASQMGGMHVGGGNPQANGGGDMYGAHMYGQNAGGQGGQGVGQGGQVFPADESTINGQDNVFTPLLLSSLNLFSLSILSNQSSLQKKTQCAAARAAINTHVHIVSPLPDPQNLLLFLNPKTIVPF
Protein: Pentatricopeptide repeat-containing protein At1g74900, mitochondrial (Protein ORGANELLE TRANSCRIPT PROCESSING DEFECT 43) (Q9S7R4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the trans-splicing of intron 1 of the mitochondrial nad1 transcript encoding the ND1 subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I).
Subcellular location: Mitochondrion {ECO:0000305}.
Interaction partners:
- Nuclear intron maturase 2, mitochondrial
- Transmembrane 9 superfamily member 4
- Nuclear intron maturase 4, mitochondrial
- Nuclear intron maturase 1, mitochondrial
- DEAD-box ATP-dependent RNA helicase 53, mitochondrial
- RCC1 domain-containing protein RUG3, mitochondrial
- NADH-ubiquinone oxidoreductase chain 1
- NADH-ubiquinone oxidoreductase chain 1
- Transmembrane 9 superfamily member 5
- NADH-ubiquinone oxidoreductase chain 2
Sequence:
MKRLFSKSLCTSAAGANLKPPPADSAAIAKLILSSPNTTHQDDQFLLSTKTTPWTPNLVNSVLKRLWNHGPKALQFFHFLDNHHREYVHDASSFDLAIDIAARLHLHPTVWSLIHRMRSLRIGPSPKTFAIVAERYASAGKPDKAVKLFLNMHEHGCFQDLASFNTILDVLCKSKRVEKAYELFRALRGRFSVDTVTYNVILNGWCLIKRTPKALEVLKEMVERGINPNLTTYNTMLKGFFRAGQIRHAWEFFLEMKKRDCEIDVVTYTTVVHGFGVAGEIKRARNVFDEMIREGVLPSVATYNAMIQVLCKKDNVENAVVMFEEMVRRGYEPNVTTYNVLIRGLFHAGEFSRGEELMQRMENEGCEPNFQTYNMMIRYYSECSEVEKALGLFEKMGSGDCLPNLDTYNILISGMFVRKRSEDMVVAGKLLLEMVERGFIPRKFTFNRVLNGLLLTGNQAFAKEILRLQSKSGSRLLRKFRL
Protein: BARP protein (Q38CV4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSITFHNLWLLLTVLCTAGIRADPSKEECPDLGGYPSADDVLVLCYLAEQLRGLPDTISSALVNAAAASSKAFEAKVQAEEAVELAESKGLNVTKAKEAAVRATLAAEAAATAASNVEINAANISAFSIDFLESANLLLFEVRDAKDVGEDVRIVAQRCTGEANFVTVASLTNALDNVTSLYSVYGKGTASLSMESVALLEELKMLEDGLKKSQVAVSVAADAADQSKLLVDAVEVSGNTAKGAVNNHNTANNESNKATRNKDQDEGRTVGNNDKEFTITSEDYTKKNQGENGDLSSITLTEDSGSSFIAKYPFHLCTIFTFYTLL
Protein: Tetrahydroberberine oxidase (THB oxidase) (EC 1.3.3.8) ((S)-tetrahydroprotoberberine oxidase) (AmSTOX) (F1BVB7)
Organism: Argemone mexicana (Mexican prickly poppy)
Function: Catalyzes the oxidation of different tetrahydroprotoberberines, such as (S)-canadine, (S)-scoulerine and (S)-tetrahydropalmatine.
Interaction partners:
Sequence:
MIPNSSSSSILSLLVLLLFSTSSSWATNSIHEDFLNCLSIYKSSFPIPIYTSKNSSFNTLFRSSARNLRFLSPNSTQKPEFIITPTLESHVQTTVVCSKKHGLDLKVRSGGHDVEGLSYVSDSPYVMIDLVDFRNITVNVKNATAWIQAGSSLGEVYYKVGNESKNTLGFPAGFCPTVGVGGHISGGGFGSLVRKYGLASDQVIDARIVTVNGEILNKETMGKDLYWAIRGGGANNFGVLLSWKVKLVPVTPIVTVATIDRTLEQGATNLVHKWQFVADRLHEDVYIGLTMVTANTSRAGEKTVVAQFSFLFLGNTDRLLQIMEESFPELGLKRNDTTEMSWVESHVYFYRRGQPIEFLWDRDHLTKSFLKVKSDYVREPISKLGLEGIWKRYVGGDSPAMLWTPFGGRMNQISEFESPYPHRAGNIYNIMYVGNWLNENESEKQLNWMRSFYSYMGRYVSKNPRSAYLNYKDLDLGVNDNNVSEYIRYLKARSWGRKYFKNNFEKLVKVKSMVDPDNFFKNKQSIPPIRSWGKELEAINIVI
Protein: Serine/threonine-protein kinase RsbT (EC 2.7.11.1) (Anti-sigma-B factor RsbT) (Switch protein/serine kinase) (P42411)
Organism: Bacillus subtilis (strain 168)
Function: Provides the crucial link between the upstream module (communication of environmental stress) and the downstream module (integration of the environmental signals with signals of energy stress) that compose the signal transduction pathway controlling the sigma-B factor. Phosphorylates and inactivates its specific antagonist protein RsbS thanks to its serine kinase activity. Upon phosphorylation of RsbS, RsbT is released to stimulate RsbU, a PP2C phosphatase, thereby initiating the signaling cascade that ultimately activates sigma-B. The activity of the RsbU phosphatase may be stimulated by a long-lived interaction with RsbT and the serine kinase function of RsbT is not required to directly modify RsbU. Also phosphorylates RsbR thanks to its threonine kinase activity, preventing it to phosphorylate RsbT.
Interaction partners:
- Phosphoserine phosphatase RsbX
- Phosphoserine phosphatase RsbU
- RsbT co-antagonist protein RsbRA
- RsbT antagonist protein RsbS
- Anti-sigma-B factor antagonist
- Serine-protein kinase RsbW
- Blue-light photoreceptor
- RsbT co-antagonist protein RsbRB
- RsbT co-antagonist protein RsbRC
- RsbT co-antagonist protein RsbRD
Sequence:
MNDQSCVRIMTEWDIVAARQLGRNVAKELGFGTVDQARITTAISELARNIYLYAGKGQIGIEQVADRGKKGLKIIAEDQGPGIPDIRKVMEDGFSTSGGLGAGLPGVKRLMDEFSLNSVAGEGTEIQAIKWLR
Protein: 4-trimethylaminobutyraldehyde dehydrogenase (TMABA-DH) (TMABADH) (EC 1.2.1.47) (Aldehyde dehydrogenase family 9 member A1) (EC 1.2.1.3) (Formaldehyde dehydrogenase) (EC 1.2.1.46) (Gamma-aminobutyraldehyde dehydrogenase) (EC 1.2.1.19) (Q9JLJ3)
Organism: Rattus norvegicus (Rat)
Function: Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine with high efficiency (in vitro). Can catalyze the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction, but with low efficiency.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:10702312}. Cytoplasm {ECO:0000269|PubMed:1799975}.
Interaction partners:
- Gamma-butyrobetaine dioxygenase
- All-trans-retinol dehydrogenase [NAD
- Alcohol dehydrogenase class-3
- Peroxisomal bifunctional enzyme
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Acetyl-coenzyme A synthetase
- 4-aminobutyrate aminotransferase, mitochondrial
- Amine oxidase [flavin-containing] B
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Amine oxidase [flavin-containing] A
Sequence:
MSTGTFVVSQPLNYRGGARVEPVDASGTEKAFEPATGREIATFKCSGEKEVNLAVENAKAAFKIWSKKSGLERCQVLLEAARIIKERRDEIAIMETINNGKSIFEARLDVDTSWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCLGIGAWNYPFQIACWKSAPALACGNAMIFKPSPFTPVSALLLAEIYTKAGAPNGLFNVVQGGAATGQFLCQHRDVAKVSFTGSVPTGMKIMEMAAKGIKPITLELGGKSPLIIFSDCNMKNAVKGALLANFLTQGQVCCNGTRVFVQKEIADAFTKEVVRQTQRIKIGDPLLEDTRMGPLINAPHLERVLGFVRSAKEQGATVLCGGEPYAPEDPKLKHGYYMTPCILTNCTDDMTCVKEEIFGPVMSILTFETEAEVLERANDTTFGLAAGVFTRDIQRAHRVAAELQAGTCYINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQLKTVCVEMGDVESAF
Protein: LD08056p (Septin interacting protein 2, isoform B) (Q7KTL5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Salto, isoform A
Sequence:
MSGLKKFQNTEEWRQKLRQFLMTERLPKKPVKMDETKDMRYSLEIDEDLRRPLEARAKKVLAVNSASQRTVNLGEDTMYEAGDLEHLDDGDDSFSAFERMCDKTGSDPDSTLFQYLHSEDRSQVMARARDHSTDDQKEIDALRRMLEAVGTEDDLLENESPVKGAECTHLEDIEAPSRFWDNTLAGMDETSSDSGLTPKALTKVSPVKMVGLLRPSTIIEDSELESSDVSSHTSFQSARTLKTNASSSYETATDTSLSGTLLNVDELFYAAIAKAKPPGMSKGEELELLSDLHGSLRELASLPKDEVEEEEDDIEDTIIELSSSDDEEVQLVPEVKQEDTSRVSSVHGKDHTEQKPAEKSVENKENSLHFNDTMEEMEYMMQKGMEYMAGGAPSVAAVKADCPVLPKTKQSTFVVSPKPEPKSPAVAFLQPSIPLRSSNQPQTVVGSSSTGRKPLNVGLTMEWTKKKFFSAASGIPQRRQNQIKQPYANIVSPIRTYTQKSGTAPLMSTFRPTSSDMLSTLAISELEQESRLCHPKALFATKDETPKSSEAESLIINGIDSAADLLPKKAYISSEIKHVVDERTPLPMPKVPQIQKYLNSAVEPTVMRHDGKMKMPGEAVRNPSSSHIPRRANHSLADLSLASGDVSLYTIRDAQKF
Protein: eIF-4F 25 kDa subunit (Q8MZD6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASAQVQSFDIMKQQDQQHQLNIIHKHHHHHEGVPLESNSPEPIDEEIYQVEYKHPLEHVWTLWYLENDRTKHWRDMLNEITEIDSVETFWSLYHTIKTPAELKIGCDYSVFKKGIKPMWEDEANIKGGRWLVTVSKSAKAELDQIWLDILLLMVGQNFEYSDEICGAVINIRNKSNKISVWTANGSNEMAILEIGQKLKILLHLQSHSLQYQLHSDAMSKFNSGVKSVYTL
Protein: DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) (PEP) (Plastid-encoded RNA polymerase subunit beta) (RNA polymerase subunit beta) (Q6ENI4)
Organism: Oryza nivara (Indian wild rice) (Oryza sativa f. spontanea)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Plastid, chloroplast.
Interaction partners:
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase RpoA/D/Rpb3-type domain-containing protein
- DNA-directed RNA polymerase subunit
- Uncharacterized protein
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerase RBP11-like dimerisation domain-containing protein
- RNA polymerase Rpb4/RPC9 core domain-containing protein
- Uncharacterized protein
- Uncharacterized protein
- DNA-directed RNA polymerase
Sequence:
MLRNGNEGMSTIPGFSQIQFEGFCRFINQGLAEELEKFPTIKDPDHEISFQLFAKGYQLLEPSIKERDAVYESLTYSSELYVSARLIFGFDVQKQTISIGNIPIMNSLGTFIINGIYRIVINQILLSPGIYYRSELDHKGISIYTGTIISDWGGRSELAIDKKERIWARVSRKQKISILVLSSAMGSNLKEILDNVSYPEIFLSFPNAKEKKRIESKEKAILEFYQQFACVGGDLVFSESLCEELQKKFFQQKCELGRIGRRNMNRRLNLDIPQNSTFLLPRDVLAATDHLIGMKFETGILDDDDMNHLKNKRIRSVADLLQDQFGLALGRLQHAVQKTIRRVFIRQSKPTPQTLVTPTSTSILLITTYETFFGTYPLSQVFDQTNPLTQTVHGRKVSCLGPGGLTGRTASFRSRDIHPSHYGRICPIDTSEGINVGLTGSLAIHARIDHWWGSVESPFYEISEKAKKKKERQVVYLSPNRDEYYMIAAGNSLSLNRGIQEEQVVPARYRQEFLTIAWEQIHVRSIFPFQYFSIGGSLIPFIEHNDANRALMSSNMQRQAVPLSRSEKCIVGTGLERQTALDSRVSVIAEREGKIISTNSHKILLSSSGKTISIPLVTHRRSNKNTCMHQKPRVPRGKSIKKGQILAEGAATVGGELALGKNVLVAYMPWEGYNFEDAVLISERLVYEDIYTSFHIRKYEIQTDTTSQGSAEKITKEIPHLEEHLLRNLDRNGVVKLGSWVETGDILVGKLTPQIASESSYIAEAGLLRAIFGLEVSTSKETSLKLPIGGRGRVIDVKWIQRDPLDIMVRVYILQKREIKVGDKVAGRHGNKGIISKILPRQDMPYLQDGTPVDMVFNPLGVPSRMNVGQIFESSLGLAGDLLKKHYRIAPFDERYEQEASRKLVFSELYEASKQTKNPWVFEPEYPGKSRIFDGRTGDPFEQPVLIGKSYILKLIHQVDEKIHGRSTGPYSLVTQQPVRGRAKQGGQRIGEMEVWALEGFGVAHILQEILTYKSDHLIARQEILNATIWGKRVPNHEDPPESFRVLVRELRSLALELNHFLVSQKNFQVNREEV
Protein: KN motif and ankyrin repeat domain-containing protein 2 (D3ZD05)
Organism: Rattus norvegicus (Rat)
Function: Involved in transcription regulation by sequestering in the cytoplasm nuclear receptor coactivators such as NCOA1, NCOA2 and NCOA3 (By similarity). Involved in regulation of caspase-independent apoptosis by sequestering the proapoptotic factor AIFM1 in mitochondria (By similarity). Pro-apoptotic stimuli can induce its proteasomal degradation allowing the translocation of AIFM1 to the nucleus to induce apoptosis (By similarity). Involved in the negative control of vitamin D receptor signaling pathway (By similarity). Involved in actin stress fibers formation through its interaction with ARHGDIA and the regulation of the Rho signaling pathway (By similarity). May thereby play a role in cell adhesion and migration, regulating for instance podocytes migration during development of the kidney (By similarity). Through the Rho signaling pathway may also regulate cell proliferation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q63ZY3}. Mitochondrion {ECO:0000250|UniProtKB:Q63ZY3}.
Interaction partners:
- Rho GDP-dissociation inhibitor 1
- Kinesin-like protein KIF21A
- FERM domain containing kindlin 2
Sequence:
MAQVLHVPAPFPGTPGQASSAAFPNKEPDPPYSVETPYGYRLDLDFLKYVDDIEKGHTLRRVPVQRRPRLGSLPRGPGSWWTSTESLCSDASGDSRHSAYSYCGRGFYPQYGALETRSGTNPRVERTLLDARRRLEDQAAAPSSGGLGSLTPSAAGSTSSLAGVGLLPPTPRSSGLSTPVAPSAGHLAHVREQMAGALRKLRQLEEQVKLIPVLQVKLSVLQEEKRQLTVQLKSQKFLGHPSGTRSRSELCLDLPEAPDDPAVLETRSVGTWVRERDLGIPDGEAALVAKVAVLETQLKKALQELRAAQTQQVDLQPQAWPPPDTQVRVDTVRVVEGPREVEVAASTAAGAPAQRAQSLEPYGAGLKALATSAENTLVFRSHEVVETMCPLPTASTSNMHTAKKISITERNCTGAARMADPPPSPAEPSPSSPYPAAEPENPAPAAQDTTDRELTRPVASQDSQAAEGAGGASLGVQSALKRKEVPADPDVHQRNLQFVGINGGYESSSEDSSTAENSEHESTENEAPEPPVRVLSTAEGPQLRPLGPAVGKTSQDERQLSQESQRVPEAKVAPGPDPEEEIRMDLSPDLISACLALEKYLENPNALTERELKVAYTTVLQEWLRLACRSDAHPELVRRHLVTFRAMSARLLDYVVNIADSNGNTALHYSVSHANFPVVRQLLDSGVCQVDKLNRAGYSPIMLTALATLKTQDDIDTILQLFRLGNVNAKASQAGQTALMLAVSHGRVDVVKALLACEVDVNMQDEDGSTALMCACEHGHKEITGLLLAVPSCDISLTDRDGSTALMVALDAGQSEIASMLYSRMNIKCSFAPMSDYESPASSSAEE