wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B delta isoform (PP2A subunit B isoform B55-delta) (PP2A subunit B isoform PR55-delta) (PP2A subunit B isoform R2-delta) (PP2A subunit B isoform delta) (Q66LE6)
Organism: Homo sapiens (Human)
Function: B regulatory subunit of protein phosphatase 2A (PP2A) that plays a key role in cell cycle by controlling mitosis entry and exit. The activity of PP2A complexes containing PPP2R2D (PR55-delta) fluctuate during the cell cycle: the activity is high in interphase and low in mitosis. During mitosis, activity of PP2A is inhibited via interaction with phosphorylated ENSA and ARPP19 inhibitors. Within the PP2A complexes, the B regulatory subunits modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P56932}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A catalytic subunit beta isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Alpha-endosulfine
- cAMP-regulated phosphoprotein 19
- Serine/threonine-protein kinase greatwall
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform
- Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit delta isoform
Sequence:
MAGAGGGGCPAGGNDFQWCFSQVKGAIDEDVAEADIISTVEFNYSGDLLATGDKGGRVVIFQREQENKSRPHSRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQQNAAHFLLSTNDKTIKLWKISERDKRAEGYNLKDEDGRLRDPFRITALRVPILKPMDLMVEASPRRIFANAHTYHINSISVNSDHETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHPHQCNVFVYSSSKGTIRLCDMRSSALCDRHSKFFEEPEDPSSRSFFSEIISSISDVKFSHSGRYMMTRDYLSVKVWDLNMESRPVETHQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSAIMTGSYNNFFRMFDRDTRRDVTLEASRESSKPRASLKPRKVCTGGKRRKDEISVDSLDFNKKILHTAWHPVDNVIAVAATNNLYIFQDKIN
Protein: J protein JJJ2 (P46997)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- DnaJ protein homolog XDJ1
- Protein CAJ1
- Diphthamide biosynthesis protein 4
- Auxilin-like clathrin uncoating factor SWA2
- J domain-containing protein APJ1
- J protein JJJ1
- Pre-mRNA-splicing factor CWC23
- Zuotin
- Protein SIS1
- ER-localized J domain-containing protein 5
Sequence:
MSQVIEPQLDRTTYYSILGLTSNATSSEVHKSYLKLARLLHPDKTKSDKSEELFKAVVHAHSILTDEDQKLRYDRDLKIKGLHTYQPKKNCHIFKTKAKESQGASPTLGQSEAYHRQNKPYEQQPYGFGVGKKMTSSSKSKVPIFKSFNLKSYQRNHYYSSKKERKHGSPDIDSLFHETNGASKVRMTDAGKMDTNSQFQEIWEILGKNAYTHKSYSEDPNSCLGSALSDHEEEEEAGKQQQQQQQQQQQQQHYGMTSKSSSPDEEKKNNKEPKRESRVSPEENGEEETGHKQFKLPKTSTFSSGSHDSNLQSPFYNHEYRHYARSKFECKNQFRKSVSPIKEIPATTSANEGWNILRDIIEKLNISNVDDRNKDLLFRRDEIGDKNHSDSIDIENLSIKEPKGMKRRKKDDISLEELFQSLPREKDYFMMDAINDSLESINLFKKPKTTQSHEQGGTFAQAESNRAKFKPLLEQCGITPEILDLEIPEIPEFDAVADLETLKLNVQLFNNQCNKLKETIHQVSLQRLRADTQFSDMLTQKQSIMVWKTYLEFDKSLMDKLNILQERQMQVIKIFSERCDGKV
Protein: Pglyrp6 protein (B7ZUU1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MGRQFISVCLRKGQDGFKRRASSEANTQSDFIIRGYLALNYSVFMMDLRLFSLLMLFACGIAEATTLKRMDDFISAVESIEAVNPALSMLDVLKGLRKASGLETDLSQQLLGDAHPELTMDPSVASNIHELINHHVSDITEEGVVLTLDGSNVALAPLLLGLEAGLQSIDLYPLTLTENLLNSFVHHVQNQESSALLGTKGYWDSIKSPRVYTLSGLPSLATDALIIGGMDGFILGSEMASSDHPEESLSSLLRSYYSQKLDDAAPRLISQKRRMNFRNMADFSLMKTQVVRALTVRRNLNQDERKKLDDVVNEGFEEFVHVYAVCPNIITRSQWGAASYIGSPSYLSLPVRYLFIHHTYQPSKPCTTFEQCAAEMRSMQRYHQQSNGWSDIGYSFVAGSDGNLYEGRGWNWVGAHTYGYNSIGYGVCFIGDYTSTLPASSAMNMVRYDFTYCATNGGRLSKSYSLYGHRQAAATECPGNTLYRQIQTWERYQSYLP
Protein: Exocyst complex component 3-like protein 2 (HBV X-transactivated gene 7 protein) (HBV XAg-transactivated protein 7) (Q2M3D2)
Organism: Homo sapiens (Human)
Interaction partners:
- Exocyst complex component 4
- Exocyst complex component 7
- Exocyst complex component 2
- Exocyst complex component 5
- Exocyst complex component 8
- Exocyst complex component 1
- Exocyst complex component 6
- Exocyst complex component 1-like
- Exocyst complex component 6B
- Exocyst complex component 3-like protein
Sequence:
MPILKNLGVSDPKVPRAGTLPLRSSRNPFEEVSGLEEEEAGELGSLPNGTSCRRRATLEKLAGLAPFRLGWAPGRRAGSPGDGQPRSFLGRVLVPGIRRSSADFGLLARLHGTRAHGDEEAAGEAARRLAFLRLGRGSKPQRASLAERVVPAGEAAPEPPPKVPEPPKMKEPLSVLEILSLIQQRELARADEHILELEAEELAPSRGGAPGPPKAEGAGGGRRARDVALLYEALQRELWALVRETLAGPGPGACAGAGAVAQLGQVLVQEEAADGRRGPGAARKLRARWAEAVARAARERLEAAAPGAPGGLAGQLEALRARLLEDMAVVRGRLAPAYPAGLGAFGVYLRGYHGALAEWLGASARRRLPLADRYALLHWHNQVYPREVLGLVDMAALENGELGPLLSPGTLRGLEDECVTDVKAQTRAALLRVLQEDEEHWGSLEDQPSSLAQDVCELLEEHTERAPRISQEFGERMAHCCLGGLAEFLQSFQQRVERFHENPAVREMLPDTYISKTIALVNCGPPLRALAERLARVGPPESEPAREASASALDHVTRLCHRVVANLLFQELQPHFNKLMRRKWLSSPEALDGIVGTLGAQALALRRMQDEPYQALVAELHRRALVEYVRPLLRGRLRCSSARTRSRVAGRLREDAAQLQRLFRRLESQASWLDAVVPHLAEVMQLEDTPSIQVEVGVLVRDYPDIRQKHVAALLDIRGLRNTAARQEILAVARDLELSEEGALSPPRDRAFFADIPVPRPSFCLSLPLFLGRLPLSRLARPSLACLPRPRPPSLARPRAQR
Protein: bZIP transcription factor 12 (OsBZIP12) (Abscisic acid responsive elements-binding factor 1) (ABA responsive element binding factor 1) (ABRE-binding factor 1) (OsABF1) (Q0JHF1)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Transcription activator that binds to the ABA-responsive elements (ABREs) in vitro. Involved in abiotic stress responses and abscisic acid (ABA) signaling. Involved in the signaling pathway that induces growth inhibition in response to D-allose.
Subcellular location: Nucleus {ECO:0000269|PubMed:20039193}.
Interaction partners:
- Serine/threonine-protein kinase SAPK2
- Serine/threonine-protein kinase SAPK10
- Serine/threonine-protein kinase SAPK6
- Serine/threonine-protein kinase SAPK4
Sequence:
MMASRVMASSSPSHTASDLARFAAGRGGGGSAGLGSMNVEEILRGIYADMPTPALPLVGGDRPMSPLPAPDVAAAPRTAEEVWKEITGAGVAAAAGGVVPPAAAAAAAPAVVAGAGAGTGAEMTLEDFLAREGAVKEDEAVVTDPSAAKGQVVMGFLNGAEVTGGVTGGRSRKRHLMDPMDRAAMQRQKRMIKNRESAARSRERKQAYIAELESLVTQLEEENAKMFKEQEEQHQKRLKELKEMVVPVIIRKTSARDLRRTNSMEW
Protein: E3 ubiquitin-protein ligase RNF166 (EC 2.3.2.27) (RING finger protein 166) (RING-type E3 ubiquitin transferase RNF166) (Q96A37)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein ligase that promotes the ubiquitination of different substrates. In turn, participates in different biological processes including interferon production or autophagy. Plays a role in the activation of RNA virus-induced interferon-beta production by promoting the ubiquitination of TRAF3 and TRAF6. Also plays a role in the early recruitment of autophagy adapters to bacteria. Mediates 'Lys-29' and 'Lys-33'-linked ubiquitination of SQSTM1 leading to xenophagic targeting of bacteria and inhibition of their replication.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26456228}.
Interaction partners:
- Protein mono-ADP-ribosyltransferase PARP11
- E3 ubiquitin-protein ligase LRSAM1
Sequence:
MAMFRSLVASAQQRQPPAGPAGGDSGLEAQYTCPICLEVYHRPVAIGSCGHTFCGECLQPCLQVPSPLCPLCRLPFDPKKVDKATHVEKQLSSYKAPCRGCNKKVTLAKMRVHISSCLKVQEQMANCPKFVPVVPTSQPIPSNIPNRSTFACPYCGARNLDQQELVKHCVESHRSDPNRVVCPICSAMPWGDPSYKSANFLQHLLHRHKFSYDTFVDYSIDEEAAFQAALALSLSEN
Protein: Chromatin accessibility complex 16kD protein (Q9V452)
Organism: Drosophila melanogaster (Fruit fly)
Function: Histone-like protein which promotes nucleosome sliding of ATP-dependent nucleosome remodeling complexes. Part of the chromatin-accessibility complex (CHRAC) which uses energy/ATP to increase the general accessibility of DNA in chromatin. As an heterodimer with Chrac-14, binds DNA and facilitates nucleosome sliding by Acf. As part of the CHRAC complex, required for oogenesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:10856248, ECO:0000269|PubMed:11447119}.
Interaction partners:
- DNA polymerase epsilon subunit 3
- Chromatin-remodeling complex ATPase chain Iswi
- ATP-dependent chromatin assembly factor large subunit
- Nuclear factor Y-box B, isoform A
- Nuclear transcription factor Y subunit
- Nucleosome-remodeling factor subunit NURF301
- Toutatis, isoform E
- Chromatin assembly factor 1 p55 subunit
- Inorganic pyrophosphatase
- C-terminal-binding protein
Sequence:
MGEPRSQPPVERPPTAETFLPLSRVRTIMKSSMDTGLITNEVLFLMTKCTELFVRHLAGAAYTEEFGQRPGEALKYEHLSQVVNKNKNLEFLLQIVPQKIRVHQFQEMLRLNRSAGSDDDDDDDDDDDEEESESESESDE
Protein: Kinesin, putative (Q388Z9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSGIYAISIPHIFRVDQVLDERCSNEELFEKLVYDRILSSAEQPDTSCFLAYGHTNSGKTHTIAGGRREAGLLSLAARAVLDMYGYLEVAMIEVYGENVHDLLAQGERRLIRRRAGPDGVAIIVEDLTTCSLSTLQEWEAVSAFGMETRRTAPTERNSRSSRSHALFTIKSRGLRLCMVDLAGSERQTTYSPQLNSESIAINKSLSRLSTVLEALSTIRRRPDGSSSYVNFRDTTLTVLLQRYLCGASMTVFVACIHPDVQFVQETMSTMRYTQRLKHIKTKPPPQKPNDDSSLFHPKEHKNLLEELLALRKIVGINPCAGVAAGNDDTLKTKLYQDNCAPPAPPQDAAPRVEGPDRSERSIMRHKQRLLRSKDIRRVAGWLVSRTLSMLPQLSVGFDDYFDDYLPGEIQVVGFVSLMACLPPCSKTEALNGLAFLDVGDPSIGLSMLDAGIPACVGLHKLSCKEVHSWEVHEYNETNNIFLLAFFKVDEQLVEPLGASGSPFACCGGLLTLEPLMPLALVFGAPLNAPNEVKENVLQHLVTLQSEQHQPAGASNDTDASQSVHKKSNDSHGSVPFFNSEVLDALSDYSYHYEVGEDSLIGSPVGPQRKALTDHNEGQNGDGFRSQISWESVQFQEDLTEMVCCRAVGSADIDEADDPEPSSLSSPSTFCGEEKELNPVPLPNSVAVRAVSCDIDPEKGEQSPQSVGEQIITDSADQCDVETLDDQPSLHAGGDESEISFKEVELTVGTTANTSSSPGLLESQPKSSHILVACEEENRLDCPRGEILELSGTLASESPEVHKGKGKKTKRENRDNHRDRDPVKQGCHYCVIM
Protein: Cytochrome P450 7A1 (24-hydroxycholesterol 7-alpha-hydroxylase) (EC 1.14.14.26) (CYPVII) (Cholesterol 7-alpha-hydroxylase) (Cholesterol 7-alpha-monooxygenase) (EC 1.14.14.23) (P22680)
Organism: Homo sapiens (Human)
Function: A cytochrome P450 monooxygenase involved in the metabolism of endogenous cholesterol and its oxygenated derivatives (oxysterols). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (CPR; NADPH-ferrihemoprotein reductase). Functions as a critical regulatory enzyme of bile acid biosynthesis and cholesterol homeostasis. Catalyzes the hydroxylation of carbon hydrogen bond at 7-alpha position of cholesterol, a rate-limiting step in cholesterol catabolism and bile acid biosynthesis. 7-alpha hydroxylates several oxysterols, including 4beta-hydroxycholesterol and 24-hydroxycholesterol. Catalyzes the oxidation of the 7,8 double bond of 7-dehydrocholesterol and lathosterol with direct and predominant formation of the 7-keto derivatives.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305|PubMed:11013305, ECO:0000305|PubMed:2384150}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305|PubMed:11013305, ECO:0000305|PubMed:2384150}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Sterol 26-hydroxylase, mitochondrial
- Bile acid receptor
- Cholesterol 25-hydroxylase
- Cholesterol 24-hydroxylase
- 3 beta-hydroxysteroid dehydrogenase type 7
- Nuclear receptor subfamily 0 group B member 2
- Cytochrome P450 1A2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Cytochrome P450 1A1
- Steroid 17-alpha-hydroxylase/17,20 lyase
Sequence:
MMTTSLIWGIAIAACCCLWLILGIRRRQTGEPPLENGLIPYLGCALQFGANPLEFLRANQRKHGHVFTCKLMGKYVHFITNPLSYHKVLCHGKYFDWKKFHFATSAKAFGHRSIDPMDGNTTENINDTFIKTLQGHALNSLTESMMENLQRIMRPPVSSNSKTAAWVTEGMYSFCYRVMFEAGYLTIFGRDLTRRDTQKAHILNNLDNFKQFDKVFPALVAGLPIHMFRTAHNAREKLAESLRHENLQKRESISELISLRMFLNDTLSTFDDLEKAKTHLVVLWASQANTIPATFWSLFQMIRNPEAMKAATEEVKRTLENAGQKVSLEGNPICLSQAELNDLPVLDSIIKESLRLSSASLNIRTAKEDFTLHLEDGSYNIRKDDIIALYPQLMHLDPEIYPDPLTFKYDRYLDENGKTKTTFYCNGLKLKYYYMPFGSGATICPGRLFAIHEIKQFLILMLSYFELELIEGQAKCPPLDQSRAGLGILPPLNDIEFKYKFKHL
Protein: Molybdenum cofactor sulfurase (MCS) (MOS) (MoCo sulfurase) (EC 2.8.1.9) (Abscisic acid protein 3) (Low expression of osmotically expressive genes protein 5) (Molybdenum cofactor sulfurtransferase) (Q9C5X8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sulfurates the molybdenum cofactor. Sulfation of molybdenum is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and 1 sulfur atom in active form. Modulates cold stress- and osmotic stress-responsive gene expression by acting as key regulator of abscisic acid (ABA) biosynthesis.
Interaction partners:
- Molybdopterin biosynthesis protein CNX1
- Abscisic-aldehyde oxidase
- Iron-sulfur cluster assembly protein 1
- Iron-sulfur cluster assembly protein 3
- Iron-sulfur cluster assembly protein 2
- Zeaxanthin epoxidase, chloroplastic
- SufE-like protein 2, chloroplastic
- Xanthoxin dehydrogenase
- 9-cis-epoxycarotenoid dioxygenase NCED3, chloroplastic
- Adenylyltransferase and sulfurtransferase MOCS3
Sequence:
MEAFLKEFGDYYGYPDGPKNIQEIRDTEFKRLDKGVVYLDHAGSTLYSELQMEYIFKDFTSNVFGNPHSQSDISSATSDLIADARHQVLEYFNASPEDYSCLFTSGATAALKLVGETFPWTQDSNFLYTMENHNSVLGIREYALAQGASACAVDIEEAANQPGQLTNSGPSIKVKHRAVQMRNTSKLQKEESRGNAYNLFAFPSECNFSGLRFNLDLVKLMKENTETVLQGSPFSKSKRWMVLIDAAKGCATLPPDLSEYPADFVVLSFYKLFGYPTGLGALLVRNDAAKLLKKTYFSGGTVAASIADIDFVKRRERVEEFFEDGSASFLSIAAIRHGFKLLKSLTPSAIWMHTTSLSIYVKKKLQALRHGNGAAVCVLYGSENLELSSHKSGPTVTFNLKRPDGSWFGYLEVEKLASLSGIQLRTGCFCNPGACAKYLELSHSELRSNVEAGHICWDDNDVINGKPTGAVRVSFGYMSTFEDAKKFIDFIISSFASPPKKTGNGTVVSGRFPQLPSEDLESKESFPSHYLKSITVYPIKSCAGFSVIRWPLCRTGLLHDREWMVQGLTGEILTQKKVPEMSLIKTFIDLEEGLLSVESSRCEDKLHIRIKSDSYNPRNDEFDSHANILENRNEETRINRWFTNAIGRQCKLLRYSSSTSKDCLNRNKSPGLCRDLESNINFANEAQFLLISEESVADLNRRLEAKDEDYKRAHEKLNPHRFRPNLVISGGEPYGEDKWKTVKIGDNHFTSLGGCNRCQMINISNEAGLVKKSNEPLTTLASYRRVKGKILFGTLLRYEIDEKRQCWIGVGEEVNPDIE
Protein: Nitrite reductase [NAD(P)H] (EC 1.7.1.4) (P22944)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Nitrate reductase
- Nitrate transporter
- Nitrate reductase
- Nitrate/nitrite transporter
- Glutamine synthetase
- Glutamine synthetase
- NADP-specific glutamate dehydrogenase
- Nitrilase
- CN hydrolase domain-containing protein
- Nitrogen regulatory protein areA
Sequence:
MPLLDGPRNGETVTASAHNGIPIIDGVDPSTLRGDIDQDPNRRQKIVVVGLGMVAVAFIEKLVKLDSERRKYDIVVIGEEPHIAYNRVGLSSYFEHRKIEDLYLNPKEWYGSFKDRSFDYYLNTRVTDVFPQHKTVKTSTGDIVSYDILVLATGSDAVLPTSTPGHDAKGIFVYRTISDLERLMEFAANHKGQTGVTVGGGLLGLEAAKAMTDLEDFGSVKLIDRNKWVLARQLDGDAGSLVTKKIRDLGLEVLHEKRVAKIHTDDDNNVTGILFEDGQELDCCCICFAIGIRPRDELGGSTGIQCAKRGGFVIDESLRTSVNDIYAIGECASWENQTFGIIAPGIEMADVLSFNLTNPDKEPKRFNRPDLSTKLKLLGVDVASFGDFFADRDGPKFLPGQRPSAESIGAADPNREEEPQVKALTYRDPFGGVYKKYLFTMDGKYLLGGMMIGDTKDYVKLNQMVKSQKPLEVPPSEFILGAQSGGEENADDLDDSTQICSCHNVTKGDVVESVKSGTCKTIADVKSCTKAGTGCGGCMPLVQSIFNKTMLDMGQEVSNNLCVHIPYSRADLYNVIAIRQLRTFDDVMKSAGKCPDSLGCEICKPAIASILSSLFNPHLMDKEYHELQETNDRFLANIQRNGTFSVVPRVPGGEITADKLIAIGQVAKKYNLYCKITGGQRIDMFGARKQDLLDIWTELVDAGMESGHAYAKSLRTVKSCVGTTWCRFGVGDSVGMAIRLEQRYKSIRAPHKFKGAVSGCVRECAEAQNKDFGLIATEKGFNIFVGGNGGAKPRHSELLAKDVPPEEVIPILDRYVIFYIRTADKLQRTARWLESLPGGIEYLKDVVLNDKLGIAAEMERQMQELVDSYFCEWTETVRNPKRRKYFQQFANTDETVENVEIVKEREQVRPTYWPKDGANEDFKGHQWSSLSWQPVIKADYFSDGPPAISSANIKRGDTQLAIFKVKGKYYATQQMCPHKRTFVLSDGLIGDDDNGKYWVSCPYHKRNFELNGEQAGRCQNDEAMNIATFPVEEREDGWIYMKLPPVEELDSVLGTEKWKVKKGEAVDPFEAYDKKYSGMKGKRAGAKGIEGSKPTRSPSNTIDW
Protein: Virulence transcriptional regulatory protein PhoP (Acid shock protein 29) (ASP29) (P0DM78)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Member of the two-component regulatory system PhoP/PhoQ which regulates the expression of genes involved in virulence, adaptation to acidic and low Mg(2+) environments and resistance to host defense antimicrobial peptides. Essential for intramacrophage survival of S.typhimurium. In low periplasmic Mg(2+), PhoQ phosphorylates PhoP, resulting in the expression of PhoP-activated genes (PAG) and repression of PhoP-repressed genes (PRG). In high periplasmic Mg(2+), PhoQ dephosphorylates phospho-PhoP, resulting in the repression of PAG and may lead to expression of some PRG. Essential for transcription of spiC inside macrophages by controlling the expression of the two-component regulatory system SsrB/SpiR (SsrA) and Pir at transcriptional and post-transcriptional levels respectively. Promotes expression of the two-component regulatory system PmrA/PmrB via activation of pmrD gene. Is required to attenuate bacterial growth within fibroblast cells and to enhance bacterial resistance to bile in intestinal cells. Negatively regulates prgH, which is required for invasion of epithelial cells. PhoP uses multiple mechanisms to promote transcription and activates promoters for PAG at low (uM range) Mg(2+) concentrations (Probable). Involved in acid tolerance.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Virulence sensor histidine kinase PhoQ
- Sensor protein BasS
- Phosphate regulon sensor protein PhoR
- Sensor histidine kinase SsrA
- Sensor histidine kinase EnvZ
- Protein MgtC
- histidine kinase
- Signal transduction protein PmrD
- histidine kinase
- PhoP/PhoQ regulator MgrB
Sequence:
MMRVLVVEDNALLRHHLKVQLQDSGHQVDAAEDAREADYYLNEHLPDIAIVDLGLPDEDGLSLIRRWRSSDVSLPVLVLTAREGWQDKVEVLSSGADDYVTKPFHIEEVMARMQALMRRNSGLASQVINIPPFQVDLSRRELSVNEEVIKLTAFEYTIMETLIRNNGKVVSKDSLMLQLYPDAELRESHTIDVLMGRLRKKIQAQYPHDVITTVRGQGYLFELR
Protein: Plasmalemma vesicle-associated protein (MECA-32 antigen) (Plasmalemma vesicle protein 1) (PV-1) (Q91VC4)
Organism: Mus musculus (Mouse)
Function: Endothelial cell-specific membrane protein involved in the formation of the diaphragms that bridge endothelial fenestrae. It is also required for the formation of stomata of caveolae and transendothelial channels. Functions in microvascular permeability, endothelial fenestrae contributing to the passage of water and solutes and regulating transcellular versus paracellular flow in different organs. Plays a specific role in embryonic development.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Membrane, caveola {ECO:0000250|UniProtKB:Q9WV78}; Single-pass type II membrane protein {ECO:0000255}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9WV78}. Note=Membrane-associated protein of caveolae. Found in fenestral and stomatal diaphragms in fenestrated endothelia and transendothelial channels. Also colocalized with CAV1 in perinuclear region. {ECO:0000250|UniProtKB:Q9WV78}.
Interaction partners:
- Claudin-5
- Platelet endothelial cell adhesion molecule
Sequence:
MGLSMDRSPYARTGDQQRGCWYYLRYFFLFVSLIQFLIILGLVLFMIYGNVHATTESSLRATEIRADSLYSQVVGLSASQANLSKQLNISLLVKETVMQQLLTTRREMERINASFRQCQGDLITYINYNRFIAAIILSEKQCQEQLKEVNKTCEALLFKLGEKVKTLEMEVAKEKAVCSKDKESLLAGKRQTEEQLEACGKARERQQQEQQVTEENLRKVQSLCIPLDQEKFQADVLSAWRDSLIYRTLETLPYHYQLMPEYASLRRTCESLPGIMTTKIEELARGLRAGIERVTRENAELRRQKLELERAAQAAQEARARAGTEAQARETQLRAECARQTQLALEEKAALRAQRDNLERELEARKRELEQLRTEVDVRISALDTCVKAKSLPAVPPRVSGPPPNPPPIDPASLEEFKKRILESQRLPVVNPAAQPSG
Protein: Alanine--glyoxylate aminotransferase 2 homolog 1, mitochondrial (EC 2.6.1.44) (Beta-alanine-pyruvate aminotransferase 1) (Q940M2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14671022}.
Interaction partners:
- Serine--glyoxylate aminotransferase
- Glutamate--glyoxylate aminotransferase 2
- Glutamate--glyoxylate aminotransferase 1
- Branched-chain-amino-acid aminotransferase 5, chloroplastic
- Alanine aminotransferase 2, mitochondrial
- Alanine aminotransferase 1, mitochondrial
- Aldehyde dehydrogenase family 7 member B4
- 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial
- Aldehyde dehydrogenase family 3 member F1
- Aldehyde dehydrogenase family 3 member I1, chloroplastic
Sequence:
MALQRQLLKRATSDIYHRRAISLLRTDFSTSPSIADAPPHIPPFVHQPRPYKGPSADEVLQKRKKFLGPSLFHYYQKPLNIVEGKMQYLYDESGRRYLDAFAGIVTVSCGHCHPDILNAITEQSKLLQHATTIYLHHAIGDFAEALAAKMPGNLKVVYFVNSGSEANELAMMMARLYTGSLEMISLRNAYHGGSSNTIGLTALNTWKYPLPQGEIHHVVNPDPYRGVFGSDGSLYAKDVHDHIEYGTSGKVAGFIAETIQGVGGAVELAPGYLKSVYEIVRNAGGVCIADEVQTGFGRTGSHYWGFQTQDVVPDIVTMAKGIGNGLPLGAVVTTPEIASVLASKILFNTFGGNPVCSAGGLAVLNVIDKEKRQEHCAEVGSHLIQRLKDVQKRHDIIGDVRGRGLMVGIELVSDRKDKTPAKAETSVLFEQLRELGILVGKGGLHGNVFRIKPPMCFTKDDADFLVDALDYSISRL
Protein: Tropomodulin, isoform Q (A0A0B4KHW6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MSDIEDVFGGSAEETKPEPDAQSKTSVVTEHTEEVIPGETEKMVTETIDEDGDVVEETTEVTRKTVKRTMKITETSATTKTTTLTTPAKLYGKDLSEYDDVDVESLLAQLSPEEITILAKEVDPDDNFLPPDQRNSYECTKEATGPLNRKQLIEHINKQAIETPDQPEFEPFVQGKVRGKKWVPPPRDARDIEAEEQIAIDMGEEYEHALNDATQEEIIDLAAILGFHSMMNQDQYHASLLNKGQPVGLGWDGITKSTQQKLFPMDPPNNTDVEESIKRVKDDDSKLIDLNLNNIKNISDEKLEQLFAALPQNEHLEVLSLTNVGLTDKTALLLAAAIEKSKTLRVLNVETNFISPPVIVKLVQALLKCHTIEEFRASNQRSAVLGNKIEMEITDLVEKNSSLLRLGLHLEFNDARHRVAAHLQRNIDRIRKDLELRLQFRFFNNLHRKSTRIQ
Protein: Elongation factor 1-alpha (Q3LUM3)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
- Elongation factor 1-gamma-like
- Elongation factor 1-gamma-like
- Elongation factor 1-gamma-like
- Elongation factor 1-beta 2-like isoform X1
- Elongation factor 1-beta 2-like
- Elongation factor 1-delta-like
- Elongation factor 1-delta-like
- Elongation factor 1-beta 2-like
- GTP-binding nuclear protein
- GTP-binding nuclear protein
Sequence:
MGKEKVHINIVVIGHVDSGKSTTTGHLIYKLGGIDKRVIERFEKEAAEMNKRSFKYAWVLDKLKAERERGITIDIALWKFETTKYYCTVIDAPGHRDFIKNMITGTSQADCAVLIIDSTTGGFEAGISKDGQTREHALLAFTLGVKQMICCCNKMDATTPKYSKARYDEIVKEVSSYLKKVGYNPDKIPFVPISGFEGDNMIERSTNLDWYKGPTLLEALDQINEPKRPSDKPLRLPLQDVYKIGGIGTVPVGRVETGVLKPGMVVTFGPSGLTTEVKSVEMHHEALSEALPGDNVGFNVKNVAVKDLKRGFVASNSKDDPAKEAASFTSQVIIMNHPGQIGNGYAPVLDCHTSHIAVKFSELLTKIDRRSGKELEKEPKFLKNGDAGMIKMVPTKPMVVETFSEYPPLGRFAVRDMRQTVAVGVIKSVEKKDPTGAKVTKSAAKKK
Protein: Replication factor A protein 1 (Single-stranded DNA-binding protein p68 subunit) (Q92372)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: As part of the replication protein A (RPA/RP-A), a single-stranded DNA-binding heterotrimeric complex, may play an essential role in DNA replication, recombination and repair. Binds and stabilizes single-stranded DNA intermediates, preventing complementary DNA reannealing and recruiting different proteins involved in DNA metabolism.
Subcellular location: Nucleus.
Interaction partners:
- Replication factor A protein 2
- DNA repair and recombination protein rad22
- Replication factor A protein 3
- DNA repair protein rhp51
- Protein kinase rad3
- DNA polymerase delta catalytic subunit
- DNA replication ATP-dependent helicase/nuclease dna2
- Swi1-interacting protein swi3
- ATP-dependent DNA helicase pfh1
- Mating-type switching protein swi1
Sequence:
MAERLSVGALRIINTSDASSFPPNPILQVLTVKELNSNPTSGAPKRYRVVLSDSINYAQSMLSTQLNHLVAENKLQKGAFVQLTQFTVNVMKERKILIVLGLNVLTELGVMDKIGNPAGLETVDALRQQQNEQNNASAPRTGISTSTNSFYGNNAAATAPAPPPMMKKPAAPNSLSTIIYPIEGLSPYQNKWTIRARVTNKSEVKHWHNQRGEGKLFSVNLLDESGEIRATGFNDQVDAFYDILQEGSVYYISRCRVNIAKKQYTNVQNEYELMFERDTEIRKAEDQTAVPVAKFSFVSLQEVGDVAKDAVIDVIGVLQNVGPVQQITSRATSRGFDKRDITIVDQTGYEMRVTLWGKTAIEFSVSEESILAFKGVKVNDFQGRSLSMLTSSTMSVDPDIQESHLLKGWYDGQGRGQEFAKHSVISSTLSTTGRSAERKNIAEVQAEHLGMSETPDYFSLKGTIVYIRKKNVSYPACPAADCNKKVFDQGGSWRCEKCNKEYDAPQYRYIITIAVGDHTGQLWLNVFDDVGKLIMHKTADELNDLQENDENAFMNCMAEACYMPYIFQCRAKQDNFKGEMRVRYTVMSINQMDWKEESKRLINFIESAQ