wanglab/gogpt-training-data huggingface dataset:
Protein: Lipid II flippase MurJ (Peptidoglycan biosynthesis protein MurJ) (P0AF16)
Organism: Escherichia coli (strain K12)
Function: Involved in peptidoglycan biosynthesis. Transports lipid-linked peptidoglycan precursors from the inner to the outer leaflet of the cytoplasmic membrane.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23935042}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_02078, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:23935042}.
Interaction partners:
- Probable peptidoglycan glycosyltransferase FtsW
- Peptidoglycan glycosyltransferase MrdB
- UDP-N-acetylglucosamine--N-acetylmuramyl-
- Peptidoglycan D,D-transpeptidase FtsI
- UDP-N-acetylglucosamine 1-carboxyvinyltransferase
- Penicillin-binding protein 1B
- Bifunctional riboflavin kinase/FMN adenylyltransferase
- Peptidoglycan D,D-transpeptidase MrdA
- Phospholipase A1
- UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase
Sequence:
MNLLKSLAAVSSMTMFSRVLGFARDAIVARIFGAGMATDAFFVAFKLPNLLRRIFAEGAFSQAFVPILAEYKSKQGEDATRVFVSYVSGLLTLALAVVTVAGMLAAPWVIMVTAPGFADTADKFALTSQLLKITFPYILLISLASLVGAILNTWNRFSIPAFAPTLLNISMIGFALFAAPYFNPPVLALAWAVTVGGVLQLVYQLPHLKKIGMLVLPRINFHDAGAMRVVKQMGPAILGVSVSQISLIINTIFASFLASGSVSWMYYADRLMEFPSGVLGVALGTILLPSLSKSFASGNHDEYNRLMDWGLRLCFLLALPSAVALGILSGPLTVSLFQYGKFTAFDALMTQRALIAYSVGLIGLIVVKVLAPGFYSRQDIKTPVKIAIVTLILTQLMNLAFIGPLKHAGLSLSIGLAACLNASLLYWQLRKQKIFTPQPGWMAFLLRLVVAVLVMSGVLLGMLHIMPEWSLGTMPWRLLRLMAVVLAGIAAYFAALAVLGFKVKEFARRTV
Protein: ALX homeobox protein 1 (Cartilage homeoprotein 1) (CART-1) (Q15699)
Organism: Homo sapiens (Human)
Function: Sequence-specific DNA-binding transcription factor that binds palindromic sequences within promoters and may activate or repress the transcription of a subset of genes. Most probably regulates the expression of genes involved in the development of mesenchyme-derived craniofacial structures. Early on in development, it plays a role in forebrain mesenchyme survival. May also induce epithelial to mesenchymal transition (EMT) through the expression of SNAI1.
Subcellular location: Nucleus {ECO:0000269|PubMed:8756334, ECO:0000269|PubMed:9753625}.
Interaction partners:
Sequence:
MEFLSEKFALKSPPSKNSDFYMGAGGPLEHVMETLDNESFYSKASAGKCVQAFGPLPRAEHHVRLERTSPCQDSSVNYGITKVEGQPLHTELNRAMDNCNSLRMSPVKGMQEKGELDELGDKCDSNVSSSKKRRHRTTFTSLQLEELEKVFQKTHYPDVYVREQLALRTELTEARVQVWFQNRRAKWRKRERYGQIQQAKSHFAATYDISVLPRTDSYPQIQNNLWAGNASGGSVVTSCMLPRDTSSCMTPYSHSPRTDSSYTGFSNHQNQFSHVPLNNFFTDSLLTGATNGHAFETKPEFERRSSSIAVLRMKAKEHTANISWAM
Protein: MPN domain-containing protein (O61792)
Organism: Caenorhabditis elegans
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 14
- Proteasomal ubiquitin receptor ADRM1 homolog
- 26S protease regulatory subunit 6A
- Probable 26S proteasome regulatory subunit 10B
- 26S proteasome non-ATPase regulatory subunit 2
- 26S proteasome non-ATPase regulatory subunit 14
- 26S proteasome non-ATPase regulatory subunit 6
- 26S proteasome non-ATPase regulatory subunit 4
- 26S proteasome regulatory subunit 7
- PCI domain-containing protein
Sequence:
MAPTNKDGDVATVKAVDVLKQKAGAHHCLGNVHANLPVNKVTVHPLVLLSVVDHFNRVSKTQSVKRVVGVLLGSMKKDKTLDIGNSFAVPFDEDDKDKSTWFLDMDYLESMYGMFYKVAAKEKIVGWYHTGPKLHKNDIAINEQLKRFCPNPVLVIIDAEPKNIGLPTEAYIEVQEVHDDGTPPIKTFEHVPSDIGAEEAEEVGVEHLLRDIKDQTAGTLSQRITDQLMGLRGLQSQLESIEKYLHDIVRGTLPVNHHVIYYVQEVLNLLPDVTHPDYIVSQNVQTNDQLMCVYMGSLVRSVVALHNLIDNKISLQKAEKEQETGEAEKKKDEKDKKDKKDEKKDEKKEKDSKSSTPNTPKK
Protein: Low density lipoprotein receptor-related protein 4 (A0A2R8PYI8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Agrin
- Muscle, skeletal receptor tyrosine-protein kinase isoform 3 precursor
- Protein Wnt
- Docking protein 7.
- Caveolin
- 43 kDa receptor-associated protein of the synapse
- Protein Wnt
Sequence:
MRTVLIWENLDRPRDIVVDPIGGFMYWTDWGANPKIERAGMDAWNRTVIISSNLTWPNGLAIDYSTERLYWADASVKTIEYGNFDGSGRQVLIGSQLPHPFGLTLHEDRIYWTDWQSKSIQSADKLTGLDRKTLAENLENLMDIHMFHNHRTKVQTGCLVNNGGCSHLCLLAPAPKSWSCACPTGINLQADGKTCAHGLMTTDGLAVDSVGRKIYWTDTGTNRIEVANLNGSMRKVLVWQNLDSPRAIALYHEMGYMYWTDWGEHAKLERSSMDGSDRVVLINNNLGWPNGLAVDKAGSQLLWADAHTERIEASDLNGSNRRTLVSPVQHPYGLTVLGSHMYWTDWQSRSIHRADKNTGENAIIIRSSLPGLMDIQAVDRTASAGLNKCGRRNGGCSHLCLPRLNGTSCACPTGVLLKADGRSCEDLPETYLLFSNRVSVRRISLDTHDHTDVFVPVAELQNVISLDYDSVERKLYYTDVSLDVIRRVNLDGSDMETVISSGLKTTDGLAVDWVARNMYWTDTGRNTIEVAHLDGTSRKVLVNNSLDEPRAIAVFPSKGFLFWTDWGHIAKIERAFLDGTDRKVLINTDLGWPNGLTLDYDTRRIFWVDAHLDRIESSDLNGKLRQILISPVSHPFALTQQERWIYWTDWQTKSIQRVDKHTGRSKETVLANVEGLMDIIVVSPQRQSGTNHCAANNGGCTHLCLARSNSFICACPDEADSRPCSTIAGHVPASPEKDTTGTQTPRKQATEKPHQGLSLVNCTEMNLSLEDCFQNSVISAPRDESPHISYVIGGALSILAILILIAAFIIYRHKKFKFADPGVSNLTYSNPSYRTSTQEVKIETAQKPAINSQLRYKKEVQGVVDGGYTKEKIRIVEGVCLLSGEDLYWEDLRQLKACRGSGLHNCMRTETVSLQASSASLNDGETEQLLQEGDHQSECSSISTTAHHNTHPDTGWRHQRKTSTESQV
Protein: Small ribosomal subunit protein eS28 (40S ribosomal protein S28) (Q6QAT1)
Organism: Sus scrofa (Pig)
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62857}. Cytoplasm {ECO:0000269|PubMed:24930395}. Rough endoplasmic reticulum {ECO:0000269|PubMed:24930395}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62857}. Note=Detected on cytosolic polysomes. Detected in ribosomes that are associated with the rough endoplasmic reticulum. {ECO:0000269|PubMed:24930395}.
Interaction partners:
- Small ribosomal subunit protein uS3
- Small ribosomal subunit protein eS21
- 40S ribosomal protein S30
- 40S ribosomal protein S8
- 40S ribosomal protein S4
- Small ribosomal subunit protein uS9
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS4
- Small ribosomal subunit protein eS12
- Small ribosomal subunit protein uS2
Sequence:
MDTSRVQPIKLARVTKVLGRTGSQGQCTQVRVEFMDDTSRSIIRNVKGPVREGDVLTLLESEREARRLR
Protein: Helicase ATP-binding domain-containing protein (O62217)
Organism: Caenorhabditis elegans
Interaction partners:
- BRCT domain-containing protein
- DNA mismatch repair protein S5 domain-containing protein
- Mismatch repair endonuclease PMS2
- Breast cancer type 1 susceptibility protein homolog
- FANCD2
- RecQ-like DNA helicase blm-1
- DNA repair endonuclease XPF
- DNA polymerase kappa
- DNA polymerase theta
- XPA C-terminal domain-containing protein
Sequence:
MSSSDAFWRMFANKNKGKSNTRSAFQVVKEEQPSTSTEPDDKKPLHHEIAGEMIKNPAKGKRKRVQIKNDEYEQLMMLGVPVRVPRGLSLYSTQKLMIVRILTALKNSQNVLGESPTGSGKTMALLASTCAWLKQYIDEKRESKEKCEIHGFSGKTQVVFTNDIGIPLESKVYEEPPEEEEFIEPVPVKNDKLFEAQWEHDFTPHTPGETPPVTLKEELEPVKKPEPVETKCTCLPRVRIYYGTRTHKQIAQVVKEFSRLPYAKILKHTILASREQSCINPAARKHADISQYCKEVNSAHSIGCSFKSAMKPRFEKALPLRDHLERNGTVVFDMEKIVETLAISYPQLCPYFSTNRILTQDADIIFCPFSYLVDPLIRNSSDVQIRNSIVILDEAHNIEDTCREAASFSFTEKELDDSILSLRIKRKAVDTELDKTGIEEKLLHIPDREVHLKEFRGHLLYLEHLILEMLRWIRQVSTEAKTPARGGQDGVKTCTISSANLFTSLTDPENGVDLFTPPLTPKHAAVAASFSAITKHNEPEMQYFDAFKPSSTAIVCIEKWLYFQSYFGNQQYQSTYRLNISIEPINQNGRFNHTFDADVSMSTSFGNPRPTTTRSSAGPRNMQYKEENAWLADAAADGDDWKDPSMSETGHKPISEGCKTTISLWCMSPALSFFDAFNETRSIVLASGTLCPMDTLKTELGMEFKQQVEGDQVINKDNIFAAVLPIGPFGNRIQCTYRNTSDPESSFYCELGAIIKYVCSNVPAGILCFLPSYRVLDQLKQCMIRNSTMRQIEMKKVVLYEPRRSSELTSVMDQFDAAIFDPSRFGANINGSLMFAVFRGKVSEGIDFADDRARVVISVGIPYPNAMDDQVNAKKLYNDQNSKEKGILTGDEWYTTQAYRALNQALGRCLRHKNDWGAMLMIDERLERQTGNLVGGASSARVSKWIRAQLKSYPSFKEFNANFREFIQRRHAVEKAKKENFCE
Protein: Retinol dehydrogenase 12 (EC 1.1.1.300) (Q8BYK4)
Organism: Mus musculus (Mouse)
Function: Retinoids dehydrogenase/reductase with a clear preference for NADP. Displays high activity towards 9-cis, 11-cis and all-trans-retinal. Shows very weak activity toward 13-cis-retinol. Also exhibits activity, albeit with lower affinity than for retinaldehydes, towards lipid peroxidation products (C9 aldehydes) such as 4-hydroxynonenal and trans-2-nonenal (By similarity). Plays an important function in photoreceptor cells to detoxify 4-hydroxynonenal and potentially other toxic aldehyde products resulting from lipid peroxidation. Has no dehydrogenase activity towards steroids (By similarity).
Interaction partners:
- Lecithin retinol acyltransferase
- Retinaldehyde dehydrogenase 3
- Beta,beta-carotene 15,15'-dioxygenase
- Retinal dehydrogenase 2
- Cytochrome P450 26A1
- Aldehyde dehydrogenase 1A1
- All-trans-retinol 13,14-reductase
- Retinol dehydrogenase 5
- Aldehyde dehydrogenase, cytosolic 1
- Aldehyde oxidase 1
Sequence:
MLFILVLLTSFLSILYLTAPSIRKFFAGGVCTTNVQIPGKVVVITGANTGIGKETARELARRGARVYIACRDVLKGESAASEIRADTKNSQVLVRKLDLSDTKSIRAFAERFLAEEKKLHILINNAGVMMCPYSKTTDGFETHFGVNHLGHFLLTYLLLERLKESAPARVVNLSSIAHLIGKIRFHDLQGQKRYCSAFAYGHSKLANLLFTRELAKRLQGTGVTAYAVHPGVVLSEITRNSYLLCLLWRLFSPFFKSTSQGAQTSLHCALAEDLEPLSGKYFSDCKRMWVSSRARNKKTAERLWNVSCELLGIQWE
Protein: LP10092p (Q95SX0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}.
Interaction partners:
Sequence:
MWRQAAEFHLRGGASETAASSLEELLKLNPNDTKVLAQLVIAYAQFQPKRALELSRKLPKLETLTTASEIDALEAANWVMSAKAAKKTANTKVEPSPSTPLEKKKNRNRKRKGKLPKNYNAEVAPDPERWLPKYERTGFRKKRGGARGKDVIKGSQGMASGAADQYDMSSRVNLTKNSPATPVYQETAPGPRQQHRKGGHKKKKGGRF
Protein: Protein NPAT (Q8BMA5)
Organism: Mus musculus (Mouse)
Function: Required for progression through the G1 and S phases of the cell cycle and for S phase entry. Activates transcription of the histone H2A, histone H2B, histone H3 and histone H4 genes in conjunction with MIZF. Also positively regulates the ATM, MIZF and PRKDC promoters. Transcriptional activation may be accomplished at least in part by the recruitment of the NuA4 histone acetyltransferase (HAT) complex to target gene promoters (By similarity). Required for early embryonic development.
Subcellular location: Nucleus {ECO:0000269|PubMed:17003125}. Note=Concentrates in Cajal bodies tethered to histone gene clusters. {ECO:0000250}.
Interaction partners:
- U7 snRNA-associated Sm-like protein LSm11
- Cyclin-dependent kinase 2
- Histone H4 transcription factor
- U7 snRNA-associated Sm-like protein LSm10
Sequence:
MLLPSDVARLVLGYLQQENLTSTCQTFILESSNLKEYAEHCTDEGFIPACLLSLFGKNLTTILNEYVAMKAKETSNDVPTIMSSLWKKLDHTLSQIRSMHSSPGFAAHQRARTRNGIAEIKRQRWLASQAAPVSSELLVLPYASGQFTTSPLVATQAVKPTGPISTPVRSNIVVVNQSQPQSTVTNTAGESLNIIPGPQERKTQTSLMSPGRRKSESQKKSLTSSGPHSSRNFQDPNAFAVEKQMVIENAREKILSNKSLQEKLAENINKFLTSDSSVAQVPKQTDSNPTEPETSIDELLGLPSEIHMSEEAIQDILEQTESDPAFQALFDLFDYGKTKNNKNMPQISSQPMETNSNIVLPEETNLTIKSSFETEESDGQSGQPPFCTSYQNEDVLLNDLKSGNSHDVLPQESQENFSQISSNIQKKTFKTAIPAEQKCALDITLESVSNLSDFNQRGSSAECNEHCSELFASQIPTEAEVAVGEKNSLSADILSQSQYQPDQPSVPVTSFVSLGGETNDKNLVLSGKNSQLLSQSTPLTTKPSKSQLCENSNNIIKVKTNPQASESADSSETANRKTETNTVSPAAAQPQADCQDNSPLQSKPPPGIGESLGVNVTEKIEIHLEEPAPSDKQLSNDAASVDLNPTESKTEPLQSASAQEPEPPSVKDGDTIFLSLSEHNSCEEVALVLGEGNPVKNNNSLSSESGGSVGVSPETQNTDGKTSNSTEVDASSIVSLKIIISDDPFVSSDAELNSAVSSISGENLPTIILSSKSPAKNAEFVTCLSSEETASAVVSVEVGDSGSMEQNLLVLKPEEPMVNNTQNEDGIAFSANVAPCVPKDGGYIQLMPTTSTAFGNSSNILIATCMTDSTALGPTVSQSNVVVLPGSSAPMTAQPPQQQLQTPPKSNSAFAVSQAVSPNFSQGSAIIIASPVQPVLQGMVGMIPVSVVGQNGNTFSTPPQQVLHMPLAAPVCNRSIAQLPIPQKSQKAQGLRNKLITGKQVNNLTNLSSLSEACHTQRTEASDKNIATELGKKMEDTTISLSGERVAPPSKPFESHRRVLCFDSTVSSVANTQGSLYKMTSENKEKKEASFSHLDSPILSSTLKPPPNNAIKREREKTVPKILSKSETASSRHTTVKEVQSEKKVSPTEVALESLHKATANKENELCGDGERPKNADTSKLPGGQQNGSLRNEKAIASLQELTKKQATPSNNKNATSVGGTVKDQKQEQSKPASSLIGAEILQDVPIHSPANRSADTDLPVPRTPGSGAGEKHKEEPSDSMKAPASRRCGEEGSMPRVMIPPVTADLPACSPASETGSENSVSMAAHTLMILSRAAIARTTATPLKDNTQQFRTSSRSTTKKRKIEELDECERNSRTSGKNLANSSVPMKKKKIKKKKLPSSFPAGMDVDKFLLSLHYDE
Protein: Dihydromonapterin reductase (H(2)-MPt reductase) (EC 1.5.1.50) (Dihydrofolate reductase) (DHFR) (EC 1.5.1.3) (P0AFS3)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the reduction of dihydromonapterin to tetrahydromonapterin. Also has lower activity with dihydrofolate.
Interaction partners:
- Dihydrofolate reductase
- Thymidylate synthase
- Serine hydroxymethyltransferase
- Dihydrofolate synthase/folylpolyglutamate synthase
- Methionine synthase
- Dihydroneopterin aldolase
- Bifunctional purine biosynthesis protein PurH
- Aminomethyltransferase
- Formyltetrahydrofolate deformylase
- Phosphoribosylglycinamide formyltransferase
Sequence:
MGKTQPLPILITGGGRRIGLALAWHFINQKQPVIVSYRTHYPAIDGLINAGAQCIQADFSTNDGVMAFADEVLKSTHGLRAILHNASAWMAEKPGAPLADVLACMMQIHVNTPYLLNHALERLLRGHGHAASDIIHFTDYVVERGSDKHIAYAASKAALDNMTRSFARKLAPEVKVNSIAPSLILFNEHDDAEYRQQALNKSLMKTAPGEKEVIDLVDYLLTSCFVTGRSFPLDGGRHLR
Protein: NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 12 (Q8BME2)
Organism: Mus musculus (Mouse)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU363103}; Peripheral membrane protein {ECO:0000256|RuleBase:RU363103}; Matrix side {ECO:0000256|RuleBase:RU363103}.
Interaction partners:
Sequence:
MRMELVEVLKRGVQQVTGHGGLRGLLRVFFRANDIRIGTLVGEDKYGNKYYEDNKQFFGRHRWVIYTTEMNGKNTFWDVDGSMVPPEWHRWLHCMTDDPPTTNPPTARKFIWTNHKFNVSATPEQYVPYSTTRKKIHEWVPPSTPYK
Protein: G-protein-signaling modulator 3 (Q6MG88)
Organism: Rattus norvegicus (Rat)
Function: Interacts with subunit of G(i) alpha proteins and regulates the activation of G(i) alpha proteins.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- RNA helicase
- G-protein-signaling modulator 1
Sequence:
MEAERPQEDGEQSLPQDDQGWPPVNSTARPWRSAPPSPPPPGTRHTALGPRSGSLLSLQTELLLDLVAEAQSRRLEEQRAAFHTPKVPPSLAPTPPRLLEDKEQLYSTILSHQCQRIEAQRSDPPLPPGGQELLELLLRVQGGGRMEDQRSRPPTHTC
Protein: Catechol O-methyltransferase (COMT) (EC 2.1.1.6) (O07431)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catechol O-methyltransferase that can use various catechol-like compounds such as gallic acid (GA), 3,4-dihydroxy-5-methoxy-benzoic acid (5OMeBA), protocatechuic acid (PCA), 3,4-dihydroxy-benzaldehyde (DHA), dopamine, caffeic acid (CA), luteolin, quercetin, and 5-hydroxyuridine.
Interaction partners:
- Glucosyl-3-phosphoglycerate synthase
- Diglucosylglycerate octanoyltransferase
- Conserved protein
Sequence:
MGMDQQPNPPDVDAFLDSTLVGDDPALAAALAASDAAELPRIAVSAQQGKFLCLLAGAIQARRVLEIGTLGGFSTIWLARGAGPQGRVVTLEYQPKHAEVARVNLQRAGVADRVEVVVGPALDTLPTLAGGPFDLVFIDADKENNVAYIQWAIRLARRGAVIVVDNVIRGGGILAESDDADAVAARRTLQMMGEHPGLDATAIQTVGRKGWDGFALALVR
Protein: Acyl-CoA:6-aminopenicillanic-acid-acyltransferase, putative (AFU_orthologue AFUA_3G12620) (C8V264)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Acetylglutamate kinase
- Isopenicillin N synthase
- Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 40 kDa form
- argininosuccinate lyase
- Arginine biosynthesis bifunctional protein ArgJ
- Ornithine carbamoyltransferase, mitochondrial
- Hypothetical arginase family protein
- Arginase
- Argininosuccinate synthase
- Amino-acid acetyltransferase, mitochondrial
Sequence:
MAVKQIVCSGTPYEIGHKHGSQASEEICRAIAFYAKMFAKHSNLDWPQVQELARDFDGLIKHRWPRYYEELKGIADGAKTDLIDIIALNVRTEIVFGRFSDGCTSLYYQNSEHSFQGQNWDWDTEQAVNLIQLTVIQQDLPTIKMITEAGIIGKIGLNSTGVGVCFNAIRAKGLDKTRIPVHLGLRIALESSSALQAVENLEKIGMASSAHILIGDATTAIGLEFTSSTFARIPVNQKGFIVHSNHMLLPHSGIDEPAWLEDSPVRVQTMSENIEKLQGTLSWASFGGLFKDESNYPCSINRAAGGGSDLATLFNIIMDLRTKRVEVIMGRPSDAAAERVILAFE
Protein: Sigma-54 dependent transcriptional regulator (Q5DYQ0)
Organism: Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri)
Interaction partners:
- Autoinducer phosphorelay protein LuxU
- histidine kinase
- histidine kinase
- Autoinducer repressor protein LuxO
- Glycosyl transferases group 1
- Sulphate transporter, anti-sigma factor antagonist
- RNA polymerase sigma-54 factor
- Two-component response regulator, sigma factor PP2C-like phosphatase
- ATPase involved in chromosome partitioning
- Sensory/regulatory protein RpfC
Sequence:
MLQKVLLVEDSTSLAILYKQYVKDEPYEFFHVTTGEQAKAFMEKNPPHLVILDLKLPDMSGQDVLAWMKEKQLPTAVIIATAHGTINIAVNLLQNGADDFIEKPIQAERLKTSIANHLKRNKLEGLVEDLQNTFNRKQYQGFIGSSLPMQAVYKIIDSVAPTTASVFIYGESGTGKEVCAEAIHYQSKRSNKPFVAINCGAIPRDLMESEIFGHIKGAFTGATTDRKGAAMLANGGTLFLDELCEMELEMQKKLLRFLQTGRFTPLGGSKELSTDIRIICATNRDPLTEVNEGRFREDLYYRVHVVPIHMPPLRERGTDIIDIATFFLKKYAKEDHKKFKALKRNVELRLCNYSWPGNVRQLQNIIRNVVVLHNDTHVAIEHLPPPLNQPVTNKATPVASKPSFTAPSQLSRNMETADVQHNQTEQQLSSSSEGQTLETSATDAINTSVIRPMADIEREVIQNAIDHCDGNVLNAAVLLELSPSTLYRKKQAWEAYEESE
Protein: Fatty acid elongase 3-like (Protein ELO3-like) (EC 2.3.1.-) (Elongation of fatty acids protein 3-like) (Protein HIGH EXPRESSION OF OSMOTICALLY RESPONSIVE GENES 3) (Very long-chain fatty acid condensing enzyme HOS3) (VLCFA condensing enzyme HOS3) (Q9SYY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable very long-chain fatty acid (VLCFA) elongase that controls VLCFA composition and functions to inhibit abscisic acid (ABA)-mediated stress responses, including regulation of stomatal aperture, maintenance of primary root growth and inhibition of germination. VLCFA pathway and products may function as signaling components acting upstream of sphingosine-1-phosphate, ceramide and the heterotrimeric G-protein complex, in lipid-mediated regulation of abiotic stress signaling.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Elongator complex protein 1
- Protein STRICTOSIDINE SYNTHASE-LIKE 3
Sequence:
MSTALINSITYFLSEHPYIVGFRWSNSQSWGSTWSFLFTSISLYIAVSSSLHILLSAVRRSNRSVPLGHIPEIHSLLMSILSATIFAGILLSAAAEIRDTRWLWRRSKTATPLQWLLCFPLGTRPSGRVFFWSYVFYLTRFLHMFRTIFAVLRSRRLAVSQLFCNSVMAFTSFLWLEFSQSYQILAILSTTLVYSVVYGYRFWTGFGLPGSAFPSFVVNCQLVLVGCNLVSHAGVLTMHLFKGGCNGIGAWGLNSVLNGAILLLFLNFYVRMHSPMRRHINKMNSQRNA
Protein: Latrophilin-like protein LAT-2 (G5ECX0)
Organism: Caenorhabditis elegans
Function: May have a role in pharyngeal pumping during feeding.
Subcellular location: Cell membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- G-protein coupled receptor seb-2
- Teneurin-1
Sequence:
MAKQLKYPFLIFIISLAQCQVSNQNVNLCQSNICQNGGTCLVASSVPATATCPKNSIYYMGSCYVFDTTLRNWNDAALYCNNMNSATLPLVESAEDQAFFAGYLQAMIPSNPPADMRPPPDGIWTAVRGVNNVTRASWVYYPGSFLVTDTFWAPQEPNIYVNYNDVCVALQSDSFYREWTTALCTILKYTVCKVAPTQIQAKYVAQCSCPNGYGGQTCETQSTTNQQASTQRTCGSNDFQFSCPNDQTITVDFASFGAQESSMCNQASQSREQTCSNVNSLQTVINACQGLQSCEIRNLTSTFSNTPCPVPQEQYLETRMRCETAQQPSCLSGLIQFDSRCYSMTIETNEKKQRTMEDAQTYCSQSGGSIITSPPDALLQQIVQKVNAETKKTVNFWIGTPNNCQLLMVTGSSTSYSQCPSSPSSTANVICSTVPQSTASVSARPTQSAPVDPVSQTMARREVYTGVQPPSVPDSINKPRYCKKEKKDGITYEQTRACMLHEQPCPDPQNVEGTVTRYCNCQTAKWETPDTTNCTHRWVAEMETAIKDNQPVEDISSTVNRQLKSTIERTLFGGDITGTVRLSNDMLSLARNQFSVLNDRNLRENKARNFTENLGGSGDQLLSPVAATVWDQLSSTIRIQHASKLMSVLEQSVLLLGDYMTDQKLNLQYINWAMEVERSEPEVQTFGAAASPNVQDDMGMMRVMAAAPPAPQPETNTTIMFPSLKLSPTITLPSASLLSSLASPTPVAGGGPSILSSFQDDTPVGMASTPNLNRNPVKLGYYAFAGFGQLLNNNNDHTLINSQVIGASIQNATQSVTLPVDHPVTFTFQHLTTKGVSNPRCVYWDLMESKWSTLGCTLIATSSNSSQCSCTHLTSFAILMDISGQVGRLSGGLASALDVVSTIGCAISIVCLALSVCVFTFFRNLQNVRNSIHRNLCLCLLIAELVFVIGMDRTGNRTGCGVVAILLHYFFLSSFCWMLLEGYQLYMMLIQVFEPNRTRIFLYYLFCYGTPAVVVAISAGIKWEDYGTDSYCWIDTSTPTIWAFVAPIIVIIAANIIFLLIALKVVLSVQSRDRTKWGRIIGWLKGSATLLCLLGITWIFGFLTAVKGGTGTAFAWIFTILNCTQGIFIFVLHVVLNEKVRASIVRWLRTGICCLPETSSAAYNSRSFLSSRQRILNMIKVNGHSYPSTASTDDKEKQLTPITKTTDWLSRLPNQDSVSIPESNFNNLNGTLENSNLNSAEIKEEDEIPELRRRVTVDLNPMIVSNNEIERMSHASSDPRGSQIIEVTAVEKKAPVKRIKFPLGAKQSERGSQHRTKAKVIAPPESPVSESGSKDYRF
Protein: Rho guanine nucleotide exchange factor 5 (H0Y895)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XVVVPTLKQHSHPPPLALGSGLHAPHKGPLPQASDPAVARQHRPLPSTPDSSHHAQATPRWRYNKPLPPTPDLPQPHLPPISAPGSSRIYRPLPPLPIIDPPTEPPPLPPKSRGRSRSTRGGHMNSGGHAKTRPACQDWTVPLPASAGRTSWPPATARSTESFTSTSRSKSEVSPGMAFSNMTNFLCPSSPTTPWTPELQGPTSKDEAGVSEHPEAPAREPLRRTTPQQGASGPGRSPVGQARQPEKPSHLHLEKASSWPHRRDSGRPPGDSSGQAVAPSEGANKHKGWSRQGLRRPSILPEGSSDSRGPAVEKHPGPSDTVVFREKKPKEVMGGFSRRCSKLINSSQLLYQEYSDVVLNKEIQSQQRLESLSETPGPSSPRQPRKALVSSESYLQRLSMASSGSLWQEIPVVRNSTVLLSMTHEDQKLQEVKFELIVSEASYLRSLNIAVDHFQLSTSLRATLSNQEHQWLFSRLQDVRDVSATFLSDLEENFENNIFSFQVCDVVLNHAPDFRRVYLPYVTNQTYQERTFQSLMNSNSNFREVLEKLESDPVCQRLSLKSFLILPFQRITRLKLLLQNILKRTQPGSSEEAEATKAHHALEQLIRDCNNNVQSMRRTEELIYLSQKIEFECKIFPLISQSRWLVKSGELTALEFSASPGLRRKLNTRPVHLHLFNDCLLLSRPRESEKLRWISALAMPREELDLLECYNSPQVQCLRAYKPRENDELALEKADVVMVTQQSSDGWLEGVRLSDGERGWFPVQQVEFISNPEVRAQNLKEAHRVKTAKLQLVEQQA
Protein: Ras-related protein Rab-5C (EC 3.6.5.2) (L1880) (RAB5L) (P51148)
Organism: Homo sapiens (Human)
Function: Protein transport. Probably involved in vesicular traffic.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}; Cytoplasmic side {ECO:0000250|UniProtKB:P20339}. Early endosome membrane {ECO:0000250|UniProtKB:P20339}; Lipid-anchor {ECO:0000250|UniProtKB:P20339}. Melanosome {ECO:0000269|PubMed:17081065}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. {ECO:0000269|PubMed:17081065}.
Interaction partners:
- Ras-related protein Rab-5A
- Early endosome antigen 1
- Ras-related protein Rab-5B
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Rab GDP dissociation inhibitor beta
- Ras and Rab interactor 1
- Rab GDP dissociation inhibitor alpha
- Rabenosyn-5
- Rab proteins geranylgeranyltransferase component A 1
- Rab GTPase-binding effector protein 1
Sequence:
MAGRGGAARPNGPAAGNKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQTVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNTDTFARAKNWVKELQRQASPNIVIALAGNKADLASKRAVEFQEAQAYADDNSLLFMETSAKTAMNVNEIFMAIAKKLPKNEPQNATGAPGRNRGVDLQENNPASRSQCCSN
Protein: Adenylate cyclase (EC 4.6.1.1) (ATP pyrophosphate-lyase) (Adenylyl cyclase) (P00936)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the formation of the second messenger cAMP from ATP. Its transcript is probably degraded by endoribonuclease LS (rnlA), decreasing cAMP levels and the negative regulator Crp-cAMP, which then induces its own transcription again.
Subcellular location: Cytoplasm.
Interaction partners:
- DNA-binding transcriptional dual regulator CRP
- 3',5'-cyclic adenosine monophosphate phosphodiesterase CpdA
- PTS system glucose-specific EIIA component
- GTP pyrophosphokinase
- Pyruvate kinase I
- Anaerobic ribonucleoside-triphosphate reductase
- Bifunctional
- Pyruvate kinase II
- Nucleoside diphosphate kinase
- Nucleoside triphosphate pyrophosphohydrolase
Sequence:
MYLYIETLKQRLDAINQLRVDRALAAMGPAFQQVYSLLPTLLHYHHPLMPGYLDGNVPKGICLYTPDETQRHYLNELELYRGMSVQDPPKGELPITGVYTMGSTSSVGQSCSSDLDIWVCHQSWLDSEERQLLQRKCSLLENWAASLGVEVSFFLIDENRFRHNESGSLGGEDCGSTQHILLLDEFYRTAVRLAGKRILWNMVPCDEEEHYDDYVMTLYAQGVLTPNEWLDLGGLSSLSAEEYFGASLWQLYKSIDSPYKAVLKTLLLEAYSWEYPNPRLLAKDIKQRLHDGEIVSFGLDPYCMMLERVTEYLTAIEDFTRLDLVRRCFYLKVCEKLSRERACVGWRRAVLSQLVSEWGWDEARLAMLDNRANWKIDQVREAHNELLDAMMQSYRNLIRFARRNNLSVSASPQDIGVLTRKLYAAFEALPGKVTLVNPQISPDLSEPNLTFIYVPPGRANRSGWYLYNRAPNIESIISHQPLEYNRYLNKLVAWAWFNGLLTSRTRLYIKGNGIVDLPKLQEMVADVSHHFPLRLPAPTPKALYSPCEIRHLAIIVNLEYDPTAAFRNQVVHFDFRKLDVFSFGENQNCLVGSVDLLYRNSWNEVRTLHFNGEQSMIEALKTILGKMHQDAAPPDSVEVFCYSQHLRGLIRTRVQQLVSECIELRLSSTRQETGRFKALRVSGQTWGLFFERLNVSVQKLENAIEFYGAISHNKLHGLSVQVETNHVKLPAVVDGFASEGIIQFFFEETQDENGFNIYILDESNRVEVYHHCEGSKEELVRDVSRFYSSSHDRFTYGSSFINFNLPQFYQIVKVDGREQVIPFRTKSIGNMPPANQDHDTPLLQQYFS