wanglab/gogpt-training-data huggingface dataset:
Protein: GRAAL2 protein (Q9BI19)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMAQWLLGLWLAILLVHRPGAKAYRSGSGYHSEQSEPVGLSATGNAHSSYGGDQQQPIYHRDSACPPHFTGLVAYPHDCHRYVNCFDGSPTIQTCSPGTLFNDRTQVCDHPSNVVCPSAESASTRLGRLRQLDSEPKCQPGVNGLQPHPSDCSKFLNCANGQAFIMDCAPGTAFSPASLVCVHKDLAKCGSGTGAVRDDTSGTGYPALPFDDLGCPPGTRGLRPHPHDVHKYLRCGIGVKPQVEQCPRGHIFDGSSSVCVYSDSPRTSSSSFTSAEIQVNYLLCPVGAVGQFVHPFDQTKFLSCKDGKSAVQNCQPNYVFSISRRYCQLKAQLAFTDYVTLIISEISYEYSLILKSCPGNINGIFLYPYDAKKYVQCSSGGRMSILSCGPQMAFSVSQRSCLPSHQVHISDRVQFWQEVQVQTTYTSQDLRANVQSQLSSLRSCPPNVQKNYPYPFHAGHYVRCQYGALEIICCPTGQRYSLSHRQCVPRSLLSAHDYLDYSYISAELSTEFMVDRSTLSCPPQAQGLYLHPFDCTKYVRCWNQQTFIESCTPGEIFSFSNQKCVPKEQCKGPTDHVEYLIETTTVTTYDSDGPESASSLAKTGDISCPPGASGNHAHPFDCTKFLECSNGETFVKNCGPGTAFSTAKHICDHANQVDCSGRNSLPEQSQVTQNNIATSYPTKPLDILPILKTSPPSYPHAEHLTDLLCPSGVNGQFVHPFDQTKFLLCQAGKLAVQSCQSGYVFSISKSICQPKTQLVYSDYVTYKVSVISIDQTAKSMILSACPDGTNGLHLYPYDAGKYVRCSDGGKMSIQSCENQMAFSSSERACRPSRLLSTEDRVRFREELQIQTTYSSQDIQIQQSPLKECPSVLRGNYPYPFHAGHFVNCQNGHLQIVSCPPTALYSLSQRECVVRQLLSPHDYLDYAYISVQFSTNIIHDTTALSCPPQAQGYYLHPFDCTKYIVCWEKQTHIESCPQGEAFSISQQKCVARDKITQAYDRVEYLEDTQHELSHEEAEEEEQTEPESNLSLDGGNQPPGKYQAPYYSNGGYPTPSQNNGGYQTPSQNNGGYQAPFQNNGGYQPSYQGNGGYTPTYQNPFEGYHQPNQSSYQTNGGYQPPLPPHGGYQPPSQTYGGFQQPNRTYEDFHNPSQTVGGFQPPYSVKGGYQPHNQLNGGYNQPNQSSSFQANGGYQPPSQVNRGYQTSFESNGGYQPPLETNKGHQVPSQINGGYQPRVDGNRGYQPPNELNGGYQPPNELNGAYPAPSQLNGGYQPPLEGNLGYRPLSQQNSGYQPPQPSTGGYQPPFQSTGSGHYPGQDAPYAIPTPLLCPEKVSGLFPNPFDATGYLTCIDGHTLPRQCQPLDVFSVSQGYCLPEQHVNKTDRVPFERTQTYQDNSLDCPRDFLGFVVYPFDCSKYLSCGPSGMKLLNCPGEQHYSISHGFCKPVDQVQREDRLYTINELHIIFEWTQKMMIVGAVTACPEGITGTLPHPRVPTKYLRCGPGQAEMYDCPSQQIFSVSRRVCVLDDKLSSYDRTDYLVRGVNSGWMDPSNDNRQSKSYETSGRDQFGNRYTTRTTTTTRVIGDRWTDMNMQRPSGVGVEQNPHHHHHGYNPGWSGQETSYVQRGPTQSTLYVEGSLQPNHARETSRTEQTLDPSTTYASTNFQRSTRRAELDPDTLTATTMKTNWHAPGHSRDYHRRHPNLPDPFTEHHPNSSPHQHQHHHRHPHEHSADFHLRHPELPNPFPLKNETPQHQDLNDDWDLLPNSNAEEVTPKLATRSSFNTQCDFDCGNGQCLKKEEICDGKKNCPNGKDEANCPPSDYEVRLSGGESPNMGRIEVKANGQWGYVCDDKFGLKDADVVCRELGFQMGAQEVRGSSFYAPPNQDFNYLMDEVECHGNETKLGQCAFKGWGVHNCGVDEVAGVTCKVPVMKCPNNYWLCHTSKECIPPAFVCDNTPDCADKSDECAAVCQAPVQYRLEGGRNSNEGRLEVKHHGVWGSVCDDDFNLKSAQVACNSMGFFGPAKIEKNIFGNSNGPIWLDQVMCFGNETSIDQCNHWNWGEHNCNHTEDVALHCSAGPPPRSQRYSQTQIKGGRSLGRETTPKTYSQIGLWERSSKAVHTPRRCGIFKDDLTDEYAHREERVVRGNVAQRGRHPWQATIRTRGRGGISSHWCGAVVISKRHLLTAAHCLYGSPKGAYFVRVGDHYANIAESSEVDSFIENWYLHENFRKGTHMNNDIALVVLKTPLKFSDYVQPICLPDKNAELVEDRKCTISGWGSIKSGVSTPAQVLGSAELPILADHVCKQSNVYGSAMSEGMFCAGSMDESVDACEGDSGGPLVCSDDDGETLYGLISWGQHCGFKNRPGVYVRVNHYIDWIYEKINESLLRF
Protein: Fructose-1,6-bisphosphatase isozyme 2 (FBPase 2) (EC 3.1.3.11) (D-fructose-1,6-bisphosphate 1-phosphohydrolase 2) (Muscle FBPase) (O00757)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate.
Subcellular location: Cell junction {ECO:0000250}. Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere, Z line. Note=In neonatal cardiomyocytes, distributed throughout the cytosol, accumulating in the intercalated disks which occur at the Z line of cardiomyocytes and connect adjacent cells, and also located in the nucleus; dissociates from the Z line following an increase in cytosolic Ca(2+) concentration (By similarity). In muscle precursor cells, localizes predominantly to the nucleus and to a lesser extent to the cytoplasm at the proliferative phase, while mainly localizing to the cytoplasm at the differentiation phase (By similarity). Colocalizes with ALDOA and alpha-actinin on both sides of the Z line of skeletal muscle; dissociates rapidly from the Z line following an increase in cytosolic Ca(2+) concentration. {ECO:0000250}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Transaldolase
- ATP-dependent 6-phosphofructokinase, muscle type
- Fructose-1,6-bisphosphatase 1
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 2
- 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase 3
- ATP-dependent 6-phosphofructokinase, liver type
- ATP-dependent 6-phosphofructokinase, platelet type
- Transketolase-like protein 2
- Fructose-bisphosphate aldolase B
Sequence:
MTDRSPFETDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMVQSSYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILGSPEDVQEYLTCVQKNQAGS
Protein: Ribokinase (RK) (EC 2.7.1.15) (Q9H477)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P25332, ECO:0000255|HAMAP-Rule:MF_03215}. Nucleus {ECO:0000250|UniProtKB:P25332, ECO:0000255|HAMAP-Rule:MF_03215}.
Interaction partners:
- Ribose-5-phosphate isomerase
- Deoxyribose-phosphate aldolase
- Transketolase
- Transketolase-like protein 2
- Transketolase-like protein 1
- Ribose-phosphate pyrophosphokinase 3
- Ribose-phosphate pyrophosphokinase 2
- Ribose-phosphate pyrophosphokinase 1
- Phosphopentomutase
- Glucose-6-phosphate isomerase
Sequence:
MAASGEPQRQWQEEVAAVVVVGSCMTDLVSLTSRLPKTGETIHGHKFFIGFGGKGANQCVQAARLGAMTSMVCKVGKDSFGNDYIENLKQNDISTEFTYQTKDAATGTASIIVNNEGQNIIVIVAGANLLLNTEDLRAAANVISRAKVMVCQLEITPATSLEALTMARRSGVKTLFNPAPAIADLDPQFYTLSDVFCCNESEAEILTGLTVGSAADAGEAALVLLKRGCQVVIITLGAEGCVVLSQTEPEPKHIPTEKVKAVDTTGAGDSFVGALAFYLAYYPNLSLEDMLNRSNFIAAVSVQAAGTQSSYPYKKDLPLTLF
Protein: tRNA splicing endonuclease subunit 54 (Q9VTV4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- tRNA-splicing endonuclease subunit Sen34
- tRNA splicing endonuclease subunit 15, isoform A
- tRNA-intron lyase
- Protein CLP1 homolog
- 2'-phosphotransferase
- Probable arginine--tRNA ligase, mitochondrial
- tRNA
Sequence:
MDTKTQDSEYVEIHPKNSYLSAQELIAHRHTEFEPPSGGLKRTKNEGTAAEVEELKRAQEYLRAQLSVPRIERLGGRALAIWNEEQQVAEVKRKDGKFENFGYSEQGKLYLEYYEAMFLLEVGRLQLEYCGLVVSIEQAYVLLLGELESERYTNYLVYSALSRSGYIVVKHVPPKEIPQEVTSADCIWALLKEKVGNLPVPDHIKTSPIYPIAEKRMEDLKELITSQKAEDPNIVVDPIDLKFGQRKRMAVEKPIEEPASKKEKFSTTGRSLVDQLKGEFAYAKFEEIFEKFDLVQLESQDYTKDELDTPSALKIIFDLHLHNRGFKKSAPNAPNFNVIILPSQVAFPTHDKISKIKHLLTAPLLVISVSESKQIQAFLYYIS
Protein: Dephospho-CoA kinase, putative (EC 2.7.1.24) (Q583T2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- riboflavin kinase
Sequence:
MLLVGLTGGIACGKSTVSLLLKESHHIVVVDSDLVVRELQRPFMPCTRKIARRWPNCVDPQSGEVNRAALGSIIFSDPSARRALARIMNFPIFRATMKMVIGLWWQSLRQQLRGQGPLLVVLDVPLLYESNIYTWLVDRVVVVSCSEEQQVERMAKRNGLTREQALQRINAQMPISEKCKRADRVIHNEESLSELEHSVADTVAWMQQQSGGRVAFALSGALAVGVSLGAVVVYCCLRIVF
Protein: Dachs, isoform E (M9MRE4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Serine/threonine-protein kinase Warts
- Extracellular serine/threonine protein kinase four-jointed
- SH3 domain-containing protein Dlish
- Insulin-like receptor
- TATA-box-binding protein
- Cadherin-related tumor suppressor
- Transcription initiation factor IIB
- Discs overgrown protein kinase
- Transcription initiation factor TFIID subunit 2
- Negative cofactor 2alpha
Sequence:
MLLPDQTYADYDVGRHQLLTYHKSRSRGLKSKLQRSKSSDASSSSYERTVDFFENIPDFHGESLSTFLYSPSAEQDAQAKGDEVRLERNRLADDDEDQDSESTSQSDDCEDDDVLRLCEDFLCRHRMRPDFFCQYHKAVSSTTPSPKQTKTSTPIVQCKSASPPVKVQSDLKDFKSNRTSAVVERFAKFSAIYTLPVPKRKKACNKTTGNITDASSSNEAVHLQQRLKSLSTELVTLRNRLHVGHGPGQGQSQGNGAQPVAPAPNAGPKANNFDLNASSPNLNLSSSGAGLSASAVQQHTNGHHTTSKNHSFSHTLPANSGSGGGGGAGGGAVVSARNTSIPHPLPHQLAEKPGLSHQQSGSGHGQSTGTLPHMSGMGSILGQNSHSHAPVNNNSNNSNTLPMRTSNSGHLGINGGGVGHHLSHAHSQQLPFIPQSKHTNPCQSVKTLPFGFGFSESQQKMQQQQQQGNSSPKDMQDLIHLSGPLTEHAVMRTLQARFNERRYFTNVGPILLSINPYLDVGNPLTLTSTRAMPLAPQLQKIVQEAVRQQSETGYPQAIILSGTSGAGKTANAMLMLRQLFAIAGGGPETDAFKHLAAAFTVLRSLGSAKTTTNSESSRIGQFIEVQVTDGALYRTKIHCYFLDQTRVIRPLPKEKNYHIFYQLLAGLSREERQKLHLDGYSPANLRYLRGDIGQNEQEDAARFQAWKTCLGILGIPFLDVVRVLAAVLLLGNVQFIDGGGLEVDVKGETELNSVASLLGVPPAALFRGLTTRTHNVRGQLVKSVCGDGDANMTRDCLAKALYCRTVATIVRRANSLKRLGSTLGTLSSDSNESVHNQADVASQHASTIGGGNAGSKSMAALNNAVRHATSDGFIGILDMFGFEEPSPHAHLEHLCINLCAETMQHFYNTHIFKSSVESCRDEGIVCDTEVDYVDNVPCIDLISSLRTGLLSMLDAECSVRGTAESYVTKLKVQHRSSTRLETKPTAEPHDPRMFLIRHFAGRVEYDTTDFLDTNRDVVPDDLVGVFYKHTCNFGFATHLFGSELKALYAQQQAPRGLSFRISPTSHSDLLNGDEPVSTLTQDFHTRLDNLLRTLVHARPHFVRCIRSNGTEAARSFDRATVVRQIRSLQVLETVNLMASGFPHRMRFKQFNARYRMLAPFRLLRRSEDKALEDCQLILKYAMEQPPVLDGSVTLAWAPGKRHVFLSEGIRQHLEHLRTEIRHKSATLMQATWRGWWWRKKMGNGGAKRSKIPGLQQAPLPNNKTTPNSAAQNKAASSTMAALAAVAAAAPISVPRLSAKTTSLGIGGTVARPRPQPIAGTPPPDPQEKCDQKIIQQTCNLFGLDLERPPPVPPSRSYTITGNSKISYPQNRVMKMNFPEEGQSEAPQLKKGEAVTVVGASTVRGHLMVEHKGQSFHVPFQFMTLSK
Protein: Protein CASC3 (Q9VB04)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cytoplasm, Stress granule {ECO:0000256|ARBA:ARBA00004210}. Cytoplasm, perinuclear region {ECO:0000256|ARBA:ARBA00004556}. Nucleus speckle {ECO:0000256|ARBA:ARBA00004324}.
Interaction partners:
Sequence:
MAEVEKPTAATPPTDIPQATAAPASEAPVAVTPTADTTVDVEPGTSPTQEPNSNSHPHDSEYDTASDLEGGEDYDDEESASGSASGSGSEEESETDDEDDEVGSETDDGEGEQAMDRSVADSEAQKKVDEDRSNPQYIPKRGTFYEHDDRTAETEGEILIEPENGAGQAAAEPNGELNGLAAAGATPTGQTPQISQASKTMRKWQPASGGDRWSHDRFEATEQAPKSRAELLQTYGYDIRNEDAPPRARRRRRYTRGPSKYSRNWEDEQAYLKASNKERKPPRPQDFPALNERKPRGPRTSSSREEKENRRSVAAEGLVPEKQQPLASSSNPHRSQERERERERERERDREPKNRNFGRMNGGPGRQNGMEFKKNNRGQQLRERERGPDQLDNRNQKPSTPRSNQQQQPQQQPHHQQQPQQQRQPSQPQQSPQTPLSTSNLSQRLQQVQQRNDPSHVGSVQMHSLASQNQAPQQQQQQPLHQEQRNAPKRYSSLRRSQQEASQHLAEQQQQQMQQQLHLQQQQQQQQSQIMIQDPHVLMQIAYQQQELQAQLQTMQLGPPTAAGAVPTPPKPHAPPAAAYPQAQAAPYYVTGTEPVPVPVPQAPYVNPASAAYLPTTPAAVAYAQAGPPVVTQPTPPPAQAPPATQPAQPYQNYNTVGGTTYFVPPAQTTSRPSALPQRRPTNAIPILPPSEKHKVKGGAKEEGISDNIDHIIDNMFVQRPSAFQATGEGATPGGGTKEEAAATPPAAEQNLQPVPATGQE
Protein: Probable fatty acyl-CoA reductase 5 (EC 1.2.1.84) (Q0WRB0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the reduction of fatty acyl-CoA to fatty alcohols. Catalyzes specifically the formation of C18:0 fatty alcohol. Provides the fatty alcohols required for synthesis of suberin in roots, seed coat and wound-induced leaf tissue. Provides the fatty alcohols required for synthesis of alkyl hydroxycinnamates in root waxes.
Interaction partners:
- Wax ester synthase/diacylglycerol acyltransferase 1
- Omega-hydroxypalmitate O-feruloyl transferase
- Cytochrome P450 86B1
- Glycerol-3-phosphate acyltransferase 5
- Cytochrome P450 86A1
- Fatty alcohol:caffeoyl-CoA acyltransferase
- 3-ketoacyl-CoA synthase 2
- Transcription factor MYB41
- Probable 3-ketoacyl-CoA synthase 21
- 3-ketoacyl-CoA synthase 20
Sequence:
MELNCVQFLRNKTILVTGATGFLAKVFVEKILRVQPNVKKLYLLVRASDNEAATKRLRTEVFEKELFKVLRQNLGDEKLNTLLYEKVVSVPGDIATDQLGINDSHLRERMQKEIDIVVNVAATTNFDERYDVGLGINTFGALNVLNFAKKCVKVQLLLHVSTAYVCGEKPGLIPEKPFIMEEIRNENGLQLDINLERELMKQRLKELNEQDCSEEDITLSMKELGMERAKLHGWPNTYVFTKSMGEMLLGKHKENLPLVIIRPTMITSTLSEPFPGWIEGLRTVDSVIIAYGKGVLKCFLVDVNSVCDMIPVDMVANAMITAAAKHAGGSGVHMVYHVGSSHQNPVTFGEIHEIAVRYFTKNPLRSRNGSLITVSKVRFIPTMALFSLYMTLRYKLPLQLLKLVDIIYPWRNGDKYGDKNRKIELVMRLVELYEPYVLFKGIFDDRNTKSLCANQKEEEIKNTEKLMFDFDPKGINWGDYLTNIHISGLVTHVLKK
Protein: G2/mitotic-specific cyclin-B1 (P30277)
Organism: Rattus norvegicus (Rat)
Function: Essential for the control of the cell cycle at the G2/M (mitosis) transition.
Subcellular location: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}.
Interaction partners:
- Cell division cycle protein 20 homolog
- Cyclin-dependent kinase 1
- Serine/threonine-protein kinase PLK1
- Cyclin-dependent kinase 2
- Cell division cycle protein 27 homolog
- Baculoviral IAP repeat-containing protein 5
- Anaphase-promoting complex subunit 4
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Anaphase-promoting complex subunit 10
- Fizzy-related protein homolog
Sequence:
MALRVTRNTKINTENKAKVSMAGAKRVPVAVAASKPLLRSRTALGDIGNKVSEQSRIPLKKETKKLGSGTVTVKALPKPVDKVPVCEPEVELDEPEPEPVMEVKHSPEPILVDTPSPSPMETSGCAPAEEYLCQAFSDVILAVSDVDADDGGDPNLCSEYVKDIYAYLRQLEEEQSVRPKYLLGREVTGNMRAILIDWLIQVQMKFRLLQETMYMTVSIIDRFMQDSCVPKKMLQLVGVTAMFIASKYEEMYPPEIGDFAFVTNNTYTKHQIRQMEMKILRVLNFSLGRPLPLHFLRRASKIGEVDVEQHTLAKYLMELSMLDYDMVHFAPSQIAAGAFCLALKILDNGEWTPTLQHYLSHTEESLLPVMQHLAKNIVMVNRGLTKHMTIKNKYATSKHAKISTLAQLNCTLVQNLSKAVTKA
Protein: Myogenic factor 6 (Myf-6) (Muscle-specific regulatory factor 4) (Q01795)
Organism: Gallus gallus (Chicken)
Function: Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein.
Subcellular location: Nucleus.
Interaction partners:
- PAX7 protein
- Paired box 3
- Myocyte enhancer factor 2D
- Myocyte enhancer factor 2B
- Myogenic factor 5
- Growth/differentiation factor 8
- Myoblast determination protein 1 homolog
- Transcription factor 12
Sequence:
MMMDLFETGSYFFYLDGENGALQQLEMAEGSPLYPGSDGTLSPCQDQLPPEAGSDSSGEEHVLAPPGLQPPHCPGQCLIWACKTCKRKSAPTDRRKAATLRERRRLKKINEAFEALKRRTVANPNQRLPKVEILRSAISYIERLQDLLHRLDQQDKMQEVAADPFSFSPKQGNVPGSDFLSTCGSDWHSASDHSRALGGSPKAGGSMVESSASSSLRCLSSIVDSISSDEPKLPGAEEAVEK
Protein: KH domain-containing, RNA-binding, signal transduction-associated 1b (KH domain-containing, RNA-binding, signal transduction-associated protein 1b) (Zgc:85948) (Q6NW62)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transmembrane emp24 domain-containing protein 1a precursor
- mRNA-capping enzyme
- Transcription factor 25
- Tyrosine-protein kinase
- Tyrosine-protein kinase.
Sequence:
MESENKYLPQLLAERDSLDPSFTHAMKLISAEIEKIEKGDTEKDTESYLDLFTMKNIKLKERILIPVKQYPKFNFVGKILGPQGNTIKRLQEETGAKISVLGKGSMRDKNKEEELRKNGEPKYAHLSMELHVFIEVFAPVPDAYMRMAHAMEEIKKFLFPDMMDDICQEQFMEMKFLNGGQEHGGRGRGGPPIRGRGGLPPPGAPRGRGMPPRGGGRGGPPRGGAARGAPAGRGGPSAQLPRGAASNRARPPAPGAPRMPPPPQTQESYDEYSYDESYADTGYESYDSYYSQPQAAETEYYDYGHGETQEGYENYAQDNWNGTPRTAAAAGGKAPTQRQTKPGFREHPYGRY
Protein: Uncharacterized protein (Q388I3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIHPKLMPYQELALRRVNVQQQSFASQYVGTDKIGGGGATAITPSGSSAGMSRTTSARSEVALSPGTVFPGPSATPASSAIQKSRPHARDALLTGCGTNSTAPASIARPGIKRRDEWSTALHDIEPFVLPQQLLCGSPPNRQKHVRVHYIADQYDRQWLTQLPVATTTTKGKTGSIESSVTPQATRHKISLTLFEDLITAFELGSYMNAEVPIHRQPVSTFEGVTATGADTTVVEEVRRYWLSKRQALGGNVPCIPALRMDVREDNQNSLCHSDILQYCPLPFSYRDCPVPLVKRLLPRCAAREENTGGENGGQKEVVGRKRERRSCESGIKIEDHNDETVVEVGELERQMLATAGLKVAQAVLEREEWKLAHTHIVLYELSLLRRLSVLDGDVSPSVGFPSSSSHAGGGHASTLWASDEDLQGEWVGENELGGEPYDSVTGRGAAAALESVMAIERRHC
Protein: RNA polymerase sigma-K factor (Sigma-27) (Stage IV sporulation protein CB) (P12254)
Organism: Bacillus subtilis (strain 168)
Function: Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is responsible for the expression of sporulation specific genes in the mother cell.
Interaction partners:
Sequence:
MVTGVFAALGFVVKELVFLVSYVKNNAFPQPLSSSEEKKYLELMAKGDEHARNMLIEHNLRLVAHIVKKFENTGEDAEDLISIGTIGLIKGIESYSAGKGTKLATYAARCIENEIVITKGGCIHPSLIRFNIYGVRIHNGNFFHDKVNNCFFIFKSMPPLFVMNNEILMHLRALKKTKKDVSLHDPIGQDKEGNEISLIDVLKSENEDVIDTIQLNMELEKVKQYIDILDDREKEVIVGRFGLDLKKEKTQREIAKELGISRSYVSRIEKRALMKMFHEFYRAEKEKRKKAKGK
Protein: MucC (SoxR reducing system protein RseC) (Transcriptional regulator) (Q57429)
Organism: Pseudomonas aeruginosa
Interaction partners:
Sequence:
MIEEQGRVVATEPGAVWVETVRRSTCSSCSANAGCGQGLMQRLGVGAGRARVRALSDLSLRVGDAVVLGIHEDLLLRASVLFYLFPLLGFFVAALLATRAGLVEPLIIVSGLAGLLAAWLLVRRHARRHADDPASQPVVLRALISGPSDSA
Protein: Blue light- and temperature-regulated antirepressor BluF (Blrp) (P75990)
Organism: Escherichia coli (strain K12)
Function: Binds to and releases the BluR repressor from its bound DNA target in a blue light-dependent (470 nm) fashion. A shift to low temperature also triggers a BluF-mediated relief of repression by BluR, suggesting BluF may serve as a thermometer. Blue light may act to increase the affinity of BluF for BluR, allowing it to be released from its operator. The protein has a reversible photocycle, and undergoes structural changes, probably in the EAL domain, in response to light.
Interaction partners:
- HTH-type transcriptional repressor BluR
- Probable diguanylate cyclase DgcF
- Probable diguanylate cyclase CdgI
- Cyclic di-GMP phosphodiesterase PdeH
- Probable diguanylate cyclase DgcI
- Diguanylate cyclase DgcM
- Cyclic di-GMP phosphodiesterase PdeL
- Diguanylate cyclase DgcP
- Probable two-component-system connector protein YmgA
- Probable diguanylate cyclase DgcE
Sequence:
MLTTLIYRSHIRDDEPVKKIEEMVSIANRRNMQSDVTGILLFNGSHFFQLLEGPEEQVKMIYRAICQDPRHYNIVELLCDYAPARRFGKAGMELFDLRLHERDDVLQAVFDKGTSKFQLTYDDRALQFFRTFVLATEQSTYFEIPAEDSWLFIADGSDKELDSCALSPTINDHFAFHPIVDPLSRRIIAFEAIVQKNEDSPSAIAVGQRKDGEIYTADLKSKALAFTMAHALELGDKMISINLLPMTLVNEPDAVSFLLNEIKANALVPEQIIVEFTESEVISRFDEFAEAIKSLKAAGISVAIDHFGAGFAGLLLLSRFQPDRIKISQELITNVHKSGPRQAIIQAIIKCCTSLEIQVSAMGVATPEEWMWLESAGIEMFQGDLFAKAKLNGIPSIAWPEKK
Protein: Pentatricopeptide repeat-containing protein DWY1, chloroplastic (DYW-domain protein 1) (P0C7R1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a major role in single RNA editing events in chloroplasts. Acts as a site-recognition transacting factor involved in the edition of the site 1 of ndhD (ndhD-1 site corresponding to cytidine-2), which is a plastid-encoded subunit of the NADH-plastoquinone oxidoreductase. The interaction with CRR4 is required for its function in editing the ndhD-1 site.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:23001034}.
Interaction partners:
- Pentatricopeptide repeat-containing protein At2g45350, chloroplastic
- NAD
- Multiple organellar RNA editing factor 9, chloroplastic
- Multiple organellar RNA editing factor 2, chloroplastic
- Multiple organellar RNA editing factor 8, chloroplastic/mitochondrial
- Organelle RRM domain-containing protein 1
- Zinc finger protein VAR3, chloroplastic
- Multiple organellar RNA editing factor 1, mitochondrial
- Pentatricopeptide repeat-containing protein At3g02330, mitochondrial
Sequence:
MALEAAFSMSFCSFSVPKAIFCERETSSFQRITSRAKGIAGESQVQSSDGVETQVKETSPKVFDKLPERNLDTWSGGRETARGLSGSVVRNTVRKDTTLRHISPSSHSTKVRGDKPEISGGEKKAIVDRSKAYVKLKSLGKEVRDAGYVPETKYVLHDIDEEAKEKALMHHSERLAIAFGIINTPPGTTIRVMKNLRICGDCHNFIKILSSIEDREIIVRDNKRFHHFRDGNCSCGDYW
Protein: General regulatory factor 9 (F4IP55)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGSGKERDTFVYLAKLSEQAERYEEMVESMKSVAKLNVDLTVEERNLLSVGYKNVIGSRRASWRIFSSIEQKEAVKGNDVNVKRIKEYMEKVELELSNICIDIMSVLDEHLIPSASEGESTVFFNKMKGDYYRYLAEFKSGNERKEAADQSLKAYEIATTAAEAKLPPTHPIRLGLALNFSVFYYEIMNAPERACHLAKQAFDEAISELDTLNEESYKDSTLIMQLLRDNLTLWTSDISEEGGDDAHKTNGSAKPGAGGDDAEVSIRDSFTRGKSN
Protein: N-acetyltransferase domain-containing protein (O01546)
Organism: Caenorhabditis elegans
Interaction partners:
- AAA_lid_7 domain-containing protein
- FIP
- ELM2 domain-containing protein
- Nose resistant-to-fluoxetine protein N-terminal domain-containing protein
- C-type lectin domain-containing protein
- PAW domain-containing protein
- DUF4140 domain-containing protein
- G-protein coupled receptors family 1 profile domain-containing protein
- C-type lectin domain-containing protein
- SNF2 N-terminal domain-containing protein
Sequence:
MGVTTDLNVPKGIKVVLNPTQEYFDQFQEWITETERWNYRRTEYKLWCTAFEKFWLYMAIDEENDECVSVVSLALQRNSDGKKLYSIGNYYCVPEWRGRGVSNKLFVQVMKHVGKENCTLFGAVKMSPLYATRFNFALMNEFWHMFADIDVVDLVIPAMPNGFTCKKIEDNDWEKLHEYDETICDLDRRKFMKMNLSVAGTIARIVFNESGKIVGFGAIKMATGNELIMSPLYAETLDAATALMSTLLKGIPAILSFSSLITIYPDVNNDVPRLLSLISNNNYETHQAYRHQFTEEMMDFPQHKIYGTDEISHSPC
Protein: Probable 3',5'-cyclic phosphodiesterase pde-5 (EC 3.1.4.17) (P91119)
Organism: Caenorhabditis elegans
Function: Redundantly with pde-1, plays a role in the AFD thermosensory neurons to regulate microvilli receptive ending morphology, possibly by regulating cGMP levels.
Interaction partners:
- adenylate cyclase
- Adenylate kinase
- Adenosine kinase
- AMP deaminase
- GMP reductase
- Probable adenylate kinase isoenzyme ZK673.2
- guanylate kinase
- Putative cytosolic 5'-nucleotidase 3
- 5'-nucleotidase
- Adenylate kinase isoenzyme 1
Sequence:
MDDASVLKYLQENPKLVEDFVVSNEISPETFKRWAVRRTMKYKNVKNGTSGGTGAWTEPDLSMKRRVILETSDNRTRILYEITQCCGQLIGTNSIELIVQNDEGAFSCRKTENGELKLKKVKTSKSADYIQTIVNAGNQTIAEIHFYTQLDSTEKSIVNAVCTWAAATNYYSELYTHKQEGSDGQDIHENIAKQRKLSNFLLDVARSIFHDIVSMDAVIIKVMNFAQKLVDADRASLFLVDSKNAQIYARIFDVGTGDEEHVRVNSEGQKEIRFDMSKGIAGYVASTGEGLNIENAYEDERFNADVDSKTGYTTKTILCMPILIRGIVIGVVQMVNKHDGVFTRQDEDAFEIFAVYCGLALHHAKLYDKIRRSEQKYRVALEVLAYHSVCNADEVNKLKKIEINNRIVELETIDFNGMRLSELEKPLYAVYMFKTLFADTLRFDTEDLIRFVLTVRKNYRRVAYHNWAHGWSVAHAMFATLMNSPDAFTKLEALALYVSCLCHDLDHRGKNNAYMKTMSTPLASIYSTSVMERHHFNQTVTILQQDGHNILKSLSSEDYKKTLSLIKHCILATDLALFFSNKAKLNVILDNNTFDINRQEHRLLTQAVMMTGCDLVASAKPWNIQTETVKVIFEEFYDQGDAERLSGKEPIPMMDRQQAHMLPQMQVGFMRGICMPCYDLIARIFPKNDKMRERCEYNAKKWEELAEEQRKKQEALAQQNGEANETQE
Protein: Aldehyde dehydrogenase family 3 member A2 (EC 1.2.1.3) (EC 1.2.1.94) (Aldehyde dehydrogenase 3) (Fatty aldehyde dehydrogenase) (P47740)
Organism: Mus musculus (Mouse)
Function: Catalyzes the oxidation of medium and long-chain aliphatic aldehydes to fatty acids. Active on a variety of saturated and unsaturated aliphatic aldehydes between 6 and 24 carbons in length. Responsible for conversion of the sphingosine 1-phosphate (S1P) degradation product hexadecenal to hexadecenoic acid.
Subcellular location: Membrane {ECO:0000269|PubMed:25286108}. Microsome membrane {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein {ECO:0000250|UniProtKB:P51648}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P51648}; Single-pass membrane protein {ECO:0000250|UniProtKB:P51648}; Cytoplasmic side {ECO:0000250|UniProtKB:P30839}.
Interaction partners:
- Peroxisomal bifunctional enzyme
- Aldo-keto reductase family 1 member A1
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Acetyl-coenzyme A synthetase, cytoplasmic
- 4-aminobutyrate aminotransferase, mitochondrial
- Aldehyde oxidase 1
- Aldehyde oxidase 3
- Alpha-aminoadipic semialdehyde dehydrogenase
- Amine oxidase [flavin-containing] B
Sequence:
MERQVLRLRQAFRSGRSRPLRFRLQQLEALRRMVQEREKEILAAIAADLSKSELNAYSHEVITILGEIDFMLGNLPELASARPAKKNLLTMMDEAYVQPEPLGVVLIIGAWNYPFVLTMQPLVGAIAAGNAAIVKPSELSENTAKILAELLPQYLDQDLYAIVNGGIPETTELLKQRFDHILYTGNTAVGKIVMEAAAKHLTPVTLELGGKSPCYIDRDCDLDVACRRIAWGKYMNCGQTCIAPDYILCEASLQNQIVQKIKETVKDFYGENIKASPDYERIINLRHFKRLQSLLKGQKIAFGGEMDEATRYLAPTILTDVDPNSKVMQEEIFGPILPIVSVKNVDEAINFINDREKPLALYVFSRNNKLIKRVIDETSSGGVTGNDVIMHFTVNSLPFGGVGASGMGAYHGKYSFDTFSHQRPCLLKGLKGESVNKLRYPPNSESKVSWAKFFLLKQFNKGRLGMLLFVCLVAVAAVIVKDQL
Protein: Stationary-phase-induced ribosome-associated protein (Protein D) (SRA) (30S ribosomal protein S22) (P68191)
Organism: Escherichia coli (strain K12)
Function: Although this protein associates with the 30S subunit of the ribosome it is not considered to be a bona fide ribosomal protein.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:21903814}. Note=Enriched in the periphery of the cell, excluded from the nucleoid (PubMed:21903814). {ECO:0000269|PubMed:21903814}.
Interaction partners:
- Small ribosomal subunit protein bS16
- Small ribosomal subunit protein bS18
- Ribosome-associated ATPase
- Small ribosomal subunit protein uS9
- Ribosome-associated inhibitor A
- DNA protection during starvation protein
- Protein ElaB
- Peroxiredoxin OsmC
- Small ribosomal subunit protein uS2
- Small ribosomal subunit protein uS14
Sequence:
MKSNRQARHILGLDHKISNQRKIVTEGDKSSVVNNPTGRKRPAEK