wanglab/gogpt-training-data huggingface dataset:
Protein: Eukaryotic translation initiation factor 4B, isoform F (L7EEF1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASAGKKGKKNKGTVISLQSFLCNSDAPVGTTQVSKKIRNLDGDDSDDGSGTLPLVYQLPTAPRANRIFDDNSIPHKAPFIAYINNLPFDANEDDLYEFFEGINLISLRLPREDGENGRSRGFGYVELENREDLIHVLSLPDPSIKGRRIRIELSNENDQQSRQKSNRRFDGFGNNGDNRDSGNWRRDSQNNGSNFGYSSNFERSFNRERKSLPDRDDVNTPGSWRTSARPQSIDTSPTRREVEQVSEKYREGRVKIADRYSREETSKVEEERPKLNLKPRTLPLPDVKTIEFEKCDVDEFNLDKQGGTSSLNVFGSAKPVDTAARELEIEQRLALARKQDKGRREQGLNEKLAELQVDKNDNESLSATVSWRTNQDYKESDKINKCPGRNF
Protein: N-terminal acetyltransferase A complex catalytic subunit NAA10 (AtNAA10) (EC 2.3.1.255) (Q9FKI4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalytic subunit of the NatA N-alpha-acetyltransferase complex. Required for male gametocyte development, embryogenesis, suspensor development and the formation of the quiescent center (QC) in the root meristem. Involved in plant immunity through the regulation of SNC1 and RPM1 stability.
Interaction partners:
- N-terminal acetyltransferase A complex auxiliary subunit NAA15
- Acyl-CoA N-acyltransferases
- DNA-binding enhancer protein-like protein
- N-terminal acetyltransferase B complex auxiliary subunit NAA25
- Histone acetyltransferase MCC1
- N-alpha-acetyltransferase 60
- GCN5-related N-acetyltransferase 4, chloroplastic
- Large ribosomal subunit protein uL23z
- Large ribosomal subunit protein uL23y
- Large ribosomal subunit protein uL18y
Sequence:
MVCIRRATVDDLLAMQACNLMCLPENYQMKYYLYHILSWPQLLYVAEDYNGRIVGYVLAKMEEESNECHGHITSLAVLRTHRKLGLATKLMTAAQAAMEQVYEAEYVSLHVRRSNRAAFNLYTETLGYKINDVEAKYYADGEDAYDMRKNLKGKQNHHHAHGHHHHHGGGCCSGDAKVVETAQAVDGKAVSK
Protein: Uncharacterized protein C4D7.07c (O14173)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein C2G2.14
- Centromere protein mis12
Sequence:
MMSRKRQASSNDFFDMEQLLIANDALVHQNHSTPNHASDELSVNDPSPLSRGLQSDVNSNISRNISNTFFKKSIFFFVYYCKQALEFISTVFSIIKFLLNRRKVSFLLSFLLLFSLFLLIPNDGRVNIKFFYKDFVDRIPFRFIPSNFNISFGKHLEQAKSLFKSKFGNSSSTYNERDSIMPLLKLQSNLTEAKTLLYQNPISPEDVLLHFWDRNLMSTYDLKIQDINDSVNPLLNTYLDFIEKDIYLVSHLPVSEKHPGNIPISLVNKSVQAICSFAEHYNLLRNPSYRGFLRINNGESIFNLLCIEDLHESVNLDILCLKDILRNIAQSSKEAMYIVKRHNSSQSFYGNRSTTNFSIINSGLYLKKDAAKNLLAKQFDATYSYYHKDLEESVHQKLNSNLEKRVEKYIKHSCSQRNVADHPDFALKVVGAVVDYGWTFPKPKFSDILRDYWGKKANLPTALLDTSINSNWCNYEDTVQVSVRLNRPMYVRHISLIFPIHGDDSYFPREIQMFGLINDINYQILSNMNNLVLLATIPVSLSSVFEVNYYYLPKFSDTPGLLEEAYFNTFVFRAFSKNESLTSQICLYHIGIHGKEINEEF
Protein: Vomeronasal type-1 receptor 52 (Pheromone receptor VN3) (Vomeronasal receptor 3) (Vomeronasal type-1 receptor A7) (Q9EP79)
Organism: Mus musculus (Mouse)
Function: Putative pheromone receptor implicated in the regulation of social and reproductive behavior.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MNKDHTLYCSVYIRNAFFSEIGIGISANSCLLLFHTFMFIRGHRPRLTDLPIGFVALIHLVMLLLAAYITEDFFMSSGGWDDITCKLVIFLHRFFRSLSVCATCLLSVFQAIILCPQSSHLAKLKQNSPHQLSYFFIFLSIFYTSISSHILIAAIPTQNITFVNLIYITNSCSFLPLSSSMQHTFSTLLAFRNVFVIGLMGLSTCYMATLLCRHKTRSQRLQNSKLSPKATPEQRALRTILMLMSFFLLMSTFDSIISYSRTILQGNPLPFCFQILVAHSYAAVSPLLVLSNEKRITNLLISMYEKIVL
Protein: Melanoma-associated antigen D2 (11B6) (Breast cancer-associated gene 1 protein) (BCG-1) (Hepatocellular carcinoma-associated protein JCL-1) (MAGE-D2 antigen) (Q9UNF1)
Organism: Homo sapiens (Human)
Function: Regulates the expression, localization to the plasma membrane and function of the sodium chloride cotransporters SLC12A1 and SLC12A3, two key components of salt reabsorption in the distal renal tubule.
Interaction partners:
- Nucleosome assembly protein 1-like 1
- Nucleosome assembly protein 1-like 4
- Guanine nucleotide-binding protein G
- Melanoma-associated antigen D1
- Cellular tumor antigen p53
- Guanine nucleotide-binding protein G
- Chondrosarcoma-associated gene 1 protein
Sequence:
MSDTSESGAGLTRFQAEASEKDSSSMMQTLLTVTQNVEVPETPKASKALEVSEDVKVSKASGVSKATEVSKTPEAREAPATQASSTTQLTDTQVLAAENKSLAADTKKQNADPQAVTMPATETKKVSHVADTKVNTKAQETEAAPSQAPADEPEPESAAAQSQENQDTRPKVKAKKARKVKHLDGEEDGSSDQSQASGTTGGRRVSKALMASMARRASRGPIAFWARRASRTRLAAWARRALLSLRSPKARRGKARRRAAKLQSSQEPEAPPPRDVALLQGRANDLVKYLLAKDQTKIPIKRSDMLKDIIKEYTDVYPEIIERAGYSLEKVFGIQLKEIDKNDHLYILLSTLEPTDAGILGTTKDSPKLGLLMVLLSIIFMNGNRSSEAVIWEVLRKLGLRPGIHHSLFGDVKKLITDEFVKQKYLDYARVPNSNPPEYEFFWGLRSYYETSKMKVLKFACKVQKKDPKEWAAQYREAMEADLKAAAEAAAEAKARAEIRARMGIGLGSENAAGPCNWDEADIGPWAKARIQAGAEAKAKAQESGSASTGASTSTNNSASASASTSGGFSAGASLTATLTFGLFAGLGGAGASTSGSSGACGFSYK
Protein: Nectin cell adhesion molecule 1 (A0A8I5ZLI7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell junction, adherens junction {ECO:0000256|ARBA:ARBA00004536}. Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MARMGLAGAAGRWWGLALGLTAFFLPGTHTQVVQVNDSMYGFIGTDVILHCSFANPLPTVKITQVTWQKASNGSKQNMAIYNPTMGVSVLPPYEKRVEFLRPSFIDGTIRLSHLELEDEGMYICEFATFPTGNRESQLNLTVMAKPTNWIEGTQAVLRARKGQDDKVLVATCTSANGKPPSVVSWETRLKGEAEYQEIRNPNGTVTVISRYRLVPSREAHRQSLACIVNYHLDRFRESLTLNVQYEPEVTIEGFDGNWYLQRTDVKLTCKADANPPATEYHWTTLNGSLPKGVEAQNRTLFFRGPINYSLAGTYICEATNPIGTRSGQVEVNITEKPFPQGGPGSATRLLGGALAMVLILGMTLAVFLLYRWQQKSQLGIDISGMDLSPSQKLEPTPDRESQLAPEDIQGLHLELGRQQEEDLPLQPPYYDLGVSPTYQPLVSMAKP
Protein: Sodium channel protein Nach (Pickpocket protein 4) (O61365)
Organism: Drosophila melanogaster (Fruit fly)
Function: Part of a complex that plays a role in tracheal liquid clearance. Probable role in sodium transport.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Putative gustatory receptor 36c
- Osiris 10a
- Putative gustatory receptor 98c
- Ionotropic receptor 67c
- Major facilitator superfamily
- Peptidase M14 domain-containing protein
- FI01017p
- Putative gustatory receptor 58c
- Metalloendopeptidase
- Potassium channel domain-containing protein
Sequence:
MGHQEELKPEQVDLKVTPFVGYLRRTWSDFCATSSIHGLKYTRDEDTNKIVHLVWLLISVVMFICAVVMARTFYMDYRSSPTRMNVESDNTPVNRLYFPPVTICPDVLFNMQKSEAFLNTLRLPKGAELRGILRKLHIFYGFMLDDERYSAEDIEQMEALLFLNNLTIPEFVEHLRWNCDEILYRCRFNGEIMDCSKIFQLSKTFFGHCCSFNLRQKGWVNNKLNNLESFKVFHLNSLNFTAQRAIGGLRYGLSVVVRYKDDNYDPLQSYSYGVKLLIQEADAFPSAHSAAKFIAFNSETFAAVRPQETFCSSAVKALIIEERNCVFQNEFPMRYFSDYVYPNCELNCRVTNMVKFCGCHTYFFDFNRTSDRICTFRDIPCLVDNFANIITRKKSTQCYCPLTCEHIDYDVQLTNFPLELNMPVADKFYSGLAKNDGVLHVFINSFSYRRLRRDLLSNMVTLVSNLGSAFSLFVGMSMLSVVEIIYYFSVILRKNYKLECETRSQMLHKKPKFAWPKANDTHSKEQKSVFIIHKS
Protein: Nostrin (BM247 homolog) (Nitric oxide synthase traffic inducer) (Nitric oxide synthase trafficker) (eNOS-trafficking inducer) (Q8IVI9)
Organism: Homo sapiens (Human)
Function: Multivalent adapter protein which may decrease NOS3 activity by inducing its translocation away from the plasma membrane.
Subcellular location: [Isoform 1]: Cell membrane {ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:16376344}; Peripheral membrane protein {ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:16376344}; Cytoplasmic side {ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:16376344}. Cytoplasmic vesicle {ECO:0000269|PubMed:12446846}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16234328, ECO:0000269|PubMed:16376344}. Note=Enriched in selected actin structures (PubMed:16234328, PubMed:16376344).; SUBCELLULAR LOCATION: [Isoform 3]: Nucleus {ECO:0000269|PubMed:18980613}.
Interaction partners:
- Nitric oxide synthase 3
- Caveolin-1
- Dynamin-2
- Actin nucleation-promoting factor WASL
Sequence:
MRDPLTDCPYNKVYKNLKEFSQNGENFCKQVTSVLQQRANLEISYAKGLQKLASKLSKALQNTRKSCVSSAWAWASEGMKSTADLHQKLGKAIELEAIKPTYQVLNVQEKKRKSLDNEVEKTANLVISNWNQQIKAKKKLMVSTKKHEALFQLVESSKQSMTEKEKRKLLNKLTKSTEKLEKEDENYYQKNMAGYSTRLKWENTLENCYQSILELEKERIQLLCNNLNQYSQHISLFGQTLTTCHTQIHCAISKIDIEKDIQAVMEETAILSTENKSEFLLTDYFEEDPNSAMDKERRKSLLKPKLLRLQRDIEKASKDKEGLERMLKTYSSTSSFSDAKSQKDTAALMDENNLKLDLLEANSYKLSSMLAELEQRPQPSHPCSNSIFRWREKEHTHSYVKISRPFLMKRLENIVSKASSGGQSNPGSSTPAPGAAQLSSRLCKALYSFQARQDDELNLEKGDIVIIHEKKEGGWWFGSLNGKKGHFPAAYVEELPSNAGNTATKA
Protein: S-formylglutathione hydrolase (EC 3.1.2.12) (Q7KSB5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU363068}.
Interaction partners:
- Alcohol dehydrogenase class-3
- Carnosine dipeptidase 2, isoform A
- Vacuolar protein sorting-associated protein 29
- Branched-chain-amino-acid aminotransferase
Sequence:
MGRNFLRLPSVSGRSSFVYSIVACSNLPKRRSIVLSFGHIMTENMTLEQLSANKCFEGEQRVYRHRSDTLKCDMTFGVFLPPAALEGKPCPVLFFLSGLTCTHENFIQKSGFQQHAARHNLIVVNPDTSPRGVEIAGQDDAYDFGSGAGFYVDAKEEPWSKHYKMYSYVTQELVDVVNANLPVVPGKRGIFGHSMGGHGALICALKNPGLYQSVSAFAPIANPTECPWGKKAFAGYLGSNPDDWALWDATHLVSQYESTPQELFIDQGAADNFLAGKQLLPENLLAAADGNDHIQTIFKQREGYDHSYFYIATFVAEHIAYHAALLTASA
Protein: Glycerol kinase (EC 2.7.1.30) (ATP:glycerol 3-phosphotransferase) (Glycerokinase) (GK) (O51257)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Function: Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate.
Interaction partners:
- Glycerol-3-phosphate dehydrogenase, anaerobic
- Glycerol uptake facilitator
- PTS system glucose-specific EIIA component
- Glycerol-3-phosphate O-acyltransferase, putative
- Transmembrane protein
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- Periplasmic serine protease DO
- Triosephosphate isomerase
- RNA polymerase sigma factor
- Putative ankyrin repeat protein BB_0399
Sequence:
MKYILSIDQGTTSSRAMVFDKNANIKGFAQKEFTQIYPQPSWVEHDPTEIWGSQLGVITEAMANARILPNEIDAIGITNQRETTVIWEKNTGKPIYNAIVWQDRRTAKICDQLKKEGKDKIILEKTGLVLDSYFSGTKIMWILDNVEGARQRAENGELCFGTIDTWILWNLTQKKEHATDYSNASRTLLLNIKTLEWDDELLSILNVPRAILPELKESSTIYGKTDKALFGAEIPIAGIAGDQFAATFGQACLKKGMAKNTYGTGCFLTVNIGKEPIISHDKLLTSIAWGRKKSVTYVLEGSVFIGGAVIQWLRDGLEFFRKSSDAEALASSVSDNGGVYFVPAFVGLGAPHWDSYARGTIIGITRGSTKAHITRAALESIAFQSFDILNTMKKSIPNFEIQELRVDGGASQNNLLMQFQADLLECKVVRPKITETTALGAAYLAGLATGYWQSAEEIVSLWQVDKIFEPSMPKNQKEKLLENWNKAVGKAKSWIQNSHSS
Protein: Penicillin-binding protein activator LpoB (PBP activator LpoB) (Lipoprotein activator of PBP from the outer membrane B) (P0AB38)
Organism: Escherichia coli (strain K12)
Function: Regulator of peptidoglycan synthesis that is essential for the function of penicillin-binding protein 1B (PBP1b). Stimulates transpeptidase and transglycosylase activities of PBP1b in vitro. May also contribute to outer membrane constriction during cell division, in complex with PBP1b.
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}; Lipid-anchor {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}; Periplasmic side {ECO:0000269|PubMed:21183073, ECO:0000269|PubMed:21183074}. Note=Localizes to the divisome and to the lateral wall.
Interaction partners:
- Penicillin-binding protein 1B
- Uncharacterized protein YcfL
- Penicillin-binding protein 1A
- Cell division protein FtsN
- Penicillin-binding protein activator LpoA
- Purine nucleoside phosphoramidase
- Thiamine kinase
- UPF0227 protein YcfP
- Peptidoglycan D,D-transpeptidase FtsI
- Cell division coordinator CpoB
Sequence:
MTKMSRYALITALAMFLAGCVGQREPAPVEEVKPAPEQPAEPQQPVPTVPSVPTIPQQPGPIEHEDQTAPPAPHIRHYDWNGAMQPMVSKMLGADGVTAGSVLLVDSVNNRTNGSLNAAEATETLRNALANNGKFTLVSAQQLSMAKQQLGLSPQDSLGTRSKAIGIARNVGAHYVLYSSASGNVNAPTLQMQLMLVQTGEIIWSGKGAVSQQ
Protein: Pseudokinase FAM20A (Q96MK3)
Organism: Homo sapiens (Human)
Function: Pseudokinase that acts as an allosteric activator of the Golgi serine/threonine protein kinase FAM20C and is involved in biomineralization of teeth. Forms a complex with FAM20C and increases the ability of FAM20C to phosphorylate the proteins that form the 'matrix' that guides the deposition of the enamel minerals.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q8CID3}. Golgi apparatus {ECO:0000269|PubMed:23468644}. Endoplasmic reticulum {ECO:0000250|UniProtKB:Q8CID3}.
Interaction partners:
- Extracellular serine/threonine protein kinase FAM20C
- Enamelin
- Ameloblastin
- Amelotin
- Amelogenin, X isoform
- Protein FAM83H
- Serine protease 23
- Matrix remodeling-associated protein 8
- WD repeat-containing protein 72
Sequence:
MPGLRRDRLLTLLLLGALLSADLYFHLWPQVQRQLRPRERPRGCPCTGRASSLARDSAAAASDPGTIVHNFSRTEPRTEPAGGSHSGSSSKLQALFAHPLYNVPEEPPLLGAEDSLLASQEALRYYRRKVARWNRRHKMYREQMNLTSLDPPLQLRLEASWVQFHLGINRHGLYSRSSPVVSKLLQDMRHFPTISADYSQDEKALLGACDCTQIVKPSGVHLKLVLRFSDFGKAMFKPMRQQRDEETPVDFFYFIDFQRHNAEIAAFHLDRILDFRRVPPTVGRIVNVTKEILEVTKNEILQSVFFVSPASNVCFFAKCPYMCKTEYAVCGNPHLLEGSLSAFLPSLNLAPRLSVPNPWIRSYTLAGKEEWEVNPLYCDTVKQIYPYNNSQRLLNVIDMAIFDFLIGNMDRHHYEMFTKFGDDGFLIHLDNARGFGRHSHDEISILSPLSQCCMIKKKTLLHLQLLAQADYRLSDVMRESLLEDQLSPVLTEPHLLALDRRLQTILRTVEGCIVAHGQQSVIVDGPVEQLAPDSGQANLTS
Protein: Exostosin-1 homolog (Multiple exostoses homolog 1) (Related to mammalian RIB protein 1) (O01704)
Organism: Caenorhabditis elegans
Function: Required for the biosynthesis of heparan sulfate by positively regulating N-acetylglucosamine transferase II (GlcNAcT-II) and glucuronyl transferase II (GlcAT-II) activities of glycosyltransferase rib-2. Probably not directly involved in chondroitin sulfate biosynthesis but negatively regulates chondroitin sulfate levels. Maternally required for normal ventral epidermal enclosure and for embryo elongation during the early stages of embryonic development. In addition, involved in the elongation of the pharyngeal isthmus and in the organization of the actin cytoskeleton in the pharyngeal muscles during the later stages embryonic development. In adults, regulates egg-laying and the normal morphogenesis of the vulva. Also involved in the directed migration of hermaphrodite-specific neurons.
Subcellular location: Endoplasmic reticulum {ECO:0000305}. Golgi apparatus {ECO:0000305}.
Interaction partners:
- Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase 1
- HtrL domain containing
- Probable dual specificity protein kinase madd-3
- Heparan-sulfate 6-O-sulfotransferase
- D-glucuronyl C5-epimerase
- Heparan sulfate 2-O-sulfotransferase hst-2
- Sulfotransferase domain-containing protein
- Sulfotransferase domain-containing protein
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase sqv-8
Sequence:
MQNVMKFHLVIFMLFGSVRLQNPTIERKQCTMSNCFDFSKCSTSKKVYIHPMEKRFEESPQSVIYSKILKHFLESNHYTNDPNEACIFLLGIDTTDRDVRSQNYVKNVNDYIESLDPSVWNNGRNHLIFNFYHGTFPDYDDHNLNFDTGEAMIARASSSENNFIKVFDVSLPLFHENHPYEIKESKSERNDDRIENQRKYLVSFKGKRYVYGIGSGTRNLVHHLHNGDDIVMVTTCKHNNDWQVYQDDRCQRDNDEYDRWEYDELLANSTFCLVPRGRRLGSFRFLETLRSGCVPVVISDSWILPFSETIDWNSAAIVVAERDALSIPELLMSTSRRRVKELRESARNVYDAYLRSIQVISDHVLRIIFKRIDNKIELEDHQ
Protein: Sorting nexin-31 (Q8N9S9)
Organism: Homo sapiens (Human)
Function: May be involved in protein trafficking.
Interaction partners:
Sequence:
MKMHFCIPVSQQRSDALGGRYVLYSVHLDGFLFCRVRYSQLHGWNEQLRRVFGNCLPPFPPKYYLAMTTAMADERRDQLEQYLQNVTMDPNVLRSDVFVEFLKLAQLNTFDIATKKAYLDIFLPNEQSIRIEIITSDTAERVLEVVSHKIGLCRELLGYFGLFLIRFGKEGKLSVVKKLADFELPYVSLGSSEVENCKVGLRKWYMAPSLDSVLMDCRVAVDLLYMQAIQDIEKGWAKPTQAQRQKLEAFQKEDSQTKFLELAREVRHYGYLQLDPCTCDYPESGSGAVLSVGNNEISCCITLPDSQTQDIVFQMSRVKCWQVTFLGTLLDTDGPQRTLNQNLELRFQYSEDSCWQWFVIYTKQAFLLSSCLKKMISEKMVKLAAENTEMQIEVPEQSKSKKYHIQQSQQKDYSSFLSRKSKIKIAKDDCVFGNIKEEDL
Protein: Cathelicidin-3 (CATH-3) (Fowlicidin-3) (Q2IAL6)
Organism: Gallus gallus (Chicken)
Function: May bind bacterial lipopolysaccharide (LPS). May have antimicrobial activity and play a role in the innate immune response (By similarity).
Subcellular location: Secreted {ECO:0000250}. Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cathelicidin-2
- Cathelicidin-B1
- Cathelicidin-1
- Transcription factor p65
- Nuclear factor NF-kappa-B p105 subunit
- Transcription factor Jun
- Gallinacin-1
- Gallinacin-2
- Gallinacin-7
- Transforming growth factor beta regulator 4.
Sequence:
MLSCWVLLLALLGGACALPAPLGYSQALAQAVDSYNQRPEVQNAFRLLSADPEPGPNVQLSSLHNLNFTIMETRCQARSGAQLDSCEFKEDGLVKDCAAPVVLQGGRAVLDVTCVDSMADPVRVKRFWPLVPVAINTVAAGINLYKAIRRK
Protein: Forkhead box protein G1 (O73862)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00089}.
Interaction partners:
Sequence:
MLDMGERKEVKMIPKSSFSINSLVPEAVQSDNHHHHHHQQQQHHHRTVHEEEEKTPLPAQVQEQKSENTCAKSDNSSHDSSSTDEKEKQEEKRDAKEGEGGKEGDKKNGKYEKPPFSYNALIMMAIRQSPEKRLTLNGIYEFIMKNFPYYRENKQGWQNSIRHNLSLNKCFVKVPRHYDDPGKGNYWMLDPSSDDVFIGGTTGKLRRRSTTSRAKLAFKRGARLTSTGLTFMDRAGSLYWPMSPFLSLHHPRASSALSYNGASSAYPSHPMSYSTMLTQNSLGNNHSFPASNGLSVDRLVNGEIPYATHHLTAAALAASVPCGLSVPCSGTYSLNPCSVNLLAGQTSYFFPHVPHPSMTSQSSTSMSSRAASSSSPQTASSLPCDSLRPSLSSFSSGLSSGLSDYFTHQNQGSTSNPLIH
Protein: V-type proton ATPase subunit a, Golgi isoform (V-ATPase a 2 subunit) (Similar to VPH1 protein 1) (V-ATPase 101 kDa subunit) (V-ATPase subunit AC115) (Vacuolar proton translocating ATPase subunit a 2) (P37296)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons. V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartments. Is present only in Golgi- and endosome-residing V-ATPase complexes; enzymes containing this subunit have a 4-fold lower ratio of proton transport to ATP hydrolysis than complexes containing the vacuolar isoform and do not dissociate V1 and V0 in response to glucose depletion.
Subcellular location: Endosome membrane {ECO:0000269|PubMed:7514599}; Multi-pass membrane protein {ECO:0000255}. Golgi apparatus membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:7514599}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- V-type proton ATPase catalytic subunit A
- V-type proton ATPase subunit d
- V-type proton ATPase subunit c''
- V-type proton ATPase subunit B
- V-type proton ATPase subunit H
- V-type proton ATPase subunit E
- V-type proton ATPase subunit D
- V-type proton ATPase subunit c'
- V-type proton ATPase subunit G
- V-type proton ATPase subunit F
Sequence:
MNQEEAIFRSADMTYVQLYIPLEVIREVTFLLGKMSVFMVMDLNKDLTAFQRGYVNQLRRFDEVERMVGFLNEVVEKHAAETWKYILHIDDEGNDIAQPDMADLINTMEPLSLENVNDMVKEITDCESRARQLDESLDSLRSKLNDLLEQRQVIFECSKFIEVNPGIAGRATNPEIEQEERDVDEFRMTPDDISETLSDAFSFDDETPQDRGALGNDLTRNQSVEDLSFLEQGYQHRYMITGSIRRTKVDILNRILWRLLRGNLIFQNFPIEEPLLEGKEKVEKDCFIIFTHGETLLKKVKRVIDSLNGKIVSLNTRSSELVDTLNRQIDDLQRILDTTEQTLHTELLVIHDQLPVWSAMTKREKYVYTTLNKFQQESQGLIAEGWVPSTELIHLQDSLKDYIETLGSEYSTVFNVILTNKLPPTYHRTNKFTQAFQSIVDAYGIATYKEINAGLATVVTFPFMFAIMFGDMGHGFILFLMALFLVLNERKFGAMHRDEIFDMAFTGRYVLLLMGAFSVYTGLLYNDIFSKSMTIFKSGWQWPSTFRKGESIEAKKTGVYPFGLDFAWHGTDNGLLFSNSYKMKLSILMGYAHMTYSFMFSYINYRAKNSKVDIIGNFIPGLVFMQSIFGYLSWAIVYKWSKDWIKDDKPAPGLLNMLINMFLAPGTIDDQLYSGQAKLQVVLLLAALVCVPWLLLYKPLTLRRLNKNGGGGRPHGYQSVGNIEHEEQIAQQRHSAEGFQGMIISDVASVADSINESVGGGEQGPFNFGDVMIHQVIHTIEFCLNCISHTASYLRLWALSLAHAQLSSVLWDMTISNAFSSKNSGSPLAVMKVVFLFAMWFVLTVCILVFMEGTSAMLHALRLHWVEAMSKFFEGEGYAYEPFSFRAIIE
Protein: Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta (A0A6I8MWY4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MRQWSPPPQLGAGAQPAGRGDPLISAPIPPPRLRRASGWKDPTYPRPTEPSLERASSKCQPGTPAASLCLADSPDQHRTMPPGPASRANVGSRPHTVANGHELFEVSEERDEEVAAFCHMLDILRTGSDIQDYSLTGCVWSTVTPSPEHLGDEVNLKVTVLCDSLREPLTFTCNCSSTVDLLIHQTLCYTHDELREVDVGDFVLKPCGLEEFLQNKHALGSHEYIQYCRKFDISIRLQLM
Protein: HNF1 homeobox a (Hepatocyte nuclear factor 1-alpha) (Q8UVH4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|PROSITE-ProRule:PRU00108}.
Interaction partners:
Sequence:
MDGGESRRSEGSGRLSALQEQLVWSLLGSGLSKELLIQAMGDLERERASSGGERADRADCESSEEGEMDNPPPIYRELEKLPPEEAARQRAQVDQLLQEDPWHVAKMVKSYMQQHNLPQREVVESTGLNQSHLSQHLNKGTPMKNQKRAALYSWYTKKQAEISQQFTNASRGVMSGEEPGEDVRKGRRNRFKWGPASLQILFQAYERQKNPSKEEREGLVEECNRAECLQRGVSPSQLAGLGSNLVTEVRVYNWFANRRKEEAFRHKLALDVPYSSQSAASTCQTLPSSPSPGLKYSQTVVCESLGTVRSSGGEDRGASVRLASPVQLEPSHTLLETHHHKPASVGGSLPPVSTLTSLHGMSGSSAGAPGLFIPSVMSLGDSSLLIGLTSSQPQTVPIINNVGGGFTTLQPISFQQPLHASPQQPIAQQLQSHIAPSSFMATMAQLPCHMYSKADLSSYPSSSLLSQAMVIADSSSIGTLTNLTAVRQILTTDPEGHTESAIEEESLHLQSTSPEPGSSGSLDLYPQSQTSETHSSHLQLSSPAGDIDPYIPAQMVSTAQ
Protein: Aldehyde dehydrogenase, dimeric NADP-preferring (EC 1.2.1.5) (Aldehyde dehydrogenase 4) (Aldehyde dehydrogenase family 3 member A1) (Dioxin-inducible aldehyde dehydrogenase 3) (P47739)
Organism: Mus musculus (Mouse)
Function: ALDHs play a major role in the detoxification of alcohol-derived acetaldehyde (Probable). They are involved in the metabolism of corticosteroids, biogenic amines, neurotransmitters, and lipid peroxidation (Probable). Oxidizes medium and long chain aldehydes into non-toxic fatty acids. Preferentially oxidizes aromatic aldehyde substrates. Comprises about 50 percent of corneal epithelial soluble proteins. May play a role in preventing corneal damage caused by ultraviolet light.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25286108}.
Interaction partners:
- All-trans-retinol dehydrogenase [NAD
- All-trans-retinol dehydrogenase [NAD
- Cytochrome P450 2E1
- Alcohol dehydrogenase class-3
- Alcohol dehydrogenase 1
- Aldo-keto reductase family 1 member A1
- Amine oxidase [flavin-containing] A
- Amine oxidase [flavin-containing] B
- Acetyl-coenzyme A synthetase, cytoplasmic
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
Sequence:
MSNISSIVNRARDAFNSGKTRPLQFRVEQLEALQRMINENLKGISKALASNLRKNEWTSYYEEVAHVLDEIDFTIKGLSDWAEDEPVAKTRQTQEDDLYIHSEPLGVVLVIGAWNYPFNLTIQPMVGAIAAGNAVVLKPSEVSDHMADLLSTLIPQYMDKDLYPVIKGGVPETTELLKEKFDHIMYTGSTAVGKIVMAAAAKHLTPVTLELGGKSPCYVDKDCDLDVACRRIAWGKFMNSGQTCVAPDYILCDPSIQNEIVEKLKKSLKDFYGEDAKQSHDYGRIINDRHFQRVINLIDSKKVAHGGTWDQPSRYIAPTILVDVDPQSPVMQEEIFGPVMPIVCVRSLDEAIKFINQREKPLALYVFSNNDKVIKKMIAETSSGGVTANDVIVHITVPTLPFGGVGNSGMGAYHGKKSFETFSHRRSCLVRSLRNEEANKARYPPSPAKMPRH
Protein: Transcriptional regulator BlaI (P9WMJ5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Transcription regulator that binds to an inverted DNA repeat with the consensus sequence 5'-TAC[GT]AC-NNNNN-GT[AC]GTA-3' and regulates genes involved in antibiotic transport, detoxification and cell wall function. Also regulates its own transcription. Binds DNA as a dimer.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Possible sensor-transducer protein BlaR
- GMP reductase
- 6-phosphogluconate dehydrogenase, decarboxylating
Sequence:
MAKLTRLGDLERAVMDHLWSRTEPQTVRQVHEALSARRDLAYTTVMTVLQRLAKKNLVLQIRDDRAHRYAPVHGRDELVAGLMVDALAQAEDSGSRQAALVHFVERVGADEADALRRALAELEAGHGNRPPAGAATET
Protein: Pectate lyase E (EC 4.2.2.2) (Q5B7Z3)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Pectinolytic enzyme consist of four classes of enzymes: pectin lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Among pectinolytic enzymes, pectin lyase is the most important in depolymerization of pectin, since it cleaves internal glycosidic bonds of highly methylated pectins. Favors pectate, the anion, over pectin, the methyl ester.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Pectinesterase A
Sequence:
MYQPLLLLPLLLTSAFANPHDPHIHHSLEKRASFPIPSSKGSVTFSSPKTISGTFDGGMKTYGRGVKCTGQDEGGDEDAVFILKDGATLKNAIIGADQIEGVHCEGSCTIENVWWTDVCEDALSLKGSGSGTHKIIGGGARNADDKVIQHNSGGKVIIQDFTVQNFGKLYRACGNCKKQFKRTVKISGVKASSGKALVGINSNYGDTASIKGCATSVKEICVEYEGTNNNSKEPKKKSSGPSSYCKYSEPLSKC
Protein: DShc (Q24080)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPKNGDAGNRSGSGTTSDGCIYPDDVIMGVGVAFNVRYTGCVEVKTSMKSLDFETRTQLARECINRVCEAAGLKSAGKRRLTNFISDRPSMQHAGTNIIINVSSRALSLSNVETGEVIANHNMPRISFASGGDNDTLDFLAYIAKNEDEWAACYVLECAGGQSEDLIVTIGKAFALRFNALSRLNDPSADCNINQSCKENVKEYYNDLPNKLPPEVPEPQQQQVQQPLHPHAPRVAQLNLKKPRDRLSSNLIDLNSPPPDQTTNKLGHFDPLQATTAANSVLPSVRDVFDGPQCPLTAEVWFHAGISRPISERLLQQDGDFLVRESQGKRGQYVLTGLEGKTPKHLLLIDPEGVVRTKDRIFDSISHLINYHWAHALPIISEDSELVLRNPVRRPQQDQAASPITSASS