wanglab/gogpt-training-data huggingface dataset:
Protein: NADH dehydrogenase [ubiquinone] iron-sulfur protein 3, mitochondrial (Q86NC2)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable NADH dehydrogenase flavoprotein 2, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 9, mitochondrial
- Probable NADH dehydrogenase iron-sulfur protein 7, mitochondrial
- NADH dehydrogenase 1 beta subcomplex subunit 6
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 12
- NADH dehydrogenase 1 beta subcomplex subunit 9
- NADH dehydrogenase 1 beta subcomplex subunit 4
- NADH dehydrogenase 1 beta subcomplex subunit 8
- NADH dehydrogenase 1 beta subcomplex subunit 11, mitochondrial
- Probable NADH dehydrogenase iron-sulfur protein 8, mitochondrial
Sequence:
MLGSVIRQAVSRQIVRNSPISTTAAVAQTNQTGDKKESPKKPTIWKIDEHKRERLANFGKYAAECLPKFVQKVQFAAGDELELLIHPSGVVPVLSFLKGNHSAQFTNLTFITGMDVPTRKNRLEVIYSLYSVRFNARVRVRTYTDEIAPIDSATPVFKGADWFEREVYDMYGVWFNNHPDLRRILTDYGFEGHPFRKDYPLSGYNEVRYDPELKRVVYEPSELAQEFRKFDLNTPWETFPAFRNQSITSGYETILEVAEPTPATPQNK
Protein: Trifunctional UDP-glucose 4,6-dehydratase/UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose-reductase RHM1 (Protein REPRESSOR OF LRX1 1) (Rhamnose biosynthetic enzyme 1) (AtRHM1) [Includes: UDP-glucose 4,6-dehydratase (EC 4.2.1.76); UDP-4-keto-6-deoxy-D-glucose 3,5-epimerase/UDP-4-keto-L-rhamnose 4-keto-reductase (EC 1.1.1.-) (EC 5.1.3.-)] (Q9SYM5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Trifunctional enzyme involved in UDP-beta-L-rhamnose biosynthesis, a precursor of the primary cell wall components rhamnogalacturonan I (RG-I) and rhamnogalacturonan II (RG-II). Plays a major role in supplying UDP-rhamnose for flavonol biosynthesis. Catalyzes the dehydration of UDP-glucose to form UDP-4-dehydro-6-deoxy-D-glucose followed by the epimerization of the C3' and C5' positions of UDP-4-dehydro-6-deoxy-D-glucose to form UDP-4-keto-beta-L-rhamnose and the reduction of UDP-4-keto-beta-L-rhamnose to yield UDP-beta-L-rhamnose (By similarity).
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:19056285, ECO:0000269|PubMed:21502189}.
Interaction partners:
- UDP-glucose 6-dehydrogenase 3
- UDP-glucose 6-dehydrogenase 2
- UDP-glucose 6-dehydrogenase 1
- UDP-glucose 6-dehydrogenase 4
- Putative UDP-glucose 6-dehydrogenase
- Bifunctional dTDP-4-dehydrorhamnose 3,5-epimerase/dTDP-4-dehydrorhamnose reductase
- UDP-glucose 4-epimerase 2
- Bifunctional UDP-glucose 4-epimerase and UDP-xylose 4-epimerase 1
- UDP-glucose 4-epimerase 5
- UDP-glucose 4-epimerase 4
Sequence:
MASYTPKNILITGAAGFIASHVANRLIRSYPDYKIVVLDKLDYCSNLKNLNPSKHSPNFKFVKGDIASADLVNHLLITEGIDTIMHFAAQTHVDNSFGNSFEFTKNNIYGTHVLLEACKVTGQIRRFIHVSTDEVYGETDEDALVGNHEASQLLPTNPYSATKAGAEMLVMAYGRSYGLPVITTRGNNVYGPNQFPEKLIPKFILLAMRGQVLPIHGDGSNVRSYLYCEDVAEAFEVVLHKGEVGHVYNIGTKKERRVNDVAKDICKLFNMDPEANIKFVDNRPFNDQRYFLDDQKLKKLGWSERTTWEEGLKKTMDWYTQNPEWWGDVSGALLPHPRMLMMPGGRHFDGSEDNSLAATLSEKPSQTHMVVPSQRSNGTPQKPSLKFLIYGKTGWIGGLLGKICDKQGIAYEYGKGRLEDRSSLLQDIQSVKPTHVFNSAGVTGRPNVDWCESHKTETIRANVAGTLTLADVCREHGLLMMNFATGCIFEYDDKHPEGSGIGFKEEDTPNFTGSFYSKTKAMVEELLKEYDNVCTLRVRMPISSDLNNPRNFITKISRYNKVVNIPNSMTVLDELLPISIEMAKRNLKGIWNFTNPGVVSHNEILEMYRDYINPEFKWANFTLEEQAKVIVAPRSNNEMDASKLKKEFPELLSIKESLIKYAYGPNKKT
Protein: Alpha-tubulin N-acetyltransferase 1 (Alpha-TAT) (Alpha-TAT1) (TAT) (EC 2.3.1.108) (Acetyltransferase mec-17 homolog) (A0A1U9X797)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_03130}. Membrane, clathrin-coated pit {ECO:0000256|HAMAP-Rule:MF_03130}. Cell junction, focal adhesion {ECO:0000256|HAMAP-Rule:MF_03130}. Cell projection, axon {ECO:0000256|HAMAP-Rule:MF_03130}. Cytoplasm, cytoskeleton {ECO:0000256|HAMAP-Rule:MF_03130}. Cytoplasm, cytoskeleton, spindle {ECO:0000256|HAMAP-Rule:MF_03130}.
Interaction partners:
Sequence:
MWLTWPFCFLTITLREEGVCHLESVDLQQQIMTIIDELGKASAKAQNLSAPITSASRMQSNRHVVYILKDSSARPAGKGAIIGFIKVGYKKLFVLDDREAHNEVEPLCILDFYIHESVQRHGHGRELFQYMLQKERVEPHQLAIDRPSQKLLKFLNKHYNLETTVPQVNNFVIFEGFFAHQHRPPAPSLRATRHSRAAAVDPTPAAPARKLPPKRAEGDIKPYSSSDREFLKVAVEPPWPLNRAPRRATPPAHPPPRSSSLGNSPERGPLRPFVPEQELLRSLRLCPPHPTARLLLAADPGGSPAQRRRTRGTPPGLVAQSCCYSRHGGVNSSSPNTGNQDSKQGEQETKNRSASEEQALSQDGSGEKPMHTAPPQAPAPPAQSWTVGGDILNARFIRNLQERRSTRPW
Protein: Cholesteryl ester transfer protein (Lipid transfer protein I) (G3HIK4)
Organism: Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus)
Function: Involved in the transfer of neutral lipids, including cholesteryl ester and triglyceride, among lipoprotein particles. Allows the net movement of cholesteryl ester from high density lipoproteins/HDL to triglyceride-rich very low density lipoproteins/VLDL, and the equimolar transport of triglyceride from VLDL to HDL. Regulates the reverse cholesterol transport, by which excess cholesterol is removed from peripheral tissues and returned to the liver for elimination (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P11597}. Note=Secreted in plasma. {ECO:0000250|UniProtKB:P11597}.
Interaction partners:
- Apolipoprotein B-100
- Apolipoprotein F
- Apolipoprotein E
- P-type phospholipid transporter
- Phosphatidylcholine-sterol acyltransferase
- Hepatic triacylglycerol lipase
- Lipoprotein lipase
- Apolipoprotein A-II
- Apolipoprotein B-100
- ATP-binding cassette sub-family G member 1
Sequence:
MLAVTLLSLALLGSTCACSTSTSYEAGIVCRITKAALLVLNQETAKVIQTAFQRASYPDIKGERSMMLLGRVTYGLHNIQISHLSIASSQVELVEAKSVDVSIQNASVIFKGTLNYGYKGAWGLNIEQSVDFEIESAIDLQINTKLTCDSGHVRTDAPDCSISFHKLLLHLQGEREPGWTKQLFTNIISFTLKMVLKGQVCKEINVISNIMADFVQTRAANIISDRDIEVDISLTRSPIITATYLESHHKGHFIYKNISEVLPLPAFSPTLLGDTRMLYFWFSEQVLDSLAKAAFQDGRLQLNLAETELKVVLETWHFNPNQEIIPEVITGFPSPGQVTVHCPRRPTISCQNKGVVVSSPVVMEFLFPHKDGQDSVTHTFEEDIVATIQASYSKKKLFLSLVDFQIKPKTTSNMAESSESIQNFLQLMITTVGIPEIMSRLEVALTTLMNSKGLDLFDIINPEIITRDGFLLLQMDFGFPEHLLVDFLQSLN
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q9W227)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Zinc finger Ran-binding domain-containing protein 2
- LD10780p
- LD38375p
- rRNA 2'-O-methyltransferase fibrillarin
- HEAT repeat-containing protein 1 homolog
- LD47550p
- rRNA 2'-O-methyltransferase fibrillarin
- Nucleolar protein 6
- peptidylprolyl isomerase
- FK506-binding protein 59
Sequence:
MKLFLSVFVVALVAGVVVADDSKGPKVTEKVFFDITIGGEPAGRIEIGLFGKTVPKTVENFKELALKPQGEGYKGSKFHRIIKDFMIQGGDFTKGDGTGGRSIYGERFEDENFKLKHYGAGWLSMANAGKDTNGSQFFITTKQTSWLDGRHVVFGKILSGMNVVRQIENSATDARDRPVKDVVIANSGTLPVSEAFSVAKADATD
Protein: Sodium-coupled monocarboxylate transporter 2 (Electroneutral sodium monocarboxylate cotransporter) (Low-affinity sodium-lactate cotransporter) (Solute carrier family 5 member 12) (Q1EHB4)
Organism: Homo sapiens (Human)
Function: Acts as an electroneutral and low-affinity sodium (Na(+))-dependent sodium-coupled solute transporter. Catalyzes the transport across the plasma membrane of many monocarboxylates such as lactate, pyruvate, nicotinate, propionate, butyrate and beta-D-hydroxybutyrate. May be responsible for the first step of reabsorption of monocarboxylates from the lumen of the proximal tubule of the kidney and the small intestine. May play also a role in monocarboxylates transport in the retina (By similarity). Mediates electroneutral uptake of lactate, with a stoichiometry of 2 Na(+) for each lactate (By similarity).
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:17692818}; Multi-pass membrane protein {ECO:0000269|PubMed:17692818}. Note=Detected at the brush border membrane of the kidney. Colocalizes with viementin in Mueller cells. {ECO:0000250|UniProtKB:Q49B93}.
Interaction partners:
- Solute carrier family 22 member 12
- CCAAT/enhancer-binding protein delta
- Solute carrier family 22 member 11
- Solute carrier family 2, facilitated glucose transporter member 9
Sequence:
MEVKNFAVWDYVVFAALFFISSGIGVFFAIKERKKATSREFLVGGRQMSFGPVGLSLTASFMSAVTVLGTPSEVYRFGASFLVFFIAYLFVILLTSELFLPVFYRSGITSTYEYLQLRFNKPVRYAATVIYIVQTILYTGVVVYAPALALNQVTGFDLWGSVFATGIVCTFYCTLGGLKAVVWTDAFQMVVMIVGFLTVLIQGSTHAGGFHNVLEQSTNGSRLHIFDFDVDPLRRHTFWTITVGGTFTWLGIYGVNQSTIQRCISCKTEKHAKLALYFNLLGLWIILVCAVFSGLIMYSHFKDCDPWTSGIISAPDQLMPYFVMEIFATMPGLPGLFVACAFSGTLSTVASSINALATVTFEDFVKSCFPHLSDKLSTWISKGLCLLFGVMCTSMAVAASVMGGVVQASLSIHGMCGGPMLGLFSLGIVFPFVNWKGALGGLLTGITLSFWVAIGAFIYPAPASKTWPLPLSTDQCIKSNVTATGPPVLSSRPGIADTWYSISYLYYSAVGCLGCIVAGVIISLITGRQRGEDIQPLLIRPVCNLFCFWSKKYKTLCWCGVQHDSGTEQENLENGSARKQGAESVLQNGLRRESLVHVPGYDPKDKSYNNMAFETTHF
Protein: 4-coumarate--CoA ligase-like 7 (EC 6.2.1.-) (4-coumarate--CoA ligase isoform 6) (At4CL6) (Q9M0X9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors. Acts as a carboxylate--CoA ligase that can use various carboxylates as substrates. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:15677481}.
Interaction partners:
- Cinnamoyl-CoA reductase 2
- Trans-cinnamate 4-monooxygenase
- Cinnamoyl-CoA reductase 1
- Cytochrome P450 84A1
- F5F19.5 protein
- Flavone 3'-O-methyltransferase 1
- Phenylalanine ammonia-lyase 4
- Phenylalanine ammonia-lyase 1
- Phenylalanine ammonia-lyase 3
- Phenylalanine ammonia-lyase 2
Sequence:
MEKSGYGRDGIYRSLRPTLVLPKDPNTSLVSFLFRNSSSYPSKLAIADSDTGDSLTFSQLKSAVARLAHGFHRLGIRKNDVVLIFAPNSYQFPLCFLAVTAIGGVFTTANPLYTVNEVSKQIKDSNPKIIISVNQLFDKIKGFDLPVVLLGSKDTVEIPPGSNSKILSFDNVMELSEPVSEYPFVEIKQSDTAALLYSSGTTGTSKGVELTHGNFIAASLMVTMDQDLMGEYHGVFLCFLPMFHVFGLAVITYSQLQRGNALVSMARFELELVLKNIEKFRVTHLWVVPPVFLALSKQSIVKKFDLSSLKYIGSGAAPLGKDLMEECGRNIPNVLLMQGYGMTETCGIVSVEDPRLGKRNSGSAGMLAPGVEAQIVSVETGKSQPPNQQGEIWVRGPNMMKGYLNNPQATKETIDKKSWVHTGDLGYFNEDGNLYVVDRIKELIKYKGFQVAPAELEGLLVSHPDILDAVVIPFPDEEAGEVPIAFVVRSPNSSITEQDIQKFIAKQVAPYKRLRRVSFISLVPKSAAGKILRRELVQQVRSKM
Protein: Cytochrome c oxidase subunit 4 isoform 1, mitochondrial (Cytochrome c oxidase polypeptide IV) (Cytochrome c oxidase subunit IV isoform 1) (COX IV-1) (P13073)
Organism: Homo sapiens (Human)
Function: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Electrons originating from reduced cytochrome c in the intermembrane space (IMS) are transferred via the dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1 to the active site in subunit 1, a binuclear center (BNC) formed by heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2 water molecules using 4 electrons from cytochrome c in the IMS and 4 protons from the mitochondrial matrix.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}.
Interaction partners:
- Cytochrome c oxidase subunit 6A1, mitochondrial
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome c oxidase subunit 6C
- Cytochrome c oxidase subunit 2
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome c oxidase subunit 5B, mitochondrial
- Cytochrome c oxidase subunit 6B1
- Cytochrome c oxidase subunit 3
- Cytochrome c oxidase subunit 7C, mitochondrial
Sequence:
MLATRVFSLVGKRAISTSVCVRAHESVVKSEDFSLPAYMDRRDHPLPEVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRGSNEWKTVVGGAMFFIGFTALVIMWQKHYVYGPLPQSFDKEWVAKQTKRMLDMKVNPIQGLASKWDYEKNEWKK
Protein: Hepatocyte nuclear factor 4 alpha (F1NZ15)
Organism: Gallus gallus (Chicken)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU004334}.
Interaction partners:
- Hepatocyte nuclear factor 1-alpha
- Forkhead box A2
- Ch2H9orf152
- RRM domain-containing protein.
- Ovalbumin
Sequence:
MIMRLSKALIDMEMADYSAALDPAYTTLEFENMQVLAMGSDTSPSEAANLNTSNSIGVSALCAICGDRATGKHYGASSCDGCKGFFRRSVRKNHMYSCRFNRQCVVDKDKRNQCRYCRLKKCFRAGMKKEAVQNERDRISTRRSSYEDSSLPSINVLLQAEVLAQQISSPVLVMNGDIRGKKIANIADVCESMKQQLLVLVEWAKYIPAFCELPLDDQVALLRAHAGEHLLLGVAKRSMVFKDVLLLGNDHIVPRNCPELVEVSRVAIRILDELVLPFQELQIDDNEYACLKAIIFFDPDAKGLSDPSKIKRMRYQVQVSLEDYINDRQYDSRGRFGELLLLLPVLQSITWQMIEQIQFVKLFGMAKIDNLLQEMLLGGSSSETPHAHHPLHPHLIQENLGTNVIVANTMPPQMHNGQMSTPETPQPSPPAGSGPEQYKLLPGAIATVAKQPTSIPQPAITKQEVI
Protein: Malonyl-CoA decarboxylase family protein (Malonyl-CoA decarboxylase like protein) (Putative malonyl-CoA decarboxylase) (Q7Y1Z8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Acetyl-CoA carboxylase 1
- Acetyl-CoA carboxylase 2
- Biotin carboxylase, chloroplastic
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta, chloroplastic
- Methylmalonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase 2, chloroplastic
- Acetyl-CoA acetyltransferase 1
- Biotin carboxyl carrier protein of acetyl-CoA carboxylase 1, chloroplastic
- Acetyl-CoA acetyltransferase 2
- Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha, chloroplastic
Sequence:
MSKKNLAILLRARMRSNNPSKFSLSQFPKEIQSNPQENHSRDHIVQNSNDFGTTGRVYDVVRETMHSAISASKTGVLDITLNDFQEGYFSLSLEDREKLLLVLAKEYDVNREQVRELVKQYLGLETPASDDDKGALSSVFYRIERNLRHALRPTYEVLFERLNTHPGGLRFLSILRADLLSILSKENTPSLRTLDSFLKEKLGMWLSPATLELHQITWDDPASLLEKIVAYEAVHPISNLLDLKRRLGIGRRCFGYFHPSVPGEPLIFIEVALMETVAQTIQEVLWDNPPIPENQATCALFYSISSTQPGLAGINLGKFLIKRVITLVKKDMPHVSTFATLSPIPGFMQWLLSKLSSQSRFAEDERGTQSNSPSSTFSEKVLLPEEEHALMTLSDESSSGSNGMEVLLNLLSVKNCDWATSPRLLPVLEPILMRLCARYLLQEKKRGKALDSVANFHLQNGAMVERINWMADRSEKGIRQSGGIMVNYVYRLENIEDYAQSYFGSGKIHASPGIHSRL
Protein: FOG-1 protein (RRM domain-containing protein) (G5EBS6)
Organism: Caenorhabditis elegans
Interaction partners:
- Anti-proliferative protein domain-containing protein
- Fem-3 mRNA-binding factor 1
- Fem-3 mRNA-binding factor 2
- Poly
- Nanos-type domain-containing protein
- Defective in germ line development protein 3
- Female germline-specific tumor suppressor gld-1
- Sex-determination protein fem-3
- F-box domain-containing protein
- Poly
Sequence:
MFPSGHNEKWTRGYQRENSLLHHDDEFRSFQRRTDCPQHFYQQTNGYEHSLFGEKAGFHEASAQNLLMHLASQISPMEFAKLQLELLASQNKQRPHRGAGFGSYLMSPPATVSSSRSTVLCCNPAPPYASHCQSPAASDDFGHHFGSFDSMSAYNFHNNNQQQRREAHVSRDGKSFDQGNIYTAEDVHTVVKNHRNENNQRVVSNKVFVGGISHMMNRKIINKFFGQFGTVFVDWPVKQKPNSRGKSIAIGSYSYLFLVYSDEQSVIKLMSACHRNSQNDFFVSVPGFRDMIQIRPWFIYNGFYILEKARHNRIIDIHRTVFLGGLPRIVTAEEIAQMFSEFGVVLLVTIDIDQDYGYPKGAARVTFERDSAFNRALEKKFLKFDNIDSSKTMIEIKPYVMEDVGCDECGGLWFNPFLSIYDHLKCAKDDHQKEQKMAEIKNFNMWSSRSPFSLNSGDGHDDLITKMDAGFKKNCNLACTYSNRENEKNETEMGARKFLEMVKSFGLEKEKTVTVNGNEYPIGPDLWDKFLPAPKYDVGTEPVRMNPEAKLQQFLRMKRTNVYSNKSAYCKEAPCRQYYCPSCSNKLHSGPNQHTLLPAGKPERRPRKDKNMYLVNMGK
Protein: Transcription factor MYB44 (Myb-related protein 44) (AtMYB44) (Myb-related protein R1) (AtMYBR1) (Q9FDW1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor. Represses the expression of protein phosphatases 2C in response to abscisic acid (ABA). Confers resistance to abiotic stresses dependent of ABA. In response to auxin, activates the transcription of the auxin-responsive gene IAA19. The IAA19 transcription activation by MYB44 is enhanced by direct interaction between MYB44 and PYL8. Transcriptional activator of WRKY70 by direct binding to its promoter region, especially at 5'-TAACNG-3' and 5'-CNGTTA-3' symmetric motifs. Activates salicylic acid (SA)- mediated defenses and subsequent resistance to biotrophic pathogen P.syringae pv. tomato DC3000, but represses jasmonic acid (JA)-mediated defenses responses against the necrotrophic pathogen A.brassicicola.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000269|PubMed:18162593}.
Interaction partners:
- Abscisic acid receptor PYL9
- Abscisic acid receptor PYL8
- Mitogen-activated protein kinase 3
- Probable WRKY transcription factor 33
- Transcription factor MYC2
- Zinc finger protein ZAT10
- Probable WRKY transcription factor 70
- Basic leucine zipper 8
Sequence:
MADRIKGPWSPEEDEQLRRLVVKYGPRNWTVISKSIPGRSGKSCRLRWCNQLSPQVEHRPFSAEEDETIARAHAQFGNKWATIARLLNGRTDNAVKNHWNSTLKRKCGGYDHRGYDGSEDHRPVKRSVSAGSPPVVTGLYMSPGSPTGSDVSDSSTIPILPSVELFKPVPRPGAVVLPLPIETSSSSDDPPTSLSLSLPGADVSEESNRSHESTNINNTTSSRHNHNNTVSFMPFSGGFRGAIEEMGKSFPGNGGEFMAVVQEMIKAEVRSYMTEMQRNNGGGFVGGFIDNGMIPMSQIGVGRIE
Protein: Lipase 2 (EC 3.1.1.3) (Q93J06)
Organism: Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145)
Function: Catalyzes the hydrolysis of fatty acid esters with a preference for long chain fatty acids (C16-C18).
Subcellular location: Secreted {ECO:0000269|Ref.2}.
Interaction partners:
Sequence:
MPKPALRRVMTATVAAVGTLALGLTDATAHAAPAQATPTLDYVALGDSYSAGSGVLPVDPANLLCLRSTANYPHVIADTTGARLTDVTCGAAQTADFTRAQYPGVAPQLDALGTGTDLVTLTIGGNDNSTFINAITACGTAGVLSGGKGSPCKDRHGTSFDDEIEANTYPALKEALLGVRARAPHARVAALGYPWITPATADPSCFLKLPLAAGDVPYLRAIQAHLNDAVRRAAEETGATYVDFSGVSDGHDACEAPGTRWIEPLLFGHSLVPVHPNALGERRMAEHTMDVLGLD
Protein: IP15679p (Metal response element-binding transcription Factor-1, isoform B) (Metal response element-binding transcription Factor-1, isoform D) (Metal response element-binding transcription Factor-1, isoform E) (Metal response element-binding transcription Factor-1, isoform G) (Q8IQC5)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRTHTQERPYKCPEDDCGKAFTASHHLKTHRRTHTGEKPYPCQEDSCQKSFSTSHSLKSHKKTHQRQLQNKGRKKRPLKTQQTKCSDQEQKDPQQEEQEEEEFIKEDQPEMTLLNPGSHCSETTSTDSGVVLQTLTPQDHLSNVFILQGNEPLILPETSQAYQLSYAAEEEIPSPWIDAGVLVSKPIIPMAPLTDACVALPTEMPSFVNLKPTFGNAVSGNMGDPQPETMDVDPTVETSLPTPTLELNQPNIEELLKQDSFENEEDMETESLLNDILMTIDNNSALLQATLQQASQVPSDASGLVELDIRDNKPTLKQITADAGICNCTNCKCDQTKSCHGGDCGAAAAQQTTRTGAPTTTTTTTTMNSSGGKRICGSVVPTKKVSKRETEMNQNIEDVALLLQNLASMSSGGSSGGGGGCCGGGAVKPAPSGGGCCGEPKAPKPVNAGCGCARPSAPSSGGCCGSGVASTPKPTGGCCSGNQKPAPTATAASSPSCCCSGKGEVQEPPVISSASSAPAAAVKGNACTCKSPAEGVANGCCVVICIKTLQALRKVLTRRNLNLMLCPQQN
Protein: Chorismate mutase 3, chloroplastic (AtCM3) (EC 5.4.99.5) (CM-3) (Q9C544)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May play a role in chloroplast biogenesis.
Subcellular location: Plastid, chloroplast {ECO:0000250|UniProtKB:B4FNK8}.
Interaction partners:
- Chorismate synthase, chloroplastic
- Arogenate dehydratase/prephenate dehydratase 2, chloroplastic
- Arogenate dehydratase 4, chloroplastic
- Arogenate dehydratase 5, chloroplastic
- Arogenate dehydratase 3, chloroplastic
- Arogenate dehydratase/prephenate dehydratase 1, chloroplastic
- Arogenate dehydratase/prephenate dehydratase 6, chloroplastic
- Bifunctional aspartate aminotransferase and glutamate/aspartate-prephenate aminotransferase
- Arogenate dehydrogenase 1, chloroplastic
- Shikimate kinase 2, chloroplastic
Sequence:
MEAKLLKPAFYNSPNLNLTNSSRLISRLSIWNDKSKVGLSSGSLFLRLSAASPIRYSRGLLRVDESEYLKLESIRHSLIRQEDSIIFNLLERAQYRYNADTYDEDAFTMEGFQGSLVEFMVRETEKLHAKVDRYKSPDEHPFFPQCLPEPILPPIQYPQVLHRCAESININKKVWNMYFKHLLPRLVKPGDDGNCGSAALCDTMCLQILSKRIHFGKFVAEAKFRENPAAYETAIKEQDRTQLMQLLTYETVEEVVKKRVEIKARIFGQDITINDPETEADPSYKIQPSLVAKLYGERIMPLTKEVQIEYLLRRLD
Protein: Ep300 protein (Q5RJS0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
QQQQQQQRMQHHMQQMQQGNMGQMGQLPQALGAEAGASLQAYQQRLLQQQMGSPAQPNPMSPQQHMLPNQAQSPHLQGQQIPNSLSNQVRSPQPVPSPRPQSQPPHSSPSPRMQPQPSPHHVSPQTSSPHPGLVAAQAANPMEQGHFASPDQNSMLSQLASNPGMANLHGASATDLGLSADSADLSSNLSQSTLDIH
Protein: Ephrin-B3 (O35393)
Organism: Mus musculus (Mouse)
Function: Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Ephrin type-A receptor 4
- Ephrin type-B receptor 2
- Ephrin type-B receptor 6
- Ephrin type-B receptor 3
- Ephrin type-B receptor 1
- Ephrin type-B receptor 4
- Cytoplasmic protein NCK2
- Ephrin type-A receptor 1
- Regulator of G-protein signaling 3
- Ephrin-B1
Sequence:
MGAPHFGPGGVQVGALLLLGFAGLVSGLSLEPVYWNSANKRFQAEGGYVLYPQIGDRLDLLCPRARPPGPHSSPSYEFYKLYLVEGAQGRRCEAPPAPNLLLTCDRPDLDLRFTIKFQEYSPNLWGHEFRSHHDYYIIATSDGTREGLESLQGGVCLTRGMKVLLRVGQSPRGGAVPRKPVSEMPMERDRGAAHSAEPGRDTIPGDPSSNATSRGAEGPLPPPSMPAVAGAAGGMALLLLGVAGAGGAMCWRRRRAKPSESRHPGPGSFGRGGSLGLGGGGGMGPREAEPGELGIALRGGGTADPPFCPHYEKVSGDYGHPVYIVQDGPPQSPPNIYYKV
Protein: Protocadherin X-linked 11 (B5AK95)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
LVSNIAKRLFHLNTTTGLITVKEPLDREESPSHKLLVLATDGGSTPARATVLVNVTDINDNVPSIDIRYIVNPTNGTVLLSENAPLNTKIALITVMDKDSEHNGRVTCFTDHEVPFRLRPVFSNQFLLETAAFLDFESTREYAIKLLAADAGKPPLNQSSMLLIKVKDENDNAPVFTQSFISLSVPENNSPGAQLTKISATDADSGQNAEISYMLGFDAPPEFNLDQRTGILTAVKKLDREKQEKYYFTVLAQDNGIPPLMSNATVFVTVLDQNDNSPIFTHNEYNFYVPESLPKHGTVGLITVTDPDYGENSAVTLSILDVNDQFTIDPQSGVIRPNISFDRERQESYTFYVKAEDGGRVSRSSTARVTINVVDVNDNKPIFIDPPSNYSFEWVLPSTNPGTVVFKVVAIDDDIGMNAEVLYSIVGGNTKGLFMIEQTSGNITLKEKCMVSDLGLHRVIVKANDLGQPDSLFNVVNVNFFINESVPNATLIYELVRRSIDAPANQNTETTSASSPTTDYVKIMVAIVAGTITVVLVIFITAVVRCRQPPHLK
Protein: Sensor protein BasS (EC 2.7.13.3) (P30844)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system BasS/BasR Autophosphorylates and activates BasR by phosphorylation.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- Transcriptional regulatory protein BasR
- Phosphoethanolamine transferase EptA
- Transcriptional regulatory protein PhoP
- Transcriptional regulatory protein QseB
- PhoP/PhoQ regulator MgrB
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Signal transduction protein PmrD
- Transcriptional regulatory protein CpxR
- UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase aminotransferase)
- Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase
Sequence:
MHFLRRPISLRQRLILTIGAILLVFELISVFWLWHESTEQIQLFEQALRDNRNNDRHIMREIREAVASLIVPGVFMVSLTLFICYQAVRRITRPLAELQKELEARTADNLTPIAIHSATLEIEAVVSALNDLVSRLTSTLDNERLFTADVAHELRTPLAGVRLHLELLAKTHHIDVAPLVARLDQMMESVSQLLQLARAGQSFSSGNYQHVKLLEDVILPSYDELSTMLDQRQQTLLLPESAADITVQGDATLLRMLLRNLVENAHRYSPQGSNIMIKLQEDDGAVMAVEDEGPGIDESKCGELSKAFVRMDSRYGGIGLGLSIVSRITQLHHGQFFLQNRQETSGTRAWVRLKKDQYVANQI
Protein: Cytochrome P450 CYP82J17 (PpCYP82J17) (EC 1.14.14.-) (A0A517FND1)
Organism: Trigonella foenum-graecum (Fenugreek)
Function: Involved in the biosynthesis of spiroketal steroid and saponin natural products from cholesterol such as diosgenin and analogs (e.g. furostanol and spirostanol), plant defense compounds used as main precursors for the industrial production of steroid hormones. During the 5,6-spiroketalization of cholesterol, may catalyze the 27-monohydroxylation of furostanol-type steroid to an intermediate product that undergoes a stereospecific formation of the terminal heterocycle to yield diosgenin.
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MDSFLSQPITIVLAILSVLLYNIWKIRKPSNKFQKGMKLPQLSFALPLIGHLHLLGNQIPLAKTFASFADKYGPIFQIRLGAYPTLVISNKEAIKECFTTNDKILASRTKSTHGILLGYNHASFACAPYGRFWAKIRKVTMLELLSSRRVESLRHVYESEIDTLVKDLSLYVKVGKVEVVISEWMERLTFNIITKMICGKRYFEYLQDVDDVEANGNIVKLIKEVMHISGELVPKDVIPILGWFGFEGEVLKSMKRVSRDLDEVVGKWVEEHIEKSDDGVNNSNEKQDLIDVMLSVIEDDPDSGNDRDTIIKANIVNLMIAGSDTTSTTMTWILVLLLNNMNALKRAQEEIDQHIGRDRKIESSDIKNLVYLQAIVKETLRLHPTLPLSIPHEATEDCNIQGYYVPKGTRLFTNVWKLHRDPSIWLEPEKFSPERFINENGEIDHESHQFEYLPFGLGRRACPGSMFATQVIHIAVARLIHLFDFEVPINEVVDMKQGTGLILSKFTPLKVLLTPRLPYELYQ