wanglab/gogpt-training-data huggingface dataset:
Protein: ADP-dependent glucokinase (ADP-GK) (ADPGK) (EC 2.7.1.147) (RbBP-35) (Q9BRR6)
Organism: Homo sapiens (Human)
Function: Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. GDP and CDP can replace ADP, but with reduced efficiency (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Glucose-6-phosphate isomerase
- Hexokinase-4
- Phosphopentomutase
- Hexokinase-1
- Hexokinase-3
- Hexokinase-2
- Hexokinase HKDC1
- Fructose-bisphosphate aldolase A
- Glucose-6-phosphatase 3
- Galactose mutarotase
Sequence:
MALWRGSAYAGFLALAVGCVFLLEPELPGSALRSLWSSLCLGPAPAPPGPVSPEGRLAAAWDALIVRPVRRWRRVAVGVNACVDVVLSGVKLLQALGLSPGNGKDHSILHSRNDLEEAFIHFMGKGAAAERFFSDKETFHDIAQVASEFPGAQHYVGGNAALIGQKFAANSDLKVLLCGPVGPKLHELLDDNVFVPPESLQEVDEFHLILEYQAGEEWGQLKAPHANRFIFSHDLSNGAMNMLEVFVSSLEEFQPDLVVLSGLHMMEGQSKELQRKRLLEVVTSISDIPTGIPVHLELASMTNRELMSSIVHQQVFPAVTSLGLNEQELLFLTQSASGPHSSLSSWNGVPDVGMVSDILFWILKEHGRSKSRASDLTRIHFHTLVYHILATVDGHWANQLAAVAAGARVAGTQACATETIDTSRVSLRAPQEFMTSHSEAGSRIVLNPNKPVVEWHREGISFHFTPVLVCKDPIRTVGLGDAISAEGLFYSEVHPHY
Protein: Lysophospholipid acyltransferase 7 (LPLAT 7) (EC 2.3.1.-) (EC 2.3.1.23) (EC 2.3.1.n6) (EC 2.3.1.n7) (Farjavit) (Frj) (Membrane-bound acyltransferase 7) (MBOA 7) (Q9VMD5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Acyltransferase that mediates the acylation of lysophospholipids to produce phospholipids (glycerophospholipids). Highest activity with lysophosphatidylinositol (1-acyl-sn-glycero-3-phospho-(1D-myo-inositol) or LPI) producing phosphatidylinositol (1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol) or PI) (LPIAT activity), but also converts lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) to phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity), lysophosphatidylserine (1-acyl-2-hydroxy-sn-glycero-3-phospho-L-serine or LPS) to phosphatidylserine (1,2-diacyl-sn-glycero-3-phospho-L-serine or PS) (LPSAT activity), and lysophosphatidylethanolamine (1-acyl-sn-glycero-3-phosphoethanolamine or LPE) producing phosphatidylethanolamine (1,2-diacyl-sn-glycero-3-phosphoethanolamine or PE) (LPEAT activity). Has a preference for unsaturated fatty acid arachidonoyl-CoA ((5Z,8Z,11Z,14Z)-eicosatetraenoyl-CoA). Glycerophospholipids are important structural and functional components of cellular membrane, acyl-chain remodeling regulates the molecular species distribution of glycerophospholipids which can affect membrane fluidity and curvature.
Subcellular location: Membrane {ECO:0000269|PubMed:19864461}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- O-acyltransferase
- O-acyltransferase
- 1-Acylglycerol-3-phosphate O-acyltransferase 4, isoform A
- 1-Acylglycerol-3-phosphate O-acyltransferase 3, isoform E
Sequence:
MSIDDVIYVICLLGCIGAGSYVKKIADEGQRKLVSTGLGVLVVVIVSGLHSLHCFVSLALGTAAVLLVHPSKGHLVTFAVMFGYLVFFRIFDFYFGIPGHTNMIQMILTLKVSGIAFEKTAAWKRLQAHDEQKKNDQRDVHQESPIEITDYDVELQSLSAAEILHYSFNYIGVLTGPYYRYRTYRDYFEMPFKTYAPTVEATLEKLKYAVFYCALYLATNYMWPLDYALSDEFFNDRSFVYRLLYVWPTFFTFRARIYTGLTLSECVCTMAGFGAYPDESDPNNGEGPRKRYQHLKRDADKHTYNFTTIVNTRVLEVERCWTFREGMKHWNVCVQYWLAVNVYKLFPSKKYRTGATLLCSAYWHGFRPGHYFCIMGAPFYVSLEDMWDKLVRKSATGTSRRVIDVIFWIFKWFAFSYLGEAFLLSSFGNIWRFYSSVYHIGYISWAAMTALGFYLTSQRKAAERRKKRAAEKAAGGDGIAAAIEKEKAQ
Protein: ER membrane protein complex subunit 4 (Q9VNQ3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477}.
Interaction partners:
- ER membrane protein complex subunit 7
- ER membrane protein complex subunit 6
- ER membrane protein complex subunit 1
- ER membrane protein complex subunit 3
- Membrane magnesium transporter
- ER membrane protein complex subunit 10
- ER membrane protein complex subunit 2
- ER membrane protein complex subunit 8/9 homolog
- ER membrane protein complex subunit 2
- Vacuolar protein sorting-associated protein 28 homolog
Sequence:
MSAKQNPKKLKWALDFNGSKNADIPSPLGYNPSALVNQSEVVRDQRLVIKKSWDLALGPLKNIPMNLFIMYMSGNSISIFPIMMVGMMLIRPIKAIFTTQVTSKMAEGAQGTGQRIVYFLGNLANVALALYKCQSMGLLPTHASDWLAFVQPQTRLEYYGGGISFV
Protein: Uncharacterized protein (F4IGJ2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MILCWLNRVDEWKDPSEEALAGGRGMFCVVPLTKTLFQTASQSVSFLLPNSMESFDFFNQLLTFLQMNSAVKFLDMKFQKLANPMHNPSGDLGSKSNVLD
Protein: Lipooligosaccharide biosynthesis protein lic2B (EC 2.-.-.-) (Q57394)
Organism: Haemophilus influenzae
Function: Involved in extracellular lipooligosaccharide (LOS) biosynthesis and virulence expression. Involved in the synthesis of the oligosaccharide moiety of the LOS molecule by adding GalNAc (By similarity).
Interaction partners:
Sequence:
MHINYVISLTSAYQRREHIQKEFSQQNIPFEFFDALKPSKELTSLIEKFIPNLLHAKLTEGEKACFMSHYMLWQKCFSEDLPYIYIFEDDVLLGENADKFLAEDEWLEEAFKQTDKFILRFETFLNFSKCKDKKIKPYSGRKILKLVSENCGAAGYVISREAVKQLSAHICSLTSNHLLAIDLLMFNIFNQSTYQVSPGVCVQEGQLYPKDIKLHSQLETERQKYLSVKKKRTLKTVLISLAGKPKKILRKIYRKLFISKHIVPFR
Protein: Cabin1 protein (Q6PH97)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
RLLPGRPPRDRGPESRSAELSLEELSISTRQQPAPLAPSPAAPTTTAAPTTMAARGAGHSEEAPPRPNRKRKLLEDTESGKTLLLDAYRVWQQGQKGMAYDLSRIEKIMSETYMLIKQVDEETALEQAVKFCQVHLGAATQRQASGDTPTTPKHPKDSRENFFPATVVPTVPDPTAPDALQRPSDSHLKPVLATVITCPPSASASIPDLSTDPGIPRPHRPETTPSRAPLSPEGEEASGVTEGASTLPQEPRYSHQIKMAATGHLAEQHCWPVEVACQTGAEPTCSQGLSTASSTKVPSSGSTQTAESHQGKTESSRAKSRLLPNMPKLVIPSATTKSPPEITVTPPTPTLLSPKGSISEETKQKLKSAILSAQSAANVRKESLCQPALEVLETSSQESSLESETDEDDDFMDV
Protein: Radial spoke head protein 9 homolog (Q9D9V4)
Organism: Mus musculus (Mouse)
Function: Component of the axonemal radial spoke head which plays an important role in ciliary motility. Essential for both the radial spoke head assembly and the central pair microtubule stability in ependymal motile cilia. Required for motility of olfactory and neural cilia and for the structural integrity of ciliary axonemes in both 9+0 and 9+2 motile cilia (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:30383886, ECO:0000269|PubMed:34871179, ECO:0000305|PubMed:32203505}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:30185526, ECO:0000305|PubMed:36417862}. Cell projection, kinocilium {ECO:0000250|UniProtKB:Q5TYW6}.
Interaction partners:
- Radial spoke head protein 4 homolog A
- Radial spoke head 1 homolog
- Radial spoke head protein 6 homolog A
- Dynein axonemal intermediate chain 2
- Radial spoke head protein 3 homolog B
- Dynein axonemal intermediate chain 1
- Coiled-coil domain-containing protein 39
- Dynein axonemal assembly factor 1
- Radial spoke head protein 3 homolog A
- Dynein axonemal heavy chain 5
Sequence:
MDADSLLLSLELASGSGQGLSPDRRASLLTSLMLVKRDYRFARVLFWGRILGLVADYYIAQGLSEDQLAPRKTLYSLNCTEWSLLPPATEEMAMQISVVSGRFMGDPSHEYEHTELQKVNEGEKVFDEEVVVQIKEETRLVSIIDQIDKAVAIIPRGALFKTPFGVTHVNRTFEGLPLSEVRKLSSYFHFREAIDLKNKTLLEKSDLEPSLDFLDSLEYDIPRGSWSIQMERGNALVVLRSLLWPGLTFYHAPRTKNYGYIYVGTGEKNMDLPFML
Protein: Class II aldolase/adducin N-terminal domain-containing protein (G8JYB0)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004413}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004413}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004413}.
Interaction partners:
Sequence:
MIGRKEKERERPYYRDPDDPEYIKDLQRPAVIKEDLSEMERRKRVQQILESKSFCHELEEVIRQECDTARTDPDHLQVLQKLSDLTVPQGNMSFGNLHTYGGNTIAIADLRGNEKYSKAERIQRNKLACLFRLADLFQWSQGIHNEISYRTNDEDNTFLMNPFGLLYHEITAATIVKIDENGKILDCGTLKAGVNQPAFLLHSAIYKAHPMVRCILHMHTAIVAAVASMKCGLLPLCKEAMVLGPVGYHDYQDIGDDDIQFDEIIANLGDKNVLFLRNQGFLVVGDTIEHATFLANNTVIACETQVRAARAGLDNLIIPEEKAIQRAFRNSRNTNSLKRNGTVDWRVGELEWESWMRVLDHANFQTGHVYRQPQLRPKSAMSTSMVNNNDVAVPPTTSAYGQIDETNLESVSAHRLALLRKEQERVRWMNSPNAYQKVEFLEYGADNPKKITKWVHDVNVPSASGTPVKISSVHQFSPASSNPKEFKEKQKAIKENNRLGTLSAGPQSQILDSVTYEDIALLIKPDNDGTVGQSSTADRAILIGTASKGIIDRQFQHHAQVYHQIYAPNPFSVETDADIKKYVDMVKAKNSQSAPVSARSGYSQYDEVEADTVSLMQGVREHKLSQAALSASDDGLNAGISPNNVRTSEESVNTSYMSQSVVFDCDHPSPMSISTEYPEKVKMTRFSSTQGTSEGIFVTTWCLFVFSLFFRAHQLTNQ
Protein: Galactan 5-O-arabinofuranosyltransferase (EC 2.4.2.46) (Arabinofuranosyltransferase AftA) (P9WN03)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Involved in the biosynthesis of the arabinogalactan (AG) region of the mycolylarabinogalactan-peptidoglycan (mAGP) complex, an essential component of the mycobacterial cell wall. Catalyzes the addition of the first key arabinofuranosyl (Araf) residue from the sugar donor decaprenyl-phospho-arabinose (DPA) on the C-5 of a 6-linked galactofuranosyl (Galf) of the galactan domain, thus 'priming' the galactan for further elaboration by other arabinofuranosyltransferases. It is not able to add an Araf residue to a terminal Galf.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16595677}; Multi-pass membrane protein {ECO:0000269|PubMed:16595677}.
Interaction partners:
- Probable arabinosyltransferase C
- Probable arabinosyltransferase A
- Probable arabinosyltransferase B
- Terminal beta-
- Alpha-
- Decaprenylphosphoryl-2-keto-beta-D-erythro-pentose reductase
- Decaprenylphosphoryl-beta-D-ribose oxidase
- Arabinogalactan biosynthesis recruiting protein Rv3789
- Alpha-
- Galactofuranosyltransferase GlfT2
Sequence:
MPSRRKSPQFGHEMGAFTSARAREVLVALGQLAAAVVVAVGVAVVSLLAIARVEWPAFPSSNQLHALTTVGQVGCLAGLVGIGWLWRHGRFRRLARLGGLVLVSAFTVVTLGMPLGATKLYLFGISVDQQFRTEYLTRLTDTAALRDMTYIGLPPFYPPGWFWIGGRAAALTGTPAWEMFKPWAITSMAIAVAVALVLWWRMIRFEYALLVTVATAAVMLAYSSPEPYAAMITVLLPPMLVLTWSGLGARDRQGWAAVVGAGVFLGFAATWYTLLVAYGAFTVVLMALLLAGSRLQSGIKAAVDPLCRLAVVGAIAAAIGSTTWLPYLLRAARDPVSDTGSAQHYLPADGAALTFPMLQFSLLGAICLLGTLWLVMRARSSAPAGALAIGVLAVYLWSLLSMLATLARTTLLSFRLQPTLSVLLVAAGAFGFVEAVQALGKRGRGVIPMAAAIGLAGAIAFSQDIPDVLRPDLTIAYTDTDGYGQRGDRRPPGSEKYYPAIDAAIRRVTGKRRDRTVVLTADYSFLSYYPYWGFQGLTPHYANPLAQFDKRATQIDSWSGLSTADEFIAALDKLPWQPPTVFLMRHGAHNSYTLRLAQDVYPNQPNVRRYTVDLRTALFADPRFVVEDIGPFVLAIRKPQESA
Protein: Microspherule protein N-terminal domain-containing protein (Q388W1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MYCHAGVPSTSPSPTDFSEVHKILCGHIKQGNNFSVAAAVALEPLHGSSEFWRTCGYRSGIVSALLASSLGVQRETDQLSHLEPMTVADVYAMLRHVVDENAHLRQIIARLESGECDPDDGSGGITSSTERLRSLISEGYDALTGRSSPCMGEYDCGQTPGKWKTCSNGAAGTKRRRDSPEVTEWAYVRPESPVPASETLSPAANSGDDTVDEAEQNNALDVLEQLPALPGTTRTVSSFDAVGEMVNRGAGGPSLHPTNPSEFRVGSERGSTIETHSSSEVSNFANVGVGTSSGKQKRYKFSASEDEAIIKGLARFTKGQQRFQQIYYAYRSVWHPARTVSQLYDHWRGTLRYKVIQQQGYRGKNSVAARSPEKASNMENNE
Protein: Fatty acid-binding protein, intestinal (B5X5J4)
Organism: Salmo salar (Atlantic salmon)
Interaction partners:
Sequence:
MTYNDTWKVDRSENYEKFMEQMGVNMVKRKLAAHDNLKITLEQTGDKFVVKEASSFRTLDMEFTLGVTFEYALADGTMLSGSWGMEGDMMKGTFTRKDNGKVLKTTRAIVGEELVQSYSYDGVEAKRIFKRG
Protein: Centrin-2 (Caltractin isoform 1) (P41208)
Organism: Homo sapiens (Human)
Function: Plays a fundamental role in microtubule organizing center structure and function. Required for centriole duplication and correct spindle formation. Has a role in regulating cytokinesis and genome stability via cooperation with CALM1 and CCP110.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843, ECO:0000269|PubMed:37934472}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23591820, ECO:0000269|PubMed:32110738, ECO:0000269|PubMed:32946374, ECO:0000269|PubMed:37934472}. Nucleus envelope {ECO:0000269|PubMed:23591820}. Nucleus, nuclear pore complex {ECO:0000269|PubMed:23591820}. Nucleus {ECO:0000305}. Note=Localizes to the inner scaffold in the central region of centrioles and to the distal end of centrioles. {ECO:0000269|PubMed:37934472}.
Interaction partners:
- UV excision repair protein RAD23 homolog B
- Transcription and mRNA export factor ENY2
- PCI domain-containing protein 2
- DNA repair protein complementing XP-C cells
- Germinal-center associated nuclear protein
- Protein SFI1 homolog
- UV excision repair protein RAD23 homolog A
- DNA excision repair protein ERCC-1
- Centrin-3
- Centrosomal protein POC5
Sequence:
MASNFKKANMASSSQRKRMSPKPELTEEQKQEIREAFDLFDADGTGTIDVKELKVAMRALGFEPKKEEIKKMISEIDKEGTGKMNFGDFLTVMTQKMSEKDTKEEILKAFKLFDDDETGKISFKNLKRVAKELGENLTDEELQEMIDEADRDGDGEVSEQEFLRIMKKTSLY
Protein: Riboflavin synthase (RS) (EC 2.5.1.9) (P0AFU8)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-ribityllumazine, resulting in the formation of riboflavin and 5-amino-6-(D-ribitylamino)uracil.
Interaction partners:
- GTP cyclohydrolase-2
- 3,4-dihydroxy-2-butanone 4-phosphate synthase
- Riboflavin biosynthesis protein RibD
- 6,7-dimethyl-8-ribityllumazine synthase
- Bifunctional riboflavin kinase/FMN adenylyltransferase
- Phytase AppA
- 5-amino-6-
- NAD
- 5-amino-6-
- Class B acid phosphatase
Sequence:
MFTGIVQGTAKLVSIDEKPNFRTHVVELPDHMLDGLETGASVAHNGCCLTVTEINGNHVSFDLMKETLRITNLGDLKVGDWVNVERAAKFSDEIGGHLMSGHIMTTAEVAKILTSENNRQIWFKVQDSQLMKYILYKGFIGIDGISLTVGEVTPTRFCVHLIPETLERTTLGKKKLGARVNIEIDPQTQAVVDTVERVLAARENAMNQPGTEA
Protein: histidine kinase (EC 2.7.13.3) (Q9FRY7)
Organism: Zea mays (Maize)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MGGKYRAARTKRWWRGLAAAGWVLTAVVCSAVMHWTLRRDSMDRAEERLVSMCEERARMLQEQFGVTVNHVHAIAILISTFNFEKSPPAIDQDTFAKYTARTSFERPLLNGVAFAQRVFHHEREMFESQQGWVMNTMQREPAPPQVEYAPVIFSQDTVSYLARIDMMSGEEDRENIFRARTTGKAVLTNPFRLLGSNHLGVVLTFAVYRPDLPADASVEQRVEATIGYLGGAFDVESLVENLLSKLAGNQDIVVNVYDVTNASDAMVLYGPSSLDEQVPFLHVSMLDFGDPFRKHEMRCRYRQKLPMPWSAITNPLGTFVIWMLLGYSIAAAYSRYDKVTEDCRKMEELKTQAEAADVAKSQFLATASHEIRTPMNGVLGMLDMLLGTDLTMTQKDYAQTAQMCGRALITLINDVLDRAKIEAGKLELEAVPFDLRSLMDDVVSLFSSKSREKCIELAVFVCDNVPKVVIGDPWRFRQILTNLVGNAVKFTERGHVFVRVCLAENSNMEANQVLHGAMNGKGGRVESTANGAFNTLSGFEAADRRNSWQYFKLLLSDKESLLDDLESENSNQSDSDRVTLAISIEDTGVGIPLQAQDRVFTPFMQADSSTSRNYGGTGIGLSISKCLAELMGGQISFTSHPSVGSTFTFSATLKHSHKDISGDSSRSLTEALPTAFKGMKAILVDGRPVRSAVTRYHLKRLGILLQVVNNMNAVVKAFPGQNGAAGSREKASILFIESDFWRPETDVQLLNHLREQKNGQLSDGHKVVLLVTSEADKDKYGSIFDIVMCKPIRASTIASSIQQLLKVEIAERKDNQNRPSFLRSLLVGKNILVVDDNKVNLRVAAAALKKYGANVSCVESGKDAISLLQPPHRFDACFMDVQMPEMDGFEATGQIRQMELKANEERKNKLASIEGSTTAEYHLPVLAMTADVIQATYEECIKSGMDGYVSKPFDEEQLYQAVSRLVVGTTDSAV
Protein: Integrin subunit alpha 8 (A0A8I5Y696)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479, ECO:0000256|RuleBase:RU003762}.
Interaction partners:
Sequence:
MSARTHRGPPENWAPPFACLCCVSAVLGMLWSPVSLAFNLDVDKLTVYSGPEGSYFGYSLDFYIPDARTASVLVGAPKANTSQPDIVEGGAVYYCPWPAERSAQCKQIPFDTTNNRKIRVNGTKEPIEFKSNQWFGATVRAHKGKVVACAPLYHWRTLKPNPAKDPVGTCYVAIQNFSAYAEHSPCRNSNVDPEGQGYCQAGFSLDFYKNGDLIVGGPGSFYWQGQVITVSVADIIANYSFKDILRKLAAEKQTDVAPASYDDSYLGYSVAAGEFTGDSLQELVAGIPRGAQNFGYVSIINSTDMTFIQNFTGEQMASYFGYTVVVSDVNNDGMDDILVGAPLFMEREFESNPREVGQVYLYLQVSALLFQDPQVLTGTETFGRFGSSVAHLGDLNQDGYNDIAIGVPFAGKDQRGKVLIYNGNARGLHSKPSQVLQGIWGSQTIPSGFGFSLRGDADIDKNDYPDLLVGAFGEGKVAVYRARPVVTVDAQLLLHPMIINLENKTCQIPEFPTPVACFSLRVCASIAGQSISNTVALMAEVQLDFLKQKGAIKRTLFLHNHQSHLIFPFVMRQQKSLHCQDFMVYLRDETEFRDKLSPINVSLNYSLDDSTFEDGLEVKPILNHYRENVVTEQAHILVDCGEDNLCVPDLRLSARPDKQEIIIGDENHLMLIINARNEGEGAYEAELFVMIPEEADYVGIERNNKGLRLLSCEYKMENVTRMVVCDLGNPMVTGTNFSLGLRFAVPRLEKTNMSINFDLQIRSSNKDNPDSNFVSVQINVTAVAQVEIRGVSHPPQIVLPIHNWEPAEEPHKEEEVGPLVEHIYEPAASPEDTPELSAFLRNATIPHLVRKRDVPVVQPHRQSPAKILNCTNIDCLQISCAVGRLGGGESAVLKVRSRLWAHTFLQRKNDPYALASLVSFEVKKIPYKEQPAKLPAGSTAIKTSVIWATPNVSFSIPLWVIILAILLGLLVLAILTLALWKCGFFDRARPPQDEMTDREQLTSDKTPEA
Protein: Transcription factor MYB3R-5 (Myb-related protein 3R-5) (Q6R032)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription factor that binds 5'-AACGG-3' motifs in gene promoters (By similarity). Transcription repressor that regulates organ growth. Binds to the promoters of G2/M-specific genes and to E2F target genes to prevent their expression in post-mitotic cells and to restrict the time window of their expression in proliferating cells.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625, ECO:0000255|PROSITE-ProRule:PRU00768}.
Interaction partners:
- NAC domain containing protein 44
- SUPPRESSOR OF GAMMA RESPONSE 1
- NAC domain containing protein 85
- Cyclin-dependent protein kinase inhibitor SMR7
- HAD superfamily, subfamily IIIB acid phosphatase
- Cyclin-dependent protein kinase inhibitor SMR5
- Cyclin-dependent protein kinase inhibitor SMR4
- Cyclin-B1-2
- EH domain-containing protein 2
- Protein ENDOSPERM DEFECTIVE 1
Sequence:
MSSSSNPPVCSPEKEERSEMKIEIQCMENKQPLAASCSSASEGSGCFFLKSPEIATPATVSSFPRRTSGPMRRAKGGWTPEEDETLRRAVEKYKGKRWKKIAEFFPERTEVQCLHRWQKVLNPELVKGPWTQEEDDKIVELVKKYGPAKWSVIAKSLPGRIGKQCRERWHNHLNPGIRKDAWTVEEESALMNSHRMYGNKWAEIAKVLPGRTDNAIKNHWNSSLKKKLEFYLATGNLPPPASKFIVLKDIADGDRDSKQSSATKPFKDSDSLTQTSSGNTDSNEVGRDHFDSSSALLEEVAASRRIGVNEYACSPVEYKPQLPNLEPISEEVRINSKAYFERSIQRKVENGFGTPKHGNLYYKSPLDYYFPSEADLQHMYGYECGCSPGAASPVSLMTTPCNKDSGLTATRSPESFLREAARTFPNTPSIFRKRRKVVLAAKTDAVVVVNGVVKEVDRKEESKDMRKSLLLETTDNCSDDEELGLNGNAFNLSPPYRLRAKRTAVIKSRQLEFTSEKEKQPDNEIEFTSAKEKQPDNEIKTSEEDKPV
Protein: Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial (EC 1.1.1.41) (Isocitric dehydrogenase subunit alpha) (NAD(+)-specific ICDH subunit alpha) (H0YKD0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MKIFDAAKAPIQWEERNVTAIQGPGGKWMIPSEAKESMDKNKMGLKGPLKTPIAAGHPSMNLLLRKTFDLYANVRPCVSIEGYKTPYTDVNIVTIRENTEGEYSGIEHV
Protein: Prolyl 4-hydroxylase alpha subunit domain-containing protein (Q9VAR7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein
- IP08087p
- FI16633p1
- Uncharacterized protein, isoform G
- FI23927p1
- MOXD1 homolog 2
- SCP domain-containing protein
- Sulfhydryl oxidase
- HDC01001
- Serpin 28Da
Sequence:
MASLLQIEDELIGYMRQYAMELQHKVNTMRTFQEEWMTRRALGPADPTSYVANPLISFPLMRRTYTDVPKLLELAREEFKPGPFQKFIDYDLSSISDVELETAVTGMLRFQGVYGMDESEMANGKLHGKQYNSRMSAADCLAVATHLENVDKGKLACKWFKVAIDQYEEKLDPVNRLLQTGRSQIYEKLGLTLLAMHDLPASQAAFRDSIGWASKEDNTDLAKHLKDKLAHMFVHVDNCRGKNLLPSKSYLRCRYLRDGSPFLRMAPVKLEQLNIEPFVGLFHDAISPAEQKDLLHLTDSRLEHRKKDSSSVEAKVDTNASDHVRRIHQRIEDITGFDLEESEPLTVSNYGIGGQDFIHLDCEQPKEFIGYYPKEYRSASAMFYLSDVQMGGYASFPDLGFGFKPRRGSALVWHNTDNSGNCDTRSLQATCPVLLGNQWVAKKWISGSGQWRRKSCRK
Protein: Protein AmpE (P0AE14)
Organism: Escherichia coli (strain K12)
Function: Putative signaling protein in beta-lactamase regulation. AmpE seems not to act as a direct sensor for beta-lactams.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- 1,6-anhydro-N-acetylmuramyl-L-alanine amidase AmpD
- Anhydromuropeptide permease
- Beta-lactamase
- Uncharacterized protein YhfK
- Inner membrane protein YeeA
- Protein TsgA
- Glucans biosynthesis protein C
- Chaperone protein YcdY
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
Sequence:
MTLFTTLLVLIFERLFKLGEHWQLDHRLEAFFRRVKHFSLGRTLGMTIIAMGVTFLLLRALQGVLFNVPTLLVWLLIGLLCIGAGKVRLHYHAYLTAASRNDSHARATMAGELTMIHGVPAGCDEREYLRELQNALLWINFRFYLAPLFWLIVGGTWGPVTLMGYAFLRAWQYWLARYQTPHHRLQSGIDAVLHVLDWVPVRLAGVVYALIGHGEKALPAWFASLGDFHTSQYQVLTRLAQFSLAREPHVDKVETPKAAVSMAKKTSFVVVVVIALLTIYGALV
Protein: Medium-chain specific acyl-CoA dehydrogenase, mitochondrial (MCAD) (EC 1.3.8.7) (Medium chain acyl-CoA dehydrogenase) (MCADH) (P11310)
Organism: Homo sapiens (Human)
Function: Medium-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats. The first step of fatty acid beta-oxidation consists in the removal of one hydrogen from C-2 and C-3 of the straight-chain fatty acyl-CoA thioester, resulting in the formation of trans-2-enoyl-CoA. Electron transfer flavoprotein (ETF) is the electron acceptor that transfers electrons to the main mitochondrial respiratory chain via ETF-ubiquinone oxidoreductase (ETF dehydrogenase). Among the different mitochondrial acyl-CoA dehydrogenases, medium-chain specific acyl-CoA dehydrogenase acts specifically on acyl-CoAs with saturated 6 to 12 carbons long primary chains.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:16020546}.
Interaction partners:
- Electron transfer flavoprotein subunit alpha, mitochondrial
- Electron transfer flavoprotein subunit beta
- 3-ketoacyl-CoA thiolase, mitochondrial
- Trifunctional enzyme subunit alpha, mitochondrial
- Enoyl-CoA delta isomerase 2
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Trifunctional enzyme subunit beta, mitochondrial
- Enoyl-CoA hydratase, mitochondrial
- Peroxisome proliferator-activated receptor alpha
- Carnitine O-palmitoyltransferase 2, mitochondrial
Sequence:
MAAGFGRCCRVLRSISRFHWRSQHTKANRQREPGLGFSFEFTEQQKEFQATARKFAREEIIPVAAEYDKTGEYPVPLIRRAWELGLMNTHIPENCGGLGLGTFDACLISEELAYGCTGVQTAIEGNSLGQMPIIIAGNDQQKKKYLGRMTEEPLMCAYCVTEPGAGSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKAPANKAFTGFIVEADTPGIQIGRKELNMGQRCSDTRGIVFEDVKVPKENVLIGDGAGFKVAMGAFDKTRPVVAAGAVGLAQRALDEATKYALERKTFGKLLVEHQAISFMLAEMAMKVELARMSYQRAAWEVDSGRRNTYYASIAKAFAGDIANQLATDAVQILGGNGFNTEYPVEKLMRDAKIYQIYEGTSQIQRLIVAREHIDKYKN
Protein: Discoidin domain-containing receptor A (Q18163)
Organism: Caenorhabditis elegans
Function: Receptor which, together with svh-4, is involved in axon guidance to establish the tracts for the ventral and dorsal nerve cords during nervous system development. May play a role in axon regeneration following injury in D-type motor neurons.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell projection, axon {ECO:0000269|PubMed:23147028}. Perikaryon {ECO:0000269|PubMed:23147028}.
Interaction partners:
- Putative cuticle collagen 99
Sequence:
MQIALVLLAIYGTTTTNTLRIDQCGENALGMQNGDIADSQITASSSFDKQSVGPQNARLHSELASGAWCPKPQINSKSYEFLQVTLNDTFLITSVETQGRYGNGTGREFASHYMIDYLRPGSQWIRYKNRTGHVYMDGNFDTTTPVIRVLDPPIVASRIRFVPSSKNTRTVCMRAEIHGCKHEGVTYYSTVPDGSRLDTLDFKDSMFEDSQIYTESGIKRGLGLLTDGFVAQASPFEKNQMNNSWIGWNRDTTDGRITILFEFEEVHNFTDVVLATFGNRIDGIDVIFSQDGKTFPLFSQISSSERQSLNNTSRRYDFRVPLHNRAGRKVRISIKFSSDWMFLTEVHFTSAANLTLLSEKIPPPSSAATQQLLVVCGIIFLTIFACVAYCVSVCLKRRQKNKSVDSNVKKDLIITHMGNKPTCHVFPSNGKLSNGHYEVANDILYARSQKSTLLSVSSKSTFSCRAIPPTWTDFNFPPPPEGREEHTYSQPVSPENSSNGSYKSVRKIQALKKYPSSALLIGKAIGEGKFTMIKECIIFGGLKCAHKSTKEEDCVHGTRALGDEIACLLQCGRHPRIVELFGVDESYNLLLEHVEYGCIRNFWMASEAPLDTEFLVRICKDIYSAMAYLESIRIVHGHFTPNNILMDGEFHAKVCSPRGPSHHAQLRYSAPESIVNNEFTHKSDAWAVATTVYEMAYQCRQRPYEELTNEQIVDNACALLDHQPNAVVPLMPTVFNYEILQLLTRCFRVDQLERPTFERLVKPFQD
Protein: Protein PRY2 (Pathogenesis-related protein 2) (P36110)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Secreted protein required for efficient export of lipids such as acetylated sterols. Acts in detoxification of hydrophobic compounds.
Subcellular location: Secreted {ECO:0000269|PubMed:11935221, ECO:0000269|PubMed:23027975}.
Interaction partners:
- Protein SVS1
- Probable family 17 glucosidase SCW10
- Cell wall protein YLR042C
- Oxysterol-binding protein homolog 4
Sequence:
MKFSKVSLLAASASVALSAPVAVTVTQHVHQAATVVVQGIVRVENGQTLTTFITKGTQTASASPVATTSAPIVVANAQVDSIATSVIQESAVVAESATFEESSTETSEAFSTATATIQAVQTSASATQDDVTTTLTSSTQPTSTTTPTTTTTSPTTTTSPTTTASPTTTASPTTATTTQSTASSTQSSSSDFSTSMVNEHNTKRALHKDTGSLTWSDTLATYAQNYADSYDCSGNLVHSGGPYGENLALGYGTTGSVDAWYNEITSYDYSNPGFSESAGHFTQVVWKGTSEVGCGLKSCGGEWGDYIICSYKAAGNVIGEFADNVMPLA
Protein: Probable fructoselysine/psicoselysine transporter FrlA (P45539)
Organism: Escherichia coli (strain K12)
Function: Is likely involved in the transport of fructoselysine and psicoselysine to the cytoplasm, where they are degraded.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Fructoselysine 6-phosphate deglycase
- Fructoselysine 6-kinase
- Fructoselysine 3-epimerase
- Probable fructoselysine utilization operon transcriptional repressor
Sequence:
MGSQELQRKLGFWAVLAIAVGTTVGSGIFVSVGEVAKAAGTPWLTVLAFVIGGLIVIPQMCVYAELSTAYPENGADYVYLKNAGSRPLAFLSGWASFWANDAPSLSIMALAIVSNLGFLTPIDPLLGKFIAAGLIIAFMLLHLRSVEGGAAFQTLITIAKIIPFTIVIGLGIFWFKAENFAAPTTTAIGATGSFMALLAGISATSWSYTGMASICYMTGEIKNPGKTMPRALIGSCLLVLVLYTLLALVISGLMPFDKLANSETPISDALTWIPALGSTAGIFVAITAMIVILGSLSSCVMYQPRLEYAMAKDNLFFKCFGHVHPKYNTPDVSIILQGALGIFFIFVSDLTSLLGYFTLVMCFKNTLTFGSIIWCRKRDDYKPLWRTPAFGLMTTLAIASSLILVASTFVWAPIPGLICAVIVIATGLPAYAFWAKRSRQLNALS