wanglab/gogpt-training-data huggingface dataset:
Protein: V-type proton ATPase subunit c3 (V-ATPase subunit c3) (V-type proton ATPase 16 kDa proteolipid subunit c3) (V-ATPase 16 kDa proteolipid subunit c3) (Vacuolar H(+)-ATPase subunit c isoform 3) (Vacuolar proton pump 16 kDa proteolipid subunit c3) (Vacuolar proton pump subunit c3) (P0DH93)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Proton-conducting pore forming subunit of the membrane integral V0 complex of vacuolar ATPase. V-ATPase is responsible for acidifying a variety of intracellular compartments in eukaryotic cells.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:18507826}; Multi-pass membrane protein {ECO:0000269|PubMed:18507826}. Note=Tonoplast.
Interaction partners:
- V-type proton ATPase subunit e2
- V-type proton ATPase subunit e1
- V-type proton ATPase subunit D
- V-type proton ATPase subunit H
- V-type proton ATPase subunit C
- V-type proton ATPase subunit F
- V-type proton ATPase catalytic subunit A
- ATP synthase subunit b, chloroplastic
- V-type proton ATPase subunit c''2
- V-type proton ATPase subunit c''1
Sequence:
MSTFSGDETAPFFGFLGAAAALVFSCMGAAYGTAKSGVGVASMGVMRPELVMKSIVPVVMAGVLGIYGLIIAVIISTGINPKAKSYYLFDGYAHLSSGLACGLAGLSAGMAIGIVGDAGVRANAQQPKLFVGMILILIFAEALALYGLIVGIILSSRAGQSRAE
Protein: Bleomycin hydrolase (EC 3.4.22.40) (A8JV24)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|PIRNR:PIRNR005700}.
Interaction partners:
Sequence:
MKNYNLDEFEFSQAFLFYWDKIERCNYFLNNVVKTAQRGEKVDGRLVSFLLLDPTSDGGQWDMLVNLITKHGLMPKKCFPESFSCESSLRMNAILKSKLREYARNLRVLMEKNPTDEEIACKIQEQMAEIYKVVGICLGIPSETFTWEYYDKSKNYQSIGPVSSLEFYERYVKPHFNVEDKVCLVTDPRPTSSYDQAYTVDCLGNVVGGRPVLYNNQSVELLLAVVTKSLKAGEAVWFGCEVSKRFASKQGIEDVDVHDFKLVFDIDIQTTFSKADRLIYGESAMTHAMVFTAVSVDKSGVAQKLRVENSWGEDRGEKGYLVMNADWFREFGFEVVVDKKYVPEDVLRVFDMDPIVLPAWDPMGTLAQ
Protein: Flocculation protein FLO5 (Flocculin-5) (P38894)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Cell wall protein that participates directly in adhesive cell-cell interactions during yeast flocculation, a reversible, asexual and Ca(2+)-dependent process in which cells adhere to form aggregates (flocs) consisting of thousands of cells. The lectin-like protein sticks out of the cell wall of flocculent cells and selectively binds mannose residues in the cell walls of adjacent cells. Activity is inhibited by mannose, but not by glucose, maltose, sucrose or galactose.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:9483793}. Membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}. Note=Covalently-linked GPI-modified cell wall protein (GPI-CWP). {ECO:0000250}.
Interaction partners:
- Flocculation protein FLO11
Sequence:
MTIAHHCIFLVILAFLALINVASGATEACLPAGQRKSGMNINFYQYSLKDSSTYSNAAYMAYGYASKTKLGSVGGQTDISIDYNIPCVSSSGTFPCPQEDSYGNWGCKGMGACSNSQGIAYWSTDLFGFYTTPTNVTLEMTGYFLPPQTGSYTFSFATVDDSAILSVGGSIAFECCAQEQPPITSTNFTINGIKPWDGSLPDNITGTVYMYAGYYYPLKVVYSNAVSWGTLPISVELPDGTTVSDNFEGYVYSFDDDLSQSNCTIPDPSIHTTSTITTTTEPWTGTFTSTSTEMTTITDTNGQLTDETVIVIRTPTTASTITTTTEPWTGTFTSTSTEMTTVTGTNGQPTDETVIVIRTPTSEGLITTTTEPWTGTFTSTSTEMTTVTGTNGQPTDETVIVIRTPTSEGLITTTTEPWTGTFTSTSTEVTTITGTNGQPTDETVIVIRTPTSEGLITTTTEPWTGTFTSTSTEMTTVTGTNGQPTDETVIVIRTPTSEGLISTTTEPWTGTFTSTSTEVTTITGTNGQPTDETVIVIRTPTSEGLITTTTEPWTGTFTSTSTEMTTVTGTNGQPTDETVIVIRTPTSEGLITRTTEPWTGTFTSTSTEVTTITGTNGQPTDETVIVIRTPTTAISSSLSSSSGQITSSITSSRPIITPFYPSNGTSVISSSVISSSVTSSLVTSSSFISSSVISSSTTTSTSIFSESSTSSVIPTSSSTSGSSESKTSSASSSSSSSSISSESPKSPTNSSSSLPPVTSATTGQETASSLPPATTTKTSEQTTLVTVTSCESHVCTESISSAIVSTATVTVSGVTTEYTTWCPISTTETTKQTKGTTEQTKGTTEQTTETTKQTTVVTISSCESDICSKTASPAIVSTSTATINGVTTEYTTWCPISTTESKQQTTLVTVTSCESGVCSETTSPAIVSTATATVNDVVTVYPTWRPQTTNEQSVSSKMNSATSETTTNTGAAETKTAVTSSLSRFNHAETQTASATDVIGHSSSVVSVSETGNTMSLTSSGLSTMSQQPRSTPASSMVGSSTASLEISTYAGSANSLLAGSGLSVFIASLLLAII
Protein: F-box/LRR-repeat protein 13 (Q9FWZ1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- F-box protein At2g20380
- F-box/kelch-repeat protein At2g22030
- F-box protein At1g31080
- F-box protein At2g07140
- Putative F-box protein At3g22940
- Putative F-box/kelch-repeat protein At4g02310
- F-box/kelch-repeat protein At4g29370
- Putative F-box only protein 10
- Putative F-box/kelch-repeat protein At1g60570
- F-box/kelch-repeat protein At2g43270
Sequence:
MDEDREKHVRAKGSDEVDWISKLPDCLLCEVLLNLPTKDVVKTSVLSRRWRNLWKHVPGLDLDNTDFQEFNTFLSFVDSFLDFNSESFLQKFILKYDCDDEYDPDIFLIGRWINTIVTRKVQHIDVLDDSYGSWEVQLPSSIYTCESLVSLKLCGLTLASPEFVSLPSLKVMDLIITKFADDMGLETLITKCPVLESLTIERSFCDEIEVLRVRSQSLLRFTHVADSDEGVVEDLVVSIDAPKLEYLRLSDHRVASFILNKPGKLVKADIDIVFNLSSVNKFNPDDLPKRTMIRNFLLGISTIKDMIIFSSTLEVIYDFSRCERLPLFRNLSVLCVEFYGYMWEMLPIFLESCPNLKTLVVKSASYQEKGENIILPGPRRFLSSLEYVKIERPLKGEAMEMKLVSYLLENSTILKKLTLCLDDSVKKEDSVILKELLAIPRLSTSSKVVVL
Protein: NEDD8-activating enzyme E1 regulatory subunit (Ubiquitin-like activation protein 1) (Q18217)
Organism: Caenorhabditis elegans
Function: Regulatory subunit of the dimeric uba-3-ula-1 E1 enzyme. E1 activates NEDD8 by first adenylating its C-terminal glycine residue with ATP, thereafter linking this residue to the side chain of the catalytic cysteine, yielding a NEDD8-rfl-1 (uba-3) thioester and free AMP. E1 finally transfers NEDD8 to the catalytic cysteine of ubc-12. Required for rfl-1 (uba-3) nuclear localization during early embryonic development.
Interaction partners:
- NEDD8-activating enzyme E1 catalytic subunit
- Ubiquitin-like protein NEDD8
- NEDD8-conjugating enzyme ubc-12
- C2H2-type domain-containing protein
- COP9 signalosome complex subunit 5
- Molybdopterin synthase catalytic subunit
- Cullin-1
Sequence:
MLPFDPSTRYDRQVRLWGEEGQASIGSTSACVLGSDSLATEILKSLVLAGVQSFYVVDDAKVEQADIGQNFFLHADDIGRSRAEATLEKLTELNPSVSGSASSQPPTALAMEDVEKLTTFSVVVAANQNEEIDTTFAKVLYNIRVPFICIKTFGLIGTIRICIKEHTIANSHEENPRPDLRLDAPFSKLIEMINETNLDEMTLEQLRHTPYILLHFKALEVFRKQRNDPEAFPSTTAERKELQAILMSFRRSSEESGTKDSENFDEAKAAVIRAFQRTTIGSSVKSILSSPQCSTSTRPFWLICEALRRFVTENNNLLPLRGTLPDMTSDSSRYTRLATLFHEKALSDAQEVLRLTREVEKERGVGDVISDDVCYRFCKNADRIRVQYGDVLDYNEETKAIVEKIRESNIDEETRNQKVDEATWMLLMRAVGRFQKEKGRYPGTNGVPVSIDAQDLKKRVEVLIREALKDEQDFTSISNKVTDTAIAEICRFGAAELHVISSYVGGIAAQEIIKLATNQYVPIDNTFIFDGHTQESATFKF
Protein: Annexin (B5XEI6)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Zymogen granule membrane {ECO:0000256|ARBA:ARBA00024321}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00024321}.
Interaction partners:
Sequence:
MAAIGNRGTVVEAAAFNVEEDVNRLRGAMKGAGTDEAAVIEVLARRTIAQRQSIKEAYKLTVGKDLADDLQGELTGNIEKVVLGLLMIAPKYDAYELRTAIKGSGTEEAALIDILASRTNAEIRAITEVYMKEHGKSLEDDIEADTSGMFKRVLVSLLTAGRDESNSVNETQAVQDAKEIYEAGEACWGTDEVKFLTVLCVRNRNHLLRVFEEYQKISGRDIEDSIKREMSGSLEDVFLAIVKCLRNKPAFFAERLYKSMKGLGTTDSVLIRIMVARAEIDMLDIKTEFSKAYGKTLHSFIHGDSSGDYRKILLELCGE
Protein: Thioredoxin (A0A1D8PU69)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Trp99p
- Thioredoxin reductase
- Peroxiredoxin TSA1-A
- peptide-methionine
- Peroxiredoxin TSA1-B
- Glutathione reductase
- Superoxide dismutase
- Thioredoxin peroxidase
- Dithiol glutaredoxin
- SUMO-conjugating enzyme UBC9
Sequence:
MVHVVTEVNEFQTLLKENNLVIVDFFATWCGPCKMIAPLLEKFQNEYSNIKFLKIDVDQLGSLAQEYNVSSMPTLILFKNGEEVNRVIGANPAAIKQALASLA
Protein: Adenosine deaminase (EC 3.5.4.4) (Adenosine aminohydrolase) (P00813)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolytic deamination of adenosine and 2-deoxyadenosine. Plays an important role in purine metabolism and in adenosine homeostasis. Modulates signaling by extracellular adenosine, and so contributes indirectly to cellular signaling events. Acts as a positive regulator of T-cell coactivation, by binding DPP4. Its interaction with DPP4 regulates lymphocyte-epithelial cell adhesion. Enhances dendritic cell immunogenicity by affecting dendritic cell costimulatory molecule expression and cytokines and chemokines secretion (By similarity). Enhances CD4+ T-cell differentiation and proliferation. Acts as a positive modulator of adenosine receptors ADORA1 and ADORA2A, by enhancing their ligand affinity via conformational change. Stimulates plasminogen activation. Plays a role in male fertility. Plays a protective role in early postimplantation embryonic development (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:11772392, ECO:0000269|PubMed:8101391}; Peripheral membrane protein; Extracellular side. Cell junction {ECO:0000269|PubMed:11772392}. Cytoplasmic vesicle lumen {ECO:0000250|UniProtKB:P03958}. Cytoplasm {ECO:0000250}. Lysosome {ECO:0000269|PubMed:8452534}. Note=Colocalized with DPP4 at the cell surface. {ECO:0000269|PubMed:11772392}.
Interaction partners:
- Dipeptidyl peptidase 4
- Purine nucleoside phosphorylase
- Adenosine deaminase 2
- Adenosine kinase
- 5'-nucleotidase
- Double-stranded RNA-specific adenosine deaminase
- Deoxycytidine kinase
- 5'
- 5'
- Cytosolic purine 5'-nucleotidase
Sequence:
MAQTPAFDKPKVELHVHLDGSIKPETILYYGRRRGIALPANTAEGLLNVIGMDKPLTLPDFLAKFDYYMPAIAGCREAIKRIAYEFVEMKAKEGVVYVEVRYSPHLLANSKVEPIPWNQAEGDLTPDEVVALVGQGLQEGERDFGVKARSILCCMRHQPNWSPKVVELCKKYQQQTVVAIDLAGDETIPGSSLLPGHVQAYQEAVKSGIHRTVHAGEVGSAEVVKEAVDILKTERLGHGYHTLEDQALYNRLRQENMHFEICPWSSYLTGAWKPDTEHAVIRLKNDQANYSLNTDDPLIFKSTLDTDYQMTKRDMGFTEEEFKRLNINAAKSSFLPEDEKRELLDLLYKAYGMPPSASAGQNL
Protein: Uncharacterized protein C16C4.19 (O94306)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Probable ribonuclease P protein subunit 1
- Ribonuclease MRP protein subunit rmp1
- Ribonucleases P/MRP protein subunit pop1
- Probable ribonuclease P protein subunit 3
- Ribonucleases P/MRP protein subunit pop3
- Ribonuclease P/MRP protein subunit POP5
- Probable ribonucleases P protein subunit pop8
- Uncharacterized protein C6C3.09
- Ribonucleases P/MRP protein subunit POP7
- Large ribosomal subunit protein uL30C
Sequence:
MDQERKLQFLLSIAAETYAISPSLSSHYLRRMFSLLEEWNLETDPKTLLHGCSKCGSLFIFGRNIKLRTISSERKARTDLKKGEVSRLGTNLEINCLVCSYVHEIPLGVPLRLHQSKQALRAKAIAESSSTKLESRKSAHNAKVKQRQRLRASGLNGILDRKKKKDEVAKSTSSLSLQDFMSPI
Protein: Granule-bound starch synthase 1, chloroplastic/amyloplastic (AtGBS1) (AtGBSS1) (EC 2.4.1.242) (Granule-bound starch synthase I) (GBSS-I) (Q9MAQ0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the synthesis of amylose. Destroyed as it is released from the starch granules during the night. The circadian expression is controlled by CCA1 and LHY transcription factors.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15347792, ECO:0000269|PubMed:25710501}. Note=Exclusively bound to starch granules and found in the soluble fraction only if PTST is absent. {ECO:0000269|PubMed:15347792, ECO:0000269|PubMed:25710501}.
Interaction partners:
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic
- Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
- 4-alpha-glucanotransferase DPE2
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme 2-2, chloroplastic/amyloplastic
- 1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
Sequence:
MATVTASSNFVSRTSLFNNHGASSCSDVAQITLKGQSLTHCGLRSFNMVDNLQRRSQAKPVSAKSSKRSSKVKTAGKIVCEKGMSVIFIGAEVGPWSKTGGLGDVLGGLPPALAARGHRVMTICPRYDQYKDAWDTCVVVQIKVGDKVENVRFFHCYKRGVDRVFVDHPIFLAKVVGKTGSKIYGPITGVDYNDNQLRFSLLCQAALEAPQVLNLNSSKYFSGPYGEDVVFVANDWHTALLPCYLKSMYQSRGVYMNAKVVFCIHNIAYQGRFAFDDYSLLNLPISFKSSFDFMDGYEKPVKGRKINWMKAAILEAHRVLTVSPYYAQELISGVDRGVELHKYLRMKTVSGIINGMDVQEWNPSTDKYIDIKYDITTVTDAKPLIKEALQAAVGLPVDRDVPVIGFIGRLEEQKGSDILVEAISKFMGLNVQMVILGTGKKKMEAQILELEEKFPGKAVGVAKFNVPLAHMITAGADFIIVPSRFEPCGLIQLHAMRYGTVPIVASTGGLVDTVKDGYTGFHIGRFNVKCEVVDPDDVIATAKAVTRAVAVYGTSAMQEMVKNCMDQDFSWKGPARLWEKVLLSLNVAGSEAGTEGEEIAPLAKENVATP
Protein: Transducin/WD40 repeat-like superfamily protein (F4K0D3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Pre-mRNA-splicing factor SYF2
- Pre-mRNA-splicing factor ATP-dependent RNA helicase DEAH7
- At2g20330/F11A3.12
- CwfJ-like family protein
- At3g05070
- Protein pleiotropic regulatory locus 1
- Protein pleiotropic regulator PRL2
- Peptidyl-prolyl cis-trans isomerase CYP18-2
- Pre-mRNA-processing factor 19 homolog 2
- Peptidyl-prolyl cis-trans isomerase CYP57
Sequence:
MDLICNSYANDSDDEPEPVTNERLTSKIAAAPSIPSKRPYPVPEERQYKPPRRPYPPHGSYSESQTSSSFSIPVPVPVPVPGRYVSKRERSLLASLSTIPTPDQSSDLSQKPYSSPTVLGSISDSDVPRHVLSSVRHRPKGSSLQTEMPSRMSISLTGHTKAVTAIDWSTSHVHLLASAGLDGAVYVWNVWSNDKKKVRAFLHHNAPVKDVKWSKQGLSLLSCGYDCTSRLFDVERGVETQSFKEDEVVGVVKFHPDNCNVFLSGGSKGSLRLWDIRANKFVHEYVRDLGPILDVEFIAGGKQFISSSDVSGRNISENAVIVWDISREVPLSNQVYVEAYTCPCIKRHPQDPVFIAQSHGNYTAIFSTNPPFKLNKYKRFEGHWVAGFPIKCNFSPDGETLASGSSDGSVYMYDYKSTALIKKLKAYEQPCVNVSYHPVLPNVVAACSWNGQVSVFE
Protein: Rho guanine nucleotide exchange factor 15 (A0A0G2JTU0)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- FYVE, RhoGEF and PH domain containing 5
Sequence:
MSAQSLPAATPPTLKPPRIIRPRPPSRHRAPHSPGPPHNGSSPKALPQISNDASASVCTSIFWEPPTGSLKPPALLPPSVSRASLDSQTSPDSPSSTPSPSPVSRRSISPEPAPCSPVPPPKPSGSSRTPLPLGPVPLQDGSASAPGTVRRLAGKFEWGAEGKAQSADSLERCSQGSTDVNGEKETLQVGLSGNGSQENGTPDAALACPPCCPCVCHVAKPGLELRWVPVGSSDDILRAPCRASPLRASRSRINPPVISHPPVVLTSYRSTAERKLLPPLKPPKPTRVRQDTSTSGELPQPDLELPSEDGIQAAPKAWEGDRPEEAPQNAPPPVALEGREEEGLEGLKELQWELPLQDEPLYQTYRAAVLSEELWGVGEDGGPSPANPGEAPTFSRLPGPRNTLWQELPAVRGSGLLESLSPQERRMQESLFEVVTSEASYLRSLRLLTDTFVLSQALRDTLTPRDHHTLFSNVQRVQSVSERFLGTLLSRVRSSPHISDLCDVVHAHAVGPFSVYVDYVRNQQYQEETYSRLMDTNVRFSAELRRLQSLPKCERLPLPSFLLLPFQRITRLRMLLQNILSQTEEGSSRQENAQKALGAVSKIIERCSAEVGRMKQTEELIRLTQRLRFHKVKALPLVSWSRRLELQGELTELGCRRGGVLFTSRPRFTPLCLLLFSDLLLITQPKSGQRLQVLDYAHRSLVQAQQVPDPSGPPTFRLSLLSNHQGRPTHRLLQAASLSDMQRWLGAFPTPGPLPCSPDTIYEDCECSQELCSEPSTPSKTEGQSLESKAPRKHLHKNPEGWLKGLPGAFPAQLVCEVTGEHERRKHLRQHQKLLEAAGPSSDTPDTPQP
Protein: Interleukin (Q7T110)
Organism: Gallus gallus (Chicken)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MMCKVLIFGCISVAMLMTTAYGASLSSAKRKPLQTLIKDLEILENIKNKIHLELYTPTETQECTQQTLQCYLGEVVTLKKETEDDTEIKEEFVTAIQNIEKNLKSLTGLNHTGSECKICGANNKKKFPDFLHELTNFVRYLQK
Protein: Cytokine induced apoptosis inhibitor 1 (H3BQ23)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MADFGISAGQFVAVVWDKSSPVEALKGLVDKLQALTGNEGRVSVENIKQLLQSAHKESSFDIILSGLVPGSTTLHSAEILAEIARILRPGGCLFLKEPVETAVDNNSKVKTASKLCSALTLSGLVEVKE
Protein: Cytochrome P450 26B1 (EC 1.14.13.-) (Cytochrome P450 retinoic acid-inactivating 2) (Cytochrome P450RAI-2) (Q811W2)
Organism: Mus musculus (Mouse)
Function: Involved in the metabolism of retinoic acid (RA), rendering this classical morphogen inactive through oxidation (By similarity). Involved in the specific inactivation of all-trans-retinoic acid (all-trans-RA), with a preference for the following substrates: all-trans-RA > 9-cis-RA > 13-cis-RA (By similarity). Generates several hydroxylated forms of RA, including 4-OH-RA, 4-oxo-RA, and 18-OH-RA (By similarity). Essential for postnatal survival. Plays a central role in germ cell development: acts by degrading RA in the developing testis, preventing STRA8 expression, thereby leading to delay of meiosis. Required for the maintenance of the undifferentiated state of male germ cells during embryonic development in Sertoli cells, inducing arrest in G0 phase of the cell cycle and preventing meiotic entry. Plays a role in skeletal development, both at the level of patterning and in the ossification of bone and the establishment of some synovial joints.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43174}. Microsome membrane {ECO:0000250|UniProtKB:O43174}; Peripheral membrane protein {ECO:0000250|UniProtKB:O43174}.
Interaction partners:
- Retinal dehydrogenase 2
- Retinaldehyde dehydrogenase 3
- Aldehyde dehydrogenase 1A1
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Aldehyde dehydrogenase, cytosolic 1
- Cytochrome P450 3A
- Cytochrome P450 3A11
- Cytochrome P450 3A13
- Cytochrome P450 3A25
Sequence:
MLFEGLELVSALATLAACLVSVTLLLAVSQQLWQLRWAATRDKSCKLPIPKGSMGFPLIGETGHWLLQGSGFQSSRREKYGNVFKTHLLGRPLIRVTGAENVRKILLGEHQLVSTEWPRSARVLLGPNTVANSIGDIHRNKRKVFSKIFSHEALESYLPKIQLVIQDTLRAWSSQPEAINVYQEAQRLTFRMAVRVLLGFSIPEEDLGHLFEVYQQFVENVFSLPVDLPFSGYRRGIQARQILQKGLEKAIREKLQCTQGKDYSDALDILIESSKEHGKEMTMQELKDGTLELIFAAYATTASASTSLIMQLLKHPAVLEKLREELRAQGLLHGGGCPCEGTLRLDTLSSLRYLDCVIKEVMRLFTPVSGGYRTVLQTFELDGFQIPKGWSVMYSIRDTHDTAPVFKDVNVFDPDRFSQARSEDKDGRFHYLPFGGGVRTCLGKHLAKLFLKVLAVELASTSRFELATRTFPRITLVPVLHPVDGLSVKFFGLDSNQNEILPETEAMLSATV
Protein: Type II secretion system core protein G (E0SM38)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell inner membrane {ECO:0000256|ARBA:ARBA00004377}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004377}.
Interaction partners:
- Type II secretion system protein J
- Type II secretion system protein H
- Type II secretion system protein K
- Secretin OutD
- Type II secretion system protein F
- Type II secretion system protein E
- Type II secretion system protein L
- Type II secretion system protein I
- Type II secretion system protein M
- Type II secretion system protein C
Sequence:
MERRQRGFTLLEIMVVIVILGVLASLVVPNLMGNKEKADRQKAISDIVALESALDMYKLDNSRYPTTEQGLGALVKKPTTPPEPRSYPQDGYIRRLPQDPWGAEYQLVSPGRHGKVDVFSYGPDGMPDTDDDIGNWNVGTSAHSNGSNGNGNP
Protein: Myosin-10 (Myosin XI D) (AtXID) (F4IVR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Myosin heavy chain that is required for the cell cycle-regulated transport of various organelles and proteins for their segregation. Functions by binding with its tail domain to receptor proteins on organelles and exerting force with its N-terminal motor domain against actin filaments, thereby transporting its cargo along polarized actin cables (By similarity).
Interaction partners:
- Protein trichome birefringence
Sequence:
MVWKHQLIGFSGIFSNVSPASVKVTVGSQVWVEDPDEAWLDGEVVEANGQEIKVNCQTKTVVAKVNAVHPKDPEFPELGVDDMTKLAYLHEPGVLLNLKARYNANEIYTYTGNILIAVNPFKRLPHLYGNEIMEQYKGTDFGELSPHPFAVADSAYRKMINEGVSQAILVSGESGAGKTESTKMLMQYLAYMGGKAESEGRSVEQQVLESNPVLEAFGNAKTVRNNNSSRFGKFVEIQFNHMGRISGAAIRTYLLERSRVCQVSDPERNYHCFYMLCAAPEQETERYQLGKPSTFHYLNQSNCHALDAIDDSKEYLATRKAMDVVGISPEEQDAIFRVVAAILHLGNIEFAKSEESDGAEPKDDKSRFHLKVAAKLFMCDEKALENSLCNRVMVTRGESITKPLDPGSAALSRDALAKIVYSKLFDWLVTKINNSIGQDSSSKYIIGVLDIYGFESFKTNSFEQFCINLTNEKLQQHFNQHVFKMEQEEYTKEEIDWSYIEFIDNQDVLDLIEKKPGGIIALLDEACMFPRSTHDTLAEKLYQTFGSHKRFTKPKLARTDFTICHYAGDVTYQTELFLDKNKDYVVGEHQSLMNSSDCSFVSSLFPKSREESSKSSKFSSIGSQFKQQLQSLLETLNTTEPHYIRCVKPNNVLKPEIFENVNVLHQLRCGGVMEAIRISCAGYPTRKPFNEFLTRFRILAPEATERSFDEVDACKKLLARVDLKGFQIGKTKVFLRAGQMAELDAHRAEVLGHSARIIQRKVITYLSRKKYLLLQSASTEIQAFCRGHIARVQFKATRREAASVRIQKQARTYICQTAFKKLCASAISIQSGLRAMAARVEFQYRTKRKAAIIIQSQIRRCLCRRRYLRTKKAAITTQCGWRVKVAHRELRKLKMAAKETGALQDAKTKLEKEVEELTSCLELEKQMRMELEQVKTQEVEDLRSALNDMKLQLGETQVTKSEEILKLQSALQDMQLEFEELAKELEMTNDLAAENEQLKDLVSSLQRKIDESDSKYEETSKLSEERVKQEVPVIDQGVIIKLEAENQKLKALVSTLEKKIDSLDRKHDVTSSNISDQLKESASSDYEMLSNLAAENERLKALVSSLENENYENDGNDSPNEQKEGPQMLKEEILAEDFSIDDEMTNKLAAENKDLYDLVDLLERKIDETEKKYEEASKLCEERLKQVVDTEKKYEEASRLCEERLKQVVDTETKLIELKTSMQRLEEKVSDMEAEDKILRQQALRNSASRKMSPQKSLDLFVFMYLFQPVENGHHESFAPIPSRRFGAMSFRRSQIEQQPHEFVDVLLKCVSKNVGFSHGKPVAAFTIYKCLIHWKLFEAEKTSVFDRIVPIFGSAIENPEDDSNLAYWLTNTSTLLFLLQRSLKSHSTTGASPKKPPQPTSFFGRMTQGFRSPSSASLSGDVVQQVDARYPALLFKQQLTAYIETIYGIFQENVKRKLAPVLSSCIQGLKDSSHEFSAETLSAESSEQNSPEKPSEENPPEKLSEDNSSGKLSEDYLAAKPSEDNSPAKPSEENSQAKLSEVNPQAKPSAENSLAKPSEENSPTETWQDVIGLLNQLLGTLKKNYVPLFLAQKIFCQTFQDINVQLFNSLLQRECCTFIMGKKVNVWLNELESWCSQATEDFVGSSWDELKNTRQALVLLVTEQKSTITYDDLTTNLCPALSTQQLYRICTLCKIDDHEDQNVSPDVISNLKLLVTDEDEDSRSFLLDNNSSIPFAADEISNSMQEKDFTNVKPAVELADNPNFHFLKE
Protein: Myosin binding subunit of myosin phosphatase (Myosin binding subunit, isoform J) (Q8MV37)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSLDARNNSAMMKRAEQLKRWEESDTNRAAPTPRHEHGRRIKFSSGCVFLAACLSGDKDEVVQLLDQGADINTANVDGLTALHQACIDDNLDMVEFLVERGADINRQDNEGWTPLHATASCGFVSIARYLVENGADVAAVNSDGDLALDLAIDVQHMAMIDYMEKMVQELNINVDEARKAEELAMLNDAKKWLRSDAAEVDRPHPKTGATALHVAAAKGYTKVLGLLLAGRGNVDRQDNDGWTPLHAASHWGQRETAEMLVESLADMDIRNYAGQSCIDVADRKIVKFLEELRANKRNKRRPSSQIRISDAMENHVEKTPTKLVRVEVRTDATKDAENVKPNQQIHAVEHPVEEEAPWRRKLPRTPSDSPTNNQVPDRELGTNSSETANDVILRRTQSFENDQKKPTVTIATSTAATAINSPSTTVQTPPIRRSFVPPVRDEESETQRKAHAKRVRETRRSTQGVTLDEIKSAEELVKKKNMGMANNNNNNNISTTTTNTISNSGNETSSASSTSAPTPSILGSNEQQDELQPPPPPTTPPPAVIPTTTTATDETEIEEVVSSPPAGQSQNDTTASFTLSAPVRRSLSTEGEADANSDPEGDQDQTVVSASYTIMPRRERLPESSENVESIRSPQKTEPVAKSSSEDKSEEPPHARPTDLPLIPAPAAPSTEAIKSSSAATTPAALESPVRLRDKRGLSGSQESETKSDTASPVSSHPDFNARDSLLSLYARRTTDSSAGGGGVGGGAGVGAGGASGAATSSSTSAAERRPSWRLKFDAGSKFKLEDITSGGTYPPNNSTIIPSAPAVMAAANLSTTTGVQRRISSGPIALNASNQSLNSVGRPVSAPSEGTNNSAYVTPSARKFETNATSTGATTAATTTSNSTSNSVSATSANHTTATAPNATSNHDDKDNDKENDNRTQTVIQRRRKPKRRSTGVVHIDMDELDPERQNESSNNDNEEKEKESGSERTSRSRLGSTASTATTSESKSSSSNDKTENGDGIDYKALWEAEKLENDKLRQMLKQKDDEAVQTRATLERFANATTKNSLSELEKRERRAMERKLSELEEELKQLDAYKSDNHRLKEENAALIRVISKLSK
Protein: RH15640p (Q6NQV8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MENLGYKEGSTKPRRMTRSISVVTKTEVEQPLTENNANNRFKSIPPNLMVRWRNNTDAMIEAQYPTAGEFEYMECGPSPPAESAPSMYDSFEEPTSELSVQICNDTLRISLIDQMKSAAGRVKLFEDIEQSNVVAEGIRTHFESASKLEKNLCYLWAAYLKRWDLIESLLEAGADLHFCDQNGISALHLSAFSGCLATLGLLVAKGLNVNLQSKCYTPLHCAAFGNAAEAAKLLINNGADISKDTSKPNCEESLLHCAVRSNALECLQIFIAEGADVNSLKPNGTNAIHLAADLGNIQCLEALLNAPNADANVRICIREKESTALHLAADEGNVECVDLLLAKGADAKLKNHRGFTPLHLAARTSSLDCVESLLRNGNADANAEDFDHRTPLHAAVGKSENAYDIMETLIQWGANVNHKDIYGFTALHLAALDGLVQCVEMLIFHGADVTTKSKKGTSALNVITRKTPASVAMIRQKLDAAITLHHSQDPVNREVELELDFRQLLQHCHPREISYLNTFVDEGQKEILEHPLCSSFLYIKWGRIRKYYIGRLIFCFSFVLFLTLYVLTALAHNCYNGSKNDNTTIPAQELCQKQSILGDMLRNNPFVMEMQWWVLVAITIVEIFRKLYGITGYSSFRHYVTQVENIMEWFVITSVFVISYIYTNKTYTFQNHIGAFAVLLGWTNLMLMIGQLPVFDVYVAMYTRVQGEFAKLFMAYSCMLIGFTISFCVIFPSSSSFANPFMGFITVLVMMIGEQDLSLLINDPEGKDPPFLLEVSAQITFVLFLLFVTIILMNLLVGIAVHDIQGLKKTAGLSKLVRQTKLISYIESALFNGYLPTWLRNLLHYTALVSPQAYRVVLCVKPLNPSEKRLPREILMKAYEVGKMRKHFGHTISSKNSAENYLSYKNKYNNNNGATTGYVLPDSDPDAGQFTTLTTKIDDNADRIEFLTQEIQELKQALISQQQQASKVIDKLLIVISNQQKQNLRK
Protein: tRNA 5-methylaminomethyl-2-thiouridine biosynthesis bifunctional protein MnmC (tRNA mnm(5)s(2)U biosynthesis bifunctional protein) [Includes: tRNA (mnm(5)s(2)U34)-methyltransferase (EC 2.1.1.61); FAD-dependent cmnm(5)s(2)U34 oxidoreductase (EC 1.5.-.-)] (P77182)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the last two steps in the biosynthesis of 5-methylaminomethyl-2-thiouridine (mnm(5)s(2)U) at the wobble position (U34) in tRNA. Catalyzes the FAD-dependent demodification of cmnm(5)s(2)U34 to nm(5)s(2)U34, followed by the transfer of a methyl group from S-adenosyl-L-methionine to nm(5)s(2)U34, to form mnm(5)s(2)U34.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- tRNA-specific 2-thiouridylase MnmA
- tRNA modification GTPase MnmE
- tRNA uridine 5-carboxymethylaminomethyl modification enzyme MnmG
- tRNA
- tRNA 2-selenouridine synthase
- tRNA U34 carboxymethyltransferase
Sequence:
MKHYSIQPANLEFNAEGTPVSRDFDDVYFSNDNGLEETRYVFLGGNQLEVRFPEHPHPLFVVAESGFGTGLNFLTLWQAFDQFREAHPQAQLQRLHFISFEKFPLTRADLALAHQHWPELAPWAEQLQAQWPMPLPGCHRLLLDEGRVTLDLWFGDINELTSQLDDSLNQKVDAWFLDGFAPAKNPDMWTQNLFNAMARLARPGGTLATFTSAGFVRRGLQDAGFTMQKRKGFGRKREMLCGVMEQTLPLPCSAPWFNRTGSSKREAAIIGGGIASALLSLALLRRGWQVTLYCADEAPALGASGNRQGALYPLLSKHDEALNRFFSNAFTFARRFYDQLPVKFDHDWCGVTQLGWDEKSQHKIAQMLSMDLPAELAVAVEANAVEQITGVATNCSGITYPQGGWLCPAELTRNVLELAQQQGLQIYYQYQLQNLSRKDDCWLLNFAGDQQATHSVVVLANGHQISRFSQTSTLPVYSVAGQVSHIPTTPELAELKQVLCYDGYLTPQNPANQHHCIGASYHRGSEDTAYSEDDQQQNRQRLIDCFPQAQWAKEVDVSDKEARCGVRCATRDHLPMVGNVPDYEATLVEYASLAEQKDEAVSAPVFDDLFMFAALGSRGLCSAPLCAEILAAQMSDEPIPMDASTLAALNPNRLWVRKLLKGKAVKAG