wanglab/gogpt-training-data huggingface dataset:
Protein: Olfactory receptor (A0A126GWR7)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU363047}.
Interaction partners:
Sequence:
MEWENHTILVEFFLKGLSGHPRLELLFFVLIFIMYVVILLGNGTLILISILDPHLHTPMYFFLGNLSFLDICYTTTSIPSTLVSFLSERKTISLSGCAVQMFLGLAMGTTECVLLGMMAFDRYVAICNPLRYPIIMSKDAYVPMAAGSWIIGAVNSAVQSVFVVQLPFCRNNIINHFTCEILAVMKLACADISDNEFIMLVATTLFILTPLLLIIVSYTLIIVSIFKISSSEGRSKASSTCSAHLTVVIIFYGTILFMYMKPKSKETLNSDDLDATDKIISMFYGVMTPMMNPLIYSLRNKDVKEAVKHLLNRRFFSK
Protein: Dystrobrevin, isoform F (A8DYB7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- GH13213p
- AT08210p
- Lateral muscles scarcer, isoform B
- AT25567p
- IP02644p
- FI16515p1
- Dystrophin, isoforms A/C/F/G/H
- EG:4F1.1 protein
- Dystroglycan 1
- Sarcoglycan alpha, isoform C
Sequence:
MELEPRVAILQDLRLQTFDSIRFASYRTASKLRYIQKSTNLHLVDIWNVIEAFRENGLNTLEPQSEVSVARLETLVSSLYHNLNKRLPTAQQVPVDSKAGLLLNWLLAAYTSDNSGKIRVFSIKVALATMCSGKLVDKLRYIFSQISDGAGQLVAWKLGEFLREVLALPAAVYESPTFHYKEGLEEEIFPAENKVTVNDFMATLMSEPGPSCLVWLPLVHRLATVETIVHPTVCSVCHKENFTGFRYRCQRCHAYQLCQECFWHGKTSLNHQNDHEVKEYSSYKSPSKQIGHSLRKSFRCVPEKTVQVLPRFPDQPEKTLNLSHIVPPSPLPSHNGFSDPSGLVHGHHGPHPGLPGQHGLFDRSSTLDSRATGRSLDSASGTAGTTMSRVAAASANDEEHRLIARYAARLAQENRAPSNLPDNATPIGTDNSRAQRELIAQLESKNKEIMREIARLRRQQETEQMAPENPALINELRALRQRKGELEGHLGALQDSRRQLMEQLEGLMRMLKNQQTASPRSTPNSSPRSGKSPPMPGGAGILGTSPMSALHAQQMQQHPMAGGVRASQQQLLQQQQQQAHGHGPFSQSQLEQLNQISSDMRSAFAANGSATPPPMRTTTATANVSAIPSLNPISNQNPNLNPDAELNEAADHLTSAISHMVSDLNAGRGRAQQLGPQPASSIPQARFIMPLEFRHIEGGESEDSSQCECNDCECGEYEEVFRTDEDLECEGAAAPFGNAYSLFPTSGVHEEDHFDYTFGQGEELSQVNRILGYRNHPELFIDDEQAGFPALHEIGETIDELQLIMHAYIMKYSLNI
Protein: Acyl-coenzyme A diphosphatase NUDT19 (EC 3.6.1.-) (EC 3.6.1.77) (Androgen-regulated protein RP2) (Nucleoside diphosphate-linked moiety X motif 19) (Nudix motif 19) (Renal CoA diphosphohydrolase) (Testosterone-regulated RP2 protein) (RP2p) (P11930)
Organism: Mus musculus (Mouse)
Function: Fatty acyl-coenzyme A (CoA) diphosphatase that hydrolyzes fatty acyl-CoA to yield acyl-4'-phosphopantetheine and adenosine 3',5'-bisphosphate. Mediates the hydrolysis of a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters and at low substrate concentrations medium and long-chain fatty-acyl-CoA esters are the primary substrates. Highest activity seen with medium-chain acyl-CoA esters and higher rates of activity seen with the unsaturated acyl-CoA esters compared with the saturated esters. Exhibits decapping activity towards dpCoA-capped RNAs in vitro.
Subcellular location: Peroxisome {ECO:0000269|PubMed:16185196, ECO:0000269|PubMed:29378847}.
Interaction partners:
- NAD-capped RNA hydrolase NUDT12
- Peroxisomal coenzyme A diphosphatase NUDT7
- m7GpppN-mRNA hydrolase NUDT17
- Nucleotide triphosphate diphosphatase NUDT15
Sequence:
MSSSSSWRRAATVMLAAGWTHSSPAGFRLLLLQRAQNQRFLPGAHVFPGGVLDAADSSPDWVRLFAPRHTPPRFGLGPEPPRQPPFPGLSHGDADPAALPDDVALRICAIREAFEEAGVLLLRPRDAAPASQEPSQALSPPAGLAEWRSRVRSDPRCFLQLCAHLDCTPDIWALHDWGGWLTPYGRTIRRFDTTFFLCCLRDIPRVEPDVAEVVGYQWLSPSEATECFLSKEIWLAPPQFYEMRRLENFASLSALYRFCSDRPSEVPEKWLPIILLTSDGTIHLLPGDELYVKDSDFLEKNMSTDKKTEEIVKEGKVLNRVVIHSPYVYEIYMTLPSENKHVYPRNYIVNKRCTAHL
Protein: Gasp, isoform A (LD05259p) (Q9VNL0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- FI03450p
- Vermiform, isoform I
- Chitin deacetylase-like 4
- LD43683p
- HL04814p
- Uninflatable, isoform C
- LD12305p
Sequence:
MKKFLVVFVALFGAAVAQSSFKCPDDFGFYPHDTSCDKYWKCDNGVSELKTCGNGLAFDATDSKYLTENCDYLHNVDCGDRTELEPPITTPHCSRLYGIFPDENKCDVFWNCWNGEPSRYQCSPGLAYDRDARVCMWADQVPECKNEEVANGFSCPAAGELANAGSFSRHAHPEDCRKYYICLEGVAREYGCPIGTVFKIGDSDGTGNCEDPEDVPGCEDYYGDLDLKSIRKSELLAGLNSEGRTKGAPKTKAASSSS
Protein: Acyl-CoA thioester hydrolase YbgC (Acyl-CoA thioesterase) (EC 3.1.2.-) (P0A8Z3)
Organism: Escherichia coli (strain K12)
Function: Thioesterase that appears to be involved in phospholipid metabolism. Some specific acyl-ACPs could be physiological substrates. Displays acyl-CoA thioesterase activity on malonyl-CoA in vitro, catalyzing the hydrolysis of the thioester bond.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:16294310}; Peripheral membrane protein {ECO:0000269|PubMed:16294310}; Cytoplasmic side {ECO:0000269|PubMed:16294310}.
Interaction partners:
- Tol-Pal system protein TolQ
- Tol-Pal system protein TolR
- Cell division coordinator CpoB
- Tol-Pal system protein TolB
- Peptidoglycan-associated lipoprotein
- Glycerol-3-phosphate acyltransferase
- Acyl-CoA thioester hydrolase YciA
- CDP-diacylglycerol--serine O-phosphatidyltransferase PssA
- 1,4-dihydroxy-2-naphthoyl-CoA hydrolase
- Acyl-CoA thioesterase 2
Sequence:
MNTTLFRWPVRVYYEDTDAGGVVYHASYVAFYERARTEMLRHHHFSQQALMAERVAFVVRKMTVEYYAPARLDDMLEIQTEITSMRGTSLVFTQRIVNAENTLLNEAEVLVVCVDPLKMKPRALPKSIVAEFKQ
Protein: CTD nuclear envelope phosphatase 1 (I3L3K5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XQYQTVRYDILPLSPVSRNRLAQVKRKILVLDLDETLIHSHHDGVLRPTVRPGTPPDFILKVVIDKHPVRFFVHKRPHVDFFLEVVSQWYELVVFTASMEIYGSAVADKLDNSRSILKRRYYRQHCTLELGSYIKDLSVVHSDLSSIVILDNSPGAYRSHPDNAIPIKSWFSDPSDTALLNLLPMLDALRFTADVRSVLSRNLHQHRL
Protein: Periplasmic nitrate reductase, electron transfer subunit (Diheme cytochrome c NapB) (P44654)
Organism: Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Function: Electron transfer subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from the membrane-anchored tetraheme c-type NapC protein and transfers these to NapA subunit, thus allowing electron flow between membrane and periplasm. Essential for periplasmic nitrate reduction with nitrate as the terminal electron acceptor.
Subcellular location: Periplasm {ECO:0000269|PubMed:11223519, ECO:0000269|PubMed:11389694}.
Interaction partners:
- Ferredoxin-type protein NapH
- Cytochrome c-type protein NapC
- Ferredoxin-type protein NapG
- Cytochrome c-type protein TorY
- Trimethylamine-N-oxide reductase
- Ferredoxin-type protein NapF
- Chaperone NapD
- Cytochrome c-552
- Dimethyl sulfoxide reductase DmsA
- Uncharacterized protein HI_1043
Sequence:
MINMTKQVSKILAGLFTALFAGSLMASDAPAVGKDLTQAAENIPPAFHNAPRQGELPALNYVNQPPMVPHSVANYQVTKNVNQCLNCHSPENSRLSGATRISPTHFMDRDGKVGSSSSPRRYFCLQCHVSQANVDPIVPNDFKPMKGYGN
Protein: Wall-associated receptor kinase 2 (EC 2.7.11.-) (Q9LMP1)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein kinase that may function as a signaling receptor of extracellular matrix component. Binding to pectin may have significance in the control of cell expansion, morphogenesis and development.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- At4g30670
Sequence:
MKVQEGLFVVAVFYLAYTQLVKGQPRKECQTRCGNVAVEYPFGTSPGCYYPGDESFNLTCNEQEKLFFGNMPVINMSLSGQLRVRLVRSRVCYDSQGKQTDYIAQRTTLGNFTLSELNRFTVVGCNSYAFLRTSGVEKYSTGCISICDSATTKNGSCSGEGCCQIPVPRGYSFVRVKPHSFHNHPTVHLFNPCTYAFLVEDGMFDFHALEDLNNLRNVTTFPVVLDWSIGDKTCKQVEYRGVCGGNSTCFDSTGGTGYNCKCLEGFEGNPYLPNGCQDINECISSRHNCSEHSTCENTKGSFNCNCPSGYRKDSLNSCTRKVRPEYFRWTQIFLGTTIGFSVIMLGISCLQQKIKHRKNTELRQKFFEQNGGGMLIQRVSGAGPSNVDVKIFTEKGMKEATNGYHESRILGQGGQGTVYKGILPDNSIVAIKKARLGNRSQVEQFINEVLVLSQINHRNVVKVLGCCLETEVPLLVYEFINSGTLFDHLHGSLYDSSLTWEHRLRIATEVAGSLAYLHSSASIPIIHRDIKTANILLDKNLTAKVADFGASRLIPMDKEQLTTIVQGTLGYLDPEYYNTGLLNEKSDVYSFGVVLMELLSGQKALCFERPHCPKNLVSCFASATKNNRFHEIIDGQVMNEDNQREIQEAARIAAECTRLMGEERPRMKEVAAELEALRVKTTKYKWSDQYRETGEIEHLLGVQILSAQGETSSSIGYDSIRNVTTLDIEAGR
Protein: Carbohydrate sulfotransferase 10 (EC 2.8.2.-) (HNK-1 sulfotransferase) (HNK-1ST) (HNK1ST) (RaHNK-1ST) (Sul-T) (O54702)
Organism: Rattus norvegicus (Rat)
Function: Catalyzes the transfer of sulfate from 3'-phosphoadenylyl sulfate (PAPS) to position 3 of terminal glucuronic acid of both protein- and lipid-linked oligosaccharides. Participates in biosynthesis of HNK-1 carbohydrate structure 3-O-sulfo-beta-D-GlcA-(1->3)-beta-D-Gal-(1->4)-D-GlcNAc-R, a sulfated glucuronyl-lactosaminyl residue carried by many neural recognition molecules, which is involved in cell interactions during ontogenetic development and in synaptic plasticity in the adult. May be indirectly involved in synapse plasticity of the hippocampus, via its role in HNK-1 biosynthesis. Sulfates terminal glucuronyl residue of the laminin globular (LG)-domain binding epitope on DAG1/alpha-dystroglycan and prevents further polymerization by LARGE1 glycosyltransferase. Likely defines the chain length of LG epitope, confering binding specificity to extracellular matrix components. Plays a role in down-regulating the steroid hormones. Sulfates glucuronidated estrogens and androgens with an impact in hormone cycle and fertility. Has a preference for glucuronyl moiety at the 3-hydroxyl group of a sterol ring rather than the 17-hydroxyl group, showing high catalytic efficiency for 17beta-estradiol 3-O-(beta-D-glucuronate) and dehydroepiandrosterone 3-O-(beta-D-glucuronate) hormones (By similarity).
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:23723439}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 2
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 1
- Sulfotransferase 1A1
- Sulfotransferase 1C1
- UDP-glucuronosyltransferase
- Sulfotransferase 2A2
- Estrogen sulfotransferase Ste2
- UDP-glucuronosyltransferase
- UDP-glucuronosyltransferase 1A1
- Sulfotransferase 1B1
Sequence:
MHHQWLLLAACFWVIFMFMVASKFITLTFKDPDGYSAKQEFVFLTAMPEAEKLRGEKHFSEVMKPTGKMLSESHPDQPPVYLERLELIRNACKEEALRNLSHTEVSKFVLDRIFVCDKHKILFCQTPKVGNTQWKKVLIVLNGAFSSIEEIPENVVHDHEKNGLPRLSSFSKIGIQKRLKTYFKFFIVRDPFERLISAFKDKFVHNPRFEPWYRHEIAPGIIRKYRKNRTETRGIQFEDFVRYLGDPNRRWLDLQFGDHIIHWVTYVKLCAPCEIKYSVIGHHETLEADAPYILKEAGIDHLVSYPTIPPGITMYNRTKVEQYFLGISKRDIRRLYARFEGDFKLFGYQKPDFLLN
Protein: Piwi domain-containing protein (H2KZD5)
Organism: Caenorhabditis elegans
Interaction partners:
- DRBM domain-containing protein
- Endoribonuclease dcr-1
- RNA-directed RNA polymerase
- High mobility group protein hmg-12
- Transcription initiation factor TFIID subunit 11
- ANK_REP_REGION domain-containing protein
Sequence:
MQSDNVGRGRGSRGGSRGGSGRGRGRGGYGDSYRPDLETRETHVTYQGKVKYEGGDRHDFNYEKTPTGSYRGSHRDGQEGSRGNRGSFRGGRGGYDRRRDDEESKAENRFGGYNRGANGGNYRGRTGGSGRGGSTQTTTVDPKYNGLILENSAEPKLKGLNSDMNQKQNPRLALNIFGLELSERTIFRHVVQMKLIDRQHNKEYILTTMSARGRGNRATKQKDNFILLDILLKQWAAKKGQQNLPAFAYDGAQSLFTLEGISLMVDIKKEDALEIPELSNFLKDSISFLSGDLEISCEPDLEKPSFVQTELNEWSDPRFYAYLDIVTSQSAIRSERYLSQSKGLYVHTQSLEELRVKWAVAAKGIHKGCRIVGANGPLPILELDPQSTQYYASIPLSQMLQYAFPRDFPPNRIVNPNMKLQRAVKLLLKDLKCNPYYDDKQIWATNTITVSDVDYNAPKDPEFRQKYPNLKFPMLPAVQCGTGPHKRLMPLEYLKVLPYQSIDRRVLEEFELTPRANAPNERWSTLQKHYDQFGFNDQVMKDFGVQICNDPFNNVSEIDGERVLAPSVAYADPVHVDDEKRDWKAQDKKFVTPATIDHLMFVLVAGYTRTWDADCDATKFVAKAFMQRCKDKGMHIGSYSMDQHNGERGSENFLTSVFKNLVTHPNYRDSSFTPFVLFISDDVPNIHECLKFEERMSDIPTQHVLLKNVKKMRDNIEKKSQGGRRAYDLTLDNIVMKANIKCGGLNYTADIPRDLACWNEVSTFVIGMDVAHPDRNAAREGNPSTVGLSCNSAENPYSFIGDFLYTDPRREAIQDEILRKFTDQSVRNFAEIRGFPKKVIIFRDGVSFGEETAALKEVEIIEQTIKTAAKSMGHSDYAPKVLAIVVKKRHHTRFYAKGGHHGNMPINPLPDTSVGGDIAEYGKRQIFIQAFRPVQGTAKVPSFLVIRDDEEVSDEHVAKMVCAVCSLHQLVNSPTSIPTPVYVAHELAKRGTGLYKAYRFKNGELFDDWETLTTQLSYSTLDRLSKVRVV
Protein: UDP-galactopyranose mutase (UGM) (EC 5.4.99.9) (UDP-GALP mutase) (Uridine 5-diphosphate galactopyranose mutase) (P37747)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the interconversion through a 2-keto intermediate of uridine diphosphogalactopyranose (UDP-GalP) into uridine diphosphogalactofuranose (UDP-GalF).
Interaction partners:
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Beta-1,6-galactofuranosyltransferase WbbI
- Putative O-antigen transporter
- Glucose-1-phosphate thymidylyltransferase 1
- Putative O-antigen polymerase
- dTDP-glucose 4,6-dehydratase 1
- Putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ
- Putative glycosyltransferase WbbK
- UDP-glucose 4-epimerase
- dTDP-4-dehydrorhamnose reductase
Sequence:
MYDYIIVGSGLFGAVCANELKKLNKKVLVIEKRNHIGGNAYTEDCEGIQIHKYGAHIFHTNDKYIWDYVNDLVEFNRFTNSPLAIYKDKLFNLPFNMNTFHQMWGVKDPQEAQNIINAQKKKYGDKVPENLEEQAISLVGEDLYQALIKGYTEKQWGRSAKELPAFIIKRIPVRFTFDNNYFSDRYQGIPVGGYTKLIEKMLEGVDVKLGIDFLKDKDSLASKAHRIIYTGPIDQYFDYRFGALEYRSLKFETERHEFPNFQGNAVINFTDANVPYTRIIEHKHFDYVETKHTVVTKEYPLEWKVGDEPYYPVNDNKNMELFKKYRELASREDKVIFGGRLAEYKYYDMHQVISAALYQVKNIMSTD
Protein: Ribonuclease R (RNase R) (EC 3.1.13.1) (Protein VacB) (P21499)
Organism: Escherichia coli (strain K12)
Function: 3'-5' exoribonuclease that releases 5'-nucleoside monophosphates and is involved in maturation of structured RNAs (rRNAs, tRNAs and SsrA/tmRNA). In stationary phase, involved in the post-transcriptional regulation of ompA mRNA stability. Shortens RNA processively to di- and trinucleotides. In vitro, exhibits helicase activity, which is independent of its RNase activity. RNases 2 and R (rnb and this entry) contribute to rRNA degradation during starvation, while RNase R and PNPase (this entry and pnp) are the major contributors to quality control of rRNA during steady state growth. Required for the expression of virulence genes in enteroinvasive strains of E.coli.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Ribonuclease E
- SsrA-binding protein
- Polyribonucleotide nucleotidyltransferase
- Ribonuclease D
- Endoribonuclease YbeY
- ATP-dependent RNA helicase RhlE
- Poly
- RNA pyrophosphohydrolase
- Ribonuclease 3
- Oligoribonuclease
Sequence:
MSQDPFQEREAEKYANPIPSREFILEHLTKREKPASRDELAVELHIEGEEQLEGLRRRLRAMERDGQLVFTRRQCYALPERLDLVKGTVIGHRDGYGFLRVEGRKDDLYLSSEQMKTCIHGDQVLAQPLGADRKGRREARIVRVLVPKTSQIVGRYFTEAGVGFVVPDDSRLSFDILIPPDQIMGARMGFVVVVELTQRPTRRTKAVGKIVEVLGDNMGTGMAVDIALRTHEIPYIWPQAVEQQVAGLKEEVPEEAKAGRVDLRDLPLVTIDGEDARDFDDAVYCEKKRGGGWRLWVAIADVSYYVRPSTPLDREARNRGTSVYFPSQVIPMLPEVLSNGLCSLNPQVDRLCMVCEMTVSSKGRLTGYKFYEAVMSSHARLTYTKVWHILQGDQDLREQYAPLVKHLEELHNLYKVLDKAREERGGISFESEEAKFIFNAERRIERIEQTQRNDAHKLIEECMILANISAARFVEKAKEPALFRIHDKPSTEAITSFRSVLAELGLELPGGNKPEPRDYAELLESVADRPDAEMLQTMLLRSMKQAIYDPENRGHFGLALQSYAHFTSPIRRYPDLTLHRAIKYLLAKEQGHQGNTTETGGYHYSMEEMLQLGQHCSMAERRADEATRDVADWLKCDFMLDQVGNVFKGVISSVTGFGFFVRLDDLFIDGLVHVSSLDNDYYRFDQVGQRLMGESSGQTYRLGDRVEVRVEAVNMDERKIDFSLISSERAPRNVGKTAREKAKKGDAGKKGGKRRQVGKKVNFEPDSAFRGEKKTKPKAAKKDARKAKKPSAKTQKIAAATKAKRAAKKKVAE
Protein: SEC14-like protein 3 (Tocopherol-associated protein 2) (Q9UDX4)
Organism: Homo sapiens (Human)
Function: Probable hydrophobic ligand-binding protein; may play a role in the transport of hydrophobic ligands like tocopherol, squalene and phospholipids.
Interaction partners:
Sequence:
MSGRVGDLSPKQAETLAKFRENVQDVLPALPNPDDYFLLRWLRARNFDLQKSEALLRKYMEFRKTMDIDHILDWQPPEVIQKYMPGGLCGYDRDGCPVWYDIIGPLDPKGLLFSVTKQDLLKTKMRDCERILHECDLQTERLGKKIETIVMIFDCEGLGLKHFWKPLVEVYQEFFGLLEENYPETLKFMLIVKATKLFPVGYNLMKPFLSEDTRRKIIVLGNNWKEGLLKLISPEELPAQFGGTLTDPDGNPKCLTKINYGGEIPKSMYVRDQVKTQYEHSVQINRGSSHQVEYEILFPGCVLRWQFSSDGADIGFGVFLKTKMGERQRAGEMTDVLPSQRYNAHMVPEDGNLTCSEAGVYVLRFDNTYSFVHAKKVSFTVEVLLPDEGMQKYDKELTPV
Protein: GTPase-interacting component 1 (P38785)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for cell size and shape control, bud site selection, bud emergence, actin cytoskeletal organization, mitotic spindle orientation/positioning, and mating projection formation in response to mating pheromone.
Subcellular location: Bud neck. Bud tip. Cytoplasm, cell cortex. Cytoplasm, cytoskeleton. Note=Concentrated at the incipient bud site of unbudded cells, at the bud tip and mother-bud neck of budded cells, and at cortical sites on large-budded cells that may delimit future bud sites in the two progeny cells.
Interaction partners:
- Cell division control protein 42
- Serine/threonine-protein kinase CLA4
- Mitotic check point protein BUB2
- Cell division control protein 12
- GTPase-interacting component 2
- Ras-related protein RSR1
- Protein ZDS2
- Serine/threonine-protein kinase STE20
- Cell division control protein 24
- Protein BNI1
Sequence:
MTEGKRLQQMELPQMKSIWIDEDQEMEKLYGFQVRQRFMNGPSTDSDEDADEDLGIVLVDSKKLALPNKNNIKLPPLPNYMTINPNINSNHKSLTNKKKNFLGMFKKKDLLSRRHGSAKTAKQSSISTPFDFHHISHANGKREDNPLESHEEKHDVESLVKFTSLAPQPRPDSNVSSKYSNVVMNDSSRIVSSSTIATTMDSHHDGNETNNTPNGNKQLDSPTDLEMTLEDLRNYTFPSVLGDSVSEKTNPSSPSVSSFSGKFKPRELSALHTPELGNCFNVDQSLNSPGNRISVDDVLKFYYQCSETSTPRNT
Protein: Eukaryotic translation initiation factor 4E nuclear import factor 1 (Eukaryotic translation initiation factor 4E transporter isoform X1) (E7FDR0)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- RNA helicase
- RNA helicase
- LSM14 homolog A
- C19orf13-like protein
- Eukaryotic translation initiation factor 4E-1B
- LSM family member 14B
- Eukaryotic translation initiation factor 4E-1A
- CCR4-NOT transcription complex subunit 1
- Transmembrane protein 185-like
- Eukaryotic translation initiation factor 4E family member 1c
Sequence:
MEKDENGENLVDPIKDSVMTSAYRYTKEELMEIKELPISNERPECLSEKYDSDGVWDPEKWHASLYPSSESSCPTEGYKKDYVDDRVPLKRRIADPRERVKDDDLEVVLSPQRRSFGGGCQVAQTALPRRPTSPLENKENESLRLGGARRIGSGRIMASRVFERDARVDKERERDRERDFKDKRFRRDFGDKRVFSERRRNDSYAEEEPEWFSGGPTSQSETIELIGFDDKILEDDKRRTKRSKKRPESVKEVECNGGLSDGPEVVRESGADQEVPHAELPEQTPGDFDFNEFFNLEKTMPGLASMIEDVLADGPVMASRFSRWFSSNRSPSGSRSSSLRSTPHEELERLAGLDPHTGSLNQGPSLYFTPISSAEHKEKVDILELLHKANIDLKPLLSSLNVNKAHLKESTSSGVVLSLEEVEVGLKGLKVQPEPAPSLPQRQSSGGGGTPFMAEHLEEALTGGAKTTARPRDSDMSAFNKLVNTMKASGTLPTLPKASGTNPQQQSVDPVLVSLTEAQVPAPQQKNIFQELLVTPHGPVPVPGLIHHRASPPLFPQRSQMQDFFPGMSPATGFHGGPQTVLDQIPDLHRARNTQPMRALPMGVDQTNLEALFQQDLAVLNRPQYQQAYNKQAHDKMFRNRPTRMNRSPVPHLPGRTSPGSTVTSVLSPSFTPTSVIKKMYESKEKSRDDLGSRPGSKEETVNSHNSQDDGPPSPSSFLEDVDTSGPQTGGVKACSTPVPTQNRHIKDPERPRPPSVTGPHTPTMLSPGPSSPFPRPQMYPVPLLPHVPLVRPPPQLHPGVMQRMLAQGIQAQQLGPTLLQTGMFPQAVDLSQLQGLPPALLGQPLYPLSPAGHPLMAPRAAGTHVQLAVMQQQLQQQQRPNLHVAPSGGPQSQSHGPHRTNQRRGASPPLGLAKWFGSDMLQQPLPSMPSTKVISVDELEFRQ
Protein: Hephaestus, isoform W (A0A0B4K6P4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MMSCPIPMPMPISSLHKSEFEPVNIGVKQMQLLHAPASTHPHPHPHQHPQHSAASAAAYQAMQVHQQQHQQQQQAAVFHHQVAAIAAQQQQQQQQAQVQHQQQMQQQFHYQAQAQAQAQAMLQTYMQLQVNSAVGVSTAPATPTKPVAAQIPGAISGPIAGPVPVSVPTQFFTAPSTPLTIIPAAAVASSAMFATAATPTSAATTPTNNVRIDEQYIYKLNYLRGSDELLSQAAVMAPASDNNNQDLATKKAKLEPGTVLAGGIAKASKVIHLRNIPNESGEADVIALGIPFGRVTNVLVLKGKNQAFIEMADEISATSMVSCYTVTPPQMRGRMVYVQFSNHRELKTDQGHNNSTAHSDYSVQSPASGSPLPLSAAANATSNNANSSSDSNSAMGILQNTSAVNAGGNTNAAGGPNTVLRVIVESLMYPVSLDILHQIFQRYGKVLKIVTFTKNNSFQALIQYPDANSAQHAKSLLDGQNIYNGCCTLRIDNSKLTALNVKYNNDKSRDFTNPALPPGEPGVDIMPTAGGLMNTNDLLLIAARQRPSLSVNGLGAPGVLPPFALGLGTPLTGGYNNALPNLAAFSLANSGALQTTAPAMRGYSNVLLVSNLNEEMVTPDALFTLFGVYGDVQRVKILYNKKDSALIQMAEPQQAYLAMSHLDKLRLWGKPIRVMASKHQAVQLPKEGQPDAGLTRDYSQNPLHRFKKPGSKNYQNIYPPSATLHLSNIPSSCSEDDIKEAFTSNSFEVKAFKFFPKDRKMALLQLLSVEEAVLALIKMHNHQLSESNHLRVSFSKSNI
Protein: Putative beta-actin-like protein 3 (Kappa-actin) (POTE ankyrin domain family member K) (Q9BYX7)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
Sequence:
MDDDTAVLVIDNGSGMCKAGFAGDDAPQAVFPSIVGRPRHQGMMEGMHQKESYVGKEAQSKRGMLTLKYPMEHGIITNWDDMEKIWHHTFYNELRVAPEEHPILLTEAPLNPKANREKMTQIMFETFNTPAMYVAIQAVLSLYTSGRTTGIVMDSGDGFTHTVPIYEGNALPHATLRLDLAGRELTDYLMKILTERGYRFTTTAEQEIVRDIKEKLCYVALDSEQEMAMAASSSSVEKSYELPDGQVITIGNERFRCPEALFQPCFLGMESCGIHKTTFNSIVKSDVDIRKDLYTNTVLSGGTTMYPGIAHRMQKEITALAPSIMKIKIIAPPKRKYSVWVGGSILASLSTFQQMWISKQEYDESGPSIVHRKCF
Protein: Probable polyketide synthase Pks7 (P94996)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Probable fatty acid synthase Fas
- Phenyloxazoline synthase MbtB
- Probable polyketide synthase Pks8
- Probable polyketide synthase Pks9
- Isonitrile lipopeptide synthase
- Probable polyketide synthase Pks17
- Malonyl CoA-acyl carrier protein transacylase
- Phthioceranic/hydroxyphthioceranic acid synthase
- Mycocerosic acid synthase-like polyketide synthase
- Phenolphthiocerol/phthiocerol polyketide synthase subunit C
Sequence:
MNSTPEDLVKALRRSLKQNERLKRENRDLLARTTEPVAVVGMGCRYPGGVDSPETLWELVAHGRDAVSEFPADRGWDVAGLFDPDPDAVGKSYTRCGGFLTDVAGFDAEFFGIAPSEALAMDPQQRLLLEVSWEALERAGIDPITLRGSQTGVFAGVFHGSYGGQGRVPGDLERYGLRGSTLSVASGRVAYVLGLQGPAVSVDTACSSSLVALHLAVQSLRLGECDLALVGGVTVMATPAMFIEFSRQRALSADGRCKAYAGAADGTAFAEGAGVLVLARLADARRLGHPVLALVRGSAVNQDGASNGLATPNGPAQQRVITAALASARLGVADVDVVEGHGTGTTLGDPIEAQAILATYGQRPADRPLWLGSIKSNIGHTSAAAGVAGVIKMVQAMRHGVLPKTLHVDVPTPHVDWSAGAVSLLTEPRPWHVPGRPRRAGVSSFGISGTNAHVILEEAPAVEPVGAAHGNDPVAVPWVLSARSAQALTNQARRLLAWVGADENVRPLDVGWSLVNTRSLFDHRAVVVGADRTQLMEGLTGLAAGVPGADVVAGRAQTVGKTAFVFPGQGAQWLGMGAQLCATAPVFAEHIHRCERALREHVEWSLLDVLRGAPGAPGLDRVDVVQPALWAVMVSLAELWRSVGVVPDAVIGHSQGEIAAAYVAGALSLRDAAAVVALRSRLLVRLGGAGGMVSLACGQPQAEKLASQWGDRLNIAAVNGVSSVVLAGETDAVTELMQRCEAEGIRARRIDVDYASHSAQVDAIREELIAALRGIEPRTSTVAFFSTVTGELMDTAGVNAEYWYRSIRQPVQFERAVRNAFDGGYRVFVESSPHPVLIAGIEETLVDCDRGATGEPIVIPTLGRDDGGVGRFWLSAGQAHVAGVGVDWRAAFADLGGRRVELPTYAFARQRFWLDGLGAVGGDLGGVGLVGAEHGLLAAVVQRPDSGGVVLTGRISVVAAPWLADHAVGPVVLFPGTGFVELALRAGDEVGCSVLQELTLQAPLVLPADGVRVQVVVGGVEQSGTRNVWVYSAAGQADSSPGWTLHAQGVLGVGSVQPAAELSVWPPVGARAMDVADGYQVLAARGYGYGPAFRGLQALWRRGAEVFADVTLPEGVPIRGFGIHPAVLDAALHAWGIVEGEQQTMLPFSWQGVCLHASGAARVRVRLAPVGRGAVSVELADPQGLPVLSVRQLMVRPVSAAALSRSTAGDRGLLEMIWTPVPLEGGDIGDDAVVWELPPHAGAQAGGDVLAAVYRGVHEVLEVLQSWLASDATGLGVVVTRGAVGPVDDDVTDLAGAAVWGLVRSAQAEHPGRVVLVDTDGSVAVEDAVGFGARSGEPQLVVRRGRVYAARLAPVAAGLTLPSASAGGWRLVAGGGGTLADVVVAPVAPVELATGQVRVAVGAVGVNFRDVLVALGMYPGGGELGVDGAGVVVEVGPGVTGLAVGDRVMGLLGLVGSEAVVDARLVTMVPAGWSLVEAAAVPVAFLTAFYGLSVLAEVAAGQKVLVHAGTGGVGMAAVSLARYWGAEVFVTASRAKWDTLRAMGFDDIHISDSRSLEFEEAFLRATEGSGVDVVLNSLAGEFTDASLRLLPSGGRFIELGKTDIRDGQTVAERHRGVRYRAFDLVEAGPDRIAAMLSEVVGLLAAGVLARLPVKTFDARCAPAAYRFVSQARHIGKVVLTIPDGPGGQSGLAGGTVVVTGGTGMAGSAVATHLVRRHGVANLVLVSRSGEQADRAAEVAALLREGGAQVAVVSCDVADRDALAALLAGLDPRYPLKGVFHAAGVLDDAVITGLTPDRVDTVLRAKVDGAWNLHELTEDMDLSAFVVFSSMAGIVGTPAQGNYAAANAFLDGLVAYRRSRGLAGLSVAWGLWEQASAMTRHLGERDRARMTQAGLAPLTTEQALGFLDTALQADRAVVVAARLDRAALAGAGAALPALFSQLAAGPTRRRIDAADTAVSMSGLVSRLHALTPERRQRELTDLVISNAAAVLGRSSSVDINAHKAFQDLGFDSLTAVELRNRLKTATGLTLSPTLIFDYPTPATLAEHLDSRLVTASGSDQQSLSDRVDDITRELVVLLDQPDLSANVKAHLRTRLQTMLTSLTTEDDDIAAATESQLFAILDEELGS
Protein: Phycocyanobilin lyase CpcT (EC 4.-.-.-) (Q8YLF9)
Organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)
Function: Catalyzes the site-selective attachment of phycocyanobilin (PCB) to 'Cys-154' of C-phycocyanin subunit beta (CpcB) and to 'Cys-153' of phycoerythrocyanin subunit beta (PecB). Does not have chromophore lyase activity for ApcA1, ApcA2, ApcB, ApcD, ApcF or PecA.
Interaction partners:
- Phycocyanobilin lyase CpcS 1
- Putative phycocyanobilin lyase CpcS 2
- Phycoerythrocyanin subunit beta
- Phycocyanobilin lyase subunit alpha
- Bilin biosynthesis protein PecE
- C-phycocyanin beta subunit
- Phycocyanobilin lyase subunit beta
- Allophycocyanin subunit beta
- Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod
- Phycoerythrocyanin alpha chain
Sequence:
MTHSTDIATLARWMAADFSNQAQAFENPPFYAHIRVCMRPLPWEVLSGVGFFVEQAYDYMLNDPYRLRVLKLMIVGDRIHIENYTVKQEENFYGASRDLNRLQTLTSESLEKLPGCNMIVEWTGNSFKGTVEPGKGCIVVRKGQKTYLDSEFEINEEKFISLDRGRDLETDAHIWGSVAGPFYFVRLHNFADEVKISAE
Protein: Dorsal interacting protein 3 (Q9NHV5)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00371}.
Interaction partners:
Sequence:
MSRKNGNQDTFPKTEKMQRYYAERETTGPEFDDRLIKLVRANPAIYDVSHPHYRRNPVRVDIWDRIANELGASSRFLQTKWKNIRYNYLQESGQANPNVRKRRFTEDLSFLQNTAQTYNVKKSQSYVAQQNGMGSDNDSNSFLYPDPEHLKIDASEGYDIIELDNSDDGSNSDDNEIVPELQLVMGESKHQLSLPTTLNGTSSXNHSHEHDQASSPASSPLLTPMVVMGNGYGQEVHLEQQQTQEQKPFKNSSLSNGEVTIEPIYKPAAIRRALPSDFLTNPFKRKATQAPLQTQVTSSFNDPIELYCLSLVDTLRSMRRSERERVKFEFANILKDAKYKDES