wanglab/gogpt-training-data huggingface dataset:
Protein: Toxin subunit YenB (B6A880)
Organism: Yersinia entomophaga
Function: Part of an orally active toxin complex (TC) with strong insecticidal effects on larvae of the Coleoptera Costelytra zealandica, Acrossidius tasmania and Adoryphorus couloni and some Lepidoptera larvae. The TC has an endochitinase activity (Probable).
Subcellular location: Secreted {ECO:0000269|PubMed:21278295}. Note=Secreted when grown at 25 degrees Celsius or less, but not when grown at 30 or 37 degrees Celsius. {ECO:0000269|PubMed:21278295}.
Interaction partners:
- Toxin subunit YenC2
- RHS2
- Toxin subunit YenC1
- Toxin subunit YenA2
- Toxin subunit YenA1
- Chitinase 1
Sequence:
MQNSQEMAITTLSLPKGGGAINGMGESVGQAGPDGMVTFSIPLPFSAGRGVAPALSLSYSSGAGNGPFGMGWQCSAMSISRRTQKGVPQYNEDDEFLSPSGEVMAIALNDSGFEDVRTANRLQGIPLPFSYKVTRYQPRLIQDFIKIEYWQPVKQTDGTPFWIIYSPDGQTHILGKNSHSRVANAENPSQIASWLLEETVTPTGEHIYYQYSGENQVNCTDAEIALHPQDSAQRYLARIDYGNISPQASLFVLDEELPNLTQWLFHLVFDYGERDISINKIPTFEGGTTGWLARPDMFSRYDFGIEIRNRRLCHQVLGFHRLEALNDRDVTDEIPVLVNRLTLDYDLNNSVSTLVAVRQVAYETDGSPITQPPLEFDYQRFDTGSIPGWQEMPQLEAFNGYQPYQMIDLYGEGTPGILYQETPGAWWYKSPQRQIGGDSNAVTYGAMKALPKIPRLQEGATLMDINGDGRLDWVITSAGVRGFHSIHSTGEWTHFTPLNTLPTEYFHPKAQLADLVGAGLSDLVLIGPKSVRLYANQQGNWAPAQDVTQAENVSLPVIGIDSRQLVAFADMLGSGQQHLVEITADSVKCWPNMGHGRFGQPLTLEGFSQPQTSFNPDRVFLADIDGSGTNDIIYAHSECLEIYLNESGNRFSKPISLLLPDGVNFDNTCQLQAADIQGLGIASLVMTVPHMSPTHWRCDLALNKPWLLNVMNNNRGAETCLFYRSSAQFWLDEKQLVEAAGQQPECHLPFPMHLHWRSEIFDEITGNRLTQEQEYAHGSWDGQEREFRGFGRLIQRDTDGFAQGTVDIPTHPSRTVSWFATGIPEIDTTLSAEFWRGDDQAFSPFSPRFTRWENDSEAGSDVAFIPSEHDAFWLNRAMKGQLLRSELYGDDGTPEAEIPYSVTEMRHQVRALPTTDATVPSAWCSTIETRSYQYQRVAADPQCSQQVVIKADRYGSPLLSVAINYPRRKKPEKSPYPDDLPETLFDSSYDTQQQQLHLTKQQQNYFHLTNDDNWLLGLPKEQRNDGYQYDQERAPANGFTLETLIASNSLIGSNQPFTYLGQSRVAYQGGVDEQPSLQALVAYGETAILDEKTLQAFVGVLDSKTRDELLFSAGYQLAPRLFRVESEPDVWVARQGYSEFGDYSQFWRPLSQRSTLLTGKTTLKWDKHYCVVIETQDAAQLVTQARYDYRFLTPYSLTDANDNQHYVVLNPFGEVIASRFWGTEAGKDAGYSTPQAKPFVVPATIEAALALSPGIPVAHCAIFEPESWMQKLTQHDVSERMADNGTLWNALLQARFVTEDGYVCALGRRRWMARHGLSVLMLTLLAEIPRTPPHSLTITTDRYDSDDQQQLRQRILFSDGFGRLLQSAQRVEAGESWQRSEDSSLVVNVSGTPALVVTDNRWAVSGRTEYDGKGQGIRVYQPYFLDDWRYLSDDSARTDLFADTHIYDPLGREYQVITAKGYRRERQYTPWFVVNQDENDTAANLAI
Protein: Cinnamoyl-CoA reductase 1 (AtCCR1) (EC 1.2.1.44) (Protein IRREGULAR XYLEM 4) (Q9S9N9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the latter stages of lignin biosynthesis. Catalyzes one of the last steps of monolignol biosynthesis, the conversion of cinnamoyl-CoAs into their corresponding cinnamaldehydes.
Interaction partners:
- Caffeoyl-CoA O-methyltransferase 1
- Trans-cinnamate 4-monooxygenase
- Shikimate O-hydroxycinnamoyltransferase
- Cytochrome P450 84A1
- 4-coumarate--CoA ligase 1
- Probable caffeoyl-CoA O-methyltransferase At4g26220
- Putative caffeoyl-CoA O-methyltransferase At1g67980
- Flavone 3'-O-methyltransferase 1
- 4-coumarate--CoA ligase 3
- 4-coumarate--CoA ligase-like 6
Sequence:
MPVDVASPAGKTVCVTGAGGYIASWIVKILLERGYTVKGTVRNPDDPKNTHLRELEGGKERLILCKADLQDYEALKAAIDGCDGVFHTASPVTDDPEQMVEPAVNGAKFVINAAAEAKVKRVVITSSIGAVYMDPNRDPEAVVDESCWSDLDFCKNTKNWYCYGKMVAEQAAWETAKEKGVDLVVLNPVLVLGPPLQPTINASLYHVLKYLTGSAKTYANLTQAYVDVRDVALAHVLVYEAPSASGRYLLAESARHRGEVVEILAKLFPEYPLPTKCKDEKNPRAKPYKFTNQKIKDLGLEFTSTKQSLYDTVKSLQEKGHLAPPPPPPSASQESVENGIKIGS
Protein: UPF0057 membrane protein At4g30650 (Q9M095)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Probable methyltransferase PMT7
- RING-H2 finger protein ATL32
- Guanylate-binding family protein
Sequence:
MASNMEVFCEILIAILLPPLGVCLKRGCCTVEFLICLVLTILGYIPGIIYALYVIVFQNREGSTELGAPLNSA
Protein: Stn1p (A0A1D8PI83)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Ten1p
Sequence:
MDRSNRLLYPRTKIDWGPGENHICLRTSTKNYYVIELFHQSPTLDKLIPLFINDINSSPNLFQIYYQIAENLTQIVLINNYPVNKVRIVGKIINEKYKSNDNYNTSTNTRTKSGSGQGINDVFLTIDDFVGSSSRIIVNLNQSKFRSQGCRLNMSNRGKIVEIEGIINNKYIYYNRYNNYNNYNNDNLLQREIDVEKFTVLSHNGNEFHIEMENWKKTLEFRNSNLLEPWVFIPSPQRNKDCQQQPLTYRFTEAELRKRNNRQNLVISSPSPINEIQPEELAFEDSLLVDAVRKSSDKTVVDSIDNDDWPQESGFEELKDDSAVVQQQQQQQQQQQQQQPNLPQIPRSSSTSRQATPLTSDTAINGTSSGLFNQLENISNKKDVTSKMDDDDNHDDDDDIIILAVNDNPVKVVTEFQVTLEIIKFIINKNFTKFKLVEIYRHNYISQLLTNLTTIQLSTLQQIPNFKNLTSFDEYKSIIFHRIRRVLQFDYELITVSQTQSVKSKNLQNLFYSLIQILHNLSDTEKQSNHELNVMDYIELLRQEKLIFGGINYKIINGIIDYILTMVLKQDRLWKYDTKNISWKYIG
Protein: Guanine nucleotide-binding protein G(Olf) subunit alpha (W5U7I9)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Interaction partners:
- adenylate cyclase
- Beta-2 adrenergic receptor
- Guanine nucleotide-binding protein G
- adenylate cyclase
- adenylate cyclase
- Adenylate cyclase type 2-like isoform X1
- adenylate cyclase
- Dopamine D1 receptor
- D
- 5-hydroxytryptamine receptor 6
Sequence:
MGCLGNSKTEDQRIDEKAQREANKKIEKQLQKERQAYKATHRLLLLGAGESGKSTIVKQMRILHVNGFNAEEKKQKILDIRKNVKDAVVTIVSAMSTLIPPVPLANPDNQFRADYIKSIAPLSDFDYTEEFFEHAKQLWDDEGVKACFERSNEYQLIDCAQYFLDRIDSVRQNDYTPTDQDLLRCRVLTSGIFETRFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVAASSSYNMVIREDNSTNRLRESLDLFRSIWNNRFLRTISVILFLNKQDMLAEKILAGKSKLEDYFPEYTRYTVPPDVTPDAGEDPKVTRAKFFIRDEFLRISTASGSDKHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQYELL
Protein: Kinesin, putative (Q38CW6)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MADMKKVTVAVRVRPILRDGISQAHVQEKFELEAIRRTGDTTLKVELERPGEPTRGSAFTFDHIFDQESTQLDVYDEAVADLVDMSLTGANSTILAYGQTGSGKTFTVLGDVKPNPLEDDLLTKDSGMFLRVLSDLMEYKRRQLARGFHVVVGLSCVEIYNENIRDLFGGTPNSPPPSIKAVMIGEEVLLPSLIIKEMTSLQAVFSEIQLAISRRKSRSTEANAVSSRSHCLFLIDILQQSTTAPAPSLTAILQTKKGTKDVEAKRISTLSGISNKNGAPIELKPGELPFDGMVYRLQGQKEPIYGSKILLADLAGSEKISRSGVTGEGLAEATAINSSLTALGNVVHSLHEGGYVSYRTSNLTRLLKPTFSHPNSRVLLLSQVSPTQMTFDETISTLHFANKVKAMKVTTSTGMEADKIQFEYVEAGRTYDGLLADLRLFAVEQQTKVGVIRRRCRQNDGLFYAPLPSGRAGTRERRQAFIESIGANKAATEEREAGKVAREREAAAWEEELRRKRKDGAESAAATHAQLLREAKEGLAAEEKAVKHQAMQEVQHAQAAGAAKLQAEEEASRALLLGRFAQVMSDFCRARLQEAARVEEEISRELNSTRMASSSGGNGSGAASEVPVEDLEYAVSCWGHSIAKKFYTNCAELRELQLQMCMIGRSCLTMERWKAEHVGTA
Protein: Protein yippee (Q9XZF0)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- WD repeat-containing protein 26 homolog
- Ran-binding proteins 9/10 homolog
- GH10162p
Sequence:
MGRIFLEHLGGLKLFNCAQCHTNLTNRSQLISTRFTGATGRAYLFKRVVNLTFSNIQERVMLTGRHMVRDVMCKNCGAKLGWMYEFATEESQKYKEGRVILEYALITEAEGFPSEAATTSH
Protein: Voltage-gated potassium channel subunit beta-1 (EC 1.1.1.-) (K(+) channel subunit beta-1) (Kv-beta-1) (P63144)
Organism: Rattus norvegicus (Rat)
Function: Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits. Modulates action potentials via its effect on the pore-forming alpha subunits (Probable). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (By similarity). Mediates closure of delayed rectifier potassium channels by physically obstructing the pore via its N-terminal domain and increases the speed of channel closure for other family members. Promotes the closure of KCNA1, KCNA2 and KCNA5 channels. Accelerates KCNA4 channel closure. Accelerates the closure of heteromeric channels formed by KCNA1 and KCNA4. Accelerates the closure of heteromeric channels formed by KCNA2, KCNA5 and KCNA6. Enhances KCNB1 and KCNB2 channel activity (By similarity). Binds NADPH; this is required for efficient down-regulation of potassium channel activity. Has NADPH-dependent aldoketoreductase activity. Oxidation of the bound NADPH strongly decreases N-type inactivation of potassium channel activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q14722}. Membrane {ECO:0000269|PubMed:15618540}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane {ECO:0000269|PubMed:16504945}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Recruited to the cytoplasmic side of the cell membrane via its interaction with pore-forming potassium channel alpha subunits. {ECO:0000250|UniProtKB:Q14722}.
Interaction partners:
- Potassium voltage-gated channel subfamily A member 1
- Potassium voltage-gated channel subfamily A member 5
- Potassium voltage-gated channel subfamily A member 4
- Potassium voltage-gated channel subfamily A member 2
- Potassium voltage-gated channel subfamily A member 6
- Voltage-gated potassium channel KCNC1
- Potassium voltage-gated channel subfamily B member 1
- A-type voltage-gated potassium channel KCND3
- Potassium voltage-gated channel subfamily A member 3
- A-type voltage-gated potassium channel KCND1
Sequence:
MQVSIACTEHNLKSRNGEDRLLSKQSSTAPNVVNAARAKFRTVAIIARSLGTFTPQHHISLKESTAKQTGMKYRNLGKSGLRVSCLGLGTWVTFGGQISDEVAERLMTIAYESGVNLFDTAEVYAAGKAEVILGSIIKKKGWRRSSLVITTKLYWGGKAETERGLSRKHIIEGLKGSLQRLQLEYVDVVFANRPDSNTPMEEIVRAMTHVINQGMAMYWGTSRWSAMEIMEAYSVARQFNMIPPVCEQAEYHLFQREKVEVQLPELYHKIGVGAMTWSPLACGIISGKYGNGVPESSRASLKCYQWLKERIVSEEGRKQQNKLKDLSPIAERLGCTLPQLAVAWCLRNEGVSSVLLGSSTPEQLIENLGAIQVLPKMTSHVVNEIDNILRNKPYSKKDYRS
Protein: Chaperone protein DNAJ, putative (Q387E9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRRFVSQQDGKATALWTNLPHARVSSAFFSSLTHESRVVQSVTCVRRVLAPPTPSIYPAFRNTFKSTKRWQGSTTSAGGDYYKLLGVKPDASQDEIKAAYKKLALEFHPDRNHDPGAEEMFKNISEAYNIIGNKTRRKEYDMQRRAETSNAGSARSSYHPGGAAYHSPPGYQHISKEEADKIFRDLFGGMRVDQIFRDFEEMQRGTRSGGRSGFPQEFGAADCSFRPSFRSESTRVYTDGLGNRMEERTFTDSHGNTYTVHTTTSEQPNASMNQRAEDYYSGHASNSGGGRFRMGNSSFRVTPRDAANDFGANYFGIRTHGRHPAVAMMILVAWSIVLGTLLFATLAFFVSHPFFTFAVLFLILLKRMRLF
Protein: Amphiphysin (O08838)
Organism: Rattus norvegicus (Rat)
Function: May participate in mechanisms of regulated exocytosis in synapses and certain endocrine cell types. May control the properties of the membrane associated cytoskeleton (By similarity).
Subcellular location: Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Dynamin-1
- Synaptojanin-1
- Myc box-dependent-interacting protein 1
- Dynamin-2
- Clathrin heavy chain 1
- Synaptojanin-2
- Epsin-1
- AP-2 complex subunit beta
- Intersectin-1
- Actin nucleation-promoting factor WAS
Sequence:
MADIKTGIFAKNVQKRLNRAQEKVLQKLGKADETKDEQFEEYVQNFKRQEAEGTRLQRELRGYLAAIKGMQEASMKLTESLHEVYEPDWYGREDVKMVGEKCDVLWEDFHQKLVDGSLLTLDTYLGQFPDIKNRIAKRSRKLVDYDSARHHLEALQSSKRKDESRISKAEEEFQKAQKVFEEFNVDLQEELPSLWSRRVGFYVNTFKNVSSLEAKFHKEIAVLCHKLYEVMTKLGDQHADKAFSIQGAPSDSGPLRIAKTPSPPEEASPLPSPTASPNHTLAPASPAPVRPRSPSQTRKGPPVPPLPKVTPTKELQQENIINFFEDNFVPEINVTTPSQNEVLEVKKEETLLDLDFDPFKPDVTPAGSAAATHSPMSQTLPWDLWTTSTDLVQPASGGSFNDFTQPQDTSLFTMQTDQNMAETEQALPTEPQAEEPPTTAAAPTAGLDLGLEMEEPKEEAAIPPGTDAGETVGTEGSTGEEAEAEKAALPAGEGESPEGAKIDVESTELASSESPQAAELEAGAPQEKVIPSVVIEPASNHEGEEHQETTTGTETREATEDVAPQGPAGEKQELATEPTPLDSQAATPAPAGAVDASLSAGDAAQELPPGFLYKVETLHDFEAANSDELTLQRGDVVLVVPSDSEADQDAGWLVGVKESDWLQYRDLATYKGLFPENFTRHLE
Protein: Alkane 1-monooxygenase 1 (EC 1.14.15.3) (Alkane hydroxylase) (AHs) (Terminal alkane hydroxylase) (Q0VKZ3)
Organism: Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2)
Function: Catalyzes the hydroxylation of n-alkanes and fatty acids in the presence of a NADH-rubredoxin reductase and rubredoxin. It preferably hydroxylases C5-C12 hydrocarbons.
Subcellular location: Cell inner membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Aldehyde dehydrogenase
- Alkane 1-monooxygenase 2
- Rubredoxin-2
- S-
- Aldehyde dehydrogenase family protein
- HTH-type transcriptional regulator AlkS
Sequence:
MSENILTEPPRSDADNEGYVDRKRHLWILSVLWPATPIIGLYLVSQTGWSIWYGLVLILWYGLVPLIDTMLGEDYSNPPESVVPKLEQDRYYKVLTYLTVPIHYAALIISAWWVSTQPIGVFEFLALALSLGIVNGLALNTGHELGHKKETFDRWMAKLVLAVVGYGHFFIEHNKGHHRDVATPMDPATSRMGESIYTFSLREIPGAFKRAWGLEEQRLSRCGKSVWSLDNEVLQPMILTVVLYAALLAFFGPLMLIFLPIQMAFGWWQLTSANYIEHYGLLREKLPNGRYEHQKPHHSWNSNHVMSNLILFHLQRHSDHHAHPTRSYQSLRDFSDLPTLPTGYPGMFFVAFFPSWFRSLMDDRVMEWAHGDINKIQIQPGMREFYEQKFGVKGSESPDTTVAK
Protein: Pimeloyl-[acyl-carrier protein] methyl ester esterase (EC 3.1.1.85) (Biotin synthesis protein BioH) (Carboxylesterase BioH) (P13001)
Organism: Escherichia coli (strain K12)
Function: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strategy to allow elongation of a temporarily disguised malonate moiety to a pimelate moiety by the fatty acid synthetic enzymes. BioH shows a preference for short chain fatty acid esters (acyl chain length of up to 6 carbons) and short chain p-nitrophenyl esters. Also displays a weak thioesterase activity. Can form a complex with CoA, and may be involved in the condensation of CoA and pimelic acid into pimeloyl-CoA, a precursor in biotin biosynthesis.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Malonyl-[acyl-carrier protein] O-methyltransferase
- 8-amino-7-oxononanoate synthase
- Acyl carrier protein
- ATP-dependent dethiobiotin synthetase BioD 1
- Adenosylmethionine-8-amino-7-oxononanoate aminotransferase
- Enoyl-[acyl-carrier-protein] reductase FabI
- Bifunctional ligase/repressor BirA
- Esterase YjfP
- DNA utilization protein YhgH
- ATP-dependent dethiobiotin synthetase BioD 2
Sequence:
MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPAEFCHLLVALKQRV
Protein: Cystathionine beta-synthase (EC 4.2.1.22) (Q6FVB8)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- cystathionine gamma-lyase
- Tryptophan synthase
- Adenosylhomocysteinase
- cystathionine gamma-synthase
- Candida glabrata strain CBS138 chromosome H complete sequence
- Cystathionine beta-lyase
- Homocysteine/cysteine synthase
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- Serine hydroxymethyltransferase, cytosolic
- phosphoserine phosphatase
Sequence:
MDSRHNVIDLVGNTPLIELKKLPKAYGIRPRVFAKLELYNPGGSIKDRIAKSMIEYAEEQGIIHPSRSTLIEPTSGNTGIGLALIGAVKGYRTIITLPEKMSNEKVSVLKALGAEIIRTPTEAAWDSPESHIGVARRLEKEIPGAIILDQYNNMKNPEAHYFGTGREIQKQLEDLKLFSHLNAVVAGAGTGGTISGISKYLKEQNPEIKIVGADPVGSILAQPENLNETEITSYKVEGIGYDFIPEVLDRSLVDVWYKTDDKPAFKYARQLISNEGVLIGGSSGSAFTALVEYCNDHPELSEDDVLVAIFPDSIRSYLTKFVDDEWLKTNDLWDDEILKRVDFDEKKKPATDDVFKGATVKDLHLKPVVAVKDNALVSDVISILRDNAFDQLPVLTQDGKLTGLVTLSQLLKKLSTGKVNNTDTIKNLYLDFRKLNNFDEVSSYNENKSGKKKFVQFTSESTLAELNKFFEKNSSAVITDGLKPVHIVTKMDLLSYLASTA
Protein: Uncharacterized protein YkgH (P77180)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Uncharacterized protein YfdF
- Uncharacterized protein YjgL
Sequence:
MREQIKQDIDLIEILFYLKKKIRVILFIMAICMAMVLLFLYINKDNIKVIYSLKINQTTPGILVSCDSNNNFACQTTMTEDVIQRITTFFHTSPDVKNREIRLEWSGDKRALPTAEEEISRVQASIIKWYASEYHNGRQVLDEIQTPSAINSELYTKMIYLTRNWSLYPNGDGCVTISSPEIKNKYPAAICLALGFFLSIVISVMFCLVKKMVDEYQQNSGQ
Protein: Zinc finger protein 804A (F1M078)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- 3',5'-cyclic-AMP phosphodiesterase 4B
Sequence:
MECYYIVISSTHLSNGHFRNIKGVFRGPLSKNGNKTLDYAEKENTIAKALEDLKANFYCELCDKQYYKHQEFDNHINSYDHAHKQRLKELKQREFARNVASKSRKDERKQEKALQRLHKLAELRKETVCAPGSGPMFKSTTVTVKENLNDVSRRESVDPVDNQQDVVHSDEKGRGGSTASAETETASNCTANNCQTGDQIQAIHRHRIGFSFAFPKKASVKLESSSAAAFSEYSDESSVEKEFSRKTRFVPSTCHLQLSSPTCELLSSEDKANSSPPEVMCLDKAAAQTEEMKITSTENNTVLTTSFCQLQLPACSDEDTCQNSAPFEDQASMETVIVNEDRPVNKSNPDIIEKNPTAPNDCTSAQMSTEENITINDVAKMETRNKIGHEPLTPTSTAEESIRFQKRPDLCKRQCDPFVPVLNKLGSTVLQWPSEMLAYTTTEPSISYSCNPLCFDFRSTKLNNNQEKSKLTLNDPFSQQKEDCCKRADCSEVPTGRVTSDESGSSKNDSPQVTTYSAAHVVSNGCDLGQNENVAQRYKHMSCTNRKTYKYNFTRSQIKRNTLNEKYNKIRLKETHEHWFHKSRRKKKRRKLCRYHRGKSAKEPEGSCKTETDRQRADETRKNPLEPVLERQSGSPERLSDLHQLADERPKTAPTHLVENENTDTTRNTESNDNALDSQNHGGENAIVVNEQANQAMIHSGKQNLTYVRTYCCWKARTPRCQEDDRCFVSQSDVKDPTQNQPVKRGYSSLTNDTERIHRKRRQHSCSYSSDENSNQQSHLGEEYLRPSNASLTSSQPKKKRRRKRSRLHIGDRTSKIKDNSNYSTMCRSSLSHPDGFAKEDIKEDTKPQENRSIKKSSEHTEQTEDKVIFHPPNPFPSEASGKDEHSVTETTPCVSSQASSDLATPVSVTGDPPNGTTDNTLLEHSQRSQTTHRNEKQIPLKVPNTERNFRHPPAKSYICRYELAETIPQGKTTESSTEWLCYNSGILNTQPPLQFKEAQVSGHAFVTTEEILAPLPLPEQALLIPLENHDKLKHLPCEVYQHIIQPTMLTNKVKFTFPPAPLPPPSTPVQPLPLQRPFCSTSVTTIHHTVLQHHAAAAAAAAAAAAAGTFKVLQPHQQFLPQVPPLARTSIPQISVGTVGPRLCPGRQPALVASPQMPIIPASVLHPSHLTFPPLPHAIFPSLLSPHPTVIPLQPLF
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q84XC0)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Interaction partners:
Sequence:
MAVVAAPKKNNSFNKKDNPNLLLGRFELGKLLGHGTFAKVHLAKNIKTGEAVAIKIISKDKILKSGLVSHIKREISILRRVRHPNIVQLFEVMATKTKIYFVMEYVRGGELFNKVAKGRLKEEVARKYFQQLICAVEFCHARGVFHRDIKPENLLLDENGNLKVSDFGLSAVSDEIKQDGLFHTFCGTPAYVAPEVLSRKGYDGGKVDIWSCGVVLFVLMAGYLPFHDPNNVMVMYKKIYKGDFRCPRWFSPELVNLLTRLLDTKPQTRISIPEIMENRWFKIGFKRIKFYVEDDVVCNLDSLGLDGNNGNDGNDDKKVLNIDEHRDEALESVSESEWDSEVVNRRKNRQLGSLPRPASLNAFDIISFSQGFDLSGLFEEKGDEARFVSGASVSKIMTKLEEVAQLVSFKVRKKDCRVSFEGSREGVKGPLSIAAEVFELTPSLVVVEVKKKGGDKVEYDRFLNTELKSALHSLTMEESAGSSCQNTPDETLQQRAFSDSAIDKHSDSIESLNLDT
Protein: Glycerol uptake protein, putative (Q387S3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Acyl carrier protein
Sequence:
MSDDEHKRHPHAQRSRHSTASPGMIGHDGNFMESFKDMLGDIYAPLKTGLKLEHVIYNACYMLLMLYGFFDVADASKQWASEFYIEPPRWSILTITSLGSTGYNGTGDAQWTSIDRGFGLLLSALALFVIGARGVRSVFHGENGVKALQRYYLFAGFLFTAFLHGPMFWLPITIIALNYVFIIILLKIKMPHWVHMAVMWTAVVSLMLSVGYYGGRLIIGPRRLGFWGGMASWVPTFNMSILRMISFNTDLYEAIHASAPARATTTRKHDNGCLDCARLRDKHPEKEVTAVRCYKFRSEYPRNVNEYNLLSYMAYMLYPPLYIGGPMSSFNAFASHCQYSTVAMTRSQLIVYGIFIIILYVTQVSMLHFVYLSALRQRGDLVMKLSTTQAAFMLYYSLAFLWLKFSLVWKTGRLAAVADGVDVPEDMRRAYSNTLSVRDFWRDWHASFNVWVVRYMYIPMGGNRRKYFSILPIFFFIAVWHDLELHLIEWAVWIIAFFLVELFVGYLWGLPLFAPVRHSKYERLLRSLAGMVSVFGLTITNMIGFATVAAPHGGSLTAQIILHILGTLNLTLFFFFLLFFFLLSATGVLLRDEEANQIKQLKERYGIVR
Protein: Neurotrimin (E7FH58)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- N-terminal Xaa-Pro-Lys N-methyltransferase 2
- Leucine-rich repeat and transmembrane domain-containing protein 1 precursor
- MICOS complex subunit
Sequence:
MKNPVLWVVLIGISIALIQQGLPVRSQGESQSDNKQMDNITIRQGETLFLSCSQGDFVTHTAWLNRSSILYAGEDKWSVDPRVSLVTLSQEEFTIKIEDVDVTDEGQYICAVQTSSRPRTTSVHIIVQVPPKIVNLSRDLVVNEGSNVTLMCLANGKPEPAIVWRMKSPSDDSLSSDSEVLDIPFISRYRAGVYECTAANDIAVDTQTVELTVNYAPSVSDGRDVGVTLGQRGVLQCEADAVPEADFEWYRDDRRIFNGLDGIEIEAAGALSRLTFFNVSEADYGNYTCVAINKLGSANTSFVLYEIIEPTSSTLLQVETSPSVLEMTSSDLEQTPLQNDLWEGPGAVQDGNSGTSTVFNPFCLLIAILQLLLKF
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (X2JKQ8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MPAALHSCEPERANTLEREMRDPTSICNVDCLLDTVSALVSDCDHESLRRLKNIEQYAAKYKPLAMQINQLRMNVEDFHFIKLIGAGAFGEVQLVRHKSSSQVYAMKRLSKFEMMKRPDSAFFWEERHIMAHANSEWIVQLHFAFQDAKYLYMVMDFMPGGDIVSLMGDYDIPEKWAIFYTMEVVLALDTIHNMGFVHRDVKPDNMLLDSYGHLKLADFGTCMRMGANGQVVSSNAVGTPDYISPEVLQSQGVDNEYGRECDWWSVGIFLYEMLFGETPFYADSLVGTYGKIMDHKNSLSFPPEVEISEQAKALIRAFLTDRTQRLGRYGIEDIKAHPFFRNDTWSFDNIRESVPPVVPELSSDDDTRNFEDIERDEKPEEVFPVPKGFDGNHLPFIGFTYTGDYQLLSSDTVDAESKEANVANSGAASNNHGHGHNHRHRPSNSNELKRLEALLERERGRSEALEQQDAGLRQQIELITKREAELQRIASEYEKDLALRQHNYKVAMQKVEQEIELRKKTEALLVETQRNLENEQKTRARDLNINDKVVSLEKQLLEMEQSYKTETENTQKLKKHNAELDFTVKSQEEKVRDMVDMIDTLQKHKEELGQENAELQALVVQEKNLRSQLKEMHKEAENKMQTLINDIERTMCREQKAQEDNRALLEKISDLEKAHAGLDFELKAAQGRYQQEVKAHQETEKSRLVSREEANLQEVKALQSKLNEEKSARIKADQHSQEKERQLSMLSVDYRQIQLRLQKLEGECRQESEKVAALQSQLDQEHSKRNALLSELSLHSSEVAHLRSRENQLQKELSTQREAKRRFEEDLTQLKSTHHEALANNRELQAQLEAEQCFSRLYKTQANENREESAERLSKIEDLEEERVSLKHQVQVAVARADSEALARSIAEETVADLEKEKTIKELELKDFVMKHRNEINAKEAALATLKEAENELHKKLGQKAAEYEDLVQQHKKQQEELALMRSSKDEEITKLLDKCKNEVLLKQVAVNKLAEVMNRRDSDLPKQKNKARSTAELRKKEKEMRRLQQELSQERDKFNQLLLKHQDLQQLCAEEQQLKQKMVMEIDCKATEIENLQSKLNETASLSSADNDPEDSQHSSLLSLTQDSVFEGWLSVPNKQNRRRGHGWKRQYVIVSSRKIIFYNSDIDKHNTTDAVLILDLSKVYHVRSVTQGDVIRADAKEIPRIFQLLYAGEGASHRPDEQSQLDVSVLHGNCNEERPGTIVHKGHEFVHITYHMPTACEVCPKPLWHMFKPPAAYECKRCRNKIHKEHVDKHDPLAPCKLNHDPRSARDMLLLAATPEDQSLWVARLLKRIQKSGYKAASYNNNSTDGSKISPSQSTRSSYKPYAVNVQRSATLPANSSLK
Protein: Ribosome maturation protein SBDS (Q7ZW65)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKKGGKRFEIACYKNKVMSWRSGAEKDLDEVLQTNTVFVNVSKGQVAKKEDLSNAFGTDDLTEICKQILSKGELQVSDKERQSQLEQMFRDIATIVAEKCVNPETKRPYTVNLIERAMKDIHFSVKANKSTKQQALEVIKQLKESIQIQRAHMRLRFVLPAKDGKRLKEKLKPLIKAVENEDFDDQLEMVCLIDPGCFRDIDELIRCETKGKGTLEVLSLKDVEEGDEKLE
Protein: Receptor tyrosine kinase-like orphan receptor 2 (A0A8I5ZRJ7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
Sequence:
KCTRRRALCVPRLGLHRFFPSEVEDSEAIDTLGQLDGPDSPLPTLKGYFLNFLEPVNNITIVQGQTAILHCKVAGNPPPNVRWLKNDAPVVQEPRRVIIRKTEYGSRLRIQDLDTTDTGYYQCVATNGLKTITATGVLYVRLGPTHSPNHNFQDDDQEDGFCQPYRGIACARFIGNRTIYVDSLQMQGEIENRITAAFTMIGTSTHLSDQCSQFAIPSFCHFVFPLCDARSRAPKPRELCRDECEVLENDLCRQEYTIARSNPLILMRLQLPKCEALPMPESPDAANCMRIGIPAERLGRYHQCYNGSGTDYRGMASTTKSGHQCQPWALQHPHSHRLSSTEFPELGGGHAYCRNPGGQMEGPWCFTQNKNVRVELCDVPPCSPRDGSKMGILYILVPSIAIPLVIACLFFLVCMCRNKQKASASTPQRRQLMASPSQDMEMPLISQHKQAKLKEISLSTVRFMEELGEDRFGKVYKGHLFGPAPGEPTQVVAIKTLKDKAEGPLREEFRQEAMLRARLQHPNIVCLLGVVTKDQPLSMVFSYCCHGDLHEFLVMRSPHSDVGSTDDDRTVKSALEPPDFVHVVAQIAAGMEFLSSHHVVHKDLATRNVLVYDKLNVRISDLGLFREVYSADYYKLMGNSLLPIRWMSPEAVMYGKFSIDSDIWSYGVVLWEVFSYGLQPYCGYSNQDVVEMIRSRQVLPCPDDCPAWVYALMIECWNEFPSGRPRFKDIHGRLRSWGNLSNYNSSAQTSGASNTTQTSSLSTSPVSNVSNARYMAPKQKAQPFPQPQFIPMKGQIRPLVPPAQLYIPVNGYQPVPAYGAYLPNFYPVQIPMQMAPQQVPPQMVPKPSSHHSGSGSTSTGYVTTAPSNTSVADRAALLSEGTEDVQNMPEDVAQSPVQEAEEEEEGSVPETELLGDSDTLQVNEAHVHLEA
Protein: 1-acylglycerol-3-phosphate O-acyltransferase ABHD5 (EC 2.3.1.51) (Abhydrolase domain-containing protein 5) (Lipid droplet-binding protein CGI-58) (Protein CGI-58) (Q6QA69)
Organism: Rattus norvegicus (Rat)
Function: Coenzyme A-dependent lysophosphatidic acid acyltransferase that catalyzes the transfert of an acyl group on a lysophosphatidic acid. Functions preferentially with 1-oleoyl-lysophosphatidic acid followed by 1-palmitoyl-lysophosphatidic acid, 1-stearoyl-lysophosphatidic acid and 1-arachidonoyl-lysophosphatidic acid as lipid acceptor. Functions preferentially with arachidonoyl-CoA followed by oleoyl-CoA as acyl group donors (By similarity). Functions in phosphatidic acid biosynthesis (By similarity). May regulate the cellular storage of triacylglycerol through activation of the phospholipase PNPLA2 (By similarity). Involved in keratinocyte differentiation (By similarity). Regulates lipid droplet fusion (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15136565}. Lipid droplet {ECO:0000269|PubMed:15136565}. Note=Colocalized with PLIN and ADRP on the surface of lipid droplets. The localization is dependent upon the metabolic status of the adipocytes and the activity of PKA.
Interaction partners:
- Patatin-like phospholipase domain-containing protein 2
- Perilipin-1
- TIR domain-containing adapter molecule 1
- Perilipin
- Perilipin-5
- Hormone-sensitive lipase
- Omega-hydroxyceramide transacylase
- Acylglycerol transacylase
- Patatin-like phospholipase domain-containing protein 5
- Monoglyceride lipase
Sequence:
MKAMAAEEEVDSADAGGGSGWLTGWLPTWCPTSTSHLKEAEEKMLKCVPCTYKKEPVRISNGNSIWTLMFSHNMSSKTPLVLLHGFGGGLGLWALNFEDLSTDRPVYAFDLLGFGRSSRPRFDSDAEEVENQFVESIEEWRCALRLDKMILLGHNLGGFLAAAYSLKYPSRVSHLILVEPWGFPERPDLADQERPIPVWIRALGAALTPFNPLAGLRIAGPFGLSLVQRLRPDFKRKYSSMFEDDTVTEYIYHCNVQTPSGETAFKNMTIPYGWAKRPMLQRIGGLHPDIPVSVIFGARSCIDGNSGTSIQSLRPKSYVKTIAILGAGHYVYADQPEEFNQKVKEICHTVD