wanglab/gogpt-training-data huggingface dataset:
Protein: Shutoff protein (100 kDa protein) (p100K) (100K-chaperone protein) (L4-100K) (Shutoff protein 100K) (P24932)
Organism: Human adenovirus C serotype 2 (HAdV-2) (Human adenovirus 2)
Function: Protein that inhibits host translation while promoting late viral translation by ribosome shunting. Blocks host cap-dependent translation by binding to eIF4G, displacing MKNK1 from cap initiation complexes and preventing EIF4E phosphorylation. Binds to the tripartite leader sequence of viral late mRNAs and recruits host eIF4G, PABPC1/poly-A binding protein and 40S ribosomes subunits on viral mRNAs, allowing ribosome shunting and efficient translation of late viral mRNAs even though conventional translation via ribosome scanning from the cap has been shut off in the host cell. During assembly, acts as a chaperone protein that helps hexon proteins assembly into trimers (Probable).
Subcellular location: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04060, ECO:0000269|PubMed:14633984}.
Interaction partners:
Sequence:
MESVEKEDSLTAPFEFATTASTDAANAPTTFPVEAPPLEEEEVIIEQDPGFVSEDDEDRSVPTEDKKQDQDDAEANEEQVGRGDQRHGDYLDVGDDVLLKHLQRQCAIICDALQERSDVPLAIADVSLAYERHLFSPRVPPKRQENGTCEPNPRLNFYPVFAVPEVLATYHIFFQNCKIPLSCRANRSRADKQLALRQGAVIPDIASLDEVPKIFEGLGRDEKRAANALQQENSENESHCGVLVELEGDNARLAVLKRSIEVTHFAYPALNLPPKVMSTVMSELIVRRARPLERDANLQEQTEEGLPAVGDEQLARWLETREPADLEERRKLMMAAVLVTVELECMQRFFADPEMQRKLEETLHYTFRQGYVRQACKISNVELCNLVSYLGILHENRLGQNVLHSTLKGEARRDYVRDCVYLFLCYTWQTAMGVWQQCLEERNLKELQKLLKQNLKDLWTAFNERSVAAHLADIIFPERLLKTLQQGLPDFTSQSMLQNFRNFILERSGILPATCCALPSDFVPIKYRECPPPLWGHCYLLQLANYLAYHSDIMEDVSGDGLLECHCRCNLCTPHRSLVCNSQLLSESQIIGTFELQGPSPDEKSAAPGLKLTPGLWTSAYLRKFVPEDYHAHEIRFYEDQSRPPNAELTACVITQGHILGQLQAINKARQEFLLRKGRGVYLDPQSGEELNPIPPPPQPYQQPRALASQDGTQKEAAAAAAATHGRGGILGQSGRGGFGRGGGDDGRLGQPRRSFRGRRGVRRNTVTLGRIPLAGAPEIGNRSQHRYNLRSSGAAGTACSPTQP
Protein: Long-chain-fatty-acid--CoA ligase ACSBG2 (EC 6.2.1.15) (EC 6.2.1.3) (Acyl-CoA synthetase bubblegum family member 2) (Arachidonate--CoA ligase ACSBG2) (A0A140VJD4)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MTGTPKTQEGAKDLEVDMNKTEVTPRLWTTCRDGEVLLRLSKHGPGHETPMTIPEFFRESVNRFGTYPALASKNGKKWEILNFNQYYEACRKAAKSLIKLGLERFHGVGILGFNSAEWFITAVGAILAGGLCVGIYATNSAEVCQYVITHAKVNILLVENDQQLQKILSIPQSSLEPLKAIIQYRLPMKKNNNLYSWDDFMELGRSIPDTQLEQVIESQKANQCAVLIYTSGTTGIPKGVMLSHDNITWIAGAVTKDFKLTDKHETVVSYLPLSHIAAQMMDIWVPIKIGALTYFAQADALKGTLVSTLKEVKPTVFIGVPQIWEKIHEMVKKNSAKSMGLKKKAFVWARNIGFKVNSKKMLGKYNTPVSYRMAKTLVFSKVKTSLGLDHCHSFISGTAPLNQETAEFFLSLDIPIGELYGLSESSGPHTISNQNNYRLLSCGKILTGCKNMLFQQNKDGIGEICLWGRHIFMGYLESETETTEAIDDEGWLHSGDLGQLDGLGFLYVTGHIKEILITAGGENVPPIPVETLVKKKIPIISNAMLVGDKLKFLSMLLTLKCEMNQMSGEPLDKLNFEAINFCRGLGSQASTVTEIVKQQDPLVYKAIQQGINAVNQEAMNNAQRIEKWVILEKDFSIYGGELGPMMKLKRHFVAQKYKKQIDHMYH
Protein: Serine/threonine-protein kinase 31 (EC 2.7.11.1) (Q99MW1)
Organism: Mus musculus (Mouse)
Interaction partners:
- RING finger protein 17
Sequence:
MWGQRLFAGTAVAQSVSFPGLVQMDEDTHYNKVEDVVGSHVEDAVTFWAQNVSKNKDIMKIGCSLSEVCPLANSVFGNLDPKKIYGGLFSEDKCWYRCKVLKTISDDKCLVRYIDYGNTEILNRSDIVEIPPELQFSSIAKKYRLWGLQIPSGQEVTQFDQGRTFLGSLIFEKEIKMRIKATYQDGTVIAQAEYGTVDIGEEVAKKGFAEKCRLTSGIDACEAKKPDPNQLALRSLKNPIPLWGRRSNQSTFSRPKGHFNGRLTLDVKYETSAGNHVTFPKESLAAGDFNLGSNVSLAKIKQDQKLIEENEKLKTEKEVLLENYKALELKVEQTAQELQQEKTATMDLTKHLESTLKTCVGTRLKNLAAKVELLKEIRHINISIRFGNDLSDAMQVLDEGSFTTLASLNELEKIWAEYNVAQEKIQTCLNENEGNILIAERNEVQQKLFVAVDVFILEVDDLPLDKRLKTLQDLATSLESVYGKAKEGTNNSEETLRKFYDWQCTKREEFASIRSETEASLQHLVAWFQSSQKVFDLSLDEPLTSEDLIGNIDEILEKTESCVCKELELSLIEQGVIDKEIILSTYSQVLQKIHSEEKFIATLLSKYKDSVEFKKQMIDCLNKNPNVDYLLSIKKTLKGLKAQLRWKLVEKSNLEESDDHDGTEIEKIKQEITQLRNSVFQEIYHEREEYEKLNSLTQKWFPELPLLYPEIGLLKYMNSGGLLTMSLERDLLDTEPMKELSSKRPLVCSEVNGQPVLLKGYSVDVDTEGRVIQRAASYHRACGYAKEESGLLPLIFLFLCKSDPVAYLMVPYYPKANLSAVQASMPLTSEEALKVMKGVARGLHTLHSANIIHGSLHQNNVFALNREQGIVGDYDFTKSESQRASVNAMVGGLSLLSPELKTGKPPSASSDLYAYGCLFLWLSVQNQEFETNEDGIPKVDQFHLDDNVKSLLCSLIYFRSSMTAEQVLNAECFLLPKGKSVPIPEKEIECTQHSREDESKMESLDRYSEKTRNGEANP
Protein: NAC domain containing protein 93 (F4KEI6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MAKKEKIEQVISMGGIMWEGLNSSLIKVDEALLKQQIREFEKGNDKEWFIITERNKVDQGLSQTKRVGNGAKRQKRVDTNGGYWHATVAAQKINAGDGVVGNKRPLAYYDRKPSEDVKTDWLMQEYSLDHNNDKVRLHFVQDLSYSTSNKEVGEEKKKQKKGEPVEASEGQQPCNAEYHQPLAPLDSCQPQPHDLAEQLDLHQPEQLQLQQPHDIVYQPQYCLLPEQHQLQPFPDNFSELNSFQQQPVMIPDDLEDFLAELMEPHSLDGDEESNNYGFFEGLFDTEGINDKTLH
Protein: Hyperpolarization-activated ion channel variant DMIH-A2B1C1 (I[[h]] channel, isoform C) (I[[h]] channel, isoform J) (I[[h]] channel, isoform K) (I[[h]] channel, isoform L) (Q56JH9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MVHFDDVSLYGTPKEEPMPNIPIVSEKVSANFLKSQLQSWFQPTDNRLAMKLFGSRKALVKERIRQKTSGHWVIHPCSSFRFYWDLCMLLLLVANLIILPVAISFFNDDLSTRWIAFNCLSDTIFLIDIVVNFRTGIMQQDNAEQVILDPKLIAKHYLRTWFFLDLISSIPLDYIFLIFNQDFSDSFQILHAGRALRILRLAKLLSLVRLLRLSRLVRYVSQWEEVYFLNMASVFMRIFNLICMMLLIGHWSGCLQFLVPMLQGFPSNSWVSINELQESYWLEQYSWALFKAMSHMLCIGYGRFPPQSLTDMWLTMLSMISGATCYALFLGHATNLIQSLDSSRRQYREKVKQVEEYMAYRKLPRDMRQRITEYFEHRYQGKFFDEELILGELSEKLREDVINYNCRSLVASVPFFANADSNFVSDVVTKLKYEVFQPGDIIIKEGTIGTKMYFIQEGVVDIVMANGEVATSLSDGSYFGEICLLTNARRVASVRAETYCNLFSLSVDHFNCVLDQYPLMRKTMETVAAERLNKIGKNPNIMHQKDEQLSNPESNTITAVVNALAAEADDCKDDDMDLKENLLHGSESSIAEPVQTIREGLPRPRSGEFRALFEGNTP
Protein: Slowpoke-binding protein (Q8IPH9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Regulator of calcium-activated channel Slo. Increases or decreases the voltage sensitivity of Slo, depending on the absence or presence of 14-3-3-zeta in the complex, respectively.
Subcellular location: Cytoplasm {ECO:0000305}. Note=Enriched in synaptic boutons.
Interaction partners:
- Calcium-activated potassium channel slowpoke
- 14-3-3 protein zeta
Sequence:
MFKFNKAAQQQRIDNRNSAVTGHDPFVRPPVPEKKVRNIMKKLHKANGLKRSNSAIEFDVSALTAANRRQIYSSNRSASSEQDNSDLSEHSEKSPLVSARLDNLARLFFSKSMPAETGSRDTIDSVLTTRPNIKYQYSALDSGNGIVERSPRERAQREKALNATQEWIQGANGRYEVIAHLDEIGSRHGKNWFLVTDASVRTDRLQTLLPLPPDCVAFEDLPPNECAREILMELLGSLHHPYIYPVLDLGFLRNSSYNYACLVTPFNSRGSLKDLIYKAQWNEPWARKYTRKPNGLPVSQVQRLGRQILEALLFLKERGFPLHGHLHSGNVILQNGAARLSGLENGLLGLSSRINAVMWSRSVTEIENVDIVCFGHLLYEMCTGQELTTPKPSMRVLEMELQHYPQIGQTRKQILEILGLIFEPPSGVCPSVEDLVLCDLFRSIDLRELRGPCFSTIKPSLSRSTLNLLQAVKKRQCASLGHSLSEANSPCTPPSTPHDRRTGVLPAPYEVFRMY
Protein: Protein ECM7 (Extracellular mutant protein 7) (Zinc-regulated gene 15 protein) (Q06200)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in cell wall organization and biogenesis.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Calcium-channel protein CCH1
- Stretch-activated cation channel MID1
- Calcium channel YVC1
- Putative uncharacterized protein YLR444C
- Transcriptional regulator CRZ1
- Calmodulin
Sequence:
MVMSRIRDTIARPFQNLTALEKVVQWLRLGTTLLIISFGLALTVGPLSSPRTLYMSRLDTYSADITTGLFTVLRESMEQSTSTEENNGVGLTTSELYILTAYTESQIKNVPQYITVSLYGRCDSTYTMVEVFDSEGNMHSVKNSTTKSTCSSIGTDYLFDYREVLESLGLDIILDYAYNKIGSQQAESSAYTTYMRSLKHKKANVLHLLYAVISFQVCMLFFMIWYYYIKGRFMNALKERALVHINSLLSLVVFIGGLISSISLAWVNYTIQSRINTELEAFGFSYHLGVTWFALLWCFAGLISVSCLAWSGLEWCISDNGTSYGGGIDDKFLGYQAGVFTDADLDDETSYSQRYPQRQSTSGEAELMRNSDTMATIRKTSDVDLNSENDANTSLDHGNPTANISNGGKHEPFATREEFELQDIRFRSSNDSEESMQRVIKPSSALQF
Protein: Nucleobase transporter (Q4QG33)
Organism: Leishmania major
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MILNFSSLAELYVYTTCVLLGVSMLMPLNALASAPAYMLDYYKYATRDPNAKPNSPIFWNHILTFYNVASVVTQALVGPTVLTPWARKLSLSFRFFMALTLMMVEVFVILVIPAGGVSQVGAMVAFFIVTIAAGVGKSYLEATCYALVGTMPPKFMSAIMFGCGFSGVLSSTLQCIIKASMEDTYDSVLRQAYLYFSLALGFMAVALAMALSLRFNSYAQEHVGEYRAIKRANEAAKGLNAEETNKAAREEMNGALSSSSKRQPFSTNPVAQGSEIYGDLIDEEAEKARCKAEGAGGSDELSECDEVRAVGRQAGDTCSDSNSDDRNLTTSEQLQRTRAWPVAKFIWPLMASCFCNFFVSLLILPSLIIPVDRTDRWFATIAILLYNCGDATGRWLSSVKLLWPSHLVLFISIGCRFIFIPLTFLCIFKYIPGHAAPHVLFALLGLTNGFFGAISMVFGPIDTRLRTEGQRVMAGQLMGVSLLAGASLSALLAMAIVPFLP
Protein: Cell division cycle 20 L homeolog (LOC398044 protein) (Q6DFD4)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
Sequence:
MAQFAFETDINSILKLDTPITNAPLARWQRKAKEGNCSSLNTSANTSTLSPMKASNRSHSSSKTPSKTPGKSGPKMQGTPSRAGGDRFIPNRSAMQMDVASFLLCKENEPVDTSPTKKEQQKAWAMNLNGFDMEEAKILRLGGRPQNAPEGYQNNLKVLYSQKTTPGSSKKTGRYIPSMPDRVLDAPDIRNDYYLNLIDWSSQNALAVALNDSVYLWNYATGDIILLLQMENSEEYISSVSWIKEGNYLAVGSSNAEVQLWDVQQQKRLRNMISHSSRVGALNWNNHILSSGSRTGHIHHHDVRVAQHHVSTLAGHTQEVCGLKWSPDGRYLASGANDNLVNVWPCVQGDSGEFSPVQTFTQHQAAVKAVAWCPWQSNVLATGGGTSDRHLRIWNVCSGTCLNSVDTHSQVCSIVWSTNYKELISGHGFAQNQLVLWKYPTMTRVTELKGHTARVLNLAMSPDGCTVASAAADETLRLWKCFEVDPVTKKEKEKARSSKSIIHQSIR
Protein: Guanylyl cyclase C (GC-C) (EC 4.6.1.2) (Heat-stable enterotoxin receptor) (STA receptor) (Intestinal guanylate cyclase) (Q3UWA6)
Organism: Mus musculus (Mouse)
Function: Guanylyl cyclase that catalyzes synthesis of cyclic GMP (cGMP) from GTP.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:P25092}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25092}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P25092}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P25092}. Note=The 145 kDa plasma membrane form of GUCY2C contains sialic acid and galactose residues, while a differencially glycosylated 130 Kda form is a high mannose form that is resident in the endoplasmic reticulum and may serve as the precursor for the cell surface form. {ECO:0000250|UniProtKB:P25092}.
Interaction partners:
- Guanylin
- Guanylate cyclase activator 2B
- Bis
- Inosine triphosphate pyrophosphatase
- Emerin
- Molybdenum cofactor biosynthesis protein 1
- cAMP and cAMP-inhibited cGMP 3',5'-cyclic phosphodiesterase 10A
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
- cGMP-specific 3',5'-cyclic phosphodiesterase
- GTP cyclohydrolase 1
Sequence:
MTSLLGLAVRLLLFQPALMVFWASQVRQNCRNGSYEISVLMMDNSAYKEPMQNLREAVEEGLDIVRKRLREADLNVTVNATFIYSDGLIHKSGDCRSSTCEGLDLLREITRDHKMGCALMGPSCTYSTFQMYLDTELNYPMISAGSYGLSCDYKETLTRILPPARKLMYFLVDFWKVNNASFKPFSWNSSYVYKNGSEPEDCFWYLNALEAGVSYFSEVLNFKDVLRRSEQFQEILTGHNRKSNVIVMCGTPESFYDVKGDLQVAEDTVVILVDLFSNHYFEENTTAPEYMDNVLVLTLPSEQSTSNTSVAERFSSGRSDFSLAYLEGTLLFGHMLQTFLENGENVTGPKFARAFRNLTFQGFAGPVTLDDSGDIDNIMSLLYVSLDTRKYKVLMKYDTHKNKTIPVAENPNFIWKNHKLPNDVPGLGPQILMIAVFTLTGILVVLLLIALLVLRKYRRDHALRQKKWSHIPSENIFPLETNETNHISLKIDDDRRRDTIQRVRQCKYDKKKVILKDLKHSDGNFSEKQKIDLNKLLQSDYYNLTKFYGTVKLDTRIFGVVEYCERGSLREVLNDTISYPDGTFMDWEFKISVLNDIAKGMSYLHSSKIEVHGRLKSTNCVVDSRMVVKITDFGCNSILPPKKDLWTAPEHLRQATISQKGDVYSFAIIAQEIILRKETFYTLSCRDHNEKIFRVENSYGKPFRPDLFLETADEKELEVYLLVKSCWEEDPEKRPDFKKIESTLAKIFGLFHDQKNESYMDTLIRRLQLYSRNLEHLVEERTQLYKAERDRADHLNFMLLPRLVVKSLKEKGIVEPELYEEVTIYFSDIVGFTTICKYSTPMEVVDMLNDIYKSFDQIVDHHDVYKVETIGDAYVVASGLPMRNGNRHAVDISKMALDILSFIGTFELEHLPGLPVWIRIGVHSGPCAAGVVGIKMPRYCLFGDTVNTASRMESTGLPLRIHMSSSTITILKRTDCQFLYEVRGETYLKGRGTETTYWLTGMKDQEYNLPSPPTVENQQRLQTEFSDMIVSALQKRQASGKKSRRPTRVASYKKGFLEYMQLNNSDHDSTYF
Protein: Inner membrane protein YigG (P27843)
Organism: Escherichia coli (strain K12)
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:11867724}; Multi-pass membrane protein {ECO:0000269|PubMed:11867724}.
Interaction partners:
- Uncharacterized protein YigF
- Inner membrane protein YiaB
- Protein RarD
- Probable D,D-dipeptide transport system permease protein DdpC
- Uncharacterized protein YqiI
- Inner membrane protein YgjV
Sequence:
MLRIFIPTSNGKISRRRYIFSFILINFIFAFLIIFFNDGEAGFLVIVSTIVLHYLVINMNCQRLRDSGFIYIKTYVFGTLAVYIISIITMIAEDFACSGNGSMIFLICYFSTFSMLMLAPTDSSKQ
Protein: Pre-mRNA-splicing factor ATP-dependent RNA helicase-like protein cdc28 (EC 3.6.4.13) (Pre-mRNA-processing protein 8) (Q10752)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in pre-mRNA splicing. Is required together with ATP and at least one other factor, for the first cleavage-ligation reaction. Functions as a molecular motor in the activation of the precatalytic spliceosome for the first transesterification reaction of pre-mRNA splicing by hydrolyzing ATP to cause the activation of the spliceosome without the occurrence of splicing (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-splicing factor cwf28
- Pre-mRNA-splicing factor spp42
- Pre-mRNA-splicing factor sap145
- Pre-mRNA-splicing factor brr2
- Pre-mRNA-splicing factor cwf3
- Pre-mRNA-splicing factor cwf26
- Pre-mRNA-splicing factor ATP-dependent RNA helicase prp16
- Pre-mRNA-splicing factor cwf10
- Pre-mRNA-splicing factor prp12
Sequence:
MSLEQYVSDKAISLLGMSEPSVVEYLIAEAKGSSSSNNLYQKLVSFGMDGDDPAVKEFAHTLYARIPREGSRPKENYNARKKKEQGILQMERLNSSYDLLIEPQSHETPGKPLKKKSRSKTPKREIARRQRDEDEWESDEYEEVVDGSASHPIEEDSVSTDFQNHDYEKSSDPETERLNDLREREEFEERLRRKDLEAATNEFVEDYSSKFSSEELALRKLADDPESWRKLASELRKKSRQQYLKPRAQQQLEILRREIRDEEQLFAGEKLTQAEIRELEKKKELLRIAEERQRLEKQATEYQMPEDYFTEQGKLDRKRKEEVLYQRYKDSNEGEQNEVTMGAAEQQRWEAQQINKALLFDQNEWLPPGEKQFDFVFDESQQIDFLLDTKLSAENPVDTDKMTDVKVEKSLESSRKSLPVYQYKDDLLKAINEYQVLLIVAETGSGKTTQLPQFLHEAGYTKGNKKICCTQPRRVAAMSVAARVAKEMDVRLGQEVGYSIRFENATSEKTVIKYLTDGMLLREFLTEPDLASYSVIIIDEAHERTLHTDILFGLVKDIARFRPDLKVLISSATIDAEKFSAYFDEAPVFYVPGRRYPVDIYYTPQPEANYIQAAITTILQIHTTQPAGDILVFLTGQDEIELMSENMQELCRILGKRIPEIILCPIYANLPSELQAKIFDPTPPGARKVVLATNIAETSITIDGVNFVIDSGFVKQNMYNPRTGMESLVSVPCSRASADQRAGRAGRVGPGKCFRLYTRRTYNNELDMVTSPEIQRTNLTNIVLLLKSLGINNLLDFDFMDAPPPETLMRSLELLYALGALNNRGELTKLGRQMAEFPTDPMLSKSLIASSKYGCVEEVLSIVSMLGEASSLFYRPKDKIMEADKARANFTQPGGDHLTLLHIWNEWVDTDFSYNWARENFLQYKSLCRARDVRDQLANLCERVEIELVTNSSESLDPIKKAITAGYFSNAARLDRSGDSYRTVKSNQTVYIHPSSSVAEKKPKVIIYFELVLTTKEYCRQITEIQPEWLLEISPHYFKPENIEELQKTQKRHKR
Protein: Cytochrome P450 2C23 (EC 1.14.14.-) (Arachidonic acid epoxygenase) (CYPIIC23) (P24470)
Organism: Rattus norvegicus (Rat)
Function: A cytochrome P450 monooxygenase involved in polyunsaturated fatty acids (PUFAs) metabolism and signaling. Catalyzes preferentially the epoxidation of double bonds of PUFAs. Converts arachidonic acid (ARA, C20:4(n-6)) primarily to stereospecific products 8R,9S-, 11R,12S-, and 14S,15R-EET. Plays a major role in the formation of EETs and hydroxy-EETs (HEETs) in kidney. Via EETs may inhibit the epithelial sodium channels (ENaCs) in nephron segments, preventing excessive sodium absorption during high dietary salt intake (By similarity). Participates in the formation of anti-inflammatory hydroxyepoxyeicosatrienoic acids (HEETs) by converting 20-hydroxyeicosatetraenoic acid (20-HETE) to 20,8,9-HEET, an activator of PPARA. Metabolizes eicosapentaenoic acid (EPA, C20:5(n-3)) to epoxyeicosatetraenoic acid (EETeTr) regioisomers, 8,9-, 11,12-, 14,15-, and 17,18-EETeTr, preferentially producing 17R,18S enantiomer. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14742258}. Microsome membrane {ECO:0000269|PubMed:14742258}.
Interaction partners:
- Bifunctional epoxide hydrolase 2
- Cytochrome P450 2E1
- Cytochrome P450 1A2
- Cytochrome P450 1A1
- Cytochrome P450, family 2, subfamily j, polypeptide 4
- Cytochrome P450 2U1
- Epoxide hydrolase 1
- Polyunsaturated fatty acid
- unspecific monooxygenase
- Prostaglandin G/H synthase 2
Sequence:
MELLGFTTLALVVSVTCLSLLSVWTKLRTRGRLPPGPTPLPIIGNLLQLNLKDIPASLSKLAKEYGPVYTLYFGTSPTVVLHGYDVVKEALLQQGDEFLGRGPLPIIEDTHKGYGLIFSNGERWKVMRRFSLMTLRNFGMGKRSLEERVQEEARCLVEELQKTKAQPFDPTFILACAPCNVICSILFNDRFQYNDKTFLNLMDLLNKNFQQVNSVWCQMYNLWPTIIKYLPGKHIEFAKRIDDVKNFILEKVKEHQKSLDPANPRDYIDCFLSKIEEEKDNLKSEFHLENLAVCGSNLFTAGTETTSTTLRFGLLLLMKYPEVQAKVHEELDRVIGRHQPPSMKDKMKLPYTDAVLHEIQRYITLLPSSLPHAVVQDTKFRDYVIPKGTTVLPMLSSVMLDQKEFANPEKFDPGHFLDKNGCFKKTDYFVPFSLGKRACVGESLARMELFLFFTTLLQKFSLKTLVEPKDLDIKPITTGIINLPPPYKLCLVPR
Protein: Candida glabrata strain CBS138 chromosome I complete sequence (Q6FQH6)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Subcellular location: Secreted, cell wall {ECO:0000256|ARBA:ARBA00004191}.
Interaction partners:
Sequence:
MQFKNVALTAAVASVAAADGYTPGNPWSTLTPSGTVACAKPEYTASFGIAVKPISSSVAKRAVVSQIGDGQIQATSAAPKPTNAAASQVADGQVQQKTTSTTKATTTLAPSSSKTSSTSTSTSCAATPLTIKESSCKNDGTLQLTLKGGVLTDGKGRVGSIVSNRQFQFDGPPPQAGAIYAGGWSITEQGNLALGNSDVFYQCLSGNFYNLYDQKIAEQCSPINLEVVSLVDC
Protein: E3 ubiquitin-protein ligase TRIM38 (EC 2.3.2.27) (RING finger protein 15) (Tripartite motif-containing protein 38) (Zinc finger protein RoRet) (O00635)
Organism: Homo sapiens (Human)
Function: E3 ubiquitin-protein and E3 SUMO-protein ligase that acts as a regulator of innate immunity. Acts as a negative regulator of type I interferon IFN-beta production by catalyzing 'Lys-48'-linked polyubiquitination of AZI2/NAP1, leading to its degradation (By similarity). Mediates 'Lys-48'-linked polyubiquitination and proteasomal degradation of the critical TLR adapter TICAM1, inhibiting TLR3-mediated type I interferon signaling. Acts as positive regulator of the cGAS-STING pathway by acting as a E3 SUMO-protein ligase: mediates sumoylation of CGAS and STING, preventing their degradation and thereby activating the innate immune response to DNA virus (By similarity). Also acts as a negative regulator of NF-kappa-B signaling independently of its E3 protein ligase activity by promoting lysosome-dependent degradation of TAB2 and TAB3 adapters.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q5SZ99}.
Interaction partners:
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- E3 ubiquitin-protein ligase TRIM56
Sequence:
MASTTSTKKMMEEATCSICLSLMTNPVSINCGHSYCHLCITDFFKNPSQKQLRQETFCCPQCRAPFHMDSLRPNKQLGSLIEALKETDQEMSCEEHGEQFHLFCEDEGQLICWRCERAPQHKGHTTALVEDVCQGYKEKLQKAVTKLKQLEDRCTEQKLSTAMRITKWKEKVQIQRQKIRSDFKNLQCFLHEEEKSYLWRLEKEEQQTLSRLRDYEAGLGLKSNELKSHILELEEKCQGSAQKLLQNVNDTLSRSWAVKLETSEAVSLELHTMCNVSKLYFDVKKMLRSHQVSVTLDPDTAHHELILSEDRRQVTRGYTQENQDTSSRRFTAFPCVLGCEGFTSGRRYFEVDVGEGTGWDLGVCMENVQRGTGMKQEPQSGFWTLRLCKKKGYVALTSPPTSLHLHEQPLLVGIFLDYEAGVVSFYNGNTGCHIFTFPKASFSDTLRPYFQVYQYSPLFLPPPGD
Protein: Pho88p (A0A1D8PTX9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Xut1p
- Pho86p
- Vacuolar transporter chaperone complex subunit 4
- Emp24p
Sequence:
MNPAVSNIVIMLVLMQVAKKLDFEDPTILFYTRAAYLGCQALTFLIYFLVRYKINAKNDLTTLKYVEPANPMSGQTEPRAVVTTVKEYDLQQVNQQIKGIFTGLAMMSFMHLYMKYTNPLFMQSISSLKSALESNIVKIHLFGVPASGDLKRPFKSAPGFLEALTGAGGVQTDKASVESAETAGAGGIKQD
Protein: Zinc finger protein 821 (O75541)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MSRRKQTNPNKVHWDQVFAGLEEQARQAMMKTDFPGDLGSQRQAIQQLRDQDSSSSDSEGDEEETTQDEVSSHTSEEDGGVVKVEKELENTEQPVGGNEVVEHEVTGNLNSDPLLELCQCPLCQLDCGSREQLIAHVYQHTAAVVSAKSYMCPVCGRALSSPGSLGRHLLIHSEDQRSNCAVCGARFTSHATFNSEKLPEVLNMESLPTVHNEGPSSAEGKDIAFSPPVYPAGILLVCNNCAAYRKLLEAQTPSVRKWALRRQNEPLEVRLQRLERERTAKKSRRDNETPEEREVRRMRDREAKRLQRMQETDEQRARRLQRDREAMRLKRANETPEKRQARLIREREAKRLKRRLEKMDMMLRAQFGQDPSAMAALAAEMNFFQLPVSGVELDSQLLGKMAFEEQNSSSLH
Protein: adenylate cyclase (EC 4.6.1.1) (O96306)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MEANLENGQKTIASTSKSHSQRQTTSRRRQNDSDVAGGVGITGGGVVILPQHVLNELYHNYSIKQRRSGLKWFVFAAALFNIWTIGIPWDQSAPTRVINCCMLLAYLALTALLHIGRRSDKPALRRFHQILLIIVPRALWLLSILHFTVYVILQPSFSPRDLLGWAILLNFLVYVTLPLQLIFLGLSIGCITYFICLSLPVGYSHWDSLLSNQLAANAVLIATAALIGLLYYFMGEAKQKRAFLEAKKSLEVKMVIEEQSAEQERLLLSVLPKHVAIKMREDLGSSSSEAFKKIYMSRHENVSILYADIVGFTAISSTYSAQDLVKMLNELFARFDRLAEKYQQLRIKILGDCYYCISGAPDERPDHAVLCVHMGLSMVKAIKYVQQKANSPVDMRVGIHTGAVLAGILGQRQWQFDVYSKDVELANKMESSGKAGRVHISDKTLAFLNGEFEVEAAFGEKREELLRIAGLKTYFITKVVKAFASPCAKKINETQAEIAHPNPNGSTTDIVSDEDDNDATLDDEELLAQNSVSNGHQIGIAVTADEEEQVKLENFKQRLKDELVTRDGHENLTKDTNIFLRFKNPQLEQLYAVYREPYSSLPLLAALLVQCIDVLYSYLVLPRSTLHFINIAAPLVPIAMLVVISLAESFSGMLPKFFVDVSKRFNDITFVRELAAIIIALTIGFSNVIDMFFFVTFVRTEHIVSESEFNVTASLESDINLAVEGMVTAEHLLPASFVEQMRDAVPTERVLYPSYLSNFGVLILIAIAVIAQLTHLTKILLLLSIAALHCYFNIFIMQDLYALEDDFEHQPIISTRYAASGLLLVAALALSTLARHMDHEDRVIFKWKTEVAEQKETANDMRQRNEALVYNVLPVHVAEHFMKNTKRSHDDLYSQSYAEVGVLFASMPNFSDFYSEETVNNQGLECLRFLNEVISDFDALLELPQFQDIIKIKTIGSTYMAASGINLQRTVRNDAPITERWSHLAILVEFALELKHALQSINEQSFNHFVLKMGINHGPITAGVIGARKPHYDIWGNTVNVASRMESTGKAGAIQVTEETCNILRLFGYTFLQRGLVAVKGKGQLMTFYLQGKSQSSAEPVASGVVVLNGQDSSAVESTSELEASDIKMPLLKMNGPEQSLEIDQDRSLRNDSAGQESVAECQSLLE
Protein: S-type anion channel SLAH2 (SLAC1-homolog protein 2) (Q9ASQ7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Slow, weak voltage-dependent S-type anion efflux channel involved in maintenance of anion homeostasis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:18305482}; Multi-pass membrane protein {ECO:0000269|PubMed:18305482}.
Interaction partners:
- Calcium-dependent protein kinase 21
- Protein ABIL1
Sequence:
MNNPRSVSPLVSPANHSDLLENQRQSGSGDFSRLEKRIGARKMKFHSKSMPRGAMFLDQEASRNFHDKRYDLFRTMSGKLERQISNLRGKPTESSLQDHKEITESLTADRYFDALQGPELETLKEKEKIVLPEDKTWPFLLRFPITSYGMCLGVSSQAIMWKTLATTEAEKFLHVTQVINHVLWWISLLLLLAVSITYLFKTILFFEAVRREFRHPIRVNFFFAPLISILFLALGIPHSIISHLPSTLWYFLMAPILFLEMKIYGQWMSGGQRRLSKVANPTNHLSIVGNFAGALLGASMGLKEGPIFFFAIGLAYYLVLFVTLYQRLPTNETLPKELHPVFFLFVAAPAVASMAWTKISASFDLGSRLAYFISLFLYFSLVCRINLFRGFKFSLAWWAYTFPMTAVASATIKYSDEVTGVATKILSVVMSGAATLTVIAVLGLTVMHAFVQRDLFPNDVVIAISAEQPKQKRWFKHLTKESYGNNERCPKILDPEDNQIDLESPPLVNVDSSTVQNSN
Protein: RNA polymerase-binding transcription factor DksA (DnaK suppressor protein) (P0ABS1)
Organism: Escherichia coli (strain K12)
Function: Transcription factor that acts by binding directly to the RNA polymerase (RNAP). Required for negative regulation of rRNA expression and positive regulation of several amino acid biosynthesis promoters. Also required for regulation of fis expression. Binding to RNAP disrupts interaction of RNAP with DNA, inhibits formation of initiation complexes, and amplifies effects of ppGpp and the initiating NTP on rRNA transcription. Inhibits transcript elongation, exonucleolytic RNA cleavage and pyrophosphorolysis, and increases intrinsic termination. Also involved, with RecN, in repair of DNA double-strand breaks. Required, probably upstream of the two-component system BarA-UvrY, for expression of CsrA-antagonistic small RNAs CsrB and CsrC.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00926, ECO:0000269|PubMed:16858726}.
Interaction partners:
- Transcription elongation factor GreA
- RNA polymerase sigma factor RpoD
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit omega
- Transcription elongation factor GreB
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- GTP pyrophosphokinase
- RNA-binding protein Hfq
- RNA polymerase sigma factor RpoS
Sequence:
MQEGQNRKTSSLSILAIAGVEPYQEKPGEEYMNEAQLAHFRRILEAWRNQLRDEVDRTVTHMQDEAANFPDPVDRAAQEEEFSLELRNRDRERKLIKKIEKTLKKVEDEDFGYCESCGVEIGIRRLEARPTADLCIDCKTLAEIREKQMAG
Protein: Uncharacterized protein (Q584T4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSVPEWARSEHSIEEAKEYLRTGNSVDFFELVSSHILREHPLDVAAFALDLVERISKLGNTLSARDYHPKRVEDNKYLQEKNVCEFLNEWILALLKERPDTDEARMSFHKRYLKSLVDGGGCSQCTSVN
Protein: Rhamnogalacturonase B (RGase B) (RHG B) (EC 3.2.1.171) (P87161)
Organism: Aspergillus niger
Function: Pectinolytic enzymes consist of four classes of enzymes: pectine lyase, polygalacturonase, pectin methylesterase and rhamnogalacturonase. Hydrolyzes alpha-D-galacturonopyranosyl-(1,2)-alpha-L-rhamnopyranosyl linkages in the backbone of the hairy regions of pectins.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MLLDKLSVLSFLGLAPIFAAAQLSGSVGPLTSASTKAATKTCNVLDYGAKADKSTDLGAPLASAFADCKSGGLVYVPSGDYALSTWARLSGGEAWALQIDGIIYRTGTDGGNMIYIEHSSDFELFSSTSEGAMQGLGYEFHADDNWSGPRLLRLYEVTDFSVHDFILVDSPSFHFSLDTCTNGEIYNMAIRGGNHGGLDGIDVWSNNIWVHDVEVTNKDECVTVKGPSKNILIESIYCNWSGGCGMGSFGSDTNVSDITYRNIYTWSSNNMMLIKSNGGSGFVENVLLENFIGHGNAYSLDIDSYWASMSAVDGDGVQLSNITVKNWKGTEAYGAERGPVKVVCADGAPCYDITIEDFAMWTEEGDSQWYSCESAYGSGYCLQDSDDHVSYSVTTSTVSSAPSGYSATSMAADLTTDFGSTVSIPIPTIPTSFYPGATPYSALMANSASTAAASSIASHATVHSSSASVAASVPSAVAPSESIPAATSAVVSSAAAIAPSPAVGAQEGSTTSAPSFAAPSGAGNSPQGPTGASGFGEKGQQGEQGEQGEQGEQGVCYV