wanglab/gogpt-training-data huggingface dataset:
Protein: PAN2-PAN3 deadenylation complex subunit pan3 (PAB1P-dependent poly(A)-specific ribonuclease) (Poly(A)-nuclease deadenylation complex subunit 3) (PAN deadenylation complex subunit 3) (Q9UST1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulatory subunit of the poly(A)-nuclease (PAN) deadenylation complex, one of two cytoplasmic mRNA deadenylases involved in mRNA turnover. PAN specifically shortens poly(A) tails of RNA and the activity is stimulated by poly(A)-binding protein pab1. PAN deadenylation is followed by rapid degradation of the shortened mRNA tails by the CCR4-NOT complex. Deadenylated mRNAs are then degraded by two alternative mechanisms, namely exosome-mediated 3'-5' exonucleolytic degradation, or deadenlyation-dependent mRNA decaping and subsequent 5'-3' exonucleolytic degradation by xrn1. May also be involved in post-transcriptional maturation of mRNA poly(A) tails. ppk26/pan3 acts as a positive regulator for PAN activity, recruiting the catalytic subunit pan2 to mRNA via its interaction with RNA and with pab1.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03181, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- PAN2-PAN3 deadenylation complex catalytic subunit pan2
- Protein adenylyltransferase SelO, mitochondrial
- Polyadenylate-binding protein, cytoplasmic and nuclear
- CCR4-Not complex 3'-5'-exoribonuclease subunit Ccr4
- PAB-dependent poly
- 5'-3' exoribonuclease 1
Sequence:
MSVRKNSPASPKPTSRSRESSRSPSVTDLKDHSKAKRTLCRNILLYGSCKHSENGCAFRHDGPFIPSSENLEQYSVKKKLNAASASFQPVRALPVKAAGAAVFVPKSQEKSLFLSRERTPVALSPGSHAINPYNNASMLVNEPFHDDSGVYYTRQNQFKPTLYNLYNPQPSPMPTLLPYERTVNGLFIDDTTRERIERKSEASRQTISALPSIISSYTSLAPLNTKLYRYKEQIGFSSWTYKCTSSIDGNAYVLKRLQDCSINIDTSTVDKLKNVFHPNIVPFHSAFHTDTFHDSSLLLIYDFYPCTTTLGELYLNNSKNSVKLEENRKIPERELWNYFFQLTIALSYLHKSGFACNKLTPSRILVDQTERIRISGCADYELVVSNKPPLEERKKQDFVDLGVVIANLATGRTDMDMSSAARAIYSTYSREFYKAVLYFVSEVPEDKNLELFLQNHIESFFPIMSSPYVECEKMERKISDAFQHGRFFNILCKIMFIIDNNRASREYPIAREKEISLIYLLRDYLFHQIDEDECPVIDLYQVLNRLGKLDAGINQAIALISRDELDCVSVSYGELKAWLDNVYEMEINS
Protein: Protein PYRICULARIA ORYZAE RESISTANCE 21 (Pi21) (Q7XL73)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in defense responses. Contributes to slowing defense responses toward Magnaporthe oryzae.
Interaction partners:
Sequence:
MGILVILVDLQCCRCDAKIRKVLGCLEEEYCIEKVEYDVKNNRVIVRGKFDPEKLCKKIWCKAGKIIKEILIVDVWPPPLPQPPPPCKPPPCEKPPEDCKPKPCHCCSCEKPKPKPKPCHCEKPKPCHCEKPKPCEKPPPCKPEEPPKPPPEKPPPKPECKLVPYPYPVPYPYAGQWCCPKPEPPKPPPEPPKEPEPPKPCGCSHAFVCVCKPAPPPPPPCGCSGGHGNCGCGIRPWPPQVWPPPPVCPPPPWCYTEDNANACSIM
Protein: Squamous cell carcinoma antigen 2 related protein 1 (Q8BHL1)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MIRFHAADVKFAVEMYRQLRESDKNIFYSPISMMTALAMLQLGAKGNTEIQIEKVLQFIETTKKTTKKSEHCDDEENVHEQFQKLITQLNKSNDDYDLKAANSIYGAKGFPFLQTFLEDIKEYYQAKVESLDFEHATEESEKKINSWVESKTNGKIKDLFPSGSLSSSTILVLVNAVYFKGQWNRKFDENHTREEKFWLNKNTSKPVQMMKQRNKFNFSFLGDVHAQIVEIPYKGKDLSMFVLLPMEIDGLKQLEEQLTTDKLLEWIKAENMHLTELYLSLPRFKVEEKYDLQVPLEHMGMVDAFDPQKADFSGMSSIPGLVVSKVLHKSFVEVNEEGTEAAAATGVEVSVRSAQIAEDFCCDHPFLFFIIHRKTNSILFFGRISSP
Protein: Uncharacterized protein (Q38CG9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRSAYCRKPSSGFMAHSNVVVALLSLVALHFVPYYIQGTVSADSGSNTTVGFRCMRPFASLPRFSSTSMDAAENCKFKRYNVLNASAVVKCESTGNATGKAEPTAVTSTCSVTIHAAFRTMGGGKDDNADAADVYRYSLQLRAINNSVVHYKGFDQNGYGLCCSFIEGAKCTWEERETSGVQEAKQEVNATTSQAPTVKEPAVVSCPLHHGEEEHIAFRGSTVKPLHRLVVGNWEARLEFWRGGPSNREVLGRLLVPFRLTDENIAQGNNNTITERSDHTTAVVVVAEQGQLTGSRGDL
Protein: Potassium channel HX13_20290 (A0A086F3E3)
Organism: Chryseobacterium sp. (strain P1-3)
Function: Potassium channel.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MTKGRLEAFSDGVLAIIITIMVLELKVPEGSSWASLQPILPRFLAYIFSFIYVGIYWNNHHHLFQTVKKVNGSILWANLHLLFWLSLMPIATEWIGTSHFAQNPVATYGIGLIMSAIAYTILENVIIRCEGENSKLKEAIHSKFKEYISIIFYVLGIATSFFYPYIAIGFYYLVALIWLIPDKRIEKSLKEN
Protein: Autophagy protein 5 (Protein autophagy 5) (AtAPG5) (Q9FFI2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for autophagy. Conjugation to ATG12 is essential for plant nutrient recycling. Involved in a negative feedback loop that modulates NPR1-dependent salicylic acid (SA) signaling and limits senescence and immunity-related programmed cell death (PCD) in plants. Involved in complete proteolysis of chloroplast stroma proteins in senescent leaves. Involved in the degradation of damaged peroxisomes.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Ubiquitin-like protein ATG12B
- Autophagy-related protein 3
- Ubiquitin-like protein ATG12A
- Autophagy-related protein 16
- Autophagy-related protein 18b
- Ubiquitin-like modifier-activating enzyme atg7
- Beclin-1-like protein
- Serine/threonine-protein kinase ATG1c
- Ubiquitin-like-conjugating enzyme ATG10
- Autophagy-related protein 8a
Sequence:
MAKEAVKYVWEGAIPLQIHLHKSDVASHPAPPPALVLAPRIGYLPLLIPLIKPYFKDSLPPGEDSIWFDYKGFPLKWYIPTGVLFDLLCAEPERPWNLTIHFRGYPCNILIPCEGEDSVKWNFVNSLKEAQYIINGNCKNVMNMSQSDQEDLWTSVMNGDLDAYTRLSPKLKMGTVEDEFSRKTSLSSPQSQQVVPETEVAGQVKTARIPVRLYVRSLNKDFENLEDVPEIDTWDDISYLNRPVEFLKEEGKCFTLRDAIKSLLPEFMGDRAQTSGEERSIDDTEEADGSREMGEIKLVRIQGIEMKLEIPFSWVVNNLMNPEFYLHISVLVKAPQR
Protein: S-formylglutathione hydrolase YeiG (FGH) (EC 3.1.2.12) (P33018)
Organism: Escherichia coli (strain K12)
Function: Serine hydrolase involved in the detoxification of formaldehyde. Hydrolyzes S-formylglutathione to glutathione and formate. Shows also esterase activity against alpha-naphthyl acetate, lactoylglutathione, palmitoyl-CoA and several pNP-esters of short chain fatty acids.
Interaction partners:
- S-
- S-formylglutathione hydrolase FrmB
- Formate dehydrogenase-O major subunit
- Formate dehydrogenase, cytochrome b556
- Formate dehydrogenase-O iron-sulfur subunit
- 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase
- Esterase YpfH
- Esterase YqiA
Sequence:
MEMLEEHRCFEGWQQRWRHDSSTLNCPMTFSIFLPPPRDHTPPPVLYWLSGLTCNDENFTTKAGAQRVAAELGIVLVMPDTSPRGEKVANDDGYDLGQGAGFYLNATQPPWATHYRMYDYLRDELPALVQSQFNVSDRCAISGHSMGGHGALIMALKNPGKYTSVSAFAPIVNPCSVPWGIKAFSSYLGEDKNAWLEWDSCALMYASNAQDAIPTLIDQGDNDQFLADQLQPAVLAEAARQKAWPMTLRIQPGYDHSYYFIASFIEDHLRFHAQYLLK
Protein: Uncharacterized protein, isoform B (M9MSJ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGPRLYPAAILILHCLLLLFLQVDSRGNQNHTQMERQRHLRAHNLHRPPYDGYDWHKHFNRDAEPKATVAKEKEEKTFKHRSGHLKKMKQTARDISNWRARSAYQKETAELEEWGRKKNITDNELKLFFDGEISTKDKYRLFGDIQTVVQILKEVIKKGAVTEKEKAMITPELKPLILRFGRMFEREFAKNTNALEALQILVHEVQKSNSRNMRHKSAKRSH
Protein: Iridoid oxidase (CrIO) (EC 1.14.14.161) (Cytochrome P450 76A26) (CrCYP76A26) (W8JIS5)
Organism: Catharanthus roseus (Madagascar periwinkle) (Vinca rosea)
Function: Component of the seco-iridoid and derivatives monoterpenoid indole alkaloids (MIAs, e.g. vincristine, quinine, and strychnine) biosynthesis pathway. Catalyzes the conversion of cis-trans-nepetalactol (iridodial) into 7-deoxyloganetic acid. Converts also iridotrial into 7-deoxyloganetic acid.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:24710322}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MATITFDSLNPVTVAISAGFLLLLIIFVKSRTGSSKRKPPGPPGWPIFGNMFDLGDLPHQTLYKLKSKYGPIVWLQLGSINTMVVQNAVSAAELFKKHDVPFCDRKVPDTLTAFNFNQGSLGMNTYGGHWRVLRRLCSMEFLVNKRMNETTDLRRRIEDNMVRWIEEDSLASKAQGGTGAVQLSRFLFLMAFNLVGNLMLSRDLMDNKDPEGREFFDCMNEILELAGTPNIADFLPLLKKLDPLGMKKRMVDNMSRTMKISSKFVQERLDNRKAGKINEKKDFLDVMLEYQGDGKDGPDKFTEQHVNIVIMEMFFAGSETTSISIEWGFTELLRNPHAFKKVREEIDRVVGVNRMVEETDMENLPYLQAVVKETLRLHPALPMLLPRNTMEDTEYMGYLIPKGTQVFVNAWAIGRDPEYWQDPLSFKPERFINSSVEYKGQHFELIPFGSGRRICVGFPLAHRVVHLTLATLVQAFDWDLGAGVKPQDIDLEERLGLTLRKKNPLNVIPKKRVHI
Protein: Tumor necrosis factor ligand superfamily member 11 (Osteoclast differentiation factor) (ODF) (Osteoprotegerin ligand) (OPGL) (Receptor activator of nuclear factor kappa-B ligand) (RANKL) (TNF-related activation-induced cytokine) (TRANCE) (CD antigen CD254) [Cleaved into: Tumor necrosis factor ligand superfamily member 11, membrane form; Tumor necrosis factor ligand superfamily member 11, soluble form] (O35235)
Organism: Mus musculus (Mouse)
Function: Cytokine that binds to TNFRSF11B/OPG and to TNFRSF11A/RANK. Osteoclast differentiation and activation factor. Augments the ability of dendritic cells to stimulate naive T-cell proliferation. May be an important regulator of interactions between T-cells and dendritic cells and may play a role in the regulation of the T-cell-dependent immune response. May also play an important role in enhanced bone-resorption in humoral hypercalcemia of malignancy (By similarity). Induces osteoclastogenesis by activating multiple signaling pathways in osteoclast precursor cells, chief among which is induction of long lasting oscillations in the intracellular concentration of Ca (2+) resulting in the activation of NFATC1, which translocates to the nucleus and induces osteoclast-specific gene transcription to allow differentiation of osteoclasts. During osteoclast differentiation, in a TMEM64 and ATP2A2-dependent manner induces activation of CREB1 and mitochondrial ROS generation necessary for proper osteoclast generation.
Subcellular location: [Isoform 1]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm.; SUBCELLULAR LOCATION: [Tumor necrosis factor ligand superfamily member 11, soluble form]: Secreted.
Interaction partners:
- Tumor necrosis factor receptor superfamily member 11B
- Tumor necrosis factor receptor superfamily member 11A
- TNF receptor-associated factor 6
- Macrophage colony-stimulating factor 1 receptor
- Nuclear factor of activated T-cells, cytoplasmic 1
- Cathepsin K
- Osteocalcin-related protein
- Osteocalcin-2
- Sclerostin
- Osteocalcin
Sequence:
MRRASRDYGKYLRSSEEMGSGPGVPHEGPLHPAPSAPAPAPPPAASRSMFLALLGLGLGQVVCSIALFLYFRAQMDPNRISEDSTHCFYRILRLHENADLQDSTLESEDTLPDSCRRMKQAFQGAVQKELQHIVGPQRFSGAPAMMEGSWLDVAQRGKPEAQPFAHLTINAASIPSGSHKVTLSSWYHDRGWAKISNMTLSNGKLRVNQDGFYYLYANICFRHHETSGSVPTDYLQLMVYVVKTSIKIPSSHNLMKGGSTKNWSGNSEFHFYSINVGGFFKLRAGEEISIQVSNPSLLDPDQDATYFGAFKVQDID
Protein: Protein NRT1/ PTR FAMILY 2.12 (AtNPF2.12) (Nitrate transporter 1.6) (Q9LFX9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Low-affinity proton-dependent nitrate transporter. Not involved in dipeptides transport. Involved in delivering nitrate for seed development.
Subcellular location: Cell membrane {ECO:0000269|PubMed:19050168}; Multi-pass membrane protein {ECO:0000269|PubMed:19050168}.
Interaction partners:
- High affinity nitrate transporter 2.7
- High-affinity nitrate transporter 2.2
- High affinity nitrate transporter 2.4
- High-affinity nitrate transporter 2.1
- Chloride channel protein CLC-a
Sequence:
MGVVENRKILPEKKLGGWRAITFILGNETLEKLGSIGVSANFMLYLRNVFHMEPVEAFNVYYLWMGLTNFAPLLGALISDAYIGRFKTIAYASLFSILGLMTVTLTACLPQLHPPPCNNPHPDECDDPNKLQLGILFLGLGFLSIGSGGIRPCSIPFGVDQFDQRTEQGLKGVASFFNWYYLTLTMVLIFSHTVVVYLQTVSWVIGFSIPTSLMACAVVLFFVGMRFYVYVKPEGSVFSGIARVIVAARKKRDLKISLVDDGTEEYYEPPVKPGVLSKLPLTDQFKFLDKAAVILDGDLTSEGVPANKWRLCSIQEVEEVKCLIRVVPVWSAGIISIVAMTTQATFMVFQATKMDRHMGPHFEIPAASITVISYITIGIWVPIYEHLLVPFLWRMRKFRVTLLQRMGIGIVFAILSMFTAGFVEGVRRTRATEMTQMSVFWLALPLILMGLCESFNFIGLIEFFNSQFPEHMRSIANSLFPLSFAAANYLSSLLVTTVHKVSGTKDHPDWLNKDLDRGKLDYFYYLIAVLGVVNLVYFWYCAHRYQYKAGSQIEDFNEEKSLLDIEPNQRHDQSPS
Protein: Protein NRT1/ PTR FAMILY 7.1 (AtNPF7.1) (Q3E9B5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAAMDPRNNGNVAPLNERERAENLEVREVVEVQDDQSVVSLMSNDSDLQKKMMKKEEKKNGGWTNAIILLVNQGLATLAFFGVGVNLVLFLTRVMGQGNAEAANNVSKWTGTVYMFSLVGAFLSDSYWGRYLTCTIFQVIFVIGVGLLSFVSWFFLIKPRGCGDGDLECNPPSSLGVAIFYLSVYLVAFGYGGHQPTLATFGADQLDDDKNSKAAFFSYFYFALNVGALFSNTILVYFEDKGLWTEGFLVSLGSAIVALVAFLAPTRQYRYVKPCGNPLPRVAQVFVATARKWSVVRPGDPHELYELEGPESAIKGSRKIFHSTKFLFLDRAAVITENDRNGTRSNAWRLCSVTQVEEAKCVMKLLPIWLCTIIYSVIFTQMASLFVEQGDVMNAYVGKFHIPAASMSVFDIFSVFVSTGIYRHIIFPYVRPTELMRMGIGLIIGIMAMVAAGLTEIQRLKRVVPGQKESELTILWQIPQYVLVGASEVFMYVGQLEFFNGQAPDGLKNLGSSLCMASMALGNYVSSLMVNIVMAITKRGENSPGWIPENLNEGHMDRFYFLIAALAAIDFVVYLIFAKWYQPISHDEDSIKGGSGGSLKKTVSELEQV
Protein: Lipase I (H0Y3S0)
Organism: Homo sapiens (Human)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MRVYIFLCLMCWVRSDNKRPCLEFSQLSVKDSFRDLFIPRIETILMMYTRNNLNCAEPLFEQNNSLNVNFNTQKKTVWLIHGYRPVGSIPLWLQNFVRILLNEEDMNVIVVDWSRGATTFIYNRAVKNTRKVAVSLSVHIKNLLKHGASLDNFHFIGVSLGAHISGFVGKIFHGQLGRITGLDPAGPRFSRKPPYSRLDYTDAKFVDVIHSDSNGLGIQEPLGHIDFYPNGGNKQPGCPKSIFSGIQFIKCNHQRAVHLFMASLETNCNFISFPCRSYKDYKTSLCVDCDCFKEKSCPRLGYQAKLFKGVLKERMEGRPLRTTVFLDTSGTYPFCNHHFAGIILYLKTERKCFLIQTHVHQRTHKMPSSIKCTCL
Protein: VPS10 domain-containing receptor SorCS3 (Q9UPU3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Beta-nerve growth factor
- PRKCA-binding protein
- Large ribosomal subunit protein mL43
- Disks large homolog 4
Sequence:
MEAARTERPAGRPGAPLVRTGLLLLSTWVLAGAEITWDATGGPGRPAAPASRPPALSPLSPRAVASQWPEELASARRAAVLGRRAGPELLPQQGGGRGGEMQVEAGGTSPAGERRGRGIPAPAKLGGARRSRRAQPPITQERGDAWATAPADGSRGSRPLAKGSREEVKAPRAGGSAAEDLRLPSTSFALTGDSAHNQAMVHWSGHNSSVILILTKLYDFNLGSVTESSLWRSTDYGTTYEKLNDKVGLKTVLSYLYVNPTNKRKIMLLSDPEMESSILISSDEGATYQKYRLTFYIQSLLFHPKQEDWVLAYSLDQKLYSSMDFGRRWQLMHERITPNRFYWSVAGLDKEADLVHMEVRTTDGYAHYLTCRIQECAETTRSGPFARSIDISSLVVQDEYIFIQVTTSGRASYYVSYRREAFAQIKLPKYSLPKDMHIISTDENQVFAAVQEWNQNDTYNLYISDTRGIYFTLAMENIKSSRGLMGNIIIELYEVAGIKGIFLANKKVDDQVKTYITYNKGRDWRLLQAPDVDLRGSPVHCLLPFCSLHLHLQLSENPYSSGRISSKETAPGLVVATGNIGPELSYTDIGVFISSDGGNTWRQIFDEEYNVWFLDWGGALVAMKHTPLPVRHLWVSFDEGHSWDKYGFTSVPLFVDGALVEAGMETHIMTVFGHFSLRSEWQLVKVDYKSIFSRHCTKEDYQTWHLLNQGEPCVMGERKIFKKRKPGAQCALGRDHSGSVVSEPCVCANWDFECDYGYERHGESQCVPAFWYNPASPSKDCSLGQSYLNSTGYRRIVSNNCTDGLREKYTAKAQMCPGKAPRGLHVVTTDGRLVAEQGHNATFIILMEEGDLQRTNIQLDFGDGIAVSYANFSPIEDGIKHVYKSAGIFQVTAYAENNLGSDTAVLFLHVVCPVEHVHLRVPFVAIRNKEVNISAVVWPSQLGTLTYFWWFGNSTKPLITLDSSISFTFLAEGTDTITVQVAAGNALIQDTKEIAVHEYFQSQLLSFSPNLDYHNPDIPEWRKDIGNVIKRALVKVTSVPEDQILIAVFPGLPTSAELFILPPKNLTERRKGNEGDLEQIVETLFNALNQNLVQFELKPGVQVIVYVTQLTLAPLVDSSAGHSSSAMLMLLSVVFVGLAVFLIYKFKRKIPWINIYAQVQHDKEQEMIGSVSQSENAPKITLSDFTEPEELLDKELDTRVIGGIATIANSESTKEIPNCTSV
Protein: Aminoacyl tRNA synthase complex-interacting multifunctional protein 2 (Multisynthase complex auxiliary component p38) (Protein JTV-1) (Q8R010)
Organism: Mus musculus (Mouse)
Function: Required for assembly and stability of the aminoacyl-tRNA synthase complex. Mediates ubiquitination and degradation of FUBP1, a transcriptional activator of MYC, leading to MYC down-regulation which is required for aveolar type II cell differentiation. Blocks MDM2-mediated ubiquitination and degradation of p53/TP53. Functions as a proapoptotic factor.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:18695251}. Nucleus {ECO:0000269|PubMed:18695251}. Note=Following DNA damage, dissociates from the aminoacyl-tRNA synthase complex and translocates from the cytoplasm to the nucleus. {ECO:0000269|PubMed:18695251}.
Interaction partners:
- Methionine--tRNA ligase, cytoplasmic
- Bifunctional glutamate/proline--tRNA ligase
- Aminoacyl tRNA synthase complex-interacting multifunctional protein 1
- Lysine--tRNA ligase
- Aspartate--tRNA ligase, cytoplasmic
- Eukaryotic translation elongation factor 1 epsilon-1
- Arginine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Glutamine--tRNA ligase
- Isoleucine--tRNA ligase, cytoplasmic
Sequence:
MPMYQVKPYHGGSAPLHVELPTCMYRLPNVHSKTTSPATDAGHVQETSEPSLQALESRQDDILKRLYELKAAVDGLSKMIHTPDADLDVTNILQADEPTTLATNTLDLNSVLGKDYGALKDIVINANPASPPLSLLVLHRLLCERYRVLSTVHTHSSVKNVPENLVKCFGEQARKQSRHEYQLGFTLIWKNVPKTQMKFSVQTMCPIEGEGNIARFLFSLFGQKHNAVTLTLIDSWVDIAMFQLREGSSKEKAAVFRSMNSALGRSPWLVGNELTVADVVLWSVLQQTGGSSGAAPTNVQRWLKSCENLAPFSTALQLLK
Protein: Aspartic proteinase CDR1 (EC 3.4.23.-) (Protein CONSTITUTIVE DISEASE RESISTANCE 1) (Q6XBF8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in salicylic acid-dependent inducible resistance responses. May release an endogenous peptide elicitor required for the activation of inducible resistance mechanisms. Possesses protease activity in vitro.
Subcellular location: Secreted, extracellular space, apoplast {ECO:0000269|PubMed:14765119}.
Interaction partners:
- Aspartic proteinase A3
- GTP-binding protein-like protein
- Subtilisin-like protease SBT3.3
Sequence:
MASLFSSVLLSLCLLSSLFLSNANAKPKLGFTADLIHRDSPKSPFYNPMETSSQRLRNAIHRSVNRVFHFTEKDNTPQPQIDLTSNSGEYLMNVSIGTPPFPIMAIADTGSDLLWTQCAPCDDCYTQVDPLFDPKTSSTYKDVSCSSSQCTALENQASCSTNDNTCSYSLSYGDNSYTKGNIAVDTLTLGSSDTRPMQLKNIIIGCGHNNAGTFNKKGSGIVGLGGGPVSLIKQLGDSIDGKFSYCLVPLTSKKDQTSKINFGTNAIVSGSGVVSTPLIAKASQETFYYLTLKSISVGSKQIQYSGSDSESSEGNIIIDSGTTLTLLPTEFYSELEDAVASSIDAEKKQDPQSGLSLCYSATGDLKVPVITMHFDGADVKLDSSNAFVQVSEDLVCFAFRGSPSFSIYGNVAQMNFLVGYDTVSKTVSFKPTDCAKM
Protein: Interferon (Q6WVG1)
Organism: Ictalurus punctatus (Channel catfish) (Silurus punctatus)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MISQYRAKNNFCVSLLKEMGGEIVPVNSSFPCEEYTEIEKAKAEDQVRFLAQATKQIISLFNAVSKVDEVKWDRRALDDFLNILNTRQLTELTKCTSTYAKRGHSPTERKLRKRFKELKKLLREAKYSADSLERIRNVVQRDLWRMDIIAANVKHKLLKRTN
Protein: Probable carboxylesterase 13 (AtCXE13) (EC 3.1.1.1) (Q9SMM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Carboxylesterase acting on esters with varying acyl chain length.
Interaction partners:
- Expansin-A13
Sequence:
MDSEIAADYSPMLIIYKSGRIERLVGETTVPPSSNPQNGVVSKDVVYSPDNNLSLRIYLPEKAATAETEASVKLPLLVYFHGGGFLVETAFSPTYHTFLTAAVSASDCVAVSVDYRRAPEHPIPTSYDDSWTALKWVFSHIAGSGSEDWLNKHADFSKVFLAGDSAGANITHHMTMKAAKDKLSPESLNESGISGIILVHPYFWSKTPVDDKETTDVAIRTWIESVWTLASPNSKDGSDDPFINVVQSESVDLSGLGCGKVLVMVAEKDALVRQGWGYWEKLGKSRWNGEVLDVVETKGEGHVFHLRDPNSEKAHELVHRFAGFIKGDK
Protein: F-box domain-containing protein (Q17962)
Organism: Caenorhabditis elegans
Interaction partners:
- Skp1-related protein
- Uncharacterized protein C40H1.2
- Tyrosine-protein phosphatase domain-containing protein
- PPM-type phosphatase domain-containing protein
- Exostosin domain-containing protein
- BPTI/Kunitz inhibitor domain-containing protein
- Glucosidase 2 subunit beta
- Beta-ureidopropionase
- Skp1-related protein
- Uncharacterized protein F23F12.3
Sequence:
MFKAFSSIMQSLQFKTDVPVIIDAETVPNECFSPIFRRLDKKSLLNCQLACHRFNDLISSDSFWIEYARILNISNVLPSLEWRRAATQKKFVGNEDNEIDTSSFNFNIKKIVLSGRGYSPITPLFISHFENARDNTISGTLRSDDFSIRANGSGIHMERDGGNGCEPHPDVSKCFVFSFTESSISVFIDLVNSGIDPWILDHVRPRIRITQKVNHRNDCAARLSFAAQLNYHETQWIERFGHVQTMSNTDHKRYKSVNKEWAQWTGQPWEDWTIEFDDYPSGIRHLTILNEGEDRQFWRGFYGPKVANIQVEVILPDEPIVKPLAVDSEKCNEDENPNAEDEDDDDDEVPPRVGVFRMPLFRRGRHMYGIPPAVARHEDEDEED
Protein: Putative metal ion transporter C27B12.12c (O13657)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Stretch-activated cation channel yam8
- eIF-2-alpha kinase activator gcn1
Sequence:
MSFQQPSNGAQGGNNNALEKTSSNEATSSSSTQVSSLSASGISVSTPRVSPFEPERNMQVQSSQHLEANVQSPVSSQTTYATPSAYAVPQESEIELHESEMVPQKPKKKKRSRRNRKASRKKIPATQSSSADMDTLHVCPTCGSCSDSKKPQSNKKHRGRRVKHSPKSTLEVPDGIPDIKALSASMGSSSQHASRYNEGRGSFDTLGTHYHLSKSRKSSSSDSLYSVSSMSIKNDSNSDSLSSSSSSDVSGSDENLPIDKTLYLSVEDPSFMVHPRRPSATKSCSAAVDCPHTTIPKPPYQSDTDLTELPTKSTAQFSDETFTVQPRLKSTHSSIADNEDREVDSQVDENTRVVEEDVCFPMQEESHVNKGIDFDELDNFAEEELQKQRQNTDHFRSRQYSTCKPFEPHWNDLSPHDPNDPSSSLHSNNAEKAAEVPLRSSYYSGGRRSVTSMSDSPYRFSFFSSNQNETIHASVLSDLLDDGATSFRSLFCPEKGVWWLDCLDPTDIEMRVLSKAFSIHPLTTEDIRVQEAREKVELFGSYYFVCFRSFEQDPELANYLEPLNMYIVVFREGLLTFHFSSATHPASVRRRARQLRDYVHVSSDWLCYALIDDITDAFVPLIRGIETETEAIEDSVLVGRSEDSSDMLRRIGECRKKTMGMFRLLYGKADVIKMLAKRCNEKWTIAPTGEIGLYLGDIQDHLVTMTSNLSQFEKILSRTHSNYLAQLTSNSIEENSRTNGALGKITLIGTLLVPMNLVTGLFGMNVPVPGRDTNNLAWFFGILGVLLGSIAIGWIITMRYNAF
Protein: Aconitate hydratase, mitochondrial (Aconitase) (EC 4.2.1.3) (Citrate hydro-lyase) (O13966)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate, a step in the citric acid cycle.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Probable isocitrate dehydrogenase, mitochondrial
- Probable citrate synthase, mitochondrial
- Isocitrate dehydrogenase subunit 2, mitochondrial
- Isocitrate dehydrogenase subunit 1, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Mitochondrial 2-methylisocitrate lyase
- Probable dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
- Probable ATP-citrate synthase subunit 1
- Probable ATP-citrate synthase subunit 2
- Probable succinate dehydrogenase flavoprotein subunit, mitochondrial
Sequence:
MFCKISRAPARMGSRIFTQSTLRSFSCAPVAANIDAKKVAMSNFEKNKFINYQRIKDNLEIVKKRLNRPLTYSEKILYGHLDDPVNQDIERGVSYLKLRPDRVACQDATAQMAILQFMSAGMPEVAVPVTVHCDHLIEAYEGGPIDLERANVTNKEVYDFLQTACAKYNIGFWRPGSGIIHQIVLENYAFPGGLLIGTDSHTPNAGGLGMVAIGVGGADAVDVMANLPWELKCPKVIGVKLTGQLKGWTSPKDVILKVAGILTVKGGTGAIVEYFGPGVESLSCTGMGTICNMGAEIGATTSIFPFNPRMSEYLRATNRSAIADYAEEFAPIIAADENAHYDQIIEIDLNTLEPHLNGPFTPDLATPISKFKEAVKKNDWPQELKVGLIGSCTNSSYEDMSRAASICQQAIDKGIKTKSLFTITPGSEQVRATLTRDGQLDTMRKAGGIVLANACGPCIGQWKRTDVKKGEKNSIVTSYNRNFTGRNDANPATHAFVTSPDIVTAMVFSGDMNFNPLTDTLKDKDGNDFKFEPPTGAGLPSKGYDPGSNTYVAPSSVNVKDVAIDPHSKRLQRLTPFKKWDGKDMKGLKILIKAKGKCTTDHISAAGPWLKYRGHLQNISNNYMIGAINAENGEANKLKDQLTGEYKTVPNVAIDYRDHGIRWVTLGEQNFGEGSSREHAALEPRYLGGAAVITKSFARIHETNLKKQGLLPLTFADPAAYDKISPFDTVDIDGLTTFAPGKPLTLVVHPADGSAEWSTKLNHTFNKDQIEWFKAGSALNHMANMHKQK
Protein: Inward rectifier potassium channel 16 (Inward rectifier K(+) channel Kir5.1) (Potassium channel, inwardly rectifying subfamily J member 16) (Q9NPI9)
Organism: Homo sapiens (Human)
Function: Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium. KCNJ16 may be involved in the regulation of fluid and pH balance. In the kidney, together with KCNJ10, mediates basolateral K(+) recycling in distal tubules; this process is critical for Na(+) reabsorption at the tubules.
Subcellular location: Membrane {ECO:0000269|PubMed:24561201}; Multi-pass membrane protein. Basolateral cell membrane {ECO:0000269|PubMed:24561201}. Note=In kidney distal convoluted tubules, located in the basolateral membrane in the presence of KCNJ10. {ECO:0000269|PubMed:24561201}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 10
- ATP-sensitive inward rectifier potassium channel 15
- Disks large homolog 4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MSYYGSSYHIINADAKYPGYPPEHIIAEKRRARRRLLHKDGSCNVYFKHIFGEWGSYVVDIFTTLVDTKWRHMFVIFSLSYILSWLIFGSVFWLIAFHHGDLLNDPDITPCVDNVHSFTGAFLFSLETQTTIGYGYRCVTEECSVAVLMVILQSILSCIINTFIIGAALAKMATARKRAQTIRFSYFALIGMRDGKLCLMWRIGDFRPNHVVEGTVRAQLLRYTEDSEGRMTMAFKDLKLVNDQIILVTPVTIVHEIDHESPLYALDRKAVAKDNFEILVTFIYTGDSTGTSHQSRSSYVPREILWGHRFNDVLEVKRKYYKVNCLQFEGSVEVYAPFCSAKQLDWKDQQLHIEKAPPVRESCTSDTKARRRSFSAVAIVSSCENPEETTTSATHEYRETPYQKALLTLNRISVESQM