wanglab/gogpt-training-data huggingface dataset:
Protein: Homeodomain interacting protein kinase, isoform C (M9PDR2)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MISLVIRRLFRKDCDCGCVDSYNSSHGPPVQQDSSAAAGAGSVGSKAGSGPGPDGIGPISSLKTAHTKVATSGGHANTQPPSKRSSSGADGDYQLVQHEVLYSLSAEYEVLEFLGRGTFGQVVKCWKRGTSEIVAIKILKNHPSYARQGQIEVSILSRLSQENADEFNFVRAFECFQHKNHTCLVFEMLEQNLYDFLKQNKFSPLPLKYIRPILEQVLTALLKLKQLGLIHADLKPENIMLVDPVRQPYRVKVIDFGSASHVSKTVCNTYLQSRYYRAPEIILGLPFCEAIDMWSLGCVVAELFLGWPLYPGSSEFDQIRYISQTQGLPTEHMLNSASKTSKFFYRDVDSTYPFWRLKTTEEHEAETNTKSKEARKYIFNCLDDIGQVNVPTDLEGGQLLAEKTDRREFIDLLKRMLTIDQERRLTPAEALNHSFTRLTHLVDYVYCNNVKASVQMMEVCRRGDFHTVQPASTLVTNFVPSSTENMTFTINNQLTSQVQRLVRDGRPLAYEGLYQIYNGRSVARQYPQTRTDSFQHQLVSNILCPPSYQTMPSPTKHVVVGSATMQPPLQVPPQQYVNVPVPVSMVEPTSGQRMLLTNRVQASGVAWPQTGRQMALVPSWPQQAPAHSLIVDSTPLFNVEEIYPKHHLNLPRNDLKKESPAHHIAKGNSYRVPRHEKKEHQQLSPVKKRVKESSPPHQQRYQRAAHVSPQYHAHHNCNYGNGSGYSASAGSVVASSAASSSNIVNGSSSSSHHHHVPVAHAQPYSSSSGHHIVSNCNANGGAGGAVVYQQPPAHAHQQHGQQPHPQSSQHPQHVKQPTITIHDTPSPTAVITISDSEDEGGEAGGAQVPVLKQRAHAQSQTSGSLLQHAPSSSCSRSSAHQQPHPHPQQQQQQQINYGDHDPEDARRRHHAAAAAAVGSPKHHHHQQQQQPAPPPQQQQQQYQPQPPPQQVLPQPQPSIKYEPGQSQKKRILAMAQSECGYQPQVPSQPSSSASLPHIPTKQEPAEFYPEYAAAPPQQLDTKRSSWAPTSSGSGVSALPLAHPKREAPSVAPISYVAPSVAPPLAHSKSSSASSSSSISAATAAAAAAAAAAAASVGPPSWGPPQVYRQPSQPPPGSVGLPGSTQPPPSSVAPHPHHHSHGHHHHQAGTPLGGSPSSTAAAALLQPDIYAQGDIYRRPTVFVSQAAPSYAYANRAVVAPPPAHNSSSRQVIPSHPLPAHIQIPTQYSQFGPLSPAQVAASKHAAHFAPTNIWYGAE
Protein: Matrix metalloproteinase-16 (MMP-16) (EC 3.4.24.-) (Membrane-type matrix metalloproteinase 3) (MT-MMP 3) (MTMMP3) (Membrane-type-3 matrix metalloproteinase) (MT3-MMP) (MT3MMP) (O35548)
Organism: Rattus norvegicus (Rat)
Function: Endopeptidase that degrades various components of the extracellular matrix, such as collagen type III and fibronectin. Activates progelatinase A. Involved in the matrix remodeling of blood vessels. The short isoform efficiently converts progelatinase A to the intermediate form but not to the mature one. It has no effect on type I, II, IV and V collagen. However, upon interaction with CSPG4, it may be involved in degradation and invasion of type I collagen by melanoma cells.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}. Note=Localized at the cell surface of melanoma cells. {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform Short]: Secreted, extracellular space, extracellular matrix.
Interaction partners:
- Proheparin-binding EGF-like growth factor
- Metalloproteinase inhibitor 2
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Metalloproteinase inhibitor 1
- Collagenase 3
- Metalloproteinase inhibitor 3
- Furin
- Metalloproteinase inhibitor 4
Sequence:
MILLAFSSGRRLDFVHRSGVFFFQTLLWILCATVCGTEQYFNVEVWLQKYGYLPPTDPRMSVLRSAETMQSALAAMQQFYGINMTGKVDRNTIDWMKKPRCGVPDQTRGSSKFNIRRKRYALTGQKWQHKHITYSIKNVTPKVGDPETRRAIRRAFDVWQNVTPLTFEEVPYSELENGKRDVDITIIFASGFHGDRSPFDGEGGFLAHAYFPGPGIGGDTHFDSDEPWTLGNPNHDGNDLFLVAVHELGHALGLEHSNDPTAIMAPFYQYMETDNFKLPNDDLQGIQKIYGPPDKIPPPTRPLPTVPPHRSVPPADPRKNDRPKPPRPPTGRPSYPGAKPNICDGNFNTLAILRREMFVFKDQWFWRVRNNRVMDGYPMQITYFWRGLPPSIDAVYENSDGNFVFFKGNKYWVFKDTTLQPGYPHDLITLGNGIPPHGIDSAIWWEDVGKTYFFKGDRYWRYSEEMKTMDPGYPKPITIWKGIPESPQGAFVHKENGFTYFYKGKEYWKFNNQILKVEPGYPRSILKDFMGCDGPTDRDKEGLSPPDDVDIVIKLDNTASTVKAIAIVIPCILALCLLVLVYTVFQFKRKGTPRHILYCKRSMQEWV
Protein: T-box transcription factor 18 (Signal element on autosome protein 1) (O02073)
Organism: Caenorhabditis elegans
Function: Transcriptional regulator involved in developmental processes. Directly binds to the promoter region of the sex-determining factor xol-1 to activate its transcription. Its activation of xol-1 transcription controls sex determination and X chromosome dosage compensation to promote male development. Has a role in the fox-1-sex-1-mediated determination of sexual fate.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00201, ECO:0000269|PubMed:16139225}.
Interaction partners:
- Homeobox protein ceh-39
- Signal element on autosome protein 2
- Steroid hormone receptor family member cnr14
- RNA-binding protein ASD-1
- XO lethal protein 1
- Sex determination protein fox-1
- Paired zinc finger protein 1
- Uncharacterized protein
- Putative T-box protein 34
- CNDH2_C domain-containing protein
Sequence:
MDTIININNNNQKYPQSAEEYHKVLCNYFITLQSAMQSTSRPSSSSPPSLPAVSSELLSSSFPTNAPESSSRDLAPKQNQFTINVVLFDEKKKKNPEENLPANGDQLATLRSLMMQINPSSPPSIPATSPQLPLAESENVPESSSTLKDHKFSLNTMLFNVKKNDAVKISLANQEQWAKFHEIGTEMMVFNSGRRLFPLLAYKVSGLDPHKLYCAGVHMIPDSAYKQEYDHDLQQWVNCLNQKKTIFKPTSEILGRIENGFKLMSLGIDMSDVKIFNIAIRKKTPLQIEKSRKPNLDKTIEVLIQYKYLPVIKIYELSNSGMEKKEIAQATFPETSFVTVSIYRNQKIKEMKTLGNKYCRTDRKQIVMEQRGELEQ
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0B4KGS4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ras-related protein Rac1
- Cdc42 homolog
- non-specific serine/threonine protein kinase
- Rho-type guanine nucleotide exchange factor, isoform F
- Ras-related protein Rac2
- AT17867p
- Ras-like GTP-binding protein RhoL
- LIM domain kinase 1
- Moesin/ezrin/radixin homolog 2
- Integrin beta-PS
Sequence:
MSFTKWFKKKGGDGGSISEIGAPTNFQRHFHVSRNQETGDLEGLPAPWVRLMNSQITRDEQDKNPDAAYHAVKYYNYSIKKKENEVFKPFITEDVIHEESKEIENYVNYKNKHKSQDPEKSDDDGSSTATETESSSGCGSSAGNSNSSSINDSSQQSTVPLDALEEVFKELKTNLEHRETLKAAPQEPPPVPPKKSPHTIPPKPQIKPKPRVTQKFSRTSDIRRDEDSDNQHKINTDTIIIKPAVGAQDAGADDNPDETILRRSKEKRAQKTDAEIYVELRAICNSDDPRERYKTTQEVGKGASGIVFIAADLQNESQVAVKTIDMKNQSSKDLILTEIRVLKDFNHKNLVNFLDAYLLEPEDQLWVVMEYMDGGPLTDVVTETVMKERQIACVCRETLYAISFLHAKGIIHRDIKSDNVLLGMDGSVKVTDFGFCANIEGDEKRQTMVGTPYWMAPEVVTRKKYGKKVDIWSIGIMAIEMIEGQPPYLYETPLRALYLIAANGRPDIKSWDKLSPNLQDFLDRCLQVEVDRRATADELLSHPFLNDCSEVKALVPNIKAAKKVLRRNVXLLCNHRTARLLYA
Protein: Acetyltransferase component of pyruvate dehydrogenase complex (EC 2.3.1.12) (Q5AYC2)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Mitochondrion {ECO:0000256|RuleBase:RU361137}.
Interaction partners:
- Pyruvate dehydrogenase E1 component subunit beta
- Pyruvate dehydrogenase E1 component subunit alpha
- 2-methylcitrate synthase, mitochondrial
- Citrate synthase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- ATP citrate synthase
- ATP citrate synthase
- Succinate--CoA ligase subunit beta, mitochondrial
- Succinyl-CoA synthetase subunit alpha, putative
- Succinate--CoA ligase subunit alpha, mitochondrial
Sequence:
MVASAVRMRVPSASFISKGACSLRRPQASYKFTAAIQHQLPALAALSRYYASKSFPPHTIISMPALSPTMTAGNIGAWQKKAGDALQPGDVLVEIETDKAQMDFEFQEEGILAKVLKESGEKDVSVGSPIAVLVEEGTDVAAFESFSLEDAGGEGAGAAPPKETQETPKEAPKASEPSTPQPAAGAYEPDTSGEKLQPSLDREPAISPAAKALALEKGVPIKALKGTGRGGQITKEDVEKYKPTAAAAAAGPASEDIPLTSMRKTIASRLQQSWNQNPHFFVSTTLSVTKLLKLRQALNASSEGKYKLSVNDFLIKACAAALRKVPQVNSSWTEENGQVVIRQHNSVDISVAVATPVGLITPIVKNAQGLGLSSISNQVKDLGKRARDNKLKPEEYQGGTFTISNMGMNPAVERFTAIINPPQAGILAVGTTRKVAVPVETEEGTSVEWDDQIIVTASFDHRVVDGAVGAEWIKELKKVVENPLELLL
Protein: DNA utilization protein HofM (P45753)
Organism: Escherichia coli (strain K12)
Function: Required for the use of extracellular DNA as a nutrient.
Interaction partners:
- DNA utilization protein HofN
- DNA utilization protein HofQ
- DNA utilization protein HofO
- DNA utilization protein HofP
- Putative electron transfer flavoprotein subunit YgcQ
- Prepilin peptidase-dependent protein D
- Probable cystine transporter YijE
Sequence:
MAFKIWQIGLHLQQQEAVAVAIVRGAKECFLQRWWRLPLENDIIKDGRIVDAQQLAKTLLPWSRELPQRHHIMLAFPASRTLQRSFPRPSMSLGEREQTAWLSGTMARELDMDPDSLRFDYSEDSLSPAYNVTAAQSKELATLLTLAERLRVHVSAITPDASALQRFLPFLPSHQQCLAWRDNEQWLWATRYSWGRKLAVGMTSAKELAAALSVDPESVAICGEGGFDPWEAVSVRQPPLPPPGGDFAIALGLALGKAY
Protein: AT30546p (Q8T8T3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
EMTTVSTEEEKQPTANCDNHQQSNNSNSKTSNDQQPSTSKAAQKLQLFRPLLNKELEDWIWQDNRQFLQDRNIFEHTYFNFMWQICGHIPQSLISETDVTCMAAKLSVSFFIETFIHAKEKPTMVPWVELLTKQFNASQEACEWFLSHMSQEPYWPVQVLIQCPNQMVRQMFQRLVIHVIQQLRASHAHLYLEVETDEDDKELIGQASCVTRFIGSLISLLEHGARANLRHLSEYFGLLCEFSRMGDEEAMYLLRIGVLKSLVDFYLGHKQTDSIDISSDNEDNSSEEALSVEKMRPASLDKMIALCASLVERSRGADFRLRLSPKDFSAIAGGKVILKKLESF
Protein: Schlafen 4 (A0A1L1SUL4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPGKVICSPEALCMKPFSQHEGYEQLVRTELGSLRKGTLVVSKSWALDLGLQEKQEVIWDVLHISQGSLLTLHVFVQGDENLEGNSSLLGKLGAELKGYYKQIALTLKQTLVNHCGYTAKIGIIVKITYLGHKTMCLYDSSAKICYPQIYYLTTKAVKDLEKALAEILGSYESFYSLPRRNWDSFMSAFLNVGSYIVYFSRNVLTHIRI
Protein: Superoxide dismutase [Cu-Zn] (EC 1.15.1.1) (D2D329)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Interaction partners:
Sequence:
MVKAVAVLSSNEGVSGTVFFSQEGDGPTTVTGNLSGLKAGLHGFHVHALGDITNGCMSTGPHFNPAGKEHGAPEDENRHAGDLGNVTVGDDGCASFSITDKQIPLTGPNSIIGRAVVVHADPDDLGKGGHELSKSTGNAGGRVACGIIGLQG
Protein: 8-oxo-dGTP diphosphatase (EC 3.6.1.55) (7,8-dihydro-8-oxoguanine-triphosphatase) (Mutator protein MutT) (dGTP pyrophosphohydrolase) (Q9HW06)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Bifunctional NAD
- Uncharacterized Nudix hydrolase PA4841
- Thiazole synthase
- Phosphomethylpyrimidine synthase
- Sulfur carrier protein ThiS
- Nudix hydrolase domain-containing protein
- Nudix hydrolase domain-containing protein
- Phosphatase NudJ
- hydroxymethylpyrimidine kinase
- Nudix hydrolase domain-containing protein
Sequence:
MKRVHVAAAVIRGSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADKHVLLDVWEVDGFSGEAHGAEGQPLAWVEPRELADYEFPAANAPIVQAARLPAHYLITPDGLEPGELISGVRKAVEAGIRLIQLRAPNMFSPEYRDLAIDIQGLCAGKAQLMLKGPLEWLGDFPAAGWHLTSAQLRKYASAGRPFPEGRLLAASCHDAEELALAASMGVEFVTLSPVQPTESHPGEPALGWDKAAELIAGFNQPVYLLGGLGPQQAEQAWEHGAQGVAGIRAFWPGGL
Protein: VRK serine/threonine kinase 3 (M0QZ79)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MISFCPDCGKSIQAAFKFCPYCGNSLPVEEHVGSQTFVNPHVSSFQGSKRGLNSSFETSPKKVKWSSTVTSPRLSLFSDGDSSESEDTLSSSERSKGSGSRPPTPKSSPQKT
Protein: Peptidyl-prolyl cis-trans isomerase cyp18 (PPIase cyp18) (SanCyp18) (EC 5.2.1.8) (Rotamase cyp18) (P83221)
Organism: Streptomyces antibioticus
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15304318}.
Interaction partners:
Sequence:
MSTVELNTSAGRIVLELNDAEAPKTVENFLAYVRSGHYDGTIFHRVISDFMIQGGGFTPDMQQKSTLAPIQNEADNGLRNDNYTVAMARTNDPHSATAQFFINVKDNAFLNHTSKTPNGWGYAVFGRVTEGQDVVDAIKGVKTGSSRGHQDVPVQPVVIESAKILG
Protein: Antigen P35 (O50962)
Organism: Borreliella burgdorferi (strain ATCC 35210 / DSM 4680 / CIP 102532 / B31) (Borrelia burgdorferi)
Interaction partners:
Sequence:
MKRNKIWKTLKLFQITLLFSCSFYSKSNNTEAISELQSSPIKLGKIKVLQKTEKIVSTQNLQNLQQSQFFKNEKEKIIKKIAQEFDENEKLINKIGPNIEMFAQTINTDIQKIEPNDQFGINKTLFTEKKDNNIDFMLKDNRLRRLFYSSLNYDENKIKKLATILAQTSSSNDYHYTLIGLIFWTGFKIQEAFESAVNILTKDEQKRLIFNFRTKTVKEIQENFEKLMQERNSWIKIVDNIIGEYDKNTGGCKADGKILGEVIRVGYEHELDSNKSMQILNNIETPLKTCCDHIHY
Protein: E3 ubiquitin-protein ligase (EC 2.3.2.27) (B7Z078)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514, ECO:0000256|RuleBase:RU367115}.
Interaction partners:
- Poly [ADP-ribose] polymerase tankyrase
- Axin
- Poly [ADP-ribose] polymerase
- Ankyrin, isoform B
- Ankyrin 2, isoform U
Sequence:
MSQQRSTEQIAASNNNTSDVIALDDDEDTDVQFVAALRPTAPVIDLCVSPSTSAAAAAAAAAAAHSGGGSGEDPAVGSASGAAASDTDSLASSPDEGALATGVDAAAAVSGEDSPSAAAAALECPICLQTCIHPARLPCGHIFCFLCVKGVAYKNRRCAMCRREIPAEFLDHPQLVNGIEDICTTRATEDGFQWYYEGRNGWWQYDDRTSQDIEDAFKKGDKSCTILVAGYVYIVDLEQLVQQRQNEPTRCRRVKRDLATIPKKGVAGLRIEGNQVTSDTVFSRPTNTANPTTVAAAASSFISTIAATDAAIRIASDIIGSTLAHADELTRGLTASNLNDDLSSSGEQSNSTNSNDAGRSPASSPASSSMQDLITRDLRNTQQVIAHNQHTIDLFEQALNDFQALAMRNYVDSSDEENNDQDQEHELREREQLEAGEQPQSNDNPQRF
Protein: AMSH-like ubiquitin thioesterase 3 (EC 3.4.19.-) (Deubiquitinating enzyme AMSH3) (Q5PNU3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Zinc metalloprotease that cleaves 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains, but is not implicated in protein degradation by the 26S proteasome, deneddylation, or desumoylation. Required for intracellular trafficking (e.g. trafficking from the Golgi to the vacuole and the vacuolar trafficking of endocytosed cargo), endocytosis and vacuole biogenesis.
Subcellular location: Membrane {ECO:0000269|PubMed:20543027}; Peripheral membrane protein {ECO:0000269|PubMed:20543027}. Cytoplasm {ECO:0000269|PubMed:26324913, ECO:0000305|PubMed:20543027}. Vacuole membrane {ECO:0000305|PubMed:20543027}; Peripheral membrane protein {ECO:0000305|PubMed:20543027}. Late endosome {ECO:0000269|PubMed:26324913}. Note=Localized in late endosome when associated with BRO1/ALIX. {ECO:0000269|PubMed:26324913}.
Interaction partners:
- Vacuolar protein sorting-associated protein 2 homolog 1
- Vacuolar protein sorting-associated protein 24 homolog 1
- Ubiquitin carboxyl-terminal hydrolase
- AMSH-like ubiquitin thioesterase 1
- AMSH-like ubiquitin thioesterase 2
- Vacuolar-sorting protein BRO1
- 26S proteasome non-ATPase regulatory subunit 6 homolog
- 26S proteasome non-ATPase regulatory subunit 11 homolog
- Ubiquitin-ribosomal protein eL40y fusion protein
- 26S proteasome non-ATPase regulatory subunit 4 homolog
Sequence:
MKIDLNKVAREIEVDNRIPLRNYYRIADNLLRQASIYREEKNVVDLYIMLLRYSSLISETIPFHRDYQASLPQERLGSRKRLRAVINELESLKPEFNQLVDKLNRVEDESRQDGSDLPVVSYSSDAVEWPPAHKASYSRPDINKPLPTSQPSWTYNNNLTSSSNRTQIDQQFQKLSFDFLPPNQATLSRHSFLGPNGLKRQMVAPKSEIKVQYPSNTDWGSADNSGLIEAGPSSSSASLNGDSQEVSTLNSVLSLDDGRWQRHSEAVNSQFISDATEDPFQFVGMKQPSPPPVLAQVHQELAQICPSKVADPRPGPAIPSLEGKEGSNSYQHLHVPVRIMDDFLRLARSNTERNLETCGVLAGSLKNRVFHITTLIIPKQESTSDSCQTLNEEEIFEVQDRLSLFPLGWIHTHPTQTCFMSSVDLHTHYSYQIMLPEAVAIVMAPTDESTPHGIFHLSDPSGVSVIRNCQQRGFHPHEESEDGNPIYEHCSHVFLNAKLKYEVLDLR
Protein: Probable inositol transporter 2 (Q9C757)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plasma membrane inositol-proton symporter. Specific for several inositol epimers, such as myoinositol and scylloinositol. D-chiroinositol, mucoinositol, alloinositol and pinitol are also transported with a lower activity. Not active with galactinol and phytate.
Subcellular location: Cell membrane {ECO:0000269|PubMed:17951450}; Multi-pass membrane protein {ECO:0000269|PubMed:17951450}.
Interaction partners:
- Putative protease Do-like 11, mitochondrial
- Putative protease Do-like 13
Sequence:
MEGGIIHGGADESAFKECFSLTWKNPYVLRLAFSAGIGGLLFGYDTGVISGALLYIRDDFKSVDRNTWLQEMIVSMAVAGAIVGAAIGGWANDKLGRRSAILMADFLFLLGAIIMAAAPNPSLLVVGRVFVGLGVGMASMTAPLYISEASPAKIRGALVSTNGFLITGGQFLSYLINLAFTDVTGTWRWMLGIAGIPALLQFVLMFTLPESPRWLYRKGREEEAKAILRRIYSAEDVEQEIRALKDSVETEILEEGSSEKINMIKLCKAKTVRRGLIAGVGLQVFQQFVGINTVMYYSPTIVQLAGFASNRTALLLSLVTAGLNAFGSIISIYFIDRIGRKKLLIISLFGVIISLGILTGVFYEAATHAPAISSLETQRFNNISCPDYKSAMNTNAWDCMTCLKASSPSCGYCSSPIGKEHPGACWISDDSVKDLCHNENRLWYTRGCPSNFGWFALLGLGLYIIFFSPGMGTVPWIVNSEIYPLRFRGICGGIAATANWISNLIVAQSFLSLTEAIGTSWTFLIFGVISVIALLFVMVCVPETKGMPMEEIEKMLERRSMEFKFWKKKSKLVEKQNQSA
Protein: Peroxisomal OPC-8:0-CoA ligase 1 (EC 6.2.1.-) (4-coumarate--CoA ligase isoform 9) (At4CL9) (4-coumarate--CoA ligase-like 5) (Q84P21)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors. Converts 12-oxo-phytodienoic acid (OPDA) and 3-oxo-2-(2'-pentenyl)-cyclopentane-1-octanoic acid (OPC-8:0) into OPDA-CoA and OPC-8:0-CoA, respectively. Follows a two-step reaction mechanism, wherein the carboxylate substrate first undergoes adenylation by ATP, followed by a thioesterification in the presence of CoA to yield the final CoA thioester (By similarity).
Subcellular location: Peroxisome {ECO:0000269|PubMed:16963437, ECO:0000269|PubMed:18267944}.
Interaction partners:
- 12-oxophytodienoate reductase 3
- Peroxisomal acyl-coenzyme A oxidase 1
- Putative peroxisomal acyl-coenzyme A oxidase 1.2
- 12-oxophytodienoate reductase 2
- 12-oxophytodienoate reductase 1
- Putative 12-oxophytodienoate reductase-like protein 1
- Acyl-coenzyme A oxidase 2, peroxisomal
- Allene oxide cyclase 3, chloroplastic
- Lipoxygenase 4, chloroplastic
- Allene oxide synthase, chloroplastic
Sequence:
MASVNSRSGFCNSNSTFYSKRTPIPLPPNPSLDVTTFISSQAHRGRIAFIDASTGQNLTFTELWRAVESVADCLSEIGIRKGHVVLLLSPNSILFPVVCLSVMSLGAIITTTNPLNTSNEIAKQIKDSNPVLAFTTSQLLPKISAAAKKLPIVLMDEERVDSVGDVRRLVEMMKKEPSGNRVKERVDQDDTATLLYSSGTTGMSKGVISSHRNLIAMVQTIVNRFGSDDGEQRFICTVPMFHIYGLAAFATGLLAYGSTIIVLSKFEMHEMMSAIGKYQATSLPLVPPILVAMVNGADQIKAKYDLSSMHTVLCGGAPLSKEVTEGFAEKYPTVKILQGYGLTESTGIGASTDTVEESRRYGTAGKLSASMEGRIVDPVTGQILGPKQTGELWLKGPSIMKGYFSNEEATSSTLDSEGWLRTGDLCYIDEDGFIFVVDRLKELIKYKGYQVAPAELEALLLTHPEITDAAVIPFPDKEVGQFPMAYVVRKTGSSLSEKTIMEFVAKQVAPYKRIRKVAFVSSIPKNPSGKILRKDLIKIATSNSKL
Protein: Voltage-gated potassium channel (KvAP) (Q9YDF8)
Organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
Function: Mediates a strong voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gradient.
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Elongation factor 2
Sequence:
MSVERWVFPGCSVMARFRRGLSDLGGRVRNIGDVMEHPLVELGVSYAALLSVIVVVVEYTMQLSGEYLVRLYLVDLILVIILWADYAYRAYKSGDPAGYVKKTLYEIPALVPAGLLALIEGHLAGLGLFRLVRLLRFLRILLIISRGSKFLSAIADAADKIRFYHLFGAVMLTVLYGAFAIYIVEYPDPNSSIKSVFDALWWAVVTATTVGYGDVVPATPIGKVIGIAVMLTGISALTLLIGTVSNMFQKILVGEPEPSCSPAKLAEMVSSMSEEEFEEFVRTLKNLRRLENSMK
Protein: Polynucleotide adenylyltransferase family protein (F4INK3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Aconitase family protein
- Poly
- Nuclear poly
- Nuclear poly
- Nuclear poly
- Nuclear poly
- Poly
- Dihydrodipicolinate reductase-like protein CRR1, chloroplastic
Sequence:
MAGFIKRKGNVFFHSQALAAVYSKLQRSNCTLAEGFMEKCSSIRQVIDEDINSVDTSKWKKVRASDAGIKNSMIPESSMNVLRLLRRQGFDAYLVGGCVRDLILNRVPKDYDVITTADLKQIRRLFHRAQVIGKRFPICHVWMGGSIIEVSSFDTVAHSDSDLEKSKEKSGVSLDTKANKNNSLFKMYSGWDIKDCKRWRNSLQRDFTINSLFYNPFDFTIYDYANGMEDLTDLKLRTLVPAHLSFKEDCARILRGLRIAARLGLSLSKDVKTAIPEFVSSVANLDQFRLIMEMNYMLAYGAAAPSILLLMKFKLLHVLLPFQAAYLDQASKTSLSSSLMLVRLFSNMDKLVSCDQPADPKLWIAVLAFHIALVRNPQEAIVVRAFAALLYHGNWSKAVEFAREHETSVIGYAPEVSKSSRKRSDEDLAEAVSEFTCLLKDTQYVLTDKEALREALYLYPDFKFSGLVFIPKKKGRDVAEGFMRLSDVESYESQKEGFSIDYVLLGKGNPCEVRFVLGKIILDTITEGTVIEPLNSVKKKQSTRNHIVPAACLEKKDELFVSKSSKEDNNNQTPVHDSNASSVLKILKRTREDSEQNNDQETEVCPRTPSGPAKNQDQSVVQMLKRRRSKEAPVSEPPKQKTSKRSRSDDQEAVGSLSVPAKIQHQSNKHDTNAPICELPKQKTSKNHSKESRKVKHNDLPVKEIKEAKQGFVSDKSMSDLLQVLEKSSQQVSSKEENNSLSSEKTNRPRKLSSLFR
Protein: Cyclin-A2 (Q98TA3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MSTQGSAVHDSDIHNQENMLSRLRGAAAKNRVENRENVNPNPKAANNRTVLGELENSQRRQLGLRGAKQGSGPQIIACKPEENARSFGERPSNRQPAAFQIHVDEPDGACSKKAPLQRSTMDCSPLTLNPTVTRLRQPLATIDLPLEASFDSPMDMSVIDCEERPTNVNEVSDYAAEIHTHLREMEVKSKPKAGYMRKQPDITNSMRAILVDWLVEVGEEYKLQNETLYLAVNYIDRFLSSMSVLRGKLQLVGTAAMLLASKFEEIYPPEVAEFVYITDDTYTKKQVLRMEHLVLTVLSFDLAAPTINQFLTQYFLHQPVSSKVESLSMFLGELSLIDCDPFLKYLPSQMAAAAFILANHTLASGSWSKSLVDLTGYSLEDLLPCVQDLHQTYLAASQHAQQAVREKYKGSKYHEVSLIEPPEKLMLN
Protein: Endoribonuclease AbiQ (ABIQ) (EC 3.1.-.-) (Toxin AbiQ) (Q9ZJ19)
Organism: Lactococcus lactis subsp. lactis (Streptococcus lactis)
Function: Toxic component of a type III toxin-antitoxin (TA) system. An endoribonuclease that is probably sequence-specific. It is neutralized by its cognate antitoxin RNA AntiQ, which has 2.8 35 nucleotide-long repeats. Cannot be cloned in L.lactis subsp. cremoris strain NZ9000 in the absence of the antitoxin gene; expression in strain NZ9000 even in the presence of antiQ inhibits growth in a bacteriostatic fashion. Confers resistance to 936 and c2 phages but not P335 phages in L.lactis, causes an abortive infection (Abi phenotype). Viral DNA is replicated but not cleaved from its concatemeric form, while the viral major structural protein is produced normally in the presence of this protein. Operon expression in E.coli confers resistance to 3 phages of the Myoviridae family (T4, RB69 and phage 2) and 1 of the Siphoviridae family (T5), but not other tested phages (T1, T3, lambda vir, HK97, Mu and pilH alpha). The presence of this operon in L.lactis subsp. lactis strain IL1403 during phage P008 infection alters the viral transcription profiles.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:9835558}.
Interaction partners:
Sequence:
MSSFFYKEILRMTLRFFTVTDEYIAYLRKFESKVHYQYENNASTYVGVVLKKNDFNYFIPLSSYKKGNPEKDKAMKKRSRIVTRLFEIGNINNPLGYLLHHNMIPVPDSELIPLPLDLKKPKHKMMQKQLIYMKSISEKIENKSEVVYRKAAHEKDGYYLKFSCDFKLLEAKATLYSKKSTFQ
Protein: C2H2-type domain-containing protein (Q8BU41)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKNHTDEKIYKCEDCGRTFYYLSMLKQHQRIHSGEKPYKCEECGKSFSFPSFLKQHQRLHCRKNAFKHEQCVNRFPPPLPLQEHEQIRTEEKPYKCGECYKTFRYHSALRIHKAVHTGERPYKCEECGKCFSSSSCLKKHQILHSEDNPYKCEECYKAFRNHSALRIHKTVHTGERPYKCQECGKCYSSPSCLKRHQILHSKYNPYKCEECGKCLSSSSCLKTHQTLHSEDKPYKCEDCSRCFCSSSSLRRHQKFHSEGNPYKCEKCDKRFSCSAGLQDHQTIHTGEKPYRCENCHKAFCYRSSLRKHKTVHTREKSTHM
Protein: Misshapen, isoform A (Q9W002)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase hemipterous
- Dreadlocks, isoform B
- Apoptotic signal-regulating kinase 1, isoform C
- Thioredoxin-2
Sequence:
MAHQQQQQLAPSVNCSLDDIDLTALKDPAGIFELIEVVGNGTYGQVYKGRHTKTGQLAAIKVMDVTEDEEEEIKLEINVLKKYSNHRNIATYYGAFIKKSPPGKDDQLWLVMEYCGAGSVTDLVKSTKGQSLKEEWIAYICREILRGLSYLHSNKVIHRDIKGQNVLLTDNAEVKLVDFGVSAQLDRTIGRRNTFIGTPYWMAPEVIACDENPDATYDNRSDLWSLGITALEMAESQPPLCDLHPMRALFLIPRNSPPRLKSKKWSKKFHGFIDTVLVKDYHQRPYTENLLKHGFIKDQPTDRQVRIQLKDHIDRCKKRKQEKEREDYRYSGSDNDDDEPQLAGEHSSIVQAPGGDTLRRNFQQIQEGRLAAEQQQQHHLMAQAQAQAAAAHAAAQAQAQLQQQQQQAAAAAAAAAHAAQQAQQAAQQAQAQQPQANRQPKPPSRQQVEEPGPPARPPQRLIVVPDPPHANRPLPPTPKCGEPAGQTPQQQQRNSQNNFKPSLPPRRPEPQPQTAAGGQGSQQQAQPEAPPRNNRQSSGLSSSGGSASGGGGSSKPAAALPQQSNNHLGQPVNPLDPLDSSDSDSEPDEPNDRARNDGTLLASDPPKPLPGLGPVSEDANTTTPLSHGSGGPPNRPLPPTPDDDDQAGDRTLIMKRKLEQNINRLQKSASTSQANVTPSRRGDESNLLRDWDFDRFFPKNANGPRGSGRGSPTTTASLSRSSQLSTLKVDTKLQRASVAEAITRPVPRGYQPLKAEPSASQSIAKEQGSASGSGSGSGSASGSGSGGSTNSPAHKRQDSDSRLPTNFERGFRRENSDFFPLAKRYSAVFSGASASGSTAGSPSAQALQRSSAVYQRNSIYSSSISSKSKENDVPGAPGAAAAGTATASAKPGPAAATTTATKGAAPKTSKSLANFHFLRPRREKTESVIVLQNAAVRAQRLQQLQQQQQQQQLQQQQQQQNRGGGGGGGGGGGGGGSSGVGADGTGLGTPGTRTSSVLPDLLSQASPATPPRHDKSSSEEYQAAISSSVHSTPSKSFIASSGSGGLGLGGGTVVGGVIISSNHSPQSTISLASSSSNSRQNSPKNSISKTRSSSSITNLLHKSASSSSANLHHLTPCSSTSSASISNPLPPHAYALQQKQRSFLTFGFGAGGSGPSRRESHVNVNVTPTSHEAANDTPEIRKYKKRFNSEILCAALWGVNLLIGTENGLMLLDRSGQGKVYQLISRRRFQQMEVLEGQNILVTISGKKNRVRVYYLSWLKSKILRTDGLSDQVERRNGWINVGDLQGAVHFKIVKYERIKFLVIALKDSIEIYAWAPKPYHKFMAFKNFGELEHRPLLVDLTIEDQSRLKVIYGSAEGFHAVDLDSAEVYDIYLPKHTQGAIIPHCIVALPNSNGMQLLLCYDNEGVYVNTVGRVSKNIVLQWGEMPTSVAYIGTGQIMGWGNKAIEIRSVESGHLDGVFMHKKAQRLKFLCERNDKVFFSSAKGASSCQIYFMTLNKPGMANW
Protein: UMP-CMP kinase 1 (EC 2.7.4.14) (Deoxycytidylate kinase 1) (CK 1) (dCMP kinase 1) (Uridine monophosphate/cytidine monophosphate kinase 1) (UMP/CMP kinase 1) (UMP/CMPK 1) (O17622)
Organism: Caenorhabditis elegans
Function: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and CMP as phosphate acceptors.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03172}.
Interaction partners:
- Ribonucleoside-diphosphate reductase large subunit
- dUTP diphosphatase
- Uracil phosphoribosyltransferase homolog
- Uroporphyrinogen-III synthase
- Nucleoside diphosphate kinase
- Uridine kinase
- Uridine 5'-monophosphate synthase
- Probable uridine-cytidine kinase
- Ribonucleoside-diphosphate reductase small chain
- Apyrase apy-1
Sequence:
MYNVVFVLGPPGSGKGTICTQIHENLGYVHLSAGDLLRAERERAGSEYGALIEGHIKNGSIVPVEITCALLENAMIASKDANGFLIDGFPRNEDNWSGWNKQMGGKVNEQFVLFLSCPVDVCIDRCLHRGQGRTDDNVESLKKRVETYNQSTFPIIEHFEKVGMVREVNSERPVTEVYEDVVKVFAAANQK