wanglab/gogpt-training-data huggingface dataset:
Protein: COP9 signalosome complex subunit 3 (Dch3) (Signalosome subunit 3) (Q8SYG2)
Organism: Drosophila melanogaster (Fruit fly)
Function: Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of the SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF. The CSN complex plays an essential role in oogenesis and embryogenesis and is required for proper photoreceptor R cell differentiation and promote lamina glial cell migration or axon targeting. It also promotes Ubl-dependent degradation of cyclin E (CycE) during early oogenesis.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:10531038}. Nucleus {ECO:0000305|PubMed:10531038}.
Interaction partners:
- COP9 signalosome complex subunit 4
- COP9 signalosome complex subunit 2
- COP9 signalosome complex subunit 6
- COP9 signalosome complex subunit 5
- COP9 signalosome complex subunit 8
- COP9 signalosome complex subunit 7
- COP9 signalosome complex subunit 1b
- COP9 signalosome subunit 1a
- Cullin-2
- Ubiquitin-like protein NEDD8
Sequence:
MGSALENYVNQVRTLSASGSYRELAEELPESLSLLARNWSILDNVLETLDMQQHSLGVLYVLLAKLHSASTANPEPVQLIQLMRDFVQRNNNEQLRYAVCAFYETCHLFTEFVVQKNLSILGIRIISRAIDQIRQLETQLTPIHADLCLLSLKAKNFSVVLPYLDADITDISTVAAECKTQQQQQSQHADANNDAKYFLLYFYYGGMIYTAVKNYERALYFFEVCITTPAMAMSHIMLEAYKKFLMVSLIVEGKIAYIPKNTQVIGRFMKPMANHYHDLVNVYANSSSEELRIIILKYSEAFTRDNNMGLAKQVATSLYKRNIQRLTKTFLTLSLSDVASRVQLASAVEAERYILNMIKSGEIYASINQKDGMVLFKDDPEKYNSPEMFLNVQNNITHVLDQVRQINKMEEEIILNPMYVKKALGSQDDDLTSQHPKTFSGDPTD
Protein: Cytosolic phospholipase A2 delta (cPLA2-delta) (EC 3.1.1.4) (Phospholipase A2 group IVD) (Q50L43)
Organism: Mus musculus (Mouse)
Function: Calcium-dependent phospholipase A2 that selectively hydrolyzes glycerophospholipids in the sn-2 position. Compared to its human ortholog, may have no preference for the fatty acid found at the sn-2 position.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:15866882}. Membrane {ECO:0000305|PubMed:15866882}; Peripheral membrane protein {ECO:0000305|PubMed:15866882}; Cytoplasmic side {ECO:0000305|PubMed:15866882}. Note=Translocates to perinuclear membranes that may correspond to endoplasmic reticulum or Golgi in a calcium-dependent fashion. {ECO:0000269|PubMed:15866882}.
Interaction partners:
- Polyunsaturated fatty acid 5-lipoxygenase
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Mitogen-activated protein kinase 3
- Phospholipase A and acyltransferase 3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Arachidonate 12-lipoxygenase, 12R-type
- Polyunsaturated fatty acid lipoxygenase ALOX8
- Mitogen-activated protein kinase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Protein kinase C alpha type
Sequence:
MWSGDRRVGMESLSPERLHGHPYQEEASVFCRLTVKILEARSLPRADLLSQADPYVTVQLPTASGMKFKTQTVTNSSHPVWNETFSFLIQSQVKNILELTIYDEDVITKDDICFKVSYDVSEILPGQLLQKTFSLNPQGPEELDVELLMERTWDPPENLITNNVLVARELSHLDVSLDRAGNTAMAAGQDKLELELMLKGSYEDTQTFFPDTAFTFSFHYMRGQDTELNGYLRGPRNSGWNSDTSVTPFNVPLMSLAAGKEMTIDIPAMKAPEGKLQLKTDCCPKELSVRLSYGLCPEEQAFLSRRKKVVAAALKQALQLDEDLNEDEVPVVGINAEGGGMRAMISLYGHLLALQKLGLLDCVTYFSGISGSTWTMAHLYRDPEWSQRDLEGPISHAREHVAKTLLKEFLPEHLASYRQTLKLREEQGYTVTVADLWGLVLESKLHGQVTDQKLSGQRAALERGQNPLPLYLSLNVKENHLETLHFKEWVEFSPYEVGFLKYGGFVPSELFGSEFFMGRLMKRLPESQICFLEGIWSNLFSVNLMDIWYDITYGKDSNNFPVDVRNSEKEFSGSAGTSSGVEAPWLESGTALAQALKGFLTGRPFHQRSANFLHGLQLHRDYCNQRHFSTWADCNLDDTPNQLTPQDPQLCLIDAGCFMNSSCPSLFRPGRQVDLIISFNYNQSLPFKGLQQSEKYSRARGLPFPRVEPSPEDHSQPQECYLFSDPTCPEAPVVLHFPLVNDSFRDHSAPGVRRSPDELKAGQVNLTGAASPYFMYNMTYKNEDFDRLLQLSDYNVQNNQGTILQALRTVLKRRASETRPLGVKT
Protein: Cytochrome c oxidase subunit 3 (Q2F8Y5)
Organism: Oryza sativa subsp. japonica (Rice)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGVKGGLHTTGAKWFMIESQRHSYHLVDPSPWPISGSLGALATTVGGVMYMHSFQGGATLLSLGLIFLLYTMFVWWRDVLRESTLEGHHTKAVQLGPRYGSILFIVSEVMFLFAFFWASSHSSLAPTVEIGGIWPPKGIGVLDPWEIPLLNTPILPSSGAAVTWAHHAILAGKEKRAVYALVATVSLALVSTGFQGMEYYQAPSTISDSIYGSTFFLATGFHGFHVIIGTLFLIVCGIRQYLGHLTKKHHVGFEAAAWYWHFVDVVRLFPFVSIYWWGGI
Protein: CSC1-like protein HYP1 (HYPOTHETICAL PROTEIN 1) (Q8GUH7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as an osmosensitive calcium-permeable cation channel.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MLLSALLTSVGINLGLCFLFFTLYSILRKQPSNVTVYGPRLVKKDGKSQQSNEFNLERLLPTAGWVKRALEPTNDEILSNLGLDALVFIRVFVFSIRVFSFASVVGIFILLPVNYMGTEFEEFFDLPKKSMDNFSISNVNDGSNKLWIHFCAIYIFTAVVCSLLYYEHKYILTKRIAHLYSSKPQPQEFTVLVSGVPLVSGNSISETVENFFREYHSSSYLSHIVVHRTDKLKVLMNDAEKLYKKLTRVKSGSISRQKSRWGGFLGMFGNNVDVVDHYQKKLDKLEDDMRLKQSLLAGEEVPAAFVSFRTRHGAAIATNIQQGIDPTQWLTEAAPEPEDVHWPFFTASFVRRWISNVVVLVAFVALLILYIVPVVLVQGLANLHQLETWFPFLKGILNMKIVSQVITGYLPSLIFQLFLLIVPPIMLLLSSMQGFISHSQIEKSACIKLLIFTVWNSFFANVLSGSALYRVNVFLEPKTIPRVLAAAVPAQASFFVSYVVTSGWTGLSSEILRLVPLLWSFITKLFGKEDDKEFEVPSTPFCQEIPRILFFGLLGITYFFLSPLILPFLLVYYCLGYIIYRNQLLNVYAAKYETGGKFWPIVHSYTIFSLVLMHIIAVGLFGLKELPVASSLTIPLPVLTVLFSIYCQRRFLPNFKSYPTQCLVNKDKADEREQNMSEFYSELVVAYRDPALSASQDSRDISP
Protein: Centrosomal protein of 170 kDa (Cep170) (Q6A065)
Organism: Mus musculus (Mouse)
Function: Plays a role in microtubule organization. Required for centriole subdistal appendage assembly.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5SW79}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:23386061}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q5SW79}. Note=Associated with the mature mother centriole. Associated with spindle microtubules during mitosis (By similarity). Localizes to the distal appendage region of the centriole (By similarity). Localizes at the centriole proximal ends (By similarity). {ECO:0000250|UniProtKB:Q5SW79, ECO:0000269|PubMed:23386061}.
Interaction partners:
- Centrosomal protein of 128 kDa
- Centriolin
- Ninein
- Coiled-coil domain-containing protein 68
- Coiled-coil domain-containing protein 120
- Kinesin-like protein KIF2A
- Outer dense fiber protein 2
- Kinesin-like protein KIF2B
- Centrosomal protein CCDC61
- Dynactin subunit 1
Sequence:
MSLTSWFLVSSGGTRHRLPREMIFVGRDDCELMLQSRSVDKQHAVINYDASMDEHLVKDLGSLNGTFVNDVRIPEQTYITLKLEDKLRFGYDTNLFTVVRGEMRVPEEALKHEKFTIQLQLSQKSSESELPKSASAKGTDSKVEAAAEVQPRATEALKSEEKPMDVSAMPRGTPLYGQPSWWGDAEEDEQRAFKANGKPEGKSQEAGASGCSTEAKHVEGQSAAASEEALFPFCREPSYFEIPTKEFQQPSQIAESTIHEIPTKDTPSSHTAGAGHASFTIEFDDSTPGKVTIRDHVTKFTSDQRHKSKKASPGTQDLPGIQTGMMAPENKVADWLAQNNPPQMVWERTEEDSKSIKSDVPVYLKRLKGNKHDDGTQSDSENAGAHRRCSKRATLEEHLRRHHSEQKKKAQSTEKHQEQAATSSTHHRGGHGVPHGKLLKQKSEEPSVSLPFLQTALLRSSGSLGHRPSQEMDVMLKNQATSASSEKDNDDDQSDKGTYTIELENPNSEEVEARKMIDKVFGVDDNQDYNRPIINEKHKGLIKDWALNSAAVVMEERKPLSTPGFHNSEEAISSSGSKRWVSQWASLAANHTRHDPEERLMELSATVENETDTGDAGVSLRSTSCTTSLASQGERKRRTLPQLPNEEKLLESSRAKVVPQRSEIGEKQDTELQEKEAQVYQSEKHDADRGLSKMSRAVNGESPKTGGDGKALLHSGSSSSKEKSETEKETSLVKQTLAKMQQQEQKEQAQWTPTKFPSKNALGHIDKCREESSKQESQLLEKVSGHSTSKGDRVIQNESKRRKAEEIPKCQASKGDKKESSKSLVRQGSFTIDKPSSNIPIELIPHINKQNSSVPTALALTSASRLRERSDSLDTDSSMDTTLILKDTEAVMAFLEAKLREDNNKTDEGPDTPSYNRDNSISPESDVDTASTISLVTGETERKSTQKRKSFTSLYKDRCSTSSPSKDVTKSGSREKIEKKAKSRSADIGARADGRKFVQSSGRIRQPSIDLTDDDQTSSVPHSAISDIMSSDQETYSCKSHGRTPLTSADEHNIHSKLEGGKATKSKTSPVASGSTSKSTTLPRPRPTRTSLLRRARLGEASDSELADADKASVASEVSTTSSTSKPPTGRRTISRIDLLAQPRRTRLGSLSARSDSEATISRSSASARTAEAVIRSGARLVPSDKLSPRTRANSISRLSDSKVKSMSSTHGSPSVNSRWRRFPTDYASTSEDEFGSNRNSPKHTRLRTSPALKTTRMQSTGSAMPASSSFKHRIKEQEDYIRDWTAHREEIARISQDLALIAREINDVAGEIDSVTSSGTAPSTTVSTAATTPGSAIDTREEVGDLHGEMHKLVDRVFDESLNFRKIPPLVHSKTPEGNNGRSVDSRPQPAEHPDHLTITRRRTWSRDEVMGDNLLLSSVFQFSRKIRQSIDKTAGKIRILFKDKDRNWDDIENKLRAESEVPIVKTSSMEISSILQELKRVEKQLQVINAMIDPDGTLEALNNMGFPNAILPSPPKQKSSPVNNHSSPSQTPALCPPETRALHPAAAGVAAAASTEFENAESEADFSIHFNRFNPDGEEEDVTVHE
Protein: Cyclin G-associated kinase (Cyclin-G-associated kinase isoform X1) (A0A0R4IWM3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000256|ARBA:ARBA00004132}.
Interaction partners:
Sequence:
MSLFQSALDFLAGPGGSGGAASRDQNDFVGQVVELGELKLRIKRVIAEGGFAFVYEAQDLGSSKDYALKRLLSNEEEKNKAIIQEVCFMKKLSGHPNVVQFCSAASISKEESDTGQAEFLILTELCRGQLVDFVKKVEQKGPMSCDTVLKIFYQSCRAVQHMHKQSPAVIHRDLKIENLLISHQGTIKLCDFGSATTLAHYPDYSWSAHKRSMVEDEITRNTTPAYRTPEMIDLYSNYPINEKQDIWALGCILYLLCFKQHPFEEGAKLQIVNGKYSIPQNDTKYTVFHQLIRSMLKINPEERLSINELVNQLQEIAAARNVNPKSPITELLEQNGGFGNNSAQLPSQINNIHNSGVYDTDPTMGGGFLDILKGGTERFLTNIKDTSSKVIQSVASYAKGDLDLSYITSRLAVMSFPAEGVESAIKNNIEDVRLFLDSRHAGHYAVYNLSKRSYRPARFHNRVSECGWQPRRAPTLKNLYSICKNMHQWLKQDQRNICIVHCLDGRAASAVVVCAFLCFCRLFSTAEAAVYMFSMKRCPPGISASHKRYIEYMCDMMAEEPIIPHSKPITIRSVAMTPVPLFNKQRNGCRPFCEVYVGDERVATTSQEYDRMRDFKMEDGRAEIPLNITVQGDVLIVIYHARSTLGGRLQAKMASMKMFQIQFHTGFVPRNASTVKFAKYDLDACDIQEKYPDLFQVHVNVEVEPQDRPSNKTPPWENFATKGLNPKILFSSRDEQQEILTKFGKPELPRQPGSTACYASDPPQSENSPDDPQTESDSPSPQSTDTNANNFFQTLDWEDTSRHFDHADGHLDDQEDLSGGSEEESVSYSAPIEGTLSRDTSEPLFEADFTNTPPEAQPDTEDLLGLNSEPGPAVPESGLKSSASNSNLLNDLLFAPQTNTVPSASNEDLMGEDAGEDLFFSNSSSQPPPATNKDFFDPFGVGSASSGSDLFGDLLGSDAANSGFKAPAPASNSSLFNLNKLASETPKMTSSASQPDLLSGWDSWATSGTSTTANLSTAANKPSMSASGVSSFSKAKSQSFDPFADLGNLGSTLPGSSSASFSGSGFKTAPSAGGPKNSGQQWQQTPRPSSGPNKPWMPPNSTARPQAVPQAAKPNYNPSFSVIGGRQERGIRGPGFGPKPKVKEDDFEDLLCTQGFGSKPDRKMPRTIAEMRKQELSKDMDPLKLQILDWIEGKERNIRALLSTLHTVLWEGETRWRPINMADLVTPDQVKRVYRKAVLVVHPDKATGQPYEQYAKMIFMELSDAWSEFENQGSKALF
Protein: Protein phosphatase 1A (EC 3.1.3.16) (Protein phosphatase 2C isoform alpha) (PP2C-alpha) (Protein phosphatase IA) (P49443)
Organism: Mus musculus (Mouse)
Function: Enzyme with a broad specificity. Negatively regulates TGF-beta signaling through dephosphorylating SMAD2 and SMAD3, resulting in their dissociation from SMAD4, nuclear export of the SMADs and termination of the TGF-beta-mediated signaling (By similarity). Dephosphorylates PRKAA1 and PRKAA2. Plays an important role in the termination of TNF-alpha-mediated NF-kappa-B activation through dephosphorylating and inactivating IKBKB/IKKB.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P35813}. Cytoplasm, cytosol {ECO:0000269|PubMed:22781750, ECO:0000269|PubMed:23088624}. Membrane {ECO:0000269|PubMed:23088624}; Lipid-anchor {ECO:0000269|PubMed:23088624}. Note=Weakly associates at the membrane and N-myristoylation mediates the membrane localization. {ECO:0000269|PubMed:23088624}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 4
- Dual specificity mitogen-activated protein kinase kinase 7
- Dual specificity mitogen-activated protein kinase kinase 3
- Dual specificity mitogen-activated protein kinase kinase 6
- Mothers against decapentaplegic homolog 2
- Mothers against decapentaplegic homolog 3
- E3 ubiquitin-protein ligase KCMF1
- Protein phosphatase 1B
- Mothers against decapentaplegic homolog 4
Sequence:
MGAFLDKPKMEKHNAQGQGNGLRYGLSSMQGWRVEMEDAHTAVIGLPSGLETWSFFAVYDGHAGSQVAKYCCEHLLDHITNNQDFRGSAGAPSVENVKNGIRTGFLEIDEHMRVMSEKKHGADRSGSTAVGVLISPQHTYFINCGDSRGLLCRNRKVHFFTQDHKPSNPLEKERIQNAGGSVMIQRVNGSLAVSRALGDFDYKCVHGKGPTEQLVSPEPEVHDIERSEEDDQFIILACDGIWDVMGNEELCDFVRSRLEVTDDLEKVCNEVVDTCLYKGSRDNMSVILICFPSAPKVSAEAVKKEAELDKYLESRVEEIIKKQVEGVPDLVHVMRTLASENIPSLPPGGELASKRNVIEAVYNRLNPYKNDDTDSASTDDMW
Protein: DNA topoisomerase 2-alpha (EC 5.6.2.2) (DNA topoisomerase II, alpha isozyme) (Q01320)
Organism: Mus musculus (Mouse)
Function: Key decatenating enzyme that alters DNA topology by binding to two double-stranded DNA molecules, generating a double-stranded break in one of the strands, passing the intact strand through the broken strand, and religating the broken strand. May play a role in regulating the period length of BMAL1 transcriptional oscillation.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P11388}. Nucleus {ECO:0000250|UniProtKB:P11388}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P11388}.
Interaction partners:
- Nucleolar and spindle-associated protein 1
- Cyclin-dependent kinase 1
- Abnormal spindle-like microcephaly-associated protein homolog
- Proliferation marker protein Ki-67
- DNA topoisomerase 1
- Baculoviral IAP repeat-containing protein 5
- Centromere protein F
- Mitotic checkpoint serine/threonine-protein kinase BUB1 beta
- Mitotic checkpoint serine/threonine-protein kinase BUB1
- Kinesin-like protein KIF11
Sequence:
MELSPLQPVNENMLMNKKKNEDGKKRLSIERIYQKKTQLEHILLRPDTYIGSVELVTQQMWVYDEDVGINYREVTFVPGLYKIFDEILVNAADNKQRDPKMSCIRVTIDPENNVISIWNNGKGIPVVEHKVEKIYVPALIFGQLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTKFTVETASREYKKMFKQTWMDNMGRAGDMELKPFSGEDYTCITFQPDLSKFKMQSLDKDIVALMVRRAYDIAGSTKDVKVFLNGNSLPVKGFRSYVDLYLKDKVDETGNSLKVIHEQVNPRWEVCLTMSERGFQQISFVNSIATSKGGRHVDYVADQIVSKLVDVVKKKNKGGVAVKAHQVKNHMWIFVNALIENPTFDSQTKENMTLQAKSFGSTCQLSEKFIKAAIGCGIVESILNWVKFKAQIQLNKKCSAVKHTKIKGIPKLDDANDAGSRNSTECTLILTEGDSAKTLAVSGLGVVGRDKYGVFPLRGKILNVREASHKQIMENAEINNIIKIVGLQYKKNYEDEDSLKTLRYGKIMIMTDQDQDGSHIKGLLINFIHHNWPSLLRHRFLEEFITPIVKVSKNKQEIAFYSLPEFEEWKSSTPNHKKWKVKYYKGLGTSTSKEAKEYFADMKRHRIQFKYSGPEDDAAISLAFSKKQVDDRKEWLTNFMEDRRQRKLLGLPEDYLYGQSTSYLTYNDFINKELILFSNSDNERSIPSMVDGLKPGQRKVLFTCFKRNDKREVKVAQLAGSVAEMSSYHHGEMSLMMTIINLAQNFVGSNNLNLLQPIGQFGTRLHGGKDSASPRYIFTMLSPLARLLFPPKDDHTLRFLYDDNQRVEPEWYIPIIPMVLINGAEGIGTGWSCKIPNFDVREVVNNIRRLLDGEEPLPMLPSYKNFKGTIEELASNQYVINGEVAILDSTTIEISELPIRTWTQTYKEQVLEPMLNGTEKTPSLITDYREYHTDTTVKFVIKMTEEKLAEAERVGLHKVFKLQSSLTCNSMVLFDHVGCLKKYDTVLDILRDFFELRLKYYGLRKEWLLGMLGAESSKLNNQARFILEKIDGKIVIENKPKKELIKVLIQRGYDSDPVKAWKEAQQKVPDEEENEESDTETSTSDSAAEAGPTFNYLLDMPLWYLTKEKKDELCKQRNEKEQELNTLKQKSPSDLWKEDLAVFIEELEVVEAKEKQDEQVGLPGKAGKAKGKKAQMCADVLPSPRGKRVIPQVTVEMKAEAEKKIRKKIKSENVEGTPAEDGAEPGSLRQRIEKKQKKEPGAKKQTTLPFKPVKKGRKKNPWSDSESDVSSNESNVDVPPRQKEQRSAAAKAKFTVDLDSDEDFSGLDEKDEDEDFLPLDATPPKAKIPPKNTKKALKTQGSSMSVVDLESDVKDSVPASPGVPAADFPAETEQSKPSKKTVGVKKTATKSQSSVSTAGTKKRAAPKGTKSDSALSARVSEKPAPAKAKNSRKRKPSSSDSSDSDFERAISKGATSKKAKGEEQDFPVDLEDTIAPRAKSDRARKPIKYLEESDDDDDLF
Protein: DNA-directed RNA polymerase subunit beta (EC 2.7.7.6) (Q4GZE8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerase subunit
- Plastid-encoded RNA polymerase subunit alpha
- DNA-directed RNA polymerase III subunit RPC3
- RNA polymerase III subunit Rpc25 domain-containing protein
- DNA-dependent RNA polymerases, putative
- Probable DNA-directed RNA polymerases I, II, and III subunit RPABC2
Sequence:
MTPRARGCDEGYATRKLALLPALINMKGLLNHHVASFDHLINVELGRILLNESNREIKSSIDPDFSIRYSGIRVCRPREIVGKGQLPKPVSPHECRTRDLTYRGDIVVDVEYTSRDRSKRICTETNIKIGTIPIMLKSSSCNLYGKGREELIAMRECPLDPGGYFIIKGVEKVCLVQEQQSKNRVIIEADDNGDIVAHVQSKTHYSISKCSVTFRKGRIVMVHRSFKEDIPIVVVLKALGMESDQQIAQHIGVSPAFQSVLFACFEHAASLNVKTQDDALHFIGERRKETFWEMDETQQRHVQKSKADSAAEFLANVLLCHIREGEVQRDWNFRHKALYVCFMVRRMVEASVDSSLLDERDFYGNKRFETTGTLMGLLFEDLLKQYNRVVKTAMDQLLSKKDTTKPFNLKQLMESKMEVIQNGMRVALSSGRWELKRFNMSRQGITQVLSRLSYISCIGMMTRLASSFEKSRKISGPRSLQPSQWGMVCPCDTPEGESCGLVKNFAILSQVTLDMDDSFVRAAAYNLGVEEVDCISPNEFLKYYTVFLNGTLMGIHRYPSRLCRGVRTLRRSGRLHPHVSIAINDRQKSVQIGCDGGRIVRLYIVVRDGKPAVTSQHLDNLSSGKCSINDFLAEGLVEFIDVNEANDCLIAVYPKDIEQYTTHLEIEPLSLLGVVAGIIPFPHHNQSARNTFQSAMGKQALGTIAYNQYIRMDTVLMLGAYPQRPLCRTKAMNLTNYEILGAGINAMVCVMSYSGYDIEDAQVYNRSSLDRGYGRCVVLRKHEVELERLPNGEYDIILPADSNVGRHSALNSDGIASKGAVVRQFDILVNKYTPVPSMEPRPNPLVYKYPQPAVVDHVVISPPGDSDRSMDVEQKIKVVTREVRGPEPGDKFSSRHGQKGVVGLITDGVNMPFNEQGICPDMIMNPHGFPSRMTVGKLLELVSSKVSALTGKFGDGTAFGGDKAEDLGEELIRHGYNYHGKDIFYSGVTGEMLRAYVFFGPIYYQRLKHMVTDKMHARATGPRSMLTRQPTEGRSRSGGLRVGEMERDCMVGYGASNLLNERLLVSSDLFTIDICRCCGFMGYNGYCSYCNAKNTVSRVNVPYAFKLLLQELQGMGISTRLSLDFMGSQ
Protein: Tensin 1 (A0A494C067)
Organism: Homo sapiens (Human)
Subcellular location: Cell junction, focal adhesion {ECO:0000256|ARBA:ARBA00004246}.
Interaction partners:
Sequence:
KTFKKVKPCGICRQVITQEGCTCKVCSFSCHRKCQAKVAAPCVPPSNHELVPITTENAPKNVVDKGEGASRGGNTRKSLEDNGSTRVTPSVQPHLQPIRNMSVSRTMEDSCELDLVYVTERIIAVSFPSTANEENFRSNLREVAQMLKSKHGGNYLLFNLSERRPDITKLHAKVLEFGWPDLHTPALEKICSICKAMDTWLNADPHNVVVLHNKGNRGRIGVVIAAYMHYSNISASADQALDRFAMKRFYEDKIVPIGQPSQRRYVHYFSGLLSGSIKMNNKPLFLHHVIMHGIPNFESKGGCRPFLRIYQAMQPVYTSGIYNIPGDSQTSVCITIEPGLLLKGDILLKCYHKKFRSPARDVIFRVQFHTCAIHDLGVVFGKEDLDDAFKDDRFPEYGKVEFVFSYGPEKIQGMEHLENGPSVSVDYNTSDPLIRWDSYDNFSGHRDDGMEEVVGHTQGPLDGSLYAKVKKKDSLHGSTGAVNATRPTLSATPNHVEHTLSVSSDSGNSTASTKTDKTDEPVPGASSATAALSPQEKRELDRLLSGFGLEREKQGAMYHTQHLRSRPAGGSAVPSSGRHVVPAQVHVNGGALASERETDILDDELPNQDGHSAGSMGTLSSLDGVTNTSEGGYPEALSPLTNGLDKSYPMEPMVNGGGYPYESASRAGPAHAGHTAPMRPSYSAQEGLAGYQREGPHPAWPQPVTTSHYAHDPSGMFRSQSFSEAEPQLPPAPVRGGSSREAVQRGLNSWQQQQQQQQQPRPPPRQQERAHLESLVASRPSPQPLAETPIPSLPEFPRAASQQEIEQSIETLNMLMLDLEPASAAAPLHKSQSVPGAWPGASPLSSQPLSGSSRQSHPLTQSRSGYIPSGHSLGTPEPAPRASLESVPPGRSYSPYDYQPCLAGPNQDFHSKSPASSSLPAFLPTTHSPPGPQQPPASLPGLTAQPLLSPKEATSDPSRTPEEEPLNLEGLVAHRVAGVQAREKQPAEPPAPLRRRAASDGQYENQSPEATSPRSPGVRSPVQCVSPELALTIALNPGGRPKEPHLHSYKEAFEEMEGTSPSSPPPSGVRSPPGLAKTPLSALGLKPHNPADILLHPTGEEDEGKVVVRLSEEPRSYVESVARTAVAGPRAQDSEPKSFSAPATQAYGHEIPLRNGTLGGSFVSPSPLSTSSPILSADSTSVGSFPSGESSDQGPRTPTQPLLESGFRSGSLGQPSPSAQRNYQSSSPLPTVGSSYSSPDYSLQHFSSSPESQARAQFSVAGVHTVPGSPQARHRTVGTNTPPSPGFGWRAINPSMAAPSSPSLSHHQMMGPPGTGFHGSTVSSPQSSAATTPGSPSLCRHPAGVYQVSGLHNKVATTPGSPSLGRHPGAHQGNLASGLHSNAIASPGSPSLGRHLGGSGSVVPGSPCLDRHVAYGGYSTPEDRRPTLSRQSSASGYQAPSTPSFPVSPAYYPGLSSPATSPSPDSAAFRQGSPTPALPEKRRMSVGDRAGSLPNYATINGKVSSPVASGMSSPSGGSTVSFSHTLPDFSKYSMPDNSPETRAKVKFVQDTSKYWYKPEISREQAIALLKDQEPGAFIIRDSHSFRGAYGLAMKVSSPPPTIMQQNKKGDMTHELVRHFLIETGPRGVKLKGCPNEPNFGSLSALVYQHSIIPLALPCKLVIPNRDPTDESKDSSGPANSTADLLKQGAACNVLFVNSVDMESLTGPQAISKATSETLAADPTPAATIVHFKVSAQGITLTDNQRKLFFRRHYPLNTVTFCDLDPQERKWMKTEGGAPAKLFGFVARKQGSTTDNACHLFAELDPNQPASAIVNFVSKVMLNAGQKR
Protein: 28S rRNA (cytosine-C(5))-methyltransferase (EC 2.1.1.-) (NOL1/NOP2/Sun domain family member 5) (Williams-Beuren syndrome chromosomal region 20A protein homolog) (Q8K4F6)
Organism: Mus musculus (Mouse)
Function: S-adenosyl-L-methionine-dependent methyltransferase that specifically methylates the C(5) position of cytosine 3438 (m5C3438) in 28S rRNA. m5C3782 promotes protein translation without affecting ribosome biogenesis and fidelity (By similarity). Required for corpus callosum and cerebral cortex development.
Subcellular location: Nucleus, nucleolus {ECO:0000250|UniProtKB:Q96P11}.
Interaction partners:
- 5-cytosine rRNA methyltransferase NSUN4
- tRNA N
- tRNA
- 18S rRNA
- Nucleolar complex protein 4 homolog
- WD repeat-containing protein 74
- Nucleolar complex protein 2 homolog
- Probable rRNA-processing protein EBP2
- Methionyl-tRNA formyltransferase, mitochondrial
- Suppressor of SWI4 1 homolog
Sequence:
MGLYAAAAAVLAGVESRQGSLKGLVYSSNFQNLKQLYALVCETQRYSAVLDAVIASAGLLRAEKKLRPHLAKVLVYELLLGKGFRGGGGRWKALLGRHQARLKAELARLKVHRGVSRNEDLLQESSRPGQAYQVPRFVRVNTLKTRPEDAIDYFKRQGFSYQGRASSLEDLRALKGQHFLLDPLLPELLVFPAQTDLHEHPLYRAGHLILQDKASCLPAMLLSPPPGSHVIDACAAPGNKTSYIAALLKNQGKIFAFDQDAKRLAAMATLVARAGVSCCELAEKDFLTVSPSDQRYSQVQYILLDPSCSGSGMLSRQLEEHGEGTPSKERLQALAGFQQRALCHALRFPSLQRLVYSTCSLCQEENEDVVQEALQHNSGTFRLAPVLPTWPHRGLSTFPGSEHCLRASPETTLTGGFFIAVFERAEVVPTPAPQTDAMDPEPLSQVPKRKRRRKAAVGASMQPST
Protein: 6-aminohexanoate-oligomer endohydrolase (EC 3.5.1.117) (6-aminohexanoate oligomer hydrolase) (Ahx endo-type-oligomer hydrolase) (Nylon hydrolase) (Nylonase) [Cleaved into: 6-aminohexanoate-oligomer endohydrolase alpha subunit; 6-aminohexanoate-oligomer endohydrolase beta subunit] (Q1EPR4)
Organism: Kocuria sp. (strain KY2)
Function: Involved in the degradation of nylon-6 oligomers. Degrades cyclic and linear oligomers of 6-aminohexanoate (Ahx) with a degree of polymerization greater than three by an endo-type mode. Cannot use Ahx cyclic dimer or the Ahx linear dimer.
Interaction partners:
Sequence:
MNTTPVHALTDIDGGIAVDPAPRLAGPPVFGGPGNAAFDLVPVRSTGRETLRFDFPGVSVGSAHYEEGPTGATVIHIPAGARTAVDARGGAVGLSGGYDFNHAICLAGGASYGLEAGAGVSGALLERLEYRTGFAEAQLVSSAVIYDFSARSTAVYPDKALGRAALEFAVPGEFPQGRAGAGMSASAGKVDWDRTEITGQGAAFRRLGDVRILAVVVPNPVGVIMDRAGGIVRGNYDAQTGVRRHPVFDYQEAFAEQLPPVTQAGNTTISAIVTNVRMSPVELNQFAKQVHSSMHRGIQPFHTDMDGDTLFAVTTDEIDLPTTPGSSRGRLSVNATALGAIASEVMWDAVLEAAK
Protein: Ecm22p (Q59KX3)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MGDSPPLTDIRSQFSTSLSYSSTQNQNEMSSNKSRSNSQLPKSQIKSSMSQLLLSENPLTSDEQAILSKSLNKSKRKSVAKNTTTNNNNNDNSNSAPKELGKKSKRRKHKNSKLGCANCKERRVKCLENLPSCTNCIKHRVKCAYLDYTEDQLNEFKKAKILQEQQEQQQEQQQEQEQQSDQETNNQQLLKTNKKVLKPKKSRTVPSFSFGRASSNPSVPSVSATGTSTSFTNQELLQQQRQHHSVPNIGTNFNTMALSSSSSSSQASSVVADDEVVEPSPVPRSNNESRVNLLPEGNDFQILFPAYPDTADFPPTTTPSRFSTPLARSAVSTAFDSKNHQSQSTSSNSLPNALNVPVNFKYTPHPVVDYDARLKELLKVIGPMILKGTSGLSQIRDIYSTWLNSFIYKAFTSDLMFYCLLNLTTNFLITNCFCDSNKYLQNSGSLTPNSRSLQLARIRTDCTNRSLQYYAYTIKGLGKVLNDESTDPDLTGSVSYILSLMSVYDTQATLNSIICFRNGLFSIFKHNDIAYEKIDPNSKVLIPTHKKLMVNIVMSIYLPGYDSHFLKEYQQLLTRFGELIFPLLHHYNSTNSGAVAPEMVSFVESNYNHLLSFTNDCLNHYISEINNTLSDINSQEELLFQMIYRWVRFFPARLIGSRKKSDPLEKMLYLFYKVFKKALFAIFPQVKFFFLRDFDSPLMLDVFASDNDYDIFVEELEHPINNCLPPELYEPILNELKSMSSYLIRVITYLQLRLNKLYKYLVVDSGIDRMKQIHADILQWGNSISDITKTRNEFKQLLGLEEVCVTSFIDKVIKQENYPSRTGEPKTAKVEHPLGTGTNIIDFMTLQPSGLLINDFDPRQ
Protein: dTDP-4-dehydrorhamnose reductase (EC 1.1.1.133) (dTDP-4-keto-L-rhamnose reductase) (dTDP-6-deoxy-L-lyxo-4-hexulose reductase) (dTDP-6-deoxy-L-mannose dehydrogenase) (dTDP-L-rhamnose synthase) (P37760)
Organism: Escherichia coli (strain K12)
Function: Involved in the biosynthesis of the dTDP-L-rhamnose which is an important component of lipopolysaccharide (LPS) (Probable). Catalyzes the reduction of dTDP-6-deoxy-L-lyxo-4-hexulose to yield dTDP-L-rhamnose (By similarity). RmlD uses NADH and NADPH nearly equally well (By similarity).
Interaction partners:
- Glucose-1-phosphate thymidylyltransferase 1
- dTDP-glucose 4,6-dehydratase 1
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Glucose-1-phosphate thymidylyltransferase 2
- dTDP-glucose 4,6-dehydratase 2
- Putative O-antigen transporter
- UDP-galactopyranose mutase
- Phosphomannomutase
- UDP-glucose:undecaprenyl-phosphate glucose-1-phosphate transferase
- Putative O-antigen polymerase
Sequence:
MNILLFGKTGQVGWELQRALAPLGNLIAFDVHSTDYCGDFSNPEGVAETVRSIRPDIIVNAAAHTAVDKAESEPEFAQLINATSVEAIAKAANEVGAWVIHYSTDYVFPGNGDMPWLETDATAPLNVYGETKLAGEKALQEYCAKHLIFRTSWVYAGKGNNFAKTMLRLAKEREELAVINDQFGAPTGAELLADCTAHAIRVALNKPDVAGLYHLVASGTTTWYDYAALVFEEARKAGIPLALNKLNAVPTTAYPTPARRPHNSRLNTEKFQQNFALVLPDWQVGVKRMLNELFTTTAI
Protein: Pre-mRNA-splicing factor prp12 (Pre-mRNA-processing protein 12) (Spliceosome-associated protein 130) (Q9UTT2)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in mRNA splicing and G2/M transition.
Subcellular location: Nucleus {ECO:0000269|PubMed:11350031}.
Interaction partners:
- Pre-mRNA-splicing factor sap61
- Pre-mRNA-splicing factor sap145
- Pre-mRNA-splicing factor ini1
- Pre-mRNA-splicing factor cdc5
- Pre-mRNA-splicing factor prp1
- Pre-mRNA-splicing factor sap62
- Uncharacterized protein C211.05
- U2 snRNP component prp10
- Splicing factor 3B subunit 6-like protein
- U2 small nuclear ribonucleoprotein A'
Sequence:
MDTFPSLFLYSLTIQNSNYVQSSCAASLSGKKAQEIVIATESRLLIYKVDATDGRMNCILNQNCFGIIRNVAPLRLTGFKRDYLVVTSDSGRITILEYNVEKNKLVPIYQETFGKSGIRRVVPGEYLAIDAKGRAAMIASVEKNKLVYVLNRDSEANLTISSPLEAHKANNICFHLIGLDTGYANPIFAALEVDYSEIDHDSTREAFTSSEKVLSYYELDLGLNHVVKRWSKVVDRNSYMLIPVPGGNDGPSGTLVISNGWISYRHLQKAFHQIPILRRQAASANAISTPWNQVNSNSANDGPLIVSAVLHKMKGSFFYLLQTGDGDLLKLTIEHDGQGNVVELRLKYFDTVPLAVQLNILKTGFLFVATEFGNHQLYQFENLGIDDDELEITSLDFQAQDNEVGTKNVHFGVRGLQNLSLVEEIPSLYSLTDTLLMKAPSSGEANQLYTVCGRGSNSSLRQLRRGLETTEIVASELPGAPIAIWTLKLNQTDVYDSYIILSFTNGTLVLSIGETVEEISDSGFLSSVSTLNARQMGRDSLVQIHPKGIRYIRANKQTSEWKLPQDVYVVQSAINDMQIVVALSNGELVYFEMSDDVEGGQLNEYQERKTLTANVTSLALGPVQEGSRRSNFMCLACDDATVRVLSLDLYTTLENLSVQALSSPANSLCIIPMNVNGVSTLYLHIGLMNGVYLRTVIDVTSGQLLDTRTRFLGPRAVKIYPITMKNQNTVLAVSSRTFLAYSYQQNLQLSPIAYSAIDHASSFASEQCPEGIVAIQKNTLKIFTVDSLQDDLKSDIYPLICTPRKIVKHPNFPVLYILQSERNFDSFKYAQENGDVGSSYTKEKQNEHTSKSWVSFISVFDMISKKIIHESPLGDNEAAFSMTAAFFKNRDEFFLVAGSATNMDLECRTCSHGNFRVYRFHDEGKKLELISHTEIDGIPMALTPFQGRMLAGVGRFLRIYDLGNKKMLRKGELSAVPLFITHITVQASRIVVADSQYSVRFVVYKPEDNHLLTFADDTIHRWTTTNVLVDYDTLAGGDKFGNIWLLRCPEHVSKLADEENSESKLIHEKPFLNSTPHKLDLMAHFFTNDIPTSLQKVQLVEGAREVLLWTGLLGTVGVFTPFINQEDVRFFQQLEFLLRKECPPLAGRDHLAYRSYYAPVKCVIDGDLCEMYYSLPHPVQEMIANELDRTIAEVSKKIEDFRVRSF