wanglab/gogpt-training-data huggingface dataset:
Protein: 17-beta-hydroxysteroid dehydrogenase type 6 (17-beta-HSD 6) (17-beta-HSD6) (EC 1.1.1.105) (EC 1.1.1.209) (EC 1.1.1.239) (EC 1.1.1.53) (EC 1.1.1.62) (17-beta-HSD9) (3-alpha->beta-hydroxysteroid epimerase) (3-alpha->beta-HSE) (Oxidative 3-alpha hydroxysteroid dehydrogenase) (Q9R092)
Organism: Mus musculus (Mouse)
Function: NAD-dependent oxidoreductase with broad substrate specificity that shows both oxidative and reductive activity (in vitro). Has 17-beta-hydroxysteroid dehydrogenase activity towards various steroids (in vitro). Converts 5-alpha-androstan-3-alpha,17-beta-diol to androsterone and estradiol to estrone (in vitro). Has 3-alpha-hydroxysteroid dehydrogenase activity towards androsterone (in vitro). Has retinol dehydrogenase activity towards all-trans-retinol (in vitro).
Subcellular location: Microsome membrane {ECO:0000269|PubMed:10537158}; Peripheral membrane protein {ECO:0000269|PubMed:10537158}; Lumenal side {ECO:0000269|PubMed:10537158}. Early endosome membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Lumenal side {ECO:0000305}.
Interaction partners:
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- Steroid 17-alpha-hydroxylase/17,20 lyase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1
- 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 2
- Polyprenal reductase
- (3R)-3-hydroxyacyl-CoA dehydrogenase (17-beta-hydroxysteroid dehydrogenase 8) (17-beta-HSD 8) (KAR alpha subunit) (Estradiol 17-beta-dehydrogenase 8) (Protein Ke6) (Ke-6) (Testosterone 17-beta-dehydrogenase 8)
- 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7
- 17-beta-hydroxysteroid dehydrogenase type 1
- NADPH-dependent 3-keto-steroid reductase Hsd3b5
Sequence:
MWFYLVTLVGLYHLLRWYRERQVVSHLQDKYVFITGCDSGFGNLLARQLDRRGMRVLAACLTEKGAEELRNKTSDRLETVILDVTKTESIVAATQWVKERVGDRGLWGLVNNAGVLQPFAYIEWYRPEDYMPIFQVNLIGLTQVTISMLFLVKKARGRIVNVSSALGRVALFGGFYSCSKYGVEAFSDVLRHEVQDFGVKVSIIEPGSFKTEMTDAELTIERTKKVWEAAPEHIKESYGQQFFDDFCSTTKRELMKCSRNLSLVTDCMEHALTSTHPRTRYSAGWDAKFFFIPLSYLPASLVDYLLAISRGKPAQAA
Protein: At3g23190 (HR-like lesion-inducing protein) (Q9LTC9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- HR-like lesion-inducing protein-like protein
- Shaggy-related protein kinase epsilon
- At2g32380
- T12C22.21 protein
Sequence:
MEKTQESVVRYGKKIEKMPYLMPAGRVVFASAFLVSAWREYYGFGLAADELRPKLGFFENQAKAIVALGILMKFVGGILFIFNTYVGAALLLVYQAILSPILYDFYNRDYDRDHFTVFYTKFKEFVEETTSADGGVAMSLYTSVVNEESRQKFIDQLNEIARIAISNPLFTPSDFNTLFIRFIKGVGIAAALACFIAMKHRHAVLIEKTSKKQKTN
Protein: Neuronal acetylcholine receptor subunit alpha-7 (nAChR7) (Nicotinic acetylcholine receptor subunit alpha-7) (P36544)
Organism: Homo sapiens (Human)
Function: After binding acetylcholine, the AChR responds by an extensive change in conformation that affects all subunits and leads to opening of an ion-conducting channel across the plasma membrane. The channel is blocked by alpha-bungarotoxin.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q05941}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:27789755}; Multi-pass membrane protein {ECO:0000255}. Note=TMEM35A/NACHO promotes its trafficking to the cell membrane (PubMed:27789755). RIC3 promotes its trafficking to the cell membrane (By similarity). {ECO:0000250|UniProtKB:Q05941, ECO:0000269|PubMed:27789755}.
Interaction partners:
- CHRNA7-FAM7A fusion protein
- Neuronal acetylcholine receptor subunit alpha-2
- Neuronal acetylcholine receptor subunit alpha-4
- Neuronal acetylcholine receptor subunit beta-4
- Neuronal acetylcholine receptor subunit beta-2
- Neuronal acetylcholine receptor subunit alpha-9
- Neuronal acetylcholine receptor subunit alpha-3
- Acetylcholine receptor subunit epsilon
- Neuronal acetylcholine receptor subunit beta-3
- Neuronal acetylcholine receptor subunit alpha-6
Sequence:
MRCSPGGVWLALAASLLHVSLQGEFQRKLYKELVKNYNPLERPVANDSQPLTVYFSLSLLQIMDVDEKNQVLTTNIWLQMSWTDHYLQWNVSEYPGVKTVRFPDGQIWKPDILLYNSADERFDATFHTNVLVNSSGHCQYLPPGIFKSSCYIDVRWFPFDVQHCKLKFGSWSYGGWSLDLQMQEADISGYIPNGEWDLVGIPGKRSERFYECCKEPYPDVTFTVTMRRRTLYYGLNLLIPCVLISALALLVFLLPADSGEKISLGITVLLSLTVFMLLVAEIMPATSDSVPLIAQYFASTMIIVGLSVVVTVIVLQYHHHDPDGGKMPKWTRVILLNWCAWFLRMKRPGEDKVRPACQHKQRRCSLASVEMSAVAPPPASNGNLLYIGFRGLDGVHCVPTPDSGVVCGRMACSPTHDEHLLHGGQPPEGDPDLAKILEEVRYIANRFRCQDESEAVCSEWKFAACVVDRLCLMAFSVFTIICTIGILMSAPNFVEAVSKDFA
Protein: Prohibitin (C9JW96)
Organism: Homo sapiens (Human)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|RuleBase:RU366048}.
Interaction partners:
Sequence:
MAAKVFESIGKFGLALAVAGGVVNSALYNVDAGHRAVIFDRFRGVQDIVVGEGTHFLIPWVQKPIIFDCRSRPRNVPVITGSKDLQNVNITLRILFRPVASQLPRIFTSIGEDYDERVLPSITTEILKSVVARFDAGELITQRELVSRQVSDDLTERAATFGLILDDVSLTHLTFGKEFTEAVEAKQVAQQEAERARFVVEKAEQQKKAAIISAEGDSKAAELIANSLATAGDGLIELRKLEAAED
Protein: Macrophage receptor with collagenous structure (M0R9F7)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MGSKETLKEEAFLGSTEDGADFDQDMLPVMETFEINDPVPKKRNGRTLCMAVMAIHLILLTAGTALLLIQVLNLQEQFQSLEMCCDNGTLAAEDKPFFSLQWARPKTHIVSGAQGLQALQAQLSWVHTSQEQLRQQVDNLTQNPELFRIKGERGSPGPKGAPGAPGIPGLPGPSAAKGEKGAAGRDGTPGVRGPQGPPGTKGEAGLQGFTGAPGKQGADGAPGPQGEKGSKGDKGLTGPKGEHGTKGDKGDLGLPGSKGDTGMKGDRGVTGSPGAQGNKGDAGKPGLPGLAGSPGAKGDQGKLGVQGPPGPPGAPGQSGAKGEPGRTGPPGPTGPPGIAGNPGAAGLKGSKGDIGIQGQKGTKGESGVPGLVGRKGDTGSPGLAGPKGEPGRAGLKGEPGMKGSSGQQGQKGEKGQKGDFNLVVRIVGGTSRGRAEVYYNNVWGTICDDGWDNNDATVFCRMLGYSSGRGLGSFGGGTGKIWLDDVSCLGTEATLWDCRKSSWGSHNCNHNEDAGVECR
Protein: Rolling pebbles, isoform B (Q9VTS9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Postsynapse {ECO:0000256|ARBA:ARBA00034110}.
Interaction partners:
- Kin of irre, isoform A
- Dumpy, isoform Q
- Protein unc-119 homolog
- Titin
- Myoblast city, isoform B
- Sticks and stones, isoform B
Sequence:
MPSLQQIALAMEGDQSELQTPPLPINPPPKVMANGIVYGFRTRHLSCIEENDSDSLHGSSIPHAYDMMQQADETFQKLNANEEQDESGSEDGGLENLDDTIAMIDESRLLEADYLDELVAEEQLQEQDEDEEESSDLVDSGNVEEDFWQPSFNRNDIMMTSVYGALNGSLTSEVSSTAAPGYSECATPRKEAEPVYATPEKRRASNRSFDSTCASLTSSLYGGSMNSSLDLKYSSLGGGDSVSGGISGTSTLRGTSVPPMDLSMISSDGVSALDWGSASVSCVLDSGDGNPAEELNEEMAAKCLSAAESDLQSIRRLLEHDASGSVCPSCRISFDKGKRRKLIDTCGHERCYSCMFRNDQCPMCMNSSLKDVDGANAQGYDTGIGGSTSTIVSPLGSPQPQLRSHAQRNAALARYMQQHRQESQSPDYHHRYASNGKLPRAAALSTNGNGFTTGTTQTVTVDVHHQLGGGGGGAAAAAKQLMANGISGHSRSSSMSHNIHAAAYSELSAAPPAFATPPTRRRFFNHKNLRSALTGGSGGGSGVGGGVGGAGGVGGGHRRTASNGGCPIDTASILSGDHTHQHHHRDNQPEGKESNALNTSTCSDSAVTRRRRKNVSNHNLKTSARHGASSENRLNRLSLAGTSVYAGHLSSLVFGKIKSLWSVNSSNSSEAGLNQLAGSDAIDHHSSFLNEKLQKDQLHARLGLLLNDPGSNGNSSSSGSGCEPISAHSTTSTTSSSGVGAASTTTSGSSQNVSPEQTLASGAGMLSGSQLSVATSHGVKEDALSLCGKFKAGCSMLHVYEALPSKSRKGNVRRSTRGQQGSSSSASAASAVGSRVTASSLAAVQLALKPLFFEVPLQEPDPPYVGRQWLVQQLSNILLGTETRVVLINGQPGTGKTAFCLQLVEYSCFGRRQMQDDPDGIYSQLQLGAHCERMRGLASHMVGYHFCQADANLTCQVPDFVHSLAAQLCQAPQLTAYRDYLLSEPHLQDILSVRECIADAERVMKLAILEPLAHLHRAGKIPAKVAVIVVDALCEAEYHRPDHGHTIASFLAQLTPHFPAWLKLVATVRTQMLELVKAPSYTQLTLDSWASSQALQQDMLDYIGARLADSPEIRMNIGGGGGQNSQSGSQPQTKFVSHLQSLSRGSMLYAKLILDLIARGQLVIKSSSYKVLPVSLAQIFLLHFNLRFPTARSFEQAAPILNICLAALYPLTLDEIYYSMEALSHGREALSWPDFMQRFKLLDGFLIKRLDNTYMFFHSSLREWLMRRDEGESNKFLCDARLGHAGIAFRLSRLQAPLSPQLTLELGHHMLKAHLYGGTSLTLLSPRDLQSYWLAGAADNISSSLGALRNVYSPNLKVSRLVLLAGASPNHRTDYMGGAPILCIAAHEGILPMVSLLLEFGADVGLTNSQGCTPLILAAMRGHCDVVRPLVAAGSSLGQLDITQRCALVHAARMGHLSVVKYLLACDWSPRPHSQDVTRSVALQQALIGAAAQAHCKILEDLLDLNETEFDLDVNGMEPSSGELALTAAARHGCIDVVGILLSRGAQIDARNRQGYSALWLAVKEGHWSVVEHLLQRGALLDEPLGQTRKTPLMIAAEEGHLELVDLLLARGAQREAQDHEGFTALSWACLRGHLAAAKTLIEHGCNRHHEDHNGRTALDLAAYQGAASLVIYILEQGGNLEHIDVHGMRPLDRAIACRNIQAVQVFLRKGAKLGPTTWSMAMGKPEILVILLNKLLEDGNVLYRKNRFQEAAHRYQYALRKISGLEQLLERNAIFAQLRTNLLLNLSRCKRKLNELDASIDLATQAIAQKPHSYEGYYARAKARMELGALNEALVDANEAMQQAAQSGVLCEVVEVLKRIQTELLTRISISSEDQTGRMSNIGGGASVAYESHHEITDL
Protein: ATP-dependent DNA helicase 2 subunit KU80 (EC 3.6.4.12) (ATP-dependent DNA helicase 2 subunit 2) (ATP-dependent DNA helicase II 80 kDa subunit) (Q9FQ09)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Single-stranded DNA-dependent ATP-dependent helicase. Involved in DNA non-homologous end joining (NHEJ) required for double-strand break repair. When associated with KU70, binds to double-stranded telomeric and non-telomeric DNA sequences, but not to single-stranded DNA. Plays a role in maintaining telomere length. Acts as a negative regulator of telomerase. Binds to and recombines double-stranded T-DNA molecules.
Subcellular location: Nucleus {ECO:0000269|PubMed:12148535}. Cytoplasm {ECO:0000269|PubMed:12148535}. Note=Predominantly in the nucleus.
Interaction partners:
- ATP-dependent DNA helicase 2 subunit KU70
- DNA ligase 4
- DNA ligase 6
- DNA repair protein XRCC4
- Double-strand break repair protein MRE11
- Telomerase reverse transcriptase
- DNA ligase 1
- DNA ligase
- DNA polymerase lambda
- Chlorophyll a-b binding protein 3, chloroplastic
Sequence:
MARNREGLVLVLDVGPAMRSVLPDVEKACSMLLQKKLIYNKYDEVGIVVFGTEETGNELAREIGGYENVTVLRNIRVVDELAAEHVKQLPRGTVAGDFLDALIVGMDMLIKMYGNAHKGKKRMCLITNAACPTKDPFEGTKDDQVSTIAMKMAAEGIKMESIVMRSNLSGDAHERVIEENDHLLTLFSSNAIAKTVNVDSPLSLLGSLKTRRVAPVTLFRGDLEINPTMKIKVWVYKKVAEERLPTLKMYSDKAPPTDKFAKHEVKVDYDYKVTAESTEVIAPEERIKGFRYGPQVIPISPDQIETLKFKTDKGMKLLGFTEASNILRHYYMKDVNIVVPDPSKEKSVLAVSAIAREMKETNKVAIVRCVWRNGQGNVVVGVLTPNVSERDDTPDSFYFNVLPFAEDVREFPFPSFNKLPSSWKPDEQQQAVADNLVKMLDLAPSAEEEVLKPDLTPNPVLQRFYEYLELKSKSTDATLPPMDGTFKRLMEQDPELSSNNKSIMDTFRGSFEVKENPKLKKASKRLLRDKPSGSDDEDNRMITYDAKENKIDIVGDANPIQDFEAMISRRDKTDWTEKAITQMKNLIMKLVENCTDEGDKALECVLALRKGCVLEQEPKQFNEFLNHLFKLCQERNLSHLLEHFMSKKITLIPKSEAADSDIVDENAGDFIVKQESMLES
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase eta-2 (EC 3.1.4.11) (Phosphoinositide phospholipase C-eta-2) (Phosphoinositide phospholipase C-like 4) (PLC-L4) (Phospholipase C-like protein 4) (Phospholipase C-eta-2) (PLC-eta2) (A2AP18)
Organism: Mus musculus (Mouse)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal network in the postnatal brain.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15899900}. Cell membrane {ECO:0000269|PubMed:15899900}. Note=Localized predominantly at the plasma membrane. {ECO:0000269|PubMed:15899900}.
Interaction partners:
- Inositol polyphosphate multikinase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Multiple inositol polyphosphate phosphatase 1
- Inositol polyphosphate-5-phosphatase A.
- Phosphatidylinositol 4,5-bisphosphate 5-phosphatase A
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Inositol-trisphosphate 3-kinase A
- Type II inositol 1,4,5-trisphosphate 5-phosphatase
- Phosphatidylinositol 4-phosphate 5-kinase-like protein 1
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Sequence:
MGGLAWGPSRAAGSSWVNASGTWEQPLRGFSGLQGGRRRGRGEKGIPEEPLCQLTPQLGLSLRVPFGLGDYGLDMPGPQPSAASQTTGAVACLAEVLLWVGGSVVVSPRWQLSLVVERCMSAMQEGTQMVKLRGSSKGLVRFYYLDEHRSCLRWRPSRKNEKAKISIDSIQEVSEGRQSEIFQRYPDSSFDPNCCFSIYHGSHRESLDLVSPSSEEARTWVTGLRYLMAGISDEDSLARRQRTRDQWLKQTFDEADKNGDGSLSISEVLQLLHKLNVNLPRQRVKQMFREADTDDHQGTLGFEEFCAFYKMMSTRRDLYLLMLTYSNHKDHLDASDLQRFLEVEQKMNGVTLESCQNIIEQFEPCLENKSKGMLGIDGFTNYTRSPAGDIFNPEHNRVHQDMTQPLSHYFITSSHNTYLVGDQLMSQSRVDMYAWVLQAGCRCVEVDCWDGPDGEPIVHHGYTLTSKILFKDVIETINKYAFIKNEYPVILSIENHCSVVQQKKMAQYLTDILGDKLDLSSVSSEDATMLPSPQMLKGKILVKGKKLPANISEDAEEGEVSDEDSADEMEDDCKLLNGDASTNRKRVENIAKKKLDSLIKESKIRDCEDPNDFSVSTLSPSGKLGRKAEAKKGQSKVEEDVEAGEDSGVSRQNSRLFMSSFSKRKKKGSKIKKVASVEEGDETLDSPGSQSRGTARQKKTMKLSRALSDLVKYTKSVGTHDVEIEVVSSWQVSSFSETKAHQILQQKPTQYLRFNQHQLSRIYPSSYRVDSSNYNPQPFWNAGCQMVALNYQSEGRMLQLNRAKFSANGDCGYVLKPQCMCQGVFNPNSEDPLPGQLKKQLALRIISGQQLPKPRDSVLGDRGEIIDPFVEVEVIGLPVDCSKEQTRVVDDNGFNPMWEETLVFTVHMPEIALVRFLVWDHDPIGRDFIGQRTLAFSSIMPGYRHVYLEGMEEASIFVHVAVSDISGKVKQTLGLKGLFLRGTKPGSLDSHAAGQPLPRPSVSQRLLRRTASAPTKSQKPSRKGFPELALGTQDAGSEGAADDVAPSSPNPALEAPTQERSGSSSPRDTRLFPLQRPISPLCSLEPIAEEPALGPGLPLQAAAPTGPSQEGSQCPVGLGAKVTSSQQTSLGAFGTLQLRIGGGRENEEPPLRPHNGGISSGPREGTSGRQTDSKSRSRVPGHLPVVRRAKSEGQVLSELSPTPAVYSDATGTDRLWQRLEPGSHRDSVSSSSSMSSNDTVIDLSLPSLGLCRSRESIPGVSLGRLTSRPCLASAARPDLPPVTKSKSNPNLRVAGGLPTAPDELQPRPLAPRLTGHHPRPPWHHLTLVGLRDCPVSAKSKSLGDLTADDFAPSFQGSTSSLSCGLGSLGVAHQVLEPGIRRDALTEQLRWLTGFQQAGDITSPTSLGPAGDGSVGGPSFLRRSSSRSQSRVRAIASRARQAQERQQRLRGQDSRGPPEEERGTPEGACSVGHEGCVDVPMPAKGAPEQVCGAADGQLLLRL
Protein: UDP-glycosyltransferase 71B8 (EC 2.4.1.-) (Q9LSY4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses low quercetin 3-O-glucosyltransferase and 4'-O-glucosyltransferase activities in vitro.
Interaction partners:
Sequence:
MNKFALVFVPFPILGHLKSTAEMAKLLVEQETRLSISIIILPLLSGDDVSASAYISALSAASNDRLHYEVISDGDQPTVGLHVDNHIPMVKRTVAKLVDDYSRRPDSPRLAGLVVDMFCISVIDVANEVSVPCYLFYTSNVGILALGLHIQMLFDKKEYSVSETDFEDSEVVLDVPSLTCPYPVKCLPYGLATKEWLPMYLNQGRRFREMKGILVNTFAELEPYALESLHSSGDTPRAYPVGPLLHLENHVDGSKDEKGSDILRWLDEQPPKSVVFLCFGSIGGFNEEQAREMAIALERSGHRFLWSLRRASRDIDKELPGEFKNLEEILPEGFFDRTKDKGKVIGWAPQVAVLAKPAIGGFVTHCGWNSILESLWFGVPIAPWPLYAEQKFNAFVMVEELGLAVKIRKYWRGDQLVGTATVIVTAEEIERGIRCLMEQDSDVRNRVKEMSKKCHMALKDGGSSQSALKLFIQDVTKYIA
Protein: Sperm-associated antigen 6 (Axoneme central apparatus protein) (Protein PF16 homolog) (Q9JLI7)
Organism: Mus musculus (Mouse)
Function: Important for structural integrity of the central apparatus in the sperm tail and for flagellar motility.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10684790}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:10684790}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:30535028}. Note=Associated with microtubules. Detected on the sperm flagellum (PubMed:10684790). Localizes in the cilium axoneme in a SPEF1-dependent manner (PubMed:30535028). {ECO:0000269|PubMed:10684790, ECO:0000269|PubMed:30535028}.
Interaction partners:
- Sperm-associated antigen 17
- Sperm-associated antigen 16 protein
- Sperm flagellar protein 2
Sequence:
MSQRQVLQVFEQYQKARTQFVQMVAELATRPQNIETLQNAGVMSLLRPLLLDVVPTIQQTAALALGRLANYNDDLAEAVVKGDILPQLVYSLAEQNRFYKKAAAFVLRAVGKHSPQLAQAIVDCGALDTLVICLEDFDPGVKEAAAWALGYIARHNTELSQAVVDAGAIPLLVLCIQEPEIALKRIAASALSDISKHSPELAQTVVDAGAIAHLAQMILNPDAKLKRQVLSALSQIAKHSVDLAEMVVEAEIFPVVLTCLKDKDEYVKKNACTLIREIAKHTPELSQLIVNAGGVAAVIDCIGSCKGNIRLPGIMMLGYVAAHSENLAMAVIISKGVPQLSICLSEEPEDHIKAAAAWALGQLGRHTPEHARAVAVTNTLPVLLSLYMSPESSEDLQLKSKKAIKNILQKCTYLPALEPFLYDAPPNILKHVVGQFSKVLPHDSKARRLFVTSGGLKKVQEIKAEPGSLLQEYINSINNCYPEEIVRYYSPGYSDTLLQRVDSYQPL
Protein: ATP-dependent zinc metalloprotease FtsH (EC 3.4.24.-) (P9WQN3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.
Subcellular location: Cell membrane {ECO:0000305|PubMed:9729123}; Multi-pass membrane protein {ECO:0000305|PubMed:9729123}; Cytoplasmic side {ECO:0000305|PubMed:9729123}. Note=Upon expression in E.coli.
Interaction partners:
- GTP cyclohydrolase 1
- Dihydroneopterin aldolase
- Uncharacterized protein Rv1488
- Protease Rv3090
- Dihydropteroate synthase
- Large ribosomal subunit protein uL13
- Large ribosomal subunit protein bL19
- Large ribosomal subunit protein bL17
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein uL2
Sequence:
MNRKNVTRTITAIAVVVLLGWSFFYFSDDTRGYKPVDTSVAITQINGDNVKSAQIDDREQQLRLILKKGNNETDGSEKVITKYPTGYAVDLFNALSAKNAKVSTVVNQGSILGELLVYVLPLLLLVGLFVMFSRMQGGARMGFGFGKSRAKQLSKDMPKTTFADVAGVDEAVEELYEIKDFLQNPSRYQALGAKIPKGVLLYGPPGTGKTLLARAVAGEAGVPFFTISGSDFVEMFVGVGASRVRDLFEQAKQNSPCIIFVDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFGDRAGVILIAATNRPDILDPALLRPGRFDRQIPVSNPDLAGRRAVLRVHSKGKPMAADADLDGLAKRTVGMTGADLANVINEAALLTARENGTVITGPALEEAVDRVIGGPRRKGRIISEQEKKITAYHEGGHTLAAWAMPDIEPIYKVTILARGRTGGHAVAVPEEDKGLRTRSEMIAQLVFAMGGRAAEELVFREPTTGAVSDIEQATKIARSMVTEFGMSSKLGAVKYGSEHGDPFLGRTMGTQPDYSHEVAREIDEEVRKLIEAAHTEAWEILTEYRDVLDTLAGELLEKETLHRPELESIFADVEKRPRLTMFDDFGGRIPSDKPPIKTPGELAIERGEPWPQPVPEPAFKAAIAQATQAAEAARSDAGQTGHGANGSPAGTHRSGDRQYGSTQPDYGAPAGWHAPGWPPRSSHRPSYSGEPAPTYPGQPYPTGQADPGSDESSAEQDDEVSRTKPAHG
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (A0A0G2K7W4)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MANDSPAKSLVDIDLSSLRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHIHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDLWSCGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETEYEYSGSEEEEEEVPEQEGEPSSIVNVPGESTLRRDFLRLQQENKERSEALRRQQLLQEQQLREQEEYKRQLLAERQKRIEQQKEQRRRLEEQQRREREARRQQEREQRRREQEEKRRLEELERRRKEEEERRRAEDEKRRVEREQEYIRRQLEEEQRHLEILQQQLLQEQAMLLECRWREMEEHRQAERLQRQLQQEQAYLLSLQHDHRRPHAQQPPPPQQQDRSKPSYHAPEPKPHYDPADRAREVEDRFRKTNHSSPEAQAKQTGRGLEPPVPSRSESFSNGNSESVHPALQRPAEPQVQWSHLASLKNNVSPVSRSHSFSDPSPKFAHHHLRSQDPCPPSRSEGLSQSSDSKSEVPEPTQKAWSRSDSDEVPPRVPVRTTSRSPVLSRRDSPLQGSGQQNSQAGQRNSTSSIEPRLLWERVEKLVPRPGSGSSSGSSNSGSQPGSHPGSQSGSGERFRVRSSSKSEGSPSQRLENAAKKPEDKKEVFRPLKPADLTALAKELRAVEDVRPPHKVTDYSSSSEESGTTDEEEEDVEQEGADDSTSGPEDTRAASSLNLSNGETESVKTMIVHDDVESEPAMTPSKEGTLIVRQSTVDQKRASHHESNGFAGRIHLLPDLLQQSHSSSTSSTSSSPSSSQPTPTMSPQTPQDKLTANETQSASSTLQKHKSSSSFTPFIDPRLLQISPSSGTTVTSVVGFSCDGLRPEAIRQDPTRKGSVVNVNPTNTRPQSDTPEIRKYKKRFNSEILCAALWGVNLLVGTESGLMLLDRSGQGKVYPLISRRRFQQMDVLEGLNVLVTISGKKDKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDLEGCVHYKVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFGELVHKPLLVDLTVEEGQRLKVIYGSCAGFHAVDVDSGSVYDIYLPTHIQCTIKPHAIIILPNTDGMELLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIRSNQTMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVYFMTLGRTSLLSW
Protein: Fgr10p (A0A1D8PM71)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MKDILVIHIGAGKHDPNKSKKYKTLLRNALSKTSIVEASDVIESSPLTNTGYGSSLNLLGKVECDASFITNDKIGAVVNMSCKNPTKELFRVFQYLDTLYESDETDLTSPVMLTYPLLKNLVPHIVDDDLVSEKSRKLYDMYKDKIFQGDYSKHCAIPHEISDTIGITHISDNETTIVTSSGGNFFKLPGRIGCAGVIGAAIARKKLDDCEICCMCSGNGEQIIKSKLAWEIANNIYNVAGDEYGKYLERKVYELNPKFYVGFIIILNYQSRVQLLYGHTTPTFYFGFRSPNQTRIILSSSDKMGHFTFGEYSLH
Protein: Uncharacterized protein YMR196W (Q04336)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- Glycogen phosphorylase
- Meiotic sister chromatid recombination protein 1
- Carboxypeptidase Y inhibitor
- Glycogen debranching enzyme
- Phosphoglucomutase 2
- Glutamate decarboxylase
- Inactive diphosphatase DCS2
- Alpha-mannosidase
Sequence:
MNKLRDKFVDSTVEEERLRENRNHEKYWYRWGPYLSERSWATVREDYSLNGDAWSNFPFEHANARVFRWGEDGLFGVSDNKQLVCMNVALWNGKDERLKERLFGLTGPQGNHGEDVKELYFYLDNTPTHSYMKALYKYPFKKAFPYKELVQKNGERGYEDKEFEVYDIDGLYRDSETGDNPYFDVFFEMAKDDENPSELNFRLTIHNRSKIDSGELYIAPQLFFRNTWAFDGTRTKDKPLLERDAEAANLINMTHKKYGNCQMVFQPSPGGFSSGTNEEEEDKEVEDIDPLLLFTDNESNLVKLFNEEKNPSEYTKDAFEEYLVQGKTDAVNPENKGTKACAVYHFKNIPPGEYVTVRYKFTNDPKNSIFKAQNLAVVDEDEFDLIFDNREEEADNFYWRITPLPISDELRNLQRQAFSGLLWTKQFYNFTYDAWYNGDANVKPRPPPNRANGRNKNWKHLYIEDILSMPDKWEYPFFASWDTAFHCIPLAMIDPEFAKRQLDLLTREWYMHPNGQIPAYEWNFNDVNPPVHAWAVYRVFKIERNMYNREDRTFLERVFQKLLLNFTWWVNRKDTEGKNVFEGGFLGLDNIGVFNRSEPLPTGGTLEQADSTGWMAFFSLQMLNIALELAKENPVYEDIASKFFEHFILISDSMSFEYATDITGEKCKEVIKQNLWNEADKFYYDAISWGDHKVQLPIRSLVGLIPLYASMTLEPSIIKQFRGFKKRVDWFVNNRPEIFDRNIASMSKKGVGERLLLSLVTKERLTAILSRLLDETEFLSPYGIRSLSKYHEKHPFEMNVNGVEYMVKYLPGESDSGMFGGNSNWRGPIWFPTSFLIMEALQRFYLYYGSDFKVECPVGSGDYLNLAEVAEELGYRMIHLFVPDENGERAIHYGDHSKFLSSDPYFRDYVPFFEYFDGDTGRGLGASHQCGWTALVAKWISDVGISCVRLPRTPRSSVATTASTESSEQGPKMKRMARRKSAKSLVNYTATILDLTEEEKRHHRIGGTHSGLTPQSSISSDKARHLMEEMNEEEGIHETVVPEDRHNFETKLIGKLKDKVKNMKVTDKAKDEDIDPMDPMSPLNKDVS
Protein: Interleukin-10 receptor subunit beta (IL-10 receptor subunit beta) (IL-10R subunit beta) (IL-10RB) (Cytokine receptor class-II member 4) (Cytokine receptor family 2 member 4) (CRF2-4) (Interleukin-10 receptor subunit 2) (IL-10R subunit 2) (IL-10R2) (CD antigen CDw210b) (Q08334)
Organism: Homo sapiens (Human)
Function: Shared cell surface receptor required for the activation of five class 2 cytokines: IL10, IL22, IL26, IL28, and IFNL1. The IFNLR1/IL10RB dimer is a receptor for the cytokine ligands IFNL2 and IFNL3 and mediates their antiviral activity. The ligand/receptor complex stimulate the activation of the JAK/STAT signaling pathway leading to the expression of IFN-stimulated genes (ISG), which contribute to the antiviral state.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Interleukin-22 receptor subunit alpha-1
- Interferon lambda-3
- Interferon lambda receptor 1
- Interferon lambda-1
- Interleukin-10 receptor subunit alpha
- Interleukin-22
- Interleukin-10
- Non-receptor tyrosine-protein kinase TYK2
- Interleukin-26
- Interferon lambda-2
Sequence:
MAWSLGSWLGGCLLVSALGMVPPPENVRMNSVNFKNILQWESPAFAKGNLTFTAQYLSYRIFQDKCMNTTLTECDFSSLSKYGDHTLRVRAEFADEHSDWVNITFCPVDDTIIGPPGMQVEVLADSLHMRFLAPKIENEYETWTMKNVYNSWTYNVQYWKNGTDEKFQITPQYDFEVLRNLEPWTTYCVQVRGFLPDRNKAGEWSEPVCEQTTHDETVPSWMVAVILMASVFMVCLALLGCFALLWCVYKKTKYAFSPRNSLPQHLKEFLGHPHHNTLLFFSFPLSDENDVFDKLSVIAEDSESGKQNPGDSCSLGTPPGQGPQS
Protein: Frizzled-4 (Fz-4) (mFz4) (CD antigen CD344) (Q61088)
Organism: Mus musculus (Mouse)
Function: Receptor for Wnt proteins. Most frizzled receptors are coupled to the beta-catenin (CTNNB1) canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin (CTNNB1) and activation of Wnt target genes. Plays a critical role in retinal vascularization by acting as a receptor for Wnt proteins and norrin (NDP). In retina, it can be activated by Wnt protein-binding and also by Wnt-independent signaling via binding of norrin (NDP), promoting in both cases beta-catenin (CTNNB1) accumulation and stimulation of LEF/TCF-mediated transcriptional programs. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues. Activation by Wnt5A stimulates PKC activity via a G-protein-dependent mechanism.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10097073}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Norrin
- Protein Wnt-5a
- Low-density lipoprotein receptor-related protein 6
- Low-density lipoprotein receptor-related protein 5
- Tetraspanin-12
- Protein Wnt-11
- Protein Wnt-7a
- Protein Wnt-7b
- Proto-oncogene Wnt-1
- Tyrosine-protein kinase RYK
Sequence:
MAWPGTGPSSRGAPGGVGLRLGLLLQFLLLLRPTLGFGDEEERRCDPIRIAMCQNLGYNVTKMPNLVGHELQTDAELQLTTFTPLIQYGCSSQLQFFLCSVYVPMCTEKINIPIGPCGGMCLSVKRRCEPVLREFGFAWPDTLNCSKFPPQNDHNHMCMEGPGDEEVPLPHKTPIQPGEECHSVGSNSDQYIWVKRSLNCVLKCGYDAGLYSRSAKEFTDIWMAVWASLCFISTTFTVLTFLIDSSRFSYPERPIIFLSMCYNIYSIAYIVRLTVGRERISCDFEEAAEPVLIQEGLKNTGCAIIFLLMYFFGMASSIWWVILTLTWFLAAGLKWGHEAIEMHSSYFHIAAWAIPAVKTIVILIMRLVDADELTGLCYVGNQNLDALTGFVVAPLFTYLVIGTLFIAAGLVALFKIRSNLQKDGTKTDKLERLMVKIGVFSVLYTVPATCVIACYFYEISNWALFRYSADDSNMAVEMLKIFMSLLVGITSGMWIWSAKTLHTWQKCSNRLVNSGKVKREKRGNGWVKPGKGNETVV
Protein: Telomerase-associated protein of 19 kDa (p19) (D2CVN7)
Organism: Tetrahymena thermophila (strain SB210)
Function: Component of a CST-like subcomplex of the holoenzyme telomerase ribonucleoprotein complex, which stimulates telomerase complementary-strand synthesis. Telomerase is an essential ribonucleoprotein enzyme that copies new telomeric repeats onto chromosome ends by repetitively synthesizing the short telomere-repeat sequence 5'-TTGGGG-3' using an RNA template component TER. The CST-like subcomplex (also named 7-4-1) binds telomeric single-stranded DNA and coordinates telomere G-strand and C-strand synthesis.
Subcellular location: Chromosome, telomere {ECO:0000305}.
Interaction partners:
Sequence:
MQQPKRNFDLYKLITDKQIDFQVADLIQDEQSSFVSVRIYGQFKCFVPKSTIQEQLDKIKNLSSKELAKNKIFKFLSEYNKNNQKQDELSHDYYGYFKVQQHQFILNLENAQREASLAVDDFYFINGRIYKTNHDILILQAHHVYQMQKPTLQLLQAASEINQN