wanglab/gogpt-training-data huggingface dataset:
Protein: Nephrocystin-3 (Q7Z494)
Organism: Homo sapiens (Human)
Function: Required for normal ciliary development and function. Inhibits disheveled-1-induced canonical Wnt-signaling activity and may also play a role in the control of non-canonical Wnt signaling which regulates planar cell polarity. Probably acts as a molecular switch between different Wnt signaling pathways. Required for proper convergent extension cell movements.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:20462968, ECO:0000269|PubMed:22085962}. Note=Localization to cilium is mediated via interaction with UNC119 and UNC119B, which bind to the myristoyl moiety of the N-terminus.
Interaction partners:
- Serine/threonine-protein kinase Nek8
- Nephrocystin-1
- Nephrocystin-4
- Protein unc-119 homolog B
- Inversin
- Ankyrin repeat and SAM domain-containing protein 6
- Serine/threonine-protein kinase Nek9
- IQ calmodulin-binding motif-containing protein 1
- Protein fantom
- Centrosomal protein of 290 kDa
Sequence:
MGTASSLVSPAGGEVIEDTYGAGGGEACEIPVEVKPKARLLRNSFRRGAGAAAGAGPGSLPRGVGAGGLLGASFKSTGSSVPELEYAAAEYERLRKEYEIFRVSKNQELLSMGRREAKLDTENKRLRAELQALQKTYQKILREKESALEAKYQAMERAATFEHDRDKVKRQFKIFRETKENEIQDLLRAKRELESKLQRLQAQGIQVFDPGESDSDDNCTDVTAAGTQCEYWTGGALGSEPSIGSMIQLQQSFRGPEFAHSSIDVEGPFANVNRDDWDIAVASLLQVTPLFSHSLWSNTVRCYLIYTDETQPEMDLFLKDYSPKLKRMCETMGYFFHAVYFPIDVENQYLTVRKWEIEKSSLVILFIHLTLPSLLLEDCEEAFLKNPEGKPRLIFHRLEDGKVSSDSVQQLIDQVSNLNKTSKAKIIDHSGDPAEGVYKTYICVEKIIKQDILGFENTDLETKDLGSEDSIPEEDDFGDVLWDIHDEQEQMETFQQASNSAHELGFEKYYQRLNDLVAAPAPIPPLLVSGGPGSGKSLLLSKWIQLQQKNSPNTLILSHFVGRPMSTSSESSLIIKRLTLKLMQHSWSVSALTLDPAKLLEEFPRWLEKLSARHQGSIIIVIDSIDQVQQVEKHMKWLIDPLPVNVRVIVSVNVETCPPAWRLWPTLHLDPLSPKDAKSIIIAECHSVDIKLSKEQEKKLERHCRSATTCNALYVTLFGKMIARAGRAGNLDKILHQCFQCQDTLSLYRLVLHSIRESMANDVDKELMKQILCLVNVSHNGVSESELMELYPEMSWTFLTSLIHSLYKMCLLTYGCGLLRFQHLQAWETVRLEYLEGPTVTSSYRQKLINYFTLQLSQDRVTWRSADELPWLFQQQGSKQKLHDCLLNLFVSQNLYKRGHFAELLSYWQFVGKDKSAMATEYFDSLKQYEKNCEGEDNMSCLADLYETLGRFLKDLGLLSQAIVPLQRSLEIRETALDPDHPRVAQSLHQLASVYVQWKKFGNAEQLYKQALEISENAYGADHPYTARELEALATLYQKQNKYEQAEHFRKKSFKIHQKAIKKKGNLYGFALLRRRALQLEELTLGKDTPDNARTLNELGVLYYLQNNLETADQFLKRSLEMRERVLGPDHPDCAQSLNNLAALCNEKKQYDKAEELYERALDIRRRALAPDHPSLAYTVKHLAILYKKMGKLDKAVPLYELAVEIRQKSFGPKHPSVATALVNLAVLYSQMKKHVEALPLYERALKIYEDSLGRMHPRVGETLKNLAVLSYEGGDFEKAAELYKRAMEIKEAETSLLGGKAPSRHSSSGDTFSLKTAHSPNVFLQQGQR
Protein: Histone H3-like centromeric protein A (Centromere protein A) (CENP-A) (GgCENP-A) (Q6XXM1)
Organism: Gallus gallus (Chicken)
Function: Histone H3-like nucleosomal protein that is specifically found in centromeric nucleosomes. Replaces conventional H3 in the nucleosome core of centromeric chromatin that serves as an assembly site for the inner kinetochore. The presence of CENPA subtly modifies the nucleosome structure and the way DNA is wrapped around the nucleosome and gives rise to protruding DNA ends that are less well-ordered and rigid compared to nucleosomes containing histone H3. May serve as an epigenetic mark that propagates centromere identity through replication and cell division (By similarity). Required for recruitment and assembly of kinetochore proteins, and as a consequence required for progress through mitosis, chromosome segregation and cytokinesis.
Subcellular location: Nucleus {ECO:0000269|PubMed:14563550}. Chromosome, centromere {ECO:0000269|PubMed:14563550}. Note=Localizes exclusively to sites of kinetochore assembly in centromeres. Occupies a compact domain at the inner kinetochore plate stretching across 2 thirds of the length of the constriction but encompassing only one third of the constriction width and height. {ECO:0000250|UniProtKB:P49450}.
Interaction partners:
- Centromere protein T
- Centromere protein S
- Centromere protein N
- Centromere protein I
- Centromere protein W
- Centromere protein U
- Kinetochore protein NDC80 homolog
- BUB1 N-terminal domain-containing protein.
- Uncharacterized protein.
- Inner centromere protein
Sequence:
MPRPKPRSPRRRGRPPPAAPPPPPARPRARRYRPGQRALREIRRYQSSTALLLRRQPFARVVREICLLFTRGVDYRWQAMALLALQEAAEAFLVHLLEDAYLCSLHARRVTLYPKDLQLARRLRGLQGEGF
Protein: Beta-galactosidase A (An-beta-gal) (EC 3.2.1.23) (Lactase A) (A2QAN3)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Function: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
Sequence:
MKLSSACAIALLAAQAAGASIKHRINGFTLTEHSDPAKRELLQKYVTWDDKSLFINGERIMIFSGEFHPFRLPVKELQLDIFQKVKALGFNCVSFYVDWALVEGKPGEYRADGIFDLEPFFDAASEAGIYLLARPGPYINAESSGGGFPGWLQRVNGTLRSSDKAYLDATDNYVSHVAATIAKYQITNGGPIILYQPENEYTSGCCGVEFPDPVYMQYVEDQARNAGVVIPLINNDASASGNNAPGTGKGAVDIYGHDSYPLGFDCANPTVWPSGDLPTNFRTLHLEQSPTTPYAIVEFQGGSYDPWGGPGFAACSELLNNEFERVFYKNDFSFQIAIMNLYMIFGGTNWGNLGYPNGYTSYDYGSAVTESRNITREKYSELKLLGNFAKVSPGYLTASPGNLTTSGYADTTDLTVTPLLGNSTGSFFVVRHSDYSSEESTSYKLRLPTSAGSVTIPQLGGTLTLNGRDSKIHVTDYNVSGTNIIYSTAEVFTWKKFADGKVLVLYGGAGEHHELAISTKSNVTVIEGSESGISSKQTSSSVVVGWDVSTTRRIIQVGDLKILLLDRNSAYNYWVPQLATDGTSPGFSTPEKVASSIIVKAGYLVRTAYLKGSGLYLTADFNATTSVEVIGVPSTAKNLFINGDKTSHTVDKNGIWSATVDYNAPDISLPSLKDLDWKYVDTLPEIQSSYDDSLWPAADLKQTKNTLRSLTTPTSLYSSDYGFHTGYLLYRGHFTATGNESTFAIDTQGGSAFGSSVWLNGTYLGSWTGLYANSDYNATYNLPQLQAGKTYVITVVIDNMGLEENWTVGEDLMKTPRGILNFLLAGRPSSAISWKLTGNLGGEDYEDKVRGPLNEGGLYAERQGFHQPEPPSQNWKSSSPLEGLSEAGIGFYSASFDLDLPKGWDVPLFLNIGNSTTPSPYRVQVYVNGYQYAKYISNIGPQTSFPVPEGILNYRGTNWLAVTLWALDSAGGKLESLELSYTTPVLTALGEVESVDQPKYKKRKGAY
Protein: Transmembrane protein 89 (A2RUT3)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
- IQ domain-containing protein F5
Sequence:
MLHVLASLPLLLLLVTSASTHAWSRPLWYQVGLDLQPWGCQPKSVEGCRGGLSCPGYWLGPGASRIYPVAAVMITTTMLMICRKILQGRRRSQATKGEHPQVTTEPCGPWKRRAPISDHTLLRGVLHMLDALLVHIEGHLRHLATQRQIQIKGTSTQSG
Protein: Uncharacterized protein (Q585P4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSSNRMFADVPTYRRGYVSPSGVKVLYSKDWAKHHPLEGDGLRPQLYLHLWKKNKGSESRLKNVRLPDTVVYEHNFPRAWYTYDAEAREINKHPGKMLDAQSIYQHFSRPTAGYEIVAQFLTTCPVDDPESLTPNGELISYSEIFTAETLREFLFNKSRKPDGILQKFVPPKGETTMRRNAQLQVSWSPLMAVVYKRTNKYRLDDHRVPVHMRAATFDGDNHLSELSLVADETKGRLDLLCREVVDHVYFTDRKLITRMVLHFRIDDDNRPWLLWCSSLRVSGDSLNPRTVRIPVTLTMRVEMLNNGSSTKDRIKKRQDRQRHLLIMDTELYELSRDNDLGHQCNASHVREAKRLGLSPKKLPKTGNNLKVPLRHPLRPAMTYFADTLLEDALRNLEINSGLPSPTLAQQELDAMAQKHAGASLEDKPEDRVKNELTAMALDAWYQVYSSTLSERPHEMPTQLVELSDPLMVVLKPEEFRNLLDILGLEPTAKASAAPVSGEGGAETGQAGGDPPTNTFRVKLGLLRPGKRLDRPLSNAERDVRNFFDDIFSERGEEIVQRCLSEEKWIW
Protein: Syncollin (Proximal small intestine-specific protein 9) (O35775)
Organism: Rattus norvegicus (Rat)
Function: Functions in exocytosis in pancreatic acinar cells regulating the fusion of zymogen granules with each other. May have a pore-forming activity on membranes and regulate exocytosis in other exocrine tissues.
Subcellular location: Zymogen granule membrane {ECO:0000269|PubMed:10753942, ECO:0000269|PubMed:11389693, ECO:0000269|PubMed:11853552}; Peripheral membrane protein {ECO:0000269|PubMed:10753942, ECO:0000269|PubMed:11389693, ECO:0000269|PubMed:11853552}; Lumenal side {ECO:0000269|PubMed:10753942, ECO:0000269|PubMed:11389693, ECO:0000269|PubMed:11853552}. Zymogen granule lumen {ECO:0000269|PubMed:11389693}. Note=Associated in a cholesterol-dependent manner with lipid rafts of zymogen granule membranes. {ECO:0000269|PubMed:11389693}.
Interaction partners:
- Colipase
- Zymogen granule membrane protein 16
- Chymotrypsin like elastase 3B
- Inactive pancreatic lipase-related protein 1
- Carboxypeptidase A1
Sequence:
MSPLCLLLLALALVAVPGARGACPVPADLKKSDGTRTCARLYENSDPYYDNCCQGPELSVDPGTDLPYLPSDWSNSASSLVVAQRCELTVWSLPGKRGKTRKFSTGSYPRLEEYRKGIFGTWAKSISGLYCKCY
Protein: Protein HEG homolog 1 (E9Q7X6)
Organism: Mus musculus (Mouse)
Function: Receptor component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity. May be acting by stabilizing endothelial cell junctions.
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Cell junction {ECO:0000269|PubMed:19151727}.
Interaction partners:
- Krev interaction trapped protein 1
Sequence:
MATPRAPRWPPPSLLLLLLLPLLLLPPAAPGARGSLPSPAHRTLLPVAGPLSPPGAGHTAPGPGVATRRGRSGRVPRGVSAAAARNRWLESNNPEPHIGCSPSYQSQEDHSGSRKGVTAQNARMSHSSSEGPENPPLLPETSAEWSNMASSHRADIAGLRRGPSPEITTAPTAHSSLLSLESLPESPSSSRSQRRITPSQTESGTSLGFLERTRELPEEGTVHTQVAGTWVSRQASHPALEPGEPTVLSQKRNSSGQEHSGPPFSWSQSHPPPSDHPSSSGSIKNGNNFTALQNPSVTQTKSMLITDTYTNGVPRTLRSLPVGVDPADETEGFPEHSRLGITSMSVRSSPSVKDSRTNSGLTEHLGDGEGTELSTENGYGLPSIHWQSDAPSFGGRQLASSSEAGDGRAMPLTEAVFRSDPSIGGGESTGRWILTKKKTSTDAAESSALHPEAGGAGGLTQSSHAAQQPRGGGEDSGMGGRSYAESSSSSSSTSSSESLDSSAPLREHSLTGLSYTREHGSDAGQRTSSDHTDHGYVPSTFTKGERTLLSITDNTSYSEASESSTSSVKISDSPSQAQPKQSSMSSDDDEPAQSSTESPVLHTSNLPTYTSTVNMPNTLVLDTGTKPVEDPSDSRVPSTQPSPSQPQPFSSALPSTRSPGSTSETTTSSPSPSPISLLVSTLAPYSVSQTTFPHPSSTLVPHRPREPRVTSVQMSTAISAIALIPSNQTANPKNQSTPQQEKPITEAKSPSLVSPPTDSTKAVTVSLPPGAPWSPALTGFSTGPALPATSTSLAQMSPALTSAMPQTTHSPVTSPSTLSHVEALTSGAVVVHTTPKKPHLPTNPEILVPHISTEGAITTEGNREHTDPTTQPIPLTTSTTSAGERTTELGRAEESSPSHFLTPSSPQTTDVSTAEMLTSRYITFAAQSTSQSPTALPPLTPVNSCTVNPCLHDGKCIVDLTGRGYRCVCPPAWQGENCSVDVNECLSSPCPPLATCNNTQGSFTCRCPVGYQLEKGICNLVRTFVTEFKLKKTFLNTTAENHSNTQELENEIAQTLNVCFSTLPGYIRTTAHVSREPSTVFISLKTTFALASNVTLFDLADRIQKYVNSCRSSAEVCQLLGSQRRVFRAGSLCKRKSPECDKETSICTDLDGVALCQCKSGYFQFNKMDHSCRACEDGYRLENETCMSCPFGLGGLNCGNPYQLITVVIAAAGGGLLLILGVALIVTCCRKSKNDISKLIFKSGDFQMSPYTDVPKNPRSQEWGREAIEMHENGSTKNLLQMTDVYYSPTNVRNPELERNGLYPAYTGLPGSRHSCIFPGQYNPSFISDESRRRDYF
Protein: LD29187p (Q95TR4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Chromosome {ECO:0000256|ARBA:ARBA00004286}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MPQKKIVMQPQLPKTSVVLPRPQQLPKNPLLVAQQQSPKTPLVNSVMGPQFPSQQPSLPVVNQITHKSMTIQRLPMLQTVQKILPKQIAPQQTPPPAHIVQKQTMPNAAMQNPPFAHRPPIVRPMTVAKISPVPTNNKVCIPMKPQMASYVSPTDPTMTAARTLPFRSSQRKTSEAPMTSTHVQGFTASATPPQRLLATPPHCAAALNEPLLLNLPPTTSITPQLTPTTTPPPAGPSAAVQQQQLAKAAAIKLNSLPEASISPVNRSPTASAKRIQPITVLKKSDEEWQRHLEQQQQKKHVQLQSSSMTTIVLVESPPTTPPTDKPEPERGPMTVEKSSIKPMATDKQSRAIKRPAVMISTKKSGLVVTEIVDLDEIPDIPPEKRGKECFPPIKNAAKAAPSVNAPFTTEYAALLRLCREVDKSTHMERLVKGELTQYYYSAPESFVMSCGFRNLVTMAMARIRSESYLVYVHLKYVLDELASRRLTKMFPTVRAIPPASQFPLPPASQFPLPPTLTTPKQPAIVKAPGQQTVMAGREQDDEVEEVTLVNVGTVSCEERRRDERIRHFYRTLHAITKRIKMLEEAEVDLNDEDSSYLQLERFKKRACQIYEKICDLKGESKSVRRQLKKPIHFKDSDYPHFNNSLSAFVNRMQDFPDYHDVLQILEKCNKEKELGLAKYEMKRIAYDAFNKVGRMLQSRRKNDLYETVTHYTANGKDPASSDPELLAKLKENNKKQTKISDILEKYALEQDLNAEERQEARLKEKKLKQVKADEEAAKLAALAEDDDKPCTSAQAAAKAAALAALKRGPAARGNVIRKKRAANGRIFKIADDGDDSEEESDSEDDDVEEFVNNFQANSDVSDADSEVEAVTSPKRDALPLAEEEDVIDITRDETGKKNDEGTPNGRLKIMSVSSLNANFVHGQDLHRKPNPMPSAKPVIADQIIISDEES
Protein: Bifunctional cytochrome P450/NADPH--P450 reductase 1 (CYP102A2) (Fatty acid hydroxylase CypD) (Flavocytochrome P450 102A2) [Includes: Cytochrome P450 102A2 (EC 1.14.14.1); NADPH--cytochrome P450 reductase (EC 1.6.2.4)] (O08394)
Organism: Bacillus subtilis (strain 168)
Function: Functions as a fatty acid monooxygenase. Catalyzes hydroxylation of a range of long-chain fatty acids, with a preference for long-chain unsaturated and branched-chain fatty acids over saturated fatty acids. Hydroxylation of myristic acid occurs mainly at the omega-2 position. Also displays a NADPH-dependent reductase activity in the C-terminal domain, which allows electron transfer from NADPH to the heme iron of the cytochrome P450 N-terminal domain. Is also able to catalyze efficient oxidation of sodium dodecyl sulfate (SDS).
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
- Polyketide synthase PksJ
- Surfactin synthase subunit 3
- Dimodular nonribosomal peptide synthase
- Polyketide synthase PksN
- Putative aldehyde dehydrogenase AldY
- Sulfite reductase hemoprotein beta-component
- Bifunctional cytochrome P450/NADPH--P450 reductase 2
- Putative aldehyde dehydrogenase AldX
- Putative aldehyde dehydrogenase YwdH
- Putative aldehyde dehydrogenase DhaS
Sequence:
MKETSPIPQPKTFGPLGNLPLIDKDKPTLSLIKLAEEQGPIFQIHTPAGTTIVVSGHELVKEVCDEERFDKSIEGALEKVRAFSGDGLFTSWTHEPNWRKAHNILMPTFSQRAMKDYHEKMVDIAVQLIQKWARLNPNEAVDVPGDMTRLTLDTIGLCGFNYRFNSYYRETPHPFINSMVRALDEAMHQMQRLDVQDKLMVRTKRQFRYDIQTMFSLVDSIIAERRANGDQDEKDLLARMLNVEDPETGEKLDDENIRFQIITFLIAGHETTSGLLSFATYFLLKHPDKLKKAYEEVDRVLTDAAPTYKQVLELTYIRMILNESLRLWPTAPAFSLYPKEDTVIGGKFPITTNDRISVLIPQLHRDRDAWGKDAEEFRPERFEHQDQVPHHAYKPFGNGQRACIGMQFALHEATLVLGMILKYFTLIDHENYELDIKQTLTLKPGDFHISVQSRHQEAIHADVQAAEKAAPDEQKEKTEAKGASVIGLNNRPLLVLYGSDTGTAEGVARELADTASLHGVRTKTAPLNDRIGKLPKEGAVVIVTSSYNGKPPSNAGQFVQWLQEIKPGELEGVHYAVFGCGDHNWASTYQYVPRFIDEQLAEKGATRFSARGEGDVSGDFEGQLDEWKKSMWADAIKAFGLELNENADKERSTLSLQFVRGLGESPLARSYEASHASIAENRELQSADSDRSTRHIEIALPPDVEYQEGDHLGVLPKNSQTNVSRILHRFGLKGTDQVTLSASGRSAGHLPLGRPVSLHDLLSYSVEVQEAATRAQIRELASFTVCPPHRRELEELSAEGVYQEQILKKRISMLDLLEKYEACDMPFERFLELLRPLKPRYYSISSSPRVNPRQASITVGVVRGPAWSGRGEYRGVASNDLAERQAGDDVVMFIRTPESRFQLPKDPETPIIMVGPGTGVAPFRGFLQARDVLKREGKTLGEAHLYFGCRNDRDFIYRDELERFEKDGIVTVHTAFSRKEGMPKTYVQHLMADQADTLISILDRGGRLYVCGDGSKMAPDVEAALQKAYQAVHGTGEQEAQNWLRHLQDTGMYAKDVWAGI
Protein: Cysteine--tRNA ligase, chloroplastic/mitochondrial (EC 6.1.1.16) (Cysteinyl-tRNA synthetase) (CysRS) (F4IPY2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for female gametophyte development. Is necessary for the fusion of central cell nuclei and programmed cell death (PCD) of the antipodals.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:10824085}. Mitochondrion {ECO:0000269|PubMed:10824085, ECO:0000269|PubMed:21135240}.
Interaction partners:
- Valine--tRNA ligase, chloroplastic/mitochondrial 2
- Leucine--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, chloroplastic/mitochondrial
- Valine--tRNA ligase, mitochondrial 1
- Methionine--tRNA ligase, cytoplasmic
- Histidine--tRNA ligase, cytoplasmic
- Probable elongation factor 1-gamma 2
- Threonine--tRNA ligase, chloroplastic/mitochondrial 2
- Probable threonine--tRNA ligase, cytoplasmic
- Asparagine--tRNA ligase, chloroplastic/mitochondrial
Sequence:
MASSVLNLFKSCRPFTPIRFSSLPKSQFRIQFPLRPGKETQLRRCFTTLSSLTDGGAPISGGKELWLHNTMSRKKELFKPKVEGKVGMYVCGVTAYDLSHIGHARVYVTFDVLLRYLKHLGYEVSYVRNFTDVDDKIIARAKELEEDPISLSRRFCEEFNRDMEQLQCLDPSVQPRVSDHIPQIIDLIKQILDNGYAYKVDGDIYFSVDKFPTYGKLSGRKLEDNRAGERVAVDTRKKHPADFALWKAAKEGEPFWESPWGRGRPGWHIECSAMSAAYLGYSFDIHGGGMDLVFPHHENEIAQSCAACDSSNISYWIHNGFVTVDSEKMSKSLGNFFTIRQVIDLYHPLALRLFLMGTHYRSPINYSDFLLESASERIFYIYQTLHDCESALGEKDSTFENGSVPSDTLTSINTFRTEFVASMSDDLLTPVTLAAMSEPLKTINDLIHTRKGKKQARREESLKALETTIRDVLTILGLMPTSYSEVLEQLKEKALKRAGLKEEDVLQRVQERTDARKNKEYERSDAIRKDLAKVGIALMDSPEGTTWRPAIPLALQEPVTTTP
Protein: T. brucei spp.-specific protein (Q580U0)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Uncharacterized protein
- Trans sialidase, putative
- Transmembrane protein
Sequence:
MPARASQRTPRGTTSKSERQVTNKENPQEQATTAPNDSTRTDIPDVVAEVQKVEAILARRRETMGAGSNGFTCGTWVALVVLEVLAFVWLSWAMDVYAMYRGARP
Protein: chitin synthase (EC 2.4.1.16) (Q9I7P4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSAMRHRPMAPPGQGPGAGTAGEHVDSDDNNFTDDESSPLTHDIYGGSQRTIQETKGWDVFRDPPIKIETGSTANQECLELTVKILKIFAYVITFIIVLTGGVIAKGTMLFMTSQVRKDKKMEYCNKDLGRDKSFVVRLPEEERVAWIWALLIAYALPEIGALIRSARICFFKTFKVPKTGHFLFVWLMESLSAVGMALLMFVVLPQIDAIQGAMLTNCLCVVPGIFGLLSRTSKEGKRFVKVIIDLAAVAAQVTGLVIWPLLENRRELWVIPVACVMISCGWWENYVSPQSPLGLVRALGRIKEEMKYTRYFCHIFLSIWKILLFFTVTLLIYWAQGEEPGNLFAMYGDAFGPHKIIVYELPAGLGGVLPDTLESANIDTVDVDAAYNTVVYVLLLQIFGAYLCYIFGKFACKILIQGFSYAFPVSLTVPLSVTFLIAACGIRIDDPCFFHDTIPDYLFFTSPSNFRFNNFVTEQMAWAWILWLLSQTWIALHIWTPKCERLATTEKLFVQPMYSSLLIDQSMALNRRRDDQADVKTEDLSEIEKEKGDEYYETISVHTDRSSAPNKPSIKSSDNITRIYSCATMWHETKDEMIEFLKSIMRMDEDQCARRVAQKYLRVLDPDYYEFETHIFFDDAFEISDHSDDDIQCNRFVKLLIATMDEAASEIHQTTIRLRPPKKYPTPYGGRLVWTLPGKTKFITHLKDKDRIRHRKRWSQVMYMYYLLGHRLMELPISVDRKDAIAENTYLLTLDGDIDFKPNAVTLLVDLMKKNKNLGAACGRIHPVGSGPMVWYQLFEYAIGHWLQKATEHMIGCVLCSPGCFSLFRGKALMDDNVMKKYTTRSDEARHYVQYDQGEDRWLCTLLLQRGYRVEYSAASDAYTHCPEGFNEFYNQRRRWVPSTIANIMDLLADAKRTIKINDNISLLYIFYQMMLMGGTILGPGTIFLMLVGAFVAAFRIDNWTSFHYNIVPILAFMFICFTCKSNIQLFVAQVLSTAYALIMMAVIVGTALQLGEDGIGSPSAIFLISMVGSFFIAACLHPQEFWCITCGLIYLLSIPSMYLLLILYSIINLNVVSWGTREVVAKKTKKELEAEKKAAEEAKKRVKQKSMLSFLQSGIGDNGDEEGSVEFSLAGLFRCIFCTHGKTSDEKQQLTSIAESLDTIKHRMDTIESAVDPHGHHASRHGRRRTTSSGSKDHHLLTSVAEKSGDESDESDSDTSAEPKQERDFLTNPYWIEDPDVRKGEVDFLSSTEIQFWKDLIDQYLYPIDNDPVEQARIASDLIELRNKSVFAFFMANALFVLIVFLLQLNKDKLHIIWPLGVKTNITYIEETSEVHISKEYLQLEPIGLVFVFFFALILIIQFTAMLFHRFGTISHILASTELNFCKKKSEDLTQDQLIDKHAVEIVKNLQRLQGIDGDYDNDSGSGPDRIARRKTIQNLEKARQPRRQIGTLDVAFKKRFLKLTADAENNPATPILTRRLTMRAETIRALEVRKNSVMAERRKSAMQTLGAKNEYGITTGAPINNNGALPNQRSGRVSNAGISIKDVFNVNGGGAEQIYGSNGGGTINQGYEHVIDEDGDGNSLRLTTRNPHPHPHHQVSWGQNTNGGGGNGTGRL
Protein: Aldo-keto reductase family 1 member C21 (EC 1.1.1.-) (17-alpha-hydroxysteroid dehydrogenase) (17-alpha-HSD) (3(or 17)-alpha-hydroxysteroid dehydrogenase) (EC 1.1.1.209) (3-alpha-hydroxysteroid dehydrogenase) (Dihydrodiol dehydrogenase type 1) (DD1) (Dihydrodiol dehydrogenase type 3) (DD3) (Q91WR5)
Organism: Mus musculus (Mouse)
Function: NADP-dependent 17-alpha-hydroxysteroid dehydrogenase that converts 5-alpha-androstane-3,17-dione into androsterone. Has lower 3-alpha-hydroxysteroid dehydrogenase activity. Has broad substrate specificity and acts on various 17-alpha-hydroxysteroids, 17-ketosteroids, 3-alpha hydroxysteroids and 3-ketosteroids. Reduction of keto groups is strictly stereoselective. Reduction of 17-ketosteroids yields only 17-alpha-hydroxysteroids. Likewise, reduction of 3-ketosteroids yields only 3-alpha-hydroxysteroids.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MNSKCHCVILNDGNFIPVLGFGTALPLECPKSKAKELTKIAIDAGFHHFDSASVYNTEDHVGEAIRSKIADGTVRREDIFYTSKVWCTSLHPELVRASLERSLQKLQFDYVDLYLIHYPMALKPGEENFPVDEHGKLIFDRVDLCATWEAMEKCKDAGLTKSIGVSNFNYRQLEMILNKPGLKYKPVCNQVECHPYLNQMKLLDFCKSKDIVLVAYGVLGTQRYGGWVDQNSPVLLDEPVLGSMAKKYNRTPALIALRYQLQRGIVVLNTSLKEERIKENMQVFEFQLSSEDMKVLDGLNRNMRYIPAAIFKGHPNWPFLDEY
Protein: Ribosomal protein S24/S35 mitochondrial conserved domain-containing protein (Q383M2)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- 50S ribosomal protein L13, putative
- Peptidyl-prolyl cis-trans isomerase
- Large ribosomal subunit protein bL21m
- Tetratricopeptide repeat
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- 50S ribosomal protein L14, putative
- Uncharacterized protein
Sequence:
MLRLSSWNLKSQHHNVLRRSRPHIHKYRELNRWQRQAQGISKWDQSHSHRPLPYVERFNPESVGLTRGTSAFAWKWWHTQYPWLPNVPPEAAQIDEAQKQERRSHRPPAWDDEFAKVVLNMNDAEIREYLMSKLTDVIFLETQRDGYELRRLDFEGKPLTSLPEPRIIENFVLEEETIRERVIYQVVEGVFRLSPTSADRRELRSVANIIDYVLTHVRAARPTDRERRQERPITSAALAVMQKCPIQPQLGFVHALPHDTRDALLQEWERMHHLDWQFGKAVYTPRSKENVRGNLTWLREDRHYDQRMKFMQEVESGEARAKHMKLIAAAAGN
Protein: Mitochondrial inner membrane protein OXA1 (Cytochrome oxidase biogenesis protein OXA1) (Oxidase assembly protein 1) (P39952)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mitochondrial inner membrane insertase that mediates the insertion of both mitochondrion-encoded precursors and nuclear-encoded proteins from the matrix into the inner membrane. Links mitoribosomes with the inner membrane. Forms pores capable of accommodating translocating protein segments. Essential for the activity and assembly of cytochrome c oxidase. Plays a central role in the translocation and export of the N-terminal part of the COX2 protein into the mitochondrial intermembrane space.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:22513091, ECO:0000269|PubMed:9171337}; Multi-pass membrane protein {ECO:0000269|PubMed:9171337}. Note=The availability of nuclear- and mitochondrial-encoded substrates influences the inner- membrane distribution. {ECO:0000269|PubMed:22513091}.
Interaction partners:
- Inner membrane mitoribosome receptor MBA1, mitochondrial
- ATP synthase subunit 9, mitochondrial
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Cytochrome c oxidase assembly protein COX18, mitochondrial
- Cytochrome c oxidase subunit 2
- Mitochondrial import inner membrane translocase subunit TIM50
- ATP synthase subunit a
- ER membrane protein complex subunit 3
- Large ribosomal subunit protein uL23m
- Mitochondrial import inner membrane translocase subunit TIM17
Sequence:
MFKLTSRLVTSRFAASSRLATARTIVLPRPHPSWISFQAKRFNSTGPNANDVSEIQTQLPSIDELTSSAPSLSASTSDLIANTTQTVGELSSHIGYLNSIGLAQTWYWPSDIIQHVLEAVHVYSGLPWWGTIAATTILIRCLMFPLYVKSSDTVARNSHIKPELDALNNKLMSTTDLQQGQLVAMQRKKLLSSHGIKNRWLAAPMLQIPIALGFFNALRHMANYPVDGFANQGVAWFTDLTQADPYLGLQVITAAVFISFTRLGGETGAQQFSSPMKRLFTILPIISIPATMNLSSAVVLYFAFNGAFSVLQTMILRNKWVRSKLKITEVAKPRTPIAGASPTENMGIFQSLKHNIQKARDQAERRQLMQDNEKKLQESFKEKRQNSKIKIVHKSNFINNKK
Protein: Ras-related C3 botulinum toxin substrate 3 (EC 3.6.5.2) (p21-Rac3) (P60763)
Organism: Homo sapiens (Human)
Function: Plasma membrane-associated small GTPase which cycles between an active GTP-bound and inactive GDP-bound state. In active state binds to a variety of effector proteins to regulate cellular responses, such as cell spreading and the formation of actin-based protusions including lamellipodia and membrane ruffles. Promotes cell adhesion and spreading on fibrinogen in a CIB1 and alpha-IIb/beta3 integrin-mediated manner.
Subcellular location: Cytoplasm. Endomembrane system. Cell projection, lamellipodium. Cytoplasm, perinuclear region. Cell membrane. Cytoplasm, cytoskeleton. Note=Membrane-associated when activated. Colocalizes with NRBP to endomembranes and at the cell periphery in lamellipodia. Colocalized with CIB1 in the perinuclear area and at the cell periphery.
Interaction partners:
- Serine/threonine-protein kinase PAK 1
- Dedicator of cytokinesis protein 2
- Serine/threonine-protein kinase PAK 4
- Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
- Proto-oncogene vav
- Engulfment and cell motility protein 1
- Plexin-B1
- Ras-related C3 botulinum toxin substrate 2
- Ras GTPase-activating-like protein IQGAP2
- Triple functional domain protein
Sequence:
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLRDDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQRGLKTVFDEAIRAVLCPPPVKKPGKKCTVF
Protein: Histone H2B.6 (H2BAt) (HTB9) (O23629)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.
Subcellular location: Nucleus {ECO:0000250}. Chromosome {ECO:0000250}.
Interaction partners:
- Histone H4
- Histone H3.1
- Histone H3.3
- Histone H3-like centromeric protein CENH3
- Histone H3-like 1
- Histone H3-like 4
- Histone H3-like 2
- Histone H3-like 3
- Histone H3-like 5
- E3 ubiquitin-protein ligase BRE1-like 1
Sequence:
MAPRAEKKPAEKKPAAEKPVEEKSKAEKAPAEKKPKAGKKLPKEAGAGGDKKKKMKKKSVETYKIYIFKVLKQVHPDIGISSKAMGIMNSFINDIFEKLASESSKLARYNKKPTITSREIQTAVRLVLPGELAKHAVSEGTKAVTKFTSS
Protein: IP13425p (Tyramine receptor II) (Tyramine receptor II, isoform B) (Tyramine receptor II, isoform C) (Tyramine receptor II, isoform D) (Q9VEG2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
Sequence:
MAALEHPDAMLPYSKLLSTALTVASGNSNSSDGTLLLIQTSAAPGGDVMATGAGAGKLGVPSMNSYLVSMAWPKSLAVAVFLVIILVTVVGNTLVILAVLTTRRLRTVTNCFVMNLAITDWLVGTCVMPPSVVLYITGTWRFGWILCDIWISLDILLCSGSILSLCAISLDRYLAVTQPLTYSKKRRSKRLALLMILVVWITALSITCPPYLGWYEVGRHQAEFVDCRYNQNKGYVVFSAMGSFFIPLTVMLYVYVKIGYVLTSRRQRIVRDAYSERTADYDVDGDNFISESEHYHCTPTKWLPNRKSRWRFNSLHDPPPSAATNAAAKGHQSSVKCSKCSKCSSATGTAGAGAGAGVVDKTLTFKHQPTFYELVEVSRLSSLIHCSAISCKYGGPCMHSTPSGMHYVGTEASFSDTCLGGNVSNNTTTTTTNTVALETNEKLEAEAKQKQQQQRSSFDHHHPHAHHHGSHGQQSHHNHHHRMPMRVSTTKRDSKTAKTLTIVMGGLIACWLPFFVYYLLIPFLPRPAVLEDLMFGFTWIGWVNCAINPFIYAFYNPDFRTAFWRLTCRPICKQKRPPNHLAMFRG