wanglab/gogpt-training-data huggingface dataset:
Protein: Pumilio domain-containing protein C56F2.08c (O60059)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Pumilio homology domain family member 6
Sequence:
MLYVSNLPVGTSSSAIHALFSAYGNVKDIWMLSPDNSAIVSYESLSSAIVARDALHNRPVFENHGPVQVMLAKPSSNYEPGNITAAVSPPASTSSKDGVVCSPTSTGASQLLKSRVDILEVARQFEMRINLDIVDSMIASAIENNKVATEILPPVETLRSRQFEASKLREIRKNIDSGFYTQEEIEVIARSMLDDVAELSSDYLGNTVVQKFFEYCSDPIKEAMLERIAPYLAAIGIHKNGTWAAQKIIDVASTEKQMDLIVKHLRPYTALLYFDQFGNYVAQCCLRFKYPKNTFLFEVMARHCCEIGQSRFGARAIRACLENENATFEQQALVVASIIINSHLLATNSNGMLLLTWLLDNSFFRNRHRLLAIHLATHLHTTCTHKLASTLIFKLINNKQEPESRNLLLKNLFFSEKDNVLTYILQDQAVGPSFIHKVITYPSIGREFLAQFHLVIKRVLINIHAQPNAVYCRLMEEVGMTSKSISPSLSGISAPSASVDSSASRLARDFGSLSLSSNSLLGSLGGLESTPAYPSYPSHIPLGTASLPLKGNLYQISRSDDIKSGAPVLDTSSLVNPTLAKSASLNNSSLLNPSSSLLRREVPAGKLTMPAYPYTTQLMNHTAGADYGLPRLSSKLPQVFPGNYPRLQQSLFPRQGELRFN
Protein: Acylphosphatase-2 (EC 3.6.1.7) (Acylphosphatase, muscle type isozyme) (Acylphosphate phosphohydrolase 2) (P14621)
Organism: Homo sapiens (Human)
Function: Its physiological role is not yet clear.
Interaction partners:
- Aldehyde dehydrogenase X, mitochondrial
- Acetyl-coenzyme A thioesterase
- 4-trimethylaminobutyraldehyde dehydrogenase
- Acetyl-coenzyme A synthetase, cytoplasmic
- Acylphosphatase-1
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
- Alpha-aminoadipic semialdehyde dehydrogenase
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Zinc finger protein 208
Sequence:
MSTAQSLKSVDYEVFGRVQGVCFRMYTEDEARKIGVVGWVKNTSKGTVTGQVQGPEDKVNSMKSWLSKVGSPSSRIDRTNFSNEKTISKLEYSNFSIRY
Protein: Protocadherin 1 isoform 2 (Q2TJI9)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
YCRQREAKSGYQAGKKETKDLYAPKPSGKAAKGSKSKGKKSKSPKPVKPVEDEDDTGLQKSLKFNLMSDAPGDSPRIHLPLNYPPGSPDLGRHYRSNSPLPSIQLQPQSPSASKKHQVVQDLPPANTFVGTGDTTSTGSEQYSDYSYRTNPPKYPSKQLPHRRVTFSATSQAQELQDPSQHSYYDSGLEESETPSSKSSSGPRLGPLALPEDHYERTTPDGSIGEMEHPENDLRPLPDVAMTGTCTRECSEFGHSDTCWMPGQSSPSRRTKSSALKLSTFVPYQDRGGQEPAGAGSPSPPEDRNTKTAPVRLLPSYSAFSHSSHDSCKDSATLEEIPLTQTSDFPPTATPASAQTAAKREIYL
Protein: Endoglin (M0RA19)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MDRSMLPLVITLLLVIYSFVPTSLAERVGCDLQRVDSTRGEVTYTTSQVSEGCVAQVANAAHEVHVLFLNLSRRKSEVELTLQASKQNGTETREVFLVFISNENVLVKLQAPEIPLHLVYNSSLEVFKGPKVNSTPLPSFTSKTQILDWAATKGTITSIAALDDPKSIVLRLGQDPKAPPFCFPEAQKDMGVTLEWQPRTQTPVQGCHLEGVTGHKEAYVLRIRSGSEAGPRTVTVTVKLSCTSGDAVLILQGPPYVSWLIDTNHNMQIWTTGEYSIKIFPENNIKGFELPDTPQGLIGEARKLNASIVTFVEIPLTSDVSLTVSSCGGGLQTSPAPVVTTPPKDTCSPELLMSLIQPKCGNDVMTLALNKKLVQTLQCTITGLAFWDSSCQAKDQDGHLVLSSTYSSCGMKVTDHVISNEVIINLPSGLPPLRKKVQCIDMDSLSFQLGLYLSPHFLQASNTIELGQQGFVQVSMSPLTSEVTVQLDSCHLDLGPEGDMVELIQSRAAKGSCVSLLSPSPEGDPRFSFLLRVYMVPTPAAGTLSCNLALHPSTLSQEVYKTVSMRLNIVSPDLSGKGLVLPSVLGITFGAFLIGALLTAALWYIYSHTREAEQPQAGNHRP
Protein: Zinc finger CCCH domain-containing protein 4 (Q6ZPZ3)
Organism: Mus musculus (Mouse)
Function: RNA-binding protein that suppresses transcription of long non-coding RNAs (lncRNAs). LncRNAs are defined as transcripts more than 200 nucleotides that are not translated into protein. Together with WDR82, part of a transcription termination checkpoint that promotes transcription termination of lncRNAs and their subsequent degradation by the exosome. The transcription termination checkpoint is activated by the inefficiently spliced first exon of lncRNAs.
Subcellular location: Chromosome {ECO:0000269|PubMed:33767452}. Note=Recruited at sites of high RNA polymerase II occupancy. {ECO:0000269|PubMed:33767452}.
Interaction partners:
- Cleavage and polyadenylation specificity factor subunit 1
- Symplekin
- Homeobox protein goosecoid
Sequence:
MEAVPGTPPPPPSESPPPPSPPPPSTPSPPPCSPDGRAATPHLLHHRLPLPDDREDGELEEGELEDDGAEEVQDPPGGQERSRKEKGEKHHSDSEEEKSHRRLKRKRKKEREKEKRRSKKRRKSKHKRHASSSDDFSDFSDDSDFSPSEKSHRKYRDYSPPYAPSHQQYSSSHNAPLPKKSYSKMDSKGYSMYEDYENEQYGEYEGDEEEDMGKEDYDDFTKELNQYRRAKEGSSRGRGSRGRGRGYRGRGSRGGSRGRGMGRGSRGRGRGSMGEHPEDEEDLYEEEIEYGESEEPMGDDDYDDYSKELNQYRRSKDSRGRGLSRGRGRGSRGGRGKGMGRGRGRGGRGGMSKGGMNDDEDFYDDDMGDGGGGSYRRSDHDKPHQQSDKKGKVICKYFVEGRCTWGDHCNFSHDIELPKKRELCKFYITGFCARAENCPYMHGDFPCKLYHTTGNCINGDDCMFSHDPLTEETRELLDKMLADDAEAGAEDEKEVEELKKQGINPLPKPPPGVGLLPTPPRPPGPPAPTSPNGRPMQGGPPPPPPPPPPPPGPPQMSLPTHEPLSPQQLQQDMYNKKIPSLFEIVVRPTGQLAEKLGVRFPGPGGPSGPMGPGPNMGPPGPMGGPMHPDMHPDMHPDMHPDMHPDMHPDMHPDMHPDMHPDMPMGPGMNPGPPMGPGGPPMMPYGPGDSPHSGMMPPIPPAQNFYENFYPQQEGMEMEPGLVGDAEDYGHYEELPGQPGEPLFPEHPLEPDSFPEGGPPGRPKAGAGVPDFLPSAQRALYLRIQQKQQEEERARRLAESSKQDRENEEGDTGNWYSSDEDEGGSSVTSILKTLRQQTSSRPQASVGEPSSSGLGDPRLQKGHPTGSRLSDPRLSRDPRLSRHAETSGGSGPGDSGPSDPRLARALPTSKAEGSLHSSPAGPSSSKGQPPAEEEEGERALREKAVNIPLDPLPGHPLRDPRSQLQQFSHIKKDVTLSKPSFARTVLWNPEDLIPLPIPKQDVPPVPAALQSLPALDPRLHRSTPPGPPNTRQRPGSTDPSTSGSNLPDFELLSRILKTVNVNTPGQSEKPSDPRVRKTPTDPRLQKPADPVAASRAAKPCPTEASPPAASPSGDSSPPATAPYDPRVLAAGGLGQGSSSGQSSVLSGISLYDPRTPNAGGKTAEPASDTSAQPKGPEGNGKGSASKAKEPPFVRKSALEQPETGKASTDGATATDRYNSYNRPRPKATAAPTAASSTPPPEGATPQPGVHNLPVPTLFGTVKPAPKTGTGSPFAGNSPAREGEQDAGSLKDVFKGFDPTASPFCQ
Protein: BolA-like protein 1 (Q9D8S9)
Organism: Mus musculus (Mouse)
Function: Acts as a mitochondrial iron-sulfur (Fe-S) cluster assembly factor that facilitates (Fe-S) cluster insertion into a subset of mitochondrial proteins (By similarity). Probably acts together with the monothiol glutaredoxin GLRX5. May protect cells against oxidative stress (By similarity).
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9Y3E2}.
Interaction partners:
- BolA-like protein 2
- Glutaredoxin-3
- Glutaredoxin-related protein 5, mitochondrial
- BolA-like protein 3
- Iron-sulfur cluster assembly enzyme ISCU
- Anamorsin
- NFU1 iron-sulfur cluster scaffold homolog, mitochondrial
- Iron-sulfur cluster assembly 2 homolog, mitochondrial
- Frataxin, mitochondrial
- Ferredoxin-2, mitochondrial
Sequence:
MLSARSAQCMVSMATRSCVSRGSAGSAAAGPVEAAIRAKLEQALSPEVLELRNESGGHAVPAGSETHFRVAVVSSRFEGMSPLQRHRLVHEALSEELAGPVHALAIQAKTPAQWRENPQLDISPPCLGGSKKTRGTS
Protein: Killer cell lectin-like receptor 6 (Lymphocyte antigen 49f) (Ly-49f) (T-cell surface glycoprotein Ly-49F) (Q60653)
Organism: Mus musculus (Mouse)
Function: Receptor on natural killer (NK) cells for class I MHC.
Subcellular location: Membrane; Single-pass type II membrane protein.
Interaction partners:
- Killer cell lectin-like receptor 4
Sequence:
MSEPEVTYSTVRLHKSSRLQKLVRHEETQGPREAGYRKCSVCWQLIVKALGILCFLLLITVAVLAVKIFQYGQHNQEIHETLNYHHNCSNMQSDFNLKEEMLTNRSIDSRPGNELLESLNREQNRGYSETKTDLDSSQDTGTGVKYWFCYRTKCYYFIMNKNTWSGCKQNCQHYSLPLVKIDDENELKFLQFQVIPDSYWIGLSYDKEKKEWAWIDNGQSKLDMKIRKMNFKPGGCVFLSKRRLEDTNCKNSHYCICGKKLDKFPH
Protein: Internal virion protein gp16 (Ejection protein gp16) (E protein gp16) (Q01146)
Organism: Salmonella phage P22 (Bacteriophage P22)
Function: Inner capsid protein that plays a role in viral DNA ejection into the host cell.
Subcellular location: Virion {ECO:0000269|PubMed:328927}.
Interaction partners:
Sequence:
MKVTANGKTFNFPDGTSTEDIGAAVDEYFAGQASAAETQPAEQQEEPQQPEQSLMQRAGDLLTGGQSAGQIAEQAGRGLVNIPFDVLQGGASLINAISQGLGGPKVLDDVYRPVDRPTDPYAQAGESIGGYLIPGAGVAGNMAIGSVAEAANQQGDFAGNVAKNAAVNLGAQGLLSGAAKLVGRGITAARGEIAPEARQLIDTAESMGVKPMTSDMIKPGNAFTRSLMQGGEGALLGTGGKRAEQYAIRSKLLGDYFDRVGGYNPDDIVKSMTSTVGGRKNAAGAVRDEIVNRMGSAPVGTTNSINAIDTNIARLEKLGTSADQRLLTALKNLKGELNSGNVDFDLLQQHRTAFRTNVQGDAMVFPNQAKAATNMVENAMTRDLRNAVGKSLGPQDAAKYLKSNSDFANIYNKVLNKRISNTLNKARSEYTPELINTVVFSRKPSDIKRIWSSLDNKGKDAMRAAYISKIAEKTGDSPAKFITEVNKLKAQSGGEIYNTIFSGRHMKELDALHDVLRQTARSDSANVVTQTGQALANPVRLGAAIPTLGKSLAAEAGYGLAMRVYESKPIRNMLLRLANTKPGTPAYERALNQAATAVRPLLANEATRQ
Protein: Complement factor H-related 4 (E9Q8B6)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGFCSMLLLSNILLTAWLSTAKGEVKSCEFPQFKYGRLYYEEILRPNFPVSIGNKYSYKCDNGFSPPSGIFWDYLRCTVQGWEPEVPCVRKCVFHYVENGQSAYWEKIYVQGQSLKVQCYNGYSLQNGQDTMTCTENGWSPPPKCIRIKTCSVSDIEIENGFFSESFRTYALNRETSYRCKQGYVTNTGETSGSITCLQNGWSPQPSCIKSCERPVFENSVTKNNSTWFKLNDKLDYECLIGYENEYKHTKGSITCTYYGWSDTPSCYEIECSVPILDRKLVVSPRKEKYRVGDLLEFSCRSGHRVGPDSVQCYHFGWSPSFPTCKAGQVASCAQPPEIPNGEINGAKRVEYSHGEVVGYDCKPRFLLKGPNKIQCVDGMWTTLPVCVEEERTCGDIPELEHGSVKFSVPPYHHGDSVEFTCAETFTMIGLGSVFCLSGKWTQLPKCVATDQLEKCRVLKSTDIEAIKPKRKEFQHNSTMYYKCRDKQEYEHSICINGKWNPEPNCIRKISCPPPPQIPNTQVIETTVKYLDGEKLSVLCQDNYLTQDPEEMMCKDGRWQSLPHCIEKIPCSQPPTIEHGSIKLPRTSEKRRKSIEFSSHEHGTTFSYVCDDGFRIPEENGVACYMGKWSTPPRCVGLPCGPPPSIPLGTVSLELESYQHGEEVTYHCSTGFGIDGPALIKCEGGKWSDPPKCINSRGKCGPPPPIDNGDITSLSLPEYEPFSSVDYQCQKYYLLKGKKTITCRNGKWSEPPTCLHACIIPENIMEARKIILKWRHTKNIYSHSGEDIEFECKYGYHKARGSPPFRTKCISGTINYPICE
Protein: Myosin-14 (Myosin heavy chain 14) (Myosin heavy chain, non-muscle IIc) (Non-muscle myosin heavy chain IIc) (NMHC II-C) (Q6URW6)
Organism: Mus musculus (Mouse)
Function: Cellular myosin that appears to play a role in cytokinesis, cell shape, and specialized functions such as secretion and capping.
Interaction partners:
- Myosin light polypeptide 6
- Myosin-11
- Myosin regulatory light polypeptide 9
- Actin, cytoplasmic 1
- Myosin-9
- Myosin, light chain 12A, regulatory, non-sarcomeric
- Actin, cytoplasmic 2
- Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
- Myosin regulatory light chain 12B
- Actin, aortic smooth muscle
Sequence:
MAAVTMSVSGRKVASRPGPVPEAAQSFLYAPRTPNVGGPGGPQVEWTARRMVWVPSELHGFEAAALRDEGEEEAEVELAESGRRLRLPRDQIQRMNPPKFSKAEDMAELTCLNEASVLHNLRERYYSGLIYTYSGLFCVVINPYKQLPIYTEAIVEMYRGKKRHEVPPHVYAVTEGAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAHVASSPKGRKEPGVPASVSTMSYGELERQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDIAGYIVGANIETYLLEKSRAIRQAKDECSFHIFYQLLGGAGEQLKADLLLEPCSHYRFLTNGPSSSPGQERELFQETLESLRVLGLLPEEITAMLRTVSAVLQFGNIVLKKERNTDQATMPDNTAAQKLCRLLGLGVTDFSRALLTPRIKVGRDYVQKAQTKEQADFALEALAKATYERLFRWLVLRLNRALDRSPRQGASFLGILDIAGFEIFQLNSFEQLCINYTNEKLQQLFNHTMFVLEQEEYQREGIPWTFLDFGLDLQPCIDLIERPANPPGLLALLDEECWFPKATDKSFVEKVAQEQGSHPKFQRPRNLRDQADFSVLHYAGKVDYKASEWLMKNMDPLNDNVAALLHQSTDRLTAEIWKDVEGIVGLEQVSSLGDGPPGGRPRRGMFRTVGQLYKESLSRLMATLSNTNPSFVRCIVPNHEKRAGKLEPRLVLDQLRCNGVLEGIRICRQGFPNRILFQEFRQRYEILTPNAIPKGFMDGKQACEKMIQALELDPNLYRVGQSKIFFRAGVLAQLEEERDLKVTDIIVSFQAAARGYLARRAFQRRQQQQSALRVMQRNCAAYLKLRNWQWWRLFIKVKPLLQVTRQDEVLQARAQELQKVQELQQQSAREVGELQGRVAQLEEERTRLAEQLRAEAELCSEAEETRARLAARKQELELVVTELEARVGEEEECSRQLQSEKKRLQQHIQELESHLEAEEGARQKLQLEKVTTEAKMKKFEEDLLLLEDQNSKLSKERRLLEERLAEFSSQAAEEEEKVKSLNKLRLKYEATISDMEDRLKKEEKGRQELEKLKRRLDGESSELQEQMVEQKQRAEELLAQLGRKEDELQAALLRAEEEGGARAQLLKSLREAQAGLAEAQEDLEAERVARAKAEKQRRDLGEELEALRGELEDTLDSTNAQQELRSKREQEVTELKKALEEESRAHEVSMQELRQRHSQALVEMAEQLEQARRGKGVWEKTRLSLEAEVSELKAELSSLQTSRQEGEQKRRRLESQLQEVQGRSSDSERARSEAAEKLQRAQAELESVSTALSEAESKAIRLGKELSSAESQLHDTQELLQEETRAKLALGSRVRALEAEAAGLREQMEEEVVARERAGRELQSTQAQLSEWRRRQEEEAAVLEAGEEARRRAAREAETLTQRLAEKTEAVERLERARRRLQQELDDATVDLGQQKQLLSTLEKKQRKFDQLLAEEKAAVLRAVEDRERIEAEGREREARALSLTRALEEEQEAREELERQNRALRAELEALLSSKDDVGKNVHELERARKAAEQAASDLRTQVTELEDELTAAEDAKLRLEVTVQALKAQHERDLQGRDDAGEERRRQLAKQLRDAEVERDEERKQRALAMAARKKLELELEELKAQTSAAGQGKEEAVKQLKKMQVQMKELWREVEETRSSRDEMFTLSRENEKKLKGLEAEVLRLQEELAASDRARRQAQQDRDEMAEEVASGNLSKAATLEEKRQLEGRLSQLEEELEEEQNNSELLKDHYRKLVLQVESLTTELSAERSFSAKAESGRQQLERQIQELRARLGEEDAGARARQKMLIAALESKLAQAEEQLEQESRERILSGKLVRRAEKRLKEVVLQVDEERRVADQVRDQLEKSNLRLKQLKRQLEEAEEEASRAQAGRRRLQRELEDVTESAESMNREVTTLRNRLRRGPLTFTTRTVRQVFRLEEGVASDEEEAEGAEPGSAPGQEPEAPPPATPQ
Protein: Cytochrome b5 reductase 4 (EC 1.6.2.2) (Flavohemoprotein b5/b5R) (b5+b5R) (N-terminal cytochrome b5 and cytochrome b5 oxidoreductase domain-containing protein) (cb5/cb5R) (Q7L1T6)
Organism: Homo sapiens (Human)
Function: NADH-cytochrome b5 reductase involved in endoplasmic reticulum stress response pathway. Plays a critical role in protecting pancreatic beta-cells against oxidant stress, possibly by protecting the cell from excess buildup of reactive oxygen species (ROS). Reduces a variety of substrates in vitro, such as cytochrome c, feericyanide and methemoglobin.
Subcellular location: Endoplasmic reticulum {ECO:0000269|PubMed:10611283, ECO:0000269|PubMed:15131110}. Note=Soluble protein.
Interaction partners:
- Cytochrome b5
- Cytochrome b5 type B
- Dihydroorotate dehydrogenase
- Dihydropyrimidine dehydrogenase [NADP
- Uridine 5'-monophosphate synthase
- Stearoyl-CoA desaturase
- NADPH:adrenodoxin oxidoreductase, mitochondrial
- Cytochrome c
- NADPH--cytochrome P450 reductase
Sequence:
MLNVPSQSFPAPRSQQRVASGGRSKVPLKQGRSLMDWIRLTKSGKDLTGLKGRLIEVTEEELKKHNKKDDCWICIRGFVYNVSPYMEYHPGGEDELMRAAGSDGTELFDQVHRWVNYESMLKECLVGRMAIKPAVLKDYREEEKKVLNGMLPKSQVTDTLAKEGPSYPSYDWFQTDSLVTIAIYTKQKDINLDSIIVDHQNDSFRAETIIKDCLYLIHIGLSHEVQEDFSVRVVESVGKIEIVLQKKENTSWDFLGHPLKNHNSLIPRKDTGLYYRKCQLISKEDVTHDTRLFCLMLPPSTHLQVPIGQHVYLKLPITGTEIVKPYTPVSGSLLSEFKEPVLPNNKYIYFLIKIYPTGLFTPELDRLQIGDFVSVSSPEGNFKISKFQELEDLFLLAAGTGFTPMVKILNYALTDIPSLRKVKLMFFNKTEDDIIWRSQLEKLAFKDKRLDVEFVLSAPISEWNGKQGHISPALLSEFLKRNLDKSKVLVCICGPVPFTEQGVRLLHDLNFSKNEIHSFTA
Protein: Cilia- and flagella-associated protein 300 (A0CY51)
Organism: Paramecium tetraurelia
Function: Cilium- and flagellum-specific protein that plays a role in axonemal structure organization and motility. Plays a role in outer and inner axonemal dynein arm assembly.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29727692}. Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:29727692}. Note=Localizes predominantly in the cytoplasm and weakly in cilia. Transported within cilia in an intraflagellar transport (IFT)-dependent manner. Accumulates at the ciliary tips during ciliogenesis. {ECO:0000269|PubMed:29727692}.
Interaction partners:
- non-specific serine/threonine protein kinase
- Chromosome undetermined scaffold_13, whole genome shotgun sequence
- Chromosome undetermined scaffold_160, whole genome shotgun sequence
- Chromosome undetermined scaffold_6, whole genome shotgun sequence
- Chromosome undetermined scaffold_301, whole genome shotgun sequence
- Chromosome undetermined scaffold_130, whole genome shotgun sequence
- Chromosome undetermined scaffold_97, whole genome shotgun sequence
- Chromosome undetermined scaffold_33, whole genome shotgun sequence
- Chromosome undetermined scaffold_160, whole genome shotgun sequence
- Chromosome undetermined scaffold_151, whole genome shotgun sequence
Sequence:
MQIESDNQVTNQSYSFFRQENTILDDKKFMEILQKWGLQHSIKVSTFLFDIKFDHLNPNQFLLDLFNSKDVRGSLHYVSFKQNVLLSQIKFQPLTCKSIKLDLFDKLTEDKIVVKGHIKQCFEEQFENIQIADELRKALVLEDSEQYCVFNEADRQELLFKLFQILVLGGQLCQYEDEIQAYLDWTKYLYKNTVNARKYADKDEIYIDSYAYDIRKLENSYSSDHPQNVMYVVVNPSLRIVNIIENQWLKVW
Protein: Bifunctional heparan sulfate N-deacetylase/N-sulfotransferase (EC 2.8.2.8) (Glucosaminyl N-deacetylase/N-sulfotransferase) (Sulfateless) [Includes: Heparan sulfate N-deacetylase (EC 3.-.-.-); Heparan sulfate N-sulfotransferase (EC 2.8.2.-)] (Q9V3L1)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential bifunctional enzyme that catalyzes both the N-deacetylation and the N-sulfation of glucosamine (GlcNAc) of the glycosaminoglycan in heparan sulfate. Modifies the GlcNAc-GlcA disaccharide repeating sugar backbone to make N-sulfated heparosan, a prerequisite substrate for later modifications in heparin biosynthesis. Plays a role in diffusion of morphogen wingless (wg) via its role in heparan sulfate proteoglycans (HSPGs) biosynthesis, HSPGs being required for movement of wg morphogens. Required for wg signaling during both embryonic and imaginal disk development. Also required for FGF receptor signaling.
Subcellular location: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.
Interaction partners:
- heparosan-N-sulfate-glucuronate 5-epimerase
- Division abnormally delayed protein
- Exostosin-3
- Dally-like, isoform A
- Exostosin-2
- Exostosin-1
- UDP-glucose 6-dehydrogenase
- Syndecan
- Heparin sulfate O-sulfotransferase
- Heparan-sulfate 6-O-sulfotransferase
Sequence:
MTISGGNQHNNNANRKYEKLIKQPQMQFGSSVTGTQTDVDSCRDADADANAVRQDFSNFNKHFGNGHAITDRTMLLRLEDDVTTAAGIVTYKGKSNGNGNGNGNGSIGSISLDFNGSPTSSTSIGIASGSSSNTHLASGGGVGGIGGSEPAGWMCHCCNLIARRCFGINVRRCVLALLAITMVSIFYYTHYVDTGVFNGLIQRDTHPAPIINCRMINSGGKHIRNASPAPDHRSEARLRIDPKVLVFVETTYSGLGRDIAELLVYNRIKYKIEVAGKSLPVLTNLDKGRYGVIVFENLDKYLNMDKWNRELLDKYCREYSVGIVGFVSPSEETLVGAQLRDFPLFVNTNLRLRDASLNPLSSVLRLTRAGETAWGALPGDDWAVFQHNHSTYEPVEWAQRNTQEYPADSVGQVQLPLTTVLQDRGQLDGIQRVLFGSSLRFWLHRLVFLDALSYLSHGQLSLNLERMILVDIDDIFVGEKGTRLRPDDVRALIATQKNIAAMVPGFRFNLGFSGKYYHHGTREENLGDDFLLQNVQEFNWFSHMWKHQQPHLYDNLTLLMAEMHLNYAFAVDHNIPTDSGYSISPHHSGVYPAHELLYMAWKKVWNVKVTSTEEYPHLRPARLRRGFIHRNIMVLPRQTCGLFTHTMYIDRYPGGRDKLDESIQGGELFQTIVYNPINIFMTHMSNYGSDRLALYTFQSVIKFLQCWTNLKLASAPPVQLAEMYFRLHPEEVDPVWGNPCDDVRHKKIWSKTKNCDSLPKFLVIGPQKTGTTALYTFLSMHGSIASNIASPETFEEVQFFNGNNYYRGLDWYMDFFPSESLPNTSSPMPTQLGSPRFMFEKSATYFDGEAVPKRSHALLPHAKIVTILISPAKRAYSWYQHQRSHGDVIANNYSFYQVITASDSAPRALKDLRNRCLNPGKYAQHLEHWLAYYPAQQLHIIDGEQLRLNPIDVMNELQRFLKIQPLLDYSNHLRYDVKKGFYCQAVSEKRNKCLGKSKGRQYPAMDERSAKLLQRYYLNHNTALVKLLKKLGSRPIPQWLKDDLSTGT
Protein: Penton protein (CP-P) (Penton base protein) (Protein III) (P12538)
Organism: Human adenovirus C serotype 5 (HAdV-5) (Human adenovirus 5)
Function: Major capsid protein that self-associates to form penton base pentamers, each in the shape of a pentagon, situated at the 12 vertices of the pseudo T=25 capsid. Involved in virus secondary attachment to host cell after initial attachment by the fiber protein. Binds host integrin heterodimer ITGAV-ITGB5 (alphaV-beta5) thereby triggering clathrin-mediated endocytosis of virions. Mediates initial virus attachment to CXADR-negative cells. Binding to integrins ITGAV-ITGB5 also seems to induce macropinocytosis uptake of the virus. As the virus enters the host cell, penton proteins are shed concomitant with virion acidification in the endosome.
Subcellular location: Virion {ECO:0000255|HAMAP-Rule:MF_04052, ECO:0000269|PubMed:20798312}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04052}. Note=Located at each vertex of the virion. Present in 60 copies per virion. {ECO:0000255|HAMAP-Rule:MF_04052}.
Interaction partners:
Sequence:
MRRAAMYEEGPPPSYESVVSAAPVAAALGSPFDAPLDPPFVPPRYLRPTGGRNSIRYSELAPLFDTTRVYLVDNKSTDVASLNYQNDHSNFLTTVIQNNDYSPGEASTQTINLDDRSHWGGDLKTILHTNMPNVNEFMFTNKFKARVMVSRLPTKDNQVELKYEWVEFTLPEGNYSETMTIDLMNNAIVEHYLKVGRQNGVLESDIGVKFDTRNFRLGFDPVTGLVMPGVYTNEAFHPDIILLPGCGVDFTHSRLSNLLGIRKRQPFQEGFRITYDDLEGGNIPALLDVDAYQASLKDDTEQGGGGAGGSNSSGSGAEENSNAAAAAMQPVEDMNDHAIRGDTFATRAEEKRAEAEAAAEAAAPAAQPEVEKPQKKPVIKPLTEDSKKRSYNLISNDSTFTQYRSWYLAYNYGDPQTGIRSWTLLCTPDVTCGSEQVYWSLPDMMQDPVTFRSTRQISNFPVVGAELLPVHSKSFYNDQAVYSQLIRQFTSLTHVFNRFPENQILARPPAPTITTVSENVPALTDHGTLPLRNSIGGVQRVTITDARRRTCPYVYKALGIVSPRVLSSRTF
Protein: At3g48510 (AtIII18x5-like protein) (Q9SMP6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Short-chain dehydrogenase reductase 4
- Short-chain dehydrogenase reductase 3a
Sequence:
MDGRGGCCIARYAIGSGPYDLSKADRIMLRFRPIAPKPASPGGVNPVSSGDSGGGSSDVSFRSASRRKRKCHQLKENGGNAKRCTRRKTSDKPVVHGSANAVTLSLLPEKPIDLKAAVEKQKRQGPLWLSFKDGGGMLTPAYQTPEIVQRTVVISSCMTVERVTDAWIDGYGLGRSDEERKMNLVRDTCPGFISDGSGRVTWTNDAYRKMARDIIPVEEGAPEITSGDSFHVIVRLVMRERPMLTSPGFTCRMKLQYTCQNRERGSVTVPCDVWRMDVGGGFAWRLDVKAALCL
Protein: NADPH--cytochrome P450 reductase 2 (CPR) (OsCPR2) (P450R) (EC 1.6.2.4) (Q0J705)
Organism: Oryza sativa subsp. japonica (Rice)
Function: This enzyme is required for electron transfer from NADP to cytochrome P450 in microsomes (By similarity). It can also provide electron transfer to heme oxygenase and cytochrome B5 (By similarity). Can reduce cytochrome c in vitro.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03212, ECO:0000269|PubMed:23053415}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03212}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03212}.
Interaction partners:
- Probable 5'-adenylylsulfate reductase 1, chloroplastic
- Os05g0503300 protein.
- Nitrate reductase
- Nitrate reductase
- Nitrate reductase 1
- Os02g0765900 protein
- Ferredoxin--nitrite reductase, chloroplastic
- Os01g0357500 protein
- Anamorsin homolog 2
- Anamorsin homolog 1
Sequence:
MESSAGPMELVAALLRGLTPRAEQLLQLSSGGGEAAAGGAAEARAAVATVAAALLGCAFLVLWRRVSAGRKRKREEAERSAAAVAGVGKGGKNASAAAGEEAGGADGRKRVTVFFGTQTGTAEGFAKALAEEAKSRYDKAIFKVVDLDEYAMEDEEYEERLKKEKISLFFVATYGDGEPTDNAARFYKWFTEGNERGVWLNDFQYAIFGLGNRQYEHFNKVAKVVDELLVEQGGKRLVPVGLGDDDQCIEDDFNAWKETLWPELDQLLRDENDVSTGTTYTAAIPEYRVEFVKPDEAAHLERNFSLANGYAVHDAQHPCRANVAVRRELHTPASDRSCTHLEFDIAGTGLTYETGDHVGVYTENCLEVVEEAERLLGYSPEAFFTIHADKEDGTPLGGGSLAPPFPSPITVRNALARYADLLNSPKKSALVALATYASDSTEADRLRFLASPAGKDEYAQWVVASQRSLLEVMAEFPSAKPPLGVFFAAVAPRLQPRYYSISSSPSMAPTRIHVTCALVHEKTPAGRVHKGVCSTWIKNAIPSEETKDCSWAPVFVRQSNFKLPADPSVPVIMIGPGTGLAPFRGFLQERLSQKQSGAELGRSVFFFGCRNSKMDFIYEDELNTFLEEGALSELVLAFSREGPTKEYVQHKMSQKASEIWDMISQGGYIYVCGDAKGMARDVHRVLHTIVQEQGSLDSSKAESFVKSLQTEGRYLRDVW
Protein: Candida glabrata strain CBS138 chromosome I complete sequence (Q6FR42)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- glycerol-1-phosphatase
- glycerol kinase
- alcohol dehydrogenase
- alcohol dehydrogenase
- Candida glabrata strain CBS138 chromosome F complete sequence
- glycerol-1-phosphatase
- glycerol-1-phosphatase
Sequence:
MAALHKNTSTLKLNTGAHIPVIGLGTWQSSENEGYNATLEALKAGYRHIDTAAIYKNEEEIGRAIRDSNIPRNELFVTTKLWGTQHRNPTEALDQSLKRLGLDYVDLYLMHWPVALKTDLIKDGNLLQIPEREDGSRDVDLEDWNFVKTWELMQELPKEKARAIGVSNFSINNLKELLNSKGNKVVPAANQIEIHPLLPQDELINFCKEKGIVLEAYSPLGSTDAPILKEEEITEIAKKNGVNAGQLVISWHAQRGYVVLPKSVKPERIHGNQETFKLSDEDFATLSNYAKKHGERRVVSPNWGPFKPFV
Protein: Bifunctional diacylglycerol cholinephosphotransferase/ethanolaminephosphotransferase (Q59M00)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
- Phosphatidyl-N-methylethanolamine N-methyltransferase
- Phosphatidylserine decarboxylase proenzyme 2
- choline-phosphate cytidylyltransferase
- ethanolamine-phosphate cytidylyltransferase
- Phosphatidylethanolamine N-methyltransferase
- Bifunctional choline kinase/ethanolamine kinase
- Phospholipase
- Phosphatidate phosphatase
- Lysophospholipid acyltransferase
Sequence:
MGLFIPTNKLQNLKLYKYSSEDHSIISKYILKKWWNFFVQIFPLSMAPNVVTLLGLFFIIGNLMTVFYYDPYLNETQPTWCYFFYAFGLFMYQTFDGCDGCHARRTGQSGPLGELFDHSIDAINTTLGTFVFASVLKMGYGGLLLLSQFASVCNFYTSTWEEYHTHTLFLSKFSGPVEGILMICIVYIITGIFGPDIWTIDLFELNLTSLGYGYYKVDTSIIYTIIGLTSLYFNIASAMFNVSKHYKKSSTNNSTNGDKDESTKDQISQAYRGLYPFFIYYGFVFLLLWIYPQILYDYGFPLVISIGCTIAFSVGRIILAHLTLQEFPFIQYPMFVPIGQLILSKILIDIYGYGTAKVLHAISWLGCGITLGIHGIFVAEVITEITTYLDIYALSIKHKKIN