wanglab/gogpt-training-data huggingface dataset:
Protein: Chondroitin sulfate N-acetylgalactosaminyltransferase 1 (CsGalNAcT-1) (EC 2.4.1.174) (Chondroitin beta-1,4-N-acetylgalactosaminyltransferase 1) (Beta4GalNAcT-1) (Q8BJQ9)
Organism: Mus musculus (Mouse)
Function: Transfers 1,4-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to the non-reducing end of glucuronic acid (GlcUA). Required for addition of the first GalNAc to the core tetrasaccharide linker and for elongation of chondroitin chains. Important role in chondroitin chain biosynthesis in cartilage formation, and subsequent endochondral ossification. Moreover, is involved in the metabolism of aggrecan.
Subcellular location: Golgi apparatus, Golgi stack membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Galactosylgalactosylxylosylprotein 3-beta-glucuronosyltransferase 3
- Chondroitin sulfate synthase 2
- Chondroitin sulfate synthase 1
- Hexosyltransferase
- Chondroitin sulfate synthase 3
- Chondroitin sulfate N-acetylgalactosaminyltransferase 2
- Carbohydrate sulfotransferase 11
Sequence:
MVRRGLLGWISRVVILLVLLCCAISVLYMLACTPKGDQEQLGLPRANGPTGKDGYQAVLQEREEQHRNYVNSLKRQIAQLKDELQARSEQFRSGQDQASDATSLRSGWDREPKAQADLLAFLRGQVDKAEVHAGVKLATEYAAVPFDSFTLQKVYQLETGLTRHPEEKPVRKDKRDELVEAIESALESLNSPVESSPHQRPYTAADFIEGIYRTERDKGTLYELTFKGDHKHEFQRLVLFRPFGPIMKVKKEKLNLANTLINVIVPLARRVDKFRHFMQNFREMCIQQDGRVHLTVVYFGKEEMNEVKGILENTSKAANFRNFTFIQLNGEFSRGKGLDVGARFWKGSNVLLFFCDVDIYFTSEFLNTCRLNTQPGKKVFYPVLFSQYNPGVIYGHHDAVPPLGQQLVIKKETGFWRDFGFGMTCQYRSDFINIGGFDLDIKGWGGEDVHLYRKYLHSNLIVVRTPVRGLFHLWHEKHCMDELTPEQYKMCMQSKAMNEASHGQLGMLVFRHEIEAHLRKQKQKASSKKT
Protein: Rap1 GTPase-GDP dissociation stimulator 1 (F1M7Y3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
Sequence:
MDNLSDALKKLKITAADKTEGSLEGCLDCLLQALAQNNAETSEKIQGSGILQLFANLLTPQASCTAKVANIIAEVAKNEFMRIPCVDAGLISPLVQLLNSKDQEVLLQTGRALGNICYDSHSLQAQLINMGVIPTLVKLLGIHCHNAALTEMCLVAFGNLAELESSKEQFASTNIAEELVKLFKKQIEHDKREMIFEVLAPLAENDAIKLQLVEAGLVECLLEIVQQKVDSTKEDDLAELKTASDLMVLLLLGDESMQKLFEGGKGSVFQRVLSWIPSNSQQLQLAGALAIANFARNDGNCIHMVDNGIVEKLMDLLDRHVEDGNVTVQHAALSALRNLAIPVVNKAKMLSAGVTETVLKFLKSEMPPVQFKLLGTLRMLIDAQAEAAEQLGKNAKLVERLVEWCEAKDHAGVMGESNRLLSALIRHSKSKDVIKTIVQSGGIKHLVTMATSEHVIMQNEALVALALIAALELGPAEKDLASAQLVQILHRLLADERSAPEIKYNSMVLICALMGSEALHKEVQDLAFLDVVSKLRSHENKSVAQQASLTEQRLTVQS
Protein: CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase (EC 2.4.3.-) (Alpha-2,8-sialyltransferase 8D) (Polysialyltransferase) (Polysialyltransferase-1) (Sialyltransferase 8D) (SIAT8-D) (Sialyltransferase St8Sia IV) (ST8SiaIV) (Q92187)
Organism: Homo sapiens (Human)
Function: Catalyzes the polycondensation of alpha-2,8-linked sialic acid required for the synthesis of polysialic acid (PSA), which is present on the embryonic neural cell adhesion molecule (N-CAM), necessary for plasticity of neural cells.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:9852130}; Single-pass type II membrane protein {ECO:0000305}. Secreted {ECO:0000269|PubMed:9852130}.
Interaction partners:
- Neural cell adhesion molecule 1
Sequence:
MRSIRKRWTICTISLLLIFYKTKEIARTEEHQETQLIGDGELSLSRSLVNSSDKIIRKAGSSIFQHNVEGWKINSSLVLEIRKNILRFLDAERDVSVVKSSFKPGDVIHYVLDRRRTLNISHDLHSLLPEVSPMKNRRFKTCAVVGNSGILLDSECGKEIDSHNFVIRCNLAPVVEFAADVGTKSDFITMNPSVVQRAFGGFRNESDREKFVHRLSMLNDSVLWIPAFMVKGGEKHVEWVNALILKNKLKVRTAYPSLRLIHAVRGYWLTNKVPIKRPSTGLLMYTLATRFCDEIHLYGFWPFPKDLNGKAVKYHYYDDLKYRYFSNASPHRMPLEFKTLNVLHNRGALKLTTGKCVKQ
Protein: Rhomboid-like protein 19 (AtRBL19) (Q8LF05)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable rhomboid-type serine protease that catalyzes intramembrane proteolysis.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Rhomboid-like protein 18
- Rhomboid-like protein 20
- Transducin family protein / WD-40 repeat family protein
- Rhomboid-like protein 17, chloroplastic
- RHOMBOID-like protein 13
- Rhomboid-like protein 15
- RHOMBOID-like protein 10, chloroplastic
- Rhomboid-like protein 16, chloroplastic
- Large ribosomal subunit protein eL36z
- RHOMBOID-like protein 3
Sequence:
MSSPGTSMFTNFTKLCKGLALVLVVGHLVVQFIPATVPYLALIPARTIPFAWNLITSGYFELSVYGVVFSTVSLLFMGKFLEPVWGSTEFLKFIFVVNFLTYLCVFVTAIALYYITRLEVYLYMPFAGFHGVLAGLLVGIKQIIPDQEILLLKIKAKWLPSIMLILSIASSFFTLDSAAYLPTLIFGTYMGWLYLRYLQRRPETKLRGDPSDDFAFSTFFPELLRPVIDPIALIFHRMLCGRSNATSEDHDYSTSGAPLPGSDSAEASRRRERGARALEERLGTERLVPARNKDELQSDGLDNV
Protein: Serine/threonine protein phosphatase 2A 57 kDa regulatory subunit B' kappa isoform (AtB' kappa) (PP2A, B' subunit, kappa isoform) (Q93YV6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: The B regulatory subunit may modulate substrate selectivity and catalytic activity, and may also direct the localization of the catalytic enzyme to a particular subcellular compartment.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:26517938}.
Interaction partners:
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A alpha isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B beta isoform
- Serine/threonine protein phosphatase 2A 55 kDa regulatory subunit B alpha isoform
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A beta isoform
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''epsilon
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''delta
- Serine/threonine protein phosphatase 2A regulatory subunit B''beta
- Serine/threonine protein phosphatase 2A regulatory subunit B''alpha
- Probable serine/threonine protein phosphatase 2A regulatory subunit B''gamma
- Serine/threonine-protein phosphatase 2A 65 kDa regulatory subunit A gamma isoform
Sequence:
MFKQFLSKLPRKSSKSDSGELNRSSSGPVSSPVQRSGTSGGGSGPVRSNSGKRMSSAVFPASVVAGIEPLVPFKDVPSSEKLNLFVSKVSLCCVTFDFSDPGKNSIEKDVKRQTLLELLDFVASGSVKFTEPAILAMCRMCAVNLFRVFPPNYRSSSGGENDDDEPMFDPAWPHLQIVYDLLLKFITSPCLDAKVAKKYLDHAFIVRLLDLFDSEDPRERECLKTILHRVYGKFMVHRPFVRKSMSNIFYRFVFETEKHSGIAELLEIFGSIVSGFALPLKEEHKIFLWRVLIPLHKPKSVGNYFQQLSYCITQFIDKEPKLGSVVIKGLLKFWPITNSQKEVMFLGEVEEIVEAMSVMEFQKIMVPLFLRIACCVTSSHFQVSERALFLWNNDQIVNLIGHNRQAILPIMFTALEKNAQNHWNQSVLNLTLNVRKMFCEMDEALFMSCHARFKEDEAKQCSAAEKRKEVWARLENAASMKPITGKTAVLVTPRATSIAC
Protein: SOSS complex subunit B2 (Nucleic acid-binding protein 1) (Oligonucleotide/oligosaccharide-binding fold-containing protein 2A) (Sensor of single-strand DNA complex subunit B2) (Sensor of ssDNA subunit B2) (SOSS-B2) (Single-stranded DNA-binding protein 2) (hSSB2) (Q96AH0)
Organism: Homo sapiens (Human)
Function: Component of the SOSS complex, a multiprotein complex that functions downstream of the MRN complex to promote DNA repair and G2/M checkpoint. In the SOSS complex, acts as a sensor of single-stranded DNA that binds to single-stranded DNA, in particular to polypyrimidines. The SOSS complex associates with DNA lesions and influences diverse endpoints in the cellular DNA damage response including cell-cycle checkpoint activation, recombinational repair and maintenance of genomic stability. Required for efficient homologous recombination-dependent repair of double-strand breaks (DSBs) and ATM-dependent signaling pathways.
Subcellular location: Nucleus {ECO:0000269|PubMed:19605351, ECO:0000269|PubMed:19683501}. Note=Localizes to nuclear foci following DNA damage.
Interaction partners:
- Integrator complex subunit 3
- Integrator complex subunit 5
- SOSS complex subunit C
- SOSS complex subunit B1
- Integrator complex subunit 6
- Integrator complex subunit 11
Sequence:
MNRVNDPLIFIRDIKPGLKNLNVVFIVLEIGRVTKTKDGHEVRSCKVADKTGSITISVWDEIGGLIQPGDIIRLTRGYASMWKGCLTLYTGRGGELQKIGEFCMVYSEVPNFSEPNPDYRGQQNKGAQSEQKNNSMNSNMGTGTFGPVGNGVHTGPESREHQFSHAGRSNGRGLINPQLQGTASNQTVMTTISNGRDPRRAFKR
Protein: Protein kinase superfamily protein (F4I854)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MGCICSKGVRTNDDYIETNHVSIGKENPKASKKQSDSEETSVNGNEATLRLIPDDVKDTFSDEEVEELEEKKESSFEMKSCESVLQKGNVLEIVDNVGPLQPRMSRIGSVSNGDRAAKVIAGWPSWLVSVAGEAINGWIPRSADSFEKLEMIGQGTYSSVYRARDLETNQIVALKKVRFANMDPESVRFMAREIIILRRLNHPNVMKLEGLIISKASGSMYLIFEYMDHDLAGLASTPGIKFSQAQIKCYMKQLLLGLEHCHSCGVLHRDIKCSNLLLDRNNNLKIGDFGLSNFYRGQRKQPLTSRVVTLWYRPPELLLGSTDYGVTVDLWSTGCILAELFTGKPLLPGRTEVEQMHKIFKLCGSPSEEYWRRSRLRHATIFKPQHPYKRCVADTFKDLPSSALALLEVLLAVEPDARGTASSALQSEFFTTKPFPSEPSSLPRYQPRKEFDAKLREEEARRRKGSSSKQNEQKRLARESKAVPAPSANAELLASIQKRLGETNRTSISEKFNPEGDSGNGFRIEPLKGNTAQNPYPIYTNGDNHPNGSSQLRTQRSYVQRGSGQLSRFSNSMAPTRDGSQFGSMRDAIVNQRWLEDGSENFNLSQRLLEKPNGIRKDDPSSSSKESIMGYDGEKRGRIQYSGPLIPGEGNLDEMLKEHERQILLAVRRAQADKAKRDDNRQAQTLFPANGR
Protein: Coiled-coil domain-containing protein 148 (Q8NFR7)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MCAASASPDNLVFHMKNEMRNIKYKPVDYQQLRALTEAKKLASASAKLKIRKAMLTSKLSKEQTLIKQHKQVWWQEYQRLNEVRCKMESEIKSLLNEENIGNECLCDLTNFEQELSEQQCTYLKNVINPIQQLRADLKYRQHHTLQHSHPHIEFNSMKVLEEVDFVKKQLKTVFERLRLEQQRIENDLSDWSIKILDHSLEEKTNPLSELPIELESLECPYPDLKSSILSEFYKFTQKYQKKLQDFNLQLEDIYRNCQLSEEDHWIYQAILDQYPGDLFGRRTLYLDMLQRYFPHKSRHDLVEHEKYCDQYRFAIEQQNILISNWNKNKKDFIQKAVLTLTEACATHEMESMLAKDKKKQQELCADLKAKVRQWRAHQEEVARLEMEISARRREKEEEKEKLWKKKELLQRAEKKKKIKKYWAKKKQKWQEMEMRDLQRLEELKKLIAEQSLKDRERVKYRQELLERRLMEKKEVALQEAHEDKERARRLEALRKQVAVVAQFDPVRMMSDTMASKARMGIEIEEEFILQKPLFTLNTYNEQQIISDPRLRFELALREAGLHRTLYAKEILPKISPQKPPRKDMESTVFKI
Protein: CSC1-like protein At1g32090 (Q9FVQ5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts as an osmosensitive calcium-permeable cation channel.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:22430844}; Multi-pass membrane protein {ECO:0000269|PubMed:22430844}. Cell membrane {ECO:0000269|PubMed:22430844}; Multi-pass membrane protein {ECO:0000269|PubMed:22430844}.
Interaction partners:
- Ureide permease 4
- Putative vacuolar cation/proton exchanger 6
- DExH-box ATP-dependent RNA helicase DExH16, mitochondrial
- Probable zinc metalloprotease EGY1, chloroplastic
Sequence:
MATLQDIGVSALINLFGAFLFLIAFAVLRIQPINDRVYFPKWYLTGERNSPRRSDRTLVGKFVNLNYKTYFTFLNWMPQAMKMSESEIIRHAGLDSAIFLRIYTLGLKIFAPVMVLALVVLVPVNVSSGTLFFLKKELVVSNIDKLSISNVQPKSSKFFFHIAVEYIFTFWACFMLYREYNNVAIMRLQYLASQRRRPEQFTVVVRNVPDMPGHSVPDTVDQFFKTNHPEHYLCHQAVYNANTYAKLVKQRAKLQRWFDYYVLKHQRNPHKQPTCRTGFLGLWGKRVDSIEYYKQQIKEFDHNMSLERQKVLKDSKLMLPVAFVSFDSRWGAAVCAQTQQSKNPTLWLTSSAPEPRDIYWQNLAIPFISLTIRKLVIGVSVFALVFFYMIPIAFVQSLANLEGLDRVAPFLRPVTRLDFIKSFLQGFLPGLALKIFLWILPTVLLIMSKIEGYIALSTLERRAAAKYYYFMLVNVFLGSIIAGTAFEQLHSFLHQSPSQIPRTIGVSIPMKATFFITYIMVDGWAGIAGEILRLKPLVIFHLKNMFIVKTEEDRVRAMDPGFVDFKETIPSLQLYFLLGIVYTAVTPILLPFILIFFAFAYLVYRHQIINVYNQQYESCGAFWPHVHGRIIASLLISQLLLMGLLASKKAADSTPLLIILPILTLSFHKYCKHRFEPAFRQYPLEEAMAKDKLEKETEPELNMKADLADAYLHPIFHSFEKEVELSSSSSSEKETHQEETPEVRVDKHETQSSSPVTELGTSSHHHHVYNSTSPSSHYASAYEQSSSQYEYHYNTHQYEEHEYRYN
Protein: Pre-mRNA-processing factor 39 (PRP39 homolog) (Q7KRW8)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in pre-mRNA splicing.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- U1 small nuclear ribonucleoprotein 70 kDa
- Putative RNA-binding protein Alsin2
- U1 small nuclear ribonucleoprotein C
- tRNA selenocysteine-associated protein 1
- LD24714p
- RH42690p
- Small nuclear ribonucleoprotein-associated protein B
- Splicing factor 3B subunit 1
- BcDNA.LD23634
- Probable U2 small nuclear ribonucleoprotein A'
Sequence:
MASEGENVVMESPGRRTRSGRKAASPAASLPTRSTRRTSKRNVQLSDHEEEAEEQVVMVQEEEEPFRGTNTAEAPALEPQFEETQHQIEDDVEMLPAEAAGVDEKSSSFPFGTVAELHSETSDDIKETRGQAGVDTLLASLAGDNANSLPSVGGNDESDNVKKADFEYNVDSLQPQMEKMNSSEDSSSQHAIAEDLADADTSNATIVNTEIVSEDELPLPSKPEINDAEEVSDEELPAPQRAELPEDAEVISEDELPASNNNNTATEPKAPLKRKAENESVKSTEDKDASSHESSTKDKSSEQYNPGSPTSESNDAQPSEKKLKVEESEPKEKKKEKERDKDKEKDKDKDNNKDKEKERKKLPDLDKYWRAVKEDSTDFTGWTYLLQYVDNESDAEAAREAYDTFLSHYPYCYGYWRKYADYEKRKGIKANCYKVFERGLEAIPLSVDLWIHYLMHVKSNHGDDETFVRSQYERAVKACGLEFRSDKLWDAYIRWENESKRYHRVVQIYDRLLAIPTQGYNGHFDNFQDLINQHDVTITLANEEVIRLRKDFHERQQSKSSKSSSKHRRDSSSSSKDKDSKEREREKDKDKDKDKDKEKRETVGGGVGKSPKDTSETQVDESDSTTDLTTESESSHAASKPAMQIDFSDLSTLNDEEVVSIRDRAISARRKVHKLTVSAVTARWSFEEGIKRPYFHVKPLERAQLKNWKDYLDFEIEKGDRERVLVLFERCLIACALYDEFWLKMLRYLESLEDQSGVVDLVRDVYRRACRIHHPDKPSLHLMWAAFEECQMNFDDAAEILQRIDQRCPNLLQLSYRRINVERRRGALDKCRELYKHYIESTKNKGIAGSLAIKYARFLNKICHDLDAGLAALQQALERDPANTRVALQMIDLCLQRPKVDEQEVVEIMDKFMARADIEPDQKVLFAQRKVEFLEDFGSTARGLQDAQRALQQALTKAKEAQKKSDGSPSRKNSSSSKEGPVPTGSAAAAYNNGGSAAAVAGYNYGAANPYYGQQNTAAAYPSQTPQQASYDSYYNQWGYGSGGASANSGGSGYNYGQWSGYGNYY
Protein: Ubiquitin carboxyl-terminal hydrolase 5 (EC 3.4.19.12) (Deubiquitinating enzyme 5) (Ubiquitin thioesterase 5) (Ubiquitin-specific-processing protease 5) (Q09879)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Hydrolase that deubiquitinates target proteins (By similarity). Cleaves the UBL propeptide in sde2.
Subcellular location: Nucleus {ECO:0000305|PubMed:28947618}.
Interaction partners:
- Ubiquitin carboxyl-terminal hydrolase 14
- Ubp5-interacting protein ftp105
- Ubiquitin carboxyl-terminal hydrolase 15
- Putative ubiquitin thioesterase otu1
- GMP synthase
- Probable mRNA-splicing protein ubp10
- Ubiquitin thioesterase otu2
- Ubiquitin carboxyl-terminal hydrolase mug105
- Polyubiquitin
- AMSH-like protease sst2
Sequence:
MVTGETLVDSQKSLINNDTLLNEKLKEDFEENVSIDVKIHEELRRALPDYEESGFQRFTWHIKSWHELDRRAVSPQFAVGSRQFKITYFPQGTLQSAGFTSIFLEYIPSEEEKLSNKYGCCCQFAFVISNPRKPSLSVANSAHCRFSPEIVDWGFTQFAELKKLLCRQAPDVPPIVEDGALLLTAYVRILKDPTGVLWHSFNDYDSKIATGYVGLKNQGATCYMNSLLQSLYIIHAFRRIVYQIPTDSPQGKDSIAYALQRCFYNLQFMNEPVSTTELTKSFGWDSLDSFMQHDVQEFNRVLQDNLERSMRDTKVENALTNLFVGKMKSYIACVNVNFESARSEDYWDIQLNVKGMKNLEDSFRSYIQVETLEGDNCYFADTYGFQEAKKGVIFESFPPILHLQLKRFEYDFERDMMIKINDRYEFPLEFDAKAFLSPEADQSQNCEYVLYGVLVHSGDLHNGHYYALLKTEKDGPWYKYDDTRVTRATLREVLEENYGGDYIMHPPFRSPVKLKRFMSAYMLLYLRKDKLDELMNPVSADEIPEHLKEALNPSIQLAELRRKERLESHLYTKVQLITPEFYSEHHEFDIADFGNAYKEETIPQFRIKKEAKFSEFIPIVAEKLGYPQECMRFWYVVKRHNCTVRVESPVNELNSTMEEVKNVWNSQGEILRLYLEITPENELSSSLTHQNTGEWNAFIFVKYFDRKSQEISGCGTLHVNKSDEIRSICPLLCERANLPKNTPLNIYEEIKPGMVDFLRLEKTFTQSELSTGDIICFEPCRPSALEDDIVNSGFDSALKLYDFLSNKVLVLFRPRFIDQDSIIEFEMLLDRRIKYDDLCIELGQKLGIGADHIRLTTCNPLTYSAGMVVPNDSNITLYEILYSSEEEMPSNVIFYETMDVSLSDLDRKRLVRLRWLVDGLANIELVEAYINKSGDINDLFGAVCERFPDSDLRKKKVRVYEVFESRYHRDLSLRTLIRTINPAATLVGEVVPLDQLQLYPEEKIVQVHHFHKDIARIHGIPFSFVIKPQEKFIDTKLRLAARTQYPESIFSVIKFCVVDFDNNRVVYLNDEDITYDVVEKLNGTLALDRAKKDSKKPNILDRAIQMKN
Protein: Major DNA-binding protein (Q4JQU6)
Organism: Varicella-zoster virus (strain Oka vaccine) (HHV-3) (Human herpesvirus 3)
Function: Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands. Additionally, reorganizes the host cell nucleus, leading to the formation of prereplicative sites and replication compartments. This process is driven by the protein which can form double-helical filaments in the absence of DNA.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04007}. Note=In the absence of DNA replication, found in the nuclear framework-associated structures (prereplicative sites). As viral DNA replication proceeds, it migrates to globular intranuclear structures (replication compartments). {ECO:0000255|HAMAP-Rule:MF_04007}.
Interaction partners:
Sequence:
MENTQKTVTVPTGPLGYVYACRVEDLDLEEISFLAARSTDSDLALLPLMRNLTVEKTFTSSLAVVSGARTTGLAGAGITLKLTTSHFYPSVFVFHGGKHVLPSSAAPNLTRACNAARERFGFSRCQGPPVDGAVETTGAEICTRLGLEPENTILYLVVTALFKEAVFMCNVFLHYGGLDIVHINHGDVIRIPLFPVQLFMPDVNRLVPDPFNTHHRSIGEGFVYPTPFYNTGLCHLIHDCVIAPMAVALRVRNVTAVARGAAHLAFDENHEGAVLPPDITYTYFQSSSSGTTTARGARRNDVNSTSKPSPSGGFERRLASIMAADTALHAEVIFNTGIYEETPTDIKEWPMFIGMEGTLPRLNALGSYTARVAGVIGAMVFSPNSALYLTEVEDSGMTEAKDGGPGPSFNRFYQFAGPHLAANPQTDRDGHVLSSQSTGSSNTEFSVDYLALICGFGAPLLARLLFYLERCDAGAFTGGHGDALKYVTGTFDSEIPCSLCEKHTRPVCAHTTVHRLRQRMPRFGQATRQPIGVFGTMNSQYSDCDPLGNYAPYLILRKPGDQTEAAKATMQDTYRATLERLFIDLEQERLLDRGAPCSSEGLSSVIVDHPTFRRILDTLRARIEQTTTQFMKVLVETRDYKIREGLSEATHSMALTFDPYSGAFCPITNFLVKRTHLAVVQDLALSQCHCVFYGQQVEGRNFRNQFQPVLRRRFVDLFNGGFISTRSITVTLSEGPVSAPNPTLGQDAPAGRTFDGDLARVSVEVIRDIRVKNRVVFSGNCTNLSEAARARLVGLASAYQRQEKRVDMLHGALGFLLKQFHGLLFPRGMPPNSKSPNPQWFWTLLQRNQMPADKLTHEEITTIAAVKRFTEEYAALNFINLPPTCIGELAQFYMANLILKYCDHSQYLINTLTSIITGARRPRDPSSVLHWIRKDVTSAADIETQAKALLEKTENLPELWTTAFTSTHLVRAAMNQRPMVVLGISISKYHGAAGNNRVFQAGNWSGLNGGKNVCPLFTFDRTRRFIITCPRGGFICPVTGPSSGNRETTLSDQVRGIIVSGGAMVQLAIYATVVRAVGARAQHMAFDDWLSLTDDEFLARDLEELHDQIIQTLETPWTVEGALEAVKILDEKTTAGDGETPTNLAFNFDSCEPSHDTTSNVLNISGSTVPGLKRPPEDDELFDLSGIPIKHGNITMEMI
Protein: X-box-binding protein 1 (F6YIV7)
Organism: Ciona intestinalis (Transparent sea squirt) (Ascidia intestinalis)
Interaction partners:
Sequence:
MLVSQFREANYESFQSGGRRVSGQRSPPKMSVSSYSTSSSPSSASPSVDIGQAFNMENCDNIMLNIEDGNSFSGFESLQNNLDSVEVQSPPPLAQDGAFNGIDHTTNCVVKNSQPVFNQYSMIDPVGGYDHASYSSGSPVSSNEVDFSRNSSTDVFVNDKPSTSAQQQSTTPRKSFEHVTDKELRKKLKNRESAQAARDRKKAKMLSLERQISELLERNRIVETENQELRSRIQRMESESLWRMGKQEAVPEASPSYSGSIAYHRMHDQSVYPTHCEYNGYPQHTPQPCLPQHHASTASTEKHSLPSYSAYTEDGSSNTDYTQPSYVQNLWRNDSVVPSNNQVYSNGPFTSQQISKNEIMEDAILG
Protein: Uncharacterized protein (Q582V9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MKEVKGENEFLSCNVELSEGVEDIADALKLWEDQLYAVEPLLAISLKLQHLQDTTRGIVASLATSKKKLLQSTRCHKYKRQYLLKMEDTPKKETALSDFSSPDPIDEYVRLHKCKRARDVNVNVNANANTDAGDVSLSVTAEEHQTCVEALLRWVDESMPSVAEPHLTASRKKLVALLTKGESHGKAKPTKETLSNADAFCSKHWAYYAEQLHAAHNDEYAALRRVCATDIGERIRSQMKWEQSQSNSVHVVTPAASAGGLQRSFTQLLGAKDALADCQKAVTVLLSLLGGALDEYDEQTHNVIKREEAFWNNVRIAECESEALRSLSLRVKKHC
Protein: Endophilin-A1 (EEN-B1) (Endophilin-1) (SH3 domain protein 2A) (SH3 domain-containing GRB2-like protein 2) (Q99962)
Organism: Homo sapiens (Human)
Function: Implicated in synaptic vesicle endocytosis. May recruit other proteins to membranes with high curvature. Required for BDNF-dependent dendrite outgrowth. Cooperates with SH3GL2 to mediate BDNF-NTRK2 early endocytic trafficking and signaling from early endosomes.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:O35179}. Membrane {ECO:0000250|UniProtKB:O35179}; Peripheral membrane protein {ECO:0000250|UniProtKB:O35179}. Early endosome {ECO:0000250|UniProtKB:Q62420}. Presynapse {ECO:0000250|UniProtKB:O35179}.
Interaction partners:
- Synaptojanin-1
- Synaptojanin-2
- Dynamin-2
- Epidermal growth factor receptor
- E3 ubiquitin-protein ligase parkin
- Dynamin-1
- E3 ubiquitin-protein ligase CBL
- SH3 domain-containing kinase-binding protein 1
- Endophilin-A2
- Endophilin-A3
Sequence:
MSVAGLKKQFHKATQKVSEKVGGAEGTKLDDDFKEMERKVDVTSRAVMEIMTKTIEYLQPNPASRAKLSMINTMSKIRGQEKGPGYPQAEALLAEAMLKFGRELGDDCNFGPALGEVGEAMRELSEVKDSLDIEVKQNFIDPLQNLHDKDLREIQHHLKKLEGRRLDFDYKKKRQGKIPDEELRQALEKFDESKEIAESSMFNLLEMDIEQVSQLSALVQAQLEYHKQAVQILQQVTVRLEERIRQASSQPRREYQPKPRMSLEFPTGDSTQPNGGLSHTGTPKPSGVQMDQPCCRALYDFEPENEGELGFKEGDIITLTNQIDENWYEGMLHGHSGFFPINYVEILVALPH
Protein: Early meiotic induction protein 1 (Q04406)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in sporulation. Required for the full activation of the early meiotic inducer IME1.
Interaction partners:
Sequence:
MIITIKFESKEKLVSMKQYITVVGVSVNQEGTFSWRPGTFYMKIHEESAAGPFAKGAEISDLSNSSAIGCGISINQEGGDGSIRVKESSLRKKQERMSTKYPTTMSCREAFDQLTSCYSIGGQFRSYYRYGDFTSCDKQVSKFKFCIIHGNDPVKVQEWYKDQVSNNKALENTSGVIWQERETTANK
Protein: Homeobox protein OTX1 A (Orthodenticle homolog 1-like) (zOtx3) (Q90267)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in very early embryogenesis, gastrulation, and the development and subdivision of the diencephalon and the midbrain. Establishes and positions the zona limitans intrathalamica (ZLI) in the diencephalon. May play a role in the organizer function. Probably acts redundantly with otx2 in early brain development.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MMSYLKQAPYAMNGLGLGGATMDLLHPSVGYPTNPRKQRRERTTFTRTQLDILESLFAKTRYPDIFMREEVALKINLPESRVQVWFKNRRAKCRQQQQQSSTNSKIRPAKKKPSPSRESPGSESSGHFTPPAVSSSSSSSSSSSGSNPSALSGVGLISSSSSGTPVPSIWSPAPVSPVPAPPSLPDISPPASASCMQRAMSSGGGTTGVPSYPMPYNQAPSYAQGYPTSNAASYFGGMDCGSYLAPMTGHAHHHPHAHHSQLSTAAAVSGHHHPHHIGQSSGHHPHHQGYGGTALPFSSSDCLDYKEQVASSWKLNFSSAAADCLDYKDQAAWRFQVL
Protein: GDP-mannose-dependent alpha-mannosyltransferase (EC 2.4.1.-) (Guanosine diphosphomannose-dependent alpha-mannosyltransferase) (Q8NT41)
Organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)
Function: Catalyzes the addition of a mannose residue from GDP-D-mannose to GlcAGroAc2 to generate 1,2-di-O-C16/C18:1-(alpha-D-mannopyranosyl)-(1-4)-(alpha-D-glucopyranosyluronic acid)-(1-3)-glycerol(ManGlcAGroAc2).
Interaction partners:
- 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase
- Demethylmenaquinone methyltransferase
- UDP-glucose 6-dehydrogenase
- Glycosidases
Sequence:
MEIIRPMRVAIVAESFLPNVNGVTNSVLRVLEHLKANGHDALVIAPGARDFEEEIGHYLGFEIVRVPTVRVPLIDSLPIGVPLPSVTSVLREYNPDIIHLASPFVLGGAAAFAARQLRIPAIAIYQTDVAGFSQRYHLAPLATASWEWIKTVHNMCQRTLAPSSMSIDELRDHGINDIFHWARGVDSKRFHPGKRSVALRKSWDPSGAKKIVGFVGRLASEKGVECLAGLSGRSDIQLVIVGDGPEAKYLQEMMPDAIFTGALGGEELATTYASLDLFVHPGEFETFCQAIQEAQASGVPTIGPRAGGPIDLINEGVNGLLLDVVDFKETLPAAAEWILDDSRHSEMCAAAWEGVKDKTWEALCTQLLQHYADVIALSQRIPLTFFGPSAEVAKLPLWVARALGVRTRISIEA
Protein: Berberine bridge enzyme-like B (NtBBLb) (EC 1.1.1.-) (A7WPL6)
Organism: Nicotiana tabacum (Common tobacco)
Function: Involved in the biosynthesis of pyridine alkaloid natural products, leading mainly to the production of anabasine, anatabine, nicotine and nornicotine, effective deterrents against herbivores with antiparasitic and pesticide properties (neurotoxins); nornicotine serves as the precursor in the synthesis of the carcinogen compound N'-nitrosonornicotine (NNN). Catalyzes a late oxidation step subsequent to the pyridine ring condensation reaction in the biosynthesis of alkaloids.
Subcellular location: Vacuole {ECO:0000269|PubMed:21343426}.
Interaction partners:
- L-aspartate oxidase
- L-aspartate oxidase 2-a, chloroplastic
- L-aspartate oxidase 2-b, chloroplastic
- L-aspartate oxidase
- Quinolinate synthase, chloroplastic
- Quinolinate synthase, chloroplastic
Sequence:
MFPLIILISFSLTSLSATATSGAGGGVANLYTCLIDHNVHNFSIYPTKNDQSSSNYFNLLDFSLQNLRFAASYMPKPTVIILPNSKEELVSTILCCRQASYEIRVRCGGHSYEGTSYVSFDGSPFVIVDLMKLDEVSVDLDSETAWAQGGATIGQIYYAIAKVSDVHAFSAGSGPTVGSGGHISGGGFGLLSRKFGLAADNVVDALLIDADGRLLDRKAMGEDVFWAIRGGGGGNWGIIYAWKIRLLKVPKIVTTCMIYRPGSKQYVAQLLQKWQIVTPNLVDDFTLGVLLRPADLPADMKYGNSTPIEIFPQFNALYLGPKTEVLSISNEEFPELGVKNDECKEMTWIESALFFSELADINGNSSNDISRLKERYMDGKGFFKGKTDYVKKPVSMDGMLTFLVELEKNPKGYLVFDPYGGAMDKIDDQAIAFPHRKGNLFAIQYLAQWNEEDDYKSDVYMEWIRGFYNTMTPFVSSSPRGAYINYLDMDLGVNMDDDYLLRNASSRNSSSSVDAVERARAWGEMYFLHNYDRLVKAKTQIDPLNVFRHEQSIPPMLGSTQEHKYSSE