wanglab/gogpt-training-data huggingface dataset:
Protein: Peptidyl-prolyl cis-trans isomerase (PPIase) (EC 5.2.1.8) (Q581X3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- U5 small nuclear ribonucleoprotein component, putative
- Cell division control protein, putative
- PRP8 protein homologue
- Pre-mRNA-processing factor 19
- G10 protein
- Peptidyl-prolyl cis-trans isomerase
- peptidylprolyl isomerase
- Pre-mRNA-splicing factor Syf1-like N-terminal HAT-repeats domain-containing protein
- Pre-mRNA-splicing factor SYF1
- MI domain-containing protein
Sequence:
MKVVVNEMSQVVEIITNEGVISVELYDTFAPRAAESFRRFAESGQLDGAVFDRMVPTFLLECRLSEFSVYGELVGREENNHLHHTGAGILTCFGTVLESGAFFITLGPQPELDNVCTIFGRVRSGMRVVEKISRSRVAEKTFRLYTPVVVERCLTRVLPKERRPECVGGEQLDVLPQSVSRHCGTQSSILNDLE
Protein: Ankyrin repeat domain-containing protein 42 (Q3V096)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MPGVANPGPSKSRRETADSSSRKKVHFSSIHDAVRAGDVKQLSDIVERGANLNEVDALHQFTPLHWAAHSGSLECLHWLLWSGADATQTTTRGWTAAHIAAIRGQDACLQALIINGANLATQDDRGCTPLHLAATHGHSFSLQIMLRSGVDPSVTDKREWKPVHYASFHGRLGCLQLLVKWGCGIEDVDYNGNLPVHLAAMEGHLHCLKFLLSRMNSATQALKAFNDNGENVLDLAQRFLKQNVVEFIQGAQYEGSHPDDHDDLAFPGHVAAFKGDLEVLKKLIGDGVINLNERDDNGSTPMHKAAGQGHIDCLQWLIEMGAESNITNKAGETPSDVAKRFAHLAAVKLLEGLQKYEIDDIESDKDHINFFTRHGVEGSTDAKDDLCLSESDKANARMRAHKKIVELRQLLEIAESNFKHLGGITEEDLKQKKEQLESKKTINELQGQLAYERLRREKLECQLDEYRVEVDQLKETLQKIQVTSVAAMEDDSCESSKEKRRVKKKVSPGGVFVRSYQRIRTSISSQV
Protein: Fibroblast growth factor (FGF) (P91672)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MRRNLRLDWRALALLGALLSFIIAWRGLVSAMPLMAMDNNLTDSSGSTNTSTSSTSKYNSTNNSNLFSNSYLQSDHSRSSLVPSAVSERSVNQPTNQSINAEFNQSLSTHPTAITSTPQTQTQTQIQSQYPSQAEDSDQLEEPLGFVISAMPNEHLAVLSRTERSIRHQNQQQQKKHHHHHQQQQQQQHQQQQPMSPADNNFIGSKSKRLSNPRSSLNINSSSSNTPISNLDRNERSTVPQSHLAWTSRKIQLYIKNRILQILRDGVVNGTQDENSEFTILQRSTVDVGRIKLQSVATCLYLCMDACGVPYGSKDFTDDCVFNENMGLQNYNTYSSTYHSQARRVFYLALNGSGQPRRTQIPASRSLGKLSTYTNAITETVPQERVEQLIAKNFGANRVKHGVRQLCDTGKPLIELIDVARFKAPPHCSSNTSGSSSSISSSSSSSSKSSSNSSSSYVPVSAISSLSSISNSSQSESGHISSSLSGTSNSNSSSNSSSSNSSSNSSRPSGSKANKKKKPKCKPHEQEDTHNCQKRGGAGAGALRKLGPKAKRCKELREKAAAEKRAPPNCGKKNGARKNPTEAAKAVQQRPKGNIQHGGKKKPNKAGKQRQNGGKKQQQQQQHQLQQQPLQHQAKSISGGKRKHRKLDASTTTTMATSLGTPPSSHWESSSPLPAFSLSETSDRVERNVRMSSGEEQDQDNDQDQEQSDPGEQGEEETEGDGGSLEDASYEDSSSEAQGRSGAGGDDSLYYDFLCLQLIAMVLLRKRAIL
Protein: Transcriptional repressor TUP1 (P0CY34)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Represses transcription by RNA polymerase II. Represses genes responsible for initiating filamentous growth such as HWP1, RBT1, RBT2, RBT4, RBT5, RBT7 and WAP1; and this repression is lifted under inducing environmental conditions. Represses also genes which participate in pathogenesis. Crucial component of the response to farnesol. Plays an important role in the regulation of white-opaque switching.
Interaction partners:
- Transcription regulator
- Transcriptional regulator NRG1
- Transcriptional regulator SKO1
- COMPASS subunit protein
- Ash2p
- Histone-lysine N-methyltransferase, H3 lysine-4 specific
- Enhanced filamentous growth protein 1
- Repressor of filamentous growth 1
- Serine/threonine protein kinase
- Transcription factor CPH1
Sequence:
MYPQRTQHQQRLTELLDAIKTEFDYASNEASSFKKVQEDYDSKYQQQAAEMQQIRQTVYDLELAHRKIKEAYEEEILRLKNELDTRDRQMKNGFQQQQQQQQQQQQQQQQQQQQIVAPPAAPPAPPTPVTSLSVIDKSQYIVNPTQRANHVKEIPPFLQDLDIAKANPEFKKQHLEYYVLYNPAFSKDLDIDMVHSLDHSSVVCCVRFSRDGKFIATGCNKTTQVFNVTTGELVAKLIDESSNENKDDNTTASGDLYIRSVCFSPDGKLLATGAEDKLIRIWDLSTKRIIKILRGHEQDIYSLDFFPDGDRLVSGSGDRSVRIWDLRTSQCSLTLSIEDGVTTVAVSPDGKLIAAGSLDRTVRVWDSTTGFLVERLDSGNENGNGHEDSVYSVAFSNNGEQIASGSLDRTVKLWHLEGKSDKKSTCEVTYIGHKDFVLSVCCTPDNEYILSGSKDRGVIFWDQASGNPLLMLQGHRNSVISVAVSLNSKGTEGIFATGSGDCKARIWKWTKK
Protein: Ezrin (Cytovillin) (Villin-2) (p81) (P15311)
Organism: Homo sapiens (Human)
Function: Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:18046454}; Peripheral membrane protein {ECO:0000269|PubMed:18046454}; Cytoplasmic side {ECO:0000269|PubMed:18046454}. Cell projection {ECO:0000269|PubMed:18046454}. Cell projection, microvillus membrane {ECO:0000269|PubMed:18046454}; Peripheral membrane protein {ECO:0000269|PubMed:18046454}; Cytoplasmic side {ECO:0000269|PubMed:18046454}. Cell projection, ruffle membrane {ECO:0000269|PubMed:18046454}; Peripheral membrane protein {ECO:0000269|PubMed:18046454}; Cytoplasmic side {ECO:0000269|PubMed:18046454}. Cytoplasm, cell cortex {ECO:0000269|PubMed:18046454}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18046454}. Cell projection, microvillus {ECO:0000250|UniProtKB:P26040}. Note=Localization to the apical membrane of parietal cells depends on the interaction with PALS1. Localizes to cell extensions and peripheral processes of astrocytes (By similarity). Microvillar peripheral membrane protein (cytoplasmic side). {ECO:0000250|UniProtKB:P31977}.
Interaction partners:
- Na
- Moesin
- Radixin
- cAMP-dependent protein kinase catalytic subunit beta
- Intercellular adhesion molecule 1
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit gamma
- Na
- Sodium/hydrogen exchanger 1
- CD44 antigen
Sequence:
MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLERQQLETEKKRRETVEREKEQMMREKEELMLRLQDYEEKTKKAERELSEQIQRALQLEEERKRAQEEAERLEADRMAALRAKEELERQAVDQIKSQEQLAAELAEYTAKIALLEEARRRKEDEVEEWQHRAKEAQDDLVKTKEELHLVMTAPPPPPPPVYEPVSYHVQESLQDEGAEPTGYSAELSSEGIRDDRNEEKRITEAEKNERVQRQLLTLSSELSQARDENKRTHNDIIHNENMRQGRDKYKTLRQIRQGNTKQRIDEFEAL
Protein: R-spondin-1 (Roof plate-specific spondin-1) (hRspo1) (Q2MKA7)
Organism: Homo sapiens (Human)
Function: Activator of the canonical Wnt signaling pathway by acting as a ligand for LGR4-6 receptors. Upon binding to LGR4-6 (LGR4, LGR5 or LGR6), LGR4-6 associate with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering the canonical Wnt signaling pathway to increase expression of target genes. Also regulates the canonical Wnt/beta-catenin-dependent pathway and non-canonical Wnt signaling by acting as an inhibitor of ZNRF3, an important regulator of the Wnt signaling pathway. Acts as a ligand for frizzled FZD8 and LRP6. May negatively regulate the TGF-beta pathway. Has a essential roles in ovary determination. Regulates Wnt signaling by antagonizing DKK1/KREM1-mediated internalization of LRP6 through an interaction with KREM1.
Subcellular location: Secreted {ECO:0000269|PubMed:26764097, ECO:0000269|PubMed:27123103}. Nucleus {ECO:0000250|UniProtKB:Q9Z132}. Note=Seems to mainly localize to nucleoli. {ECO:0000250|UniProtKB:Q9Z132}.
Interaction partners:
- Leucine-rich repeat-containing G-protein coupled receptor 4
- Leucine-rich repeat-containing G-protein coupled receptor 5
- E3 ubiquitin-protein ligase RNF43
- E3 ubiquitin-protein ligase ZNRF3
- Leucine-rich repeat-containing G-protein coupled receptor 6
- Low-density lipoprotein receptor-related protein 5
- Low-density lipoprotein receptor-related protein 6
- Noggin
- Protein Wnt-4
- Protein Wnt-3a
Sequence:
MRLGLCVVALVLSWTHLTISSRGIKGKRQRRISAEGSQACAKGCELCSEVNGCLKCSPKLFILLERNDIRQVGVCLPSCPPGYFDARNPDMNKCIKCKIEHCEACFSHNFCTKCKEGLYLHKGRCYPACPEGSSAANGTMECSSPAQCEMSEWSPWGPCSKKQQLCGFRRGSEERTRRVLHAPVGDHAACSDTKETRRCTVRRVPCPEGQKRRKGGQGRRENANRNLARKESKEAGAGSRRRKGQQQQQQQGTVGPLTSAGPA
Protein: Hydroxyphenylpyruvate reductase (HPPR) (EC 1.1.1.237) (Q65CJ7)
Organism: Plectranthus scutellarioides (Coleus) (Solenostemon scutellarioides)
Function: Catalyzes the NAD(P)H-dependent reduction of 4-hydroxyphenylpyruvate to 4-hydroxyphenyllactate and 3,4-dihydroxyphenylpyruvate to 3,4-dihydroxyphenyllactate in the biosynthesis of rosmarinic acid. Rosmarinic acid is an ester of caffeic acid and 3,4-dihydroxyphenyllactic acid. NADP is the preferred substrate.
Interaction partners:
Sequence:
MEAIGVLMMCPMSTYLEQELDKRFKLFRYWTQPAQRDFLALQAESIRAVVGNSNAGADAELIDALPKLEIVSSFSVGLDKVDLIKCEEKGVRVTNTPDVLTDDVADLAIGLILAVLRRICECDKYVRRGAWKFGDFKLTTKFSGKRVGIIGLGRIGLAVAERAEAFDCPISYFSRSKKPNTNYTYYGSVVELASNSDILVVACPLTPETTHIINREVIDALGPKGVLINIGRGPHVDEPELVSALVEGRLGGAGLDVFEREPEVPEKLFGLENVVLLPHVGSGTVETRKVMADLVVGNLEAHFSGKPLLTPVV
Protein: Carbohydrate-binding domain-containing protein (Q54BC0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MKNINILIFIFIYLIGFVLSDDDELKIIRVERIDEIEYGSIDCSIRFNVLIDYPRPLVFVSGIGGVVNGDAKVKNGTLTIYQIRHTVLVGNNSVSFQAHDYTNYQYPYPVYINKTDYAIAQCDQLPSNVKFVSKQNRWNSISGFGTPFNWFKLLNPINLDIGKGFSNYEFVCQVPQPYGCYFYPAQNGGYQKRNYWLIVFIQATNTYIPFNPTTNVLIKSKQGTIAFNSTFDGLKDPTNPPMQLLNFESFPPINSVLSFGEMTNHATFQTQIINNKNTLTSISKEDDEMIQSQLIPLLGSTSNATFIGISEFSTATQNNKMHLQIVDNQGAKRIGGDISISTKLKDSSASFDSDIKTSIINETNFGSRYIYHTNVKFDTSYDPTMTVSFDDQFSYEVIPPSFPYGISNGTLRNHSISISSATGSFYSGNLNCYRNGDHSKSEKIANIISSNTDLNPAVISEVELFNLSFDKVLIRIKANDDISGIKYLDVFRFKIQSSDLVWGNPMNGVYEAIASVIEYSTMKTIPVISFDYKGNNQGIDQDNPIIDTNFNKVPNFPTLNYIKDKKLDPFNFTSFSFKYNDIDVSNQAFNNTLCFGLSGADKGMVPQFFLLYSPTNMKAYETDKPFIGAWDPLKNQFCIDFIIPARIFSGEINYIIFFSPFIYDRGYIINSVGSTAQLRVLSNYADQLPPIITEFNAYPSTNVNVNSEKIIGWDLRIEDLTNGLLSAEFNITSEYDLNPITIKLTPNNAVSGNDKSGVYQLRFPVSPNCRSQSYRISSAKLTDAQGHFGVTPSTYNFNPFIKFLSSNQLRINTTCPIGNNDNESPILNSFKSSLVSIDVGGFKENRTVVFEFTTSDSGSGISTRHNPLVYLSKPTSSKISCQSKLLSYTNGQANYSCSIELPYGFGAHDALLISIYGIVDNQSNMNGYSSFDLKSLGFQYSLLSQFSDIPVLESTSSITNQASTLTIYGHKFGIDSSKVTLQVNYNNGQGWKNTSVSFYAGIVLITDSITPTSTPFYVRVIVNNIISNQIIVTPTLIPTQCNYQVDQTIISKWINSEVYHYLQASITIKNNGIKPIKAFSFMMSNIDQIWGVTISSGPTYSLPSWNPTINPGNEYTFGYILKGTDVGQLVNVMVDCS
Protein: Putative cell agglutination protein pfl3 (Adhesin pfl3) (Pombe flocculin 3) (Q874R4)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: May be involved in agglutination during conjugation or other aspects of colony formation (By similarity). Induces flocculation when overexpressed.
Subcellular location: Cell surface {ECO:0000305}.
Interaction partners:
- Galactose-specific cell agglutination protein gsf2
- Putative cell agglutination protein pfl8
- Uncharacterized protein C19C7.05
- Transcription factor cbf12
- Putative GPI-anchored protein pfl2
- MADS-box transcription factor pvg4
Sequence:
MSLFPQILLRLLFLAFTLKSTSNAEKHDKVDYKDFVRRDDGDTCLRYTTIYSQGEYETTITIPPNSYSNGVSLSNGTLLSTSSPLISTSGQFTSNNVSTTSSQRHNTKTITFFSGTSDYTSVYYDTTGTDDVVYEYHPSSERHKSTNDTWSTNLPTNPTTTAIYSTSGSSNITTPYSNRITNSNTSVNDITSKYLSVGTITLTTISGSDLYTSTFPANGTTSGTVEVVIPTAGTVTETAVSGSELYTSTFPANGTTSGTVEVVIPTAGTRTVTKISGSKFFTTTTDASGTVSGTVEVVLPTAGTNTMTVVSGSRFFTSVVSASGTVSGEQVIVYPTAGMVTETIVSGSEIFNTTYPASGTRTGTVEVVIPTAGTVTETEISGSELYTSTFPANGTTSGTVEVVIPTAGTRTVTKISGSKFFTTTTDASGTVSGTVEVVLPTAGTNTMTVVSGSRFFTSVVSASGTVSGEHIIVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTAYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPAHDTVSGTVEVVEPTAGVVTETVVSGSVGYTTTYPVQGTVSGTVMIVEPTAGYVTVTTSLGSSSYATTVATASGTSTGTVLQVVPSLFPGCNSKCTSSNAFRILVENDSISPSYLTYRESDGFGIASSNPSPAGSEGIFYYDSTLKRVVTCCDERPYYRTMEGDLAKTYFFIEDEGDGTYKFKLTYGAFSEYLDVKILADSTFFFKAMDSSSSTILNQKVRASNVYFKAVPL
Protein: Phosphatidyl-N-methylethanolamine N-methyltransferase (EC 2.1.1.71) (Phospholipid methyltransferase) (PLMT) (Q9SAH5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03216}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}.
Interaction partners:
- Lysophospholipid acyltransferase 2
- Lysophospholipid acyltransferase LPEAT2
- Phospholipase D zeta 1
- Lecithin-cholesterol acyltransferase-like 4
- Triacylglycerol lipase SDP1L
- Phospholipase D gamma 3
- Non-specific phospholipase C4
- Phospholipase D delta
- Phospholipase D gamma 2
- Phospholipase D alpha 3
Sequence:
MGLLAAIGVLLPFPFYWWLWTNAQSWVNLCGRERDPSTVMARVSHVLKAAQLLSLFSVASLSWPPPLYFWPLMAFGQFLNFRVYQLLGEAGTYYGVRFGKNIPWVTEFPFGVIRDPQYVGSIMSLLACLSWVPFQYILLWSLGYVFMMFLESKEDPNARAKSIS
Protein: WW domain binding protein 2 (K7EIK1)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XGWEGSASYKLTFTAGGAIEFGQRMLQVASQASRGEVPSGAYGYSYMPSGAYVYPPPVANGMYPCPPGYPYPPPPPEFYPGPPMMDGAMGYVQPPPPPYPGPMEPPVSGPDVPSTPAAEAKAAEAAASAYYNPGNPHNVYMPTSQPPPPPYYPPEDKKTQRSFLTGTRECMSVHLVAAGWGREQGPLTLCAGRDLPPAPQPASSP
Protein: Formin-E (Diaphanous-related formin dia3) (Q5TJ57)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Formins play an important role in the nucleation of actin and the formation of linear actin filaments.
Interaction partners:
Sequence:
MDNHSSSSNPSSLSSSSSSSSSSSSFLSDHVKKEEQNGLDTIKEEIENKIENEEEEEKIEEKPIEKVEEEKIIVQKEEEEKIEEEPIEKEEEKKVEEEKFEQDNINTTVEAKTLETSTEPIATEVVDEKSITSNNENLEEQQKEDVISIPPPQQEQQEQQEQQEKQKEETKPSIREEVKEKIKGKLSEIKEEIKDIKEEIKHVIREEVTEPIIVVENNNSPPPPPPPPSITVQSSSPVSSQISSPVSSPVSSPKPSVTFNEDGRKRKEGGITASISSEDIMALSSSTSTNNKGIPKENKRTASTILRSKSSPNPGANNPNHNKDGNNSSSSSSSNNNSDNNNNSDNNSNNNNINNNNSSSNNLNYDSSDIDTEAIPKFYHDFKIHRGTSSCVYCGENTRLWSTSYKCFFCGVVCHKKCLDSMNTIPCSSAIHNIKGKNRSQTISGYAPPNSLALQAPPYISVAKPSSITNSSSKSTPSLLSAPPSQSNSNNSSPNISSKSNPNSPITTSATTTTTTATISSLSPTSISSPPIASEQPPSPLLQQQQQQQQQQQQQQQQQQQQQQQQQQISTTQLQDLNNTSEKPDDDMINLMFDTLMVDLDLNLPASKLSTTQKWLLLEQKFKLKKDELLPEYFINALKEQPSKSIFQSLVVILRTNVTKNWMCSFVQLNGVEILFEILSKSKRKDYKDDCLSCIGKVMSNPIGLNSVAQLPMAPKTITKVLRSKQYCIKSKAMAIELLTVMLLDKYVPGGCSLVLKALTKTKEKKRFSFFVRFIKDNESLELKTKALCFINVLIFEMEDMNVRVNIRSEFLRLGLYTYLREIKKTITHEKTLFTQIEIFEEMMNEDTQELDLRLEDLKRQLGIDIDDVDQVFKALKNTTSKSGLNRQLLNILQNLLVIKACDPTDGVKYFILCDTLVKQISLHKGGFEDPSNFDFRGLMVGLESATAEVTLNRKLGELEKQNIDKAMKIQEQDINIKSLLDLLKQLKDGGTAPDASMIKKIEEMIKQMEPPPPPISVKSPDDPNNAAPIVVAPIPPPPPPISGAPPPPPPPPPPMKGGAGPPPPPPPPGKLGAKKPPAGVQCRPPPKVPKPSHPLKAYQWVKLAPVKVNDSLFDKLGPMNDINLPWNQIEEEFAAKVIVREKKAIVKPKGPTQVIDPKLGQNISIFLSQFKGVEPKQLITYIQSMDESKMSRDQVKQISKLLPSREDLAALKEFLQAEDRSKLSIADQYCIDIGAFPFASEKISMFLLKSELKSRLDEVKPQIAAVSVACDEVYKSKKLIRIIEIILVLGNFINYGTPRGDISGYKLDSLIKLSDTKSSDLSSNLINTFVKYCQEKEPNLLTFADELPSLTTARKTIWSGVVADVSSIGRDVHSVKQIVETLQKSNEPFNQSIIDFLATASTEVEKLRKLLESTQENFKKLCKYFAEEEGKSQPEEFFDIFGRFITLFENATTQLQQQKEEQLKEEKRLQQKQQRQERAVRKLTTSNESASASPNHAKSTDDKSDEDDDIVNDLLMAVRDGDAFRQAKGRRRTTHQIATSKMISNNLDPSKILPTSPNKN
Protein: Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 4 (P0C6T2)
Organism: Homo sapiens (Human)
Function: Subunit of the oligosaccharyl transferase (OST) complex that catalyzes the initial transfer of a defined glycan (Glc(3)Man(9)GlcNAc(2) in eukaryotes) from the lipid carrier dolichol-pyrophosphate to an asparagine residue within an Asn-X-Ser/Thr consensus motif in nascent polypeptide chains, the first step in protein N-glycosylation. N-glycosylation occurs cotranslationally and the complex associates with the Sec61 complex at the channel-forming translocon complex that mediates protein translocation across the endoplasmic reticulum (ER). All subunits are required for a maximal enzyme activity. Specifically involved in maintaining stability of STT3A-containing OST complexes.
Subcellular location: Endoplasmic reticulum {ECO:0000305|PubMed:23606741}. Endoplasmic reticulum membrane; Single-pass type III membrane protein {ECO:0000305}. Note=The single transmembrane helix has a kink in the middle of the transmembrane span.
Interaction partners:
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3B
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit STT3A
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit DAD1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase 48 kDa subunit
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TMEM258
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 2
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit 1
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit MAGT1
- Oligosaccharyltransferase complex subunit OSTC
- Dolichyl-diphosphooligosaccharide--protein glycosyltransferase subunit TUSC3
Sequence:
MITDVQLAIFANMLGVSLFLLVVLYHYVAVNNPKKQE
Protein: [histone H3]-trimethyl-L-lysine(9) demethylase (EC 1.14.11.66) (A0A8I5ZWQ3)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGSEDHSAQNPSCKIMTFRPTMDEFRDFNRYVAYIESQGAHRAGLAKIIPPKEWKPRQTYDDIDDVVIPAPIQQVVTGQSGLFTQYNIQKKAMTVGEYRRLANSEKYCTPRHQDFDDLERKYWKNLTFVSPIYGADISGSLYDDDVAQWNIGNLRSILDMVERECGTIIEGVNTPYLYFGMWKTTFAWHTEDMDLYSINYLHFGEPKSWYAIPPEHGKRLERLAIGFFPGSSQGCDAFLRHKMTLISPIILKKYGIPFSRITQEAGEFMITFPYGYHAGFNHGFNCAESTNFATLRWIDYGKVATQCTCRKDMVKISMDVFVRILQPERYEQWKQGRDLTVLDHTRPTALSSPELSSWSASRTSLKAKLLRRQISVKESRPWRKAEEERRPSLERRREPTRRPGPASHRRRSQPKKSKPEDSRSPGEATAGVAGLDEARGCSRRETMPEEEEEEELSPSQGHEAEGVEEDGRGKPRPTKARSKKKTPSLLSPPLLSAPPALFPAEEVLRLPPQPKSPGPAMGPMAAEGGPPPTALNVVPPGVPGEETEVRPRPIIPMLYVLPRANSSDGDREHAAHPQLAPMELGPEEEDQAQAGDSQGTTSFSKLKVEIKKSRRHPLGRPPTRSPLSVVKQEASSDEEAFPFSGEDDGSDPEALRSLLSLQWKSKAASFQAERKLNAAAALSEPYCAVCTLFYPYSQSVQTEREVLATPGDSAVQPPSKSGQRTRPLIPEMCFTSSGENTEPLPANSYVGEDGTSPLISCAHCCLQVHASCYGVRPELAKEGWTCSRCAAHAWTAECCLCNLRGGALQRTTEHRWIHVICAIAVPEVRFLNVIERNPVDVSAIPEQRWKLKCVYCRKRMKRVSGACIQCSYEHCSTSFHVTCAHAAGVLMEPDDWPYVVSITCLKHRASGAGGQLLRTVSLGQIVITKNRNGLYYRCRVIGTTAQTFYEVNFDDGSYSDNLYPESITSRDCLRLGPPPEGELVELRWTDGNLYRARFISMATSLIYQVEFEDGSQLTVKRADIFTLEEELPKRVRSRLVSVLGVSIWGIEDACL
Protein: Potassium channel toxin alpha-KTx 13.2 (OsK-2) (OsK2) (P83244)
Organism: Orthochirus scrobiculosus (Central Asian scorpion)
Function: Potent and selective inhibitor of Kv1.2/KCNA2 potassium channels.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
ACGPGCSGSCRQKGDRIKCINGSCHCYP
Protein: Dynein axonemal intermediate chain 1 (Axonemal dynein intermediate chain 1) (Q5XIL8)
Organism: Rattus norvegicus (Rat)
Function: Part of the dynein complex of respiratory cilia.
Subcellular location: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9UI46}.
Interaction partners:
- Dynein axonemal heavy chain 5
- Thioredoxin domain-containing protein 3
- Dynein, axonemal, heavy chain 9
- Dynein axonemal heavy chain 7
- Dynein, axonemal, heavy chain 11
- Outer dynein arm-docking complex subunit 1
- Dynein axonemal heavy chain 17
- Dynein axonemal heavy chain 1
- Dynein axonemal intermediate chain 2
- Dynein regulatory complex subunit 2
Sequence:
MPSKQIRKQSVILTRGARKREEDSGTDVGEGADDWAQSKAAVRPPDQLELTDAELKEEFTRILTANNPHAPQNIVRYSFKERTYKLIGFVNQMAIHFSQVGNLIPKDSDEGRRQHYRDELVAGSQESVKVVTSDTEILEEEEEPKEGEGEGEGEAEGEAEAGSQTDVPAAAETTEKVIEEELMAPVQPKERKLTNQFNFSERASQTFNNPLRDRECQMEPPPRTNFSATANQWEIYDAYVDELEKLEKTKEKEKTKTPVAKKTEKMAMRKLTSMESQSDDITKVTQAAKIVERMVNQNTYDDVAQDFKYYEDAADEYRDQEGTLLPLWKFQNDKAKRLAVTALCWNPKYKDLFAVGHGSYDFMKQSRGMLLLYSMKNPSFPEYMFSSESGIMCLDMHMDHPYLVVVGYYDGNVAIYNLKKPHSQPCFRSTSKSGKHTDPVWQVKWQKDDMDHNLNFFSVSSDGRIVSWTLVKSELVHIDVIKLKDEGSTTEIPEGLQLHTVGCGTAFDFHKEIDYLFLVGTEEGKIYKCSKSYSSQFLDTYDAHNMAVDAVLWNPYHARVFISCSSDWTVKIWDHAIKTPMFIYDLNAAVGDVAWAPYSSTVFAAVTTDGKAHVFDLAVNKYEAICNQPVVAKKKNKITHVQFNPIHPIIIVGDDRGHITCLKLSPNLRKMPKEKKGQEVQKGPAVEIAKLDKLLNLVREVKTKT
Protein: Protein E6 (Q82005)
Organism: Human papillomavirus 73
Subcellular location: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04006, ECO:0000256|RuleBase:RU363123}.
Interaction partners:
Sequence:
MLFPNSEERPYKLQALCDEVNISIHDINLDCVFCQRGLYRSEVYDFAFSDLCIVYRKDKPYGVCQPCLKFYSKIREYRRYRQSVYGTTLENLTNKQLCNILIRCGKCQKPLCPLEKQKHVDEKKRFHQIAEQWTGRCTRCWRPSATVV
Protein: UPF0547 protein C16orf87 (Q6PH81)
Organism: Homo sapiens (Human)
Interaction partners:
- AT-rich interactive domain-containing protein 5B
- Mesoderm induction early response protein 3
- Mesoderm induction early response protein 1
Sequence:
MSATRAKKVKMATKSCPECDQQVPVACKSCPCGYIFISRKLLNAKHSEKSPPSTENKHEAKRRRTERVRREKINSTVNKDLENRKRSRSNSHSDHIRRGRGRPKSASAKKHEEEREKQEKEIDIYANLSDEKAFVFSVALAEINRKIINQRLIL
Protein: DNA repair and recombination protein RAD54B (EC 3.6.4.-) (RAD54 homolog B) (Q6PFE3)
Organism: Mus musculus (Mouse)
Function: Involved in DNA repair and mitotic recombination. May play an active role in recombination processes in concert with other members of the RAD52 epistasis group.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- DNA repair and recombination protein RAD54-like
- Transcriptional regulator ATRX
- Breast cancer type 1 susceptibility protein homolog
- DNA repair protein RAD51 homolog 1
- DNA repair protein RAD52 homolog
- Bifunctional 3'-5' exonuclease/ATP-dependent helicase WRN
- Protein VAC14 homolog
- DNA repair protein RAD51 homolog 2
- DNA repair protein RAD51 homolog 3
- Fanconi anemia group M protein homolog
Sequence:
MRRSAAPSQVQGKSFKKTRFIPPGRSNADVSKEITKMSPDPKLFQGAEQSQNDPGVCSSNPCPSEGIPREVGDGTRVDPLPPVHSASKEITESKAQEEEASSLLKYFSVVWCKASKKKHKKWEGDAILIVRGRSFTLKDLEGKDIGRGIGYKFKDLENVEEGQTLIIGGKEIEILGTISSDDFNSGKCFQHGSGSPAVPSSQAARKCFSNPFKSVCQSTQAQGKRWNDCRPRHNPCTPNALVMPRPDENHQRMFNRHCSPIVDVVIDPHLVHHLRPHQKDGIIFLYECVMGMRAVGKCGAILADEMGLGKTLQCISLIWTLQCQGPYGGKPVIKKTLIVTPGSLVNNWRKEFQKWLGSERIKIFTVDQDHKVEEFINSTFHSVLIISYEMLLRSLDQIKTIPFGLLICDEGHRLKNSSIKTTTALSSLSCEKTVILTGTPVQNDLQEFFALVDFVNPGILGSLSSYRKIYEEPIIISREPSSSKEERELGERRATELTRLTGRFILRRTQEVINKYLPPKIENVVFCRPGALQIELYRKLLRSQSVRFCLQGLLENSAHLICIGALKKLCNHPCLLFSSVKGKEFSSSCEENEERNLCQGLLSVFPAGYNPLQFSEEESGKLQVLVKLLAVIHELRPTEKVILVSNYRQTLNVLEEVCKRHGYACARLDGQTPVSQRQHIVDSFNSKYSTDFIFLLSSKAGGVGLNLIGGSHLILYDIDWNPATDIQAMSRVWRDGQKHPVHIYRLLTTGTIEEKIYQRQISKQGLSGAVVDLTRSSEHIQFSVEELKNLFTLHESSHCVTHDLLDCECTGEKGHTEDASEGPVASRQCQFGPQKSDALRPLSMSQLKQWKHFSGDHLNLPDPFLERIRENVSFFFQNITNQAPAV
Protein: Protein ADM2 (Intermedin) [Cleaved into: Adrenomedullin-2 (AM2) (Intermedin-long) (IMDL); Intermedin-short (IMDS)] (P61312)
Organism: Rattus norvegicus (Rat)
Function: May play a role as physiological regulators of gastrointestinal, cardiovascular bioactivities mediated by the CALCRL/RAMPs receptor complexes. Activates the cAMP-dependent pathway.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q7Z4H4}.
Interaction partners:
- Calcitonin gene-related peptide type 1 receptor
- Receptor activity-modifying protein 3
- Receptor activity-modifying protein 2
- Pro-adrenomedullin
- Receptor activity-modifying protein 1
- Islet amyloid polypeptide
- Calcitonin receptor
Sequence:
MAQLLMVTVTFGCISLLYLLPGTLSGSLGKGLRPREPPAKIPSSGPQPGHPSLRPVVWKPPHALQPQGRGNPALATVHLPQGGGSRHPGPQRHVGSRRPHAQLLRVGCVLGTCQVQNLSHRLWQLVRPSGRRDSAPVDPSSPHSYG
Protein: Reticulon-like protein (Q7KTP4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363132}.
Interaction partners:
Sequence:
MSAFGETGQNGVCKQRPLICSILDPNAWFKPERLHPQVESLIYWRDVKKSGIVFGAGLITLAAISSFSVISVFAYLSLLTLFGTVAFRIYKSVTQAVQKTNEGHPFKDYLELDLTLSHEKVQNIAGVAVAHINGFISELRRLFLVEDIIDSIKFGVILWVFTYVGAWFNGMTLVILAFVSLFTLPKVYENNKQSIDTHLDLVRSKLTEITDKIRVAIPIGNKKPEAAAESEKDK
Protein: Bursicon (Bursicon subunit alpha) (Single-chain bursicon) (A2VB89)
Organism: Apis mellifera (Honeybee)
Function: Final heterodimeric neurohormone released at the end of the molting cycle, involved in the sclerotization (tanning) of the insect cuticle, melanization and wing spreading.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9VD83}.
Interaction partners:
- Partner of bursicon
- G_PROTEIN_RECEP_F1_2 domain-containing protein.
- Uncharacterized protein.
Sequence:
MLLYHIVGASVLICLLNETAKAIIGVDECQATPVIHFLQYPGCVPKPIPSYACRGRCSSYLQVSGSKIWQMERSCMCCQESGEREASVSLFCPRAKPGEKKFRKVITKAPLECMCRPCTSVEEYAIIPQEIAGFADEGPFTTSAHFRRSSDLQ