wanglab/gogpt-training-data huggingface dataset:
Protein: Scarecrow-like protein 28 (AtSCL28) (GRAS family protein 8) (AtGRAS-8) (Q9CAN3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable transcription factor involved in plant development.
Subcellular location: Nucleus {ECO:0000269|PubMed:18500650}.
Interaction partners:
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- non-specific serine/threonine protein kinase
- Bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumin superfamily protein
- AT-hook motif nuclear-localized protein 11
- At3g10000
- NAC
Sequence:
MLAGCSSSSLLSPTRRLRSEAVAATSATVSAHFPMNTQRLDLPCSSSFSRKETPSSRPLGRSISLDNSNNNNNKPIERKTKTSGCSLKQNIKLPPLATTRGNGEGFSWNNDNNNRGKSLKRLAEEDESCLSRAKRTKCENEGGFWFEHFTGQDSSSPALPFSLTCSGDDEEKVCFVPSEVISQPLPNWVDSVITELAGIGDKDVESSLPAAVKEASGGSSTSASSESRSLSHRVPEPTNGSRNPYSHRGATEERTTGNINNNNNRNDLQRDFELVNLLTGCLDAIRSRNIAAINHFIARTGDLASPRGRTPMTRLIAYYIEALALRVARMWPHIFHIAPPREFDRTVEDESGNALRFLNQVTPIPKFIHFTANEMLLRAFEGKERVHIIDFDIKQGLQWPSFFQSLASRINPPHHVRITGIGESKLELNETGDRLHGFAEAMNLQFEFHPVVDRLEDVRLWMLHVKEGESVAVNCVMQMHKTLYDGTGAAIRDFLGLIRSTNPIALVLAEQEAEHNSEQLETRVCNSLKYYSAMFDAIHTNLATDSLMRVKVEEMLFGREIRNIVACEGSHRQERHVGFRHWRRMLEQLGFRSLGVSEREVLQSKMLLRMYGSDNEGFFNVERSDEDNGGEGGRGGGVTLRWSEQPLYTISAWTTGGN
Protein: SS18-like protein 2 (SYT homolog 2) (Q9UHA2)
Organism: Homo sapiens (Human)
Interaction partners:
- Protein SSX4
- Protein cramped-like
Sequence:
MSVAFVPDWLRGKAEVNQETIQRLLEENDQLIRCIVEYQNKGRGNECVQYQHVLHRNLIYLATIADASPTSTSKAME
Protein: Serine/threonine-protein kinase PLK4 (EC 2.7.11.21) (Polo-like kinase 4) (PLK-4) (Serine/threonine-protein kinase SAK) (O97143)
Organism: Drosophila melanogaster (Fruit fly)
Function: Serine/threonine-protein kinase that plays a central role in centriole duplication. Able to trigger procentriole formation on the surface of the mother centriole cylinder, using mother centriole as a platform, leading to the recruitment of centriole biogenesis proteins such as Sas-6. When overexpressed, it is able to induce centrosome amplification through the simultaneous generation of multiple procentrioles adjoining each parental centriole during S phase. Centrosome amplification following overexpression can initiate tumorigenesis, highlighting the importance of centrosome regulation in cancers.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:16326102, ECO:0000269|PubMed:19171756, ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:32965218}. Note=Colocalizes with Sas-4 and Patronin at the microtubule organizing center (PubMed:20946984). Colocalizes with Alms1a at the mother centrosome in male germ stem cells (PubMed:32965218). {ECO:0000269|PubMed:20946984, ECO:0000269|PubMed:32965218}.
Interaction partners:
- Asterless
- Spindle assembly abnormal 4
- Spindle assembly abnormal protein 6 homolog
- Centrosomal protein 135kDa, isoform B
- BcDNA.LD24702
- Anastral spindle 2, isoform A
- separase
- Supernumerary limbs, isoform B
- Serine/threonine-protein kinase polo
- Centriolar coiled coil protein 110kDa, isoform B
Sequence:
MLSNRAFGETIEDYEVQHLLGKGGFATVYKARCLHTHQDVAIKMIDKKLIQGTGLTNRVRQEVEIHSRLKHPSVLQLYTFFQDANYVYLVLELAHNGELHRYMNHIARPFTETEAASILKQVVAGLLYLHSHNIMHRDISLSNLLLSREMHVKIADFGLATQLKRPDERHMTMCGTPNYISPEVVSRTSHGLPADVWSVGCMLYTLLVGRPPFETDAVQSTLNKVVMSEYIMPAHLSYEAQDLINKLLKKLPHERITLEAVLCHPFMLKCSNGGHSAPGALNVFSQSMESGDSGIITFASSDSRNSQQIRSVENSGPQQVLPQIREEFKQVHHKLPYEQTGLFGQASTGLAEPNWPGAAKSSAFCMEAGNVPNSKQASLKEDRISVPPLNTKRLLPTRYKTKNAIMSILRNGEVVLEFLKFRPTYNEDRINDICRISDDGQRIIIYQPDPGRGLPVREQPPDLQIPSGDCVYNYDNLPSKHWKKYIYGARFVGLVKSKTPKVTYFSTLGKCQLMETMTDFEIRFYSGAKLLKTPSEGLKVYDRNGMLLSDYSCSESRSLIEHGNECFTHCVNISNALEVAQTKDNSCFPVTIGRRPITDVQPAQRLDGLRDTTNIAFSTPKSNQGSINFSLSTISSTRNTSDFGTNCSRSNMLAAHQNIPIKRINVPEIGIATELSHGVVQVQFYDGSVVSVIPSMQGGGITYTQPNGTSTHFGKGDDLPFPVRDRVGQIPNIQLKLKTAPLLGSGRKTDYNNAMTPKTTTPYYNRMLL
Protein: Proteoglycan 4 (Lubricin) (Megakaryocyte-stimulating factor) (Superficial zone proteoglycan) [Cleaved into: Proteoglycan 4 C-terminal part] (Q92954)
Organism: Homo sapiens (Human)
Function: Plays a role in boundary lubrication within articulating joints. Prevents protein deposition onto cartilage from synovial fluid by controlling adhesion-dependent synovial growth and inhibiting the adhesion of synovial cells to the cartilage surface.
Subcellular location: Secreted {ECO:0000269|PubMed:14976050, ECO:0000269|PubMed:32144329}.
Interaction partners:
- Aggrecan core protein
- Hemopexin
- CD44 antigen
- Toll-like receptor 2
- Cartilage oligomeric matrix protein
- Toll-like receptor 4
Sequence:
MAWKTLPIYLLLLLSVFVIQQVSSQDLSSCAGRCGEGYSRDATCNCDYNCQHYMECCPDFKRVCTAELSCKGRCFESFERGRECDCDAQCKKYDKCCPDYESFCAEVHNPTSPPSSKKAPPPSGASQTIKSTTKRSPKPPNKKKTKKVIESEEITEEHSVSENQESSSSSSSSSSSSTIRKIKSSKNSAANRELQKKLKVKDNKKNRTKKKPTPKPPVVDEAGSGLDNGDFKVTTPDTSTTQHNKVSTSPKITTAKPINPRPSLPPNSDTSKETSLTVNKETTVETKETTTTNKQTSTDGKEKTTSAKETQSIEKTSAKDLAPTSKVLAKPTPKAETTTKGPALTTPKEPTPTTPKEPASTTPKEPTPTTIKSAPTTPKEPAPTTTKSAPTTPKEPAPTTTKEPAPTTPKEPAPTTTKEPAPTTTKSAPTTPKEPAPTTPKKPAPTTPKEPAPTTPKEPTPTTPKEPAPTTKEPAPTTPKEPAPTAPKKPAPTTPKEPAPTTPKEPAPTTTKEPSPTTPKEPAPTTTKSAPTTTKEPAPTTTKSAPTTPKEPSPTTTKEPAPTTPKEPAPTTPKKPAPTTPKEPAPTTPKEPAPTTTKKPAPTTPKEPAPTTPKETAPTTPKKLTPTTPEKLAPTTPEKPAPTTPEELAPTTPEEPTPTTPEEPAPTTPKAAAPNTPKEPAPTTPKEPAPTTPKEPAPTTPKETAPTTPKGTAPTTLKEPAPTTPKKPAPKELAPTTTKEPTSTTSDKPAPTTPKGTAPTTPKEPAPTTPKEPAPTTPKGTAPTTLKEPAPTTPKKPAPKELAPTTTKGPTSTTSDKPAPTTPKETAPTTPKEPAPTTPKKPAPTTPETPPPTTSEVSTPTTTKEPTTIHKSPDESTPELSAEPTPKALENSPKEPGVPTTKTPAATKPEMTTTAKDKTTERDLRTTPETTTAAPKMTKETATTTEKTTESKITATTTQVTSTTTQDTTPFKITTLKTTTLAPKVTTTKKTITTTEIMNKPEETAKPKDRATNSKATTPKPQKPTKAPKKPTSTKKPKTMPRVRKPKTTPTPRKMTSTMPELNPTSRIAEAMLQTTTRPNQTPNSKLVEVNPKSEDAGGAEGETPHMLLRPHVFMPEVTPDMDYLPRVPNQGIIINPMLSDETNICNGKPVDGLTTLRNGTLVAFRGHYFWMLSPFSPPSPARRITEVWGIPSPIDTVFTRCNCEGKTFFFKDSQYWRFTNDIKDAGYPKPIFKGFGGLTGQIVAALSTAKYKNWPESVYFFKRGGSIQQYIYKQEPVQKCPGRRPALNYPVYGETTQVRRRRFERAIGPSQTHTIRIQYSPARLAYQDKGVLHNEVKVSILWRGLPNVVTSAISLPNIRKPDGYDYYAFSKDQYYNIDVPSRTARAITTRSGQTLSKVWYNCP
Protein: Origin recognition complex subunit 3 (Q7K2L1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Double parked, isoform A
- Origin recognition complex subunit 6
- Origin recognition complex subunit 2
- Origin recognition complex subunit 5
- Origin recognition complex subunit 4
- Origin recognition complex subunit 1
- Cell division control protein
- DNA replication licensing factor Mcm2
- DNA replication licensing factor Mcm5
- DNA replication licensing factor Mcm3
Sequence:
MDPTISVSKGCFVYKNGATRAGKKAASKRKRPAAESSSLLGKEVVQQPFYEEYRKAWNQINDHIADLQHRSYARTLEQLVDFVVGQAERDTPDEVLPTAALLTGINQPDHLSQFTALTQRLHAQRAAMVCVLQSRDCATLKAAVETLVFGLVEDNAEVEQMEDEDEDEDGAERDRKRLRRSQCTMKQLKSWYTNNFDSEQKRRQLVVILPDFECFNASVLQDLILILSAHCGSLPFVLVLGVATAMTAVHGTLPYHVSSKIRLRVFQTQAAPTGLNEVLDKVLLSPKYAFHLSGKTFKFLTHIFLYYDFSIHGFIQGFKYCLMEHFFGGNAFALCTDYSKALGRIKQLTHEDMETIRRLPSFRPYVEQINDCKRIIAVLTDDDYLKKKLPQLLRDCLLHFLLFRCSLEFLTELVGDLPRCPLGKLRRELYVNCLNRAIISTPEYKECLQMLSFLSKDEFVAKVNRALERTEQFLVEEIAPLELGEACTAVLRPKLEAIRLAVDEVVKATMATITTTSPNETRQATDHLTPVASRQELKDQLLQRSKEDKMRHQLNTPTTQFGRALQKTLQLIETQIVQDHLRALQDAPPIHELFVFSDIATVRRNIIGAPRAALHTALNNPHFYMQCKCCELQDQSLLVGTLPDLSVVYKLHLECGRMINLFDWLQAFRSVVSDSDHEEVAQEQIDPQIQARFTRAVAELQFLGYIKMSKRKTDHATRLTW
Protein: Lcmt1 protein (Q78K29)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MTPEQSANLLKWAASSFETAMFINYEQVNMDDRFGQIMIENLRRRSCDLAGVETCKSLESQKERLLLNGWETASAVNMMELYSGLPRAEVNRIESLEFLDEMELLEQLMRHYCLCWATRGGQELGLKEITY
Protein: Mineralocorticoid receptor (MR) (Nuclear receptor subfamily 3 group C member 2) (P08235)
Organism: Homo sapiens (Human)
Function: Receptor for both mineralocorticoids (MC) such as aldosterone and glucocorticoids (GC) such as corticosterone or cortisol. Binds to mineralocorticoid response elements (MRE) and transactivates target genes. The effect of MC is to increase ion and water transport and thus raise extracellular fluid volume and blood pressure and lower potassium levels.
Subcellular location: Cytoplasm. Nucleus. Endoplasmic reticulum membrane; Peripheral membrane protein. Note=Cytoplasmic and nuclear in the absence of ligand; nuclear after ligand-binding. When bound to HSD11B2, it is found associated with the endoplasmic reticulum membrane.
Interaction partners:
- Nuclear receptor coactivator 1
- Angiotensinogen
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Renin
- Glucocorticoid receptor
- 11-beta-hydroxysteroid dehydrogenase type 2
- Angiotensin-converting enzyme
- Heat shock protein HSP 90-alpha
- Prostaglandin E synthase 3
- Heat shock protein HSP 90-beta
Sequence:
METKGYHSLPEGLDMERRWGQVSQAVERSSLGPTERTDENNYMEIVNVSCVSGAIPNNSTQGSSKEKQELLPCLQQDNNRPGILTSDIKTELESKELSATVAESMGLYMDSVRDADYSYEQQNQQGSMSPAKIYQNVEQLVKFYKGNGHRPSTLSCVNTPLRSFMSDSGSSVNGGVMRAVVKSPIMCHEKSPSVCSPLNMTSSVCSPAGINSVSSTTASFGSFPVHSPITQGTPLTCSPNVENRGSRSHSPAHASNVGSPLSSPLSSMKSSISSPPSHCSVKSPVSSPNNVTLRSSVSSPANINNSRCSVSSPSNTNNRSTLSSPAASTVGSICSPVNNAFSYTASGTSAGSSTLRDVVPSPDTQEKGAQEVPFPKTEEVESAISNGVTGQLNIVQYIKPEPDGAFSSSCLGGNSKINSDSSFSVPIKQESTKHSCSGTSFKGNPTVNPFPFMDGSYFSFMDDKDYYSLSGILGPPVPGFDGNCEGSGFPVGIKQEPDDGSYYPEASIPSSAIVGVNSGGQSFHYRIGAQGTISLSRSARDQSFQHLSSFPPVNTLVESWKSHGDLSSRRSDGYPVLEYIPENVSSSTLRSVSTGSSRPSKICLVCGDEASGCHYGVVTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRLQKCLQAGMNLGARKSKKLGKLKGIHEEQPQQQQPPPPPPPPQSPEEGTTYIAPAKEPSVNTALVPQLSTISRALTPSPVMVLENIEPEIVYAGYDSSKPDTAENLLSTLNRLAGKQMIQVVKWAKVLPGFKNLPLEDQITLIQYSWMCLSSFALSWRSYKHTNSQFLYFAPDLVFNEEKMHQSAMYELCQGMHQISLQFVRLQLTFEEYTIMKVLLLLSTIPKDGLKSQAAFEEMRTNYIKELRKMVTKCPNNSGQSWQRFYQLTKLLDSMHDLVSDLLEFCFYTFRESHALKVEFPAMLVEIISDQLPKVESGNAKPLYFHRK
Protein: L(+)-tartrate dehydratase subunit alpha (L-TTD alpha) (EC 4.2.1.32) (P05847)
Organism: Escherichia coli (strain K12)
Interaction partners:
- L
- L-tartrate/succinate antiporter
- Malate dehydrogenase
- D-malate dehydrogenase [decarboxylating]
- Citrate synthase
- HTH-type transcriptional activator TtdR
- NADP-dependent malic enzyme
- Fumarate hydratase class I, anaerobic
- Fumarate hydratase class I, aerobic
- Fumarate hydratase class II
Sequence:
MMSESNKQQAVNKLTEIVANFTAMISTRMPDDVVDKLKQLKDAETSSMGKIIYHTMFDNMQKAIDLNRPACQDTGEIMFFVKVGSRFPLLGELQSILKQAVEEATVKAPLRHNAVEIFDEVNTGKNTGSGVPWVTWDIIPDNDDAEIEVYMAGGGCTLPGRSKVLMPSEGYEGVVKFVFENISTLAVNACPPVLVGVGIATSVETAAVLSRKAILRPIGSRHPNPKAAELELRLEEGLNRLGIGPQGLTGNSSVMGVHIESAARHPSTIGVAVSTGCWAHRRGTLLVHADLTFENLSHTRSAL
Protein: Non-homologous end joining protein Ku (Mt-Ku) (P9WKD9)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: With LigD forms a non-homologous end joining (NHEJ) repair enzyme. Binds linear dsDNA with 5'- and 3'-overhangs but not closed circular dsDNA nor ssDNA. One dimer binds for every 30 bp. Recruits and stimulates the ligase activity of LigD but not of T4 ligase or a human ligase complex (LIG4/XRCC4). Attenuates the 3'- to 5'-exonuclease activity of LigD. Stimulates the template-directed addition of dNTPs by LigD on 5'-overhangs and nuclease activity on 3'-overhangs.
Interaction partners:
- Multifunctional non-homologous end joining DNA repair protein LigD
- DNA ligase C
- DNA ligase D polymerase domain-containing protein
- DNA ligase D polymerase domain-containing protein
- DNA ligase B
- ATP-dependent DNA helicase UvrD1
Sequence:
MRAIWTGSIAFGLVNVPVKVYSATADHDIRFHQVHAKDNGRIRYKRVCEACGEVVDYRDLARAYESGDGQMVAITDDDIASLPEERSREIEVLEFVPAADVDPMMFDRSYFLEPDSKSSKSYVLLAKTLAETDRMAIVHFTLRNKTRLAALRVKDFGKREVMMVHTLLWPDEIRDPDFPVLDQKVEIKPAELKMAGQVVDSMADDFNPDRYHDTYQEQLQELIDTKLEGGQAFTAEDQPRLLDEPEDVSDLLAKLEASVKARSKANSNVPTPP
Protein: Otoancorin (Q7RTW8)
Organism: Homo sapiens (Human)
Function: May act as an adhesion molecule.
Subcellular location: Apical cell membrane {ECO:0000305}; Lipid-anchor, GPI-anchor {ECO:0000305}; Extracellular side {ECO:0000305}. Secreted, extracellular space, extracellular matrix {ECO:0000305}. Note=At the interface between the apical surface of the epithelia and the overlying acellular gel of the tectorial and otoconial membranes. {ECO:0000250}.
Interaction partners:
- Otogelin
- Alpha-tectorin
- Beta-tectorin
Sequence:
MSQEPTTYSLFLFLFLSHGVSSYTVPNSRQDLHPLLQNMAEEIIDGSYLNALLDLIQFQSSHVWTDDLSHRVLAYLNSRNVAFTIPSLQAAVENHLEQRLHQPQKLLEDLRKTDAQQFRTAMKCLLEDKKDGLDLKDIIIDLGEIRERALQSPGVNRSLFLITLERCFQMLNSLECVEILGKVLRGSSGSFLQPDITERLPRDLREDAFKNLSAVFKDLYDKTSAHSQRALYSWMTGILQTSSNATDDSASWVSAEHLWVLGRYMVHLSFEEITKISPIEIGLFISYDNATKQLDMVYDITPELAQAFLERISSSNFNMRNTSTIHRQAHELWALEPFPKMLGLLVCFYNDLELLDATVAQVLLYQMIKCSHLRGFQAGVQKLKAELLDIAMENQTLNETLGSLSDAVVGLTYSQLESLSPEAVHGAISTLNQVSGWAKSQVIILSAKYLAHEKVLSFYNVSQMGALLAGVSTQAFCSMKRKDISQVLRSAVSQYVSDLSPAQQQGILSKMVQAEDTAPGIVEIQGAFFKEVSLFDLRRQPGFNSTVLKDKELGRSQALFLYELLLKTTRRPEELLSAGQLVKGVTCSHIDAMSTDFFLAHFQDFQNNFALLSPYQVNCLAWKYWEVSRLSMPPFLLAALPARYLASVPASQCVPFLISLGKSWLDSLVLDSHKKTSVLRKVQQCLDDSIADEYTVDIMGNLLCHLPAAIIDRGISPRAWATALHGLRDCPDLNPEQKAAVRLKLLGQYGLPQHWTAETTKDLGPFLVLFSGDELSSIATKFPEILLQAASKMARTLPTKEFLWAVFQSVRNSSDKIPSYDPMPGCHGVVAPSSDDIFKLAEANACWALEDLRCMEEDTFIRTVELLGAVQGFSRPQLMTLKEKAIQVWDMPSYWREHHIVSLGRIALALNESELEQLDLSSIDTVASLSWQTEWTPGQAESILQGYLDDSGYSIQDLKSFHLVGLGATLCAINITEIPLIKISEFRVVVARIGTLLCSTHVLAEFKRKAEVVFGDPTEWTSSVLQELGTIAAGLTKAELRMLDKDLMPYFQPSAIKCLPDEIFKELSAEQIASLGPENAAAVTHAQRRRLSPLQLQSLQQALDGAKTHSWQDAPASAGPTRTSSSRSPAGALQSWGLWLGCPLLVLMAKLLW
Protein: Circadian locomoter output cycles protein kaput (B3DH92)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}.
Interaction partners:
- Cryptochrome circadian regulator 3a.
- Cryptochrome-1
- Cryptochrome circadian regulator 1b.
- Cryptochrome circadian regulator 4
- Cryptochrome 3
- Cryptochrome circadian regulator 3b.
- Aryl hydrocarbon receptor nuclear translocator-like 2
- Casein kinase I isoform delta-A
- CLOCK-interacting pacemaker a
- Aryl hydrocarbon receptor nuclear translocator-like 1b.
Sequence:
MSSRDRDDGSIFDGLMEEDEKDKAKRVSRNKSEKKRRDQFNVLIKELGTMLPGNTRKMDKSTILQKSIDYLRKNKENAAQSESSDIKQDWKPPFLSNEEFSQLMLEALDGFFLVMLTDGYIIYISESVTSLLEHLPSDLMDQNLLNFLPVVDHGEVYKALSSQPDIENLNSDYLKSKNQMEFCCHMLRGSVDPKKPPVYEYVKFIGNFKSLVNMPQKTRNGLEGILQHSLQPAFDDQLCFIATVRLAKPQFIKEMCMVEEPNEEFTSRHSLEWKFLLLDHRAPPIIGYMPFEVLGTSGYDYYHVDDLHSLAKCHEHLMQFGKGKSCYYRFLTKGQQWIWLQTNYYITYHQWNSRPEFIVCTHTVVSYAEVRAERRREMGIEESPPELTADKISGSETQLNNSLKKVLERFSDSRSPSTSSRSSHKSSHTAISDNTCTSTPSKLHMDVSSSPRPATVDMISQRRSSVSTQSMSSQNTTQTDSPVQISQQTQHQQQQPQQPQQVQPNALFSAQLNAMQHLKEQLEQRTRMIEANIQKQQEELRQIHEQLQRVQGPQMILQQPAQGGGPSVLLPQVGGAQNNILGIGTQASVVAIQGQNVTSTAHSGSAPQQQTLPQQQTPRSLQQNLQSSSVTQCGPVYNTMMISQPANANVVQIPSNLAPKISQANAINRFPAGQQLVTKIVTAPMACGAVMVPTSMFMGQVVTAYSPFTQQQGQTQTITLQTQPTVPADQQTQAATLQSQQQGATQQSTKQQQPFLQSTRLLHGNQPTQLILQAFPIQQQSTFTPSQQQQQQQQLKPHTQKPQKQTASSHQTDSASAQSQ
Protein: Acetyltransferase, putative (EC 2.3.1.-) (Q582D7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
Sequence:
MALTARGLFFVCALVTTSSTSFFLFACWPVLIVAALRLCTGSAPKRVISLANTYYDFVQQLWIYMMVLLLEGVLRVRIAYHLVSKGEMAREQKLADFFARPPPGRVKLIILNHRCHLDWLVMFPFLARAGIAKSLRIVLKVGLSRVPIFGWSMQLFRYLFLTRKWASDRSHVVRMMDYYKNSDGTVVFLFPEGTDLTESSVKKSNAYALRNNLPQFYQVLNPRSTGMIEMKNMIGAENIDEIVDVTMGYTDFVRGERPNEASLLNGRTPSKIHIVCTRHCFSNDQQDGWEVGDRVKGLRGKGLFSVPADDEALKNWLTDRFAKKELLLSRFYTRNPVGFDEEHIRSVFGQDCDIVSYDEDEEAARYPEITKFSRIARDLGMWYGVVFVILYWTVPVVLVLLFAGYWVLFWFVLCSILCVSAVRKVGNLSYYLIP
Protein: Transcription factor AP-2 C-terminal domain-containing protein (Q19862)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Transcription factor aptf-2
Sequence:
MSYSDYPSDIADYSSFDNMMADICNPSSSSSSNRKRQADPAPDNFAKIPAGMATQPLYFPIHYPVNSGWQSFDVNQVYNNHNMNQPGFGWVALPPPMPHNLQIPDQNSYKPRSGLPVPPPMAEFQDVNGIQQNPNEIFKNAPITSAMCTPESDISTSTNLTPDQDSAQLPLTEQELNEEKNFVVNIESPGKLAHYFLPNVESEQEPNEHIPYPYAKSLFPTFGVPVSSDGNVVAEVVDGRLPAVGTRSKYDITVDEIRRRCGAPEHMNQSALYCFFRKSKKREAINRVKQVLTVHNIPMRTMQRQRKVTCFSPFLEEEATALARDLDSISEEFLPINIIAQEMLEKLMSSGNNLDVCHRMLKNTTATITRVIKTLEVRQPKITGQEEKLKGNNLDLSYHNFSLITHGFGHPNSLSHYRSYLSIVERAVLLCEKIQNGQSLLSNEDVIPGQKPFERMSNEYFVEWQMNLYKKKLAKQMEEVEENKSQRGEHQQIHQHQLYQQHHTNTHPPMPLMPPSQMNLCPPITPIPPQNVYYY
Protein: Pre-glycoprotein polyprotein GP complex (Pre-GP-C) [Cleaved into: Stable signal peptide (SSP); Glycoprotein G1 (GP1); Glycoprotein G2 (GP2)] (P08669)
Organism: Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV)
Function: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glycoprotein transport to the cell surface plasma membrane, formation of infectious virus particles, and acid pH-dependent glycoprotein-mediated cell fusion.
Subcellular location: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Glycoprotein G1]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}.; SUBCELLULAR LOCATION: [Glycoprotein G2]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Note=Binding to the stable signal peptide masks endogenous ER localization signals in the cytoplasmic domain of G2 to ensure that only the fully assembled, tripartite GP complex is transported for virion assembly. {ECO:0000255|HAMAP-Rule:MF_04084}.
Interaction partners:
Sequence:
MGQIVTFFQEVPHVIEEVMNIVLIALSVLAVLKGLYNFATCGLVGLVTFLLLCGRSCTTSLYKGVYELQTLELNMETLNMTMPLSCTKNNSHHYIMVGNETGLELTLTNTSIINHKFCNLSDAHKKNLYDHALMSIISTFHLSIPNFNQYEAMSCDFNGGKISVQYNLSHSYAGDAANHCGTVANGVLQTFMRMAWGGSYIALDSGRGNWDCIMTSYQYLIIQNTTWEDHCQFSRPSPIGYLGLLSQRTRDIYISRRLLGTFTWTLSDSEGKDTPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFNKQAIQRLKAEAQMSIQLINKAVNALINDQLIMKNHLRDIMGIPYCNYSKYWYLNHTTTGRTSLPKCWLVSNGSYLNETHFSDDIEQQADNMITEMLQKEYMERQGKTPLGLVDLFVFSTSFYLISIFLHLVKIPTHRHIVGKSCPKPHRLNHMGICSCGLYKQPGVPVKWKR
Protein: Guanine nucleotide exchange factor in mesoderm, isoform G (LP15490p) (B3DN64)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MEQLAATSAQLLHAKPATPGTPATPTPSATKAKEFVCSEPLSPVDIVDTINFDLVAQHMERLTLADPGDLDPRAELIEAVNKTLVNKPLVRSSSAACASTICSSPLLTYARTKSLGAKASTLGGGVPIKLPTAEQLAELEEANKLSAESLDRLTDIKPKFAARLSELARLNNRPLSSSSICSTSSSSSSGSDQLLNGKLMATSYLASVESLAESENELGDQHHPPAMSVLEKTCLEIVDSERSFVEDLGQVIKGYLQDWKERACLRVDELQILFANIEEIYEFNSMLLQRLINTGRDPGRIARCFIDLRDGFDVYTTYCTSYPEAISLLTKLLQATHTYSLLASTQKLLQHRLPLGSYLLKPVQRILKYHLLLDSLRKHCDVKEVVEAHVIMRQVAHNIDQVKRKQEQQSRVKELSGILDGWLGPELTVLGELRQEGLLMEQHNKQRLVLLFATMLIITKQKEDGRLQFKTYISQNNLMLSEHLPGEPTSFYVIPFDEPRHQIKLTARNRDQKRIWTQHIKGVMLEKLDIPMRAKELVYQLGNEEDRTPDRSTWKWSLHSGSNSTPTYLERRNACRRSEIRQRNSKFKRKTVANSSSFDSFNESLEQEEESISQAKPSKPLARNNSLDDTALQKLAAAMRYRKRDAAVKEETKTPVKEPCKCDQDAKQDERIEPCSCILRDQRSRSAKSQSPVFSYKALKERSKSVPRIGGFSLDEEAEREREQDEDSAASLRGSKPDLSERKTKGKGFFEVKQYNHKTMPKKIANLKKQRSSTTKSCSRFYMDLSEFDSSSSTVLKITESTEELRPDGEIELAQEAATLDESTQDQYYSPDHETELLSPAEKSKRDAQIVLDLLKNSKEFERIYNKQQKRRESPVSPVSPDISRGPILPPPRPPSRSPPPLELEEQEKKPVEEVDSVSEEPIYETLLRNVHVPYKFSPVLGRAKSSQILKKRSKTAPAASRPESDYVTLVYSPEGVLQRVGEEVVQRDSCSSSTTSTSSNGSGSTLKRDSQSTVINLLMEAAQEHESRPLPKNSVSGSESSLLPRALKSIDNLSMAFGRSNRPPERRVSDVSEMCRQSVLHRQGSEAVGERMAHVDYADPKALFGLGVLNHSERDSVFSLTSSSSDSMCEQQRKRSGVGATFEYEQQVEDSLENDFRDSAIYSDDNEKRSGDYDVHLRRPSSPPPPPPPLGPRPHQPPQIAPKPSKDQLIQQRSGVIVCQSASRSWVLQQIENFNK
Protein: Hemagglutinin-neuraminidase (EC 3.2.1.18) (P12554)
Organism: Newcastle disease virus (strain Chicken/Australia-Victoria/32) (NDV)
Function: Mediates the viral entry into the host cell together with fusion/F protein. Attaches the virus to sialic acid-containing cell receptors and thereby initiates infection. Binding of HN protein to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion.
Subcellular location: Virion membrane {ECO:0000250|UniProtKB:Q91UL0}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q91UL0}. Host cell membrane {ECO:0000250|UniProtKB:Q91UL0}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q91UL0}.
Interaction partners:
Sequence:
MNRAVCQVALENDEREAKNTWRLVFRIAILLLTVMTLAISAAALAYSMEASTPGDLVSIPTAISRAEGKITSALGSNQDVVDRIYKQVALESPLALLNTESIIMNAITSLSYQINGAANNSGCGAPVHDPDYIGGIGKELIVDDTSDVTSFYPSAFQEHLNFIPAPTTGSGCTRIPSFDMSATHCYTHNVIFSGCRDHSHSHQYLALGVLRTSATGRVFFSTLRSINLDDTQNRKSCSVSATPLGCDMLCSKVTETEEEDYNSVIPTSMVHGRLGFDGQYHEKDLDVTTLFGDWVANYPGVGGGSFIDNRVWFPVYGGLKPSSPSDTGQEGRYVIYKRYNDTCPDEQDYQIRMAKSSYKPGRFGGKRVQQAILSIKVSTSLGEDPVLTIPPNTVTLMGAEGRVLTVGTSHFLYQRGSSYFSPALLYPMTVNNNTATLHSPYTFNAFTRPGSVPCQASARCPNSCVTGVYTDPYPLVFHRNHTLRGVFGTMLDDEQARLNLVSAVFDNISRSRITRVSSSRTKAAYTTSTCFKVVKTNKTYCLSIAEISNTLFGEFRIVPLLVEILKDDGV
Protein: Peroxisomal ATPase PEX6 (Peroxin-6) (C8VJ57)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- Peroxisomal ATPase PEX1
- Peroxisomal membrane protein PEX14
- Peroxisomal targeting signal receptor
- Peroxisomal membrane protein PEX13
- Peroxisomal membrane protein PEX14
- RING-type E3 ubiquitin transferase
- Peroxisome assembly protein 12
- Peroxin-7
- Microbody
- Ubiquitin-conjugating enzyme E2 2
Sequence:
MDLERHEFSSDQSIRRRRNFARKRLRNKTALSARLSLDHRLRGSVGVVSDDLANDLFQPPDPTDDFQDDSGIRYIAISPYLPGPSSVEALTWTIVPVRPQSAGRSNESPLPKSTIIFPDSADSLQPFVRALSKLDPTRQSPHTLRLIEIRVMDVVPLPLDTIYVTVERDLLRNHDDVQSRFGGGFTSNMNGPNGLWAKGKGAESKKYSKKAAAEVEGRLTAAVREALGTQRVVHTGDSLPLPLPPHPITYAPAPPALISFCEPVSQGLLLPTTKIVLIQARPHGNRAQRSLRPASGFLKQVAEDEADDTSNEQFYSAAEDKPVDDSTEMESTSNAEESETEGSGGNTSDTSDDSLDDMISLSAPELPQPATGVMSGMTSATPRARRMDGIHTPGSMVSNLTSSTLRPGRQGGGKVFKAEGLLRRVPNELLYPKPRDDDDVEAVVFVDISTLAKIGCFSGDWVRIEASEEPQANIFSSINLGSFNEQYGEGDWRAVKIYGLPGLPSAKPRYSIKQSGDRRLSFSQRPGVRMTPSVFVPPLLLNNMDNPRYLRISPMSLGGIGVPKSGVLHQMKTAARSPPVAKEVTLLKVSTPVSMDRALQPALFSALKQYFESKRRLLKSGDLLGISIDETLGRAVFAGTGADGQDDDITTKLGPGLDTNRAGPKKIGVAWFRVGQVIPSLPEDQDDFGEFDWGGVAVIDSATTRMVQAGSDVSRIPNTLNNGWEYWLGTKSIPKPVVDTQTIHGVVTEVPQPFVSPIQQRVRDLMAVATSSRAIQLGMKPVVILLRSQQRHIGKASLATRACAEIGLHTFPIDAYDILTEGGANGGDVKTEAYLKARAERAFHCGADCTALLIKHIEVLTADRIVSAMTEILADARVIIATTTDVEQIPEAIRSMFTHEFELTAPEEKEREGILRNAVSERSIKLAPDVDLGTVALKTAALVAGDLVDVVERASVARSTRLEKLAESASKQSPTSKITVRDVLLAGGEAVRGVTKADFDAAVDAARKNFADSIGAPKIPNVSWEDVGGLTNVKDALVETIQLPLERPELFAKGMKKRSGILFYGPPGTGKTLLAKAIATEFSLNFFSVKGPELLNMYIGESEANVRRVFQRARDARPCVVFFDELDSVAPKRGNQGDSGGVMDRIVSQLLAELDGMNGGEENSGGVFVIGATNRPDLLDTALLRPGRFDKMLYLGVSDTHEKQATILEALTRKFALAPDLSLARVSERLPLTYTGADLYALCSDAMLKAITRKATAVDEKIKQLPGGPVSTAYFFDHLSTPDDVAVMVTEEDFVAAQSELVPSVSAKELEHFERIRQMFESTDKDKQKQDANPAPTPNTIGDAIEALKLGHDINGYIGDPVTNGGDQPLSPTGTGKGKGKQPAYGSMRSVSGQSVSSSRGKGKAATSGGKSSLKSKSVSAANGNADSDSSLDGPLMGSGARGGVNSDGDDDDDDNDYIVRTDHLAKTDADGEDVD