wanglab/gogpt-training-data huggingface dataset:
Protein: Protein WBSCR14 homolog (MLX interactor) (P41846)
Organism: Caenorhabditis elegans
Function: Transcription factor that binds to the E box motif 5'-CACGTG-3', probably in a heterodimeric complex with mxl-2. Involved in modulating longevity in response to TOR signaling, dietary restriction, the decline in protein homeostasis associated with normal aging, germline signaling and the insulin-like signaling pathway. Plays a role in autophagy. Involved in regulating migration of the ray 1 precursor cells in the male tail, acting in concert with Wnt and semaphorin signaling pathways. Regulates transcription of genes encoding extracellular matrix (ECM) components which may contribute to the substratum required for migration of the neighboring ray 1 precursor cells. Involved in repressing infection by the microsporidian pathogen N.parisii, probably acting independently of its canonical partner, mxl-2.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17826759, ECO:0000269|PubMed:24699255, ECO:0000269|PubMed:27402359}. Cytoplasm {ECO:0000269|PubMed:24699255}. Mitochondrion {ECO:0000269|PubMed:27001890}. Note=Nuclear localization is promoted by conditions of dietary restriction or reduced insulin-like/IGF-1 signaling in a pha-4-dependent manner. {ECO:0000269|PubMed:24699255}.
Interaction partners:
- Max-like protein homolog 2
- Max-like protein 1
- Mad-like protein 1
- Helix-loop-helix protein 30
- Intestinal acid PHOsphatase
Sequence:
MSRGQIIHSGHFMCSNPHDDLVQDEDEEDVEVDVVEDDDKSMEASSSVHHKNKALDEKPVTFYKFGVGKTQSIAIDVSLNKLNKCIKVAYNKMTTPKWKDFKGLRLHWKQRVRLNNVIWRAYYIEFRKKQPEKPKKPFCYFAVPDDDTTHQKIEGSIVEGMYWKRKMEGVCAQYKRWRIRSKHNLVTDKGGMVATCSSTSVSSMTGELKRKRKHTVPKETIESKLRSYEPPVKLQRSQTPKHTISDEFAWDFDDLDNVFTDDFLNSLSEPYMFPDPRDVYSGNNADIMQPGLLPLQPTIEDIMMSLGDDMPDSPPFHNDRDTMRTPTNDQPSISAQQIPQMRRSASSSASLHQMQVAQAQAQSISQISQPSQQLQHQIQIQQPVAARPHEFMASSIMMDYRLMPTRQSSAITSQMLMLSQSASTLSSQPQYATSTHYSTNNSFLPIRNTMTNQHHLGHTSQHSPWNKQQQSNFLVSLPHQSHVERILNNQPPLVPPPSRSNLLPTQNDPYLPQFLQSTQPTPQPQSHDPMMAPSRSWWLDSPLTASVQSPLSVATPLPLANQTGPQTPLGQLIGSADNGFLFGGNNTPGGFKMSGTTSGVPTLSQRLEQPPISRTSTIFGNVENKPERIFTSLTSQNTPTPSPLDISSLSRLRTSSLNESWKMSHIVEGSPTYQAFAASVTTKPSILESPSTSGDISGPASVPVQASQHPPKIITPPSASSKRKEQEAAMAPLVNRQQSCDVNLLNGKMAVKVEEKSGRHYLPTTPTELKEVTKEEPLLMSAPSSVKSMRRQAPDSTLHPEERKRILHLHAEQNRRSALKDGFDQLMDIIPDLYSGGVKPTNAVVLAKSADHIRRLQAEKWDKTQKIDEAKAKIEKLNQKITSLQSNLPQSSAPSSSSQVDSKTSLETFFDRYVKEGAKKNWRFWVMSQMLKPICVTQTNSFASSVAGDSSSRNEVAASCSDWLNKNWKATELRPLASTLLVSLATNSSILAEPDTLPDYVMQQLKNPF
Protein: Nonstructural protein (Q4U3C5)
Organism: Bombyx mori densovirus 3 (isolate Silkworm/China/Zhenjiang/-) (BmDNV-3)
Subcellular location: Host nucleus {ECO:0000256|ARBA:ARBA00004147}.
Interaction partners:
Sequence:
MESKSNFRILSNEIISKPSSLISNISSPSTSLIPRSLQKSAKRLTISSLESGNGKQQMKSKLAQVQRALRFCRDYNIVKYYQFMDIPPEEYRELRTHCSKDVLETAADINYQEYYYEEVNNRLQVFLSYGDGSWGEEEEEIVMLFKHNNVDISKFCEALYSIFTMSDYRKNCIFLNGNIKTGKTLMMRLITGNFKCVGKGCNNGVNSEFYYQKFIGRSICVLEEPFLDPQTLEDFKSIFGGEGFDISCKFHNPQTLNRTPFIITSNFSLLSRGHAPSISEMAIKDRFYIFNFNNSYTPKCKLSPKNFVNVYNKYYG
Protein: Desmocollin-3 (Cadherin family member 3) (Desmocollin-4) (HT-CP) (Q14574)
Organism: Homo sapiens (Human)
Function: Component of intercellular desmosome junctions. Involved in the interaction of plaque proteins and intermediate filaments mediating cell-cell adhesion. May contribute to epidermal cell positioning (stratification) by mediating differential adhesiveness between cells that express different isoforms.
Subcellular location: Cell membrane; Single-pass type I membrane protein. Cell junction, desmosome.
Interaction partners:
- Plakophilin-2
- Junction plakoglobin
- Desmoglein-2
- Desmoplakin
- Desmoglein-3
- Desmoglein-1
- Plakophilin-3
- Transmembrane protein 43
- Plakophilin-1
- Plakophilin-4
Sequence:
MAAAGPRRSVRGAVCLHLLLTLVIFSRAGEACKKVILNVPSKLEADKIIGRVNLEECFRSADLIRSSDPDFRVLNDGSVYTARAVALSDKKRSFTIWLSDKRKQTQKEVTVLLEHQKKVSKTRHTRETVLRRAKRRWAPIPCSMQENSLGPFPLFLQQVESDAAQNYTVFYSISGRGVDKEPLNLFYIERDTGNLFCTRPVDREEYDVFDLIAYASTADGYSADLPLPLPIRVEDENDNHPVFTEAIYNFEVLESSRPGTTVGVVCATDRDEPDTMHTRLKYSILQQTPRSPGLFSVHPSTGVITTVSHYLDREVVDKYSLIMKVQDMDGQFFGLIGTSTCIITVTDSNDNAPTFRQNAYEAFVEENAFNVEILRIPIEDKDLINTANWRVNFTILKGNENGHFKISTDKETNEGVLSVVKPLNYEENRQVNLEIGVNNEAPFARDIPRVTALNRALVTVHVRDLDEGPECTPAAQYVRIKENLAVGSKINGYKAYDPENRNGNGLRYKKLHDPKGWITIDEISGSIITSKILDREVETPKNELYNITVLAIDKDDRSCTGTLAVNIEDVNDNPPEILQEYVVICKPKMGYTDILAVDPDEPVHGAPFYFSLPNTSPEISRLWSLTKVNDTAARLSYQKNAGFQEYTIPITVKDRAGQAATKLLRVNLCECTHPTQCRATSRSTGVILGKWAILAILLGIALLFSVLLTLVCGVFGATKGKRFPEDLAQQNLIISNTEAPGDDRVCSANGFMTQTTNNSSQGFCGTMGSGMKNGGQETIEMMKGGNQTLESCRGAGHHHTLDSCRGGHTEVDNCRYTYSEWHSFTQPRLGEKLHRCNQNEDRMPSQDYVLTYNYEGRGSPAGSVGCCSEKQEEDGLDFLNNLEPKFITLAEACTKR
Protein: Probable ATP-dependent RNA helicase DDX46 (EC 3.6.4.13) (DEAD box protein 46) (PRP5 homolog) (Q7L014)
Organism: Homo sapiens (Human)
Function: Plays an essential role in splicing, either prior to, or during splicing A complex formation.
Subcellular location: Nucleus speckle {ECO:0000269|PubMed:12234937}. Nucleus, Cajal body {ECO:0000269|PubMed:12234937}. Note=Present in Cajal bodies (CBs) and nuclear speckles. {ECO:0000269|PubMed:12234937}.
Interaction partners:
- Splicing factor 3B subunit 1
- Splicing factor 3A subunit 3
- Splicing factor 3A subunit 2
- Splicing factor 3A subunit 1
- Splicing factor 3B subunit 5
- Splicing factor 3B subunit 2
- Splicing factor 3B subunit 3
- Small nuclear ribonucleoprotein Sm D1
- U2 small nuclear ribonucleoprotein A'
- PHD finger-like domain-containing protein 5A
Sequence:
MGRESRHYRKRSASRGRSGSRSRSRSPSDKRSKRGDDRRSRSRDRDRRRERSRSRDKRRSRSRDRKRLRRSRSRERDRSRERRRSRSRDRRRSRSRSRGRRSRSSSPGNKSKKTENRSRSKEKTDGGESSKEKKKDKDDKEDEKEKDAGNFDQNKLEEEMRKRKERVEKWREEQRKKAMENIGELKKEIEEMKQGKKWSLEDDDDDEDDPAEAEKEGNEMEGEELDPLDAYMEEVKEEVKKFNMRSVKGGGGNEKKSGPTVTKVVTVVTTKKAVVDSDKKKGELMENDQDAMEYSSEEEEVDLQTALTGYQTKQRKLLEPVDHGKIEYEPFRKNFYVEVPELAKMSQEEVNVFRLEMEGITVKGKGCPKPIKSWVQCGISMKILNSLKKHGYEKPTPIQTQAIPAIMSGRDLIGIAKTGSGKTIAFLLPMFRHIMDQRSLEEGEGPIAVIMTPTRELALQITKECKKFSKTLGLRVVCVYGGTGISEQIAELKRGAEIIVCTPGRMIDMLAANSGRVTNLRRVTYVVLDEADRMFDMGFEPQVMRIVDNVRPDRQTVMFSATFPRAMEALARRILSKPIEVQVGGRSVVCSDVEQQVIVIEEEKKFLKLLELLGHYQESGSVIIFVDKQEHADGLLKDLMRASYPCMSLHGGIDQYDRDSIINDFKNGTCKLLVATSVAARGLDVKHLILVVNYSCPNHYEDYVHRAGRTGRAGNKGYAYTFITEDQARYAGDIIKALELSGTAVPPDLEKLWSDFKDQQKAEGKIIKKSSGFSGKGFKFDETEQALANERKKLQKAALGLQDSDDEDAAVDIDEQIESMFNSKKRVKDMAAPGTSSVPAPTAGNAEKLEIAKRLALRINAQKNLGIESQDVMQQATNAILRGGTILAPTVSAKTIAEQLAEKINAKLNYVPLEKQEEERQDGGQNESFKRYEEELEINDFPQTARWKVTSKEALQRISEYSEAAITIRGTYFPPGKEPKEGERKIYLAIESANELAVQKAKAEITRLIKEELIRLQNSYQPTNKGRYKVL
Protein: Nucleolar RNA helicase 2-A (EC 3.6.4.13) (DEAD box protein 21-A) (Gu-alpha-A) (Nucleolar RNA helicase Gu-A) (xGu-1) (Nucleolar RNA helicase II-A) (RH II/Gu-A) (Q9DF35)
Organism: Xenopus laevis (African clawed frog)
Function: RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (By similarity). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (By similarity). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification (Probable). Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (By similarity). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (By similarity). Required to prevent R-loop-associated DNA damage and transcription-associated genomic instability (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:12851405}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q9NR30}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JIK5}. Mitochondrion {ECO:0000250|UniProtKB:Q9JIK5}.
Interaction partners:
Sequence:
MPVKVYAEEMEGESMKKKKLSETPLPKIKKRKMKNGDTEDLDLEHMAESVNGEINNNNPTPKLKKKKKPAPISDLSETAEECDGEQPDPSTPTPKKVKKKKIKESKEDSDTQEEAEQSEPQTNGVKSVKKSKKNITSDDNEPAPKKRKTDTTEITTAKECEEKVLTKEEQDINQEKIDGDFSKFPLSKETIKNLQAKGVSYLFPIQSKTFHTAYSGKDVVVQARTGTGKTFSFAIPLVEKLNEDQQPLARGRAPRVIILTPTRELAIQITNEIRSITKKLKVSCFYGGTPYQQQVFAIKDGIDFLVGTPGRVRDLVQNYRLDLTTLKHVVLDEVDMMFDMGFSEQVEEILSVRYKADPEENPQTLLFSATCPDWMYNMAKKYMRKQFEKIDLIGHRSQKAATTVEHLAIECTRSQKAAVLGDLVQVYSGSHGKTIIFCDSKLEAHTLATSCGSLKQSAKSLHGDLQQKEREVVLKGFRQGTFEVLIATNVAARGLDIPEVDLVVLYSAPKEADAYVHRSGRTGRAGRTGVCISLYEPWERHYLRNVERSTGITFKRVGVPSLLNVAKSSSADAIKSLDTVPADVIEHFKEYAQELIEQKGALTAIAAALAHISGATSIKQRSLLNMEAGCDTITLKSSVPIHSLSYAWQSIKEQLGDDVDSKIHRMCLLKDSMGVCFDVRSENLESMQERWTDTKQWQFTVATELPAIQESERNFDGPRNRGFGGRGRRPFDRRNNSRNSNRGGGGRGRNRNGGFRRGR
Protein: Missing-in-metastasis, isoform M (A0A0B4KED3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MDLSLERDSSALGSLFQQIINDMKNTSPLWEDFVAKAGKLHTCLRAAIQAIAAYLDAFQKIADAATNSRGASKEIGTALTRVCLRHKAVETRLKTFTSTIMDCLVQPLQERIEDWKRTVATIDKDHAKEYKRCRSELKKRSSDTLRLQKKARKGQTDGLQSLMDSHMQDVTLRRAELEEVEKKSLRAAMVEERLRYCSFVHMLQPVVHEECEVMSELGHLQEAMQSIALVTKEPSVLPQASEELIHDAKASINLYPESPGGGSGSQGGGCSNSLGSRKSSVCSISSMNSSGSSNSPGHHHYPRSLSQFVTPAIRLKPGESSDSGFCSSPALTTQTSNATNQTANVSTWPPHSQDGVDTLPPTADRPHTISTAYEKGHQRPPLTVYTFQNPETIHESGSCLNNGTAAPNGQPLSGQATPATQKSPAASLSRPPLPVRCSSLERPLSAQSNHRQGSGNNLLQRQCPSPIPAHITKDKSFEDSIQALNNLIGELDSFQREIDEGKVKPPSNIISGSTTSSNNNNTTTSSISSSDNNNLPATSNIEPCAISNQTNSSGCGTDISDTTSDELAGDDMDVRRRDRDRDRDLLGASDSELSRCYVSETSSLTGGLTAGGYENPTFAHFAANANREDAVSLASDSVCLGQPRHAYVDTCSDSGSAVVVIYDHQIPNTPDIEFVKQNSEIVVLRTKDPQPHALQLHEMRELQQLPANLAGSPDSSPDSAGGQAPPTATVAPAKQRLSSFRATSEQQLQLLGRGSPQRGGAAGGGSTRIGRRSSINQSKPPPPVRRSSSVTPSPNASVGLQQQPQHATLSQQNHQLSSSSEHLPPPPPFMLDAMPQIPSSALKVSETSAHNSPLKEDLTVYYDSYLDLHAYAQALASGQQPGGQQMANQQRFTLQQQHQHLHQPQQPPVYQVDATFRTSSPAAGGGGGGGIYAQPKLVNSMSSFRTSSPSPNGHAHPLPPTQPKANPNLIAQLNARLSGKQQQHQQQQHIEGIYGNQQAPGGESIYMRSGLSMSQPQQQQHFDAAAQSPNMRQAHSHQHHQPPQQQHYTCPPPLEDPPPPPIYAAGASATMPKKMARPPTGQNATHSSAYAAASSTATLPKNMMQQQQRLQHQQQYQQPAGMGIGNGNGHLGQRPQLPLPQQKLRAAQQQHLAEQQHQQQQEQQQHHQQHQQHQQRQPPIPSRHSSVQQKIFVSTNPFIQTTAVKFHSPSASPTCGSPVTGSLASIYATTSRGGHHHQQQQAQQQQHYYRDAAGGNSNGGAAYYNHNAHAHSQAHHPTGPSHLSRIADGSNQARSHLKA
Protein: Spindle pole body component SPC97 (P38863)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Involved in microtubule organization by the microtubule organizing center, the spindle pole body (SPB). Probably part of the microtubule attachment site at the SPB.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body.
Interaction partners:
- Tubulin gamma chain
- Gamma tubulin complex adapter SPC72
- Spindle pole body component 110
- Spindle pole body component SPC98
- DASH complex subunit ASK1
- Spindle pole body component SPC42
- Cell division control protein KAR1
- Cell division control protein 31
- Protein STU2
- Spindle pole component 29
Sequence:
MEIKEVDDRAELLRYTNNIPLLGKLVNHQPLWSTNPKLKSFSLEKISAPDQRRVQEALVVKDLLNVLIGLEGTYIRYFNDYEPSDPETPIEFKIAKKMDPSFKTFSRRIVRYGKQYMILTRAYEKWSDTSFGMVLQRFAYEIRRFLEDVYLKTLVERLERDFNKVPNFSIRELEQIINETEVNKQMELLYNIYEEIFREIEERRTNQSSQEDFNNFMDSMKNESSLHLRLMVAFDTTVYPVPKGGAILKIFQQKILENLGDRSSVMFLKKLLNNISQDYCTMLYEWLTQGILNDPYQEFMTYDDLEGKTDNIFDTRDRAWDTQYFIRKDVLLRDCDSEEDKNLLFKMLRTGILLKVVRASLQIPTIPSNSSDITIQEINDFADLMEGSNLELYVDKCYSRANEIFLKLFFQGYDLINVLKHLQQIFLGYQSGHNVLKFLTKNMGELTKHYRNDNNANYDKLLQNFELERQSENPNNLMRQLLMIQFDTETLPQVLSHYLQIYPEVPENNSANDDSDPLMHANNFKNMNAILFDELSKERTGAYHGSNLELYTPKSAIYHLKFDINIPYPLNIIISRTCMIKYQIILRYQLVLQYHSRLLDETWMDLNKTPSWKYRGYSHTVKRRIVRATRVLHAKMNHFIKTIMEYFNQNVIDKEVYSLEKCYRNPTLAVAIQNELEGGLTNIMTNRCLSDLIPLQLQIFDIVYKFCKFIKSMRAKLCQLDPVLYEKHKSGMMKTLNEGYRTNNGGQEDVGYQEDAALELIQKLIEYISNASSIFRKCLINFTQELSTEKFDFYDSSSVDAAGIERVLYSIVPPRSASASSQR
Protein: PHD finger protein 6 (Q9D4J7)
Organism: Mus musculus (Mouse)
Function: Transcriptional regulator that associates with ribosomal RNA promoters and suppresses ribosomal RNA (rRNA) transcription.
Subcellular location: Nucleus {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q8IWS0}. Note=Nuclear, it particularly localizes to the nucleolus. {ECO:0000250}.
Interaction partners:
- Histone lysine demethylase PHF8
- Host cell factor 1
- Histone-lysine N-methyltransferase 2A
- Histone-binding protein RBBP4
- Polycomb group protein ASXL1
- Histone-binding protein RBBP7
- U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2
Sequence:
MSSSIEQKKGSTRQRKCGFCKSNRDKECGQLLISENQKVAAHHKCMLFSSALVSSHSDNESLGGFSIEDVQKEIKRGTKLMCSLCHCPGATIGCDVKTCHRTYHYHCALHDKAQIREKPSQGIYMVYCRKHKKTAHNSEADLEESFNEHELEPSSPKTKKKSRKGRPRKTNLKGLPEDSRSTSSHGTDEMESSSYRDRSPHRSSPNDTRPKCGFCHVGEEENEARGKLHIFNAKKAAAHYKCMLFSSGTVQLTTTSRAEFGDFDIKTVLQEIKRGKRMKCTLCSQPGATIGCEIKACVKTYHYHCGVQDKAKYIENMSRGIYKLYCKNHSGNDERDEEDEERESKSRGRVAIDQQLTQQQLNGN
Protein: Transcription factor LHW (BHLH transcription factor delta) (bHLH delta) (Basic helix-loop-helix protein 156) (AtbHLH156) (bHLH 156) (Protein LONESOME HIGHWAY) (bHLH transcription factor bHLH156) (Q9XIN0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Transcription activator that regulates root development; promotes the production of stele cells in roots. Coordinately controls the number of all vascular cell types by regulating the size of the pool of cells from which they arise.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:17626058}.
Interaction partners:
- Transcription factor AIG1
- Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG4
- Transcription factor SAC51
- Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG3
- Pseudo histidine-containing phosphotransfer protein 6
- Homeobox-leucine zipper protein ATHB-8
- Thermospermine synthase ACAULIS5
- C18orf8
- Auxin response factor 5
- Dof zinc finger protein DOF5.3
Sequence:
MGVLLREALRSMCVNNQWSYAVFWKIGCQNSSLLIWEECYNETESSSNPRRLCGLGVDTQGNEKVQLLTNRMMLNNRIILVGEGLVGRAAFTGHHQWILANSFNRDVHPPEVINEMLLQFSAGIQTVAVFPVVPHGVVQLGSSLPIMENLGFVNDVKGLILQLGCVPGALLSENYRTYEPAADFIGVPVSRIIPSQGHKILQSSAFVAETSKQHFNSTGSSDHQMVEESPCNLVDEHEGGWQSTTGFLTAGEVAVPSNPDAWLNQNFSCMSNVDAAEQQQIPCEDISSKRSLGSDDLFDMLGLDDKNKGCDNSWGVSQMRTEVLTRELSDFRIIQEMDPEFGSSGYELSGTDHLLDAVVSGACSSTKQISDETSESCKTTLTKVSNSSVTTPSHSSPQGSQLFEKKHGQPLGPSSVYGSQISSWVEQAHSLKREGSPRMVNKNETAKPANNRKRLKPGENPRPRPKDRQMIQDRVKELREIIPNGAKCSIDALLERTIKHMLFLQNVSKHSDKLKQTGESKIMKEDGGGATWAFEVGSKSMVCPIVVEDINPPRIFQVEMLCEQRGFFLEIADWIRSLGLTILKGVIETRVDKIWARFTVEASRDVTRMEIFMQLVNILEQTMKCGGNSKTILDGIKATMPLPVTGGCSM
Protein: Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain] (P03435)
Organism: Influenza A virus (strain A/Victoria/3/1975 H3N2)
Function: Binds to sialic acid-containing receptors on the cell surface, bringing about the attachment of the virus particle to the cell. This attachment induces virion internalization of about two third of the virus particles through clathrin-dependent endocytosis and about one third through a clathrin- and caveolin-independent pathway. Plays a major role in the determination of host range restriction and virulence. Class I viral fusion protein. Responsible for penetration of the virus into the cell cytoplasm by mediating the fusion of the membrane of the endocytosed virus particle with the endosomal membrane. Low pH in endosomes induces an irreversible conformational change in HA2, releasing the fusion hydrophobic peptide. Several trimers are required to form a competent fusion pore.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04072}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04072}. Note=Targeted to the apical plasma membrane in epithelial polarized cells through a signal present in the transmembrane domain. Associated with glycosphingolipid- and cholesterol-enriched detergent-resistant lipid rafts. {ECO:0000255|HAMAP-Rule:MF_04072}.
Interaction partners:
Sequence:
MKTIIALSYIFCLVFAQDLPGNDNNSTATLCLGHHAVPNGTLVKTITNDQIEVTNATELVQSSSTGKICNNPHRILDGINCTLIDALLGDPHCDGFQNEKWDLFVERSKAFSNCYPYDVPDYASLRSLVASSGTLEFINEGFNWTGVTQNGGSSACKRGPDSGFFSRLNWLYKSGSTYPVQNVTMPNNDNSDKLYIWGVHHPSTDKEQTNLYVQASGKVTVSTKRSQQTIIPNVGSRPWVRGLSSRISIYWTIVKPGDILVINSNGNLIAPRGYFKMRTGKSSIMRSDAPIGTCSSECITPNGSIPNDKPFQNVNKITYGACPKYVKQNTLKLATGMRNVPEKQTRGIFGAIAGFIENGWEGMIDGWYGFRHQNSEGTGQAADLKSTQAAIDQINGKLNRVIEKTNEKFHQIEKEFSEVEGRIQDLEKYVEDTKIDLWSYNAELLVALENQHTIDLTDSEMNKLFEKTRRQLRENAEDMGNGCFKIYHKCDNACIGSIRNGTYDHDVYRDEALNNRFQIKGVELKSGYKDWILWISFAISCFLLCVVLLGFIMWACQKGNIRCNICI
Protein: Hybrid signal transduction histidine kinase I (EC 2.7.13.3) (Q86AT9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: Acts as a receptor histidine kinase for a signal transduction pathway. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain (By similarity).
Interaction partners:
Sequence:
MIYLKILEKLNQAIWLFDINKRVLIWGNQSCKKYKNIESITSLFNNSNLINDIRNGKSKHEHIDIIESNENGEILKQMIFKYSSIHISDMDARQLYLDTSINLLVNQDSHYLDYEGKRIFILVEAIEEIKFIQSPLSSSIENHNINNNQNNQNSVNINSSNKGQYNRPEPSNMGSWEWNVQNDTTKASNQFYKIIGIENDFNKKLNFNDFINKLGIQEIQPIINNCIESNSSSFEYPLRINRKNDNLVRYIQLKGEIIKKDDKVFKVLGVCHDFSEIQEAKDKLEEESKFVEALIGCLKAGIVACNSNGDLTHFNKSAQDLHGLELNDKTDRKQLLDQILKCYRSPYEQINLEKSGTPIIRALSGEFINDQEIIITPTSNQQQSSLSKSNRPRSQSNCSNGNKSQNRLSKNYSTTTTTTNNNNNNNNNNNNNNNNNNNNNSISQQQQTQVSTQQTQQQQNTTNGIGGATTSTTAAAATITSPQQIPIATKIPTKINDNEFLVLASGQEIVSKDGKTIGAFVALHDITERKRNEVILKNATEEAQRANQLKGEFLANISHELLSPMNSIIGMVGLCLDVAPRNLKEMLNDVVESSKILLDLLHQILDFTTLESNSLAVRPFPFKLRDTFNQLFKVFYTRIIEKKISLTFSIDPNIADDFYGDQNRLKQILSNLIDNAIKFSNSSNINNSISIIVEQLTHNQFKKYKDSFRSNSKTHSRLNSHDDYSIDGDYDDQDNNDSYFGRDINVSDNESAVGGFSELDEKDNSDDDDENDDENDETDENDDDTDDDTSSNTSRNNISNNLLFHNNTSGGGGGGINKREKFKKKDREGFVNLKFSIKDRGIGVPEDKHDFIFDRFFQVDGSYSRVQGGVGLGLSICKKLIEFFGGAIWFESEASQGSTFHFILSIKSVEAPSPKSPSLQSSNGSINSTTKLFESSRLKNEIYIPSLPNVQTKKVKKDSNDNGNNDSTNYGISLSNSMNNININGSTLNNNNSINNNNNSNDNGPLTSRTPSNSYYNFIASLNNTSLKSSSHNTLSSSPTGFNGISNLNISGLNNLSNLSNNPNNLNNIIGNTNGNNNTNGNNNSGISLNNSNNNIQTPNGLNNSRGSSLISTPSTKNVKKQHSCPMDLIQRIHSICTPRGPISKECGLNNLPAYSPPKSPGRSLSHGGKNYSNLISTPRGGVGYSSPPINSSSSSGGGSSTNGSNSGNSSANNSTPSSSSLSSTPLTSSNTPSPVSISSNNVNNNNQQQQTQPILSPILPLKDNSIDISDLNNINSLTPNSSNSTSTNVTQSSSNIINNGNSITIINNNPVTPNGKKIVIVPLLSLQSASSPKQSQRGYSPKQQYSPKQYSPKQQYSPKQYSPKQQQQQQQQQQQLEQLSGRMSPHKSNLSSTNLHHIHHHHIHQQQSQQHNNTTVHSNNLILNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNTTNTSNNHTSDPSKSSNSTPETSPPISSPRSNNNNNCSLTTIVGVTTPPQPSSTITTPQFQSPPILSGNSGNINLLSSNGTSSGGIEISGSQMIPQKVLVAEDNTMNQKLIKTLLTKRGFDITIAKDGKQALDFYHESKNKSILYDCILMDIQMPILSGLEATCAIREIEANEGGHIPIIAVTAHAMKGDKEKFLESGVDDYVTKPINPKLLYEVINTQICKYIEENRSSSTINENKNTINNNNNNTNNNNNNNNSSNPVNNNNSNSIDATQQELNNEKIRI
Protein: Formin-binding protein 1 (Formin-binding protein 17) (Rapostlin) (Q8R511)
Organism: Rattus norvegicus (Rat)
Function: Required to coordinate membrane tubulation with reorganization of the actin cytoskeleton during the late stage of clathrin-mediated endocytosis. Binds to lipids such as phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and promotes membrane invagination and the formation of tubules. Also enhances actin polymerization via the recruitment of WASL/N-WASP, which in turn activates the Arp2/3 complex. Actin polymerization may promote the fission of membrane tubules to form endocytic vesicles. May be required for the lysosomal retention of FASLG/FASL (By similarity). May act as a link between RND2 signaling and regulation of the actin cytoskeleton. Isoform 1 and isoform 2 promote RND2-induced neurite branching in neuronal cells.
Subcellular location: Cytoplasm, cell cortex. Cytoplasm. Cytoplasmic vesicle {ECO:0000250}. Lysosome {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}. Note=Enriched in cortical regions coincident with F-actin. Also localizes to endocytic vesicles and lysosomes. {ECO:0000250}.
Interaction partners:
- Actin nucleation-promoting factor WASL
- Actin nucleation-promoting factor WAS
- Cell division control protein 42 homolog
- F-BAR domain only protein 2
- Intersectin 2
- FCH and mu domain containing endocytic adaptor 1
- tRNA-splicing endonuclease subunit Sen2
- Sorting nexin-2
- F-BAR and double SH3 domains protein 1
- Intersectin-1
Sequence:
MSWGTELWDQFDNLEKHTQWGIDILEKYIKFVKERTEIELSYAKQLRNLSKKYQPKKNSKEEEEYKYTACKAFLSTLNELNDYAGQHEVISENMTSQITVDLVRYVQELKQERKSNFHDGRKAQQHIETCWKQLESSKRRFERDCKEADRAQQYFEKMDADINVTKADVEKARQQAQMRQQMAEDSKADYSLILQRFNQEQWEYYHTHIPNIFQKIQEMEERRIVRIGESMKTYAEVDRQVIPIIGKCLDGIVKAAESIDQKNDSQLVVEAYKSGFEPPGDIEFEDYTQPMKRTVSDNSLSSSKEGKPELKFGGKSRGKLWPFIKKNKLMTLLTSPHQPPPPPPASASPSAVPNGPQSPKQQKEPLSHRFNEFMTSKPKIHCFRSLKRGLSLKLGVTPEDFSNFPPEQRRKKLQQKVDDLNKEIQKETDQRDAITKMKDVYLKNPQMGDPASLDHKLAEVTQNIEKLRLEAHKFEAWLAEVEGRLPARSEQARRQSGLYDGQTHQTVTNCAQDRESPDGSYTEEQSQESEHKVLATDFDDEFDDEEPLPAIGTCKALYTFEGQNEGTISVVEGETLSVIEEDKGDGWTRIRRNEDEEGYVPTSYVEVYLDKNAKGS
Protein: Neurovirulence factor ICP34.5 (Infected cell protein 34.5) (protein gamma(1)34.5) (P36313)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Plays essential roles in viral nuclear egress to mediate capsid transit across the nuclear membrane and also in the inhibition of host immune response. Facilitates nuclear egress cooperatively with host C1QBP and protein kinase C/PKC to induce lamin A/C phosphorylation and subsequent reorganization. In turn, lamina disassembles and nuclear egress occurs. Recruits the serine/threonine protein phosphatase PPP1CA/PP1-alpha to dephosphorylate the translation initiation factor eIF-2A, thereby couteracting the host shutoff of protein synthesis involving double-stranded RNA-dependent protein kinase EIF2AK2/PKR. In turn, controls host IRF3 activation and subsequently inhibits host interferon response. Controls the DNA sensing pathway by interacting with and inhibiting host STING/TMEM173. Also down-modulates the host MHC class II proteins cell surface expression. Acts as a neurovirulence factor that has a profound effect on the growth of the virus in central nervous system tissue, by interqcting with host BECN1 and thereby antagonizing the host autophagy response.
Subcellular location: Host cytoplasm {ECO:0000250|UniProtKB:P08353}. Host nucleus {ECO:0000250|UniProtKB:P08353}. Host nucleus, host nucleolus {ECO:0000250|UniProtKB:P08353}. Virion {ECO:0000250|UniProtKB:P08353}. Note=At early times in infection, colocalizes with PCNA and replication proteins in the host cell nucleus, before accumulating in the host cytoplasm by 8 to 12 hours post-infection. {ECO:0000250|UniProtKB:P08353}.
Interaction partners:
Sequence:
MARRRRHRGPRRPRPPGPTGAVPTAQSQVTSTPNSEPAVRSAPAAAPPPPPAGGPPPSCSLLLRQWLHVPESASDDDDDDDWPDSPPPEPAPEARPTAAAPRPRPPPPGVGPGGGADPSHPPSRPFRLPPRLALRLRVTAEHLARLRLRRAGGEGAPEPPATPATPATPATPATPARVRFSPHVRVRHLVVWASAARLARRGSWARERADRARFRRRVAEAEAVIGPCLGPEARARALARGAGPANSV
Protein: Interferon B (C1IRY6)
Organism: Salmo salar (Atlantic salmon)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
KPCRWTQFRLGKLNDVSIGLLSDMGGLFPLMCAEENVEQMFPEDLYKNTEGEDVYVVALEAMRYVEQLYNNSLTSVTWNKTKLNMFQNVIYRQVQNLELCVVGGVWESSGDGWSVTLKTYFNKLNTVLKEKEHSACAWEIVRKEIRENLVQFKKFIDSRVKL
Protein: Myelin protein zero-like protein 2 (Epithelial V-like antigen 1) (O60487)
Organism: Homo sapiens (Human)
Function: Mediates homophilic cell-cell adhesion.
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MYGKSSTRAVLLLLGIQLTALWPIAAVEIYTSRVLEAVNGTDARLKCTFSSFAPVGDALTVTWNFRPLDGGPEQFVFYYHIDPFQPMSGRFKDRVSWDGNPERYDASILLWKLQFDDNGTYTCQVKNPPDVDGVIGEIRLSVVHTVRFSEIHFLALAIGSACALMIIIVIVVVLFQHYRKKRWAERAHKVVEIKSKEEERLNQEKKVSVYLEDTD
Protein: Tripartite motif containing 16 (K7ENN8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
ANGIKAHLEYRSAEMEKSKQELERMAAISNTVQFLEEYCKFKNTEDITFPSVYVGLKDKLSGIRKVITESTVHLIQLLENYKKKLQEFSKEEEYDIRTQVSAVVQRKYWTSKPEPSTREQFLQYAYDITFDPDTAHKYLRLQEENRKVTNTTPWEHPYPDLPSRFLHWRQVLSQQSLYLHRYYFEVEIFGAGTYVGLTCKGIDRKGEERNSCISGNNFSWSLQWNGKEFTAW