wanglab/gogpt-training-data huggingface dataset:
Protein: Glyceraldehyde dehydrogenase large chain (EC 1.2.99.8) (Glyceraldehyde dehydrogenase subunit A) (Glyceraldehyde dehydrogenase subunit alpha) (Q4J6M3)
Organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Function: Component of the glyceraldehyde dehydrogenase which is involved the nonphosphorylated Entner-Doudoroff pathway. Catalyzes the oxidation of D-glyceraldehyde to yield glycerate. When the artificial electron acceptor 2,6-dichlorophenol-indophenol (Cl2Ind) is used, the enzyme shows a broad substrate range (glyceraldehyde-3-phosphate, formaldehyde, acetaldehyde, propionaldehyde and isobutyraldehyde), but is most active with D-glyceraldehyde. It is not known which acceptor is utilized in vivo.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10095793}.
Interaction partners:
- Glyceraldehyde dehydrogenase small chain
- Glyceraldehyde dehydrogenase medium chain
- Carbon monoxide dehydrogenase small chain
- MOFRL family protein
- Carbon monoxide dehydrogenase medium chain
- 2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase
- Carbon monoxide dehydrogenase
- Conserved Archaeal protein
Sequence:
MTYTGKSIKRLNDDKFITGRSNYIDDIKIPSLYAGFVRSPYPHAIIKRIDATDALKVNGIVAVFSGKDINPMLKGGVGVLSAYVNPSLFRFKERKAFPEDNKVKYVGEPVAIVIGQDKYAVRDAIDRVNVEYEQLKPVIKMEDAEKDEVIVHDELKTNVSYKIPFKAGDIEKAFSQADKVVKVEAINERLIPNPMEPRGILSVYDGNSLSVWYSTQVPHFARSEFARIFGIPETKIRVAMPDVGGAFGSKVHIMAEELAVIASSILLRRPVRWTATRSEEMLASEARSNVFTGEVAVKKDGTVLGIKGKLLLDLGAYLTLTAGIQPTIIPVMIPGPYKVRDLEIESTAVYTTTPPITMYRGASRPEATYIIERIMSTVADELGLDDVTIRERNLIDQLPYTNPFGLRYDTGDYIRVFKDGVAKLEYNELRKWAQQERSKGHRVGVGLAFYLEICSFGPWEYGEIKVDNKGNVLVITGTTPHGQGTETAIAQIVADALQIPIEKIRVVWGDTDIVEGSFGTYGSRSLTIGGSAALKVAERVLDKMKRAAASYFNADVQEIRYENEEFSVKNDPSKKASWDEIASLATTKEPIVEKIYYENDVTFPYGVHVAVVEVDDLGMARVVEYRAYDDIGKVINPALAEAQIHGGGVQGVGQALYEKAIINENGQLSVTYADYYVPTAVEAPRFISYFADKSHPSNYPTGTKGVGEAALIVGPAAIIRAIEDAVGARFTKTPTPPEEIYKAIMSKK
Protein: Ras-related protein Rab-20 (Q9NX57)
Organism: Homo sapiens (Human)
Function: Plays a role in apical endocytosis/recycling. Plays a role in the maturation and acidification of phagosomes that engulf pathogens, such as S.aureus and M.tuberculosis. Plays a role in the fusion of phagosomes with lysosomes.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:16613320}. Cytoplasmic vesicle, phagosome {ECO:0000269|PubMed:21255211}. Cytoplasmic vesicle, phagosome membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Note=Highly enriched on apical endocytic structures in polarized epithelial cells of kidney proximal tubules (By similarity). Recruited to phagosomes containing S.aureus or M.tuberculosis (PubMed:21255211). {ECO:0000250|UniProtKB:P35295, ECO:0000269|PubMed:21255211}.
Interaction partners:
- Rab5 GDP/GTP exchange factor
Sequence:
MRKPDSKIVLLGDMNVGKTSLLQRYMERRFPDTVSTVGGAFYLKQWRSYNISIWDTAGREQFHGLGSMYCRGAAAIILTYDVNHRQSLVELEDRFLGLTDTASKDCLFAIVGNKVDLTEEGALAGQEKEECSPNMDAGDRVSPRAPKQVQLEDAVALYKKILKYKMLDEQDVPAAEQMCFETSAKTGYNVDLLFETLFDLVVPMILQQRAERPSHTVDISSHKPPKRTRSGCCA
Protein: Uncharacterized protein (O02141)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Glycerophosphocholine cholinephosphodiesterase
- Histidine-rich glycoprotein-like
- F-box protein dre-1
Sequence:
MSTIAAGRFAKDDVDQDTKWWKEYPSKHYIERARPQNYYDEFVQNAWSKSKRLARAASFTNLTYIKDKDMDFPIRKSDSVSTLAPSLALPQYCREAQRIVHTVPVYKPTVHDWYNKSYSDARWRDTHREINKPYKPLDTYISPASSHVPYYSFQTKRIFFDEKARQLAPYLKESQRYMDRYVSSRLKADDYANRFAYTAYEWRKPQDHSFNREFMTTQGVFVATPTGIPHQHYDKFGMRRLYKRTGRFFF
Protein: Dihydropyrimidine dehydrogenase [NADP(+)] (DHPDHase) (DPD) (EC 1.3.1.2) (Dihydrothymine dehydrogenase) (Dihydrouracil dehydrogenase) (Q95U76)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MGVRQRRTPQAEANPLSQKIALVGGGPASLSCATFLARLGYRDVTIYERRSYLGGLSAAEIPQYRLPIDAVNFEIDLVRDLGVRIETGRSLGTKDLTIQGLLSTGHDAVFVGIGLPEPKLNPIFAGLQPSNGFYTSKNFLPLVSDGSKPGLCACKAAAGLPKLHGNVIVLGAGDTAFDCATSALRCGARRVFVVFRKGSSGIRAVPEEVELARDERCELLPYLSPRKVIVKDGLITAMEFCRTEQNENDEWVEDEEQTQRLKANFVISAFGSGLEDQDVKAALAPLQFRGELPVVDRVTMQSSVKQVFLGGDLAGVANTTVESVNDGKVAAWSIHCQLQGLPLDTPAALPLFYTDIDAVDISVEMCGIRFENPFGLASAPPTTSTAMIRRAFEQGWGFVVTKTFGLDKDLVTNVSPRIVRGTTSGYKYGPQQGCFLNIELISEKRAEYWLKSIGELKRDFPEKIVIASIMCSFNEEDWTELAIKAEQSGADALELNLSCPHGMGERGMGLACGQDPELVEQISRWVRKAVKLPFFIKLTPNITDIVSIAAAAKRGGADGGSAINTVQGLMGLKADSTAWPAIGKEQRTTYGGVSGNATRPMALKAISDIANRVPGFPILGIGGIDSGEVALQFIHAGATVLQICSSVQNQDFTVIEDYCTALKALLYLKANPPPVDGPFWDGQSPPTPVHQKGKPVVRLTGEGKATLGFFGPYQRQRDIKMAELRSQKGALWDAEQVKATPPASNGAPNPAPRIKDVIGAALDKIGSYNKLDNKQQKVALIDDDMCINCGKCYMTCADSGYQAIEFDKDTHIPHVNDDCTGCTLCVSVCPIIDCITMVPKKIPHVIKRGVEEKIFYTHALSQCQ
Protein: Protein mms22 (Protein mus7) (O14207)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Involved in protection against replication-dependent DNA damage. May act by restoring active replication forks, repairing unusual DNA structures, and/or preventing aberrant DNA rearrangement at arrested replication forks.
Subcellular location: Nucleus {ECO:0000269|PubMed:17660542}.
Interaction partners:
- Uncharacterized protein C3H8.05c
- Uncharacterized leucine-rich repeat-containing protein C926.06c
- DNA repair and recombination protein rad22
Sequence:
MNSFLLLDHVSDSQDSGSEWSNTHGSLISQRGNEYDGITPATKEKNQNKLEILNNETTIGSTKSSVSSLPELNRNVSFEKSDQNLAETKREEENKRTEVFKKDAEHEAVVVKRDFRPRRPEQTRPYTYDFLRHQIEFKRIGLVPITVPHGFSSDRSITSKSSHKPVNVIVRNRASSRKPPLTSTHRFRRYGAVISDSDDDESNTEQDHSKESNLNTADNDLALSSTIEGKKTSTSKEALESESLLSDSDQSMTNISSNSTVSDLNLKTLKKRLRGVLPPSFLTLQEKKKLENRGVKKKTSLHKSVIEGEKIKGVARRKLHPRSTAKLSSELGNEISDSDNSISTPTPTDDSRFDTSEFLDSISRDNGWLKEDVVDQLWLPKRSLSALKKSSSLTSENPFQLNVAANAVSTIPVYRTTKTKMKKNRFKYVEVEKLPDLILESYGKKAPKFLRVFARSSSHIPKMIRRKRQMDSKKYFSFDKESDRQVIDQVLSDWYSGKHELVQQSHSYKKPSDSKSVGGNIFSVNSKKHSVNINAKTAANNGLSHLQNFSEELLKKRKLFSSLFSNNVSYKKSKKLKRTHTVHDKCQKVAKLDHYIRDNIELNSKEREHDCYEGTLAVPQVNTEIRKSSRKQKAQRFIRDDFDTVFFQSSSNPNYFTDVNPFWNIGIWSTTFNVITFRPGLSLPNNSFIKTQGLNSILQLDIVTHPFKSVYAFSCLFNIQDDVFKTFEKLKDTFETVLENLPYFTNSETVDLYNLLSFCSAFILHSQVSMGLVNLASSFLETYALVNDRVSSISGLNRSQLVEKIAVLFQTFQVVFYCEFELGNQQNINKVSWLASDLISKLLSAGQSGLLECYRNLRIQASDTTVIDTLFLESWSILNHILFHVYKKKYALWEQVNSFFDLQKKELSILEMEKIWYVIMTLNPVFQIGLNGTTHSPGNNSFWPLIIRVSESAFKMHKDGHNVKVVERYLRTVFLRIHFLISEWRWEDVAQILFLIFDFFSHRKFNDLSSEISEDTPTDFPDFVKSLDRPPNLHVTALDTCFVIYLKVILISISRLRQVDENTNSIKRIVSRLQPLHSRQYTRESPFSIKDFMSLEHTHTLLICLYWAAPENCRPSLNRIRDIVIVDNSHLKARLISLKAWLHLMKYVIKEGTDYELAQGMEWFNSILKVTFDEYLALFSNGTSVGEMQLAEYSKHQLENALIVAFHSLQDLIPNSSVYISRINVLVTEQSCRRILKDSHFFPPRVTLECILFLKKFLQYQSNTEPPKVTVVGSTSHDSQDAYFDSDVLDDNTLILEQEKFERKYEVAQILRTFVSPFLYQTISYLVGNDEDKENYIRILLLPLMECMAICASFAVEAKINDWSYYIDFGSESWERIRNTPLKRSLSTTFYSFLISYNDSFIKKHEEKVLTVWFESLGALDEDHAAQFTILLLQKNLKNPILLNLPISVKIEEISINYFKSVHLNLLTAVFCNMAKLYADAKTNGFASSQYLQSLFIHYLSSLLSSMQHSYETNGHSSDTHSLFVINSQRVVGDILQYCSQFANDRNLPALRYFMDSTKFPQPPERLEYTALRLRSYARKTLTNSASQNALFSFLKANFDVALLEQKQTETSNLLRLAMGFHNQNSSSKWDVEISSLRKFCVKELLLSYLGEGSLAAMFYSLLLLEGLSRTYNSFRRIYLQPYIQQLLCEEISVFVADLEKYALLYENKRPLLSGRIYYLISSFVAISMTNKTSGLPSSLICNLQNFLARIARDFLLELCWNIEGSEFPPPYNTVDCRSKFVKTIQQHCSADWYDNVTNIVHKSRKKKLVLPSQVEQEEEYWSGLMEVTIQIWKHDKGFLEPELDRFLNVICSYAPDMSGLPTKIKCFLDKIGYSWMTEENDFDIVLF
Protein: NADP-dependent alcohol dehydrogenase 6 (EC 1.1.1.2) (NADP-dependent alcohol dehydrogenase VI) (S-nitroso-CoA reductase) (ScorR) (EC 1.6.-.-) (ScADHVI) (Q04894)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: NADP-dependent alcohol dehydrogenase with a broad substrate specificity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- NADP-dependent alcohol dehydrogenase 7
- Magnesium-activated aldehyde dehydrogenase, cytosolic
- Aldehyde dehydrogenase [NAD
- Potassium-activated aldehyde dehydrogenase, mitochondrial
- Pyruvate decarboxylase isozyme 3
- Pyruvate decarboxylase isozyme 1
- Thiamine metabolism regulatory protein THI3
- Aldehyde dehydrogenase [NAD
- Fatty aldehyde dehydrogenase HFD1
- Aldehyde dehydrogenase 5, mitochondrial
Sequence:
MSYPEKFEGIAIQSHEDWKNPKKTKYDPKPFYDHDIDIKIEACGVCGSDIHCAAGHWGNMKMPLVVGHEIVGKVVKLGPKSNSGLKVGQRVGVGAQVFSCLECDRCKNDNEPYCTKFVTTYSQPYEDGYVSQGGYANYVRVHEHFVVPIPENIPSHLAAPLLCGGLTVYSPLVRNGCGPGKKVGIVGLGGIGSMGTLISKAMGAETYVISRSSRKREDAMKMGADHYIATLEEGDWGEKYFDTFDLIVVCASSLTDIDFNIMPKAMKVGGRIVSISIPEQHEMLSLKPYGLKAVSISYSALGSIKELNQLLKLVSEKDIKIWVETLPVGEAGVHEAFERMEKGDVRYRFTLVGYDKEFSD
Protein: Vacuolar segregation protein PEP7 (Carboxypeptidase Y-deficient protein 7) (Protein VAC1) (Vacuolar protein sorting-associated protein 19) (Vacuolar protein-targeting protein 19) (P32609)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for vacuole segregation and vacuole protein sorting. Possibly part of a complex which tethers the vacuole membrane to microtubules, either directly or via kinesin or dynein-like motor proteins. Probably functions in several interorganelle traffic pathways.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:10359603}; Peripheral membrane protein {ECO:0000269|PubMed:10359603}; Cytoplasmic side {ECO:0000269|PubMed:10359603}.
Interaction partners:
- Vacuolar protein sorting-associated protein 45
- Vacuolar protein sorting-associated protein 21
- 1-phosphatidylinositol 3-phosphate 5-kinase FAB1
- Vacuolar membrane protein PEP3
- Syntaxin PEP12
- E3 ubiquitin-protein ligase PEP5
- Vacuolar protein sorting-associated protein 3
- Ypt/Rab-type GTPase YPT7
- Vacuolar protein sorting-associated protein 8
- GTP-binding protein YPT52
Sequence:
MDLENVSCPICLRKFDNLQALNAHLDVEHGFNDNEDSLGSNDSRLVNGKQKKARSVDSSAQKLKRSHWEKFKKGKSCCHTCGRTLNNNIGAINCRKCGKLYCRRHLPNMIKLNLSAQYDPRNGKWYNCCHDCFVTKPGYNDYGEVIDLTPEFFKVRNIKREDKNLRLLQLENRFVRLVDGLITLYNTYSRSIIHNLKMNSEMSKLERTVTPWRDDRSVLFCNICSEPFGLLLRKHHCRLCGMVVCDDANRNCSNEISIGYLMSAASDLPFEYNIQKDDLLHIPISIRLCSHCIDMLFIGRKFNKDVRMPLSGIFAKYDSMQNISKVIDSLLPIFEDSLNSLKVETAKDSENTLDPKNLNDLARLRHKLLNSFNLYNTLTRQLLSVEPQSHLERQLQNSIKIASAAYINEKILPLKSLPAILNPEGHKTNEDGQKAEPEVKKLSQLMIENLTIKEVKELREELMVLKEQSYLIESTIQDYKKQRRLEEIVTLNKNLEELHSRIHTVQSKLGDHGFN
Protein: N-lysine methyltransferase SMYD2-A (EC 2.1.1.-) (Histone methyltransferase SMYD2-A) (EC 2.1.1.354) (SET and MYND domain-containing protein 2A) (Q5BJI7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Protein-lysine N-methyltransferase that methylates both histones and non-histone proteins, including p53/TP53 and RB1. Specifically trimethylates histone H3 'Lys-4' (H3K4me3) in vivo. The activity requires interaction with HSP90alpha. Shows even higher methyltransferase activity on p53/TP53. Monomethylates 'Lys-370' of p53/TP53, leading to decreased DNA-binding activity and subsequent transcriptional regulation activity of p53/TP53. Monomethylates RB1 at 'Lys-860'.
Subcellular location: Cytoplasm, cytosol {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Cellular tumor antigen p53
- Mitogen-activated protein kinase kinase kinase 2
- Ash1
- Actin-histidine N-methyltransferase
- Histone-lysine N-methyltransferase NSD2
- Heat shock protein HSP 90-alpha 1
- Histone H3.2
- Histone H3
- SET domain and mariner transposase fusion protein.
- Histone-lysine N-methyltransferase SETD7
Sequence:
MKKEGIEGTERFLSPGKGRGLKAIKHFKVGDLVFACPAYAYVLTVNERGGRCECCFTRKEGLSKCGKCKQAYYCNVECQRGDWPMHKLECSAMCAYGENWCPSETVRLVARIILKQKHQTERTPSERVLTLRELEAHLDKLDNEKNEMNDTDIAALHHFYSRHLDFPDNAALTELIAQVNCNGFTIEDEELSHLGSALFPDVALMNHSCSPNVIVTYKGTVAEVRAVQEINPEEEIFNSYIDLLYPTEDRIERLKDSYFFNCDCKECTSKSKDEAKMEIRQKLSIPPEEEEIKQMVIYARNVIEEFRRAKHYKTPSELLEICELSMEKMGAIFAETNVYMLHMMYQAMGVCLYMQDWDGAMKYGEKIIHPYSVHYPPYSLNVASMYLKLGRLYLGLEKRTQGVKALKKALAIMDIAHGKDHPYIDEIKKEMEEQT
Protein: DNA helicase/primase complex-associated protein (HEPA) (Primase-associated factor) (P16827)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Component of the helicase/primase complex. Unwinds the DNA at the replication forks and generates single-stranded DNA for both leading and lagging strand synthesis. The primase synthesizes short RNA primers on the lagging strand that the polymerase presumably elongates using dNTPs. The primase-associated factor has no known catalytic activity in the complex and may serve to facilitate the formation of the replisome by directly interacting with the origin-binding protein and the polymerase.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04010}.
Interaction partners:
Sequence:
MTAQPPLHHRHHPYTLFGTSCHLSWYGLLEASVPIVQCLFLDLGGGRAEPRLHTFVVRGDRLPPAEVRAVHRASYAALASAVTTDADERRRGLEQRSAVLARVLLEGSALIRVLARTFTPVQIQTDASGVEILEAAPALGVETAALSNALSLFHVAKLVVIGSYPEVHEPRVVTHTAERVSEEYGTHAHKKLRRGYYAYDLAMSFRVGTHKYVLERDDEAVLARLFEVREVCFLRTCLRLVTPVGFVAVAVTDEQCCLLLQSAWTHLYDVLFRGFAGQPPLRDYLGPDLFETGAARSFFFPGFPPVPVYAVHGLHTLMRETALDAAAEVLSWCGLPDIVGSAGKLEVEPCALSLGVPEDEWQVFGTEAGGGAVRLNATAFRERPAGGDRRWLLPPLPRDDGDGENNVVEVSSSTGGAHPPSDDATFTVHVRDATLHRVLIVDLVERVLAKCVRARDFNPYVRYSHRLHTYAVCEKFIENLRFRSRRAFWQIQSLLGYISEHVTSACASAGLLWVLSRGHREFYVYDGYSGHGPVSAEVCVRTVVDCYWRKLFGGDDPGPTCRVQESAPGVLLVWGDERLVGPFNFFYGNGGAGGSPLHGVVGGFAAGHCGGACCAGCVVTHRHSSGGGGSGVGDADHASGGGLDAAAGSGHNGGSDRVSPSTPPAALGGCCCAAGGDWLSAVGHVLGRLPALLRERVSVSELEAVYREILFRFVARRNDVDFWLLRFQPGENEVRPHAGVIDCAPFHGVWAEQGQIIVQSRDTALAADIGYGVYVDKAFAMLTACVEVWARELLSSSTASTTACSSSSVLSSALPSVTSSSSGTATVSPPSCSSSSATWLEERDEWVRSLAVDAQHAAKRVASEGLRFFRLNA
Protein: Protein aaim-1 (Antibacterial and aids invasion by microsporidia 1 protein) (Q5WRS0)
Organism: Caenorhabditis elegans
Function: Plays a role in promoting resistance to bacterial pathogens such as P.aeruginosa by inhibiting bacterial intestinal colonization.
Subcellular location: Secreted {ECO:0000269|PubMed:34994689}.
Interaction partners:
- Tyrosine-protein phosphatase 4
Sequence:
MRLLFFFSILYTASLCCQLKDFLPCVMQLSAQKVDFNMNPIEVIFNITTEAKLMHTCRTYSRILPCFDQKMVQCGKPSEKTQLERGKRLHSYLCAPFSLQRQKIFLRRSKCIQDVLAEPQSSVCNRNDTVFADKLQSCREMCTRPDCVSKIELSEVSTCTYINIGKKCTAEAAQFFAQMQQVLTNKEYPMQCQYDLRKKPESELKKGLPIESLVAQTTSSTTYVTVHPPALPSVIDGVVTRTSLPIMRRTDPNSKFKPRPTTSQSNGPVIKTVIVDERGAPMNQPTSTQKPKVVHKFLPNPYTTKNPNTLKNDIIRTTRTIIPVVDKHTYVPWNYKVDAVQVSTLTSALAPVKPTETVISSPPVAFNFKLPAEQTSTQPFRVEINWHDDEVKQEPTKAPGVFVSPWYLKTPSHIPPEIEFATPTPLISSPLEAVSPILSQLKSNSLNFTELGNQANNYFSAALSAFAETKKEMAHNDPWRTIIDAVAPTIHKFSPDVIPRIREEINRIQPHQQKN
Protein: Tyrosine-protein phosphatase RLPH2 (EC 3.1.3.48) (Protein RHIZOBIALE-LIKE PHOSPHATASE 2) (Q9SR62)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Protein phosphatase that dephosphorylates specifically tyrosine-phosphorylated peptides; especially active on dual-phosphorylated substrates containing a phosphothreonine-X-phosphotyrosine motif.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:26742850}.
Interaction partners:
- Shewanella-like protein phosphatase 1
- Receptor-like protein 2
- Receptor-like protein 1
- Serine/threonine-protein phosphatase 4 regulatory subunit-like protein
- Probable protein phosphatase 2C 10
- Serine/threonine-protein phosphatase BSU1
- Phosphatidylglycerophosphate phosphatase PTPMT2
- acid phosphatase
Sequence:
MAQKPRTVICVGDIHGYISKLNNLWLNLQSAIDPSDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVFLAGNHDFAFSGFLGLLPRPSDGSDLKDTWKEYSKSEETEGWYTGEGFEDMHLQGRRWAGKIKATFNSVKGMAYKGSIYDAGSTFESYGVPHGSSDLMKAVPESHKKFLTNMVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKGNNVEEQLKLLRAKDTSISKIQHLSGRKNVWDIPQELDDKHTVVVSGHHGKLHIDGMRLIIDEGGGFPDKPVAAIVLPSKKIIRDTDNLSS
Protein: DNA-directed RNA polymerase subunit Rpo10 (EC 2.7.7.6) (DNA-directed RNA polymerase subunit N) (Q980Z8)
Organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus)
Function: DNA-dependent RNA polymerase (RNAP) catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00250}.
Interaction partners:
- DNA-directed RNA polymerase subunit Rpo7
- DNA-directed RNA polymerase subunit Rpo11
- DNA-directed RNA polymerase subunit Rpo3
- DNA-directed RNA polymerase subunit Rpo12
- DNA-directed RNA polymerase subunit Rpo5
- DNA-directed RNA polymerase subunit Rpo6
- DNA-directed RNA polymerase subunit Rpo1C
- DNA-directed RNA polymerase subunit Rpo1N
- DNA-directed RNA polymerase subunit Rpo2
- Transcription factor E
Sequence:
MLIPIRCFTCGSLIADKWQSFITRVNAGENPGKVLDDLGVKRYCCRRMLLSHVDIINEVIHYTRPI
Protein: General amino-acid permease GAP2 (A0A1D8PK89)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Amino-acid permease with broad substrate specificity. GAP2 is the only amino-acid permease with very broad substrate specificity, none of the other GAP permeases is able to transport such a variety of amino acids. GAP2 is also able to transport thialysine, and thus probably also lysine. Functions as a sensor via detection of some amino acids including methionine, leading to a rapid activation of trehalase, a downstream target of PKA.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21764911, ECO:0000269|PubMed:28028545}; Multi-pass membrane protein {ECO:0000255}. Note=Under nitrogen starvation conditions, the permease is no longer in the membrane but seems to be degraded in the vacuole (PubMed:28028545). {ECO:0000269|PubMed:28028545}.
Interaction partners:
Sequence:
MPEKELDYIRSTDAAGSTEKDGGIYIDAFDKQDNAPPKKGFAKFIDGFRRADAEELGIDPNLSEAEKIAIMTANSPLTRSLKNRHLQMIAIGGSIGTGLFVGSGSSLHTGGPAGLLIAYILIGTMIYCTVMSLGELAVTFPVSGAFVTYNSRFIDPSWGFAMAWNYAMQWLVVLPLELVAAAMTVKYWDAKTNSAAFVVIFYVLIVAINFFGVRGYGEAEFIFSAVKVLAVLGFIILGIVLCAGGGPQGGYIGGKNWYIEGAPFPNGAKGVITVFVNAAFAFAGTELCGLAAAETENPRKSLPKACKQVFWRITLFYVICLTLVGLLVPWNDERLLGSSSADASASPFVISIRNAGIKGLPSVMNVVIMIAVLSVGNSSVYGSSRTLAALAASNQAPKIFGYIDKQGRPLVGIIAQLLVGLLCFLAASDKQGEVFNWLLALSGLSSIFTWGSINVCLIRFRRALAAQGRDTGELVFTSQVGVIGAIWGAFLNTVVLCLQFWIAVWPLHSSPSAEAFFSAYLTVPVVIVFYVGHKLWTKNWQVYICAKDIDIDTGRRELDLDLVKQEVAEEKAYIASLPFYRRVYNAWC
Protein: Non-structural protein 2 (NS2) (Non-structural protein 1B) (P04543)
Organism: Human respiratory syncytial virus A (strain A2)
Function: Plays a major role in antagonizing the type I IFN-mediated antiviral response. Acts cooperatively with NS1 to repress activation and nuclear translocation of host IFN-regulatory factor IRF3. Interacts with the host cytoplasmic sensor of viral nucleic acids RIGI and prevents the interaction with its downstream partner MAVS. Together with NS2, participates in the proteasomal degradation of host STAT2, IRF3, IRF7, TBK1 and RIGI through a NS-degradasome involving CUL2 and Elongin-C. The degradasome requires an intact mitochondrial MAVS. Induces host SOCS1 expression. Induces activation of NF-kappa-B. Suppresses premature apoptosis by an NF-kappa-B-dependent, interferon-independent mechanism promoting continued viral replication.
Subcellular location: Host mitochondrion {ECO:0000269|PubMed:21795342, ECO:0000269|PubMed:23877405}. Note=Most NS2 resides in the mitochondria as a heteromer with NS1. {ECO:0000269|PubMed:21795342, ECO:0000269|PubMed:23877405}.
Interaction partners:
Sequence:
MDTTHNDNTPQRLMITDMRPLSLETIITSLTRDIITHKFIYLINHECIVRKLDERQATFTFLVNYEMKLLHKVGSTKYKKYTEYNTKYGTFPMPIFINHDGFLECIGIKPTKHTPIIYKYDLNP
Protein: Leucine-rich repeat protein (LRRP) (Q383W7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSFASFVYLGHCKVMLSVVREYLEQCSQRRVEPYYAFIEHAGNSEIVADIDFAPVMAIRLLAVTLLRSRPRKGGLRLHALVLRYGVNKGEHHPPQQSKRLLPYETLAARRRTEDDIMSPVNRHLLRGLLDGVRMACIAAIRHLTRLELCGLPLSGGSAIVEVTSRLFDLLPHCCSLRVLKLSHSTLTDRLFLQLTTAAMASAFPALKEAYFSECGLTDESARGLHSLITLNRSREQQAMWLSSFRNGNSGSRTVNAPVPRALEALDLSGNRLGDPTLKRLAIAITHDISLRVVDMSRNAVTTAGLVEFLQQGTLGGSGIESLDLSKNLITSNTSYGAEEGFACLCSCPEQLLLTRITGIRQCRTGSPASHGGTRLVPKGPPSPAFDRPTISTSPIPKSQASSRGQSLSAGTVVTGAEQIAAAAPLSRTTRQMSISSAVVIEGSAPETGRSSLSSILPDKERSLAVHNVYTRSSTAHVSAAMSTKPSSCKRCPGGTPSTVHPPASEKTQNQVIPDLIPQGPAPRFQPLLFSSPGGQEQQWYGVPLYITLPFNPLGGLQTAPLAPVKHDVAVGTASLQSSPQRDDADELESGPHTSNGGSESGVGDVFEEKMVEPLNSDRWEMGEWKAKEQRFLEALVVRLENHETSTAELVERNHQLTRESLKGLKEELSQRIREVLEEQRSEQRRLDMRLAAERELQDPEETLTNQLVQLIHTGMKSIHDQMAKPVGTSAAKSDIGMGASGKASCQTTQDYLREVKGFLKGLGW
Protein: Ras-related protein Rab-28 (P51157)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasm, cytoskeleton, cilium basal body. Note=Expressed in the basal body and ciliary rootlet of the photoreceptors. {ECO:0000250}.
Interaction partners:
- Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit delta
Sequence:
MSDSEEESQDRQLKIVVLGDGASGKTSLTTCFAQETFGKQYKQTIGLDFFLRRITLPGNLNVTLQIWDIGGQTIGGKMLDKYIYGAQGVLLVYDITNYQSFENLEDWYTVVKKVSEESETQPLVALVGNKIDLEHMRTIKPEKHLRFCQENGFSSHFVSAKTGDSVFLCFQKVAAEILGIKLNKAEIEQSQRVVKADIVNYNQEPMSRTVNPPRSSMCAVQ
Protein: Myosin-15 (Myosin heavy chain 15) (Q9Y2K3)
Organism: Homo sapiens (Human)
Function: Muscle contraction.
Subcellular location: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils.
Interaction partners:
- Myosin light chain 1/3, skeletal muscle isoform
- Myosin regulatory light chain 12B
- Myosin regulatory light chain 12A
- Myosin regulatory light chain 11
- Myosin regulatory light polypeptide 9
- Myosin light polypeptide 6
- Myosin light chain 3
- Myosin light chain 5
Sequence:
MDLSDLGEAAAFLRRSEAELLLLQATALDGKKKCWIPDGENAYIEAEVKGSEDDGTVIVETADGESLSIKEDKIQQMNPPEFEMIEDMAMLTHLNEASVLHTLKRRYGQWMIYTYSGLFCVTINPYKWLPVYQKEVMAAYKGKRRSEAPPHIFAVANNAFQDMLHNRENQSILFTGESGAGKTVNSKHIIQYFATIAAMIESRKKQGALEDQIMQANTILEAFGNAKTLRNDNSSRFGKFIRMHFGARGMLSSVDIDIYLLEKSRVIFQQAGERNYHIFYQILSGQKELHDLLLVSANPSDFHFCSCGAVTVESLDDAEELLATEQAMDILGFLPDEKYGCYKLTGAIMHFGNMKFKQKPREEQLEADGTENADKAAFLMGINSSELVKCLIHPRIKVGNEYVTRGQTIEQVTCAVGALSKSMYERMFKWLVARINRALDAKLSRQFFIGILDITGFEILEYNSLEQLCINFTNEKLQQFFNWHMFVLEQEEYKKESIEWVSIGFGLDLQACIDLIEKPMGILSILEEECMFPKATDLTFKTKLFDNHFGKSVHLQKPKPDKKKFEAHFELVHYAGVVPYNISGWLEKNKDLLNETVVAVFQKSSNRLLASLFENYMSTDSAIPFGEKKRKKGASFQTVASLHKENLNKLMTNLKSTAPHFVRCINPNVNKIPGILDPYLVLQQLRCNGVLEGTRICREGFPNRLQYADFKQRYCILNPRTFPKSKFVSSRKAAEELLGSLEIDHTQYRFGITKVFFKAGFLGQLEAIRDERLSKVFTLFQARAQGKLMRIKFQKILEERDALILIQWNIRAFMAVKNWPWMRLFFKIKPLVKSSEVGEEVAGLKEECAQLQKALEKSEFQREELKAKQVSLTQEKNDLILQLQAEQETLANVEEQCEWLIKSKIQLEARVKELSERVEEEEEINSELTARGRKLEDECFELKKEIDDLETMLVKSEKEKRTTEHKVKNLTEEVEFLNEDISKLNRAAKVVQEAHQQTLDDLHMEEEKLSSLSKANLKLEQQVDELEGALEQERKARMNCERELHKLEGNLKLNRESMENLESSQRHLAEELRKKELELSQMNSKVENEKGLVAQLQKTVKELQTQIKDLKEKLEAERTTRAKMERERADLTQDLADLNERLEEVGGSSLAQLEITKKQETKFQKLHRDMEEATLHFETTSASLKKRHADSLAELEGQVENLQQVKQKLEKDKSDLQLEVDDLLTRVEQMTRAKANAEKLCTLYEERLHEATAKLDKVTQLANDLAAQKTKLWSESGEFLRRLEEKEALINQLSREKSNFTRQIEDLRGQLEKETKSQSALAHALQKAQRDCDLLREQYEEEQEVKAELHRTLSKVNAEMVQWRMKYENNVIQRTEDLEDAKKELAIRLQEAAEAMGVANARNASLERARHQLQLELGDALSDLGKVRSAAARLDQKQLQSGKALADWKQKHEESQALLDASQKEVQALSTELLKLKNTYEESIVGQETLRRENKNLQEEISNLTNQVREGTKNLTEMEKVKKLIEEEKTEVQVTLEETEGALERNESKILHFQLELLEAKAELERKLSEKDEEIENFRRKQQCTIDSLQSSLDSEAKSRIEVTRLKKKMEEDLNEMELQLSCANRQVSEATKSLGQLQIQIKDLQMQLDDSTQLNSDLKEQVAVAERRNSLLQSELEDLRSLQEQTERGRRLSEEELLEATERINLFYTQNTSLLSQKKKLEADVARMQKEAEEVVQECQNAEEKAKKAAIEAANLSEELKKKQDTIAHLERTRENMEQTITDLQKRLAEAEQMALMGSRKQIQKLESRVRELEGELEGEIRRSAEAQRGARRLERCIKELTYQAEEDKKNLSRMQTQMDKLQLKVQNYKQQVEVAETQANQYLSKYKKQQHELNEVKERAEVAESQVNKLKIKAREFGKKVQEE
Protein: Tumor susceptibility gene 101 protein (O76258)
Organism: Caenorhabditis elegans
Subcellular location: Endosome {ECO:0000256|ARBA:ARBA00004177}.
Interaction partners:
- VPS37 C-terminal domain-containing protein
- Vacuolar protein sorting-associated protein 28 homolog
- Hepatocyte growth factor-regulated tyrosine kinase substrate
- Multivesicular body subunit 12A
- Signal transducing adapter molecule 1
- Vacuolar protein-sorting-associated protein 36
- Vacuolar protein-sorting-associated protein 25
- Charged multivesicular body protein 3
- Charged multivesicular body protein 6
- MAM domain-containing protein
Sequence:
MSAHQVQQCLQRAGGKYADSAKKDIIGALSQFKDLSPGTDTFMFPDGKRRTAFRLKGTIPVYYKGACYNIPVTVYLWDTHPYYAPICYVNPTSTMVIKESEHVNKEGKVFLPYLNEWRFPGYDLSGLLQVMAMVFQEKCPVFARSAANSATNASATNPSAGSSASSTPTPYPSSQPTMPTPYPTGSGAAPYPPSSTPYPSAGAMGYNPYMNVPQSTPYPMGASGASPYPSASSNPAPPPPRPPPVTAQTSVSSSSGGTIQADTIRASVMSAVEEKIRAKLRERMGTNSAEMASIRTTSDELREGQQKLKRMLEELETQRSSLQTACEIYTAKKAELAKALSDAGGTDAPPIDEAIDAAFPLHRQIVLNYAKDLTCDDVIYSLGQSLKKRQITLAEYLRHVRDVSREQFIYRATMQKCRRTAGLPI