wanglab/gogpt-training-data huggingface dataset:
Protein: Uncharacterized protein F31E3.4 (P53015)
Organism: Caenorhabditis elegans
Interaction partners:
- PAN2-PAN3 deadenylation complex subunit PAN3
- Target of EGR1 protein 1
- CCR4-NOT transcription complex subunit 7
- poly
- Endonuclease/exonuclease/phosphatase domain-containing protein
- CCR4-NOT transcription complex subunit let-711
- 3'-5' exoribonuclease parn-1
- Polyadenylate-binding protein
- Polyadenylate-binding protein
- Proliferating cell nuclear antigen
Sequence:
MASATTNQGNEWRFVAPININTTTENTVSCVKFDPHEDLFWIGSSTGKVTSLLPTNHFTRYSAFVVSNISGVHSLEPTESLIFTLSDTMLRATTRQGIPVAKFTSPSMTKMAASCHMPGTSTFIMGGFQEKLIHYDFVKEKEIRTTELKASENAIIIRYNGTNTFTADTRGNVFVKNSKNCETIHTLDCHQDQVLDFDVQGNKLITCGVSMNRLKNMDQFIKVYDLRMYKALSPIGMPYLPQFARFMPSYCERVCVTYQTMYNQPGQTATWSNHPAGVKMFDLNSNGNSAEFPIETSLISAFDFSSNKNFIAVGNHCGIVNVFADRDQPQVNENSKETVFAAPPVQPPLSFAIDDTTQTFGSIPLGFSQEPLVSDWPTELTQIVYRRRKPPTEQTNVKSIHYLSQIKNPRINSKLKRHNIVPYFFEQEELIEASNDHGSKEEAPQEMKRIKVSKLYKKRPLIVNQVPARRGNSQDETQETYTWNIIRHVTMQSTHGMNLVANTLVQVAYSLSPIRSIVLRHICTEDSCITCELHFLFTAFSSKIGDNSGMLTNNLAWALARNGVSLKAGGVLSATQQIIKTVIDDVARTDASGSICSKFDRHLRCIRCRGLQQQESVTDHLLKLNYAPVYQASLCQLIEKSLHIGDDSGEIECEDCKQMSRMECKRKVRELSPVLLIDTNASSNGFVEFWRRQLSLFERKPGGNRSSALGTVPESPSEKKNCRFGTDCRNKKTCKFVHGLVDWPAEQTKLLEDVDLPEWAHYIPSRIAAQLCEGIVRLSDVSDLPDYDEPSAVIYELDAMIHAVGNGENDVNWTHPVTLLRESPVISSSWTLINEQLVSRLHDHEARHIDGRWKLPALLAYKKKNFDVKTSEDIISNDLFLAEENLASNGMTSLAVQSLEELPKEKELVGLDAEFIKIKTDLLEFDGKTVQMRAVGRASCVDSTGERIIFDDHVKLTDDVEVVDYLTKFSGIVKADLCPTTSEKYLTTHKRLLLRMHVLIQRGVTFVGHALHNDFTVLNVHVAESQIIDTVTLMRLGTQRMLSLQFLVKEILGETIQMEAHDSVVDARYALKLYRKYLEIKEQGLLGSEMRRIYTILPCPSPNQTSSPLVVSTTRKTPEDTNPADAAPKSV
Protein: Membrane protein (M protein) (E1 glycoprotein) (Matrix glycoprotein) (Membrane glycoprotein) (K9N7A1)
Organism: Middle East respiratory syndrome-related coronavirus (isolate United Kingdom/H123990006/2012) (MERS-CoV) (Betacoronavirus England 1)
Function: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins.
Subcellular location: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04202}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04202}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04202, ECO:0000269|PubMed:24318862}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04202}. Note=Largely embedded in the lipid bilayer. {ECO:0000255|HAMAP-Rule:MF_04202}.
Interaction partners:
Sequence:
MSNMTQLTEAQIIAIIKDWNFAWSLIFLLITIVLQYGYPSRSMTVYVFKMFVLWLLWPSSMALSIFSAVYPIDLASQIISGIVAAVSAMMWISYFVQSIRLFMRTGSWWSFNPETNCLLNVPFGGTTVVRPLVEDSTSVTAVVTNGHLKMAGMHFGACDYDRLPNEVTVAKPNVLIALKMVKRQSYGTNSGVAIYHRYKAGNYRSPPITADIELALLRA
Protein: Transcriptional repressor NF-X1 (m-Nfx.1) (EC 2.3.2.-) (Nuclear transcription factor, X box-binding protein 1) (B1AY10)
Organism: Mus musculus (Mouse)
Function: Binds to the X-box motif of MHC class II genes and represses their expression. May play an important role in regulating the duration of an inflammatory response by limiting the period in which MHC class II molecules are induced by interferon-gamma. Together with PABPC1 or PABPC4, acts as a coactivator for TERT expression. Mediates E2-dependent ubiquitination.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Ubiquitin-protein ligase E3A
- Paired amphipathic helix protein Sin3a
- Presenilin-1
Sequence:
MAEAPPVSGTFKFNTDAAEFIPQERKTSGLNCGTQRRLDSSRIGRRNYSSSPPCHLPRHIPYEDISAVHQHSYASGSKPKSPQGFFQSSNKSLKNHGLQNQPWQKARNEKHQNRNKKAQGLSEQTSDTSSLESVARSESGTNPREHSPSESEKEVVIADPRGAKPKKAAQLTYNYGRGPKAKGRLRSEWGNRMSPKSEDENTRPVAISHTDSSDASCRKPVVDPCVCRRNEQRRYPQKRPPWEVEGARPRPGRNPPKQESQRHINAGPKTNMSPIPKDNLRERPTKSACDTGNLAVVSKSSRRVNQEKTAVRRQDPQVLSPFPRGKQNHMLKNVETHTGSLIEQLTTEKYECMVCCELVQVTAPVWSCQSCFHVFHLNCIKKWARSPASHADGQSGWRCPACQNVSAHVPNTYTCFCGKVKNPEWSRNEIPHSCGEVCRKKQPGQDCPHSCNLLCHPGPCPPCPAFTTKTCECGRTRHTVRCGQPVSVHCSNACENILNCGQHHCAELCHGGQCQPCRIILNQVCYCGSTSRDVLCGTDVGKSDGFGDFSCLKICGKDLKCGSHTCSQVCHPQPCQPCPRLPHLVRYCPCGQTPLSQLLEHGSNARKTCMDPVPSCGKVCGKPLACGSSDFIHTCEKLCHEGDCGPCSRTSVISCRCSFRTKELPCTSLKSEDATFMCDKRCNKKRLCGRHKCNEICCVDKEHKCPLICGRKLRCGLHRCEEPCHRGNCQTCWQASFDELTCHCGASVIYPPVPCGTRPPECTQTCARIHECDHPVYHSCHSEEKCPPCTFLTQKWCMGKHELRSNIPCHLVDISCGLPCSAMLPCGMHKCQRLCHKGECLVDEACKQPCTTPRGDCGHPCMAPCHPSLPCPVTACKAKVELQCECGRRKEMVICSEASGTYQRIVAISMASKITDMQLGDSVEISKLITKKEVQQARLQCDEECAALERRKRLAEAFDITDDSDPFNVRSSASKFSDSLKDDARKDLKFVSDVEKEMETLVEAVNKGKNNKKSHCFPPMNRDHRRIIHDLAQVYGLESISYDSEPKRNVVVTAVRGKSVCPPTTLTSVIERETQTRPPPPIPHHRHQADKAPGSSTLQKIVKEAVIDYFDVQD
Protein: 3-ketodihydrosphingosine reductase TSC10 (EC 1.1.1.102) (3-dehydrosphinganine reductase) (KDS reductase) (Temperature-sensitive CSG2 suppressor protein 10) (P38342)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the reduction of 3-ketodihydrosphingosine (KDS) to dihydrosphingosine (DHS).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:19141869}; Multi-pass membrane protein {ECO:0000269|PubMed:19141869}.
Interaction partners:
- Serine palmitoyltransferase 2
- Serine palmitoyltransferase 1
- Sphingolipid C4-hydroxylase SUR2
- Ceramide synthase LAC1
- Ceramide synthase LAG1
- Sphingoid long chain base kinase 5
- Sphingoid long chain base kinase 4
- Dihydrosphingosine 1-phosphate phosphatase LCB3
- Alkaline ceramidase YDC1
- Dihydrosphingosine 1-phosphate phosphatase YSR3
Sequence:
MKFTLEDQVVLITGGSQGLGKEFAKKYYNEAENTKIIIVSRSEARLLDTCNEIRIEAHLRRETTDEGQVQHKLAAPLDLEQRLFYYPCDLSCYESVECLFNALRDLDLLPTQTLCCAGGAVPKLFRGLSGHELNLGMDINYKTTLNVAHQIALAEQTKEHHLIIFSSATALYPFVGYSQYAPAKAAIKSLVAILRQELTNFRISCVYPGNFESEGFTVEQLTKPEITKLIEGPSDAIPCKQACDIIAKSLARGDDDVFTDFVGWMIMGMDLGLTAKKSRFVPLQWIFGVLSNILVVPFYMVGCSWYIRKWFRENDGKKAN
Protein: Basigin (O55108)
Organism: Mus musculus (Mouse)
Subcellular location: Basolateral cell membrane {ECO:0000256|ARBA:ARBA00023768}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00023768}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}.
Interaction partners:
Sequence:
RPAPAAAPPPCRLVQEVNSKTQLTCSLNSSGVDIVGHRWMRGGKVLQEDTLPDLHTKYIVDADDRSGEYSCIFLPEPVGRSEINVEGPPRIKVGKKSEHSSEGELAKLVCKSDASYPPITDWFWFKTSDTGEEEAITNSTEANGKYVVVSTPEKSQLTISNLDVNVDPGTYVCNATNAQGTTRETISLRVRSRMAALWPFLGIVAEVLVLVTIIFIYEKRRKPDQTLDEDDPGAAPLKGSGTHMNDKDKNVRQRNAT
Protein: Chemokine-like protein TAFA-5 (Q91WE9)
Organism: Mus musculus (Mouse)
Function: Acts as a chemokine-like protein by regulating cell proliferation and migration through activation of G protein-coupled receptors (GPCRs), such as S1PR2 and FPR2. Stimulates chemotactic migration of macrophages mediated by the MAPK3/ERK1 and AKT1 pathway. Blocks TNFSF11/RANKL-induced osteoclast formation from macrophages by inhibiting up-regulation of osteoclast fusogenic and differentiation genes. Stimulation of macrophage migration and inhibition of osteoclast formation is mediated through the GPCR FPR2. Acts as an adipokine by negatively regulating vascular smooth muscle cell (VSMC) proliferation and migration in response to platelet-derived growth factor stimulation via GPCR S1PR2 and G protein GNA12/GNA13-transmitted RHOA signaling (By similarity). Inhibits injury-induced cell proliferation and neointima formation in the femoral arteries.
Subcellular location: Secreted {ECO:0000269|PubMed:29453251}.
Interaction partners:
Sequence:
MAPSPRTSSRQDATALPSMSSTFWAFMILASLLIAYCSQLAAGTCEIVTLDRDSSQPRRTIARQTARCACRKGQIAGTTRARPACVDARIIKTKQWCDMLPCLEGEGCDLLINRSGWTCTQPGGRIKTTTVS
Protein: Serine/threonine transporter SstT (Na(+)/serine-threonine symporter) (P0AGE4)
Organism: Escherichia coli (strain K12)
Function: Involved in the import of serine and threonine into the cell, with the concomitant import of sodium (symport system).
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01582, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01582}.
Interaction partners:
- Serine transporter SdaC
- D-serine/D-alanine/glycine transporter
- Threonine/serine transporter TdcC
- Dipeptide-binding protein
Sequence:
MTTQRSPGLFRRLAHGSLVKQILVGLVLGILLAWISKPAAEAVGLLGTLFVGALKAVAPILVLMLVMASIANHQHGQKTNIRPILFLYLLGTFSAALAAVVFSFAFPSTLHLSSSAGDISPPSGIVEVMRGLVMSMVSNPIDALLKGNYIGILVWAIGLGFALRHGNETTKNLVNDMSNAVTFMVKLVIRFAPIGIFGLVSSTLATTGFSTLWGYAQLLVVLVGCMLLVALVVNPLLVWWKIRRNPFPLVLLCLRESGVYAFFTRSSAANIPVNMALCEKLNLDRDTYSVSIPLGATINMAGAAITITVLTLAAVNTLGIPVDLPTALLLSVVASLCACGASGVAGGSLLLIPLACNMFGISNDIAMQVVAVGFIIGVLQDSCETALNSSTDVLFTAAACQAEDDRLANSALRN
Protein: Calcium-transporting ATPase (EC 7.2.2.10) (B7CED8)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane {ECO:0000256|RuleBase:RU361146}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU361146}.
Interaction partners:
Sequence:
MPEYGASLEELRALMEYRSAEAKEKIETDYGGTTGLCERLKTDPNNGLPNNEEELERRRNVFGANEIPPHPPKCFLQLVWEALQDVTLVILLVSAIVSLALSFYRPPGEDTAGSDDSEHDAGWIEGVAILISVIVVVLVTALNDYTKERQFRGLQAKIETEHRFFVLRGGQSVQVVVNELVVGDIAQIKYGDLIPSDGIIIQSNDLKMDESSLTGESDQIRKSPEHDPIILSGTHVMEGSGKMLVTAVGVNSQTGIIMTLLGAAKTVAEEERKTAKREERRSRSSVKSHHHHHHHHHREHRDSHHQAQNQNGGDGASGAEEGTAQALLDSKGDEAMANGKAVAAAESDGKKERSVLQAKLTRLAIQIGYAGSFVAGCTVLILIIRFCISRYAIDGKSFSLADFQHFINFLIIGVTVLVVAVPEGLPLAVTLSLAYSVKKMMLDNNLVRHLDACETMGNATAICSDKTGTLTTNRMTVVQSFVNDVHYKDTPKIESLDQNTAKLMMDCISINSSYSSQVIPPKQLGEQATQLGNKTECGMLGFVLALGKSYQEIRDRHPEETIPKVYTFNSVRKSMSTVINLPDGGYRVFSKGASEIVTKRCKYFLGKNGTLTKFSSKDAENLVRDVIEPMASDGLRTICVAYKDYVPSSKKTADNQIAYSSEPDWENEEMIVGDMTAIAVLGIQDPVRPEVPAAITRCQEAGITVRMVTGDNINTARSIATACGILKPGEDFIALEGKEFNARIRDENGEVSQEKLDLIWPKLRVLARAQPSDKYVLVKGIIDSRVTDSREVVAVTGDGTNDGPALKKADVGFAMGIAGTDVAKEASDIILTDDNFTSIVKAVMWGRNVYDSIAKFLQFQLTVNVVAVVVAFVGACAIQDTPLKAVQMLWVNLIMDTLASLALATEMPTEELLKRKPYGRTSPLISRTMCKNILGHAVYQLVILFTLIFYGEVCFNIPSGRWAPLHSPPSKHFTIVFNTFVMMTLFNEINARKIHGERNIFKGLFSNPIYYVIWIATMISQVVIIQFGGRWFSTSALNTTEWLWCLAFGVGTLLWGQIVTSIPTGSLPANMTIGSGEAPTNDPLMPDYEDSDTHEKRSGQILWVRGLTRLQTQIRVVKAFQAGLDRREPSLTGQSAARLREISRQLRLQVDSENRSRSTSRGNIKETNNL
Protein: HCG1811249, isoform CRA_e (Laminin subunit alpha-3) (A0A0A6YYF2)
Organism: Homo sapiens (Human)
Subcellular location: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000256|ARBA:ARBA00004302}.
Interaction partners:
Sequence:
MPPAVRRSACSMGWLWIFGAALGQCLGYSSQQQRVPFLQPPGQSQLQASYVEFRPSQGCSPGYYRDHKGLYTGRCVPCNCNGHSNQCQDGSGICVNCQHNTAGEHCERCQEGYYGNAVHGSCRACPCPHTNSFATGCVVNGGDVRCSCKAGYTGTQCERCAPGYFGNPQKFGGSCQPCSCNSNGQLGSCHPLTGDCINQEPKDSSPAEECDDCDSCVMTLLNDLATMGEQLRLVKSQLQGLSASAGLLEQMRHMETQAKDLRNQLLNYRSAISNHGSKIEGLERELTDLNQEFETLQEKAQVNSRKAQTLNNNVNRATQSAKELDVKIKNVIRNVHILLKQISGTDGEGNNVPSGDFSREWAEAQRMMRELRNRNFGKHLREAEADKRESQLLLNRIRTWQKTHQGENNGLANSIRDSLNEYEAKLSDLRARLQEAAAQAKQANGLNQENERALGAIQRQVKEINSLQSDFTKYLTTADSSLLQTNIALQLMEKSQKEYEKLAASLNEARQELSDKVRELSRSAGKTSLVEEAEKHARSLQELAKQLEEIKRNASGDELVRCAVDAATAYENILNAIKAAEDAANRAASASESALQTVIKEDLPRKAKTLSSNSDKLLNEAKMTQKKLKQEVSPALNNLQQTLNIVTVQKEVIDTNLTTLRDGLHGIQRGDIDAMISSAKSMVRKANDITDEVLDGLNPIQTDVERIKDTYGRTQNEDFKKALTDADNSVNKLTNKLPDLWRKIESINQQLLPLGNISDNMDRIRELIQQARDAASKVAVPMRFNGKSGVEVRLPNDLEDLKGYTSLSLFLQRPNSRENGGTENMFVMYLGNKDASRDYIGMAVVDGQLTCVYNLGDREAELQVDQILTKSETKEAVMDRVKFQRIYQFARLNYTKGATSSKPETPGVYDMDGRNSNTLLNLDPENVVFYVGGYPPDFKLPSRLSFPPYKGCIELDDLNENVLSLYNFKKTFNLNTTEVEPCRRRKEESDKNYFEGTGYARVPTQPHAPIPTFGQTIQTTVDRGLLFFAENGDRFISLNIEDGKLMVRYKLNSELPKERGVGDAINNGRDHSIQIKIGKLQKRMWINVDVQNTIIDGEVFDFSTYYLGGIPIAIRERFNISTPAFRGCMKNLKKTSGVVRLNDTVGVTKKCSEDWKLVRSASFSRGGQLSFTDLGLPPTDHLQASFGFQTFQPSGILLDHQTWTRNLQVTLEDGYIELSTSDSGGPIFKSPQTYMDGLLHYVSVISDNSGLRLLIDDQLLRNSKRLKHISSSRQSLRLGGSNFEGCISNVFVQRLSLSPEVLDLTSNSLKRDVSLGGCSLNKPPFLMLLKGSTRFNKTKTFRINQLLQDTPVASPRSVKVWQDACSPLPKTQANHGALQFGDIPTSHLLFKLPQELLKPRSQFAVDMQTTSSRGLVFHTGTKNSFMALYLSKGRLVFALGTDGKKLRIKSKEKCNDGKWHTVVFGHDGEKGRLVVDGLRAREGSLPGNSTISIRAPVYLGSPPSGKPKSLPTNSFVGCLKNFQLDSKPLYTPSSSFGVSSCLGGPLEKGIYFSEEGGHVVLAHSVLLGPEFKLVFSIRPRSLTGILIHIGSQPGKHLCVYLEAGKVTASMDSGAGGTSTSVTPKQSLCDGQWHSVAVTIKQHILHLELDTDSSYTAGQIPFPPASTQEPLHLGGAPANLTTLRIPVWKSFFGCLRNIHVNHIPVPVTEALEVQGPVSLNGCPDQ
Protein: Response regulator protein TodT (I7CA98)
Organism: Pseudomonas putida (strain DOT-T1E)
Function: Member of the two-component regulatory system TodS/TodT involved in the regulation of toluene degradation. Phosphorylated TodT activates transcription of the tod operon (todXFC1C2BADEGIH). Binds specifically to three boxes in the tod promoter region in a cooperative manner. Boxes-1 and -2 are pseudopalindromes and Box-3 is a half-palindrome.
Subcellular location: Cytoplasm {ECO:0000250}.
Interaction partners:
Sequence:
MPARWGCLFPGKYPCQTGLRHMSDRASVIYILDDDNAVLEALSSLVRSIGLSVECFSSASVFLNDVNRSACGCLILDVRMPEMSGLDVQRQLKELGEQIPIIFISGHGDIPMAVKAIKAGAVDFFTKPFREEELLGAIRAALKLAPQQRSNAPRVSELKENYESLSKREQQVLKFVLRGYLNKQTALELDISEATVKVHRHNIMRKMKVSSIQDLVRVTERLKDSLE
Protein: Cyclin-dependent kinase D-3 (CDKD;3) (EC 2.7.11.22) (EC 2.7.11.23) (CDK-activating kinase 2-At) (CAK2-At) (Q9LMT0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May form a stable complex with cyclin CYCH1-1 that phosphorylates human CDK2 and the C-terminal domain (CTD) of the large subunit of RNA polymerase II.
Subcellular location: Nucleus {ECO:0000269|PubMed:15486101}.
Interaction partners:
- Cyclin-H1-1
- General transcription and DNA repair factor IIH subunit TFB4
- Pentatricopeptide repeat-containing protein At4g30825
- General transcription factor IIH subunit 2
- General transcription and DNA repair factor IIH subunit TFB2
- General transcription and DNA repair factor IIH helicase subunit XPD
- General transcription and DNA repair factor IIH subunit TFB1-1
- General transcription and DNA repair factor IIH subunit TFB1-3
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB1
- General transcription and DNA repair factor IIH helicase/translocase subunit XPB2
Sequence:
MPEQPKKVADRYLKQEVLGQGTYGVVFKATDTKTEQTVAIKKIRLGKQREGVNITALREIKMLKELKHPHIILLIDAFPHKENLHLVFEFMETDLEAVIRDSNIFLSPADIKSYLLMTFKGLAYCHDKWVLHRDMKPNNLLIGVDGQLKLADFGLARIFGSPNRKFTHQVFARWYRAPELLFGAKQYGAAVDVWAVACIFAELLLRRPFLQGNSDIDQLSKIFAAFGTPKADQWPDLTKLPDYVEYQFVPAPSLRSLFPAVSDDALDLLSKMFTYDPKARISIKQALEHRYFTSAPAPTDPAKLPKPVPKQDGKSSYGKHEAITVQSPPRKLRRVMPERGRVDSLKSHVDKDQQAPMSLDFTILAERPPNRPTITSADRSHLKRKLDLEFQ
Protein: Small ribosomal subunit protein mS45 (37S ribosomal protein S35, mitochondrial) (O60096)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Required for mitochondrial protein synthesis. Has a role in mitochondrial integrity and cell respiration.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:18245278}.
Interaction partners:
- Small ribosomal subunit protein uS4m
- Small ribosomal subunit protein bS18m
- Small ribosomal subunit protein uS11m
- Small ribosomal subunit protein uS5m
- Small ribosomal subunit protein mS35
- Small ribosomal subunit protein bS16m
- Small ribosomal subunit protein mS29
- Small ribosomal subunit protein uS7m
- Small ribosomal subunit protein uS12m
- Small ribosomal subunit protein uS15m
Sequence:
MRNSVEFSQLGLKTAFNLSQNKTYTSAVKKQFFSTGAFLSNGGNIDLNKHTQKNIDSKYVACNSRSVTPPNDVASSVSKNTLRHKQRLMMAQWLMSPEVQKAKSSSSGNVGLGPNTNQPFPLNPFFKPPRPISHSLRMKITDEYLQGASIEVLARKFNTSPQRIEALIKLRRINDEFEEKKKPILHSYNEVMEKMLNACTKPEMMQFNDGNDIPLRSNPVSLWKSLPEGETFTPQEAAKILKWPSIEELNMRQNATHFHKTSDEHKDLNEDEELISSSPSEVGKRVFRLIDLSTGNVYRRDTGGDIYVKRKKSTT
Protein: Ubiquitin conjugation factor E4 (EC 2.3.2.-) (Ubiquitin fusion degradation protein 2) (UB fusion protein 2) (Q9HE05)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: E4 ubiquitin chain-elongation enzyme specifically involved in polyubiquitin chain assembly. Binds to cdc48 and elongates mono- and diubiquitinated ERAD substrates presented by the ufd1-npl4-cdc48 (UNC) AAA ATPase complex to a chain length of 4 to 6 ubiquitin moieties. Delivers these polyubiquitinated substrates to downstream ERAD components, which target them to the proteasome. Enhances ubiquitination at 'Lys-48', but not at 'Lys-29' of the Ub moiety.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10759889}. Nucleus {ECO:0000269|PubMed:10759889}.
Interaction partners:
- Ubiquitin fusion degradation protein 1
- Cell division cycle protein 48
- Nuclear protein localization protein 4
- UV excision repair protein rhp23
- Putative ubiquitin thioesterase otu1
- Deubiquitination-protection protein dph1
- UBX domain-containing protein 3
- ATPase family gene 2 protein
- UBX domain-containing protein 10
- Uncharacterized J domain-containing protein C17A3.05c
Sequence:
MSDLEKIRLKRLAKLQQTNSEANSSKEPKESNIAPEPKKPDLKKRFIGSKATTSNSEQKEISPPVTSGAPKHRLFSKDEWMHFITCQALNITLSETDSSKYYLEGFKKDLEEEGSPLLFNENNVDSALLSRLSTTGNNTFSYLLQSWSFLYQYKKRLPKDENQDFKIHYLSLLKSLLVSYAGIVVMLPDTFNSETIDLAEVLIGAEGIPLEFLSEFVQRFEHENLDELFIPVLESLSLKIGLMNVDTVQMNVMQIILQLVSLKPIALLLPKLPSWNPTNNAGEIEYKTFLGRISSLSVFTQDVASRYFSNSTERSAQNISSSISSLKLTMSTYQDVLFQIFNTLIRTSTSLRESVLDFFAMVVNANHKRQSIQVNHFDITSDACMLNFSHVLSRLSEPFLDIGCSKIDRVQVEYFRRNPRVDIKEETKLNADQKASESFYSKPAEGSNNFISDIFFLNLAFHHYGVNATFKALEQLVQSIRDSEKLKERLETEQQNMSGSFQATRLTAQLSRLDQRLDLDRSFVHCYEIMLTQTSDTSRSFSFLNFVAIWLSRLADGQSSTYPKMPLSLPFNENAPEAFKCLPEYFIETITDYMLSLFKTSSSTLTLHSLEPLCEFCVSFLTQANYIKNPYLRAKLAEILYFGVQTHVGRSELLLDVVRTSKVATRWLLPALMAFYIEIESTGQSTQFYDKFNIRFYICEVFRTIWKQPAYFGKLEQEQKTNLPFFVKFVALMLNDATYLLDEALLKLTEIHNLQSLLADAISNSNSNQNVQESQSNLAAAERQASTYCQLGNETIFMLKLFTSSIPKAFCAVEIVDRLAAMLNYNLQALCGPKCSNLKVEDPTKYHFNAKTLLSIIFDVYLNLCNEPAFVEAVAHDGRSYSKEIFERATSIMTKHNLKSSFDIEAIKEFVNRVEAFRLQEATEEEDMGDIPDYFLDPLMFTIMKDPVVLPRSGISIDRSTIKAHLLSDATDPFNRTPLTLDDVTPNDTLREEINTFLKSKRNKHSRNSE
Protein: Structure-specific endonuclease subunit slx1 (EC 3.1.-.-) (Q9P7M3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the slx1-slx4 structure-specific endonuclease that resolves DNA secondary structures generated during DNA repair and recombination. Has endonuclease activity towards branched DNA substrates, introducing single-strand cuts in duplex DNA close to junctions with ss-DNA. Has a preference for stem-loop (SL) and splayed arm Y structures. Introduces a single-strand cut in duplex DNA on the 3' side of a double-strand/single-strand junction with respect to the single-strand moving 3' to 5' away from the junction. Plays a critical role in maintaining the integrity of the ribosomal DNA (rDNA) loci, where it has a role in re-starting stalled replication forks. The complex initiates homologous recombination (HR) events, used to maintain rDNA copy number, in the rDNA repeats that are processed by a mechanism that requires rad22, but not rhp51. It is also required for suppression of methyl methanesulfonate (MMS) and UV-C irradiation hypersensitivity of the structural maintenance of chromosome (SMC) protein mutant, smc6-74, by overexpression of brc1. Has Holliday junction resolvase activity in vitro.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:16467377}. Note=Associates with chromatin at rDNA repeat protrusions. {ECO:0000269|PubMed:14528010, ECO:0000269|PubMed:16467377}.
Interaction partners:
- Structure-specific endonuclease subunit slx4
- Crossover junction endonuclease mus81
- Crossover junction endonuclease eme1
- RecQ-mediated genome instability protein 1
- Exodeoxyribonuclease 1
- Probable asparagine--tRNA ligase, cytoplasmic
- DNA topoisomerase 3
- ATP-dependent DNA helicase hus2/rqh1
- DNA mismatch repair protein msh3
- DNA repair protein rhp51
Sequence:
MDLCNFYCCYLLKSNRTQSSGAVYIGSTPDPPRRLRQHNGEIVGGASKTKHGRPWSISCLVYGFPNKVSALKFEWNWQNLGISRYTKDCDFRSKKQKTIMYCLKGLKHLVDSDTWRRWPLNITFLNKTAFSKWNQLGKTYGNINVYFDEEWLNGFHEKVIQKTYDHKLCLRKTISEPVKCNLCYECIESDELRANCPFTDCNSINHLTCLASSFLTEECQVLPIEGMCTKCKRVLRWREFLSTVFTTSLETDERDFESENRIEIIDLELEK
Protein: Serine/threonine-protein kinase US3 (EC 2.7.11.1) (P04413)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Function: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and inhibition of host immune response. Phosphorylates UL31 and UL34, two critical regulators of capsid budding from nucleus to endoplasmic reticulum, thereby facilitating virion egress. Modulates and redistributes host components of the nuclear envelope, including LMNA, emerin/EMD and the nuclear matrix protein MATR3. In turn, facilitates nuclear pore impairment and capsid release through impaired nuclear envelope. Phosphorylates envelope glycoprotein B (gB), probably to direct it to the cell surface. Promotes virus intracellular spread by restructuring host cell cytoskeleton. Blocks host apoptosis to extend cell survival and allow efficient viral replication. Promotes viral gene expression by phosphorylating host HDAC2 to reduce viral genome silencing. Strongly inhibits TCR-activated signal transduction in T-cells by reducing the ubiquitination of LAT and TRAF6, leading to a suboptimal activation of LAT. Subverts host antiviral innate immunity by inhibiting type I interferon production through hyperphosphorylation of beta-catenin/CTNNB1. In addition, phosphorylates the RNA sensor RIGI and the transcription factor IRF3 to prevent the RLR-mediated antiviral signaling pathway. Hyperphosphorylates host RELA and thereby dampens NF-kappa-B signaling.
Subcellular location: Host cytoplasm {ECO:0000269|PubMed:24807716}. Host nucleus {ECO:0000250}.
Interaction partners:
Sequence:
MACRKFCRVYGGQGRRKEEAVPPETKPSRVFPHGPFYTPAEDACLDSPPPETPKPSHTTPPSEAERLCHLQEILAQMYGNQDYPIEDDPSADAADDVDEDAPDDVAYPEEYAEELFLPGDATGPLIGANDHIPPPCGASPPGIRRRSRDEIGATGFTAEELDAMDREAARAISRGGKPPSTMAKLVTGMGFTIHGALTPGSEGCVFDSSHPDYPQRVIVKAGWYTSTSHEARLLRRLDHPAILPLLDLHVVSGVTCLVLPKYQADLYTYLSRRLNPLGRPQIAAVSRQLLSAVDYIHRQGIIHRDIKTENIFINTPEDICLGDFGAACFVQGSRSSPFPYGIAGTIDTNAPEVLAGDPYTTTVDIWSAGLVIFETAVHNASLFSAPRGPKRGPCDSQITRIIRQAQVHVDEFSPHPESRLTSRYRSRAAGNNRPPYTRPAWTRYYKMDIDVEYLVCKALTFDGALRPSAAELLCLPLFQQK
Protein: peptide-methionine (S)-S-oxide reductase (EC 1.8.4.11) (Peptide-methionine (S)-S-oxide reductase) (O02089)
Organism: Caenorhabditis elegans
Interaction partners:
- Probable methionine-R-sulfoxide reductase B
- Probable thioredoxin-2
- Thioredoxin domain-containing protein
- Probable glutathione reductase 2
- 10 kDa heat shock protein, mitochondrial
- Putative dihydrofolate reductase
- Methionine synthase reductase
- sulfite oxidase
- ABC transporter domain-containing protein
Sequence:
MAYLERAYFGLQCFWGESAWAKLKGVVVTRVGYAGGKQPNPTYKNIKDHTEITEITFDPKVIEYSKLTNFFWKHHNPAERRKKQYQSAILYVNDDQKKVAEETLKVAKDKHGDIETYIEPLDKFYQAEDYHQKYWFRQKKILFDELSLLDTQVAEGELATKLNAYCAGFQDFHDLERLAKEYGLKDSFVNKVKDYALSGGDPRNCHA
Protein: Beta-basrubin (P83187)
Organism: Basella alba (Malabar spinach) (Basella rubra)
Function: Possesses antifungal activity against B.cinerea, M.arachidicola and F.oxysporum but not C.comatus and R.solani. Inhibits HIV-1 reverse transcriptase and cell-free translation.
Interaction partners:
Sequence:
KIMAKPSKFYEQLRGR