wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleoporin NUP159 (Nuclear pore protein NUP159) (P40477)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Active directional transport is assured by both, a Phe-Gly (FG) repeat affinity gradient for these transport factors across the NPC and a transport cofactor concentration gradient across the nuclear envelope (GSP1 and GSP2 GTPases associated predominantly with GTP in the nucleus, with GDP in the cytoplasm). NUP159 plays an important role in several nuclear export pathways including poly(A)+ RNA, pre-ribosome, and protein export.
Subcellular location: Nucleus, nuclear pore complex {ECO:0000269|PubMed:10684247, ECO:0000269|PubMed:17546040, ECO:0000269|PubMed:23223634, ECO:0000269|PubMed:25646085}. Nucleus membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Nucleoporin NUP84
- Nucleoporin NSP1
- ATP-dependent RNA helicase DBP5
- Nucleoporin NUP100/NSP100
- Nucleoporin NUP82
- Nucleoporin NUP145
- mRNA export factor GLE1
- Nucleoporin NUP49/NSP49
- Nucleoporin NUP116/NSP116
- Nucleoporin NUP133
Sequence:
MSSLKDEVPTETSEDFGFKFLGQKQILPSFNEKLPFASLQNLDISNSKSLFVAASGSKAVVGELQLLRDHITSDSTPLTFKWEKEIPDVIFVCFHGDQVLVSTRNALYSLDLEELSEFRTVTSFEKPVFQLKNVNNTLVILNSVNDLSALDLRTKSTKQLAQNVTSFDVTNSQLAVLLKDRSFQSFAWRNGEMEKQFEFSLPSELEELPVEEYSPLSVTILSPQDFLAVFGNVISETDDEVSYDQKMYIIKHIDGSASFQETFDITPPFGQIVRFPYMYKVTLSGLIEPDANVNVLASSCSSEVSIWDSKQVIEPSQDSERAVLPISEETDKDTNPIGVAVDVVTSGTILEPCSGVDTIERLPLVYILNNEGSLQIVGLFHVAAIKSGHYSINLESLEHEKSLSPTSEKIPIAGQEQEEKKKNNESSKALSENPFTSANTSGFTFLKTQPAAANSLQSQSSSTFGAPSFGSSAFKIDLPSVSSTSTGVASSEQDATDPASAKPVFGKPAFGAIAKEPSTSEYAFGKPSFGAPSFGSGKSSVESPASGSAFGKPSFGTPSFGSGNSSVEPPASGSAFGKPSFGTPSFGSGNSSAEPPASGSAFGKPSFGTSAFGTASSNETNSGSIFGKAAFGSSSFAPANNELFGSNFTISKPTVDSPKEVDSTSPFPSSGDQSEDESKSDVDSSSTPFGTKPNTSTKPKTNAFDFGSSSFGSGFSKALESVGSDTTFKFGTQASPFSSQLGNKSPFSSFTKDDTENGSLSKGSTSEINDDNEEHESNGPNVSGNDLTDSTVEQTSSTRLPETPSDEDGEVVEEEAQKSPIGKLTETIKKSANIDMAGLKNPVFGNHVKAKSESPFSAFATNITKPSSTTPAFSFGNSTMNKSNTSTVSPMEEADTKETSEKGPITLKSVENPFLPAKEERTGESSKKDHNDDPKDGYVSGSEISVRTSESAFDTTANEEIPKSQDVNNHEKSETDPKYSQHAVVDHDNKSKEMNETSKNNERSGQPNHGVQGDGIALKKDNEKENFDSNMAIKQFEDHQSSEEDASEKDSRQSSEVKESDDNMSLNSDRDESISESYDKLEDINTDELPHGGEAFKAREVSASADFDVQTSLEDNYAESGIQTDLSESSKENEVQTDAIPVKHNSTQTVKKEAVDNGLQTEPVETCNFSVQTFEGDENYLAEQCKPKQLKEYYTSAKVSNIPFVSQNSTLRLIESTFQTVEAEFTVLMENIRNMDTFFTDQSSIPLVKRTVRSINNLYTWRIPEAEILLNIQNNIKCEQMQITNANIQDLKEKVTDYVRKDIAQITEDVANAKEEYLFLMHFDDASSGYVKDLSTHQFRMQKTLRQKLFDVSAKINHTEELLNILKLFTVKNKRLDDNPLVAKLAKESLARDGLLKEIKLLREQVSRLQLEEKGKKASSFDASSSITKDMKGFKVVEVGLAMNTKKQIGDFFKNLNMAK
Protein: Protein E7 (A0MPS7)
Organism: Human papillomavirus type 16
Subcellular location: Host cytoplasm {ECO:0000256|HAMAP-Rule:MF_04004}. Host nucleus {ECO:0000256|HAMAP-Rule:MF_04004}. Note=Predominantly found in the host nucleus. {ECO:0000256|HAMAP-Rule:MF_04004}.
Interaction partners:
Sequence:
MHGDTPTLHEYMLDLQPETTDLYCYEQLNDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDFTLRLCVQSTHVDIRTLEDLLMGTLGIVCPICSQKP
Protein: Small toxic protein IbsC (C1P615)
Organism: Escherichia coli (strain K12)
Function: Toxic component of a type I toxin-antitoxin (TA) system. Overexpression causes cessation of growth and rapid membrane depolarization. Overexpression induces stress-response, the psp phage shock and a number of membrane protein genes.
Interaction partners:
Sequence:
MMRLVIILIVLLLISFSAY
Protein: Arginine--pyruvate transaminase AruH (EC 2.6.1.84) (Q9HUI9)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the conversion of L-arginine into 2-ketoarginine via transamination. L-arginine is the best substrate, but it can also use L-lysine, L-methionine, L-leucine, ornithine and L-glutamine, which indicates that it may have a broader physiological function in amino acid catabolism.
Interaction partners:
- Probable 2-ketoarginine decarboxylase AruI
- Arginine N-succinyltransferase subunit alpha
- Biosynthetic arginine decarboxylase
- Lysine decarboxylase LdcA
- Arginine N-succinyltransferase subunit beta
- Argininosuccinate lyase
- Arginine deiminase
- D-amino acid dehydrogenase 1
- Guanidinobutyrase
- Bifunctional chorismate mutase/prephenate dehydratase
Sequence:
MRYSDFTQRIAGDGAAAWDIHYRALARVEQGEEILLLSVGDPDFDTPAPIVQAAIDSLLAGNTHYADVRGKRALRQRIAERHRRRSGQAVDAEQVVVLAGAQCALYAVVQCLLNPGDEVIVAEPMYVTYEAVFGACGARVVPVPVRSENGFRVQAEEVAALITPRTRAMALNSPHNPSGASLPRATWEALAELCMAHDLWMISDEVYSELLFDGEHVSPASLPGMADRTATLNSLSKSHAMTGWRVGWVVGPAALCAHLENLALCMLYGSPEFIQDAACTALEAPLPELEAMREAYRRRRDLVIECLADSPGLRPLRPDGGMFVMVDIRPTGLSAQAFADRLLDRHGVSVLAGEAFGPSAAGHIRLGLVLGAEPLREACRRIALCAAELLGQA
Protein: Protein DECREASED SIZE EXCLUSION LIMIT 1 (AtDSE1) (Protein ALUMINUM TOLERANT 2) (Protein EMBRYO DEFECTIVE 2757) (Protein TANMEI) (Q3MV14)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the formation of X-, Y-shaped and twinned plasmodesmata (PD), thus modelating PD size exclusion limit and regulating cell-to-cell transport. Cell cycle checkpoint regulator that monitors and responds to DNA damage such as DNA cross-links, and triggers the halt of the cell cycle progression in the presence of DNA cross-linking agents. Mediates the active process of aluminum- (Al) dependent root growth inhibition and thus is required for response to Al toxicity. Required for both early and late phases of embryo development as well as during seedling growth. Essential for signal transduction and development of both male and female organs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22345493, ECO:0000269|PubMed:22411811}. Nucleus {ECO:0000269|PubMed:22345493, ECO:0000269|PubMed:22411811}. Note=Translocates from the cytoplasm to the nucleus in response to DNA damage mediated by treatment with AlCl(3), mitomycin C (MMC), or cisplatin (CDDP). {ECO:0000269|PubMed:22345493}.
Interaction partners:
- DEAD-box ATP-dependent RNA helicase 47, mitochondrial
- AT3g05090/T12H1_5
- Ribosome biogenesis protein WDR12 homolog
- Mitotic checkpoint protein BUB3.3
- Mitotic checkpoint protein BUB3.1
- WD repeat-containing protein VIP3
- Transducin/WD40 repeat-like superfamily protein
- Protein ANTHESIS POMOTING FACTOR 1
- Protein RAE1
- Notchless protein homolog
Sequence:
MSKRPPPDPVAVLRGHRHSVMDVSFHPSKSLLFTGSADGELRIWDTIQHRAVSSAWAHSRANGVLAVAASPWLGEDKIISQGRDGTVKCWDIEDGGLSRDPLLILETCAYHFCKFSLVKKPKNSLQEAESHSRGCDEQDGGDTCNVQIADDSERSEEDSGLLQDKDHAEGTTFVAVVGEQPTEVEIWDLNTGDKIIQLPQSSPDESPNASTKGRGMCMAVQLFCPPESQGFLHVLAGYEDGSILLWDIRNAKIPLTSVKFHSEPVLSLSVASSCDGGISGGADDKIVMYNLNHSTGSCTIRKEITLERPGVSGTSIRVDGKIAATAGWDHRIRVYNYRKGNALAILKYHRATCNAVSYSPDCELMASASEDATVALWKLYPPHKSL
Protein: 116 kDa U5 small nuclear ribonucleoprotein component (U5 snRNP-specific protein, 116 kDa) (A0A8I6AI35)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDEDEDEDDVGEHDDDHPGMEVVLHEDKKYYPTAEEVYGPEVETIVQEEDTQPLTEPIIKPVKTKKFTLMEQTLPVTVYEMDFLADLMDNSELIRNVTLCGHLHHGKTCFVDCLIEQTHPEIRKRYDQDLCYTDILFTEQERGVGIKSTPVTVVLPDTKGKSYLFNIMDTPGHVNFSDEVTAGLRISDGVVLFIDAAEGVMLNTERLIKHAVQERLAVTVCINKIDRLILELKLPPTDAYYKLRHIVDEVNGLISMYSTDENLILSPLLGNVCFSSSQYSICFTLGSFAKIYADTFGDINYQEFAKRLWGDIYFNPKTRKFTKKAPSSSSQRSFVEFILEPLYKILAQVVGDVDTSLPRTLDELGIHLTKEELKLNIRPLLRLVCKKFFGEFTGFVDMCVQHIPSPKVGAKPKIEHTYTGGVDSDLGEAMSDCDPDGPLMCHTTKMYSTDDGVQFHAFGRVLSGTIHAGQPVKVLGENYTLEDEEDSQICTVGRLWISVARYHIEVNRVPAGNWVLIEGVDQPIVKTATITEPRGNEEAQIFRPLKFNTTSVIKIAVEPVNPSELPKMLDGLRKVNKSYPSLTTKVEESGEHVILGTGELYLDCVMHDLRKMYSEIDIKVADPVVTFCETVVETSSLKCFAETPNKKNKITMIAEPLEKGLAEDIENEVVQITWNRKKLGEFFQTKYDWDLLAARSIWAFGPDATGPNILVDDTLPSEVDKALLGSVKDSIVQGFQWGTREGPLCDELIRNVKFKILDAVVAQEPLHRGGGQIIPTARRVVYSAFLMATPRLMEPYYFVEVQAPADCVSAVYTVLARRRGHVTQDAPIPGSPLYTIKAFIPAIDSFGFETDLRTHTQGQAFSLSVFHHWQIVPGDPLDKSIVIRPLEPQPAPHLAREFMIKTRRRKGLSEDVSISKFFDDPMLLELAKQDVVLNYPM
Protein: Ornithine utilization regulator (P72171)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Probably activates the ArgJ gene that encodes ornithine acetyltransferase. Binds to its own promoter-operator region. Probably binds ornithine.
Interaction partners:
- Metal-dependent hydrolase
- DUF2066 domain-containing protein
- Probable transcriptional regulator
- MmsAB operon regulatory protein
- Photosynthesis system II assembly factor Ycf48/Hcf136-like domain-containing protein
- Thiol:disulfide interchange protein DsbD 2
- Probable transcriptional regulator
Sequence:
MKQPLNFTAELVPVAYAEALLDLVAEYGVSRQALFDAARVRPEVLDSPNGRLSFLDFNQLTYSAQALCGEPALGLVLGQRLNVSAHGILGYAVLSSANLGKAIQFALKYYRVLGLAYELELVLDDGRAELRAVESMPLGAASVFAAEGLMATLYSIACFLVGEPLQDVRVGFAYPPPAHARRYAEVFGVAAEFEQPWHWLSMPSEYLERPMALANPATVQMCEQQCEALLATLDVQEGLLTRVRRLLLARPGDFPDLEQAARELHTSGRSLRRHLSSLGTTYQQVLDDVRKRLALQYLTTTQLPLYEIALLLGFNDSSNFRRAFRKWTGKLPSDYREAP
Protein: Spore coat protein SP60 (P15270)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- HECT-type E3 ubiquitin transferase
- Spore coat protein SP70
- Spore coat protein SP85
- Extracellular matrix protein A
- Prespore-specific protein A
- Prestalk protein
- Spore coat protein SP96
Sequence:
MKILSLLVVGALCMGGKVYGEVNGDWNNNGDWNNNGDWNNNGDWNNNGPILDCSTLQCPPRYHCEVNNGNRQCVEDQITLPPFDKCDNVHCPKGFNCKYDWEKDLALCVPWRPYPPVCRTRCPEGHECKVDEWGKECCVKIKCDDICDLRCPKGHECKIKHDGSKCCVRSWRPRPHKPHPRPPICRLRCPPGHECKHDEHGKECCVKKRHHDRCDLKCKRGYECKIKHDGSKCCVKRTPKRPCCKPNSCARDEKCVATKDRIICVKPTCDNTRCPPNYHCICGDKIDGVKCVPDCKKARCDDVECPDFHRCVERRGGILSCEFDPPRQPRSLDWAENENDDRDYDDRDYDDDEYDGDYDGRDGDYDGDYDGDYDDDNYYGDDDYDNDWDNDNDWGNDWDNDWDNEDGDNWNDDDFQDANDEWDY
Protein: Griffithsin (GRFT) (P84801)
Organism: Griffithsia sp. (strain Q66D336) (Red alga)
Function: Mixed specificity lectin with anti-HIV activity. Binds to HIV envelope glycoproteins, including exterior membrane glycoprotein gp120, and inhibits viral entry into cells. Binding to gp120 is dependent on gp120 being glycosylated, and is inhibited by mannose, glucose and N-acetylglucosamine.
Interaction partners:
Sequence:
SLTHRKFGGSGGSPFSGLSSIAVRSGSYLDXIIIDGVHHGGSGGNLSPTFTFGSGEYISNMTIRSGDYIDNISFETNMGRRFGPYGGSGGSANTLSNVKVIQINGSAGDYLDSLDIYYEQY
Protein: Probable aquaporin PIP1-5 (AtPIP1;5) (Plasma membrane intrinsic protein 1d) (PIP1d) (Q8LAA6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aquaporins facilitate the transport of water and small neutral solutes across cell membranes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15060130}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- PAMP-induced secreted peptide 1
Sequence:
MEGKEEDVNVGANKFPERQPIGTAAQTESKDYKEPPPAPFFEPGELKSWSFYRAGIAEFIATFLFLYVTVLTVMGVKRAPNMCASVGIQGIAWAFGGMIFALVYCTAGISGGHINPAVTFGLFLARKLSLTRALFYIVMQCLGAICGAGVVKGFQPGLYQTNGGGANVVAHGYTKGSGLGAEIVGTFVLVYTVFSATDAKRSARDSHVPILAPLPIGFAVFLVHLATIPITGTGINPARSLGAAIIYNKDHAWDDHWIFWVGPFIGAALAALYHQIVIRAIPFKSKT
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (F1M754)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
LDEEEIKLEINMLKKYSHHRNIATYYGAFIKKSPPGHDDQLWLVMEFCGAGSITDLVKNTKGNTLKEDWIAYISREILRGLAHLHIHHVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRVRPLSSPPPPKPLPLLSLSKKFFSFIEGCLVKNYMQRPSTEQLLKHPFIRDQPNERQVRIQLKDHIDRTRKKRGEKDETEYEYSGSEEEEEEVPEQEGEPSSIVNVPGESTLRRDFLRLQQENKERSEALRRQQLLQEQQLREQEEYKRQLLAERQKRIEQQKEQRRRLEEQQRREREARRQQEREQRRREQEEKRRLEELERRRKEEEERRRAEDEKRRVEREQEYIRRQLEEEQRHLEILQQQLLQEQAMLLHDHRRPHAQQPPPPQQQDRSKPSYHAPEPKPHYDPADRAREVQWSHLASLKNNVSPVSRSHSFSDPSPKFAHHHLRSQDPCPPSRSEGLSQSSDSKSEVPEPTQKAWSRSDSDEVPPRVPVRTTSRSPVLSRRDSPLQGSGQQNSQAGQRNSTSSIEPRLLWERVEKLVPRPGSGSSSGSSNSGSQPGSHPGSQSGSGERFRVRSSSKSEGSPSQRLENAAKKPEDKKEVFRPLKPAVRIDLTALAKELRAVEDVRPPHKVTDYSSSSEESGTTDEEEEDVEQEGADDSTSGPEDTRAASSLNLSNGETESVKTMIVHDDVESEPAMTPSKEGTLIVRQTQSASSTLQKHKSSSSFTPFIDPRLLQISPSSGTTVTSVVGFSCDGLRPEAIRQDPTRKGSVVNVNPTNTRPQSDTPEIRKYKKRFNSEILCAALWGVNLLVGTESGLMLLDRSGQGKVYPLISRRRFQQMDVLEGLNVLVTISGKKDKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDLEGCVHYKVVKYERIKFLVIALKSSVEVYAWAPKPYHKFMAFKSFGELVHKPLLVDLTVEEGQRLKVIYGSCAGFHAVDVDSGSVYDIYLPTHIQCTIKPHAIIILPNTDGMELLVCYEDEGVYVNTYGRITKDVVLQWGEMPTSVAYIRSNQTMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVYFMTLGRTSLLSW
Protein: Hyaluronoglucosaminidase (Hyaluronidase) (EC 3.2.1.35) (Mu toxin) (P26831)
Organism: Clostridium perfringens (strain 13 / Type A)
Function: Putative virulence factor which is likely to act on connective tissue during gas gangrene.
Subcellular location: Secreted.
Interaction partners:
- Probable PTS system
- Probable PTS system
- exo-alpha-sialidase
- O-GlcNAcase NagJ
- Probable alpha-N-acetylglucosaminidase
- exo-alpha-sialidase
- Beta-N-acetylhexosaminidase
- Sialidase-like protein
- Probable PTS system enzyme
- PTS EIIB type-1 domain-containing protein
Sequence:
MNKNIRKIITSTVLAAMTISVLPSNLVVFATDGITENFYEIYPKPQEISYSGGEFQISDEINIVYDDGIDTYTKKRVDEVLEASNLEATVSNEIVPGKTNFLVGINESGGVVDNYFNKNIPHDESFFDEKMDANIVSVKDGVIGVIGEDTDSAFYGVTTLKHVFNQLEEGNKIQSFRADDYAEVAHRGFIEGYYGNPWSNEDRAELMKFGGDYKLNQYVFAPKDDPYHNSKWRDLYPEEKLSEIKKLAQVGNETKNRYVYALHPFMNNPVRFDTEENYQNDLGVIKAKFTQLLENDVRQFAILADDASAPAQGASMYVKLLTDLTRWLEEQQSTYPDLKTDLMFCPSDYYGNGSSAQLKELNKAEDNVSIVMTGGRIWGEVDENFANNFMNNISTEGHPGRAPFFWINWPCSDNSKQHLIMGGNDTFLHPGVDPSKIDGIVLNPMQQAEANKSALFAIADYAWNIWDNKEEADENWNDSFKYMDHGTAEETNSSLALREISKHMINQNMDGRVRPLQESVELAPKLEAFKQKYDSGASIKEDALELIAEFTNLQKAADYYKNNPGNERTRDQIIYWLNCWEDTMDAAIGYLKSAIAIEEGDDEAAWANYSEAQGAFEKSKTYGFHYVDHTEYAEVGVQHIVPFIKSMGQNLSVVIGSIVDPNRIIATYISNRQDAPTGNPDNIFDNNASTELVYKNPNRIDVGTYVGVKYSNPITLNNVEFLMGANSNPNDTMQKAKIQYTVDGREWIDLEEGVEYTMPGAIKVENLDLKVRGVRLIATEARENTWLGVRDINVNKKEDSNSGVEFNPSLIRSESWQVYEGNEANLLDGDDNTGVWYKTLNGDTSLAGEFIGLDLGKEIKLDGIRFVIGKNGGGSSDKWNKFKLEYSLDNESWTTIKEYDKTGAPAGKDVIEESFETPISAKYIRLTNMENINKWLTFSEFAIISDELENAGNKENVYTNTELDLLSLAKEDVTKLIPTDDISLNHGEYIGVKLNRIKDLSNINLEISNDTGLKLQSSMNGVEWTEITDKNTLEDGRYVRLINTSNEAVNFNLTKFEVNSNEVYEPSLVDAYVGDDGAKKAVDGDLKTRVKFLGAPSTGDTIVYDLGQEILVDNLKYVVLDTEVDHVRDGKIQLSLDGETWTDAITIGDGVENGVDDMFSTPLKNGYKHGNQSGGIVPIDSAYVEGDNLNQKARYVRILFTAPYRHRWTVINELMINNGEYISTVNDPTYISNPIEERGFAPSNLRDGNLTTSYKPNTNNGEISEGSITYRLSEKTDVRKVTIVQSGSSISNAKVMARVGDGSENVTDQWVQLGTLSNSLNEFINRDYNNIYEIKIEWTDVAPNIYEIITLNQEFEFPVNDSLKAKYDELINLSGDEYTLSSFETLKEALNEAKSILDDSNSSQKKIDKALEKLNKAEERLDLRATDFEDFNKVLTLGNSLVEEEYTAESWALFSEVLEAANEANKNKADYTQDQINQIVIDLDASIKALVKETPEVDKTNLGELINQGKSLLDESVEGFNVGEYHKGAKDGLTVEINKAEEVFNKEDATEEEINLAKESLEGAIARFNSLLIEESTGDFNGNGKIDIGDLAMVSKNIGSTTNTSLDLNKDGSIDEYEISFINHRILN
Protein: Zinc finger protein 131 (P52739)
Organism: Homo sapiens (Human)
Function: Plays a role during development and organogenesis as well as in the function of the adult central nervous system (By similarity). May be involved in transcriptional regulation as a repressor of ESR1/ER-alpha signaling.
Subcellular location: Nucleus {ECO:0000269|PubMed:17306895, ECO:0000269|PubMed:22467880, ECO:0000269|PubMed:23404503}. Note=Sumoylation does not affect nuclear localization.
Interaction partners:
- BRCA2-interacting transcriptional repressor EMSY
- E3 SUMO-protein ligase CBX4
- E3 ubiquitin-protein ligase UHRF2
Sequence:
MEAEETMECLQEFPEHHKMILDRLNEQREQDRFTDITLIVDGHHFKAHKAVLAACSKFFYKFFQEFTQEPLVEIEGVSKMAFRHLIEFTYTAKLMIQGEEEANDVWKAAEFLQMLEAIKALEVRNKENSAPLEENTTGKNEAKKRKIAETSNVITESLPSAESEPVEIEVEIAEGTIEVEDEGIETLEEVASAKQSVKYIQSTGSSDDSALALLADITSKYRQGDRKGQIKEDGCPSDPTSKQVEGIEIVELQLSHVKDLFHCEKCNRSFKLFYHFKEHMKSHSTESFKCEICNKRYLRESAWKQHLNCYHLEEGGVSKKQRTGKKIHVCQYCEKQFDHFGHFKEHLRKHTGEKPFECPNCHERFARNSTLKCHLTACQTGVGAKKGRKKLYECQVCNSVFNSWDQFKDHLVIHTGDKPNHCTLCDLWFMQGNELRRHLSDAHNISERLVTEEVLSVETRVQTEPVTSMTIIEQVGKVHVLPLLQVQVDSAQVTVEQVHPDLLQDSQVHDSHMSELPEQVQVSYLEVGRIQTEEGTEVHVEELHVERVNQMPVEVQTELLEADLDHVTPEIMNQEERESSQADAAEAAREDHEDAEDLETKPTVDSEAEKAENEDRTALPVLE
Protein: Small ribosomal subunit protein eS32B (60S ribosomal protein L41-B) (Large ribosomal subunit protein eL41B) (P0CT82)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongation factor 3
- mRNA export factor elf1
- Large ribosomal subunit protein eL39
- Small ribosomal subunit protein RACK1
- Large ribosomal subunit protein eL29
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL38A
- Large ribosomal subunit protein eL38B
- Small ribosomal subunit protein eS17B
- Small ribosomal subunit protein eS17A
Sequence:
MRDKWRKKRVRRLKRKRRKMRARSK
Protein: Fatty-acid and retinol-binding protein 1 (Av-FAR-1) (Av20) (Q8MZJ8)
Organism: Acanthocheilonema viteae (Filarial nematode worm) (Dipetalonema viteae)
Function: Binds retinol and different fatty acids.
Subcellular location: Secreted {ECO:0000269|PubMed:12106870, ECO:0000269|PubMed:9223154}.
Interaction partners:
Sequence:
MYHQLILMALIGVIMANVVPFSMSNIPEEYKEFIPEEVKNFYKNLTQEDRQILRELASKHATFTNEDAALEALKNKSDKLYQKAVELRNFVKAKIDSLKPDAKAFVDEIIAKVRSLRPEDGQKLDVEKLKQAARDIIAKYEALNEETKEELKAPFPNTTKIITNEKFTRIANSFLQKN
Protein: Response regulator protein FleR (Q9I4N3)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Member of the two-component regulatory system FleS/FleR that regulates the expression of multiple genes involved in flagellar synthesis, adhesion, swarming, motility and antibiotic resistance. May function as a transcriptional activator by direct binding to a cis-acting sequence upstream of the target genes (Probable).
Interaction partners:
- Sensor protein kinase FleS
- Flagellar M-ring protein
- Flagellar biosynthesis protein FlhF
- Flagellar hook-basal body complex protein FliE
- Antiactivator FleN
- RNA polymerase sigma-54 factor
- Flagellar motor switch protein FliG
- Flagellar biosynthesis protein FlhA
- RNA polymerase sigma factor FliA
- Peptidoglycan hydrolase FlgJ
Sequence:
MAAKVLLVEDDRALREALSDTLLLGGHEFVAVDSAEAALPVLAREAFSLVISDVNMPGMDGHQLLGLIRTRYPHLPVLLMTAYGAVDRAVEAMRQGAADYLVKPFEARALLDLVARHALGQLPGSEEDGPVALEPASRQLLELAARVARSDSTVLISGESGTGKEVLANYIHQQSPRAGKPFIAINCAAIPDNMLEATLFGHEKGSFTGAIAAQPGKFELADGGTILLDEISEMPLGLQAKLLRVLQEREVERVGARKPINLDIRVLATTNRDLAAEVAAGRFREDLYYRLSVFPLAWRPLRERPADILPLAERLLRKHSRKMNLGAVALGPEAAQCLVRHAWPGNVRELDNAIQRALILQQGGLIQPADLCLTAPIGMPLAAPVPVPMPAMPPATPPSVEIPSPAAGQDASGALGDDLRRREFQVIIDTLRTERGRRKEAAERLGISPRTLRYKLAQMRDAGMDVEAYLYAI
Protein: Serine--tRNA ligase, cytoplasmic (EC 6.1.1.11) (Seryl-tRNA synthetase) (SerRS) (Seryl-tRNA(Ser) synthetase) (P07284)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser).
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49591}.
Interaction partners:
- Arginine--tRNA ligase, cytoplasmic
- Arginine--tRNA ligase, mitochondrial
- Peroxisomal protein PEX21
- Tryptophan--tRNA ligase, cytoplasmic
- Leucine--tRNA ligase, cytoplasmic
- Cysteine--tRNA ligase
- Glutamine--tRNA ligase
- Threonine--tRNA ligase, cytoplasmic
- Valine--tRNA ligase, mitochondrial
- Leucine--tRNA ligase, mitochondrial
Sequence:
MLDINQFIEDKGGNPELIRQSQKARNASVEIVDEIISDYKDWVKTRFELDELNKKFNKLQKDIGLKFKNKEDASGLLAEKEKLTQQKKELTEKEQQEDKDLKKKVFQVGNIVHPSVVVSNDEENNELVRTWKPEDLEAVGPIASVTGKPASLSHHEILLRLDGYDPDRGVKICGHRGYFFRNYGVFLNQALINYGLQFLAAKGYIPLQAPVMMNKELMSKTAQLSEFDEELYKVIDGEDEKYLIATSEQPISAYHSGEWFEKPQEQLPIHYVGYSSCFRREAGSHGKDAWGVFRVHAFEKIEQFVITEPEKSWEEFEKMISYSEEFYKSLKLPYRIVGIVSGELNNAAAKKYDLEAWFPYQKEYKELVSCSNCTDYQSRNLEIRCGIKKMGDREKKYVHCLNSTLAATQRALCCILENYQTEDGLVVPEVLRKYIPGEPEFLPFVNELPKNSTSSKDKKKKN
Protein: Diguanylate cyclase DgcZ (DGC) (EC 2.7.7.65) (Zinc-sensory diguanylate cyclase) (P31129)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the synthesis of cyclic-di-GMP (c-di-GMP) via the condensation of 2 GTP molecules. May act as a zinc sensor that controls, via c-di-GMP, post-translational events. Overexpression leads to a strong repression of swimming; swimming returnes to normal when residues 206-207 are both mutated to Ala. Overexpression also leads to a reduction in flagellar abundance and a 20-fold increase in c-di-GMP levels in vivo. Required for aminoglycoside-mediated induction of biofilm formation, it also plays a lesser role in biofilm production in response to other classes of translation inhibitors. The c-di-GMP produced by this enzyme up-regulates poly-GlcNAc production as well as the biofilm synthesis protein PgaD, although c-di-GMP is probably not the main inducing principle. C-di-GMP is a second messenger which controls cell surface-associated traits in bacteria.
Interaction partners:
- Cyclic di-GMP phosphodiesterase PdeH
- Cyclic di-GMP phosphodiesterase PdeL
- Oxygen sensor protein DosP
- Probable cyclic di-GMP phosphodiesterase PdeC
- Probable cyclic di-GMP phosphodiesterase PdeI
- Probable cyclic di-GMP phosphodiesterase PdeG
- Probable cyclic di-GMP phosphodiesterase PdeK
- Probable cyclic di-GMP phosphodiesterase PdeN
- Probable cyclic di-GMP phosphodiesterase PdeD
- Probable cyclic di-GMP phosphodiesterase PdeB
Sequence:
MIKKTTEIDAILLNLNKAIDAHYQWLVSMFHSVVARDASKPEITDNHSYGLCQFGRWIDHLGPLDNDELPYVRLMDSAHQHMHNCGRELMLAIVENHWQDAHFDAFQEGLLSFTAALTDYKIYLLTIRSNMDVLTGLPGRRVLDESFDHQLRNAEPLNLYLMLLDIDRFKLVNDTYGHLIGDVVLRTLATYLASWTRDYETVYRYGGEEFIIIVKAANDEEACRAGVRICQLVDNHAITHSEGHINITVTAGVSRAFPEEPLDVVIGRADRAMYEGKQTGRNRCMFIDEQNVINRV
Protein: Transmembrane protein 70, mitochondrial (Q9BUB7)
Organism: Homo sapiens (Human)
Function: Scaffold protein that participates in the c-ring assembly of mitochondrial ATP synthase (F(1)F(0) ATP synthase or complex V) by facilitating the membrane insertion and oligomer formation of the subunit c/ATP5MC1 through its interaction. Therefore, participates in the early stage of mitochondrial ATP synthase biogenesis and also protects subunit c/ATP5MC1 against intramitochondrial proteolysis. In addition, binds the mitochondrial proton-transporting ATP synthase complexes I and may play a role in the stability of its membrane-bound subassemblies.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:20937241, ECO:0000269|PubMed:24576557, ECO:0000269|PubMed:33359711}; Multi-pass membrane protein {ECO:0000269|PubMed:20937241, ECO:0000269|PubMed:24576557}. Note=Mostly located within the inner cristae membrane. {ECO:0000269|PubMed:33359711}.
Interaction partners:
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- NADH dehydrogenase iron-sulfur protein 5
- ATP synthase mitochondrial F1 complex assembly factor 2
- Opalin
- FAD-dependent oxidoreductase domain-containing protein 1
- ATP synthase F
- ATP synthase mitochondrial F1 complex assembly factor 1
- Distal membrane-arm assembly complex protein 2
- ATP synthase F
- Transmembrane protein 242
Sequence:
MLFLALGSPWAVELPLCGRRTALCAAAALRGPRASVSRASSSSGPSGPVAGWSTGPSGAARLLRRPGRAQIPVYWEGYVRFLNTPSDKSEDGRLIYTGNMARAVFGVKCFSYSTSLIGLTFLPYIFTQNNAISESVPLPIQIIFYGIMGSFTVITPVLLHFITKGYVIRLYHEATTDTYKAITYNAMLAETSTVFHQNDVKIPDAKHVFTTFYAKTKSLLVNPVLFPNREDYIHLMGYDKEEFILYMEETSEEKRHKDDK