wanglab/gogpt-training-data huggingface dataset:
Protein: Protein phosphatase 1, regulatory subunit 13 like (F1LW07)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- Cellular tumor antigen p53
- Serine/threonine-protein phosphatase PP1-alpha catalytic subunit
- Cellular tumor antigen p53
- Tumor protein p73
- Tumor protein 63
- Hypoxia-inducible factor 1-alpha inhibitor
Sequence:
MDSEAFQQARDLLDLNFQSLAMKHMDLKQMELDTAAAKVDELTKQLESLWSDSPAPPGTQAGVPSRMSRYSTSPVPEHFGSRGSLQKIAADGVEARFGRSESAPSLHPYSPLSPKGRPSSPRTSIYLQPTTPDPYSSLDRAPSPRPRAFEGTGSPHGRAPSPRPGTGPVRQPGPPTPFDYLGRAGSPRGSPLAEGPQAFFPERGPSPRPPAAAYDTSATFGSPLLGAGGSAFAPPLRAQDDSTLRRRPPKAWNESDLDVAYEKKSSQTASYERLDVFTRPASPGLQLLPWRESSLDGLGASGKDNITSATLPRNYKVSPLASDRRSDVGSYRRSMGSAGPSGTLPRSWQPVSRIPMPPSSPQPRSTPRQRPIPLSMIFKLQNAFWEHGASRAVLPGSPIFSRAPPPKLPPQPPPQPQLPPQPQPQMPPQSQPQPQTPVPQQTWSPMNEGLLKSPAELEPEPELEGLLAPVLESGDADEGTVTRPLSPTRLQPALPPEAQTVPELEEVARVLAEIPRPLKRRGSMEQSPAAALPPTHKKQYQQIINRLFHRHGGPGPGGPEPELSTITEGSEARAGPPAPAPPAPIPPPAPAQSNPPEQPQSMEMRSVLRKVGSPRKARRARLNPLVLLLDAALTGELDVVQQAVKEMNDPSQPNEEGITALHNAICGANYPIVDFLIAAGANVNSPDSHGWTPLHCAASCNDTAICTALVQHGAAIFATTLSDGATAIEKCDPYREGYADCATYLADVEQSMGLMHNGVVYALWDYSAEFGDELSFREGESVTVLRRDGPEETDWWWAALHGQEGYVPRNYFGLFPRVKSQRSKI
Protein: Vacuolar protein sorting-associated protein 11 homolog (Q91W86)
Organism: Mus musculus (Mouse)
Function: Plays a role in vesicle-mediated protein trafficking to lysosomal compartments including the endocytic membrane transport and autophagic pathways. Believed to act as a core component of the putative HOPS and CORVET endosomal tethering complexes which are proposed to be involved in the Rab5-to-Rab7 endosome conversion probably implicating MON1A/B, and via binding SNAREs and SNARE complexes to mediate tethering and docking events during SNARE-mediated membrane fusion. The HOPS complex is proposed to be recruited to Rab7 on the late endosomal membrane and to regulate late endocytic, phagocytic and autophagic traffic towards lysosomes. The CORVET complex is proposed to function as a Rab5 effector to mediate early endosome fusion probably in specific endosome subpopulations. Required for fusion of endosomes and autophagosomes with lysosomes. Involved in cargo transport from early to late endosomes and required for the transition from early to late endosomes (By similarity).
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:Q9H270}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H270}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle {ECO:0000305}. Early endosome {ECO:0000305}. Cytoplasmic vesicle, autophagosome {ECO:0000305}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000305}.
Interaction partners:
- Vacuolar protein sorting-associated protein 18 homolog
- Vacuolar protein sorting-associated protein 8 homolog
- Vacuolar protein sorting-associated protein 16 homolog
- Vam6/Vps39-like protein
- Vacuolar protein sorting-associated protein 41 homolog
- Transforming growth factor-beta receptor-associated protein 1
- Vacuolar protein sorting-associated protein 33A
- Vacuolar fusion protein CCZ1 homolog
- Vacuolar protein sorting-associated protein 33B
- Vesicle transport through interaction with t-SNAREs homolog 1A
Sequence:
MAAYLQWRRFVFFEKELVKEPLGNDGAAPGAAPVSGSAASKFLCLPPGITVCDSGRGSLVFGDMEGQIWFLPRSLQLTGFQAYKLRVTHLYQLKQHNILASVGEDEEGINPLVKIWNLEKRDGGNPLCTRIFPAIPGTEPTVVSCLTVHENLNFMAIGFTDGSVTLNKGDITRDRHSKTQILHKGNYPVTGLAFRQAGKTTHLFVVTTENVQSYIVSGKDYPRVELDTHGCGLRCSALSDPSQDLQFIVAGDECVYLYQPDERGPCFAFEGHKLIVHWFRGYLVIVSRDRKVSPKSEFTSRDSQNSDKQILNIYDLCNKFIAYSAGFEDIVDVLAEWGSLYVLTRDGRVHALQEKDTQTKLEMLFKKNLFEMAINLAKSQHLDSDGLAQIFMQYGDHLYSKGNHDGAVQQYIRTIGKLEPSYVIRKFLDAQRIHNLTAYLQTLHRQSLANADHTTLLLNCYTKLKDSSKLEEFIKTKSESEVHFDVETAIKVLRQAGYYSHALYLAENHAHHEWYLKIQLEDIKNYQEALRYIGKLPFEQAESNMKRYGKTLMHHIPEQTTQLLKGLCTDYRPSLEGRGDREALSCRASSEEFIPIFANNPRELKAFLEHMSEVQPDSPQGIYDTLLELRLQNWAHEKDPQAKEKLHAEAISLLKSGRFCDVFDKALVLCQMHDFQDGVLYLYEQGKLFQQIMHYHMQHEQYRQVIAVCERHGEQEPSLWEQALSYFARKEEDCKEYVAAVLRHIENKSLMPPLLVVQTLAHNSTATLSIIRDYLVQKLQKQSQQIAQDELRVRRYREETTRIRQEIQELKASPKIFQKTKCSICNSALELPSVHFLCGHSFHQHCFESYSESDADCPTCLPENRKVMDMIRAQEQKRDLHDQFQHQLKCSNDSFSVIADYFGRGVFNKLTLLTDPPTARLTPSLEAGLQRDLLMHSRRGT
Protein: Cta9p (A0A1D8PCF2)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
Sequence:
MSITLNSSAQQNGNLWDPIKPNFIFSSNISSKIYNLIHAPRKGNQSPYVIKINIQLNNLVSRNKSMKLSDLQDLINIHSNKHYILRILKQESWEYKPSEEIFIVTVKLILLDCSKEAIEFEQNESYTILKQCQFMDEIESYIKKIYLKYSEEEYSAYDISDSTIECSESEDNGELFGRYLEPLKSNDTLIDEFKKIFHDISDEEKSFKHNHDFIENISNLRHNDDDEEDIVEEESPNIDVKEKNSSLSPETPFMAKPENGALRLDDLIEVSCENEDDFELQNIPNPSLELPVSPSKHGFAEDDEVIKISRQSPFHSPTKARRANDLSRRTSNTSFSMISDERYGLEYAYNSHNEDVPSFIKENKKFKFIKVGKVQKFVNLFEEQKNQKEPVTSSRPSSRIASRVTSRTASRTASRTVSRSASMERVI
Protein: Conserved protein (O07754)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Conserved protein
- F420H
- Uncharacterized protein
- Conserved protein
- Uncharacterized protein Rv1526c
- Possible oxygenase
- TIGR02611 family protein
- Conserved protein
Sequence:
MTTLNEAAALAAAERGLAVVSTVRADGTVQASLVNVGLLPHPVSGEPSLGFTTYGKVKLGNLRARPQLAVTFRNGWQWATVEGRAQLVGPDDPRPWLVDGERLRLLLREVFTAAGGTHDDWDEYDRVMAQEQRAVVLITPTRIYSNG
Protein: Serine/threonine-protein phosphatase PP1 isozyme 5 (EC 3.1.3.16) (Type one protein phosphatase 5) (P48485)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Serine/threonine-protein phosphatase that possesses phosphatase activity toward para-nitrophenyl phosphate (pNPP) in vitro.
Subcellular location: Nucleus {ECO:0000269|PubMed:19329567}. Cytoplasm {ECO:0000269|PubMed:19329567}.
Interaction partners:
- Protein phosphatase 1 regulatory subunit INH3
- RNA polymerase II subunit A C-terminal domain phosphatase SSU72
- Flowering time control protein FY
- Protein ANTHESIS POMOTING FACTOR 1
- Transducin/WD40 repeat-like superfamily protein
- Cleavage and polyadenylation specificity factor subunit 2
- Cleavage and polyadenylation specificity factor subunit 3-I
- Putative 26S proteasome non-ATPase regulatory subunit 8 homolog B
- 30-kDa cleavage and polyadenylation specificity factor 30
- Serine/threonine-protein phosphatase PP1 isozyme 2
Sequence:
MAQQGQGSMDPAVLDDIIRRLLDYRNPKAGTKQAMLNDSEIRQLCFVSREIFLQQPCLLELAAPVKICGDIHGQYSDLLRLFEYGGFPPAANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFNVKLWKVFTDTFNCLPVAAVIDEKILCMHGGLSPELINVEQIKNIERPTDVPDAGLLCDLLWSDPSKDVKGWGMNDRGVSYTFGADKVAEFLIKNDMDLVCRAHQVVEDGYEFFADRQLVTMFSAPNYCGEFDNAGALMSVDESLMCSFQILKPVDRRSRFF
Protein: Sister-chromatid cohesion protein 3 (AtSCC3) (Stromalin protein) (O82265)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential component of cohesin complex, a complex required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Required for centromere cohesion maintenance at anaphase I and for the monopolar orientation of the kinetochores during both male and female meiosis. Also involved in mitosis.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00750, ECO:0000269|PubMed:16176934}. Chromosome {ECO:0000269|PubMed:16176934}. Note=In pollen mother cells (PMC), localized in nucleus from meiotic interphase up to and including metaphase I. During interphase, detected as foci in the nucleus. During leptotene and by zygotene and pachytene, localized in condensing chromosomes on chromatin, delineating the chromosome axis. At diplotene and diakinesis, remains on the chromosome axis at lower levels. At metaphase I, confined to the arms of each bivalent chromosomes. Excluded from centromeric regions.
Interaction partners:
- Structural maintenance of chromosomes protein 3
- Structural maintenance of chromosomes protein 4
- Sister chromatid cohesion 1 protein 4
- Sister chromatid cohesion 1 protein 1
- Sister chromatid cohesion protein SCC2
- Sister chromatid cohesion 1 protein 2
- Sister chromatid cohesion 1 protein 3
- Protein CHROMOSOME TRANSMISSION FIDELITY 7
- Meiosis-specific protein ASY1
- Sister chromatid cohesion protein SCC4
Sequence:
MEDSPQGLKRSRDPDQDQDDDSGEAGKADGSGGENQERSSDQIELDDDDFQETRPKPKRSRTHPPQQNLIEVVKGNGDLISKAVKIWVERYEDSPSLATTELLSMLFQACGAKYSIKDDLLDETDVDDVVVSLVNLARAGELEDYQSSRKKELKNFKENLVSFWNNLIIECQNGPLFDRVLFDKCMDYIIALSCTPPRVYRQTATLMGLQLVTSFISVANTLGSQRETTQRQLNAESKKRADGPRVDSLNKRLSVTHEQITTLEDMMRKIFTGLFVHRYRDIDNDIRMSCIQSLGIWILSYPSLFLQDLYLKYLGWTLNDKNAGVRKASLLALQKLYEMDENVPTLGLFTQRFSNRMIEMADDVDMSAAVCAIGLVKQLLRHQLIPDDDLGPLYDLLIDQPQEIRRAIGELVYDHLIAQKFNSSPSSLTGHDDSSSEIHIFRMLQILREFSTDPILCVYVIDDVWEYMKAMKDWKCIISMLLDQNPRTGSTTDEDSTNLIRLLFVSIRKAVGEKIIPSTDNRKQYHSKAQREIFENNRKDITVAMMKNYPQLLRKFMADKAKVSSLVEIIIFMKLELYSLKRQEQSFKAAVRLIKDAFFKHGEKEALRSCVKAITFCASESKGELQDFSRGKLKDLEDELLDKITSAIREVKDGNDEYSLLVNLKRLYELQLSKPVLVESMFDEIALTLHNFRNLDEEVICFLLLNMHMYLAWYLHSIINCEAISEASLSSLISKRDTLFEELSYFLNGIEESKKYGNQLSNRICAILAETWCLFRKSNYDSGKLERLGYCPDSVFLEKFWKLCAEMFNTSDETDEEDENKEYIEETNRDVSVIAACKLVASDVVPKDYLGPEIISHLGMHGPGVTGIIKNLITFLRKKEDDISNIYLESLKRAYHRYSSELSSGREESRVDKCLEEWRELAGGLSGMYIGAARNKYRLEILSVVKEGVEFAFRDAPKQLLFLEVAILPFATRLSVSDIIDIKKDVQGRIVHVNTDEDPSGWRPCFTFLETLEEKCLKNEDLQDDKEAANVRRRGRPRKRPETERKRLFDEQSGSDEDESISGGSDREDKLDEDAPLIETIRSAARRKALKGERSKGH
Protein: Tubulin alpha chain (H2L2E8)
Organism: Caenorhabditis elegans
Interaction partners:
- Tubulin beta chain
- Tubulin beta-2 chain
- Tubulin beta chain
- Tubulin beta-4 chain
- Tubulin beta chain
- Tubulin beta-1 chain
- Dynein heavy chain, cytoplasmic
- Calponin homology domain-containing protein
- WD_REPEATS_REGION domain-containing protein
- Serine/threonine-protein kinase zyg-8
Sequence:
MFVFNMREVISIHVGQAGVQIGNACWELYCLEHGIQPDGTMPSDQQADGESFTTFFSDTGNGRYVPRSIFVDLEPTVVDEIRTGTYKKLFHPEQMITGKEDAANNYARGHYTVGKELIDTVLDRIRRLADNCSGLQGFFVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLSVDRPSYTNLNRIISQVVSSITASLRFDGALNVDLNEFQTNLVPYPRIHFPLAAYTPLISADKAYHEALSVNDITNSCFEPANQMVKCDPRHGKYMAVCLLYRGDVVPKDVNTAIAAIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVPRAVCMLSNTTAIAEAWSRLDYKFDLMYAKRAFVHWYVGEGMEEGEFTEAREDLAALEKDYEEVGADSNEGGNEEEGEEY
Protein: Guanine nucleotide-binding protein subunit beta-5 (Gbeta5) (Transducin beta chain 5) (P62882)
Organism: Rattus norvegicus (Rat)
Function: Enhances GTPase-activating protein (GAP) activity of regulator of G protein signaling (RGS) proteins, hence involved in the termination of the signaling initiated by the G protein coupled receptors (GPCRs) by accelerating the GTP hydrolysis on the G-alpha subunits, thereby promoting their inactivation (Probable). Increases RGS9 GTPase-activating protein (GAP) activity, hence contributes to the deactivation of G protein signaling initiated by D(2) dopamine receptors (By similarity). May play an important role in neuronal signaling, including in the parasympathetic, but not sympathetic, control of heart rate (By similarity).
Subcellular location: Membrane {ECO:0000250|UniProtKB:P62881}.
Interaction partners:
- Regulator of G-protein signaling 7
- Regulator of G-protein signaling 6
- Regulator of G-protein signaling 9
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Phosducin-like protein
- T-complex protein 1 subunit epsilon
- Adhesion G protein-coupled receptor L1
- Adhesion G protein-coupled receptor L2
Sequence:
MATDGLHENETLASLKSEAESLKGKLEEERAKLHDVELHQVAERVEALGQFVMKTRRTLKGHGNKVLCMDWCKDKRRIVSSSQDGKVIVWDSFTTNKEHAVTMPCTWVMACAYAPSGCAIACGGLDNKCSVYPLTFDKNENMAAKKKSVAMHTNYLSACSFTNSDMQILTASGDGTCALWDVESGQLLQSFHGHGADVLCLDLAPSETGNTFVSGGCDKKAMVWDMRSGQCVQAFETHESDVNSVRYYPSGDAFASGSDDATCRLYDLRADREVAIYSKESIIFGASSVDFSLSGRLLFAGYNDYTINVWDVLKGSRVSILFGHENRVSTLRVSPDGTAFCSGSWDHTLRVWA
Protein: MYB transcription factor (MYB-related transcription factor-like protein) (Myb domain protein 121) (Putative transcription factor MYB121) (Q9LRU5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- At4g07820 superfamily protein)
Sequence:
MLDWGVQGHHQKHDHDIYQQQHQQQGCRKGPWTLEEDKLLAEYVTSHGEGRWSTVAKCAGLNRSGKSCRLRWVNYLRPGLKRGQITPQEEGIILELHSLWGNKWSTIARYLPGRTDNEIKNYWRTHYKKNQKSSSKQDKVKKSLSRKQQQVDLKPQPQAQSENHQSQLVSQDHMNIDNDHNIASSLYYPTSVFDDKLYMPQSVATTSSDHSMIDEGHLWGSLWNLDEDDPHSFGGGSGQGTAADIDEKFPDSGIEAPSCGSGDYSYTGVYMGGYIF
Protein: LD45221p (Minus) (Q9W1N8)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MATIGNKINNSYESEPSTGSGSSLSENNESHISDEDHMNLPYLMKPKALSSQPIKETPTPPNPKTGSQESQFLGFGDSPYGQVNKRLYGSQLQNLKLPEVEPPAVRRPSPGKIVFPRFYDTLIEENSCNAVDMAVSVATTATTTTGSLSFDGKIKSLTAKPEIQDKPGPSNATNPRLSNVLETSLNTSQQKFNNERSPDLFADSDDEADNDEQPEKEPPTRLEDLPEVLEESQCTSDARARSSLNAPTESSFVDEQTMDLSSTQLNANDPRSHFLENCRRERELYRRIRRCLQGVRPPPSVTAPDVDVIKMVLSMKSNVLNFLSKDSPPSTPRIEDSGISETTSLFRPSHSLSEAQNMGWRDVLGVRHHGLSYNLNKAAEQNEYLSMSVVDRYVGVETATSYVRSPSSAKKRNMRMKMLTQSPGNRLSHLAKRRAIFSSANLATNSQKLNSSIGPQIMLDKKKVRNKRKATPKRKTPGSKKKARKTPSSSARKRLYRTDLIKPGPSRETSKRALFQSPAKTLQQQQLMPPKPLFKPEIANRVERSKRALFSPDHQGSSNQLESILKRKRNACDDDEDSADLASQSSKLFRAESSGPSGLTPRALKIKSQSFCIGAGSSTAGVQLKLAQHAAATPGQTRLSLGLSGSSSNLVNPASFASGTPLASKLHRAHSEMSATPNSSMTDNQRKKLLWAVSQALQEKKITPKHEQFRQHAADLTRIVKRIFQEFYLGHSSSNSETLLRLAKKFAFSVIAGKNADDVYLQARSQECEAKRLSSTRLSGYIGPEEFAQRKLLLSQTSVVGSAAGSARSLHNIFGSENSIDSFGLSQMSLPTNACSETQSSIVDRISEDLFCKERQPIRPNASLQNSSSKSNLGGLALRENMDCEARRSAQKNFTGKDQQNISPYFGGGGSNSSARKFQMPPVGNSNHSGGKAKRQISFDC
Protein: ATPase family AAA domain containing 2 (A0A0B4J211)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQKMIPASQRAVTSPGQALSTVVKPLLQNTVDKILEALQRVFPHAEFRTNKTLDSDISCPLLESDLAYSDDDVPSVYENGLSQKSSHKAKDNFNFLHLNRNACYQPMSFRPRILIVGEPGFGQGSHLAPAVIHALEKFTVYTLDIPVLFGVSTTSPEETCAQVIREAKRTAPSIVYVPHIHVWWEIVGPTLKATFTTLLQNIPSFAPVLLLATSDKPHSALPEEVQELFIRDYGEIFNVQLPDKEERTKFFEDLILKQAAKPPISKKKAVLQALEVLPVAPPPEPRSLTAEEVKRLEEQEEDTFRELRIFLRNVTHRLAIDKRFRVFTKPVDPDEVPDYVTVIKQPMDLSSVISKIDLHKYLTVKDYLRDIDLICSNALEYNPDRDPGDRLIRHRACALRDTAYAIIKEELDEDFEQLCEEIQESRKKRGCSSSKYAPSYYHVMPKQNSTLVGDKRSDPEQNEKLKTPSTPVACSTPAQLKRKIRKKSNWYLGTIKKRRKISQAKDDSQNAIDHKIESDTEETQDTSVDHNETGNTGESSVEENEKQQNASESKLELRNNSNTCNIENELEDSRKTTACTELRDKIACNGDASSSQIIHISDENEGKEMCVLRMTRARRSQVEQQQLITVEKALAILSQPTPSLVVDHERLKNLLKTVVKKSQNYNIFQLENLYAVISQCIYRHRKDHDKTSLIQKMEQEVENFSCSR
Protein: KEOPS complex subunit Bud32 (EC 3.6.-.-) (Atypical serine/threonine protein kinase Bud32) (EC 2.7.11.1) (Q9UYB9)
Organism: Pyrococcus abyssi (strain GE5 / Orsay)
Function: Component of the KEOPS complex that is required for the formation of a threonylcarbamoyl group on adenosine at position 37 (t(6)A37) in tRNAs that read codons beginning with adenine. The complex is probably involved in the transfer of the threonylcarbamoyl moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. Bud32 has ATPase activity in the context of the KEOPS complex and likely plays a supporting role to the catalytic subunit Kae1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P53323}.
Interaction partners:
- tRNA N6-adenosine threonylcarbamoyltransferase
- KEOPS complex subunit Cgi121
- KEOPS complex subunit Pcc1
- Threonylcarbamoyl-AMP synthase
Sequence:
MKLIKQGAEAKIYLAEFSELYFDYPIKVIVKERIKKRYRIPEIDLKLRKERTIREARILRRAKEFGVNVPYVFEVDTKNMIIVMEYIEGERLKELLEKLPMEERLKVCREVGRQIGKLHEAGIVHGDLTTSNMILREGKVYFIDFGLAEFDDTIEAQGVDLHLLKRAMESTHYKWFERGFEEVLKGYIEIRGEDKGREIREKIREIELRGRYRERSWITQ
Protein: TRAF family member-associated NF-kappa-B activator (TRAF-interacting protein) (I-TRAF) (P70347)
Organism: Mus musculus (Mouse)
Function: Adapter protein involved in I-kappa-B-kinase (IKK) regulation which constitutively binds TBK1 and IKBKE playing a role in antiviral innate immunity. Acts as a regulator of TRAF function by maintaining them in a latent state. Blocks TRAF2 binding to LMP1 and inhibits LMP1-mediated NF-kappa-B activation. Negatively regulates NF-kappaB signaling and cell survival upon DNA damage. Plays a role as an adapter to assemble ZC3H12A, USP10 in a deubiquitination complex which plays a negative feedback response to attenuate NF-kappaB activation through the deubiquitination of IKBKG or TRAF6 in response to interleukin-1-beta (IL1B) stimulation or upon DNA damage. Promotes UBP10-induced deubiquitination of TRAF6 in response to DNA damage. May control negatively TRAF2-mediated NF-kappa-B activation signaled by CD40, TNFR1 and TNFR2. Essential for the efficient induction of IRF-dependent transcription following infection with Sendai virus.
Subcellular location: Cytoplasm.
Interaction partners:
- TNF receptor-associated factor 3
- Inhibitor of nuclear factor kappa-B kinase subunit epsilon
- Serine/threonine-protein kinase TBK1
- NF-kappa-B essential modulator
- Tumor necrosis factor receptor type 1-associated DEATH domain protein
- TANK-binding kinase 1-binding protein 1
- Tumor necrosis factor
- Tumor necrosis factor receptor superfamily member 1A
- TNF receptor-associated factor 6
- 5-azacytidine-induced protein 2
Sequence:
MSLKRHSLRRNACHLETRAGIPTILYSDATGQRGMDKNIGEQLNRAYEAFRQACMDRDSAVRELQQKQTENYEQRIREQQEQLSFQQNLIDRLKSQLLLVDSSRDNSYGYVPLLEDSDRRKNNLTLDEPHDKVKLGTLRDKQSKVRRQEVSSGKESAKGLNIPLHHERDNIEKTFWDLKEEFHRICLLAKAQKDHLSKLNIPDIATDTQCSVPIQCTDKTEKQEALFKPQAKDDINRGMSCVTAVTPRGLGRDEEDTSFESLSKFNVKFPPMDNDSIFLHSTPEAPSILAPATPETVCQDRFNMEVRDNPGNFVKTEETLFEIQGIDPITSAIQNLKTTDKTNPSNLRATCLPAGDHNVFYVNTFPLQDPPDAPFPSLDSPGKAVRGPQQPFWKPFLNQDTDLVVPSDSDSELLKPLVCEFCQELFPPSITSRGDFLRHLNTHFNGET
Protein: DNA-(apurinic or apyrimidinic site) lyase (EC 4.2.99.18) (E5KPM6)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQSPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYFQLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNNNIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLGLGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKGLLGNAFDGHQLLRPLIFCQDHLREGPPIGRGDSQGEELEPQLPSSLSSIPYGFCDHCWTKDVDDPPLVTHPSPGSRDGHMTQAWPVKVVSPLATVIGHVMQASLLAL
Protein: Cyclic nucleotide-gated channel alpha-3 (CNG channel alpha-3) (CNG-3) (CNG3) (Cone photoreceptor cGMP-gated channel subunit alpha-3) (Gustatory cyclic nucleotide-gated cation channel) (CNGgust) (Q9ER33)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q16281}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Cyclic nucleotide gated channel subunit beta 3
- Cyclic nucleotide-gated channel subunit beta 1.
- Phosphodiesterase
- G protein subunit alpha transducin 2
- Phosphodiesterase
- Melanopsin
- Guanylate cyclase 2D
- Retinal cone rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma
- Sodium/potassium/calcium exchanger 1
- Gametogenetin
Sequence:
MAKVNTQCSQPSPRQLSVKDAADRDLDQVENGLGRSHSPCEETSSTVHQGIVMETGELAGAAQSLFTSQGPARVSRFIISIRAWAARHLHHEDPTPDSFLDRFHGAELKEVSSQERNAQPNPGGQEPPEGGKGRKKDPIVVDPSSNIYYRWLTAIALPVFYNWCLLVCRACFDELQSEHLTLWLVLDYSADALYVVDMLVRARTGFLEQGLMVRDTKRLWKHYTKTLHFKLDILSLIPTDLAYLKLGMNYPELRFNRLLRFSRLFEFFDRTETRTNYPNVFRIGNLVLYTLIIIHWNACIYFAISKFIGFGTDSWVYPNTSKPEYGRLSRKYIYSLYWSTLTLTTIGETPPPVKDEEYLFVVIDFLVGVLIFATIVGNVGSMISNMNASRAEFQAKIDSIKQYMQFRKVTKDLETRVIRWFDYLWANRKTVDEKEVLKNLPDKLKAEIAINVHLDTLKKVRIFQDCEAGLLVELVLKLRPAVFSPGDYICKKGDIGREMYIIKEGKLAVVADDGVTQFVVLSDGSYFGEISILNIKGSKSGNRRTANIRSIGYSDLFCLSKDDLMETLTEYPDAKRALEEKGRQILMKDNLIDDDLVTARADARNIEEKVEYLESSLDGLQTRFARLLAEYSASQMKLKQRLSQLESQMTRRGHGFSPDRENSEDASKAD
Protein: Induced myeloid leukemia cell differentiation protein Mcl-1b (Mcl1b protein) (Myeloid cell leukemia sequence 1b) (Q568W5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MFAGRNNDNGFWPCTGLQSKPLVIPELKAHNQFAVDSLQGSVPSSPSDETGDYPPTALDMDTREIIDTFLIIFTGLPHSKSGRKQVLSTMRRVVDNLAVKHELAYKGMIARLNLEQKGEDVSFIKQVATELFSDGTTNWGRIASLLTFGAMLCKYQNDRGHSKYVRLVGEEISSYLLTEQRDWILRNKAWDGFVEFFHVPDTEAAVRNTLLTIGGVATLSAALAYWIR
Protein: UDP-glycosyltransferase 76C5 (EC 2.4.1.-) (Q9FI97)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Gamma-soluble NSF attachment protein
- Nicotinate N-methyltransferase 1
- Copper ion binding protein
- Phosphoglycerate mutase family protein
- Leucine-rich repeat
- Nicotinate phosphoribosyltransferase 2
- Nicotinate phosphoribosyltransferase 1
- Insecticidal crystal toxin domain-containing protein
- Expressed protein
- Glycine-rich protein 3 short isoform
Sequence:
MEKSNGLRVILFPLPLQGCINPMIQLAKILHSRGFSITVIHTCFNAPKASSHPLFTFLEIPDGLSETEKRTNNTKLLLTLLNRNCESPFRECLSKLLQSADSETGEEKQRISCLIADSGWMFTQPIAQSLKLPILVLSVFTVSFFRCQFVLPKLRREVYLPLQDSEQEDLVQEFPPLRKKDIVRILDVETDILDPFLDKVLQMTKASSGLIFMSCEELDHDSVSQAREDFKIPIFGIGPSHSHFPATSSSLSTPDETCIPWLDKQEDKSVIYVSYGSIVTISESDLIEIAWGLRNSDQPFLLVVRVGSVRGREWIETIPEEIMEKLNEKGKIVKWAPQQDVLKHRAIGGFLTHNGWSSTVESVCEAVPMICLPFRWDQMLNARFVSDVWMVGINLEDRVERNEIEGAIRRLLVEPEGEAIRERIEHLKEKVGRSFQQNGSAYQSLQNLIDYISSF
Protein: Protein SAN1 (P22470)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Plays a specific role in mating-type regulation of yeast, by acting post-translationally to control the stability or activity of the SIR4 proteins.
Interaction partners:
- E3 ubiquitin-protein ligase UBR1
- ERAD-associated E3 ubiquitin-protein ligase DOA10
- FACT complex subunit SPT16
- Regulatory protein SIR4
- Cell division control protein 13
- E3 ubiquitin-protein ligase HUL5
- ERAD-associated E3 ubiquitin-protein ligase HRD1
- E3 ubiquitin-protein ligase UBR2
- Ubiquitin-conjugating enzyme E2 1
- Heat shock protein SSA1
Sequence:
MSESGQEQNRGTNTSPNNAENNNNSNAASGPLNGGAEQTRNITVSIQYSYFTPERLAHLSNISNNDNNENNSAASGSTIANGTGPSFGIGNGGHQPDGALVLSFRDVPASTPQDRLNSFISVAAQLAMERFNRLLNRPKGISKDEFDKLPVLQVSDLPKAEGPLCSICYDEYEDEVDSTKAKRKRDSENEEESEGTKKRKDNEGAPLRTTADNDSNPSITNATVVEPPSIPLTEQQRTLNDEETNPSYKHSPIKLPCGHIFGRECIYKWSRLENSCPLCRQKISESVGVQRAAQQDTDEVAANEAAFERIRRVLYDPTAVNSTNENSSAPSENTSNTTVPTIGNASSGEQMLSRTGFFLVPQNGQPLHNPVRLPPNDSDRNGVNGPSSTTQNPPSNSGGSNNNQSPRWVPIPLTLFQFHSPNPNPSASDSSASPSAANGPNSNNTSSDATDPHHNRLRAVLDHIFNVAQRGTSDTSATTAPGAQTVHNQGRNDSSSSDTTQGSSFLENISRLTGHFTNGSRDNNNDNNHSNDQQRGGSTGENNRNNLFSSGVASYRNQNGDVTTVELRNNNSAAFPPTDENPSQGQGSSSSDTTIHNDVPNDNNEQRSSQ
Protein: Cystathionine gamma-synthase (Eurofung) (C8VHB0)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Homocysteine synthase
- Cystathionine beta-synthase
- Cystathionine beta-lyase
- 5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase
- Cysteine synthase 1
- Homocysteine S-methyltransferase
- cystathionine gamma-lyase
- Sulfite reductase subunit beta
- Cysteine synthase 2
- Homoserine O-acetyltransferase
Sequence:
MTHRSDEALIKFQYDWPAAFMLIAEIAAHFLICRHNSSQNSGLQGQFSPSSYTLSHIAGAAGQFDLETRVLSPKIMLQEPGGPVPPNTDHAVSVSLPTWEANVAYEEGELWLVNKMQCGYPRFFVHPIIQELAQEIVARFGNPEYEATTLFPSPNTARVCHTFILSRISREEAHKIRVLDFVPTKELETELSTIQSLLSCVIYPKEHAKIAKQAWQHTGDGVSSRRGEFCLGALKDGLLTERKNVTGDATRQIIHKGPRRYQGKGSINGIGKVSSHNAVSANKPHEGRESVQFIEERFGRNLSTSLASKAKIAVRRRIAGVLTADVELNEALEKASQEGRVAGLSESDVFLFPSGMSSIFNSHRLLLEARGSMKSVCFGFPYIDTLKILEKWGPGCVFYGRGSSEDLNDLEARLAGGERFLALFTEFPGNPLLKTPDLKRIRALANKYEFAVVVDETVGNFLNINVLSHADIVVSSLTKIFSGDSNVMGGSAVLNPHGRYYPLLKDTFNRGYEDNLWVEDAVFLERNSRDFVSRIEKINHTTEVITAMLQESPIVKNVYYPKFSPTLPFYEAFRTPNGGYGGLFSVTFHSTAEAIAFFDNLEVHKGPSLGTNFTLSSPYTLLAHYSELDWASSFGVEFDLVRISVGLEDVPLLRAKVQQALDAVAKISK
Protein: Protein virE1 (7.1 kDa virulence protein) (P08063)
Organism: Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens (strain C58))
Function: Involved in DNA transformation; controls virE2 polymerization and prevents virE2 binding to DNA.
Interaction partners:
Sequence:
MVIIKLNANKNMPVLAVEKPQEIHKEELSDHHQSNGFTSLDLEMIELENFVLHCPLPEENLAG