wanglab/gogpt-training-data huggingface dataset:
Protein: Kinetochore-associated protein 1 isoform X1 (A0A1L8I190)
Organism: Xenopus laevis (African clawed frog)
Interaction partners:
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Uncharacterized protein.
- Dual specificity protein kinase TTK
- Kinesin motor domain-containing protein
- Kinesin motor domain-containing protein
- Abnormal spindle-like microcephaly-associated protein homolog isoform X3
- Uncharacterized protein.
Sequence:
MWNDIELLANDDTGSCRLNIDSRQESGTALYQVDTLLKISSHEKIQCNPQLFACSSNEGCVIVADRSVSLLDSICQSLQLQLQFDTEVDVVGLCHEGQFLLVGERNGNIHLIHVLSRQILITKPLVPNGSKTNEQTYQKLLLERDSSDEGVYHVFVLTNGGLYCIMYFHLAQINEAIENMDFSSSKELEGKIKTCFISTEQYHTSGCLNLVIGDLMSDIHLIIGGKGDYVLSKWKMDPIKKHIALQGLADSSMIQGAKKFQVLNNLLFVLDEDDILSVWDVYTLVMVWDWTSCRISDFLLSTEGDSLSSVSQQRHANLKLVALTVPNTKQMRNLTVYSLPAMNLLYSIEVSDLSTLVQTGINMDTIYLLEGIYDSHERTPDCTVSVLALRCLTEALPENRLSRLLHKHRFEEAENFAIQFGLDVELVYKVKLNIVLEKLASASIGSYGQILWQEMVDEAKANLQKIKDDNFVVEYCINAPWPTYETTLDMLNYAKARILRKEEKTLPASSDDLQVSITDVLRAQARLTTFYSAFGAEKFSGIAWTEFLNNEDILKDILFQLEEINLPCAQYLWLRHQGEFESKFDEKMLEILLNTIPANIPSHELCPWFKNILIPFVRRIVPKGQRIITKWLEHRARGLELTDKANWPENGYEMAEVYFVSKNPGELGLASSWLWIPLKEDGDCEEVQQLMKLVTNLQELVELYRKYNCKLVLSDFEKETTVTIVFRMLDKVLAPELIPSTLEKVIRPYMYQHNLQEEELLLQYIKDLLERCSSRSASLFETAWEAKAMAVISCMSDTDLIFDAVLQIMYGAVVPWSDAVEQLVKQHLEMDHPKVKLLQESYRLMEMNKLLRGYGIRGFNLANEKQIMSLVKYILKQDSPSSLEDALKIFQAYMLPSVEVYIIRIVQLIYMNRGDDCLNLLKSLTPAEAEITIERLSLWARIALQENLGGSDECKEDQKMIAKTLVEILKFQMCAQNENLLKSELCEANLQMFEAISSLQEDFDIFLSLEDYENRSLVSQLRDEHIIAYETTKSKSKSGKPSELHPTFDENTKIPSTESRLYRLALLLQVTEQELGAELALRALAIGKVEKALQICRDLYEHHCNPQTGHLLFLVSQKLSDMLEANTPMVIPAGMNLPAVIYEMSCQASTICSPDLLLDALELCKYTQLAMEFYKQCQIEDYGFMAKTATFGADRDQYEEWTYEDYFSEDGIVLDPLVVLPVAYDITTALVPSTAGKKMYPLDCACLANCSYVKGKNFLLPAKTPISALVENLQECSQCELTLRLVIRTFGTCLQHGVSNNMENRLSAKLYDEKVLAETKAFIFAFGEKIATLIKDTAMALLHKVFNCRVVDCDLALGYCTLLSKSEVFKKLWDVINNAWQNYTKIQAVAVVGAQLSLLYNEEEEKMKFEDLITDAEWGLQLSNFGISFQSVFRQRSERKKELLGTLVQSSHVDTALILKYCSTFKLDSDAALQLYIETLLLSASNFKHGEDDSTKDFVQTSNSDPVTKAKEIIPLLKSTQHLVVSLSGILDKLDPYDYETIEGVLQVIIVADEKNTYIQLSQAIGLINHLKSYKRIAPPSDLEHQYIMEHGLSMPPTAQTRLPFHLLFFKTVSSFWGIISAELSEESFPTLLLISKLMKVSLDTLYMMASKHVFEKNLRPKALKLKNAEHCSIITKETARTVLTIQSYLQSISNPEWAAAIAHKIAQELPTGPDKIHALKFCLHLAEKWKKNVSSENDAHEKADVFIKKLSVQYQRSATENVLITHKLNTPELLKQIGKPANLIVSLYEHSSVEQRIRHPTGRDYPDIHTAAKQISEVNNLNMSKICTLLLEKWICPPAVPQADKNKDVFGDIHGDEDLRRVIYLLQPYPVDYSSRMLYAIATSATSPIGDNQLTYAHRSRALQCLIHLADTDTVISLIKKPIDQVKYYLKCCIYLSEFEFLNIPYTLESFHSSPKEGMIKGLWKNHSHEPRAVKLVTELSLEYKVYDPQLWGGLLQKILGFNLMHYLRKVLVAISGVHCLWEIPNFSRAWRSAILSPFVTASCPPSPSQMEECYECFVVLLKCPVLADLDVVGIAKQYAQIDLPAFTLGCLLLIPHMEKKEQQIQGFLSTCNPETVLQQVADCMNTGEVAGFASQIRDLILSNIIEKHQIERFVKTKYFSMLKRQAIQSDRVRSIAECLANTHCWDEAADLVKEYLKCRGKPIQKNATSADTVKAFLNDHSDI
Protein: Calcium/calmodulin-dependent protein kinase type 1G (EC 2.7.11.17) (CaM kinase I gamma) (CaM kinase IG) (CaM-KI gamma) (CaMKI gamma) (CaMKIG) (CaMK-like CREB kinase III) (CLICK III) (Q7TNJ7)
Organism: Rattus norvegicus (Rat)
Function: Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade. In vitro phosphorylates transcription factor CREB1 (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Nitric oxide synthase 3
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Calcium/calmodulin-dependent protein kinase type II subunit beta
- Calcium/calmodulin-dependent protein kinase type II subunit delta
- Cyclic AMP-responsive element-binding protein 1
- calcium/calmodulin-dependent protein kinase
Sequence:
MGRKEEEDCSSWKKQTTNIRKTFIFMEVLGSGAFSEVFLVKQRVTGKLFALKCIKKSPAFRDSSLENEIAVLKRIKHENIVTLEDIYESTTHYYLVMQLVSGGELFDRILERGVYTEKDASLVIQQVLSAVKYLHENGIVHRDLKPENLLYLTPEENSKIMITDFGLSKMEQNGVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESKLFEKIKEGYYEFESPFWDDISESAKDFICHLLEKDPNERYTCEKALRHPWIDGNTALHRDIYPSVSLQIQKNFAKSKWRQAFNAAAVVHHMRKLHMNLHSPSVRQEVENRPPVSPAPEVSRPGSHDSSITEAPILDPSTPLPALTRLPCSHSSRPSAPGGRSLNCLVNGSLRISSSLVPMQQGPLATGPCGCCSSCLNIGNKGKSSYCSEPTLFRKANKKQNFKSEVMVPVKAGGSTHCRAGQTGVCLIM
Protein: Transmembrane inner ear (Q9XXE7)
Organism: Caenorhabditis elegans
Interaction partners:
- Transmembrane channel-like protein 1
- Arrestin C-terminal-like domain-containing protein
- EF-hand domain-containing protein
Sequence:
MPSGNEEINHLSALDQFVAPGLRLWMLIALVGGVLLIMIVIVCCFMRIRIPRTKRQIDLIAAKRKLRKSTKNSAEANAHNDERAQAIVMNSMPSGGGGGAPSTSSSRHTGSRIQSQV
Protein: Inactive adenylate kinase (Adenylate kinase-like protein 2) (C0H582)
Organism: Plasmodium falciparum (isolate 3D7)
Function: Lacks adenylate kinase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:22819813}.
Interaction partners:
- Bifunctional dihydrofolate reductase-thymidylate synthase
- Guanylate kinase
- ATP synthase subunit gamma
Sequence:
METLLHSEILKKYKEETNEYIKKKNVEKLFDIILKNVLINKPDNIYLYIYNNIYSFLLNKIFIMGPPVLKITSMLSSHISEFFNYYHISLPILIQQYKLNKGESSNNKIIVNDEIISFILKENIHNLDSKKKKGYIVEGYPNNNLQAYSCLKYLPSHVFVLYADEEYIYKKYEEENDIAIFSYTQKKDYDINEPHEINNIDVKPLKDQVLSYIRNISDMLTILGTNKKVLNLHDFNDQMLIDHVKNEVSKNKDEWDSTLNGDI
Protein: Secreted frizzled-related protein 5 (sFRP-5) (Q9WU66)
Organism: Mus musculus (Mouse)
Function: Soluble frizzled-related proteins (sFRPS) function as modulators of Wnt signaling through direct interaction with Wnts. They have a role in regulating cell growth and differentiation in specific cell types. SFRP5 may be involved in determining the polarity of photoreceptor, and perhaps, other cells in the retina.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Protein Wnt-11
- Protein Wnt-5a
- Protein Wnt-3a
- Protein Wnt-10b
- Protein Wnt-5b
- Protein Wnt-2
- Protein Wnt-7b
- Protein Wnt-8b
- Proto-oncogene Wnt-1
- Proto-oncogene Wnt-3
Sequence:
MWVAWSARTAALALLLGALHGAPTRGQEYDYYGWQAEPLHGRSYSKPPQCLDIPADLPLCHTVGYKRMRLPNLLEHESLAEVKQQASSWLPLLAKRCHSDTQVFLCSLFAPVCLDRPIYPCRSLCEAARAGCAPLMEAYGFPWPEMLHCHKFPLDNDLCIAVQFGHLPATAPPVTKICAQCEMEHSADGLMEQMCSSDFVVKMRIKEIKIDNGDRKLIGAQKKKKLLKAGPLKRKDTKKLVLHMKNGASCPCPQLDNLTGSFLVMGRKVEGQLLLTAVYRWDKKNKEMKFAVKFMFSYPCSLYYPFFYGAAEPH
Protein: Protocadherin beta-2 (PCDH-beta-2) (Q9Y5E7)
Organism: Homo sapiens (Human)
Function: Potential calcium-dependent cell-adhesion protein. May be involved in the establishment and maintenance of specific neuronal connections in the brain.
Subcellular location: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
- Protocadherin beta-5
Sequence:
MEAGEGKERVPKQRQVLIFFVLLGIAQASCQPRHYSVAEETESGSFVANLLKDLGLEIGELAVRGARVVSKGKKMHLQFDRQTGDLLLNEKLDREELCGPTEPCVLPFQVLLENPLQFFQAELRIRDVNDHSPVFLDKEILLKIPESITPGTTFLIERAQDLDVGTNSLQNYTISPNFHFHLNLQDSLDGIILPQLVLNRALDREEQPEIRLTLTALDGGSPPRSGTALVRIEVVDINDNVPEFAKLLYEVQIPEDSPVGSQVAIVSARDLDIGTNGEISYAFSQASEDIRKTFRLSAKSGELLLRQKLDFESIQTYTVNIQATDGGGLSGTCVVFVQVMDLNDNPPELTMSTLINQIPENLQDTLIAVFSVSDPDSGDNGRMVCSIQDDLPFFLKPSVENFYTLVISTALDRETRSEYNITITVTDFGTPRLKTEHNITVLVSDVNDNAPAFTQTSYTLFVRENNSPALHIGSVSATDRDSGTNAQVTYSLLPPQDPHLPLASLVSINADNGHLFALQSLDYEALQAFEFRVGAADRGSPALSSEALVRVLVLDANDNSPFVLYPLQNGSAPCTELVPRAAEPGYLVTKVVAVDGDSGQNAWLSYQLLKATEPGLFGVWAHNGEVRTARLLRERDAAKQRLVVLVKDNGEPPRSATATLHVLLVDGFSQPYLLLPEAAPAQAQADLLTVYLVVALASVSSLFLFSVLLFVAVRLCRRSRAASVGRCSVPEGPFPGQMVDVSGTGTLSQSYQYEVCLTGGSGTNEFKFLKPIIPNFVAQGAERVSEANPSFRKSFEFT
Protein: D-aminoacyl-tRNA deacylase (PfDTD) (EC 3.1.1.96) (D-Tyrosyl-tRNA(Tyr) deacylase) (Gly-tRNA(Ala) deacylase) (Gly-tRNA(Gly) deacylase) (Q8IIS0)
Organism: Plasmodium falciparum (isolate 3D7)
Function: D-aminoacyl-tRNA deacylase, with no observable activity on tRNAs charged with their cognate L-amino acid. Probably acts by rejecting L-amino acids from its binding site rather than specific recognition of D-amino acids. Catalyzes the hydrolysis of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-tRNA(Tyr). Hydrolyzes correctly charged, achiral, glycyl-tRNA(Gly). Deacylates mischarged D.melanogaster and E.coli glycyl-tRNA(Ala). Probably acts via tRNA-based rather than protein-based catalysis. Acts on tRNAs only when the D-amino acid is either attached to the ribose 3'-OH or transferred to the 3'-OH from the 2'-OH through rapid transesterification. Binds a number of other D-amino acids (D-Arg, D-Glu, D-His, D-Lys, D-Ser), suggesting it may also deacylate other mischarged tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:20007323}.
Interaction partners:
- threonine--tRNA ligase
- glycine--tRNA ligase
- Tyrosine--tRNA ligase
- tyrosine--tRNA ligase
- 4a-hydroxytetrahydrobiopterin dehydratase
Sequence:
MRVVIQRVKGAILSVRKENIGENEKELEIISEIKNGLICFLGIHKNDTWEDALYIIRKCLNLRLWNNDNKTWDKNVKDLNYELLIVSQFTLFGNTKKGNKPDFHLAKEPNEALIFYNKIIDEFKKQYNDDKIKIGKFGNYMNIDVTNDGPVTIYIDTHDINLNK
Protein: Uracil phosphoribosyltransferase (EC 2.4.2.9) (UMP pyrophosphorylase) (UPRTase) (P9WFF3)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate.
Interaction partners:
- Orotidine 5'-phosphate decarboxylase
- Thymidine phosphorylase
- Bifunctional protein PyrR
- Purine nucleoside phosphorylase
- Uridylate kinase
- GMP synthase
- Adenine phosphoribosyltransferase
- Ribose-5-phosphate isomerase B
- Cytidine deaminase
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MQVHVVDHPLAAARLTTLRDERTDNAGFRAALRELTLLLIYEATRDAPCEPVPIRTPLAETVGSRLTKPPLLVPVLRAGLGMVDEAHAALPEAHVGFVGVARDEQTHQPVPYLDSLPDDLTDVPVMVLDPMVATGGSMTHTLGLLISRGAADITVLCVVAAPEGIAALQKAAPNVRLFTAAIDEGLNEVAYIVPGLGDAGDRQFGPR
Protein: Propionate catabolism operon regulatory protein (P77743)
Organism: Escherichia coli (strain K12)
Function: Involved in the transcriptional regulation of the propionate catabolism operon.
Interaction partners:
- RNA polymerase sigma-54 factor
- 2-methylcitrate dehydratase
- 2-methylisocitrate lyase
Sequence:
MAHPPRLNDDKPVIWTVSVTRLFELFRDISLEFDHLANITPIQLGFEKAVTYIRKKLANERCDAIIAAGSNGAYLKSRLSVPVILIKPSGYDVLQALAKAGKLTSSIGVVTYQETIPALVAFQKTFNLRLDQRSYITEEDARGQINELKANGTEAVVGAGLITDLAEEAGMTGIFIYSAATVRQAFSDALDMTRMSLRHNTHDATRNALRTRYVLGDMLGQSPQMEQVRQTILLYARSSAAVLIEGETGTGKELAAQAIHREYFARHDARQGKKSHPFVAVNCGAIAESLLEAELFGYEEGAFTGSRRGGRAGLFEIAHGGTLFLDEIGEMPLPLQTRLLRVLEEKEVTRVGGHQPVPVDVRVISATHCNLEEDMQQGRFRRDLFYRLSILRLQLPPLRERVADILPLAESFLKVSLAALSAPFSAALRQGLQASETVLLHYDWPGNIRELRNMMERLALFLSVEPTPDLTPQFMQLLLPELARESAKTPAPRLLTPQQALEKFNGDKTAAANYLGISRTTFWRRLKS
Protein: Potassium channel toxin alpha-KTx 6.15 (Hemitoxin) (P85528)
Organism: Hemiscorpius lepturus (Scorpion)
Function: Blocks voltage-gated potassium channels rKv1.1/KCNA1 (IC(50)=13 nM), rKv1.2/KCNA2 (IC(50)=16 nM) and rKv1.3/KCNA3 (IC(50)=2 nM).
Subcellular location: Secreted {ECO:0000269|PubMed:18699777}.
Interaction partners:
Sequence:
IKCTLSKDCYSPCKKETGCPRAKCINRNCKCYGCS
Protein: Ankyrin 3 (A0A087WTF3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
XFLVSFMVDARGGSMRGSRHHGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLGPVIVEIPHFGSMRGKERELIVLRSENGETWKEHQFDSKNEDLTELLNGMDEELDSPEELGKKRICRIITKDFPQYFAVVSRIKQESNQIGPEGGILSSTTVPLVQASFPEGALTKRIRVGLQAQPVPDEIVKKILGNKATFSPIVTVEPRRRKFHKPITMTIPVPPPSGEGVSNGYKGDTTPNLRLLCSITGGTSPAQWEDITGTTPLTFIKDCVSFTTNVSARFWLADCHQVLETVGLATQLYRELICVPYMAKFVVFAKMNDPVESSLRCFCMTDDKVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNFYSFKENRLPFSIKIRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLPAHKKIEKTDRRQSFASLALRKRYSYLTEPGMKTVERSTGATRSLPTTYSYKPFFSTRPYQSWTTAPITVPGPAKSGFTSLSSSSSNTPSASPLKSIWSVSTPSPIKSTLGASTTSSVKSISDVASPIRSFRTMSSPIKTVVSQSPYNIQVSSGTLARAPAVTEATPLKGLASNSTFSSRTSPVTTAGSLLERSSITMTPPASPKSNINMYSSSLPFKSIITSAAPLISSPLKSVVSPVKSAVDVISSAKITMASSLSSPVKQMPGHAEVALVNGSISPLKYPSSSTLINGCKATATLQEKISSATNSVSSVVSAATDTVEKVFSTTTAMPFSPLRSYVSAAPSAFQSLRTPSASALYTSLGSSISATTSSVTSSIITVPVYSVVNVLPEPALKKLPDSNSFTKSAAALLSPIKTLTTETHPQPHFSRTSSPVKSSLFLAPSALKLSTPSSLSSSQEILKDVAEMKEDLMRMTAILQTDVPEEKPFQPELPKEGRIDDEEPFKIVEKVKEDLVKVSEILKKDVCVDNKGSPKSPKSDKGHSPEDDWIEFSSEEIREARQQAAASQSPSLPERVQVKAKAASEKDYNLTKVIDYLTNDIGSSSLTNLKYKFEDAKKDGEERQKRVLKPAIALQEHKLKMPPASMRTSTSEKELCKMADSFFGTDTILESPDDFSQHDQDKSPLSDSGFETRSEKTPSAPQSAESTGPKPLFHEVPIPPVITETRTEVVHVIRSYDPSAGDVPQTQPEEPVSPKPSPTFMELEPKPTTSSIKEKVKAFQMKASSEEDDHNRVLSKGMRVKEETHITTTTRMVYHSPPGGEGASERIEETMSVHDIMKAFQSGRDPSKELAGLFEHKSAVSPDVHKSAAETSAQHAEKDNQMKPKLERIIEVHIEKGPQSPCERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEGPIFDYGNISGTRSFADENNVFHDPVDGWQNETSSGNLESCAQARRVTGGLLDRLDDSPDQCRDSITSYLKGEAGKFEANGSHTEITPEAKTKSYFPESQNDVGKQSTKETLKPKIHGSGHVEEPASPLAAYQKSLEETSKLIIEETKPCVPVSMKKMSRTSPADGKPRLSLHEEEGSSGSEQKQGEGFKVKTKKEIRHVEKKSHS
Protein: Nanos-type domain-containing protein (O62486)
Organism: Caenorhabditis elegans
Interaction partners:
- Fem-3 mRNA-binding factor 1
- PUM-HD domain-containing protein
- Fem-3 mRNA-binding factor 2
- CCR4-NOT transcription complex subunit let-711
- PUM-HD domain-containing protein
- Defective in germ line development protein 3
- Poly
- FOG-1 protein
- Female germline-specific tumor suppressor gld-1
- Anti-proliferative protein domain-containing protein
Sequence:
MSGQQFQQHSQQQQQRAPTVYNNNNKKNGGSAANSNQNNNNPHHTSTTDSVPNSTANVSSAISFEYSEPPGNTTRTTPDSGLGTDDQKGTPQQTRAPPGFHRAAYHRNSGQQQFSQMRPQPPHTGPPNGMTYYGGTVGAPGYQQQQPPPQEGYDQQQQFGGGSDGGQYQRGPPGGYRQYQQMESGGPPSGYADDNNGGNNNFVIHGPNDNFDGRPQYNPQAGPPPQNQQQMMNSGNYEIDQYRGQGPPPGNTYQQQGHSGQAQYYAGPVIQQRPPPPHNAQSYGQYRGPQGPQGQIIQMMPHNPQNQQQQQQHPMLYPMVYVPVPAPRVFRQEPAGGASSLEKDGGNARKSKRNSQNEDDGQQHQHQNEQQPQQGYHQQDFVSNPLWNQMPVGYAPPGNFTQPQQQHQQMDQQQAVQMQHQMQMFQQMQPYGMPQGGPPPPHAAASMMNHPHQQNHPHMNAQMTQQQHPGQYLPQQYMQMVPPPHHQMQQMQQQGRRPGGVEPLMGGPPYQMSGQINQMGGPIRGGFGMQQQQPMGYFNSGRGGNAGSGRGRGGSRGHGYQHSRQNSNQSYNSSQSYPQNRGNFDSSSQYQSDSQQVDESVTQLTNRIEHLQPVSSRAGSPSKQILQLVESKDDQTSTENSESPSRSSTPKHRKKTPKKDFKVDQEASIEATKTEISEENPKTDDIQSKDDVTSKSELHCYRCEHYQLPAEEVSSHNIRKDNGDLWCEHMKKIKCGHCEATGEQGHHPLICPKKKEEERVAKSRESSQKPIDPQEISDDQDDTVPDVPDQIVEQDNQSHKSRHNSENRSGGRGYGQNYSHSYGGNSTGSYRGRSSGGSGGSGRGGGRGGYSRGHGGGSGGGQRGNYQNKRK
Protein: UDP-glycosyltransferase 708D1 (EC 2.4.1.360) (UDP-glucose:2-hydroxyflavanone C-glucosyltransferase) (I1L3T1)
Organism: Glycine max (Soybean) (Glycine hispida)
Function: UDP-glucose-dependent glucosyltransferase catalyzing the c-glucosylation of the A ring of 2-hydroxynaringenin. Also active toward phloretin, but not toward naringenin and apigenin.
Interaction partners:
Sequence:
MSSSEGVVHVAFLPSAGMGHLNPFLRLAATFIRYGCKVTLITPKPTVSLAESNLISRFCSSFPHQVTQLDLNLVSVDPTTVDTIDPFFLQFETIRRSLHLLPPILSLLSTPLSAFIYDITLITPLLSVIEKLSCPSYLYFTSSARMFSFFARVSVLSASNPGQTPSSFIGDDGVKIPGFTSPIPRSSVPPAILQASSNLFQRIMLEDSANVTKLNNGVFINSFEELEGEALAALNGGKVLEGLPPVYGVGPLMACEYEKGDEEGQKGCMSSIVKWLDEQSKGSVVYVSLGNRTETRREQIKDMALGLIECGYGFLWVVKLKRVDKEDEEGLEEVLGSELSSKVKEKGVVVKEFVDQVEILGHPSVGGFLSHGGWNSVTETVWKGVPCLSWPQHSDQKMSAEVIRMSGMGIWPEEWGWGTQDVVKGDEIAKRIKEMMSNESLRVKAGELKEAALKAAGVGGSCEVTIKRQIEEWKRNAQAN
Protein: Cysteine-rich receptor-like protein kinase 29 (Cysteine-rich RLK29) (EC 2.7.11.-) (Q8S9L6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 705A1
- Protein ROH1A
- Plant intracellular Ras-group-related LRR protein 2
Sequence:
MEHVRVIFFFACFLTLAPFHAFAQVDSYEFDPDFNCVDRGNFTANSTFAGNLNRLVSSLSSLKSQAYGFYNLSSGDSSGERAYAIGLCRREVKRDDCVSCIQTAARNLTKQCPLTKQAVVWYTHCMFRYSNRTIYGRKETNPTKAFIAGEEISANRDDFERLQRGLLDRLKGIAAAGGPNRKYAQGNGSASAGYRRFYGTVQCTPDLSEQDCNDCLVFGFENIPSCCDAEIGLRWFSPSCNFRFETWRFYEFDADLEPDPPAIQPADSPQSAARTERTGKGKGGSKVIIAIVIPILLVALLAICLCLVLKWRKNKSGYKNKVLGKSPLSGSIAEDEFSNTESLLVHFETLKTATDNFSSENELGRGGFGSVYKGVFPQGQEIAVKRLSGNSGQGDNEFKNEILLLAKLQHRNLVRLIGFCIQGEERLLVYEFIKNASLDQFIFDTEKRQLLDWVVRYKMIGGIARGLLYLHEDSRFRIIHRDLKASNILLDQEMNPKIADFGLAKLFDSGQTMTHRFTSRIAGTYGYMAPEYAMHGQFSVKTDVFSFGVLVIEIITGKRNNNGGSNGDEDAEDLLSWVWRSWREDTILSVIDPSLTAGSRNEILRCIHIGLLCVQESAATRPTMATVSLMLNSYSFTLPTPLRPAFVLESVVIPSNVSSSTEGLQMSSNDVTVSEFSPR
Protein: Ragulator complex protein LAMTOR3 (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 3) (Mitogen-activated protein kinase kinase 1-interacting protein 1) (Q5U204)
Organism: Rattus norvegicus (Rat)
Function: As part of the Ragulator complex it is involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids. Activated by amino acids through a mechanism involving the lysosomal V-ATPase, the Ragulator functions as a guanine nucleotide exchange factor activating the small GTPases Rag. Activated Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated. Adapter protein that enhances the efficiency of the MAP kinase cascade facilitating the activation of MAPK2 (By similarity).
Subcellular location: Late endosome membrane {ECO:0000250|UniProtKB:O88653}; Peripheral membrane protein {ECO:0000250|UniProtKB:O88653}; Cytoplasmic side {ECO:0000250|UniProtKB:O88653}. Note=Recruited to lysosome and endosome membranes by LAMTOR1. {ECO:0000250|UniProtKB:O88653}.
Interaction partners:
- Late endosomal/lysosomal adaptor, MAPK and MTOR activator 2.
- Ragulator complex protein LAMTOR5
- Ragulator complex protein LAMTOR1
- Ragulator complex protein LAMTOR4
- Neutral amino acid transporter 9
- Ras-related GTP-binding protein
- Ras-related GTP-binding protein
- Regulatory-associated protein of mTOR
- Ras-related GTP-binding protein A
- Dual specificity mitogen-activated protein kinase kinase 1
Sequence:
MADDLKRFLYKKLPSVEGLHAIVVSDRDGVPVIKVANDSAPEHALRPGFLSTFALATDQGSKLGLSKNKSIICYYNTYQVVQFNRLPLVVSFIASSNANTGLIVSLEKELAPLFEELIKVVEVS
Protein: Amyloid protein-binding protein 2 (Amyloid beta precursor protein-binding protein 2) (APP-BP2) (Protein interacting with APP tail 1) (Q92624)
Organism: Homo sapiens (Human)
Function: Substrate-recognition component of a Cul2-RING (CRL2) E3 ubiquitin-protein ligase complex of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation. The C-degron recognized by the DesCEND pathway is usually a motif of less than ten residues and can be present in full-length proteins, truncated proteins or proteolytically cleaved forms. The CRL2(APPBP2) complex specifically recognizes proteins with a -Arg-Xaa-Xaa-Gly degron at the C-terminus, leading to their ubiquitination and degradation. The CRL2(APPBP2) complex mediates ubiquitination and degradation of truncated SELENOV selenoproteins produced by failed UGA/Sec decoding, which end with a -Arg-Xaa-Xaa-Gly degron. May play a role in intracellular protein transport: may be involved in the translocation of APP along microtubules toward the cell surface.
Subcellular location: Nucleus {ECO:0000269|PubMed:11742091}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9843960}. Membrane {ECO:0000269|PubMed:9843960}; Peripheral membrane protein {ECO:0000269|PubMed:9843960}. Note=Associated with membranes and microtubules. {ECO:0000269|PubMed:9843960}.
Interaction partners:
- Cullin-2
- Kelch domain-containing protein 3
- Kelch domain-containing protein 2
- Protein fem-1 homolog C
- Elongin-B
- Protein fem-1 homolog B
- PRAME family member 6
- Amyloid-beta precursor protein
- Kelch domain-containing protein 10
- Protein fem-1 homolog A
Sequence:
MAAVELEWIPETLYNTAISAVVDNYIRSRRDIRSLPENIQFDVYYKLYQQGRLCQLGSEFCELEVFAKVLRALDKRHLLHHCFQALMDHGVKVASVLAYSFSRRCSYIAESDAAVKEKAIQVGFVLGGFLSDAGWYSDAEKVFLSCLQLCTLHDEMLHWFRAVECCVRLLHVRNGNCKYHLGEETFKLAQTYMDKLSKHGQQANKAALYGELCALLFAKSHYDEAYKWCIEAMKEITAGLPVKVVVDVLRQASKACVVKREFKKAEQLIKHAVYLARDHFGSKHPKYSDTLLDYGFYLLNVDNICQSVAIYQAALDIRQSVFGGKNIHVATAHEDLAYSSYVHQYSSGKFDNALFHAERAIGIITHILPEDHLLLASSKRVKALILEEIAIDCHNKETEQRLLQEAHDLHLSSLQLAKKAFGEFNVQTAKHYGNLGRLYQSMRKFKEAEEMHIKAIQIKEQLLGQEDYEVALSVGHLASLYNYDMNQYENAEKLYLRSIAIGKKLFGEGYSGLEYDYRGLIKLYNSIGNYEKVFEYHNVLSNWNRLRDRQYSVTDALEDVSTSPQSTEEVVQSFLISQNVEGPSC
Protein: Chemotaxis protein CheW (P06110)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Involved in the transmission of sensory signals from the chemoreceptors to the flagellar motors.
Subcellular location: Cytoplasm.
Interaction partners:
- Protein-glutamate methylesterase/protein-glutamine glutaminase
- Chemotaxis protein CheY
- Methyl-accepting chemotaxis protein I
- Chemotaxis protein CheA
- Chemotaxis protein methyltransferase
- Motility protein B
- Aerotaxis sensor receptor
- Protein phosphatase CheZ
- Methyl-accepting chemotaxis protein II
- Methyl-accepting chemotaxis protein
Sequence:
MTGMSNVSKLAGEPSGQEFLVFTLGNEEYGIDILKVQEIRGYDQVTRIANTPAFIKGVTNLRGVIVPIVDLRVKFCEGDVEYDDNTVVIVLNLGQRVVGIVVDGVSDVLSLTAEQIRPAPEFAVTLSTEYLTGLGALGERMLILVNIEKLLNSEEMALLDIAASHVA
Protein: endothelin-converting enzyme 1 (EC 3.4.24.71) (Q6IE65)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000256|ARBA:ARBA00004250}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004194}; Single-pass membrane protein {ECO:0000256|ARBA:ARBA00004194}. Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004606}.
Interaction partners:
Sequence:
MNVALQELGSGGSMVEYKRAKLQDEELPEVTVEGRAIQDSLEVGSQKRTRQLFGSHTQLELVLAGLILVLAALLLGCLVALWVHTDPVHSTCITEACIRVAGKILESLDRGVSPCQDFYQFSCGGWIRRNPLPSGRSRWNTFNSLWDQNQAILKHLLENSTFNSSSEAERKTRSFYLSCLHLERIEKLGAKPLQDLIDKIGGWNITGPWDEDNFMEVLKAVAGTYRAAPFFTVYVGADSKSSNSNIIQVDQSGLFLPSRDYYLNRTANEKVLAAYLDYMVELGMLLGGQPTSTRAQMQQVLELEIQLATITVPQDQRRDEEKIYHKMSISELQTLAPSMDWLEFLSFLLSPLELGDSEPVVVYGTEYLQQVSELINRTEPSILNNYLIWNLVQKTTSSLDQRFETAQEKLLETLYGTKKSCTPRWQTCISNTDDALGFALGSLFVKATFDRQSKEIAEGMISEIRAAFEETLENLVWMDEKTRLAAKEKADAIYDMIGFPDFILEPRELDDVYDGYEVSEDSFFQNMLNLYNFSAKVMADQLRKPPSRDQWSMTPQTVNAYYLPTKNEIVFPAGILQAPFYAHNHPKALNFGGIGVVMGHELTHAFDDQGREYDQEGNLRPWWQNESLTAFQNHTACMEEQYNQYQVNGERLNGLQTLGENIADNGGLKAAYNAYKAWLRKHGEEQPLPAVGLTNHQLFFVGFAQVWCSVRTPESSHEGLVTDPHSPARFRVLGTLSNSRDFLRHFGCPVGSPMNPGQLCEVW
Protein: Isethionate sulfite-lyase activating enzyme (EC 1.97.1.-) (GRE activase IseH) (Glycyl-radical enzyme activating enzyme IseH) (Q727N0)
Organism: Nitratidesulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / CCUG 34227 / NCIMB 8303 / VKM B-1760 / Hildenborough) (Desulfovibrio vulgaris)
Function: Involved in an anaerobic respiration pathway that converts the sulfonate isethionate (2-hydroxyethanesulfonate) to ammonia, acetate and sulfide. Catalyzes activation of the isethionate sulfite-lyase IseG under anaerobic conditions by generation of an organic free radical on a glycine residue, via a homolytic cleavage of S-adenosyl-L-methionine (SAM).
Interaction partners:
- Isethionate sulfite-lyase
- Formate acetyltransferase, putative
- hydrogenase gamma
- Pyruvate:ferredoxin oxidoreductase
- Nitrogen fixation protein NifU
- L-aspartate oxidase, putative
- Adenylyl-sulphate reductase, alpha subunit
- succinate dehydrogenase
Sequence:
MSSIADRKTTGITFNIQKYSVHDGPGIRTVVFLKGCPLKCRWCSNPESQRKSVELAYNTGRCLTLAKCVRCVEICTAGAISRAEDDTISIDRALCNDCEQLCSGACPSNALITYGAHKTVDEVLRAVEQDSLFYARSGGGMTISGGEPFAQPAFTLALLREARRRRVHTAVETCGYASWDDMAAALPFLNYVLYDIKNLDDARHKEATGVSNQRIVENLRALRAEFPGIPVLVRTPVIPGFNDNEADIAAIAALTRELGVSYQLLPYHRLGTQKYHFLDREAPMGEVTLDAETMRRLEAVVAQTADS