wanglab/gogpt-training-data huggingface dataset:
Protein: ADAM metallopeptidase domain 9 (E9PTA4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
Interaction partners:
- Protein kinase C and casein kinase substrate in neurons 3
- Sorting nexin
Sequence:
MGPRALSPLASLRLRWLLACGLLGPVLEAGRPDSEQTVHLSSYEIVTPWRLSRERREALRPSSKQISYVIQAQGKQHIIHLERNTDLLPNDFVVYTYDEEGSLLSDHPNVQSHCHYRGYVEGVPNSTVAVSACFGLRGLLHLENASFGIEPLHNSSHFEHVFYPMDDVHQEPLRCGVSNRDTEQEATQGEEEEHPSVTQLLRRRRAVLPQTRYVELFIVVDKERYNMMGRNQTAVREEMIRLANYLDSMYIMLNIRIVLVGLEIWTDRNPINIIGGAGDVLGNFVQWREKFLITRRRHDSAQLVLKKGFGGTAGMAFVGTVCSRSHAGGINVFGQITVETFASIVAHELGHNLGMNHDDGRECFCAAKSCIMNSGASGSRNFSSCSAEDFEKLTLNKGGSCLLNIPKPDEAYSAPSCGNKLVDPGEECDCGTPKECELDPCCEGSTCKLKSFAECAYGDCCKDCQFLPGGSMCRGKTSECDVPEYCNGSSQFCPPDVFIQNGYPCWNSKAYCYNGVCQYYDAQCQVIFGSKAKAAPRDCFIEVNSKGDRFGNCGVSGSNYKTCATGNALCGKLQCENVQEMPVFGIVPAIIQTPSRGTKCWGVDFQLGSDVPDPGMVNEGTKCDAGKICRNFQCVNASVLNYDCDIQGKCHGHGVCNSNKNCHCEDGWAPPHCDTKGYGGSVDSGPTYNAKSTALRDGLLVFFFLIIPLVAAAFFLFIKRDELRKTFRKKRSQMSDGRNQANASRPPGDPSVSRPPGGPSVSRPPGGPNVSRPPGGPNVSRPPGGPSVSRPPPVHGNRFPVPTYAIKQPPQFPSRPPPPQPKIPSQGNLIPARPAPAPPLYSSLT
Protein: Transcription factor GTE7 (Bromodomain-containing protein GTE7) (Protein GLOBAL TRANSCRIPTION FACTOR GROUP E7) (Q7Y214)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Emb|CAB72159.1
- Protein GRAVITROPIC IN THE LIGHT 1
- AT3G14870 protein
- At1g53380
- At2g32130)
- F28N24.3 protein)
- Ubiquitin carboxyl-terminal hydrolase 18
- Zinc finger CCCH domain-containing protein 26
- Alba DNA/RNA-binding protein
- Amino acid transporter AVT1B
Sequence:
MAPAVFATLNEPSYQEQCGAVFMRKFTNQSVTENTNNLPLFNPNPNPNFERSNSSKQCDDSSEFGSYATFNLAGYTSSQLRELKKRFTSELKQIRILRERIESGTFETQQGYTIPEVPAVRSAPLNNFTGEKNDLGPKKKKQKKNVSGLKRSNQFGPSDPESEKLLAGMLNTCSQILVKLMKHKWAWVFNTPVDVVGLGLHDYHQVVKKPMDLGTVKLNLDKGFYVSPIDFATDVRLTFDNAMTYNPKGQDVYFMADKLLDHFDGMFNPAFKKFEAQQLKLTGSSSRPEPDFKPDFKQRQWNQNPPMVANPRKGTEQISIAKKLDSVKPPQPTLPPQLVEPSRVQSPSPPPPPPVIQPELPQPQPPPPQLEIEVEAPPDVSEVSKGRKGKLPKPKAKDPNKRLMTMEEKSKLGMNLQDLPPEKLGQLLQILRKRNGHLAQDGDEIELDIEAVDNETLWELDRFVTNYKKMASKIKRQGFIRNVSTPPRNMASVAEMGSAEKRTRRGDAGEEDVDIGEDIPIEDYPSVEIERDGTAVAAAASSGSSSSGSSSSSGGSSSSSDSGSGGSSSGSDSDADSVQSPFVEAKEAQC
Protein: Sodium channel protein (K4DIA1)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU361132}.
Interaction partners:
Sequence:
MANFLLPRGTSSFRRFTRESLAAIEKRMAEKQARGSTTLQESREGLPEEEAPRPQLDLQASKKLPDLYGNPPQELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPIRRAAVKILVHSLFNMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIIMAYVSENIKLGNLSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTALNGTNGSVEADGLVWESLDLYLSDPENYLLKNGTSDVLLCGNSSDAGTCPEGYRCLKAGENPDHGYTSFDSFAWAFLALFRLMTQDCWERLYQQTLRSAGKIYMIFFMLVIFLGSFYLVNLILAVVAMAYEEQNQATIAETEEKEKRFQEAMEMLKKEHEALTIRGVDTVSRSSLEMSPLAPVNSHERRSKRRKRMSSGTEECGEDRLPKSDSEDGPRAMNHLSLTRGLSRTSMKPRSSRGSIFTFRRRDLGSEADFADDENSTAGESESHHTSLLVPWPLRRTSAQGQPSPGTSAPGHALHGKKNSTVDCNGVVSLLGAGDPEATSPGSHLLRPVMLEHPPDTTTPSEEPGGPQMLTSQAPCVDGFEEPGARQRALSAVSVLTSALEELEESRHKCPPCWNRLAQRYLIWECCPLWMSIKQGVKLVVMDPFTDLTITMCIVLNTLFMALEHYNMTSEFEEMLQVGNLVFTGIFTAEMTFKIIALDPYYYFQQGWNIFDSIIVILSLMELGLSRMSNLSVLRSFRLLRVFKLAKSWPTLNTLIKIIGNSVGALGNLTLVLAIIVFIFAVVGMQLFGKNYSELRDSDSGLLPRWHMMDFFHAFLIIFRILCGEWIETMWDCMEVSGQSLCLLVFLLVMVIGNLVVLNLFLALLLSSFSADNLTAPDEDREMNNLQLALARIQRGLRFVKRTTWDFCCGLLRQRPQKPAALAAQGQLPSCIATPYSPPPPETEKVPPTRKETRFEEGEQPGQGTPGDPEPVCVPIAVAESDTDDQEEDEENSLGTEEESSKQTPEDSCSEGSTADMTNTAELLEQIPDLGQDVKDPEDCFTEGCVRRCPCCAVDTTQAPGKVWWRLRKTCYHIVEHSWFETFIIFMILLSSGALAFEDIYLEERKTIKVLLEYADKMFTYVFVLEMLLKWVAYGFKKYFTNAWCWLDFLIVDVSLVSLVANTLGFAEMGPIKSLRTLRALRPLRALSRFEGMRVVVNALVGAIPSIMNVLLVCLIFWLIFSIMGVNLFAGKFGRCINQTEGDLPLNYTIVNNKSQCESLNLTGELYWTKVKVNFDNVGAGYLALLQVATFKGWMDIMYAAVDSRGYEEQPQWEYNLYMYIYFVIFIIFGSFFTLNLFIGVIIDNFNQQKKKLGGQDIFMTEEQKKYYNAMKKLGSKKPQKPIPRPLNKYQGFIFDIVTKQAFDVTIMFLICLNMVTMMVETDDQSPEKINILAKINLLFVAIFTGECIVKLAALRHYYFTNSWNIFDFVVVILSIVGTVLSDIIQKYFFSPTLFRVIRLARIGRILRLIRGAKGIRTLLFALMMSLPALFNIGLLLFLVMFIYSIFGMANFAYVKWEAGIDDMFNFQTFANSMLCLFQITTSAGWDGLLSPILNTGPPYCDPTLPNSNGSRGDCGSPAVGILFFTTYIIISFLIVVNMYIAIILENFSVATEESTEPLSEDDFDMFYEIWEKFDPEATQFIEYSVLSDFADALSEPLRIAKPNQISLINMDLPMVSGDRIHCMDILFAFTKRVLGESGEMDALKIQMEEKFMAANPSKISYEPITTTLRRKHEEVSAMVIQRAFRRHLLQRSLKHASFLFRQQAGSGLSEEDAPEREGLIAYVMSENFSRPLGPPSSSSISSTSFPPSYDSVTRATSDNLQVRGSDYSHSEDLADFPPSPDRDRESIV
Protein: Cyclin-dependent kinase 4 inhibitor D (p19-INK4d) (P55273)
Organism: Homo sapiens (Human)
Function: Interacts strongly with CDK4 and CDK6 and inhibits them.
Subcellular location: Nucleus {ECO:0000269|PubMed:9482106}. Cytoplasm {ECO:0000269|PubMed:9482106}.
Interaction partners:
- Cyclin-dependent kinase 6
- Cyclin-dependent kinase 4
- G1/S-specific cyclin-D3
- G1/S-specific cyclin-D2
- G1/S-specific cyclin-D1
- Cyclin-dependent kinase inhibitor 1B
- Cyclin-dependent kinase inhibitor 1C
- Cyclin-dependent kinase inhibitor 1
- Cyclin-dependent kinase 2
- Cyclin-L2
Sequence:
MLLEEVRAGDRLSGAAARGDVQEVRRLLHRELVHPDALNRFGKTALQVMMFGSTAIALELLKQGASPNVQDTSGTSPVHDAARTGFLDTLKVLVEHGADVNVPDGTGALPIHLAVQEGHTAVVSFLAAESDLHRRDARGLTPLELALQRGAQDLVDILQGHMVAPL
Protein: Large ribosomal subunit protein eL33 (60S ribosomal protein L35a) (A0A8I6GLI9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
LDSHNVSLCLRLWCKAIFAGYKRGLRNQREHTALLKIEGVYARDETEFYLGKRCAYVYKAKNNTVTPGGKPNKTRVIWGKVTRAHGNSGMVRAKFRSNLPAKAIGHRIRVMLYPSRI
Protein: Erythrocyte membrane protein 1, PfEMP1 (Q8IBX0)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MAAAGSGGQGARDVLEQFGEIVQKKVHNEVDAYREELKGKLWEAKFVGVSHVPSDPCQLNHEYHTNVTTGKDDPCDRRWPVRFSDESRSQCTKNRIKDSTSDTVGACAPYRRLHVCDQNLEQIRPEQITSTDNLLADVCLAAKHEGESIIKNYPQDRNNNEVICTALARSFADIGDIIRGKDLYRGDKGEKKKLEENLKNIFANIYEELKNGKTNGKKGEIETRYKKDDEDGNFFQLREDWWNANRNDIWKALTCHAPPDAQYTKKGPHNHITESNKGQCRCFSGDPPTNMDYVPQYLRWFEEWAEEFCRKRKKKLQNAQKFCRDESSKLYCSLNGYDCKATIRANDEYTISQACAKCFFSCHRFVKWIDNQKLELEKQKKKYDEEINVTTETSKKTEHGRINIIYAKKFYDILKEQYGKVDNFLELLSNQKECKNHPEVKGKNSIDFKNDNDTFSRTEICEPCPWCGVKKQEDGNWKRLERGHPHCPKKPPYTPPDGAKCTEIDVLYTGERNNDILDKLKEFCRSEGKNERKTDFKNEQWKCYYKDSYNNKCVLQPDRDLGIEKKVKNYVDFMMFWINHMLKDSIDWRKYIKRCINNSASNECKKNMCFKNCQCFEKWINKKQDEWNKIKKHYNNEKGFGEFGSYNTLEYILEEDFFKGISEAYGSVDAIERIKNITKNHVSTEEITNAENEEFAIDILLKHELEEAQECKNNNPEDQKCNEPHDEEEYEDEHEEEVYVNNPCAKPSGNYPALAHNVAYQMHEVAKTQLRTRGGRNALRANAAEGKYKNNNKEFTFNGNICSINENHSNCNHNYSSGPCGGKDGRNEMFEVKDGWKSGADVSKEHAEDVFLPPRRQHFCTSNLENLNTNSKGLSDGTLASHSLLGDVLLSANKEAGFIKDKYKNQPTLGGFKDEATICRAMKYSFADIGDIIKGTDLWDGNKEETDTQRNLVTIFGKIKDKIRDEATKKKYSDAQKHLQLRKDWWEANRDQVWKAMQCGNDNPCSGVSGVPLDDYIPQRLRWMTEWAEWFCKMQSQEYNKLMEACTGCMKKGKDGEGCTQKTQECALCKAACDAYKKEIEKWQRQWNNMQVPYITLYEQARTVRDGTVIGDVSDQQVIAFFKELHQQNGGKKSVDTVYSTAAGYVHQEAIMNCEKQTQFCKNKNGENSISGTQNNQKYAFMQPPKGYEKACSCEDYYKAADPQDDACTIVKQLLGNKGAADDIQGCKKKYDGINPYPSWKCDKSLVDEDGVCMPPRRQNLCVHYLTQLDDKDDENKLREAFIKSAAAETFVLWQNYNSKNDNDAQLLDSGIIPPEFLRSMFYTFGDYRDICLDTDISAKTPDGDLEQAKENIGKVFQKIGPKTANHKPPRGITREDWWKEYGSQIWKGMLCALSYDNETRIMNERVRKQLMDSIYNYHILKNHLENFAERHPFFRWFIEWTDEFCQEQKKEYNDLVQKCTGCNEQTCDSECETCKSQCGQYEKFITQWKSQWEKQSGKYDKLYAEAKVTSTPTTDPIETKLLKHLKELKDHSTNSDKYSTAGRYMKEEGYINDCELSKQNKFEKNCNDGSNDNYAFRTYPNDHQTKCDCKKKEAPPPEPPANVVPKVIPKSRTPREAGSSHLQNALLSSTIMWSIGIGFAAFTYFFLKKKTKSSVGNLFQILQIPKSDYDIPTKLSPNRYIPYTSGKYRGKRYIYLEGDSGTDSGYTDHYSDITSSSESEYEELDINDIYVPGSPKYKTLIEVVLEPSGNNTTASGKNTPSDTQNDIQNDGIPSSKITDNEWNTLKDDFISQYLQSEQPKDVPNDYSSGDIPFNTQPNTLYFDKPEEKPFIMSIHDRDLYSGEEYNYNVNMSTNSMDDIPINSHNNVYSGIDLINDTLSGNKHIDIYDEVLKRKENELFGTNHVKQTSIHSVAKLTNSDPIHNQLELFHKWLDRHRNMCEKWENHHERLAKLKEEWENETHSGNTHPSDSNKTLNTDVSIQIHMDDPKPINQFTNMDTILEDLEKYNEPYYDVQDDIYYDVNDHDTSTADSNAMDVPSKVQIEMDVNTKLVKEKYPIADVWDI
Protein: D-alanyl-D-alanine dipeptidase (D-Ala-D-Ala dipeptidase) (EC 3.4.13.22) (P77790)
Organism: Escherichia coli (strain K12)
Function: Catalyzes hydrolysis of the D-alanyl-D-alanine dipeptide. May have a role in cell-wall turnover.
Subcellular location: Cytoplasm {ECO:0000305|PubMed:9751644}.
Interaction partners:
- Probable D,D-dipeptide-binding periplasmic protein DdpA
- Probable D,D-dipeptide transport ATP-binding protein DdpD
- Probable D,D-dipeptide transport ATP-binding protein DdpF
- Probable D,D-dipeptide transport system permease protein DdpC
- Probable D,D-dipeptide transport system permease protein DdpB
- Succinylornithine transaminase
Sequence:
MSDTTELVDLAVIFPDLEIELKYACADNITGKAIYQQARCLLHKDAITALAKSISIAQLSGLQLVIYDAYRPQQAQAMLWQACPDPQYVVDVTVGSNHSRGTAIDLTLRDEHGNILDMGAGFDEMHERSHAYHPSVPPAAQRNRLLLNAIMTGGGFVGISSEWWHFELPQAASYPLLADQFSCFISPGTQHVS
Protein: Sucrose synthase 5 (AtSUS5) (EC 2.4.1.13) (Sucrose-UDP glucosyltransferase 5) (F4K5W8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Sucrose-cleaving enzyme that provides UDP-glucose and fructose for various metabolic pathways. Functions in callose synthesis at the site of phloem sieve elements.
Subcellular location: Secreted, cell wall {ECO:0000269|PubMed:19470642}.
Interaction partners:
- Granule-bound starch synthase 1, chloroplastic/amyloplastic
- Glucose-1-phosphate adenylyltransferase small subunit, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 2, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 3, chloroplastic
- Glucose-1-phosphate adenylyltransferase large subunit 1, chloroplastic
- Probable glucose-1-phosphate adenylyltransferase large subunit, chloroplastic
- alpha-D-xyloside xylohydrolase
- UTP--glucose-1-phosphate uridylyltransferase 1
- UTP--glucose-1-phosphate uridylyltransferase 2
- Beta-fructofuranosidase, insoluble isoenzyme CWINV3
Sequence:
MEMTSGSLGNGIPEAMGQNRGNIKRCLEKYIENGRRVMKLNELMDEMEIVINDVTQRRRVMEGDLGKILCFTQAVVIPPNVAFAVRGTPGNWQYVKVNSSNLSVEALSSTQYLKLKEFLFDENWANDENALEVDFGALDFTLPWLSLSSSIGNGLSFVSSKLGGRLNDNPQSLVDYLLSLEHQGEKLMMNETLNTARKLEMSLILADVFLSELPKDTPFQAFELRFKECGFEKGWGESAGRVKETMRILSEILQAPDPQNIDRFFARVPRIFNVVIFSVHGYFGQTDVLGLPDTGGQVVYILDQVKALEDELLQRINSQGLNFKPQILVVTRLIPDAKKTKCNQELEPIFGTKYSNILRIPFVTENGILRRWVSRFDIYPYLERFTKDATTKILDILEGKPDLIIGNYTDGNLVASLMANKLGITQATIAHALEKTKYEDSDIKWKEFDPKYHFSSQFTADLISMNSADFIIASTYQEIAGSKERAGQYESHMSFTVPGLYRVVSGINVFDPRFNIAAPGADDSIYFPFTAQDRRFTKFYTSIDELLYSQSENDEHIGYLVDKKKPIIFSMARLDVVKNLTGLTEWYAKNKRLRDLVNLVIVGGFFDASKSKDREEISEIKKMHSLIEKYQLKGQFRWITAQTDRTRNGELYRSIADTRGAFVQPAHYEAFGLTVIEAMSCGLVTFATNQGGPAEIIVDGVSGFHIDPSNGEESSDKIADFFEKSGMDPDYWNMFSNEGLQRINECYTWKIYANKVINMGSTYSYWRHLNKDQKLAKQRYIHSFYNLQYRNLVKTIPILSDIPEPPPLPPKPLVKPSASKGSKRTQPRLSFRLFGA
Protein: Expressed protein (Q2QXE3)
Organism: Oryza sativa subsp. japonica (Rice)
Interaction partners:
Sequence:
MAVGDALRRLCEEARWSYAVFWKAIGAADPVHLVWEDGFCGHASCSAGSEASEAGCESGGAVCTLVRKIMASQVHVVGEGTIGRAAFTGNHQWIVHETANDHGLRSEVVAAEMNNQFRAGIKTIAIIPVLPRGVLQLGSTSVILENISSVQQYKKLCCQLNNRSSMVASASAKNDLSQKVQSRSLHGLPSIHPYEQCYGHDARALSSSTSANTGRNTSLLKVAQRNDQAIREQVLYAPDMRFRQQLPYSDRRVDINTHSSAMSSGFISSISASVEKYPLLTNNIGQVEHGNMEESSGPRNVLLKSLSCRNPVVHENTNTSLFHGGDEVPAFLNSHGSFDFLQAGPRVVEANLYNNGTSSQVLDQRCSSTSGMAGYKPSVSYKFPHSAQFIVKMENPRRQSFQDPAAPSSGSDVQVSSGLKTTTRQFNPEHMCQNKKTNEVNDSSAAVSTQDVKNMDRHKILDISNERTSSFVMDPSTENDLFDIFGTDFHQLHRSLDGDLSWNTAKPQSSDRDAPESSIYLDSSPAFGAQEDEFSYSGIFSLTDTDQLLDAVISNVNPGGKQISGDSASCKTSLTDIPSTSYCGSKETKQCKSSGAPPLLIKNELAVSNFVKQPCFLEKAEDGCLSQNNGVQKSQIRLWIESGQNMKCESVSASNSKGLDTANKANRKRSRPGESPKPRPKDRQLIQDRIKELRELVPNGAKCSIDALLEKTIKHMVFLQSVTKHADNLKDSNESKIHGGGENGPLLKDYFEGGATWAFDVGSQSMTCPIIVEDLDRPRQMLVEMLCEDRGIFLEIADFIKGLGLTILRGVMEARKNKIWARFTVEANRDVTRMEIFLSLMRLLEPSCDGGGGGVGDNPNNVKIPPGIVQHPVIPATGHLR
Protein: Nuclear apoptosis-inducing factor 1 (Q69YI7)
Organism: Homo sapiens (Human)
Function: Induces apoptosis.
Subcellular location: Nucleus {ECO:0000269|PubMed:16378748, ECO:0000269|PubMed:18339812}.
Interaction partners:
- Integrator complex subunit 5
- Integrator complex subunit 3
- Integrator complex subunit 6
- Putative nuclease HARBI1
- Vacuolar protein sorting-associated protein 16 homolog
Sequence:
MAVPAKKRKMNFSEREVEIIVEELELKKHLLVNHFNAGVPLAAKSAAWHGILRRVNAVATCRRELPEVKKKWSDLKTEVRRKVAQVRAAVEGGEAPGPTEEDGAGGPGTGGGSGGGGPAVAPVLLTPMQQRICNLLGEATIISLPSTTEIHPVALGPSATAAAATVTLTQIPTETTYHTLEEGVVEYCTAEAPPPLPPETPVDMMAQHADTSVKPQALKSRIALNSAKLIQEQRVTNLHVKEIAQHLEQQNDLLQMIRRSQEVQACAQERQAQAMEGTQAALSVLIQVLRPMIKDFRRYLQSNTANPAPASDPGQVAQNGQPDSIIQ
Protein: Nuclear poly(A) polymerase 2 (PAP(II)) (Poly(A) polymerase II) (EC 2.7.7.19) (Polynucleotide adenylyltransferase 2) (O82312)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Essential protein. Polymerase that creates the 3'-poly(A) tail of mRNA's. Also required for the endoribonucleolytic cleavage reaction at some polyadenylation sites. May acquire specificity through interaction with a cleavage and polyadenylation specificity factor (CPSF) at its C-terminus (By similarity). Mediates the polyadenylation of RNAs that are associated with polynucleotide phosphorylase (e.g. PNP1).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P25500, ECO:0000255|PROSITE-ProRule:PRU00768}. Cytoplasm {ECO:0000269|PubMed:19956626}.
Interaction partners:
- 30-kDa cleavage and polyadenylation specificity factor 30
- Cleavage and polyadenylation specificity factor subunit 2
- FIP1[V]-like protein
- Symplekin
- HEAT repeat-containing protein
- Cleavage stimulation factor subunit 77
- Cleavage stimulating factor 64
- Cleavage and polyadenylation specificity factor subunit 3-I
- Cleavage and polyadenylation specificity factor subunit 1
- Flowering time control protein FY
Sequence:
MVSTQQRTDDDSSQPVKASLKSYGITEPLSIAGPSAADVKRNLELEKFLVDEGLYESKEETMRREEVVVRIDQIVKHWVKQLTRQRGYTDQMVEDANAVIFTFGSYRLGVHGPMADIDTLCVGPSYVNREEDFFIFFRDILAEMEEVTELQPVTDAHVPVMKFKFQGISIDLLYASISLLVIPQDLDISNSSVLCDVDEQTVRSLNGCRVADQILKLVPNSEHFRTTLRCLKYWAKKRGVYSNVTGFLGGVNWALLVARLCQFYPNAIPSMLVSRFFRVYTQWRWPNPVMLCAIEEDDLSFPVWDPRKNHRDRYHLMPIITPAYPCMNSSYNVSQSTLRVMTEQFQFGNTICQEIELNKQHWSSLFQQYMFFEAYKNYLQVDVLAADAEDLLAWKGWVESRFRQLTLKIERDTNGMLMCHPQPNEYVDTSKQFRHCAFFMGLQRADGFGGQECQQFDIRGTVDEFRQEVNMYMFWRPGMDVHVSHVRRRQLPSFVFPNGYKRSRQSRHQSQQCREPGDEGVGSLSDSVERYAKRKNDDEIMNSRPEKREKRASCSLHTLDAASPDSSGITTSGTPQIGIVPGPRAECLVTGDLVCNVTSLPNVEVEAEKFISKITELRKFSQYEHTSGSEQILEVDSRALVQSYHDLAEPVAKHVRPDLSALLACEGGQNKEIGHDMGSESINDTDTQHLPRRLNVNEDVDEVEREAKLGEIAGGVLWNGHCGRNLDHEGFVTPANLDSAVENRNLHSDGLFKSGLPEELQSNSLLSGTGKLDDGARSESLQNEMMRHVFLQPIIGLCKS
Protein: BMP/retinoic acid-inducible neural-specific protein 3 (Q8K1M7)
Organism: Rattus norvegicus (Rat)
Function: Inhibits neuronal cell proliferation by negative regulation of the cell cycle transition. Promotes pituitary gonadotrope cell proliferation, migration and invasion, when overexpressed. May play a role in cell pituitary tumor development (By similarity).
Subcellular location: Secreted {ECO:0000305}. Mitochondrion {ECO:0000269|PubMed:17138656}.
Interaction partners:
Sequence:
MIWRRRAGAELSSLMALWEWIVLSLHCWVLAVAAVSDQHATSPFDWLLSDKGPFHRSQEYTDFVDRSRQGFSTRYKIYREFGRWKVNNLAVERRNFLGSPLPLAPEFFRNIRLLGRRPTLQQITENLIKKYGTHFLLSATLGGEESLTIFVDKRKLSKRPEGSETSTNSSSVTLETLHQLAASYFIDRDSTLRRLHHIQIASTAIKVTETRTGPLGCSNYDNLDSVSSVLVQSPENKIQLQGLQVLLPDYLQERFVQAALSYIACNSEGEFICKENDCWCLCGPKFPECNCPSMDIQAMEENLLRITETWKAYNSDFEDSDEFKFFMKRLPMNYFLNTSTIMHLWTMDSNFQRRYEQLENSMKQLFLKAHRIVHKLFSLSKRCHKQPLISLPRQRTSTYWLTRIQSFLYCNENGLLGSFSEETHSCTCPNDQVVCTAFLPCTVGDASACLTCAPDNRTRCGTCNTGYMLSQGLCKPEVAESTDHYIGFETDLQDLEMKYLLQKTDRRIEVHAIFISNDMRLNSWFDPSWRKRMLLTLKSNKYKSSLVHMILGLSLQICLTKNSTLEPVLAVYINPFGGSHSESWFMPVSESSFPDWERTKLDLPLQCYNWTLTLGNKWKTFFETVHIYLRSRIKANGPNSNESIYYEPLEFIDPSRNLGYMKINNIQVFGYSMHFDPEAIRDLILQLDYPYTQGSQDSALLQLLEIRDRVNKLSPPGQRRLDLFSCLLRHRLKLSTSEVVRIQSALQAFNAKLPNTVDYDTTKLCS
Protein: Dishevelled segment polarity protein 3 (D4ADV8)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
- Axin-2
- Vang-like protein 2
- Protein naked cuticle homolog
- Vang-like protein
- Dishevelled segment polarity protein 2
- Segment polarity protein dishevelled homolog DVL-1
- Prickle homolog 3
- Prickle planar cell polarity protein 2
- Prickle-like protein 1
- Prickle planar cell polarity protein 4
Sequence:
MGETKIIYHLDGQETPYLVKLPLPAERVTLADFKGVLQRPSYKFFFKSMDDDFGVVKEEISDDNAKLPCFNGRVVSWLVSAEGSHPEPAPFCADNPSELPPSMERTGGIGDSRPPSFHPHASGGSQENLDNDTETDSLVSAQRERPRRRDGPEHAARLNGTTKGERRREPGGYDSSSTLMSSELETTSFFDSDEDDSTSRFSSSTEQSSASRLMRRHKRRRRKQKVSRIERSSSFSSITDSTMSLNIITVTLNMEKYNFLGISIVGQSNERGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNEINFENMSNDDAVRVLREIVHKPGPITLTVAKCWDPSPRGCFTLPRSEPIRPIDPAAWVSHTAAMTGTFPAYGMSPSLSTITSTSSSITSSIPDTERLDDFHLSIHSDMAAIVKAMASPESGLEVRDRMWLKITIPNAFIGSDVVDWLYHNVEGFTDRREARKYASNLLKAGFIRHTVNKITFSEQCYYIFGDLCGNMANLSLHDHDGSSGASDQDTLAPLPHPGAAPWPMAFPYQYPPPPHPYNPHPGFPELGYSYAGGSASSQHSEGSRSSGSNRSGSDRRKEKDPKAGDSKSGGSGSESDHTTRSSLRGPRERAPSERSGPAASEHSHRSHHSLTSSLRSHHTHPSYGPPGVPPLYGPPMLMMTPPPAAMGPPGAPPGRDLASVPPELTASRQSFRMAMGNPTKNFGLFDFL
Protein: NLRP1 protein (Q96AM0)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPLDPYHSVTWGHAQGSHHFVFGELRVRPILESLRDEPDPDPRPSREGPAGRVGALARGGPEPCDAASPPGGASCAPELARPREDKSAQQAKLEGGTRLCCRCPEESRLVPGGAVSPGDHVLEVSGTRGTCGCRPRRHAGPELAHS
Protein: Protease regulatory ATPase subunit 4 (EC 3.6.4.8) (Q38BP7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Proteasome regulatory non-ATP-ase subunit
- Proteasome subunit beta
- Proteasome regulatory non-ATP-ase subunit 5
- 26S proteasome regulatory subunit 4 homolog
- Proteasome subunit alpha type
- Proteasome subunit alpha type
- Probable 26S proteasome regulatory subunit rpn-6.2
- 26S proteasome regulatory non-ATPase subunit
- Proteasome subunit alpha type
- Proteasome regulatory ATPase subunit 5
Sequence:
MQERQEEYASLSEREQLRQDVIAKTIRRNESRARVREVAKAMEASERELMRVVDQLSALMSIGHFVGEILHKVDEERFIVQSVSGARHLVGYKKSIKPEKLKIGTRVALEITTLTIVKVLPREVDPQVYNMQVMENEKNISFQEIGGLQEQMRQMREVVELPLTNPELFVRVGISPPKGVLLYGPPGTGKTLLAKAIASNVDAAFLKIVASSIVDKYIGESARVLREMFAFARDHEPCIIFIDEVDAIGGKRIEGSSSDREVQRTLMELLHQMDGFEKLGKVKVIMATNRPDTLDPALMRPGRLDRKIEIGLPNEAGRLDVLKIHASKITKQGDIDYDSIVKLSEGFNGADLRNVCTEAGMFALRAGRDYVINEDFNKATRKVADSKKLESAPHQYSEQ
Protein: NACHT, LRR and PYD domains-containing protein 1 homolog (EC 3.4.-.-) [Cleaved into: NACHT, LRR and PYD domains-containing protein 1, C-terminus (NLRP1-CT); NACHT, LRR and PYD domains-containing protein 1, N-terminus (NLRP1-NT)] (A0A386CAB9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Acts as the sensor component of the nlrp1 inflammasome, which mediates inflammasome activation in response to various pathogen-associated signals, leading to subsequent pyroptosis. Inflammasomes are supramolecular complexes that assemble in the cytosol in response to pathogens and other damage-associated signals and play critical roles in innate immunity and inflammation. Acts as a recognition receptor (PRR): recognizes specific pathogens and other damage-associated signals, and mediates the formation of the inflammasome polymeric complex (By similarity). In response to pathogen-associated signals, the N-terminal part of nlrp1 is degraded by the proteasome, releasing the cleaved C-terminal part of the protein (NACHT, LRR and PYD domains-containing protein 1, C-terminus), which polymerizes to initiate the formation of the inflammasome complex: the inflammasome recruits and activate pro-inflammatory caspases (caspa and/or caspb), leading to pyroptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:30150286}. Note=Co-localizes with pycard, caspa and caspb in the cytoplasm. {ECO:0000269|PubMed:30150286}.; SUBCELLULAR LOCATION: [NACHT, LRR and PYD domains-containing protein 1, C-terminus]: Inflammasome {ECO:0000269|PubMed:30150286}.
Interaction partners:
- Caspase a
- Bcl-2-like protein 1
- Apoptosis regulator Bcl-2
- Apoptosis-associated speck-like protein containing a CARD
- NOD2a protein
- Caspase b,-like
- Apoptosis regulator Bcl-2
- Caspase b
- Gasdermin Ea
Sequence:
MSSDYTDRNNLASAIKTLGDMLEKDEAFQRLMYNASTKGEINRGRVNKVFLKALLSAGDKVGEFLNELIDHLNLFKVLGDFSWNPPVLKEAELNERTSQLRTQQHKYVERVSGFSHYGFGETGTPARGDITSPRGPQVASIEEDLATSKLAELLLAVGDHLEKIEKKGQFLPENVERFSLDCFITSESVKLSSEAVELAPCYTEPVIIQRSKEQTEKYCQEYVRSPHTSSHLLSNDKTQSIRIGQLFSPDSDGNTPKTVILCGDSGRGKSFVLEKIILDWVHLEHHFENFDAVFLLKYEELKCLSEEMSLTELLSRSCSLTSDQISQILQLTPEKVLFLIDGIDDFSFNAHIQISSPTDPSQKAPVISIIHCLMRDLLLVESSVIVTTRYTAAAELSSLCKRPQRFTEIEGFSERRVQEYFQKFFQDEQLFKKAYESMKTNETLLTFCSVPLLCWMVCFCLKKDADQVMTELKTTTSIYVHFVSTLLEDHHQSQSFLRSLGQLAEEGMKNRQNLFDEKSVTRTGLDPATRVFMNKIYLKRKKKHELLFKFKHLSFQEFFAALYYIMLDEEESWCKVSELFNMMESEALIHRSPPIFRGRLSNPIPSVMMFLCGLFNKKVSSSLFEKMKSTFSHNVKLKKKELKKKLMKMIPAMIRQYGFELFALHCLYELQDERFVTKVLETHKFIDLSNVSLRSTDCLVLCYCLRLCPNIRELNFMNCDLTAAKLKILQPALGLCETLRFSVEHLSEIGDLIQILSESKILRELKVREDEYGVESPRWSFNLSVTRGDVLLTLSSSEKNPSFSSVLNIRLTCAQSQISRTDWTLFLQRLRKTGTLTEDSSADDDHVSLQLSSLHSVGLKSLDLTLVSLNESWASGIISLIQNCTSLQQLKVSVTGLLLEEGLKLLKKSLTDPHCTVIIEGRRNCSEPSEEHLRQSYEKVEIHFKPKLLEELAELSICNPGSSALNIHCQSCVDVADSDQWVQVEPSVCRGEGGTEFRITTPAGRFQCSRTRMRWVCDGDVTLHYRAVDGHFLNAELERLQCERVAPVLDVNVISGKLEEAHLPHYMCLAESDPALTNAVKLLSVEDEGISLESVELTRFHAKILQPMFSPKTVLVKLGIPVKVHCDLLIFMTHTCPIILNVYFFPSDSLVEENIKTEEKSSHQIKCSRPEAPLQMKKQHSLEVPDAVVQPEAIKLRGNMKPNFFQVKQPVVNDITMILSRVDDQKSVWTGTIWKKLIDIKLNKTESDLFQSGQKHKTSQPAHSFDKAQFFDTHWCNLIKSVENVDTVADKLLQKQIIHEQFYSEIIHHKSTSEESMRKICVIVRKGSAAVKEIFISILLQENPNLLNHLPSSDS
Protein: Reactive oxygen species modulator 1 (Protein MGR2 homolog) (Q9VUM2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- SD19278p
- Mitochondrial import inner membrane translocase subunit Tim21
- Mitochondrial import inner membrane translocase subunit Tim16
- AT05822p
- Mitochondrial import inner membrane translocase subunit TIM44
- Cytochrome b-c1 complex subunit 9
- Mitochondrial import inner membrane translocase subunit Tim16
- NADH dehydrogenase 1 beta subcomplex subunit 7
- Cytochrome b-c1 complex subunit 8
- NADH dehydrogenase 1 alpha subcomplex subunit 13
Sequence:
MPLPTSSFSQQGPTCFDKMKTGFIIGFCVGMASGAVFGGFSALRYGLRGRELINNVGKTMVQGGGTFGTFMAIGTGIRC
Protein: RNA-binding protein ZC3H20 (CCCH zinc finger protein ZC3H20) (Q57XK8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Function: RNA-binding protein involved in regulation of mRNA stability. Promotes mRNA stabilization by recruiting MKT1 and PBP1 (By similarity). Stabilizes mRNA required for differentiation from the bloodstream form to the procyclic form, and maintenance of the procyclic form. Stabilizes transcripts encoding membrane and mitochondrial proteins, including AQP1 and GPEET2 procyclin.
Interaction partners:
Sequence:
MQLVASPLETRRDIMCFEKGVECMVVVDPATRKLRIPLSCVYPTRAHQRTTIPSLCLLFLDGRCRQGTQCHQVHAALNVVAALRSQVDYLPICCALHGDRDYVNALDNRSWMSRVVVHVPDATYGGGYIPLARFSYTTPISRLLDALFHSTPQAEGQDGAQWESRAFGTPPSCLVLEAGDITLCRLHVQDRCRYAEECNYLHICKEVARCDRGLTLGQRPRSWKKPPSSSPSGGCFVVTASGTSMPPPPAAAAACDAPTPVSGGWTCPGSPTGSLFGANRSVTLGDASVTTQPAVVRCCDPSSCTEAHSVVDCGQAHIPFSLSRQVSDIHMRQVSSTFFPSDNLSLDVDPSTSGDCLAEQGCGMTPNIVVVTRNGKGGRERWHYNPYGTNGTDRGIEKGEGRGRN
Protein: Alanine dehydrogenase (AlaDH) (EC 1.4.1.1) (O28608)
Organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)
Function: Catalyzes the NAD(+)-dependent oxidative deamination of L-alanine to pyruvate, and the reverse reaction, the reductive amination of pyruvate. Its physiological role is not known. Cannot use NADP(+) instead of NAD(+) as a cosubstrate. In the deamination direction, can also efficiently use L-2-aminobutyrate as substrate. In the reductive amination direction, also exhibits high activity with 2-oxobutyrate and oxaloacetate as substrate. In contrast to bacterial homologs, does not exhibit any ornithine cyclodeaminase activity.
Interaction partners:
- Myo-inositol-1-phosphate synthase
- Diphthamide synthase domain-containing protein
Sequence:
METLILTQEEVESLISMDEAMNAVEEAFRLYALGKAQMPPKVYLEFEKGDLRAMPAHLMGYAGLKWVNSHPGNPDKGLPTVMALMILNSPETGFPLAVMDATYTTSLRTGAAGGIAAKYLARKNSSVFGFIGCGTQAYFQLEALRRVFDIGEVKAYDVREKAAKKFVSYCEDRGISASVQPAEEASRCDVLVTTTPSRKPVVKAEWVEEGTHINAIGADGPGKQELDVEILKKAKIVVDDLEQAKHGGEINVAVSKGVIGVEDVHATIGEVIAGLKDGRESDEEITIFDSTGLAIQDVAVAKVVYENALSKNVGSKIKFFRI