wanglab/gogpt-training-data huggingface dataset:
Protein: Ceramide transfer protein (Collagen type IV alpha-3-binding protein) (A0A2R8YEK8)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Golgi apparatus {ECO:0000256|ARBA:ARBA00004555}.
Interaction partners:
Sequence:
MSDNQSWNSSGSEEDPETESGPPVERCGVLSKWTNYIHGWQDRWVVLKNNALSYYKSEDETEYGCRGSICLSKAVITPHDFDECRFDISVNDSVWYLRAQDPDHRQQWIDAIEQHKTESGYGSESSLRRHGSMVSLVSGASGYSATSTSSFKKGHSLREKLAEMETFRDILCRQVDTLQKYFDACADAVSKDELQRDKVVEDDEDDFPTTRSDGDFLHSTNGNKEKLFPHVTPKGINGIDFKGEAITFKATTAGILATLSHCIELMVKREDSWQKRLDKEGPNSLINEEEFFDAVEAALDRQDKIEEQSQSEKVRLHWPTSLPSGDAFSSVGTHRFVQKVEEMVQNHMTYSLQDVGGDANWQLVVEEGEMKVYRREVEENGIVLDPLKATHAVKGVTGHEVCNYFWNVDVRNDWETTIENFHVVETLADNAIIIYQTHKRVWPASQRDVLYLSVIRKIPALTENDPETWIVCNFSVDHDSAPLNNRCVRAKINVAMICQTLVSPPEGNQEISRDNILCKITYVANVNPGGWAPASVLRAVAKREYPKFLKRFTSYVQEKTAGKPILF
Protein: Uncharacterized protein, isoform B (A1ZAQ3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Uncharacterized protein, isoform C
- Uncharacterized protein, isoform C
- Trio, isoform A
- Cysts, isoform C
- Uncharacterized protein, isoform C
- Guanine nucleotide-binding protein subunit alpha
- FI17866p1
- Ras-related protein Rac1
Sequence:
MADEDLSPLPFRRERNLSNRNFNKRNSRRRISHQAAEQERHSSTLVSSNLESNDVARPVSSVSSSSSSIQLSYSVNSDTDSSYRHRSLLKMHEAESVGGLGTESTPESPMSPQTPDPALLDVRQKVHRFEAFRTNICFIKQERHSLKLLENRRHPSFEDQSEDHHTPPATPPRRIRLPGLGSRGSSRSSSIPSFQAGIHEVRSEDEVDQISDFETDSHTAAEEYLVVDTTSEVVPSEEVADSKVDQQQVQRSISADQSKEALTLPLKMRNDFPRNYRSTPRRKTEIIGTTNEHLVGKFHSVYQPKDEEEEVEIELRDKSDKCVHPILEELIKTEEAYVNNLFTGIENYGNIFQRKDLPLGLRGKKYDLFGNIEQIAEFHRDEFLPMLQRNRRDLKRLFDEFLQFLDQHCFYGYVIFTMNKQKSLKLCDLYKNYFTSIRLERDDKLGINSFLVQPIQRMARYPLLLTQFINTFFKNRDIVMKPLIESCCRLEKRLRALLTTTNESEIINDIVDCHEFNVYYQGKFRKVNEFQVLDHKLKRSYRSKVFIFDKCIIYTEIKGKNLLFHGRYPCEHIGISAKTKSFTLYYERRKQQECEFTADPVQIAIWLDLIRDMINNYANEERQKLQERYSRENDHLHRKAPSFSLYRDSNRFSSDSGIGNIWIMPKADEDTISNRTTWYAAT
Protein: Voltage-gated sodium channel subunit (Q6TMY8)
Organism: Ruegeria pomeroyi
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MQRMQAFIDRPGFGRFITAVIMLNAVVLGMETSPYLMERWGGLILAADRICLGIFIVEIALKLTAQRQRFFLNGWNLFDFVIVGIALIPAAGGLSVLRALRILRVLRVISVAPRLRRVVEGFITALPGMASVFLLMTIIFYIGAVIATKLFAASFPDWFGDLGLSAYTLFQIMTLESWSMGIVRPVMQVYPYAWLFFVPFIMITTFAVVNLLVGLIVNSMQDAHHAEDGERTDAYRDEVLARLEQIDQRLNALGETKK
Protein: Ribulose-phosphate 3-epimerase (EC 5.1.3.1) (Q54YE7)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
- Transketolase
- Ribose-5-phosphate isomerase
- 6-phosphogluconate dehydrogenase, decarboxylating
- RRM domain-containing protein
- Eukaryotic translation initiation factor 3 subunit D
- 2-oxoisovalerate dehydrogenase subunit alpha, mitochondrial
- Uncharacterized protein
- Glucose-6-phosphate 1-dehydrogenase
- Probable gluconokinase
- Uncharacterized protein
Sequence:
MSLKPIICPSLLSSDFAFLARDSNYMLECGADWLHIDVMDNHFVPNLTLGAPIVKSLRKHTKGYFDCHLMVTNPETMIEDFKNAGANSITFHIEATEPRGITQKVITQIKEAGMKVALCVKPKTPIEEVFPYVDQLDFVLIMTVEPGFGGQSFMKDMMPKVKTLRSKYPNLNIQVDGGLDPSTIDMAAEAGANVIVAGSALFKPNQDPKETIKLFKDSINKHSSN
Protein: Anionic antimicrobial peptide 2 (P85216)
Organism: Galleria mellonella (Greater wax moth)
Function: Antimicrobial protein. Has antibacterial activity against the Gram-positive bacteria M.luteus (MIC=86.6 uM), L.monocytogenes (MIC=86.6 uM), and S.lutea (MIC=86.6 uM). Lacks antibacterial activity against the Gram-positive bacteria B.circulans and S.aureus, and the Gram-negative bacteria E.coli D31, E.coli ATCC 25922, and S.typhimurium. Has antifungal activity against P.pastoris (MIC=86.6 uM) and P.stipitis (MIC=90.9 uM), but lacks antifungal activity against A.niger, C.albicans, C.albidus, C.fructus, C.wickerhamii, F.oxysporum, S.cerevisiae, S.pombe, T.harzianum, and Z.marxianus.
Subcellular location: Secreted {ECO:0000269|PubMed:17194500}.
Interaction partners:
Sequence:
ETESTPDYLKNIQQQLEEYTKNFNTQVQNAFDSDKIKSEVNNFIESLGKILNTEKKEAPK
Protein: Misshapen-like kinase 1 (EC 2.7.11.1) (GCK family kinase MiNK) (MAPK/ERK kinase kinase kinase 6) (MEK kinase kinase 6) (MEKKK 6) (Misshapen/NIK-related kinase) (Mitogen-activated protein kinase kinase kinase kinase 6) (F1LP90)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine kinase which acts as a negative regulator of Ras-related Rap2-mediated signal transduction to control neuronal structure and AMPA receptor trafficking. Required for normal synaptic density, dendrite complexity, as well as surface AMPA receptor expression in hippocampal neurons. Can activate the JNK and MAPK14/p38 pathways and mediates stimulation of the stress-activated protein kinase MAPK14/p38 MAPK downstream of the Raf/ERK pathway. Phosphorylates: TANC1 upon stimulation by RAP2A, MBP and SMAD1. Has an essential function in negative selection of thymocytes, perhaps by coupling NCK1 to activation of JNK1.
Subcellular location: Cytoplasm {ECO:0000250}. Postsynaptic density {ECO:0000269|PubMed:21048137}. Cell projection, axon {ECO:0000269|PubMed:21048137}. Cell projection, dendrite {ECO:0000269|PubMed:21048137}.
Interaction partners:
- Striatin
- Alpha-endosulfine
- cAMP-regulated phosphoprotein 19
Sequence:
MGDPAPARQSDFIFLVALRDPAGIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKQEINMLKKYSHHRNIATYYGAFIKKSPPGNDDQLWLVMEFCGAGSVTDLVKNTKGNALKEDCIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVGRRNTFIGTPYWMAPEVIACDENPDATYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPRNPPPRLKSKKWSKKFTDFIDTCLIKTYLSRPPTEQLLKFPFIRDQPTERQVRIQLKDHIDRSRKKRGEKEETEYEYSGSEEEDDSHGEEGEPSSIMNVPGESTLRREFLRLQQENKSNSEALKQQQQLQQQQQRDPEAHIKHLLHQRQRRIEEQKEERRRVEEQQRREREQRKLQEKEQQRRLEDMQALRREEERRQAEREQEYKRKQLEEQRQSERLQRQLQQEHAYLNSQKQQQQQQQQQQQQQQQQILPGDRKPLYHYGRGINPADKPAWAREVEERARMNKQQNSPLAKTKPSSAGPEPPIPQASPSPPGPLSQTPPMQRPVEPQEGPHKSLVAHRVPLKPYAAPVPRSQSLQDQPTRNLAAFPASHDPDPAAVPTPTATPSARGAVIRQNSDPTSEGPGPSPNPPSWVRPDNEAPPKVPQRTSSIATALNTSGAGGSRPAQAVRARPRSNSAWQIYLQRRAERGTPKPPGPPAQPPGPPNTSSNPDLRRSDPGWERSDSVLPASHGHLPQAGSLERNRNRVGASTKLDSSPVLSPGNKAKPEDHRSRPGRPADFVLLKERTLDEAPKPPKKAMDYSSSSEEVESSEDEEEEGDGEPSEGSRDTPGGRSDGDTDSVSTMVVHDVEEVSGTQPSYGGGTMVVQRTPEEERSLLLADSNGYTNLPDVVQPSHSPTENSQGQSPPTKDGGGDYQSRGLVKAPGKSSFTMFVDLGIYQPGGSGDTIPITALVGGEGGRLDQLQFDVRKGSVVNVNPTNTRAHSETPEIRKYKKRFNSEILCAALWGVNLLVGTENGLMLLDRSGQGKVYGLIGRRRFQQMDVLEGLNLLITISGKRNKLRVYYLSWLRNKILHNDPEVEKKQGWTTVGDMEGCGHYRVVKYERIKFLVIALKNSVEVYAWAPKPYHKFMAFKSFADLPHRPLLVDLTVEEGQRLKVIYGSSAGFHAVDVDSGNSYDIYIPVHIQSQITPHAIVFLPNTDGMEMLLCYEDEGVYVNTYGRIIKDVVLQWGEMPTSVAYICSNQIMGWGEKAIEIRSVETGHLDGVFMHKRAQRLKFLCERNDKVFFASVRSGGSSQVYFMTLNRNCIMNW
Protein: RPM1 interacting protein 13 (Q9SK71)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Resistance protein interactor which positively enhances RPM1-mediated resistance to necrotrophic bacterial pathogens Pseudomonas syringae pv. tomato DC3000 harboring type III effector protein AvrRpm1 or AvrB, but prevents the hypersensitive response (HR) controlled by RPM1. Together with ARF1, promotes leaf senescence and cell death, probably by facilitating the translocation of ARF1 into the nucleus, and activates ROS-related enzymes (e.g. POD, CAT and SOD).
Subcellular location: Nucleus {ECO:0000269|PubMed:32446355}.
Interaction partners:
- Disease resistance protein RPM1
- AT4G38060 protein
- RuvB-like protein 1
Sequence:
MGSGNHVDIVDVSSGEEDVDTRGDVEYTDWLNGVMEPVDDTSDSTDIVEVLSEVRGGVNSQYRKPNSSNQALEDDDDCVILDCDPDKTRETTSVDDDDDDDVLVVGQKGEIACRDFPHPRHSCAKYAFNSTSHEKYCDMCHCYVCDIRAPCPYWCIAVSSIDHCHANDKEKIWKNQREYFRTGYMPTAPSSKPTPSILRVPKNTLLRKNHVEIRPCSSSTRVANPSSVKARHRIRQPIPHNQGLQSQPAQSLSTVRDSVIQKDRSSYRFSLRSRVASSAGNGISIRFNNAQVSQSSHHSSSTVAPTLNPETYTQQRNVRDHCTALPGSQSNVFTRHADQNIRGSGNRQFQTNVDRFAPSKAPLTAEDSHTATVQQQPGINENVLETKLSEFEKWLMENPNPTGPVSPLPEPGNQDYASTLSFDFETFLND
Protein: Coatomer subunit zeta-2 (Zeta-2-coat protein) (Zeta-2 COP) (Q9P299)
Organism: Homo sapiens (Human)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex.
Subcellular location: Cytoplasm {ECO:0000250}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasmic vesicle, COPI-coated vesicle membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it. Shows a significant preference for ERGIC and cis-Golgi apparatus compared with trans-Golgi network. {ECO:0000250}.
Interaction partners:
- Coatomer subunit alpha
- Coatomer subunit beta'
- Coatomer subunit gamma-1
- Coatomer subunit gamma-2
- Coatomer subunit epsilon
- Coatomer subunit delta
- Coatomer subunit beta
- Coatomer subunit zeta-1
- Transmembrane emp24 domain-containing protein 7
- N-terminal kinase-like protein
Sequence:
MQRPEAWPRPHPGEGAAAAQAGGPAPPARAGEPSGLRLQEPSLYTIKAVFILDNDGRRLLAKYYDDTFPSMKEQMVFEKNVFNKTSRTESEIAFFGGMTIVYKNSIDLFLYVVGSSYENELMLMSVLTCLFESLNHMLRKNVEKRWLLENMDGAFLVLDEIVDGGVILESDPQQVIQKVNFRADDGGLTEQSVAQVLQSAKEQIKWSLLK
Protein: RNA polymerase-binding transcription factor CarD (A0R561)
Organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis)
Function: Controls rRNA transcription by binding to the RNA polymerase (RNAP). Required for the stringent response to starvation, oxidative and genotoxic stresses as well as control of rRNA under normal growth conditions.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- RNA polymerase-binding protein RbpA
- DNA-directed RNA polymerase subunit beta'
- DNA-directed RNA polymerase subunit omega
- DNA-directed RNA polymerase subunit alpha
- RNA polymerase sigma factor SigA
- 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
- RNA polymerase sigma factor
- 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
- Transcriptional regulator WhiB7
Sequence:
MIFKVGDTVVYPHHGAALIEAIETRTIKGEQKEYLVLKVAQGDLTVRVPADNAEYVGVRDVVGQEGLDKVFQVLRAPHTEEPTNWSRRYKANLEKLASGDVNKVAEVVRDLWRRDQERGLSAGEKRMLAKARQILVGELALAENTDDAKAETILDEVLAAAS
Protein: Large ribosomal subunit protein P2A (60S acidic ribosomal protein P2-alpha) (A2) (L12EI) (L40C) (P08094)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays an important role in the elongation step of protein synthesis.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Small ribosomal subunit protein uS12B
- Small ribosomal subunit protein eS6B
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS3
- Large ribosomal subunit protein eL14
- Large ribosomal subunit protein eL6
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein eS21
- Large ribosomal subunit protein eL18A
Sequence:
MKYLAAYLLLTVGGKDSPSASDIESVLSTVGIEAESERIETLINELNGKDIDELIAAGNEKLATVPTGGAASAAPAAAAGGAAPAAEEAAKEEAKEEEESDEDMGFGLFD
Protein: Stumps, isoform D (A0A0B4KFZ6)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MPTKGSCRLFSCVSGQRRPSKEEEEDYVDMEMNNCGNVNNTSGSSASGFLGSPGYNMDDILIITAKHSERAYLRATFLKNHFDKITKQRGRKPFNFLHIKIDDGPFSEEIAHKYQNTALQIVILCPALLALPHSFLMTQLSAIIRVEKVLAILLDVSEEKVKEMHKSALPSYYKWRRCVVRDNDQVQISNILGIATDILGRALCQRPPCQDSSGGGGGGLSRSFSSCTEGFTVLPKKVKLGQNKVVALLAEPLEKNDTLKLQVEKSGELIELRNFKCRNPYTLQFNIPEACMEISTMIEIRIEKNNKSLGARPIKCESRLRELEQLLRIEDSPIEFMCHALGIGPVERDALDQHLLQCFQRNMPPNFHLLSGPSERQPHFFTRLESSPEEYPTLLHFAARWGLNRLCIQLMECPGGDTACGVRNCAGRTPAELAEQEGHHKLAQNIVSFAEFHELTTMYHYFKGVTPPGESCPKPSANVVIEAHPVKAGKTNKPPKELPTAEYMEMSSGSERENTPEVRTKTETLAISNLNYISVETEDENLQASVAEKKVESEKKLPEAGNQPGPEKTTNELRINEPPYYQSKEQNQQPKELKNQSKSLDEVDAAPLYQTDKFSQECSQLLENQLGNDYVLQPSNVPVAQDDGNYLFQPSNRPVEEPLRLNRCTNRQPGYGTLKRSASDASAASHTRSNADDELAEIMHDFKNNVLSIRDVEVLVERWKHRNDVQQSFREKQDQIDQLRREYERIQEQVKSHLKRETPFERIKKFFLRSKTPGGNDSLLDETKSSIATSCSFKSAGGVSSSAGAGRPISSLSLQSVSSSSSSSGRLSTGSNCSGASLGDSGTHSDHEDRRFPHCRMMDNYMVPPTPRPVFTPSSTPGDERHQIVFPSPMSSCQRLNTPTSPTGSEHYQMFPSNIPVYGSQPLVGSQSSNYLNTIMEAKEQAETQHYQNQNGVTLQPIKLNERSNIIYGKLTKSSSASGCSSFKPKQIPVPCPQVGSIEVQAEVYQNVGDVAPEKDSKAEEETPNYMNC
Protein: Burkholderia TALE-like protein 1 (Modular DNA-binding domain protein BurrH1) (E5AV36)
Organism: Mycetohabitans rhizoxinica (strain DSM 19002 / CIP 109453 / HKI 454) (Paraburkholderia rhizoxinica)
Function: Binds to dsDNA in a sequence-specific manner. Also binds a DNA/RNA duplex when the recognized sequence is in the DNA strand. Each tandem core repeat recognizes a single nucleotide in the target DNA via its base-specifying residue (BSR, residue 13 of each repeat); altering this amino acid changes sequence specificity.
Interaction partners:
Sequence:
MSTAFVDQDKQMANRLNLSPLERSKIEKQYGGATTLAFISNKQNELAQILSRADILKIASYDCAAHALQAVLDCGPMLGKRGFSQSDIVKIAGNIGGAQALQAVLDLESMLGKRGFSRDDIAKMAGNIGGAQTLQAVLDLESAFRERGFSQADIVKIAGNNGGAQALYSVLDVEPTLGKRGFSRADIVKIAGNTGGAQALHTVLDLEPALGKRGFSRIDIVKIAANNGGAQALHAVLDLGPTLRECGFSQATIAKIAGNIGGAQALQMVLDLGPALGKRGFSQATIAKIAGNIGGAQALQTVLDLEPALCERGFSQATIAKMAGNNGGAQALQTVLDLEPALRKRDFRQADIIKIAGNDGGAQALQAVIEHGPTLRQHGFNLADIVKMAGNIGGAQALQAVLDLKPVLDEHGFSQPDIVKMAGNIGGAQALQAVLSLGPALRERGFSQPDIVKIAGNTGGAQALQAVLDLELTLVEHGFSQPDIVRITGNRGGAQALQAVLALELTLRERGFSQPDIVKIAGNSGGAQALQAVLDLELTFRERGFSQADIVKIAGNDGGTQALHAVLDLERMLGERGFSRADIVNVAGNNGGAQALKAVLEHEATLNERGFSRADIVKIAGNGGGAQALKAVLEHEATLDERGFSRADIVRIAGNGGGAQALKAVLEHGPTLNERGFNLTDIVEMAANSGGAQALKAVLEHGPTLRQRGLSLIDIVEIASNGGAQALKAVLKYGPVLMQAGRSNEEIVHVAARRGGAGRIRKMVAPLLERQ
Protein: Isoaspartyl peptidase (EC 3.4.19.5) (Beta-aspartyl-peptidase) (EcAIII) (Isoaspartyl dipeptidase) [Cleaved into: Isoaspartyl peptidase subunit alpha; Isoaspartyl peptidase subunit beta] (P37595)
Organism: Escherichia coli (strain K12)
Function: Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function.
Interaction partners:
- Glutathione import ATP-binding protein GsiA
- Glutathione-binding protein GsiB
- Glutathione transport system permease protein GsiC
- L-asparaginase 2
- L-asparaginase 1
- Asparagine synthetase B
- Adenylosuccinate synthetase
- Glutathione transport system permease protein GsiD
- Aspartate aminotransferase
- Aspartate ammonia-lyase
Sequence:
MGKAVIAIHGGAGAISRAQMSLQQELRYIEALSAIVETGQKMLEAGESALDVVTEAVRLLEECPLFNAGIGAVFTRDETHELDACVMDGNTLKAGAVAGVSHLRNPVLAARLVMEQSPHVMMIGEGAENFAFARGMERVSPEIFSTSLRYEQLLAARKEGATVLDHSGAPLDEKQKMGTVGAVALDLDGNLAAATSTGGMTNKLPGRVGDSPLVGAGCYANNASVAVSCTGTGEVFIRALAAYDIAALMDYGGLSLAEACERVVMEKLPALGGSGGLIAIDHEGNVALPFNTEGMYRAWGYAGDTPTTGIYREKGDTVATQ
Protein: Achaete-scute homolog 1 (ASH-1) (hASH1) (Class A basic helix-loop-helix protein 46) (bHLHa46) (P50553)
Organism: Homo sapiens (Human)
Function: Transcription factor that plays a key role in neuronal differentiation: acts as a pioneer transcription factor, accessing closed chromatin to allow other factors to bind and activate neural pathways. Directly binds the E box motif (5'-CANNTG-3') on promoters and promotes transcription of neuronal genes. The combination of three transcription factors, ASCL1, POU3F2/BRN2 and MYT1L, is sufficient to reprogram fibroblasts and other somatic cells into induced neuronal (iN) cells in vitro. Plays a role at early stages of development of specific neural lineages in most regions of the CNS, and of several lineages in the PNS. Essential for the generation of olfactory and autonomic neurons. Acts synergistically with FOXN4 to specify the identity of V2b neurons rather than V2a from bipotential p2 progenitors during spinal cord neurogenesis, probably through DLL4-NOTCH signaling activation. Involved in the regulation of neuroendocrine cell development in the glandular stomach (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q02067}.
Interaction partners:
- Neurogenin-2
- POU domain, class 3, transcription factor 2
- Myelin transcription factor 1-like protein
- Transcription factor 12
- POU domain, class 3, transcription factor 3
- Homeobox protein DLX-2
- DNA-binding protein inhibitor ID-4
- Cyclic AMP-responsive element-binding protein 1
- Paired mesoderm homeobox protein 2B
- Histone acetyltransferase p300
Sequence:
MESSAKMESGGAGQQPQPQPQQPFLPPAACFFATAAAAAAAAAAAAAQSAQQQQQQQQQQQQAPQLRPAADGQPSGGGHKSAPKQVKRQRSSSPELMRCKRRLNFSGFGYSLPQQQPAAVARRNERERNRVKLVNLGFATLREHVPNGAANKKMSKVETLRSAVEYIRALQQLLDEHDAVSAAFQAGVLSPTISPNYSNDLNSMAGSPVSSYSSDEGSYDPLSPEEQELLDFTNWF
Protein: Cytoplasmic polyadenylation element binding protein 1 (A0A087X171)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MALSLEEEAGRIKDCWDNQEAPALSTCSNANIFRRINAILDNSLDFSRVCTTPINRGIHDHLPDFQDSEETVTSRMLFPTSAQESSRGLPDANDLCLGLQSLSLTGWDRPWSTQDSDSSAQSSTHSVLSMLHNPLGNVLGKPPLSFLPLDPLGSDLVDKFPAPSVRGSRLDTRPILDSRSSSPSDSDTSGFSSGSDHLSDLISSLRISPPLPFLSLSGGGPRDPLKMGVGSRMDQEQAALAAVTPSPTSASKRWPGASVWPSWDLLEAPKDPFSIEREARLHRQAAAVNEATCTWSGQLPPRNYKNPIYSCKVFLGGVPWDITEAGLVNTFRVFGSLSVEWPGKDGKHPRCPPKGYVYLVFELEKSVRSLLQACSHDPLSPDGLSEYYFKMSSRRMRCKEVQVIPWVLADSNFVRSPSQRLDPSRTVFVGALHGMLNAEALAAILNDLFGGVVYAGIDTDKHKYPIGSGRVTFNNQRSYLKAVSAAFVEIKTTKFTKKVQIDPYLEDSLCHICSSQPGPFFCRDQVCFKYFCRSCWHWRHSMEGLRHHSPLMRNQKNRDSS
Protein: Hepatocyte nuclear factor 4-alpha (HNF-4-alpha) (Nuclear receptor subfamily 2 group A member 1) (Transcription factor 14) (TCF-14) (Transcription factor HNF-4) (P22449)
Organism: Rattus norvegicus (Rat)
Function: Transcriptional regulator which controls the expression of hepatic genes during the transition of endodermal cells to hepatic progenitor cells, facilitating the recruitment of RNA pol II to the promoters of target genes (By similarity). Activates the transcription of CYP2C38 (By similarity). Represses the CLOCK-BMAL1 transcriptional activity and is essential for circadian rhythm maintenance and period regulation in the liver and colon cells (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Nuclear receptor subfamily 0 group B member 2
- Forkhead box protein O1
- Hepatocyte nuclear factor 1-alpha
- Nuclear receptor coactivator
- Histone lysine acetyltransferase CREBBP
- Sterol regulatory element-binding protein 1
- Hepatocyte nuclear factor 1-beta
- Nuclear receptor coactivator 2
- Catenin beta-1
Sequence:
MRLSKTLADMDMADYSAALDPAYTTLEFENVQVLTMGNDTSPSEGANLNSSNSLGVSALCAICGDRATGKHYGASSCDGCKGFFRRSVRKNHMYSCRFSRQCVVDKDKRNQCRYCRLKKCFRAGMKKEAVQNERDRISTRRSSYEDSSLPSINALLQAEVLSQQITSPISGINGDIRAKKIANITDVCESMKEQLLVLVEWAKYIPAFCELLLDDQVALLRAHAGEHLLLGATKRSMVFKDVLLLGNDYIVPRHCPELAEMSRVSIRILDELVLPFQELQIDDNEYACLKAIIFFDPDAKGLSDPGKIKRLRSQVQVSLEDYINDRQYDSRGRFGELLLLLPTLQSITWQMIEQIQFIKLFGMAKIDNLLQEMLLGGSASDAPHAHHPLHPHLMQEHMGTNVIVANTMPSHLSNGQMCEWPRPRGQAATPETPQPSPPSGSGSESYKLLPGAITTIVKPPSAIPQPTITKQEAI
Protein: Calcium/calmodulin-dependent protein kinase type II subunit gamma (CaM kinase II subunit gamma) (CaMK-II subunit gamma) (EC 2.7.11.17) (Q13555)
Organism: Homo sapiens (Human)
Function: Calcium/calmodulin-dependent protein kinase that functions autonomously after Ca(2+)/calmodulin-binding and autophosphorylation, and is involved in sarcoplasmic reticulum Ca(2+) transport in skeletal muscle and may function in dendritic spine and synapse formation and neuronal plasticity. In slow-twitch muscles, is involved in regulation of sarcoplasmic reticulum (SR) Ca(2+) transport and in fast-twitch muscle participates in the control of Ca(2+) release from the SR through phosphorylation of the ryanodine receptor-coupling factor triadin. In the central nervous system, it is involved in the regulation of neurite formation and arborization. It may participate in the promotion of dendritic spine and synapse formation and maintenance of synaptic plasticity which enables long-term potentiation (LTP) and hippocampus-dependent learning. In response to interferon-gamma (IFN-gamma) stimulation, catalyzes phosphorylation of STAT1, stimulating the JAK-STAT signaling pathway (By similarity).
Subcellular location: Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 4
- Calmodulin-like protein 6
- Calcium/calmodulin-dependent protein kinase type II subunit delta
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
- Calcium/calmodulin-dependent protein kinase type II subunit beta
- Calmodulin-1
- Glutamate receptor ionotropic, NMDA 2B
Sequence:
MATTATCTRFTDDYQLFEELGKGAFSVVRRCVKKTSTQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIHQILESVNHIHQHDIVHRDLKPENLLLASKCKGAAVKLADFGLAIEVQGEQQAWFGFAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGYPPFWDEDQHKLYQQIKAGAYDFPSPEWDTVTPEAKNLINQMLTINPAKRITADQALKHPWVCQRSTVASMMHRQETVECLRKFNARRKLKGAILTTMLVSRNFSAAKSLLNKKSDGGVKKRKSSSSVHLMPQSNNKNSLVSPAQEPAPLQTAMEPQTTVVHNATDGIKGSTESCNTTTEDEDLKGRVPEGRSSRDRTAPSAGMQPQPSLCSSAMRKQEIIKITEQLIEAINNGDFEAYTKICDPGLTSFEPEALGNLVEGMDFHKFYFENLLSKNSKPIHTTILNPHVHVIGEDAACIAYIRLTQYIDGQGRPRTSQSEETRVWHRRDGKWLNVHYHCSGAPAAPLQ
Protein: ESX-1 secretion-associated protein EspD (P9WJD5)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Required for ESX-1 function. Required for the maintenance of adequate cellular levels of both EspA and EspC. Facilitates EsxA secretion.
Subcellular location: Secreted {ECO:0000269|PubMed:22155774}. Note=Export does not exclusively require ESX-1. May require one (or more) of the other ESX / type VII secretion systems (T7SS). {ECO:0000269|PubMed:22155774}.
Interaction partners:
- ESX-1 secretion-associated protein EspC
- ESX-1 secretion-associated protein EspA
- Transposase
- Uncharacterized protein
- 6 kDa early secretory antigenic target
- ESAT-6-like protein EsxB
Sequence:
MDLPGNDFDSNDFDAVDLWGADGAEGWTADPIIGVGSAATPDTGPDLDNAHGQAETDTEQEIALFTVTNPPRTVSVSTLMDGRIDHVELSARVAWMSESQLASEILVIADLARQKAQSAQYAFILDRMSQQVDADEHRVALLRKTVGETWGLPSPEEAAAAEAEVFATRYSDDCPAPDDESDPW
Protein: Lipase 10 (EC 3.1.1.3) (Q9P4E5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Secreted {ECO:0000269|PubMed:11131027}.
Interaction partners:
Sequence:
MKTLLIFLAFLSSIFASLIGLTPPSKDSFYSPPVGFATAKPGDILKIRNTPSAPSSLYLPIVVKNAWQLLIRSEDSFGNPNAFVATLIQPLNANPSKLVSYQSWEDASHIDCSPSYGMQFKSPATTVTTQIDMTLIVPLLQNGYYVIIPDYEGPKSTFTVGRQSGKATLNSIRAALQTGAFSGIKKTAKVALWGYSGGSLATGWAISLQSKYAPELKENLIGAAVGGFATNITAVAEAVDGTVFSGFIPLALNGLANEYPDFKKRLYGEVKLSARSTMEKGSQNCLAASLVGYPMSQYFTGQNRAFEKGWGLLQDEVFNKTIEDNLLLKLDKTYLPQVPVLIYHGTIDEIIPIKDANAQYQIWCDRGIQSLEFAEDLSAGHLAETFTGAPAALSWIDARFSGKPAVNGCQRTIRSSNVLYPGISITIRIYFEGISKTIFGVNLGSGVNADKSISNKFFAYIRKYI