wanglab/gogpt-training-data huggingface dataset:
Protein: Casein kinase II subunit beta-2 (CK II beta-2) (P40229)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a complex role in regulating the basal catalytic activity of the alpha subunit. The tetrameric holoenzyme CK2, composed of two alpha and two beta subunits, phosphorylates the transcription factor PIF1 after an exposure to light, resulting in a proteasome-dependent degradation of PIF1 and promotion of photomorphogenesis. CK2 phosphorylates translation initiation factors. May participate in the regulation of the initiation of translation.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:16926165}. Nucleus {ECO:0000269|PubMed:16926165}.
Interaction partners:
- Casein kinase II subunit alpha-1
- Casein kinase II subunit alpha-3
- Casein kinase II subunit alpha-2
- Casein kinase II subunit alpha-4, chloroplastic
- FACT complex subunit SSRP1
- Protein CCA1
- 2-oxoglutarate
- Ribosomal RNA-processing 7 protein
- Nucleolar protein
- FACT complex subunit SPT16
Sequence:
MYRERGMVGSKSEVVDRKRINEIHDNRPSHSMSQPVNGKGKVTSTSVLMGKQQLHDKESSRSGSISKTNISDAVDISDTDSEESEVSGSDGEDTSWISWFCNLRGNEFFCEVDDDYIQDDFNLCGLSHQVPYYDYALDLILDVESSHGEMFTEEQNELIESAAEMLYGMIHARFILTSKGLASMLDKYKNYDFGRCPRVYCCGQPCLPVGQSDIPRASTVKIYCPKCEDVYYPRSKYQGNIDGAYFGTTFPHLFLMTYGHLKPQKASQSYTQRVFGFKLHKP
Protein: Transmembrane protein (Q9FJP0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MSLSLPSRYALFSGSTPVRISRRSNLCFAVSAARASRRDSISFPQPIFLRHVISTQSNFEIDRNYRAHASSIGSFEDSSSSNLLEDASSDGFDLGSFVSFAEALCILSSAVISVVLAVNYVVVGEIGKKVLSLGFVGLVGSVATGSWLRRRQWMRICKGARESEGTNLIRRLEKLEKDLKSSTSIVRVLSRHLEKLGIRFRVTRKALKEPISETAALAQKNSEATRVLVAQQEILEKELGEIQKVLLAMQEQQRKQLELILTIAKSSKLFESSTSSKQSPSEQRKNKAEEPSTPKQILVQ
Protein: Guanylate-binding protein/Atlastin C-terminal domain-containing protein (Q9D3E4)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MVQRLSLPTDTLQELLDVHAACEKEAMAVFMEHSFKDENQQFLKKLVELIGEAKVLFLLKNEEASDKYCQEELDRLSKDLMDNISTFSVPGGHRLYMDMREKIEHDYWQVPRKGVKAREVFQSFLQSQAIIESSILQADTALTAGQKAIAEERTKKEAAEKEQDLLRQKQKEQQEYMEAQEKRNKENIEQLRRKLEQEREQLIKDHNMMVEKKLKAQKALLEEGFKKKAEEMDGEIQQLKHNIEDMKKKQWFHFRYYYKRSASLFFLPFQ
Protein: Bacterial virulence domain-containing protein (Q9I538)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Interaction partners:
- Phosphatidylglycerol lysyltransferase
- histidine kinase
- Small-conductance mechanosensitive channel
Sequence:
MSVVKRHWRRFLVAALVLIVGAALLLWSRPAAQAKLEALDLDDGGHATLAEPGEKPRSRVVVIAAPEQQLNDAQMLNLAHDSAARVIQYFPPENGDCRAQQSRLEAVIARLGGKPNLVAGIGPGSTTAWRWLASQDDDKAKALSVGFDIALAERDCDAPLPHQASHGQWLLAWNDNPDDDTAVFVRKQSSAETSISDYDTPLSDVLAHQLRLQLQGNAEALPVLEVPAAQPSDIVTLFYSGDGGWRDLDKDSAEHMASMGYPVVGIDTLRYYWQHKSPEQSAADLSKLMQHYREKWGAKRFVLAGYSFGADILPAIYNRLPGKDQQQVKAMLLLALARTGSFEIEVEGWLGKAGEEAATGPEMARLPAAKVFCIYGAEEKDESGCTQSQAVGEKLELPGGHHFDEDYLSLAKKMLQAIRDRENAPDA
Protein: Tubulin beta chain (B1PBW4)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain-like
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain
- Tubulin alpha chain-like
- Tubulin alpha chain
- Tubulin alpha chain
Sequence:
MREILHIQGGQCGNQIGAKFWEVICDEHGIDNTGKYNGDSDLQLERINVYYNEASGGRYVPRAVLMDLEPGTMDSVRSGLFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELIDSVLDVVRKEAENCDCLQGFQVCHSLGGGTGSGMGTLLISKIREEYPDRMMLTFSVFPSPKVSDTVVEPYNATLSVHQLVENADECMVLDNEALYDICFRTLKLATPTFGDLNHLISATMSGVTCCLRFPGQLNSDLRKLAVNLIPFPRLHFFMVGFAPLTSRGSQQYRNLTVPELTQQMWDAKNMMCAADPRHGRYLTASAMFRGKMSTKEVDEQMINVQNKNSSYFVEWIPNNVKSSVCDIPPKGLKMASTFIGNSTSIQEMFRRVSEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVAEYQQYQDATADDEYEEGEEEEEEAA
Protein: ATPase synthesis protein 25, mitochondrial (OLI1 mRNA stabilization factor) (Q03153)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: mRNA stabilization factor specific for the 0.95 kb OLI1 mRNA. Also involved in OLI1 ring formation.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:18216280}; Peripheral membrane protein {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:18216280}; Matrix side {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:18216280}.
Interaction partners:
- ATP synthase subunit 9, mitochondrial
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL14m
- Nuclear control of ATPase protein 2
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL3m
- Mitochondrial inner membrane protease ATP23
- Large ribosomal subunit protein uL23m
- Inner membrane assembly complex subunit 22
- mRNA-binding protein PUF3
Sequence:
MNKFCLLPFHGKRIGVANIPFTILFKKGPYFLHSHITAVYYSTKGKNDSHEQSRVSKKSTFTPLETPWYLRIVDNEKELMEGKKNNHHTMNKELEIPKTSPNSLRKIADLLTGKLGLDDFLVFDLRKKSPNSVSAVNKLGDFMVICTARSTKHCHKSFLELNKFLKHEFCSSAYVEGNFNERQESRRKRRLARKSNLSKLLGRSSECSAKDLNSEAWYMIDCRVDGIFVNILTQRRRNELNLEELYAPENEKSKFQNIDSGNVPTISGVNEISSNNNILLGLRRLAQQRRRYSTINPNGLSNLRYFLQKEDFKGANKIIQSSSGTETHNIRTLEHVKNTLKDLVGQERKVDVVQWKSLFDEHSTFLTINQSAAYWPLRLEYAILLNKADPQFYSDRVFLKDYLLLKKSLGQELIREDLIALLEMVLKTQHSSHSYFNLVKQNRVIIRALNLFKGLQTEDDGSVVYDEVVISLLLNSMVADERVKLRSLYETIDHIFQTFGDKLTSGMIVSILQNLAKIKDWNKLLQVWEAITPTEGEGQDKRPWNEFINVINQSGDSHVISKIVNNGHLLWIRRLNVNVTPELCNSIKALLKTAGMENSTLEEFLVRGTNNQ
Protein: Intermediate cleaving peptidase 55, mitochondrial (EC 3.4.11.-) (AtICP55) (Protein INTERMEDIATE CLEAVAGE PEPTIDASE 55) (F4HZG9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Aminopeptidase which cleaves preprotein intermediates that carry destabilizing N-ter amino acid residues after the mitochondrial processing peptidase (MPP) cleavage site and is thus critical for stabilization of the mitochondrial proteome.
Subcellular location: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:25732537}.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus {ECO:0000269|PubMed:25732537}.
Interaction partners:
- Mitochondrial intermediate peptidase, mitochondrial
- Mitochondrial inner membrane protease ATP23
- Mitochondrial metalloendopeptidase OMA1
- ALBINO3-like protein 3
- Mitochondrial ATP-independent inner membrane protease subunit 2
- Peptidase S24/S26A/S26B/S26C family protein
- Mitochondrial ATP-independent inner membrane protease subunit 1a
- Mitochondrial inner membrane protease subunit 2
- Probable mitochondrial-processing peptidase subunit beta, mitochondrial
- Mitochondrial ATP-independent inner membrane protease subunit 1b
Sequence:
MQFLARNLVRRVSRTQVVSRNAYSTQTVRDIGQPTPASHPHLMAEGEVTPGIRIEEYIGRRKKLVELLPENSLAIISSAPVKMMTDVVPYTFRQDADYLYLTGCQQPGGVAVLSDERGLCMFMPESTPKDIAWEGEVAGVDAASEVFKADQAYPISKLPEILSDMIRHSSKVFHNVQSASQRYTNLDDFQNSASLGKVKTLSSLTHELRLIKSPAELKLMRESASIACQGLLKTMLHSKGFPDEGILSAQVEYECRVRGAQRMAFNPVVGGGSNASVIHYSRNDQRIKDGDLVLMDMGCELHGYVSDLTRTWPPCGKFSSVQEELYDLILQTNKECIKQCKPGTTIRQLNTYSTELLCDGLMKMGILKSRRLYHQLNPTSIGHYLGMDVHDSSAVGYDRPLQPGFVITIEPGVYIPSSFDCPERFQGIGIRIEDDVLITETGYEVLTGSMPKEIKHIETLLNNHCHDNSARTSPVSLCKVKGLHTNRNPRRLF
Protein: Transcription factor MafK (Erythroid transcription factor NF-E2 p18 subunit) (Q61827)
Organism: Mus musculus (Mouse)
Function: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves (By similarity). However, they act as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1/NRF1, NFE2L2/NRF2 and NFE2L3/NRF3, and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NF-E2 transcription factor (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Transcription factor NF-E2 45 kDa subunit
- Nuclear factor erythroid 2-related factor 2
- Transcription regulator protein BACH1
- Transcription regulator protein BACH2
- Transcription factor MafG
- Histone deacetylase 3
- Endoplasmic reticulum membrane sensor NFE2L1
- Nuclear factor erythroid 2-related factor 3
- Fos-related antigen 2
- Transcription factor Jun
Sequence:
MTTNPKPNKALKVKKEAGENAPVLSDDELVSMSVRELNQHLRGLTKEEVTRLKQRRRTLKNRGYAASCRIKRVTQKEELERQRVELQQEVEKLARENSSMRLELDALRSKYEALQTFARTVARGPVTPTKVATTSVITIVKSAELSSTSVPFSAAS
Protein: Protein AF-9 homolog (P53930)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the SWR1 complex which mediates the ATP-dependent exchange of histone H2A for the H2A variant HZT1 leading to transcriptional regulation of selected genes by chromatin remodeling. Component of the NuA4 histone acetyltransferase complex which is involved in transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4 and H2A. The NuA4 complex is also involved in DNA repair. Yaf9 may also be required for viability in conditions in which the structural integrity of the spindle is compromised.
Subcellular location: Cytoplasm. Nucleus.
Interaction partners:
- Chromatin modification-related protein EAF6
- Chromatin modification-related protein EAF7
- SWR1-complex protein 5
- SWR1-complex protein 4
- Vacuolar protein sorting-associated protein 72
- Chromatin modification-related protein EAF3
- Vacuolar protein sorting-associated protein 71
- Enhancer of polycomb-like protein 1
- Something about silencing protein 5
- Chromatin modification-related protein YNG2
Sequence:
MAPTISKRIKTLSVSRPIIYGNTAKKMGSVKPPNAPAEHTHLWTIFVRGPQNEDISYFIKKVVFKLHDTYPNPVRSIEAPPFELTETGWGEFDINIKVYFVEEANEKVLNFYHRLRLHPYANPVPNSDNGNEQNTTDHNSKDAEVSSVYFDEIVFNEPNEEFFKILMSRPGNLLPSNKTDDCVYSKQLEQEEIDRIEIGIEKVDKEIDELKQKLENLVKQEAINGS
Protein: Trans-sialidase, putative (Q585U3)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MRVVYQRFFPVLLLLLSLEHLCSRHACADEGEEGGVNHTVGGNLTGTHSYRSPSLLSIGDSLVTVSETWDPSDTEQYVDVITEYSAHYGAPAVTQVAVRNDTLDFHAVYKHKEDRESTMHPTAVAIDGMIFVLIFCKNIGASGNQTGDAVIMPHVAKGVVLPGGATGNVWVNWTQLMPIRSLLPKVIEGKRVSMFFGGGGNTIVMTKGTLVMPVQMVRTDDQRFATIIYSSNNGTSWTVAKGFTDSGCRESSVLIWKRKMLLVARSDDGYTKVFESDYMGDVWTESLGTISRVLGNSPDRRGPGNQGSAITIPLGNETVMFFTQTTVSNSSDSNEGDINRIDQRIWFSDGSRMVKVGHIYWNDHLSSSRSYLLYSNNRLLCAYEMGAEKAYAITVRSLVGELENARFARETWARQDAYISGICSSAKESAPCASGVPVDGLVGLLSSMVNGTAWVDAYFSVNANFVGGLAGPAGLTFEGTARGGRWPVGVQGQNQRFHFANTHFTLVLTLTIHEQTAPRAPVLVTRLYENGSYIDLEFSYTDDKRWHIKYGAEYGSTSGQWALNQEHQLAFVLRGGTIAVYLDGKRMPTMARMLAGNGNLLNITHFYIGGYGTVKQSPRDRLTIRNAMLYNRPLKKAEIDKLFAAKSGITAATKGIEPLTPKWNHKTKDLEPQSGDGRADHAFRTPSWALPLFVLHLYSLFM
Protein: General odorant-binding protein 2 (GOBP 2) (Q95VP2)
Organism: Epiphyas postvittana (Light brown apple moth)
Function: Present in the aqueous fluid surrounding olfactory sensory dendrites and are thought to aid in the capture and transport of hydrophobic odorants into and through this fluid.
Interaction partners:
Sequence:
MASYWAVCVVLVAGSHLVAGTAEVMSHVTAHFGKALEQCREESGLSTAVLEEFQHFWRDDFEVVHRELGCAILCMSNKFSLMQDDARMHHENMHDYVKSFPQGEVLSAKMVELIHNCEKPYDDIKDDCERVVKVAACFKVDAKKAGIAPEVAMIEAVMEKY
Protein: Thioredoxin reductase 1, cytoplasmic (TR) (EC 1.8.1.9) (Peroxidase TXNRD1) (EC 1.11.1.2) (Thioredoxin reductase TR1) (Q9JMH6)
Organism: Mus musculus (Mouse)
Function: Reduces disulfideprotein thioredoxin (Trx) to its dithiol-containing form. Homodimeric flavoprotein involved in the regulation of cellular redox reactions, growth and differentiation. Contains a selenocysteine residue at the C-terminal active site that is essential for catalysis. Also has reductase activity on hydrogen peroxide (H2O2).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10721726}.
Interaction partners:
- Thioredoxin
- Selenide, water dikinase 2
- Selenocysteine lyase
- Cystathionine gamma-lyase
- Selenide, water dikinase 1
- Kynurenine--oxoglutarate transaminase 3
- Kynurenine--oxoglutarate transaminase 1
- Thioredoxin reductase 2, mitochondrial
- Thioredoxin reductase 3
- Thioredoxin, mitochondrial
Sequence:
MPVDDCWLYFPASRGRTFVQTVWVAPTCPNCCWFPGFLPPVPRPPHVPRVLLRGPRGAVLPASRPSKTLPSSSQTPCPTDPCICPPPSTPDSRQEKNTQSELPNKKGQLQKLPTMNGSKDPPGSYDFDLIIIGGGSGGLAAAKEAAKFDKKVLVLDFVTPTPLGTRWGLGGTCVNVGCIPKKLMHQAALLGQALKDSRNYGWKVEDTVKHDWEKMTESVQSHIGSLNWGYRVALREKKVVYENAYGRFIGPHRIVATNNKGKEKIYSAERFLIATGERPRYLGIPGDKEYCISSDDLFSLPYCPGKTLVVGASYVALECAGFLAGIGLDVTVMVRSILLRGFDQDMANKIGEHMEEHGIKFIRQFVPTKIEQIEAGTPGRLRVTAQSTNSEETIEGEFNTVLLAVGRDSCTRTIGLETVGVKINEKTGKIPVTDEEQTNVPYIYAIGDILEGKLELTPVAIQAGRLLAQRLYGGSNVKCDYDNVPTTVFTPLEYGCCGLSEEKAVEKFGEENIEVYHSFFWPLEWTVPSRDNNKCYAKIICNLKDDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTLSVTKRSGGDILQSGCUG
Protein: N-alpha-acetyltransferase 35, NatC auxiliary subunit (Embryonic growth-associated protein) (Protein MAK10 homolog) (Q6PHQ8)
Organism: Mus musculus (Mouse)
Function: Auxillary component of the N-terminal acetyltransferase C (NatC) complex which catalyzes acetylation of N-terminal methionine residues. Involved in regulation of apoptosis and proliferation of smooth muscle cells.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16484612}.
Interaction partners:
- N-alpha-acetyltransferase 30
- N-alpha-acetyltransferase 38, NatC auxiliary subunit
- N-alpha-acetyltransferase 25, NatB auxiliary subunit
- N-alpha-acetyltransferase 20
- N-alpha-acetyltransferase 50
- N-alpha-acetyltransferase 10
- N-alpha-acetyltransferase 15, NatA auxiliary subunit
- N-alpha-acetyltransferase 11
- Small nuclear ribonucleoprotein E
- N-alpha-acetyltransferase 16, NatA auxiliary subunit
Sequence:
MVMKATVDDDASGWELGVPEKMEKSSTSWVDITQDFEDACRELKLGELLHDKLFGLFEAMSAIEMMDPKMDAGMIGNQVNRKVLNFEQAIKDGTIKIKDLSLPELIGIMDTCFCCLITWLEGHSLAQTVFTCLYIHNPDFIEDPAMKAFALGILKICDIAREKVNKAAVFEEEDFQSMTYGFKMANSVTDLRVTGMLKDVEDDLQRRVKSTRSRQGEERDPEVELEHQQCLAAFSRVKFTRVLLTVLIAFTKKETSAVAEAQKLMVQAADLLSAIHTSLHHGIQAQNGTTKGDHPIMMGFEPLVNQRLLPPTFPRYAKIIKREEMVNYFSRLIDRIKTVCEVVNLPNLHCILDFFCEFSEQSPCVLSRSLLQTTFLVDNKKVFGTHLMQDMVKDALRSFVSPPVLSPKCCLYNNHQAKDCIDSFVTHCVRPFCSLVQIHGHNRARQRDKLGHILEEFATLQDEAEKVDAALHTMLLKQEPQRQHLACLGTWVLYHNLRIMIQYLLSGFELELYSMHEYYYIYWYLSEFLYAWLMSTLSRADGSQMAEERIMEEQQKGRSSKKTKKKKKVRPLSREITMSQAYQNMCAGMFKTMVAFDMDGKVRKPKFELDSEQVRYEHRFAPFNSVMTPPPVHYLQFKEMSDLNKYSPPPQSPELYVAASKHFQQAKMILENIPNPDREVSRILKVAKPNFVVMKLLAGGHKKESKVPPEFDFSVHKYFPVVKLV
Protein: GH08338p (Q95TA4)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSVQDHNWDVLIFTQQWPVTTCYHWREENPDQECSLPQKKEFWTIHGIWPTKLHQMGPNFCNNSANFDPSKLNPIEDRLETFWPDLKGMDSTEWLWKHEWQKHGTCAMLVEELDNELKYFEQGLTWREEYIMSRILDASDIHPDSNNTVAAINNAIVKALGKNPSIHCLYDGKHGISYLSEIRICFSKSLELIDCDGIKQGDAVPVGVPGGTIITNCHIGSLVHYPSLVPPLQRKSHWKLPLVNVYKLLQFLMWFTL
Protein: Serine/threonine-protein kinase ENV7 (EC 2.7.11.1) (Late endosome and vacuole interface protein 7) (Q12003)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Serine/threonine-protein kinase involved in vacuolar processing and morphology.
Subcellular location: Vacuole membrane {ECO:0000269|PubMed:14562095}; Peripheral membrane protein {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Casein kinase I homolog 3
- Uncharacterized protein ANR2
- Endonuclease NBR9
Sequence:
MISIVLELFQNLCCCRGFSDATIRVNDKRYRIQRLLGEGGMSFVYLVQLSKNSLIIDNGIATPELYALKKIICPSVESISNGMREIENYKRFQSPYVIKSIDSQVMQEKDGSKTIYIVLPYYSLGSLQDSINRRLLEGTFVSEAECVRIMLGVTRGLLCLHDPASRQDNATSRVNVDAVSMTYSDETAMLLEDTPLEMDMLSSNSAGSIAYAHRDITPSNILFSSDGLPVIGDLGSCSQADITIENRHQLSELQEWVNDNCTLPYTPPELLNLKLNQVLSSKVDIWSLGCTFYTLMFGISPFEREEQIHGASLTYAINTGKYSFPRNSRFSEGLLSVIKKCIQVDPIQRPTTSQLLNLLQDLDT
Protein: Phosphatidylinositol 3-kinase regulatory subunit beta (PI3-kinase regulatory subunit beta) (PI3K regulatory subunit beta) (PtdIns-3-kinase regulatory subunit beta) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit beta) (PI3-kinase subunit p85-beta) (PtdIns-3-kinase regulatory subunit p85-beta) (O08908)
Organism: Mus musculus (Mouse)
Function: Regulatory subunit of phosphoinositide-3-kinase (PI3K), a kinase that phosphorylates PtdIns(4,5)P2 (Phosphatidylinositol 4,5-bisphosphate) to generate phosphatidylinositol 3,4,5-trisphosphate (PIP3). PIP3 plays a key role by recruiting PH domain-containing proteins to the membrane, including AKT1 and PDPK1, activating signaling cascades involved in cell growth, survival, proliferation, motility and morphology. Binds to activated (phosphorylated) protein-tyrosine kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Indirectly regulates autophagy (By similarity). Promotes nuclear translocation of XBP1 isoform 2 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement.
Interaction partners:
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphoinositide 3-kinase regulatory subunit 5
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Epidermal growth factor receptor
- RAC-alpha serine/threonine-protein kinase
Sequence:
MAGAEGFQYRAVYPFRRERPEDLELLPGDLLVVSRVALQALGVADGGERCPHNVGWMPGFNERTRQRGDFPGTYVEFLGPVALARPGPRPRGPRPLPARPLDGSSESGHILPDLAEQFSPPDPAPPILVKLVEAIEQAELDSECYSKPELPATRTDWSLSDLEQWDRTALYDAVKGFLLALPAAVVTPEAAAEAYRALREVAGPVGLVLEPPTLPLHQALTLRFLLQHLGRVARRAPSPDTAVHALASAFGPLLLRIPPSGGEGDGSEPVPDFPVLLLERLVQEHVEEQDAAPPALPPKPSKAKPAPTALANGGSPPSLQDAEWYWGDISREEVNERLRDTPDGTFLVRDASSKIQGEYTLTLRKGGNNKLIKVFHRDGHYGFSEPLTFCSVVELISHYRHESLAQYNAKLDTRLLYPVSKYQQDQVVKEDSIEAVGAQLKVYHQQYQDKSREYDQLYEEYTRTSQELQMKRTAIEAFNETIKIFEEQGQTQEKCSKEYLERFRREGNEKEMQRILLNSERLKSRIAEIHESRTKLEQDLRAQASDNREIDKRMNSLKPDLMQLRKIRDQYLVWLTQKGARQRKINEWLGIKNETEDQYSLMEDEDALPHHEERTWYVGKINRTQAEEMLSGKRDGTFLIRESSQRGCYACSVVVDGDTKHCVIYRTATGFGFAEPYNLYGSLKELVLHYQHASLVQHNDALTVTLAHPVRAPGPGPPSAAR
Protein: Uncharacterized protein (Q57YM4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MVRWGGPRFEFYFTRDFLNHEYLIKKEEAQRAAFIHSKREHERAKEDARFAEAEQKKAQLQEEAQRLMSAEVEEAARRAAAEAAAQNTAHARRLRRLKELAVPVIRGSSAHSAGSHGCVMYPTPKGVPLPMGRDRAPYTPGVDRHRIVPPPPEPGAHKPWQGSGTAWMTDKNNDWQKQYYFTKSKRPAETLRERRACIDKMERCHTNEGAAKKPPVNQDESPANDQREIPTFGTERQHDEMGSESESERPLSIFSHGSSNAPIRALGTQHMGDISTKEEVREFLRRYPTGVVPPRDRRAAPPNFNGMNLTELTSSLIKMQKCNLCGGHP
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (Q388P9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MTPPVRLGPYCLGEKLGFGNFSTVRLATDEGGKKFAVKIIDKTRLRKEKMEDQMLREVAIMRSIKHRNVIDLHDVLESANHYYLVLEFVSGGELFDKIVAAKRFDEPTARRYFQQLIAGVHHCHGKGFAHRDLKPENLLLDAVGVLKISDFGLGNRQQDILLKTVCGTPNYVAPEVLMERGYNGLCADIWSCGVILYVMLAGRLPFEDRSMRHLLARIERGEYSMVRHVSDAAKDLIARMLVVNPKKRITLEAIISHPWFVVDWDPKCLNESA
Protein: Modulator of VRAC current 1 (A6PVC3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MTQEPFREELAYDRMPTLERGRQDPASYAPDAKPSDLQLSKRLPPCFSHKTWVFSVLMGCIPSAIVSFTVSRRNANVIPNFQILFVSTFAVTTTCLIWFGCKLVLNPSAININFNLILLLLLELLMAATVIIAARSSEEDCKKKKGSMSDSANILDEVPFPARVLKSYSVVEVIAGISAVLGGIIALNVDDSVSGPHLSVTFFWILVACFPSAIASHVAAECP
Protein: Muscarinic acetylcholine receptor M2 (P10980)
Organism: Rattus norvegicus (Rat)
Function: The muscarinic acetylcholine receptor mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins. Primary transducing effect is adenylate cyclase inhibition. Signaling promotes phospholipase C activity, leading to the release of inositol trisphosphate (IP3); this then triggers calcium ion release into the cytosol (By similarity).
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Note=Phosphorylation in response to agonist binding promotes receptor internalization. {ECO:0000250}.
Interaction partners:
- Guanine nucleotide-binding protein subunit gamma
- Proteinase-activated receptor 1
- Muscarinic acetylcholine receptor M1
- Guanine nucleotide-binding protein subunit gamma
- Lysophosphatidic acid receptor 4
- Lysophosphatidic acid receptor 5
- Lysophosphatidic acid receptor 1
- Lysophosphatidic acid receptor 2
- Lysophosphatidic acid receptor 6
- Lysophosphatidic acid receptor 3
Sequence:
MNNSTNSSNNGLAITSPYKTFEVVFIVLVAGSLSLVTIIGNILVMVSIKVNRHLQTVNNYFLFSLACADLIIGVFSMNLYTLYTVIGYWPLGPVVCDLWLALDYVVSNASVMNLLIISFDRYFCVTKPLTYPVKRTTKMAGMMIAAAWVLSFILWAPAILFWQFIVGVRTVEDGECYIQFFSNAAVTFGTAIAAFYLPVIIMTVLYWHISRASKSRIKKEKKEPVANQDPVSPSLVQGRIVKPNNNNMPGGDGGLEHNKIQNGKAPRDGVTENCVQGEEKESSNDSTSVSAVASNMRDDEITQDENTVSTSLGHSRDDNSKQTCIKIVTKAQKGDVCTPTSTTVELVGSSGQNGDEKQNIVARKIVKMTKQPAKKKPPPSREKKVTRTILAILLAFIITWAPYNVMVLINTFCAPCIPNTVWTIGYWLCYINSTINPACYALCNATFKKTFKHLLMCHYKNIGATR
Protein: P2X purinoceptor 2 (P2X2) (ATP receptor) (Purinergic receptor) (P49653)
Organism: Rattus norvegicus (Rat)
Function: Ion channel gated by extracellular ATP involved in a variety of cellular responses, such as excitatory postsynaptic responses in sensory neurons, neuromuscular junctions (NMJ) formation, hearing, perception of taste and peristalsis. In the inner ear, regulates sound transduction and auditory neurotransmission, outer hair cell electromotility, inner ear gap junctions, and K(+) recycling. Mediates synaptic transmission between neurons and from neurons to smooth muscle (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:15313628}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P56373}.
Interaction partners:
- P2X purinoceptor 3
- P2X purinoceptor 6
- P2X purinoceptor 1
- P2X purinoceptor 4
- P2X purinoceptor 5
- Glutamate receptor ionotropic, NMDA 2C
- Glutamate receptor ionotropic, NMDA 1
- Glutamate receptor ionotropic, NMDA 2D
- Glutamate receptor ionotropic, NMDA 2A
- P2Y purinoceptor 4
Sequence:
MVRRLARGCWSAFWDYETPKVIVVRNRRLGFVHRMVQLLILLYFVWYVFIVQKSYQDSETGPESSIITKVKGITMSEDKVWDVEEYVKPPEGGSVVSIITRIEVTPSQTLGTCPESMRVHSSTCHSDDDCIAGQLDMQGNGIRTGHCVPYYHGDSKTCEVSAWCPVEDGTSDNHFLGKMAPNFTILIKNSIHYPKFKFSKGNIASQKSDYLKHCTFDQDSDPYCPIFRLGFIVEKAGENFTELAHKGGVIGVIINWNCDLDLSESECNPKYSFRRLDPKYDPASSGYNFRFAKYYKINGTTTTRTLIKAYGIRIDVIVHGQAGKFSLIPTIINLATALTSIGVGSFLCDWILLTFMNKNKLYSHKKFDKVRTPKHPSSRWPVTLALVLGQIPPPPSHYSQDQPPSPPSGEGPTLGEGAELPLAVQSPRPCSISALTEQVVDTLGQHMGQRPPVPEPSQQDSTSTDPKGLAQL
Protein: Eumenine mastoparan-OD (EMP-OD) (Venom peptide 1) (OdVP1) (VP1) (P86146)
Organism: Orancistrocerus drewseni (Solitary wasp)
Function: Has potent hemolytic activity against ovine erythrocytes at micromolar concentrations. Also exhibits strong antimicrobial activity against the fungi C.albicans and B.cinerea, and weaker activity against the Gram-negative bacterium E.coli and Gram-positive bacterium S.aureus.
Subcellular location: Secreted {ECO:0000269|PubMed:18695936, ECO:0000269|PubMed:19857508}. Target cell membrane {ECO:0000305}. Note=Has an amphipathic alpha-helical conformation. {ECO:0000305|PubMed:21184791}.
Interaction partners:
Sequence:
MKQTIVIVLLAAVAMMACLQMVAAEPLPEAAPAPSPLAEAEALASPIAEALANPEALASPEAGRILSFIKGLAEHLGKK