wanglab/gogpt-training-data huggingface dataset:
Protein: Aurora kinase (EC 2.7.11.1) (Increase-in-ploidy protein 1) (Spindle assembly checkpoint kinase) (P38991)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for high-fidelity chromosome segregation during the later part of each cell cycle. Acts in opposition to the phosphatase PP1. Has a role in attaching the kinetochores to the microtubules and ensuring that sister kinetochores connect to opposite poles. The promotion of bi-orientation is achieved by selectively detaching kinetochore-microtubule attachments that are not under tension. Phosphorylates histone H3 to form H3S10ph during mitosis and meiosis. Phosphorylates RGD1 in vitro.
Subcellular location: Nucleus. Cytoplasm, cytoskeleton, spindle. Chromosome, centromere, kinetochore. Note=Associates with the mitotic spindle and on elongated and disassembling spindles. Also associated with the kinetochore.
Interaction partners:
- Inner centromere protein SLI15
- Chromosomal passenger complex protein BIR1
- Kinetochore protein NDC80
- N-terminal-borealin-like protein
- Protein BIM1
- Histone H3
- Centromere DNA-binding protein complex CBF3 subunit A
- Serine/threonine-protein phosphatase PP1-2
- Kinesin-like protein CIN8
- DASH complex subunit DAM1
Sequence:
MQRNSLVNIKLNANSPSKKTTTRPNTSRINKPWRISHSPQQRNPNSKIPSPVREKLNRLPVNNKKFLDMESSKIPSPIRKATSSKMIHENKKLPKFKSLSLDDFELGKKLGKGKFGKVYCVRHRSTGYICALKVMEKEEIIKYNLQKQFRREVEIQTSLNHPNLTKSYGYFHDEKRVYLLMEYLVNGEMYKLLRLHGPFNDILASDYIYQIANALDYMHKKNIIHRDIKPENILIGFNNVIKLTDFGWSIINPPENRRKTVCGTIDYLSPEMVESREYDHTIDAWALGVLAFELLTGAPPFEEEMKDTTYKRIAALDIKMPSNISQDAQDLILKLLKYDPKDRMRLGDVKMHPWILRNKPFWENKRL
Protein: Mushroom body defect, isoform G (Q8IR54)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MDTRSWRKVLLQWIGECHFIESNYITLEQSDLDSFFSVFIQKIQETENVKGKNELQDQPTEQSPLVQEFLAHNYPEFIAQQDDKEVDLPLDCLYVYTLLLHYSCVKKPSLFFHNICNKLPELTQTCIASFFRETVDRLLTREYLSQAIANVAVVYRQGVSTSVSPCLPSSSLSPDPRSDDAPCPSTPSSSSSQPSSSTPQLRNHREQLRLNGCEMPPPSTPKTELLEQRTKELRGIRTQLEVVRYEKALLEEQQMEKDELIKVLNKEKMMAKMELEKLRNVKLTEEHHDNESHHIMPYEFEHMKGCLLKEIGLKESLIAEITDKLHDLRVENSELSEKLNLAGKRLLEYTDRIRFLESRVDDLTRIVSSRDVMISSLESDKQELDKCLKEARDDLHNRIEVLNASSDLLDCSLSPNTTPENLASSVIDKQLREKEHENAELKEKLLNLNNSQRELCQALSSFLQKHNIDHEFPVEWTSSSLLSTISAIESKFVNTLEKSTQMKKECDVQSVCVEKLLEKCKLLSVSLGCQPKELDGFEATIPEAMESGFESSRECETILSCCHMKVVDIASKNNDLELDNERLNDKCAELKSIIDRGDQHLADINLQLIEKEKQIKDVGAEIQELRKRNINLENMLSQIADKEASAASHAQHLKQCGELLRAKYEVCRNELIAKNAAQDELVRMMMVPDGETLNGRVRQLIDLEMMHDEHNKMYAQMLKQLNELSAKHDNMTHSHLDFVKRTEIELETKNAQIMAFDEHNNHFDRFLTRIFTLLRSRNCPKSTTMGSATNFLESMHIEKRFENIEMLIEGQLLSADDLKRELDDLRSKNEELAKQNINGIIKRNKFITSLEVNTEKVKQYITDLEEEAFKRKQKVVQLENTLSKEQSNAKEMAQRLDIAQQEIKDYHVEAIRFINTIRDRLQQDFNGVNTPQQLGTCMTEFLKMYDQMEVRYEESSSLVEKLTESQAKLEMQVAELQVELENKDTNQHSGALIKQLNDTIQNLEKVNAKLSEDNTVSHTVHSKLNESLLKAQKELDLRAKIIENLEASERNLSMKLCELKDLKNKLKSSDEKIAQIKETYEEQIKALQAKCDMEAKKNEHLERNQNQSLTQLKEDALENCVLMSTKLEELQAKLQEGQQLVDSQKLELDMNRKELALVKSAYEAQTKLSDDLQRQKESGQQLVDNLKVELEKERKELAHVNSAIGAQTKLSDDLECQKESGQQLVDNLKVELEKERKELAQVKSVIEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVNSAFEAQTKLSDDLQREKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAKVKSVIEAQTKLSDDLQRQKESAQQLEAQTKLSDDLQRQKESAQQLVDNLKVELDKERKELAQVKSVIEAQTKLSDDLQRQKESAQQLVDNLKMELDKERKELAQVKSAIGAQTKLSDDLECQKESVQQLVDNLKVELEKERKELAKVNSAFEAQTKLSDDLKLQKEDAQREVFLVKERLVKEKREFEVKLATLEDIIETLEMRCTQMEEERATAYEQINKLENRCQEKDNVKSSQLQVETFKVECLHHQLKSEMATHNSLVEDLNRKLAEKVSKLDFVQSRLMTEIAEHNQVKDQLAQITDIPKVVELQHRLEAETAEREEAQNKLAVVTGRLDEITRELDNARLEHGAQILRMEETAREVGNKNAELCELIEFYRNRVEALERLLLASNQELEELNSIQSNQAEGVRDLGDTYSAAEGRQTESDQDKERYQKLALDCKILQAKYRDAKDEIKRCEKKIKDQRLEMEGKLEKMKNKMKGSRRRRWPQLMLLFIGLIILIVFFLYYILYISGINVIFKSRSPIVY
Protein: 4-1BB variant 2 (I2E6E0)
Organism: Sus scrofa (Pig)
Interaction partners:
Sequence:
MGNGYYNIVATVLLVMNFERTRSVPDPCSNCSAGTFCGKNIQELCMPCPSNSFSSTSGQKACNVCRKCEGVFRTKKECSSTSNAVCECVPGFRCLGAGCAMCEEYCQQGQELTQEGCKDCSFGTFNDEEHGVCRPWTDCSLAGKPVLMNGTKARDVVCGPRPTDFSPGHTSHVIIFFLALMSTAVFVLVSYLALRFSVVQQGRKKLLYIVKQPFLKPAQTVQEEDACSCRFPEEEEGECEL
Protein: Lysophospholipase 3 (EC 3.1.1.5) (Phospholipase B 3) (Q08108)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Sequentially removes both fatty acyl groups from diacylglycerophospholipids and therefore has both phospholipase A and lysophospholipase activities. Substrate preference is phosphatidylserine > phosphatidylinositol. Does not cleave phosphatidylcholine, phosphatidylethanolamine, phosphatidic acid and phosphatidylinositol-bisphosphate. Mainly responsible for the degradation of phosphatidylinositol in vivo.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10497163}; Lipid-anchor, GPI-anchor {ECO:0000305}.
Interaction partners:
- Lysophospholipase NTE1
- Glycerophosphocholine phosphodiesterase GDE1
- Lysophospholipid acyltransferase
- Triacylglycerol lipase 5
- Triacylglycerol lipase 4
- Lysophospholipase 2
- Lysophospholipase 1
Sequence:
MIRPLCSKIIISYIFAISQFLLAANAWSPTDSYVPGTVSCPDDINLVREATSISQNESAWLEKRNKVTSVALKDFLTRATANFSDSSEVLSKLFNDGNSENLPKIAVAVSGGGYRSMLTGAGVLAAMDNRTEGAYEHGLGGLLQSTTYLSGASGGNWLVGTLALNNWTSVQDILNNMQNDDSIWDLSDSIVTPGGINIFKTAKRWDHISNAVESKQNADYNTSLADIWGRALAYNFFPSLNRGGIGLTWSSIRDFPVFQNAEMPFPISVADGRYPGTKVINLNATVFEFNPFEMGSWDPSLNSFANVKYLGTNVSNGVPLERGKCTAGFDNAGFIMGTSSTLFNQFLLRINSTHLPSFITRLARHFLKDLSQDFNDIAVYSPNPFKDTKFLDSDYTTSIVDSDSLFLVDGGEDDENVPVLPLIQKERDVDIIFAVDNSADMRLAWPDGSSLVHTYERQFVKQGQGMSFPYVPDTNTFVNLGLNKKPTFFGCDANNLTDLQYIPPLVVYLPNAEYSFNSNQSAFKLSYSESQRRSMIQNGFEIATRNNFTDDPEFMGCVGCAIIRRKQQALNITLPPECETCFKNYCWNGTLDTTPLPDVEKDVHHSFINVNSFNSSIGQEESLYAGSSASQSSSSSSSSSSSSEIPSATATLEKKAATNSGSHLSGISVKFSAMIMLTLLMFTGAV
Protein: Amine oxidase (EC 1.4.3.-) (Q96X16)
Organism: Komagataella pastoris (Yeast) (Pichia pastoris)
Interaction partners:
Sequence:
MRLTNLLSLTTLVALAVAVPDFYQKREAVSSKEAALLRRDASAECVSNENVEIEAPKTNIWTSLAKEEVQEVLDLLHSTYNITEVTKADFFSNYVLWIETLKPNKTEALTYLDEDGDLPPRNARTVVYFGEGEEGYFEELKVGPLPVSDETTIEPLSFYNTNGKSKLPFEVGHLDRIKSAAKSSFLNKNLNTTIMRDVLEGLIGVPYEDMGCHSAAPQLHDPATGATVDYGTCNINTENDAENLVPTGFFFKFDMTGRDVSQWKMLEYIYNNKVYTSAEELYEAMQKDDFVTLPKIDVDNLDWTVIQRNDSAPIRHLDDRKSPRLVEPEGRRWAYDGEEEYFSWMDWGFYTSWSRDTGISFYDITFKGERIVYELSLQELIAEYGSDDPFNQHTFYSDISYGVGNRFSLVPGYDCPATAGYFTTDTFEYDEFYNRTLSYCVFENQEDYSLLRHTGASYSAITQNPTLNVRFISTIGNYDYNFLYKFFLDGTLEVSVRAAGYIQAGYWNPETSAPYGLKIHDVLSGSFHDHVLNYKVDLDVGGTKNRASKYVMKDVDVEYPWAPGTVYNTKQIAREVLEKEDFNGINWPENGQGILLIESAEETNSFGNPRAYNIMPGGGGVHRIVKNSRSGPETQNWARSNLFLTKHKDEELRSSTALNTNALYDPPVNFNAFLDDESLDGEDIVAWVNLGLHHLPNSNDLPNTIFSTAHASFMLTPFNYFDSENSRDTTQQVFYTYDDETEESNWEFYGNDWSSCGLEVPEPNFEDYTYGRGTRINKKMTNSDEVY
Protein: C-C chemokine receptor type 6 (C-C CKR-6) (CC-CKR-6) (CCR-6) (Chemokine receptor-like 3) (CKR-L3) (DRY6) (G-protein coupled receptor 29) (GPR-CY4) (GPRCY4) (LARC receptor) (CD antigen CD196) (P51684)
Organism: Homo sapiens (Human)
Function: Receptor for the C-C type chemokine CCL20. Binds to CCL20 and subsequently transduces a signal by increasing the intracellular calcium ion levels. Although CCL20 is its major ligand it can also act as a receptor for non-chemokine ligands such as beta-defensins. Binds to defensin DEFB1 leading to increase in intracellular calcium ions and cAMP levels. Its binding to DEFB1 is essential for the function of DEFB1 in regulating sperm motility and bactericidal activity. Binds to defensins DEFB4 and DEFB4A/B and mediates their chemotactic effects. The ligand-receptor pair CCL20-CCR6 is responsible for the chemotaxis of dendritic cells (DC), effector/ memory T-cells and B-cells and plays an important role at skin and mucosal surfaces under homeostatic and inflammatory conditions, as well as in pathology, including cancer and various autoimmune diseases. CCR6-mediated signals are essential for immune responses to microbes in the intestinal mucosa and in the modulation of inflammatory responses initiated by tissue insult and trauma. CCR6 is essential for the recruitment of both the pro-inflammatory IL17 producing helper T-cells (Th17) and the regulatory T-cells (Treg) to sites of inflammation. Required for the normal migration of Th17 cells in Peyers-patches and other related tissue sites of the intestine and plays a role in regulating effector T-cell balance and distribution in inflamed intestine. Plays an important role in the coordination of early thymocyte precursor migration events important for normal subsequent thymocyte precursor development, but is not required for the formation of normal thymic natural regulatory T-cells (nTregs). Required for optimal differentiation of DN2 and DN3 thymocyte precursors. Essential for B-cell localization in the subepithelial dome of Peyers-patches and for efficient B-cell isotype switching to IgA in the Peyers-patches. Essential for appropriate anatomical distribution of memory B-cells in the spleen and for the secondary recall response of memory B-cells (By similarity). Positively regulates sperm motility and chemotaxis via its binding to CCL20.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23765988}; Multi-pass membrane protein {ECO:0000255}. Cell surface {ECO:0000269|PubMed:12081481}.
Interaction partners:
- C-C motif chemokine 20
- Defensin beta 4A
- C-C motif chemokine 2
- Beta-defensin 1
- C-X-C motif chemokine 16
- C-C motif chemokine 19
- Beta-defensin 103
- C-C chemokine receptor type 2
- C-X-C motif chemokine 9
- C-C motif chemokine 3
Sequence:
MSGESMNFSDVFDSSEDYFVSVNTSYYSVDSEMLLCSLQEVRQFSRLFVPIAYSLICVFGLLGNILVVITFAFYKKARSMTDVYLLNMAIADILFVLTLPFWAVSHATGAWVFSNATCKLLKGIYAINFNCGMLLLTCISMDRYIAIVQATKSFRLRSRTLPRSKIICLVVWGLSVIISSSTFVFNQKYNTQGSDVCEPKYQTVSEPIRWKLLMLGLELLFGFFIPLMFMIFCYTFIVKTLVQAQNSKRHKAIRVIIAVVLVFLACQIPHNMVLLVTAANLGKMNRSCQSEKLIGYTKTVTEVLAFLHCCLNPVLYAFIGQKFRNYFLKILKDLWCVRRKYKSSGFSCAGRYSENISRQTSETADNDNASSFTM
Protein: Erlin (SPFH domain-containing protein) (Endoplasmic reticulum lipid raft-associated protein) (Stomatin-prohibitin-flotillin-HflC/K domain-containing protein) (E5RHW4)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU369041}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU369041}.
Interaction partners:
Sequence:
MAQLGAVVAVASSFFCASLFSAVHKIEEGHIGVYYRGGALLTSTSGPGFHLMLPFITSYKSVQTTLQTDEVKNVPCGTSGGVMIYFDRIEVVNFLVPNAVYDIVKNYTADYDKALIFNKIHHELNQFCSVHTLQEVYIELFDQIDENLKLALQQDLTSMAPGLVIQAVRVTKPNIPEAIRRNYELMESEKTKLLIAAQKQKVVEKEAETERKKALIEAEKVAQVAEITYGQKVMEKETEKKISEIEDAAFLAREKAKADAECYTAMKIAEANKLKLTPEYLQLMKYKAIASNSKIYFGKDIPNMFMDSAGSVSKQFEGLADKLSFGLEDEPLETATKE
Protein: Protein COS3 (P0CX13)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MKENELKNEKSVDVLSFKQLESQKIVLPQDLFRSSFTWFCYEIYKSLAFRIWMLLWLPLSVWWKLSNNCIYPLIVSLLVLFLGPIFVLVICGLSRKRSLSKQLIQFCKEITENTPSSDPHDWEVVAANLNSYLYENNVWNTKYFFFNAMVCQEAFRTTLLEPFSLKKDKAAKVKSFKDSVPYIEEALGVYFTEVEKQWKLFNTEKSWSPVGLEDAKLPKEAYRFKLTWFLKRISNIFMLIPFLNFLCCIYVSRGMCLLLRTLYLGWILFMLVQGFQNIRVLIMSMEHKMQFLSTIINEQESGANGWDEIARKMNRYLFEKKAWKNEEFFFDGIDCEWFFNHFFYRVLSAKKSMWPLPLNVELWPYIKEAQLSRSEVLLV
Protein: FYVE, RhoGEF and PH domain-containing protein 2 (Zinc finger FYVE domain-containing protein 4) (Q7Z6J4)
Organism: Homo sapiens (Human)
Function: Activates CDC42, a member of the Ras-like family of Rho- and Rac proteins, by exchanging bound GDP for free GTP. Activates JNK1 via CDC42 but not RAC1. Binds to phosphatidylinositol 4,5-bisphosphate, phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Early endosome {ECO:0000250}. Early endosome membrane {ECO:0000250}. Cell projection, ruffle membrane {ECO:0000250}. Note=Recruitment to the endosome and ruffle membrane requires the presence of phosphoinositides. {ECO:0000250}.
Interaction partners:
Sequence:
MKGASEEKLASVSNLVTVFENSRTPEAAPRGQRLEDVHHRPECRPPESPGPREKTNVGEAVGSEPRTVSRRYLNSLKNKLSSEAWRKSCQPVTLSGSGTQEPEKKIVQELLETEQAYVARLHLLDQVFFQELLKTARSSKAFPEDVVRVIFSNISSIYQFHSQFFLPELQRRLDDWTANPRIGDVIQKLAPFLKMYSEYVKNFERAAELLATWTDKSPLFQEVLTRIQSSEASGSLTLQHHMLEPVQRIPRYELLLKEYIQKLPAQAPDQADAQKALDMIFSAAQHSNAAITEMERLQDLWEVYQRLGLEDDIVDPSNTLLREGPVLKISFRRNDPMERYLFLFNNMLLYCVPRVIQVGAQFQVRTRIDVAGMKVRELMDAEFPHSFLVSGKQRTLELQARSQEEMISWMQAFQAAIDQIEKRNETFKAAAQGPEGDIQEQELQSEELGLRAPQWVRDKMVTMCMRCQEPFNALTRRRHHCRACGYVVCARCSDYRAELKYDDNRPNRVCLHCYAFLTGNVLPEAKEDKRRGILEKGSSATPDQSLMCSFLQLIGDKWGKSGPRGWCVIPRDDPLVLYVYAAPQDMRAHTSIPLLGYQVTVGPQGDPRVFQLQQSGQLYTFKAETEELKGRWVKAMERAASGWSPSWPNDGDLSD
Protein: C2H2-type domain-containing protein (Q8MNV9)
Organism: Caenorhabditis elegans
Interaction partners:
Sequence:
MSISGEDNEIILNASLSNSPDQLDVFEESRRNFLESINATVSMTSNGSKNGIEDIANRLKQNGNTTSTSLTSNSGLYPTDPTIISNHTPSMQLSCVECGVTKANSEEMEIHIKTEHLKWLPFQCPMCLVERASDAQMREHLHSSHQKNMSKFIYVDNVKAKRRLQILMDSAFSLNVSERVNAKNHPSSSTSASPYSPTSYHRGMNSSPSSGRNTSTSNGSATSAATASAQAAATAIVNHHKEKEKQTAQATADFLKLLDFTGINGEIGEHKAQSSSTRSSSGRKRPYVPTSATEAITTMELAAPSAESFLASLNSFSHAQTPENEENDHPTLFSVDDLNIDSTSTLATLFGGGARKTKYDDGEMPHDEDPLLDSLNPISVLDNVAALFGSTPDRSVETETKKTSSISKKRVLGECSKCQKPVTAGARQMHMFFHLAKDELIFRFRCKHEGCSVEHYRKDQMENHQSKAHGRIDPDMMEDRSLELFQKCQDLSMELLGTKNGTIPGPTAAKAEIAYAAQQAANAQRVRSRGHGISSTTSQSSNPANSLLAV
Protein: Probable metal-nicotianamine transporter YSL4 (Protein YELLOW STRIPE LIKE 4) (AtYSL4) (Q6R3K8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in the transport of nicotianamine-chelated metals.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Oligopeptide transporter 9
- Oligopeptide transporter 8
- Oligopeptide transporter 2
- Oligopeptide transporter 5
- Oligopeptide transporter 4
- Ferric reduction oxidase 7, chloroplastic
- Oligopeptide transporter 1
- Oligopeptide transporter 6
- Oligopeptide transporter 3
- Protein TIC 21, chloroplastic
Sequence:
METEIPRSTEISETLLLPETNLDHGEYVPEWKEQITIRGLISSALLGILFCIITHKLNLTIGIIPSLNVAAGLLGFFFIKSWTGFLSKLGFLSKPFTKQENTVIQTCVVSCYGLAYSGGFGSYLIAMDERTYKLIGSDYPGNNPEDVINPGLWWMTGFLFVVSFLGLFCLVPLRKVMILDYKLTYPSGTATAMLINSFHNNTGAELAGKQVKCLGKYLSLSLVWSCFKWFFSGIGGACGFDHFPTLGLTLFKNTFYFDFSPTFIGCGMICPHLVNCSVLLGAIISWGFLWPFISQHAGDWYPADLKANDFKGLYGYKVFIAISIILGDGLYNLIKIIVVTVKEICNKSSRQHNLPVFTDILDKSKTSVLMREKKKRDIIFLKDRIPLEFAVSGYVGLAAISTAIIPLIFPPLKWYFVLCSYLVAPGLAFCNSYGAGLTDMSMPSTYGKTGLFIVASIVGNNGGVIAGLAACGIMMSIVSTAADLMQDFKTGYLTLSSAKSMFVTQLLGTAMGCIIAPLTFWLFWTAFDIGDPDGLYKAPYAVIYREMAILGVEGFAKLPKHCLALCCGFFIAALIVNLIRDMTPPKISKLIPLPMAMAGPFYIGAYFAIDMFVGTVIMLVWERMNKKDADDYSGAVASGLICGDGIWTIPSAILSILRINPPICMYFRPS
Protein: Glucocorticoid receptor (GR) (Nuclear receptor subfamily 3 group C member 1) (P06536)
Organism: Rattus norvegicus (Rat)
Function: Receptor for glucocorticoids (GC). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors. Affects inflammatory responses, cellular proliferation and differentiation in target tissues. Involved in chromatin remodeling. Plays a role in rapid mRNA degradation by binding to the 5' UTR of target mRNAs and interacting with PNRC2 in a ligand-dependent manner which recruits the RNA helicase UPF1 and the mRNA-decapping enzyme DCP1A, leading to RNA decay (By similarity). Could act as a coactivator for STAT5-dependent transcription upon growth hormone (GH) stimulation and could reveal an essential role of hepatic GR in the control of body growth (By similarity).
Subcellular location: [Isoform A]: Cytoplasm {ECO:0000250|UniProtKB:P04150}. Nucleus {ECO:0000250|UniProtKB:P04150}. Mitochondrion {ECO:0000269|PubMed:21730050}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P04150}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P04150}. Chromosome {ECO:0000250|UniProtKB:P06537}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P06537}. Note=After ligand activation, translocates from the cytoplasm to the nucleus (By similarity). The hormone-occupied receptor undergoes rapid exchange between chromatin and the nucleoplasmic compartment. In the presence of NR1D1 shows a time-dependent subcellular localization, localizing to the cytoplasm at ZT8 and to the nucleus at ZT20. Lacks this diurnal pattern of localization in the absence of NR1D1, localizing to both nucleus and the cytoplasm at ZT8 and ZT20. Upon dexamethasone binding associates with the glucocorticoid response elements of target genes (By similarity). {ECO:0000250|UniProtKB:P04150, ECO:0000250|UniProtKB:P06537}.
Interaction partners:
- peptidylprolyl isomerase
- Mineralocorticoid receptor
- Prostaglandin E synthase 3
- Peroxisome proliferator-activated receptor gamma coactivator 1-alpha
- Peptidyl-prolyl cis-trans isomerase FKBP4
- Nuclear receptor coactivator
- Heat shock 70 kDa protein 4
- Nuclear receptor coactivator 2
- Glucocorticoid receptor
- Androgen receptor
Sequence:
MDSKESLAPPGRDEVPGSLLGQGRGSVMDFYKSLRGGATVKVSASSPSVAAASQADSKQQRILLDFSKGSTSNVQQRQQQQQQQQQQQQQQQQQQQPDLSKAVSLSMGLYMGETETKVMGNDLGYPQQGQLGLSSGETDFRLLEESIANLNRSTSVPENPKSSTSATGCATPTEKEFPKTHSDASSEQQNRKSQTGTNGGSVKLYPTDQSTFDLLKDLEFSAGSPSKDTNESPWRSDLLIDENLLSPLAGEDDPFLLEGNTNEDCKPLILPDTKPKIKDTGDTILSSPSSVALPQVKTEKDDFIELCTPGVIKQEKLGPVYCQASFSGTNIIGNKMSAISVHGVSTSGGQMYHYDMNTASLSQQQDQKPVFNVIPPIPVGSENWNRCQGSGEDSLTSLGALNFPGRSVFSNGYSSPGMRPDVSSPPSSSSAATGPPPKLCLVCSDEASGCHYGVLTCGSCKVFFKRAVEGQHNYLCAGRNDCIIDKIRRKNCPACRYRKCLQAGMNLEARKTKKKIKGIQQATAGVSQDTSENPNKTIVPAALPQLTPTLVSLLEVIEPEVLYAGYDSSVPDSAWRIMTTLNMLGGRQVIAAVKWAKAILGLRNLHLDDQMTLLQYSWMFLMAFALGWRSYRQSSGNLLCFAPDLIINEQRMSLPCMYDQCKHMLFVSSELQRLQVSYEEYLCMKTLLLLSSVPKEGLKSQELFDEIRMTYIKELGKAIVKREGNSSQNWQRFYQLTKLLDSMHEVVENLLTYCFQTFLDKTMSIEFPEMLAEIITNQIPKYSNGNIKKLLFHQK
Protein: Hypersensitive-induced response protein 2 (AtHIR2) (Q9CAR7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Cell membrane {ECO:0000305|PubMed:15060130, ECO:0000305|PubMed:17644812, ECO:0000305|Ref.8}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305|Ref.8}.
Interaction partners:
- Flotillin-like protein 3
- Calcineurin-binding protein 1
- FAD/NAD
- Flotillin-like protein 2
- AT3g47210/F13I12_260
- At1g01310 superfamily protein)
- Filament-like protein
- Haloacid dehalogenase-like hydrolase
- B3 domain-containing protein REM1
- Transmembrane protein, putative
Sequence:
MGQALGCIQVDQSNVAIKETFGKFDEVLEPGCHCLPWCLGSQVAGHLSLRVQQLDVRCETKTKDNVFVTVVASIQYRALAESAQDAFYKLSNTRNQIQAYVFDVIRASVPKLDLDSTFEQKNDIAKTVETELEKAMSHYGYEIVQTLIVDIEPDVHVKRAMNEINAASRMREAASEKAEAEKILQIKRAEGEAESKYLSGMGIARQRQAIVDGLRNSVLAFSESVPGTSSKDVMDMVLVTQYFDTLKEIGASSKSNSVFIPHGPGAVRDIASQIRDGLLQGNSAAE
Protein: Uncharacterized protein (Q38B96)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- ATP synthase, epsilon chain, putative
- ATP synthase F1 subunit gamma protein, putative
- ATPase subunit 9, putative
- ATP synthase alpha chain
- ATP synthase delta chain
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
- Uncharacterized protein
Sequence:
MIRRSCALLSSSWRDHGISYLKYLNVCTETLHSTVKESRRAKYERWSKPCYTAQRPDGAGGQETIDKVPIHTKDY
Protein: SKP1-like protein 17 (AtSK17) (Protein MEIDOS) (Q9SL65)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in ubiquitination and subsequent proteasomal degradation of target proteins. Together with CUL1, RBX1 and a F-box protein, it forms a SCF E3 ubiquitin ligase complex. The functional specificity of this complex depends on the type of F-box protein. In the SCF complex, it serves as an adapter that links the F-box protein to CUL1 (By similarity). Probably implicated in incompatibility response after hybridization.
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Cullin-1
- Cullin-like protein 3
- Cullin-2
- Putative cullin-like protein 1
- Putative cullin-like protein 2
- RING-box protein 1a
- RING-box protein 1b
- F-box protein 7
- Elongin-C
- Putative high mobility group B protein 11
Sequence:
MSSKKIVLTSSDDECFEIDEAVARKMQMVAHMIDDDCADKAIRLQNVTGKILAIIIEYCKKHVDDVEAKNEFVTWDAEFVKNIDMDTLFKLLDAADYLIVIGLKNLIAQAIADYTADKTVNEIRELFNIENDYTPEEEEELRKKNEWAFN
Protein: Complement C1q tumor necrosis factor-related protein 2 (mCTRP2) (Q9D8U4)
Organism: Mus musculus (Mouse)
Function: Involved in the regulation of lipid metabolism in adipose tissue and liver.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
Sequence:
MTIFKKVTTMISWVLLACALPCAADPMLGAFARRDFQKGGPQLVCSLPGPQGPPGPPGAPGSSGVVGRMGFPGKDGQDGQDGDRGDSGEEGPPGRTGNRGKQGPKGKAGAIGRAGPRGPKGVSGTPGKHGTPGKKGPKGKKGEPGLPGPCSCGSSRAKSAFSVAVTKSYPRERLPIKFDKILMNEGGHYNASSGKFVCSVPGIYYFTYDITLANKHLAIGLVHNGQYRIRTFDANTGNHDVASGSTILALKEGDEVWLQIFYSEQNGLFYDPYWTDSLFTGFLIYADQGDPNEV
Protein: Anterior gradient protein 2 homolog (AG-2) (hAG-2) (HPC8) (Secreted cement gland protein XAG-2 homolog) (O95994)
Organism: Homo sapiens (Human)
Function: Required for MUC2 post-transcriptional synthesis and secretion. May play a role in the production of mucus by intestinal cells (By similarity). Proto-oncogene that may play a role in cell migration, cell differentiation and cell growth. Promotes cell adhesion.
Subcellular location: Secreted {ECO:0000269|PubMed:15834940}. Endoplasmic reticulum {ECO:0000250|UniProtKB:O88312}.
Interaction partners:
- Ly6/PLAUR domain-containing protein 3
- Dystroglycan 1
- Hepatocyte nuclear factor 3-alpha
- Trefoil factor 3
- Mucin-5AC
- Trefoil factor 1
- SAM pointed domain-containing Ets transcription factor
- Estrogen receptor
- Mucin-5B
Sequence:
MEKIPVSAFLLLVALSYTLARDTTVKPGAKKDTKDSRPKLPQTLSRGWGDQLIWTQTYEEALYKSKTSNKPLMIIHHLDECPHSQALKKVFAENKEIQKLAEQFVLLNLVYETTDKHLSPDGQYVPRIMFVDPSLTVRADITGRYSNRLYAYEPADTALLLDNMKKALKLLKTEL
Protein: Apoptosis regulator BAX (Bcl-2-like protein 4) (Bcl2-L-4) (Q07812)
Organism: Homo sapiens (Human)
Function: Plays a role in the mitochondrial apoptotic process. Under normal conditions, BAX is largely cytosolic via constant retrotranslocation from mitochondria to the cytosol mediated by BCL2L1/Bcl-xL, which avoids accumulation of toxic BAX levels at the mitochondrial outer membrane (MOM). Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.
Subcellular location: [Isoform Alpha]: Mitochondrion outer membrane {ECO:0000269|PubMed:25609812, ECO:0000269|PubMed:29531808}; Single-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000269|PubMed:27558414, ECO:0000269|PubMed:29531808}. Nucleus {ECO:0000269|PubMed:36361894}. Note=Colocalizes with 14-3-3 proteins in the cytoplasm. Under stress conditions, undergoes a conformation change that causes release from JNK-phosphorylated 14-3-3 proteins and translocation to the mitochondrion membrane. Upon Sendai virus infection, recruited to the mitochondrion through interaction with IRF3 (PubMed:25609812). {ECO:0000269|PubMed:25609812}.; SUBCELLULAR LOCATION: [Isoform Beta]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Gamma]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Delta]: Cytoplasm {ECO:0000305}.
Interaction partners:
- Apoptosis regulator Bcl-2
- Bcl-2-like protein 1
- Induced myeloid leukemia cell differentiation protein Mcl-1
- Bcl-2-like protein 11
- BH3-interacting domain death agonist
- Bcl-2 homologous antagonist/killer
- Cellular tumor antigen p53
- Cytochrome c
- Non-selective voltage-gated ion channel VDAC1
- X-ray repair cross-complementing protein 6
Sequence:
MDGSGEQPRGGGPTSSEQIMKTGALLLQGFIQDRAGRMGGEAPELALDPVPQDASTKKLSECLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALCTKVPELIRTIMGWTLDFLRERLLGWIQDQGGWDGLLSYFGTPTWQTVTIFVAGVLTASLTIWKKMG
Protein: V-set and transmembrane domain-containing protein 2-like protein (Q6PDS0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MGAPLAAALGALHYLALFLQLGGATRPAGHAPWDNHVSGHALFTETPHDMTARTGEDVEMACSFRGSGSPSYSLEIQWWYLRSHRDWTDKQTWASNQLKASQQEDSGKDATKISVVKVVGSNISHKLRLSRVKPTDEGTYECRVIDFSDGGRGVPRVLCLLIPLPAPPRAPRPRGQPPGEEPGRGPTLLFLIILPGTGSGTPREAEPHQPHAGGCPARQS