wanglab/gogpt-training-data huggingface dataset:
Protein: Probable cysteine protease RD21B (EC 3.4.22.-) (Q9FMH8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Probable thiol protease.
Interaction partners:
- UPF0235 protein At5g63440
- Developmentally-regulated G-protein 3
- Mitochondrial succinate-fumarate transporter 1
- DNA polymerase epsilon subunit B
- At1g49170
- Developmentally-regulated G-protein 2
- Developmentally-regulated G-protein 1
- Casein kinase II subunit alpha-1
- Casein kinase II subunit alpha-3
- Casein kinase II subunit alpha-2
Sequence:
MGFLKLSPMILLLAMIGVSYAMDMSIISYDENHHITTETSRSDSEVERIYEAWMVEHGKKKMNQNGLGAEKDQRFEIFKDNLRFIDEHNTKNLSYKLGLTRFADLTNEEYRSMYLGAKPTKRVLKTSDRYQARVGDALPDSVDWRKEGAVADVKDQGSCGSCWAFSTIGAVEGINKIVTGDLISLSEQELVDCDTSYNQGCNGGLMDYAFEFIIKNGGIDTEADYPYKAADGRCDQNRKNAKVVTIDSYEDVPENSEASLKKALAHQPISVAIEAGGRAFQLYSSGVFDGLCGTELDHGVVAVGYGTENGKDYWIVRNSWGNRWGESGYIKMARNIEAPTGKCGIAMEASYPIKKGQNPPNPGPSPPSPIKPPTTCDKYFSCPESNTCCCLYKYGKYCFGWGCCPLEAATCCDDNSSCCPHEYPVCDVNRGTCLMSKNSPFSVKALKRTPAIPFWAKSRKHIA
Protein: Glutamate receptor ionotropic, NMDA 2A (GluN2A) (N-methyl D-aspartate receptor subtype 2A) (NMDAR2A) (NR2A) (B7ZSK1)
Organism: Xenopus laevis (African clawed frog)
Function: Component of NMDA receptor complexes that function as heterotetrameric, ligand-gated ion channels with high calcium permeability and voltage-dependent sensitivity to magnesium. Channel activation requires binding of the neurotransmitter glutamate to the epsilon subunit, glycine binding to the zeta subunit, plus membrane depolarization to eliminate channel inhibition by Mg(2+). Sensitivity to glutamate and channel kinetics depend on the subunit composition (Probable). Plays a role in dendritic branching in brain neurons and in synaptic plasticity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:28232581}; Multi-pass membrane protein {ECO:0000269|PubMed:28232581}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q00959}; Multi-pass membrane protein {ECO:0000269|PubMed:28232581}.
Interaction partners:
Sequence:
MGMFVLLLYTFLYAGDLGHGAEKSFPVLNIAVILGRTRYITERDIRSLWTRDMSLDFDVNVVTLLVNQTDPKSIITHVCDLMSGTKIHGVVFGDDTDQEAIAQILDFVSSQTFIPILGIHGGSSMIMADKDEMSTFFQFGASIKQQATVMLNIMEEYDWHVFSVITSNFPGYRDFISFIKTTVDNSFVGWEVQNYITLDTSYTDAQTLTQLKKIHSSVILLYCSKDEATYIFEEARSLGLMGYGFVWIVPSLVTGNTDIIPYEFPSGLVSVSYDDWDYGIEARVRDGLGIITTAASAMLEKHSVIPEAKTSCYGQNERNDPPLHTLHNFMINVTWDGKDLSFTEDGYQANPKLVVLLLNMEREWEKVGKWENKSLNMKYPVWPRITASLDSDHDDNHLSIVTLEEAPFVIVENIDYLTGTCVRNTVPCRKYFRLNNSTTEGTSVKKCCKGFCIDILKKLSKTVKFTYDLYLVTNGKHGKKIKNVWNGMIGEVVYKRAVMAVGSLTINEERSVAVDFSVPFVETGISVMVSRSNGTVSPSAFLEPFSASVWVMMFVMLLLVSAMAVFIFEYFSPVGYNRNLAQGKDPHGPSFTIGKAVWLLWGLVFNNSVPVQNPKGTTSKIIVSIWAFFAVIFLASYTANLAAFMIQEEFVDQVTGLSDNKFQRPHDYSPPFRFGTVPNGSTERNIRNNYPDMHQYMVKFHQKGVQDALVSLKTGKLDAFIYDAAVLNYMAGRDEGCKLVTIGSGYIFATTGYGIALQKGSRWKRPIDLALLQFVGDGEMEELEKLWLTGICHTEKNEVMSSQLDIDNMAGVFYMLAAAMALSLITFVWEHLFYWKLRFCFTGVCTGTPGLLFSISRGIYSCIHGVHIEEKKKSPDFSFTASQTNMLKLLRASKNIANLSNLNQSQCNSPKRTSDYIQRNSLLTDMVLDKGNLTYSDNRPFQQKDIYSENTYDLAMLSANCPKDNLNNYVFQGQHPLTLNESNPNTVEVAVSAEAKVNTRPRQLWKKSVETLRQTQGSVNENGTEESKSSIKNQRFLPEDGHFSDVSEASSRATCHIDSENNNKHRKSKDNLKKRPVSAKYARECSEVELSYLKIKHGPNRDKVYTIDGDKEPSFIMDQPKYSENSPDQDDEDYPDVYQDHNDNYRKTEPLQSDRTPLHSEGRLPNNDIQYKLFSKHYNLKEKNTSMSDANDRHRQNSTHCRSCLSNMPNYTGHYTARSPYKCDDCLHTGKLYDIDEDQMLHEAANSMHSEDFYEHNWLENNALHFQKKNKLRINRQHSCDNINKPREHDLGRPPRSLSLKEKERYIQENPFAKFVIVPPEKLLGNNASLFTDSLKDSKRSKSLYPDNSSDNPFLHSYQETQKLSHGRSSSDIYKQSSLPKARNDNYLRSSIKSTTSYSSRDGRVPDDMCVSEYALPYVTSNNSVYSAPRVVNSCSNRRVFKKMPSLESDV
Protein: Putative 2-dehydropantoate 2-reductase (EC 1.1.1.169) (Ketopantoate reductase) (KPA reductase) (F4KIN4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid.
Interaction partners:
- 2-oxoisovalerate dehydrogenase subunit beta 1, mitochondrial
- 2-oxoisovalerate dehydrogenase subunit beta 2, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Dihydrolipoyl dehydrogenase 2, chloroplastic
- Dihydrolipoyl dehydrogenase 1, chloroplastic
- Dihydrolipoyl dehydrogenase 1, mitochondrial
- Dihydrolipoyl dehydrogenase 2, mitochondrial
- Pyruvate dehydrogenase E1 component subunit beta-2, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-3, chloroplastic
- Pyruvate dehydrogenase E1 component subunit beta-1, mitochondrial
Sequence:
MESRCKKGYFRLAVIGLSKAKDCWEKNACAVTFIGDGGTSEGDFHAGLNFAAVMEAPVVFICRNNGWAISTHISEQFRSDGIVVKGQAYGIRSIRVDGNDALAVYSAVCSAREMAVTEQRPVLIEMMIYRVGHHSTSDDSTKYRAADEIQYWKMSRNSVNRFRKSVEDNGWWSEEDESKLRSNARKQLLQAIQAAEKWEKQPLTELFNDVYDVKPKNLEEEELGLKELIEKQPQDYMMLKELIPNWILGIGTLALRYDFQETLFNGWHAIAELQQLKLKIKLNSLLNDQADTESLKAARNSALNVIQAMIIHLVLTLKGRFSLPLTEETVRFNEPIQLNQNMVKDGGYTAELFPIRKEEQGEVRR
Protein: Peroxisomal membrane protein 11B (Peroxin-11B) (Peroxisomal biogenesis factor 11B) (Protein PEX11 homolog beta) (PEX11-beta) (Q9Z210)
Organism: Mus musculus (Mouse)
Function: Involved in peroxisomal proliferation. May regulate peroxisome division by recruiting the dynamin-related GTPase DNM1L to the peroxisomal membrane. Promotes membrane protrusion and elongation on the peroxisomal surface.
Subcellular location: Peroxisome membrane {ECO:0000250|UniProtKB:O96011}; Single-pass membrane protein {ECO:0000250|UniProtKB:O96011}.
Interaction partners:
- Peroxisomal membrane protein 11C
- Peroxisomal biogenesis factor 19
- Peroxisomal membrane protein PEX13
- Peroxisome assembly protein 12
- Peroxisomal membrane protein PEX14
- Peroxisomal membrane protein PEX16
- Peroxisomal membrane protein 11A
- ATP-binding cassette sub-family D member 3
- Peroxisome biogenesis factor 10
- Peroxisomal membrane protein 4
Sequence:
MDAWVRFSAQSQARERLCRAAQYACSLLGHALQRHGASPELQKQIRQLEGHLSLGRKLLRLGNSTDALESAKRAVHLSDVVLRFCITVSHLNRALYFACDNVLWAGKSGLAPRVDQEKWAQRSFRYYLFSLIMNLSRDAYEIRLLMEQETSAYSRRMKVSGVGVSGGVETVGPGGPGTPGGSLPQLALKFRLRILLLARVLRGHPPLLLDVLRNACDLFIPLDKLGLWRCGPGIVGLCGLISSILSILTLICPWLRLKP
Protein: POU domain, class 3, transcription factor 2 (Brain-specific homeobox/POU domain protein 2) (Brain-2) (Brn-2) (Nervous system-specific octamer-binding transcription factor N-Oct-3) (Octamer-binding protein 7) (Oct-7) (Octamer-binding transcription factor 7) (OTF-7) (P20265)
Organism: Homo sapiens (Human)
Function: Transcription factor that plays a key role in neuronal differentiation (By similarity). Binds preferentially to the recognition sequence which consists of two distinct half-sites, ('GCAT') and ('TAAT'), separated by a non-conserved spacer region of 0, 2, or 3 nucleotides (By similarity). Acts as a transcriptional activator when binding cooperatively with SOX4, SOX11, or SOX12 to gene promoters (By similarity). 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 (By similarity). Acts downstream of ASCL1, accessing chromatin that has been opened by ASCL1, and promotes transcription of neuronal genes (By similarity).
Subcellular location: Nucleus.
Interaction partners:
- Achaete-scute homolog 1
- Myelin transcription factor 1-like protein
- Transcription factor SOX-10
- Transcription factor SOX-2
- POU domain, class 3, transcription factor 1
- Sal-like protein 2
- Polyglutamine-binding protein 1
- Homeobox protein orthopedia
- E3 SUMO-protein ligase EGR2
- Neurogenin-2
Sequence:
MATAASNHYSLLTSSASIVHAEPPGGMQQGAGGYREAQSLVQGDYGALQSNGHPLSHAHQWITALSHGGGGGGGGGGGGGGGGGGGGGDGSPWSTSPLGQPDIKPSVVVQQGGRGDELHGPGALQQQHQQQQQQQQQQQQQQQQQQQQQRPPHLVHHAANHHPGPGAWRSAAAAAHLPPSMGASNGGLLYSQPSFTVNGMLGAGGQPAGLHHHGLRDAHDEPHHADHHPHPHSHPHQQPPPPPPPQGPPGHPGAHHDPHSDEDTPTSDDLEQFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLNKWLEEADSSSGSPTSIDKIAAQGRKRKKRTSIEVSVKGALESHFLKCPKPSAQEITSLADSLQLEKEVVRVWFCNRRQKEKRMTPPGGTLPGAEDVYGGSRDTPPHHGVQTPVQ
Protein: DRBM domain-containing protein (Q387M7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MWRLLFLRPRLLLFHAQTRNVVVSSPPVSSVPDASPAAAEAVVCACPCSHATNSGGLKLSLAAVMSDIKSLRKKWTRDFRLCISSEPAVVIESSAVGETAWAPLVVLDATSMSDGLVKAVDASLVSHTEKQSSATVLDLRERGEDISTAKRMLEEQFPSLRLNIDHSKGTDLQGVATHTVTVSLNARDSVDKLSSEEKAVKNAFFGESIGVSYSSTARRAIFEGFKSAGLPQPPRYAERNHNISELSVYMDIIRNATCEEVNIVPTNIGDGQVRVSVQTLSGRQISALTGKHENALPIALSCVEKAADIVSAVATEGARKRIADHPVILALPPKGIRPKEILRRLLHHSFGIEEDRVLFVTLRSTGGTFVTNVDVELGWCKPSPAGAATDELETKATPPAVVVTVAKAAGVNKKAAEALASMSAIRECFPRVFEEQLAFHPEVREIMSTTKATVNDSICPHVSKGIVEQLRWAARRQKKEIVLEGVQLLPNSENESLGIRTTRPLWATQLFMVDEEGCREFICLALDQKKSASEQKAIAIALFKHFKEECQDGVQYAMDHGLIDKNGDVPGCEGIYSSATPLPKSAFEMAAESDPFIQKLQLLPSQPILVPPRQSMLSVFRRGIQLYVDMLGEKCASDRGSGSLSLVENVEQVADNGHFRAQLYTKWIGDDTSKLRETPHEMSPLGEAAYSATAVSALFTAMKSLFEEGGPIVCASSDDAQINEICLETWRRVAALPSLPPQLPTPTPLETIAECVMTKYGLSTELRISGVGKAINVQLYGRCPTSLSNSNIKEAPQFFLGHGRGSSLLKAAVSCCQRVFVEHMQSDSHPLGVMGAEPQISGSVGVRAHGSGSLLASRIEDVKKELVDNKTVAADASVLVKVDVCFSQSERKYEASLYVVDGARTVELERISPDADLMMSLLRLTESINKEMGLPSIDKNTIMKKCDDSRQLIALKNLVGFVYGFPVIVETSMKDSLWYCHISVLLSDNIHYGIGYAVSKRKKDAVEEAAAGAIHRCFGTVTNPLKKGESHAEVSSSNPYCGFVYEGKGNE
Protein: Mitochondrial import receptor subunit TOM7 homolog (Translocase of outer membrane 7 kDa subunit homolog) (Q9P0U1)
Organism: Homo sapiens (Human)
Function: Required for assembly and stability of the TOM complex. Positive regulator of PRKN translocation to damaged mitochondria. Acts probably by stabilizing PINK1 on the outer membrane of depolarized mitochondria.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:12198123}; Single-pass membrane protein {ECO:0000269|PubMed:12198123}.
Interaction partners:
- Mitochondrial import receptor subunit TOM20 homolog
- Mitochondrial import receptor subunit TOM6 homolog
- Mitochondrial import receptor subunit TOM40 homolog
- Mitochondrial import receptor subunit TOM22 homolog
- Mitochondrial import receptor subunit TOM70
- Mitochondrial import receptor subunit TOM5 homolog
- Mitochondrial import receptor subunit TOM40B
- Serine/threonine-protein kinase PINK1, mitochondrial
- Sorting and assembly machinery component 50 homolog
- Metaxin-3
Sequence:
MVKLSKEAKQRLQQLFKGSQFAIRWGFIPLVIYLGFKRGADPGMPEPTVLSLLWG
Protein: T-box transcription factor TBX21 (T-box protein 21) (T-cell-specific T-box transcription factor T-bet) (Transcription factor TBLYM) (Q9JKD8)
Organism: Mus musculus (Mouse)
Function: Lineage-defining transcription factor which initiates Th1 lineage development from naive Th precursor cells both by activating Th1 genetic programs and by repressing the opposing Th2 and Th17 genetic programs. Activates transcription of a set of genes important for Th1 cell function, including those encoding IFN-gamma and the chemokine receptor CXCR3. Activates IFNG and CXCR3 genes in part by recruiting chromatin remodeling complexes including KDM6B, a SMARCA4-containing SWI/SNF-complex, and an H3K4me2-methyltransferase complex to their promoters and all of these complexes serve to establish a more permissive chromatin state conducive with transcriptional activation. Can activate Th1 genes also via recruitment of Mediator complex and P-TEFb (composed of CDK9 and CCNT1/cyclin-T1) in the form of the super elongation complex (SEC) to super-enhancers and associated genes in activated Th1 cells. Inhibits the Th17 cell lineage commitment by blocking RUNX1-mediated transactivation of Th17 cell-specific transcriptinal regulator RORC. Inhibits the Th2 cell lineage commitment by suppressing the production of Th2 cytokines, such as IL-4, IL-5, and IL- 13, via repression of transcriptional regulators GATA3 and NFATC2. Protects Th1 cells from amplifying aberrant type-I IFN response in an IFN-gamma abundant microenvironment by acting as a repressor of type-I IFN transcription factors and type-I IFN- stimulated genes. Acts as a regulator of antiviral B-cell responses; controls chronic viral infection by promoting the antiviral antibody IgG2a isotype switching and via regulation of a broad antiviral gene expression program.
Subcellular location: Nucleus {ECO:0000269|PubMed:10761931, ECO:0000269|PubMed:15662016, ECO:0000269|PubMed:21690296, ECO:0000269|PubMed:23616576}.
Interaction partners:
- Trans-acting T-cell-specific transcription factor GATA-3
- Runt-related transcription factor 3
- Runt-related transcription factor 1
- Interferon gamma
- B-cell lymphoma 6 protein homolog
- Lysine-specific demethylase 6B demethylase 6B)
- Granzyme B
- T-cell surface glycoprotein CD4
- Forkhead box protein P3
- Protein C-ets-1
Sequence:
MGIVEPGCGDMLTGTEPMPSDEGRGPGADQQHRFFYPEPGAQDPTDRRAGSSLGTPYSGGALVPAAPGRFLGSFAYPPRAQVAGFPGPGEFFPPPAGAEGYPPVDGYPAPDPRAGLYPGPREDYALPAGLEVSGKLRVALSNHLLWSKFNQHQTEMIITKQGRRMFPFLSFTVAGLEPTSHYRMFVDVVLVDQHHWRYQSGKWVQCGKAEGSMPGNRLYVHPDSPNTGAHWMRQEVSFGKLKLTNNKGASNNVTQMIVLQSLHKYQPRLHIVEVNDGEPEAACSASNTHVFTFQETQFIAVTAYQNAEITQLKIDNNPFAKGFRENFESMYASVDTSVPSPPGPNCQLLGGDPFSPLLSNQYPVPSRFYPDLPGQPKDMISQPYWLGTPREHSYEAEFRAVSMKPTLLPSAPGPTVPYYRGQDVLAPGAGWPVAPQYPPKMSPAGWFRPMRTLPMDPGLGSSEEQGSSPSLWPEVTSLQPEPSDSGLGEGDTKRRRISPYPSSGDSSSPAGAPSPFDKETEGQFYNYFPN
Protein: Beta-1,4 N-acetylgalactosaminyltransferase 1 (EC 2.4.1.92) ((N-acetylneuraminyl)-galactosylglucosylceramide) (GM2/GD2 synthase) (GalNAc-T) (Q00973)
Organism: Homo sapiens (Human)
Function: Involved in the biosynthesis of gangliosides GM2, GD2, GT2 and GA2 from GM3, GD3, GT3 and GA3, respectively.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q10468}; Single-pass type II membrane protein {ECO:0000255}.
Interaction partners:
- Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase
- Beta-1,3-galactosyltransferase 4
- Lactosylceramide alpha-2,3-sialyltransferase
- Acetyl-coenzyme A transporter 1
- Beta-hexosaminidase subunit alpha
- Beta-hexosaminidase subunit beta
- Beta-galactosidase
- Beta-1,4-galactosyltransferase 6
- Chondroitin sulfate synthase 2
- Electron transfer flavoprotein subunit alpha, mitochondrial
Sequence:
MWLGRRALCALVLLLACASLGLLYASTRDAPGLRLPLAPWAPPQSPRRPELPDLAPEPRYAHIPVRIKEQVVGLLAWNNCSCESSGGGLPLPFQKQVRAIDLTKAFDPAELRAASATREQEFQAFLSRSQSPADQLLIAPANSPLQYPLQGVEVQPLRSILVPGLSLQAASGQEVYQVNLTASLGTWDVAGEVTGVTLTGEGQADLTLVSPGLDQLNRQLQLVTYSSRSYQTNTADTVRFSTEGHEAAFTIRIRHPPNPRLYPPGSLPQGAQYNISALVTIATKTFLRYDRLRALITSIRRFYPTVTVVIADDSDKPERVSGPYVEHYLMPFGKGWFAGRNLAVSQVTTKYVLWVDDDFVFTARTRLERLVDVLERTPLDLVGGAVREISGFATTYRQLLSVEPGAPGLGNCLRQRRGFHHELVGFPGCVVTDGVVNFFLARTDKVREVGFDPRLSRVAHLEFFLDGLGSLRVGSCSDVVVDHASKLKLPWTSRDAGAETYARYRYPGSLDESQMAKHRLLFFKHRLQCMTSQ
Protein: Uncharacterized protein, isoform F (Uncharacterized protein, isoform G) (M9PEZ9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MIMRRASACTMPSSGGGGGAGVGSSQREEATTPGESPGGRLSRWFSIRRGSSHQYDVGGRDGRHSTASSFDTPDSGSGNSPKNGSNAVAGTGGAGSQGVALDAASPQKLANLGASKMMPGVPESEDDEATANRFDVDLMMTPGSRANGTARTAHNRLIVPMLPPAPAGLSQQQLKRRHIVAAIVHSENSYVATLQRLVNDYKKPLEECSPPVLNPVKIATLFHCLPDILHSHKLFRISLAECVRNWDRDEKIGDCFVSAFGKPQLLEIYSGFINNFSAAMELAKMEEKRKSALADFFKVKQISAHDRLSFFGLMVKPVQRFPQFILFLQDLLKYTPQGHHDRMSLQLALSQLELLAELLNESKREAEQYQAFKEMLGHISGTFNARSLSLSSVSVSDSAGGHRPRYLLREDNVTHMEFNQAGFIVKCKQRRLLLLNDKVICVSVAPKQSHDFGATEKLTFKWMFPVNDVEIVDNSTSATLSRILTAGLNRGGSLKSNGSSGANGSPYANSTLPGHGGGVSGFSGFGDPHSSPAAQLTNGADNLCSEMSTLMYDYEVISRIQDLVSSLKGSYKELNANTTRNVLNLIQGSIQRKDEEMAWVDSCCLQLIGRHKSGKEETFTFQTQTPAVKKEWITELRLAQLALDPNNSPAWERGGSHPQPAHHHPHHHPLQHPHAGAGDPRQTQEQLQLQEAVQQKQSRKMPLFVKAMPVYKSQHQTEVRCGCYYSIANDTKQSGNARRRHKQLNYLWMCSSDGTSSHITVLAQHPQQAGNLREAGAFDLFETQVSALEFVKGLDQLKSRDEPASLLGDLVWLGTDSRKILIYSARNPEQEEQLGSYSVPGAVQRILYHFDAVYVALSGATVLIFRRGNDGVWQLRDPQTIRLGDTDLVVPSLLPINMCIYASCGNRVYVMNALNGEIQRSFEVQHGATQQVNLMAHSGIGLWISLKNSTMLCLYHTETFKHLQDINIASSVLRHDGKKEQPLNNSSVYVTALMACKGLLWVGTNVGIAVTIPLPRLEGVPIISGGINMSCHAHFGPITFLLPLIPKVYPAYKPPTVGAAPLVPSMGDDLQLPAIDADPKIQELDDGAVVLRRDLAKEEMSSSNPGADSTASSPRSSKLDKQNSLDQSFTAKIRASLANSPAFHRKRFRDDPNRMSKTLPRGLGAAAAGSGAGGASAAGSGTASGNTSQHGEHGICDVYGLYGKLIFVKEDYDAEEGNQGNLMDMMYEGMRRSDPELAAIPGKVCTLDRRLRMKASRPRSLDLSNWSVDSKSSSLYTSSGSEESMGIRHFGGRSVSRNSSSASHKTSGTGSDLGNISENGLMTTADIHHHQQQQQQLNSSAKPDEMSRLGAGNSGLDKPAAAVATLKRKQKQNSKQQQQQNADGPRTVITLMGGRGYWRQMWYNGAGGSPSHKNSSSGGGGGSGSGFSGQTMQSGNPSCSPLTANSNDAHIVVWEKKLXSQELVCCCTLQQHPHQHHPPLTELWRRVGEQHQQHQQLQQAQRRGRGRVRFRGSFIQRDRSAGSDGGSGYGSGGLSGAGGSGGMLGASLKRLTKLKRGGSLKEF
Protein: Inositol 1,4,5-trisphosphate receptor (Q91908)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cytoplasmic vesicle, secretory vesicle membrane {ECO:0000256|ARBA:ARBA00004638}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004638}. Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368044}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU368044}.
Interaction partners:
Sequence:
MSDKMSSFLHVGDIVSLYAEGSVNGFINTLGLVDDRSVVQPDAGDLNNPPKKFRDCLFRLCPMNRYSAQKQFWKAAKPGASSTTDTVLLNKLHHAADLEKKQNETENRKLLGTVIQYGNVIQLLHLKSNKYLTVNKRLPALLEKNAMRVTLDEAGNEGSWFYIQPFYKLRSIGDSVVIGDKVVLNPVNAGQPLHASSQQLSDNPGCNEVNSVNCNTSWKIVLFMKWSDNKDDILKGGDVVRLFHAEQEKFLTCDEHRKKQHVFLRTTGRQSATSATSSKALWEVEVVQHDPCRGGAGYWNSLFRFKHLATGHYLAAEIDAEPDAGNARMQVVPEKMMCTLISVPEGNDISSIFELDPTTLRGGDSLVPRNSYVRLRHLCTNTWVHSTNSPIDKDEEKPVMLRIGTSPVKEDKEAFAIVPVSPAEVRDLDFANDASKVLSSIAGKLEKGTITQNERRAVTKLLEELVYFVTGLVNSGHDILEVLVNKPNRERQKLMREQNILKQIFKLLQAPFTDSGDGPMLRLEELGDQRHAPFRHICRLCYRVLRHSQQDYRKNQEYIAKQFGFMQKQIGYDVLAEDTITALLHNNRKLLEKHITAAEIDTFVSLVRKNREPRFLDYLSDLCVSMNKSIPVTQELICKAVLNPANADILIETKLVLSRFEFEGVASGESSLEAGEDEEEVWLFWKASNKEIRSRSVRELAQDAKEGQKEDQDVLNYYRYQLNLFARMCLDRQYLAINEISGQLDVDLILRCMSDENLPFDLRASFCRLMLHMHVDRDPQEQVTPVKYARLWSEIPSEIAIDDYDSSGTSRDDIKERFAQTMEFVEEYLRDVVGQRFPFADKEKNKLTFEVVNLARNLIYFGFYNFSDLLRLTKILLAIVDCVHLIANFPSGKLGKGEESKGGSNVMRSIHGVGELMTQVVLRGGGFLPMTPMAAPEGTIKAQREPEKEDILVMDTKLKIIEILQFILNVRLDYRISCLLCIFKSEFDESNAQSVEGSTEAITVVPGTLDFEHIEEQAEGIFGGSEENTPLDLDDDGGRTFLRVLLHLTMHDYPPLVSGALHLLFRHFSQRQEVLQAFKQVQLLVTSQDVDNYKQIKQDLDQLRSIVEKSELWVYKGSGPEEVTAAQAGGADKGETPGKAKKSESTSSYNYRVVKEILLRLSKLCVQENTTGRRNRKQQQRLLRNMGAHSVVLELLQIPYEKTEDTRMQEIMKIAHEFLQNFCAGNQQNQALLHKHINLFLTPGILEAVTMQHIFMNNFQLCSEINERVVQHFAHCIETHGRNVQYIKFLQTIVKAEGRYIKKCQDIVMAELVNSGEDVLVFYNDRASFQTLVQMMRSERERMDENSPLMYHIHLVELLAVCTEGKNVYTEIKCNSLLPLDDIVRVVTHEDCVPEVKIAYINFLNHCYVDTEVEMKEIYTSNHMWKLFENFLVDICRVCNSTSDRKHADIVLERYVTEIVMSIVNTFFSSPFSDQSTTLQASKLAVVHQTRQPVFVQLLQAIFRVYHCNWLLPSQKASVESCIRVLSDVAKSRTIAIPVDLDSQVNNLFLKSHNIVQKTAMSWRMSVRNAARRDSVLTASRDYRNIIERLQDIVSSLEDRLRPLVQAELSVLVDVLHRPELLFPENTDARKKCESGQFICKLIRHTKLLLEENEEKLCIKVLQTLREMMAKDRGFGDKGEALRVILVNRYYGNIRPAGRRESLTSFGNGPLSGGSSGKSGGGSIGSGSLSRSEMSLSDVQCHLDKQGASDLVIDLIMNATSDRVFHESILLAIALLEGGNTTIQHSFFCRLTEDKKSEKFFKVFFDRMKVAQQEIKATVTVNTSDLGSKKRDEEQSERETPHHQRVREPSGQITEEAKEQLIEASVATKKAYYSFRREADPDDHFSLGEGVMAVAEKGRDELEMSAVITIMQPILRFLQLLCENHNRDLQNFLRCQNNKSNYNLVCETLQFLDCICGSTTGGLGLLGLYINEKNVALINQTLESLTEYCQGPCHENQNCIATHESNGIDIITALILNDINPLGRKRMDLVLELKNNASKLLLAIMESRHDSENAERILYNMRPKELVEVIKKAYLQGEVEFEDGESGEDYAASPRNVGHNIYILAHQLARHNKELQHMLKPGVQTGEGDEALEFYAKHTAQIEIVRLDRTMEQIVFPVPSICEFLTKESKLRIYYTTERDEQGSKIHDFFQRSEDLFNEMNWQKKLRAQQVLYWCSRNMTFWSSISFNLAVLMNLLVAFFYPFVNVHGGTLDSRLSGLLWTAMLVSLAIVIVLPKPHGIRALIASTILRLIFSIGLQPTLFLLGAFNVCNKIIFLTSFVGNRGTFTRGYGAMVLDVEFLYHLLYLLICAMGVFVHEFFYSLLLFDLVYREETLLNVIKSVTRNGRSIILTAVLALILVYLFSIVGYLFFKDDFILEVDRLQNETIFPENGGTMTSELLYPEVCRVGSDTNCTHEELAQVTEEEEEEKEHTCETLLMCIVTVLSHGLRSGGGVGDVLRKPSKEEPLFAARVIYDLLFFFMVIIIVLNLIFGVIIDTFADLRSEKQKKEEVLKTTCFICGLERDKFDNKTATFEEHFKEEHNMWHYLFFIVLVKVKDSTEYTGPESYVAEMIKDRNLDWFPRMRAMSLVSSDSEGEQNELRNLQEKLESTMRLVTNLSGQLSELKDQMTEQRKQKQRIGLLGQPAHLNINPQQPA
Protein: Monothiol glutaredoxin-5, mitochondrial (Q02784)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Monothiol glutaredoxin involved in mitochondrial iron-sulfur (Fe/S) cluster transfer. Receives 2Fe/2S clusters from scaffold protein ISU1 and mediates their transfer to apoproteins, to the 4Fe/FS cluster biosynthesis machinery, or export from mitochondrion.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:11950925}.
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate-binding protein SLM1
- Iron-sulfur assembly protein 2
- Iron-sulfur cluster biogenesis chaperone, mitochondrial
- Fe-S cluster assembly protein DRE2
- BolA-like protein 1
- BolA-like protein 3
- Frataxin homolog, mitochondrial
- Iron-sulfur assembly protein 1
- Cysteine desulfurase, mitochondrial
- BolA-like protein 2
Sequence:
MFLPKFNPIRSFSPILRAKTLLRYQNRMYLSTEIRKAIEDAIESAPVVLFMKGTPEFPKCGFSRATIGLLGNQGVDPAKFAAYNVLEDPELREGIKEFSEWPTIPQLYVNKEFIGGCDVITSMARSGELADLLEEAQALVPEEEEETKDR
Protein: Protein LAZY 1 (AtLA1) (AtLAZY1) (Protein LAZY1-LIKE 1) (Q5XV40)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the regulation of shoot gravitropism. Involved in the regulation of inflorescence branch angle. Functions redundantly with LAZY2, LAZY3 and LAZY4 to control plant architecture by coupling gravity sensing to the formation of auxin gradients. Involved redundantly with LAZY2 and LAZY4 in the regulation of both shoot and root gravitropism. Mediates gravity signaling in statocytes downstream of amyloplast displacement, leading to the generation of asymmetric auxin distribution in gravity-responding organs. Regulates the direction of polar auxin transport in response to gravity through the control of asymmetric PIN3 expression in the root cap columella. Regulation of auxin flow by the three proteins LAZY1, LAZY2 and LAZY4 in statocytes influences plant architecture by controlling the growth angle of lateral shoots and lateral roots.
Subcellular location: Cell membrane {ECO:0000269|PubMed:23331961}; Single-pass membrane protein {ECO:0000255}. Nucleus {ECO:0000269|PubMed:23331961}.
Interaction partners:
- Protein TILLER ANGLE CONTROL 1
- Protein LAZY 2
- Uncharacterized protein
- Light-regulated protein 1, chloroplastic
- Zinc finger protein SHOOT GRAVITROPISM 5
- Auxin efflux carrier component 3
- Uncharacterized protein
- Auxin canalization protein
- Squamosa promoter-binding-like protein 14
- Cytochrome c-1
Sequence:
MKFWGWMHHKFRENSKEPLKDASTGNSYSILSAHPSLDSQEVYPTACAGSRYNTGFRKQVNLFQESSFAGPKQYTEEDFKDERNSDFFDGFLAIGTLGGETLLDEQPATPTFGMSFEDPAIDDADVTENDLKLISNELDKFLEAEAKEGHHQPSGRNSDTNTIASTIEAIEGVDDEEDNQPMKFPLQEYFFGSLIELPESKIAGKKDRASLGELFQITEVQDKQSENIYGKKKKQPNSAHKSAKHLVKKVLKKIHPSSRGSVSGKPEVDSTKKKFQKMVQVFHRKVHPEESIMETKIYSSVANPKSSKANSIDLTFEKVNHCHEASKRCIQYELRSSRSAKNGEHWIKTDEDYFVLEL
Protein: Chromobox protein homolog 8 (Polycomb 3 homolog) (Pc3) (hPc3) (Rectachrome 1) (Q9HC52)
Organism: Homo sapiens (Human)
Function: Component of a Polycomb group (PcG) multiprotein PRC1-like complex, a complex class required to maintain the transcriptionally repressive state of many genes, including Hox genes, throughout development. PcG PRC1 complex acts via chromatin remodeling and modification of histones; it mediates monoubiquitination of histone H2A 'Lys-119', rendering chromatin heritably changed in its expressibility.
Subcellular location: Nucleus {ECO:0000269|PubMed:21282530}.
Interaction partners:
- Polyhomeotic-like protein 2
- E3 SUMO-protein ligase CBX4
- Polycomb complex protein BMI-1
- E3 ubiquitin-protein ligase RING1
- Polyhomeotic-like protein 3
- Chromobox protein homolog 2
- E3 ubiquitin-protein ligase RING2
- Polycomb group RING finger protein 2
- Polyhomeotic-like protein 1
- Chromobox protein homolog 7
Sequence:
MELSAVGERVFAAEALLKRRIRKGRMEYLVKWKGWSQKYSTWEPEENILDARLLAAFEEREREMELYGPKKRGPKPKTFLLKAQAKAKAKTYEFRSDSARGIRIPYPGRSPQDLASTSRAREGLRNMGLSPPASSTSTSSTCRAEAPRDRDRDRDRDRERDRERERERERERERERERERGTSRVDDKPSSPGDSSKKRGPKPRKELPDPSQRPLGEPSAGLGEYLKGRKLDDTPSGAGKFPAGHSVIQLARRQDSDLVQCGVTSPSSAEATGKLAVDTFPARVIKHRAAFLEAKGQGALDPNGTRVRHGSGPPSSGGGLYRDMGAQGGRPSLIARIPVARILGDPEEESWSPSLTNLEKVVVTDVTSNFLTVTIKESNTDQGFFKEKR