wanglab/gogpt-training-data huggingface dataset:
Protein: Photosystem II reaction center protein M (PSII-M) (P72701)
Organism: Synechocystis sp. (strain ATCC 27184 / PCC 6803 / Kazusa)
Function: One of the components of the core complex of photosystem II (PSII). PSII is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that converts photonic excitation into a charge separation. This subunit is found at the monomer-monomer interface (By similarity). Involved in assembly of monomeric PSII from the CP43-less intermediate.
Subcellular location: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_00438, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00438, ECO:0000269|PubMed:34937700}.
Interaction partners:
- Photosystem II reaction center protein I
- Photosystem II reaction center protein L
- Photosystem II reaction center protein Y
- Photosystem II reaction center protein J
- Photosystem II reaction center protein X
- Photosystem II CP47 reaction center protein
- Photosystem II reaction center protein T
- Photosystem II extrinsic protein V
- Photosystem II extrinsic protein O
- Photosystem II reaction center protein K
Sequence:
MQVNNLGFIASILFVLVPTVFLLILFIQTGKQSES
Protein: Small ribosomal subunit protein eS8 (40S ribosomal protein S8) (P62247)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P62241}. Membrane {ECO:0000250|UniProtKB:P62241}; Lipid-anchor {ECO:0000250|UniProtKB:P62241}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P62241}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. {ECO:0000250|UniProtKB:P62241}.
Interaction partners:
- Small ribosomal subunit protein uS11
- Small ribosomal subunit protein eS25
- Small ribosomal subunit protein uS13
- Small ribosomal subunit protein uS5
- FAU ubiquitin-like and ribosomal protein S30 fusion b
- Small ribosomal subunit protein eS1
- Small ribosomal subunit protein uS12
- Ribosomal protein S10
- Small ribosomal subunit protein eS19
- Small ribosomal subunit protein uS2
Sequence:
MGISRDNWHKRRRTGGKRKPVHKKRKYELGRPAANTKIGPRRIHTIRVRGGNKKYRALRLDVGNFSWGSECCTRKTRIIDVVYNASNNELVRTKTLVKNCVVLVDSTPYRQWYESHYALPLGRKKGAKLTPEEEEILNKKRSKKVQKKFTLRRKTAKISPLLEEQFLQGKLLACISSRPGQCGRADGYVLEGKELEFYLRKIKAKKGK
Protein: RNA helicase (EC 3.6.4.13) (Q8I457)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKSLFFNKLKNVGKKIKINFIQILIIFLVYVNLDFFKSNINVKAIHTKKNLFIPVSNEIFYFKKNVLIKKRNKEKRYTHSKNKGSNIFLNLNEENDNTVKERKKKIKYPEIGEYNDDVNHNKNNDNNGDDSESHLNDQGKCKFSDLSEINKNIVEFLENKKGIKYMTKIQSQSFKPIYEGKDIIGRSETGSGKTLAFALPLVEKLYKMKTSNEKFEEENGSHEEDQKKNIYDDVDNDNNYDNFSYGKKYQNREHNKDPSILVLEPTRELSKQVENTFKEISQFYNFNIMSIYGGESYTYQENKLRKGIDILTGTPGRIIDHIEKKNLSLQNIKYVVLDEADEMLNLGFTHDIERILSNINLKEAQVLLYSATTPSWIKDISSKYLKNPFCIDVVDSSNKTAKNIKHIAIKTPYDIKEKALLLEDIILVKSNGGQVIIFTRTKLEADILCSEGSFKSLSFAVLHGNIAQSTREYTMQRFRQGMFQILIATDIASRGLDISNVDLVIQCFPPNYSAVYIHRAGRTGRANKKGTSLVLYSNEDKQDLIKIEKNCGIKFNMETLPNNEQVFHCASAIASKKVENVNKEILPFFHDTAKELINKSNSLKIDQIELISRCLAIIAKKEHIKKRSLINGLSETVTLNFINKNRKWSSEADIVYWVNKLSNELNVNTFNKILQIKIDNKDRASSFFDINENLAELFLQNFKTMSKIEYRKMFDLSVAQTIPEHVDLTIDYQPHTSRYQYRKKNYSYRRRPSYY
Protein: PHD-finger and DNA binding domain-containing protein (F4K0Y2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- WD-40 repeat-containing protein MSI3
- PHD finger family protein
- DDT domain-containing protein PTM
- Homeobox-DDT domain protein RLT2
- Homeobox-DDT domain protein RLT1
- DDT domain-containing protein
- Uncharacterized protein At5g25580
- Zinc-finger domain of monoamine-oxidase A repressor R1 protein
- AT5g38690/MBB18_24
- DDT domain-containing protein DDR4
Sequence:
MELVGKVVRKEIQGIGFCSGTVRSRDSSGFFEIVYENGVTEISELDEVVALVMGDGKSQENSVPVKKKRVGRKPKKRSRVARVVEIKRESSGLNEVNVDLNDGVAENSGVSEENLRGNVDLNCGPVETLGRTWDSSVTDLNRTVSESETGFDLTTGLDWNSNENLGLVNVNIDYEENCSDKRKWDIDLNMDASCDLDNAAICDFSGQKREVGFDLNVEVDVENSKDEEYSQMNGNDIVQEINMQDGNGAQDNIETGEYKEVHVAEVSSAELLEEIQKQNIVSPQDLKNLNSNGVEKDPDLPHHDAKTVDETLSDRGNSGEYTSGRRKRRKASDNPKFMSEPQLRRSARRRLARSPVSSTVTACFVEEVSPSPSISSLTEEKTWIVDGKADNISALPPKPQLPPSSPILDLDGLPVLDVFTAYSCLRSFSTLLFLSPFELKDFVEALRCMSPSLLFDSIHVSVLQILRKHLKQLAAEGDLSASACLRSLDWDTLDVVTYPLFVVEYLLCSGSKDNPGLDLTRLNFFRNDYFRQPVNLKIEILSRLCDDMTDAEVVRAELNKRSFAAEFEMELDRKTNTEVRRRKRTMMELADDFSLNNEVIDTSFDRNSDDCCFCKMDGSLLCCDGCPAAYHSKCVGLASHLLPEGDWYCPECAFDRRAPGLKPDKQIRGAEFIEIDPHGRKYYSSCGYLLVIDTDGTGSLNYYHVTDVNLVLEQLKSCSSFYAGVVSAIRKHLDIPVRPVRTISGLNSQMSVCMDKSVKGMIPSIDGFGAPLPASEKQSTSGAKKKLNKATSNGWSHNHGPRTRRKISDSATALDILNMSSEGSAETVQNGSDVQRLHEPASSSMLDIMKEPNMNSQNLAKINTRKGTKPNVQTETGYRNQYIFAQMTRSVYEEMIRKSPIRTNDMRSDEEIASTQVRTILMKTTKFQWRNIQSLYLDAWKENCGWCHSCKNSSEDAGTEINCLFNMSLGALRGLSESEVANIQSFEKNSHLLAIICQILSLESRLQGLLVGPWLNPQHSSFWREHILKASNISSLKHLLVDLEANLHHRVLSLEWLSHVDAAVVMGSAIHILIASTRSWSKTAIGKRRGTLLDSGVNPTAKKNGGLTMCWWRGGQLSRRLFNWKVLPRALISKAARQGGSMNIPGIFYPENSESAKRSRRVAWEAAVESSTTSEQLGLQIRTLQSYIKWDDIENSHLLPTLDKESRKSARLFKKAIVRRKCTEEETVKYLLDFGKRRNIPDVVSKNGCMVEESSSGRKRFWLNESHVPLHLVKGFEEKKAVRKTSKPGGSFRHSEIGKLRKRSSEGKGFSYLFERAERSESSLCEQCKKVVPLSEAASCHICKGVFHKKHIRRGEKEGMYICVPCKSEVLSKEQPTVRKRGRPPGSFRKKIGVQTQKRKKVIAARKSPRLKKTKTSMAERIAIRLKNHKKVVASKPLRRSGRQLKHVIRLQDESKVPEGSKKRKLETKRGRGRPKKVKQEISIRKARTDRCLNYWLNGLLLSRKAGNERVHQFHRERYYVPLENSDSDHDQPKCHLCGSIESKSGSTFISCELCGEWYHGDAYGLNEKNSSMVIGFRCHLCRKQSSPTCPHMRSTTSPVAS
Protein: Anaphase-promoting complex subunit 10 (APC10) (Cyclosome subunit 10) (Q8K2H6)
Organism: Mus musculus (Mouse)
Function: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the formation of 'Lys-11'-linked polyubiquitin chains and, to a lower extent, the formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains (By similarity).
Interaction partners:
- Anaphase-promoting complex subunit 7
- Anaphase-promoting complex subunit 1
- Anaphase-promoting complex subunit 2
- Anaphase-promoting complex subunit 11
- Anaphase-promoting complex subunit 4
- Cell division cycle protein 23 homolog
- Cell division cycle protein 20 homolog
- Anaphase-promoting complex subunit 13
- Cell division cycle protein 27 homolog
- Anaphase-promoting complex subunit 5
Sequence:
MTTPNKTPPGADPKQLERTATVREIGSQAVWSLSSCKPGFGVDQLRDDNLETYWQSDGSQPHLVNIQFRRKTTVKTLCIYADYKSDESYTPSKISVRVGNNFHNLQEIRQLELVEPSGWIHVPLTDNHKKPTRTFMIQIAVLANHQNGRDTHMRQIKIYTPVEESSIGKFPRCTTIDFMMYRSIR
Protein: Hsp30p (Q59TA5)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Heat shock protein 78
Sequence:
MSAAVSTLSDIIKRNDAVNVNPPNPIIDLHITEHGSDWLWAVFSVFALFAIVHGFIYSFTDVRKSGLKRALLTIPLFNSAVFAFAYYTYASNLGYTWILTEFNHAGTGFRQIFYAKFVAWFLGWPLVLAIFQIITNTSFTTTEDESDLLKKFISLFEALFTRVLAIEVFVLGLLIGALIESTYKWGYFTFAVVFQLFAIYLVINDVVVSFGSSSHSVFGNALILAFVIVWILYPVAWGLSEGGNVIQPDSEAVFYGILDLITFGVIPIILTWIAINNVDEEFFTKIWHFHLKPENEHAPTATEDVEKAVGETPRHSGDTAVAPSGVPDTGVAQAQAEAEERI
Protein: ilv operon leader peptide (ilvBN operon attenuator peptide) (P03061)
Organism: Escherichia coli (strain K12)
Function: This protein is involved in control of the biosynthesis of isoleucine, leucine, and valine.
Interaction partners:
- Acetolactate synthase isozyme 1 large subunit
- ilv operon leader peptide
- Acetolactate synthase isozyme 1 small subunit
- leu operon leader peptide
Sequence:
MTTSMLNAKLLPTAPSAAVVVVRVVVVVGNAP
Protein: Hemocyanin II (P04253)
Organism: Limulus polyphemus (Atlantic horseshoe crab)
Function: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods.
Subcellular location: Secreted, extracellular space.
Interaction partners:
Sequence:
TLHDKQIRVCHLFEQLSSATVIGDGDKHKHSDRLKNVGKLQPGAIFSCFHPDHLEEARHLYEVFWEAGDFNDFIEIAKEARTFVNEGLFAFAAEVAVLHRDDCKGLYVPPVQEIFPDKFIPSAAINEAFKKAHVRPEFDESPILVDVQDTGNILDPEYRLAYYREDVGINAHHWHWHLVYPSTWNPKYFGKKKDRKGELFYYMHQQMCARYDCERLSNGMHRMLPFNNFDEPLAGYAPHLTHVASGKYYSPRPDGLKLRDLGDIEISEMVRMRERILDSIHLGYVISEDGSHKTLDELHGTDILGALVESSYESVNHEYYGNLHNWGHVTMARIHDPDGRFHEEPGVMSDTSTSLRDPIFYNWHRFIDNIFHEYKNTLKPYDHDVLNFPDIQVQDVTLHARVDNVVHFTMREQELELKHGINPGNARSIKARYYHLDHEPFSYAVNVQNNSASDKHATVRIFLAPKYDELGNEIKADELRRTAIELDKFKTDLHPGKNTVVRHSLDSSVTLSHQPTFEDLLHGVGLNEHKSEYCSCGWPSHLLVPKGNIKGMEYHLFVMLTDWDKDKVDGSESVACVDAVSYCGARDHKYPDKKPMGFPFDRPIHTEHISDFLTNNMFIKDIKIKFHE
Protein: Beta-1,3-galactosyltransferase 5 (Beta-1,3-GalTase 5) (Beta3Gal-T5) (Beta3GalT5) (b3Gal-T5) (EC 2.4.1.-) (Beta-3-Gx-T5) (Stage-specific embryonic antigen 3 synthase) (SSEA-3 synthase) (UDP-Gal:beta-GlcNAc beta-1,3-galactosyltransferase 5) (UDP-galactose:beta-N-acetylglucosamine beta-1,3-galactosyltransferase 5) (Q9JI67)
Organism: Mus musculus (Mouse)
Function: Catalyzes the transfer of Gal to GlcNAc-based acceptors with a preference for the core3 O-linked glycan GlcNAc(beta1,3)GalNAc structure. Can use glycolipid LC3Cer as an efficient acceptor. Also catalyzes the transfer of Gal to the terminal GalNAc unit of the globoside GB4, thereby synthesizing the glycolipid GB5, also known as the stage-specific embryonic antigen-3 (SSEA-3).
Subcellular location: Golgi apparatus membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}.
Interaction partners:
- Galactoside alpha-
- Galactoside alpha-
- Beta-1,4-galactosyltransferase 4
- Beta-1,4-galactosyltransferase 1
- Galactoside 2-alpha-L-fucosyltransferase Sec1
- N-acetyllactosaminide alpha-1,3-galactosyltransferase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 2
- CMP-N-acetylneuraminate-beta-1,4-galactoside alpha-2,3-sialyltransferase
- CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1
- Beta-1,4-galactosyltransferase 3
Sequence:
MAHMKTRLVYASILMMGALCLYFSMDSFRELPFVFKKSHGKFLQIPDIDCKQKPPFLVLLVTSSHKQLAARMAIRKTWGRETSVQGQQVRTFFLLGTSDSTEEMDATTLESEQHRDIIQKDFKDAYFNLTLKTMMGMEWVYHFCPQTAYVMKTDSDMFVNVGYLTELLLKKNKTTRFFTGYIKPHDFPIRQKFNKWFVSKFEYPWDRYPPFCSGTGYVFSSDVAIQVYNVSESVPFIKLEDVFVGLCLAKLKIRPEELHTKQTFFPGGLRFSVCRFQKIVACHFMKPQDLLTYWQALENSKEQDCPAV
Protein: Secreted Ly-6/uPAR domain-containing protein 2 (Secreted LY6/PLAUR domain-containing protein 2) (Secreted Ly-6/uPAR-related protein 2) (SLURP-2) (P0DP57)
Organism: Homo sapiens (Human)
Function: Binds and may modulate the functional properties of nicotinic and muscarinic acetylcholine receptors. May regulate keratinocytes proliferation, differentiation and apoptosis. In vitro moderately inhibits ACh-evoked currents of alpha-3:beta-2-containing nAChRs and strongly these of alpha-4:beta-2-containing nAChRs, modulates alpha-7-containing nAChRs, and inhibits nicotine-induced signaling probably implicating alpha-3:beta-4-containing nAChRs. Proposed to act on alpha-3:beta-2 and alpha-7 nAChRs in an orthosteric, and on mAChRs, such as CHRM1 and CHRM3, in an allosteric manner.
Subcellular location: Secreted {ECO:0000269|PubMed:16575903}.
Interaction partners:
- Secreted Ly-6/uPAR-related protein 1
- Neuronal acetylcholine receptor subunit alpha-9
Sequence:
MQLGTGLLLAAVLSLQLAAAEAIWCHQCTGFGGCSHGSRCLRDSTHCVTTATRVLSNTEDLPLVTKMCHIGCPDIPSLGLGPYVSIACCQTSLCNHD
Protein: Histone acetyltransferase KAT6A (EC 2.3.1.48) (MOZ, YBF2/SAS3, SAS2 and TIP60 protein 3) (MYST-3) (Monocytic leukemia zinc finger protein) (Runt-related transcription factor-binding protein 2) (Zinc finger protein 220) (Q92794)
Organism: Homo sapiens (Human)
Function: Histone acetyltransferase that acetylates lysine residues in histone H3 and histone H4 (in vitro). Component of the MOZ/MORF complex which has a histone H3 acetyltransferase activity. May act as a transcriptional coactivator for RUNX1 and RUNX2. Acetylates p53/TP53 at 'Lys-120' and 'Lys-382' and controls its transcriptional activity via association with PML.
Subcellular location: Nucleus. Nucleus, nucleolus. Nucleus, nucleoplasm. Nucleus, PML body. Note=Recruited into PML body after DNA damage.
Interaction partners:
- Peregrin
- Inhibitor of growth protein 5
- Chromatin modification-related protein MEAF6
- Histone acetyltransferase KAT6B
- Histone H3.1t
- Bromodomain-containing protein 1
- Histone H3.1
- Histone H3.2
- Histone H3.3C
- Bromodomain and PHD finger-containing protein 3
Sequence:
MVKLANPLYTEWILEAIKKVKKQKQRPSEERICNAVSSSHGLDRKTVLEQLELSVKDGTILKVSNKGLNSYKDPDNPGRIALPKPRNHGKLDNKQNVDWNKLIKRAVEGLAESGGSTLKSIERFLKGQKDVSALFGGSAASGFHQQLRLAIKRAIGHGRLLKDGPLYRLNTKATNVDGKESCESLSCLPPVSLLPHEKDKPVAEPIPICSFCLGTKEQNREKKPEELISCADCGNSGHPSCLKFSPELTVRVKALRWQCIECKTCSSCRDQGKNADNMLFCDSCDRGFHMECCDPPLTRMPKGMWICQICRPRKKGRKLLQKKAAQIKRRYTNPIGRPKNRLKKQNTVSKGPFSKVRTGPGRGRKRKITLSSQSASSSSEEGYLERIDGLDFCRDSNVSLKFNKKTKGLIDGLTKFFTPSPDGRKARGEVVDYSEQYRIRKRGNRKSSTSDWPTDNQDGWDGKQENEERLFGSQEIMTEKDMELFRDIQEQALQKVGVTGPPDPQVRCPSVIEFGKYEIHTWYSSPYPQEYSRLPKLYLCEFCLKYMKSRTILQQHMKKCGWFHPPANEIYRKNNISVFEVDGNVSTIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVLTQNDVKGCHLVGYFSKEKHCQQKYNVSCIMILPQYQRKGYGRFLIDFSYLLSKREGQAGSPEKPLSDLGRLSYMAYWKSVILECLYHQNDKQISIKKLSKLTGICPQDITSTLHHLRMLDFRSDQFVIIRREKLIQDHMAKLQLNLRPVDVDPECLRWTPVIVSNSVVSEEEEEEAEEGENEEPQCQERELEISVGKSVSHENKEQDSYSVESEKKPEVMAPVSSTRLSKQVLPHDSLPANSQPSRRGRWGRKNRKTQERFGDKDSKLLLEETSSAPQEQYGECGEKSEATQEQYTESEEQLVASEEQPSQDGKPDLPKRRLSEGVEPWRGQLKKSPEALKCRLTEGSERLPRRYSEGDRAVLRGFSESSEEEEEPESPRSSSPPILTKPTLKRKKPFLHRRRRVRKRKHHNSSVVTETISETTEVLDEPFEDSDSERPMPRLEPTFEIDEEEEEEDENELFPREYFRRLSSQDVLRCQSSSKRKSKDEEEDEESDDADDTPILKPVSLLRKRDVKNSPLEPDTSTPLKKKKGWPKGKSRKPIHWKKRPGRKPGFKLSREIMPVSTQACVIEPIVSIPKAGRKPKIQESEETVEPKEDMPLPEERKEEEEMQAEAEEAEEGEEEDAASSEVPAASPADSSNSPETETKEPEVEEEEEKPRVSEEQRQSEEEQQELEEPEPEEEEDAAAETAQNDDHDADDEDDGHLESTKKKELEEQPTREDVKEEPGVQESFLDANMQKSREKIKDKEETELDSEEEQPSHDTSVVSEQMAGSEDDHEEDSHTKEELIELKEEEEIPHSELDLETVQAVQSLTQEESSEHEGAYQDCEETLAACQTLQSYTQADEDPQMSMVEDCHASEHNSPISSVQSHPSQSVRSVSSPNVPALESGYTQISPEQGSLSAPSMQNMETSPMMDVPSVSDHSQQVVDSGFSDLGSIESTTENYENPSSYDSTMGGSICGNSSSQSSCSYGGLSSSSSLTQSSCVVTQQMASMGSSCSMMQQSSVQPAANCSIKSPQSCVVERPPSNQQQQPPPPPPQQPQPPPPQPQPAPQPPPPQQQPQQQPQPQPQQPPPPPPPQQQPPLSQCSMNNSFTPAPMIMEIPESGSTGNISIYERIPGDFGAGSYSQPSATFSLAKLQQLTNTIMDPHAMPYSHSPAVTSYATSVSLSNTGLAQLAPSHPLAGTPQAQATMTPPPNLASTTMNLTSPLLQCNMSATNIGIPHTQRLQGQMPVKGHISIRSKSAPLPSAAAHQQQLYGRSPSAVAMQAGPRALAVQRGMNMGVNLMPTPAYNVNSMNMNTLNAMNSYRMTQPMMNSSYHSNPAYMNQTAQYPMQMQMGMMGSQAYTQQPMQPNPHGNMMYTGPSHHSYMNAAGVPKQSLNGPYMRR
Protein: Purine nucleoside phosphorylase LACC1 (EC 2.4.2.1) (Adenosine deaminase LACC1) (EC 3.5.4.4) (Fatty acid metabolism-immunity nexus) (Guanosine phosphorylase LACC1) (Laccase domain-containing protein 1) (S-methyl-5'-thioadenosine phosphorylase LACC1) (EC 2.4.2.28) (Q8IV20)
Organism: Homo sapiens (Human)
Function: Purine nucleoside enzyme that catalyzes the phosphorolysis of adenosine, guanosine and inosine nucleosides, yielding D-ribose 1-phosphate and the respective free bases, adenine, guanine and hypoxanthine. Also catalyzes the phosphorolysis of S-methyl-5'-thioadenosine into adenine and S-methyl-5-thio-alpha-D-ribose 1-phosphate. Also has adenosine deaminase activity. Acts as a regulator of innate immunity in macrophages by modulating the purine nucleotide metabolism, thereby regulating the metabolic function and bioenergetic state of macrophages. Enables a purine nucleotide cycle between adenosine and inosine monophosphate and adenylosuccinate that prevents cytoplasmic acidification and balances the cytoplasmic-mitochondrial redox interface. The purine nucleotide cycle consumes aspartate and releases fumarate in a manner involving fatty acid oxidation and ATP-citrate lyase activity. Participates in pattern recognition receptor (PRR)-induced cytokines in macrophages: associates with the NOD2-signaling complex and promotes optimal NOD2-induced signaling, cytokine secretion and bacterial clearance. Localizes to the endoplasmic reticulum upon PRR stimulation of macrophages and associates with endoplasmic reticulum-stress sensors, promoting the endoplasmic reticulum unfolded protein response (UPR). Does not show laccase activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8BZT9}. Nucleus {ECO:0000250|UniProtKB:Q8BZT9}. Endoplasmic reticulum {ECO:0000269|PubMed:31875558}. Peroxisome {ECO:0000269|PubMed:27478939, ECO:0000269|PubMed:27959965}. Note=Upon stimulation of the pattern-recognition receptor (PRR) NOD2, localizes to the endoplasmic reticulum. {ECO:0000269|PubMed:31875558}.
Interaction partners:
- Coiled-coil domain-containing protein 122
- Pyridoxal phosphate homeostasis protein
- Tumor necrosis factor ligand superfamily member 15
- Receptor-interacting serine/threonine-protein kinase 2
Sequence:
MAEAVLIDLFGLKLNSQKNCHQTLLKTLNAVQYHHAAKAKFLCIMCCSNISYERDGEQDNCEIETSNGLSALLEEFEIVSCPSMAATLYTIKQKIDEKNLSSIKVIVPRHRKTLMKAFIDQLFTDVYNFEFEDLQVTFRGGLFKQSIEINVITAQELRGIQNEIETFLRSLPALRGKLTIITSSLIPDIFIHGFTTRTGGISYIPTLSSFNLFSSSKRRDPKVVVQENLRRLANAAGFNVEKFYRIKTHHSNDIWIMGRKEPDSYDGITTNQRGVTIAALGADCIPIVFADPVKKACGVAHAGWKGTLLGVAMATVNAMIAEYGCSLEDIVVVLGPSVGPCCFTLPRESAEAFHNLHPACVQLFDSPNPCIDIRKATRILLEQGGILPQNIQDQNQDLNLCTSCHPDKFFSHVRDGLNFGTQIGFISIKE
Protein: Frizzled-2 (Fz-2) (hFz2) (FzE2) (Q14332)
Organism: Homo sapiens (Human)
Function: Receptor for Wnt proteins. Most of frizzled receptors are coupled to the beta-catenin canonical signaling pathway, which leads to the activation of disheveled proteins, inhibition of GSK-3 kinase, nuclear accumulation of beta-catenin and activation of Wnt target genes. A second signaling pathway involving PKC and calcium fluxes has been seen for some family members, but it is not yet clear if it represents a distinct pathway or if it can be integrated in the canonical pathway, as PKC seems to be required for Wnt-mediated inactivation of GSK-3 kinase. Both pathways seem to involve interactions with G-proteins. May be involved in transduction and intercellular transmission of polarity information during tissue morphogenesis and/or in differentiated tissues.
Subcellular location: Membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- Protein Wnt-5a
- Protein Wnt-3a
- Protein Wnt-11
- Proto-oncogene Wnt-1
- Protein Wnt-4
- Protein Wnt-5b
- Tyrosine-protein kinase RYK
- Protein Wnt-2
- Protein Wnt-6
- Protein Wnt-7b
Sequence:
MRPRSALPRLLLPLLLLPAAGPAQFHGEKGISIPDHGFCQPISIPLCTDIAYNQTIMPNLLGHTNQEDAGLEVHQFYPLVKVQCSPELRFFLCSMYAPVCTVLEQAIPPCRSICERARQGCEALMNKFGFQWPERLRCEHFPRHGAEQICVGQNHSEDGAPALLTTAPPPGLQPGAGGTPGGPGGGGAPPRYATLEHPFHCPRVLKVPSYLSYKFLGERDCAAPCEPARPDGSMFFSQEETRFARLWILTWSVLCCASTFFTVTTYLVDMQRFRYPERPIIFLSGCYTMVSVAYIAGFVLQERVVCNERFSEDGYRTVVQGTKKEGCTILFMMLYFFSMASSIWWVILSLTWFLAAGMKWGHEAIEANSQYFHLAAWAVPAVKTITILAMGQIDGDLLSGVCFVGLNSLDPLRGFVLAPLFVYLFIGTSFLLAGFVSLFRIRTIMKHDGTKTEKLERLMVRIGVFSVLYTVPATIVIACYFYEQAFREHWERSWVSQHCKSLAIPCPAHYTPRMSPDFTVYMIKYLMTLIVGITSGFWIWSGKTLHSWRKFYTRLTNSRHGETTV
Protein: Dynactin-associated protein (Full) (Q8N1N2)
Organism: Homo sapiens (Human)
Function: Plays a role in the regulation of cell proliferation. Promotes activation of the AKT1 signaling pathway. Promotes phosphorylation of AKT1 at 'Ser-473'.
Subcellular location: Golgi apparatus membrane {ECO:0000269|PubMed:20978158}; Single-pass membrane protein {ECO:0000269|PubMed:20978158}. Cell membrane {ECO:0000269|PubMed:20978158}; Single-pass membrane protein {ECO:0000269|PubMed:20978158}. Note=Concentrated at cell-cell borders. Localizes at membranes in a microtubule-dependent manner.
Interaction partners:
- Ubiquitin-like protein FUBI
Sequence:
MVADIKGNEQIEKYSWREACDTGSSRMDRKHGKYILNVEHSENQPPITHPNDQEAHSSICWCLPSNDITSDVSPNLTGVCVNPGILAHSRCLQSESCNTQVKEYCRNDWSMWKVFLACLLACVIMTAIGVLIICLVNNKGSANSSIVIQLSTNDGECVTVKPGTPSPACPPTMTTTSTVPASTATESTTSTATAATTSTEPITVAPTDHL
Protein: Nuclear autoantigenic sperm protein (NASP) (Q99MD9)
Organism: Mus musculus (Mouse)
Function: Required for DNA replication, normal cell cycle progression and cell proliferation. Forms a cytoplasmic complex with HSP90 and linker H1 histones and stimulates HSP90 ATPase activity. NASP and H1 histone are subsequently released from the complex and translocate to the nucleus where the histone is released for binding to DNA.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10893414, ECO:0000269|PubMed:12509435, ECO:0000269|PubMed:16728391}. Nucleus {ECO:0000269|PubMed:10893414, ECO:0000269|PubMed:12509435, ECO:0000269|PubMed:16728391}.
Interaction partners:
- Histone acetyltransferase type B catalytic subunit
- Histone chaperone ASF1B
- Histone chaperone ASF1A
- Histone-binding protein RBBP7
- Histone-binding protein RBBP4
- Histone H4
- Heat shock protein HSP 90-alpha
- Heat shock protein HSP 90-beta
- Histone H1.0
- Integrator complex assembly factor WDR73
Sequence:
MATESTAAAAIAAELVSADKIEDAPAPSTSADKMESLDVDSEAKKLLGLGQKHLVMGDIPAAVNAFQEAASLLGKKYGETANECGEAFFFYGKSLLELARMENGVLGNALEGVHVEEEEGEKTEDESLVENNDNVDEEAREELREQVYDAMGEKEAKKAEGKSLTKPETDKEQESEVEKGGREDMDISEPEEKLQETVEPTSKQLTESSEEAKEAAIPGLNEDEVASGKTEQESLCTEKGKSISGAYVQNKEFRETVEEGEEIISLEKKPKETSEDQPIRAAEKQGTLMKVVEIEAEIDPQVKSADVGGEEPKDQVATSESELGKAVLMELSGQDVEASPVVAAEAGAEVSEKPGQEITVIPNNGPVVGQSTVGDQTPSEPQTSAERLTETKDGSSVEEVKAELVPEQEEAMLPVEESEAAGDGVETKVAQKATEKAPEDKFKIAANEETPERDEQMKEGEETEGSEEEDRENDKAEETPNESVLEKKSLQENEEEEIGNLELAWDMLDLAKIIFKRQETKEAQLYAAQAHLKLGEVSVESENYIQAVEEFQACLSLQEQYLEAHDRLLAETHYQLGLAYGYNSQYDEAVAQFGKSIDVIEKRMAVLHEQMKEAEGSFTEYEKEIEELKELLPEIREKIEDAKESQRSGNVAELALKATLVESSTSGFTPSGAGASVSMIASRKPTDGASSSNCVTDISHLVRKKRKPEEESPRKDDAKKAKQEPEVNGGSGDAVSSGKEVSENMEAEAENQAESQTAEGTVESAATIKSTAC
Protein: DNA-directed RNA polymerase III subunit RPC3 (RNA polymerase III subunit C3) (E9PHH9)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123, ECO:0000256|RuleBase:RU367076}.
Interaction partners:
Sequence:
MTQAEIKLCSLLLQEHFGEIVEKIGVHLIRTGSQPLRVIAHDTGTSLDQVKKALCVLVQHNLVSYQVHKRGVVEYEAQCSRVLRMLRYPRYIYTTKTLYSDTGELIVEELLLNGKLTMSAVVKKVADRLTETMEDGKTMDYAEVSNTFVRLADTHFVQRCPSVPTTENSDPGPPPPAPTLVINEKDMYLVPKLSLIGKGKRRRSSDEDAAGEPKAKRPKYTTDNKEPIPDDGIYWQANLDRFHQHFRDQAIVSAVANRMDQTSSEIVRTMLRMSEITTSSSAPFTQPLSSNEIFRSLPVGYNISKQVLDQYLTLLADDPLEFVGKSGDSGGGMYVINLHKALASLATATLESVVQERFGSRCARIFRLVLQKKHIEQKQVEDFAMIPAKEAKDMLYKMLSENFMSLQVGCQ
Protein: Cdc42-interacting protein 4, isoform F (M9NDH6)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MNCLLGYLNAAQRSLSESGVATILDPRDSHLEFWDQNENLAIHTNRGIDALDKFANFLRDRVAIETEYAGKLRRLVKNYQPKKKEEEDNEFTSVQAFRNLLKEVGDLAGQREVVSESLQLQIIAGVTLLSKTLREERKKCLSDGATLQQNLTTQLSSLDRAKRNYEKAYRDSEKAVDSYKRADMDLNLSRAEVERYKNVMTSKIQQSDDAKNEYANQLQKTNNLQQQHYSMLLPSVLNRLQELDEKRTRGFREFIVGAADVESSVAPIIARCMEGIVKAGESINEKEDTFKVIERYQSGFTPPRDIPFEDLSKCDPDSVQDSHYSNSTSNHLTIRGTMSANKLKKRVGIFNIFGSNKNSLTADGQKEDFSDLPPNQRRKKLQAKIAELTQNIAQETKARDGLMKMKIVYEANSSLGNPMTVEGQLNESEHKLEKLKVDLKKYQGFLEKASQVPTATSSPQASRNQLQNGHRTSRHSNGSADDHHDDGDDQPDDAGSLSRSDSEDNVAQIQNGHNNNNNGSSASPESGLGTSHTSLPGSGQGSANENAIGEDTYYETEVETLNPVGKCRALYPFEASSEGSIPMSEGEELQVIEIDQGDGWTRVRRENNSNGWDEGFVPTSYIEITLYA
Protein: Protein CAJ1 (P39101)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Interaction partners:
- J protein JJJ2
- Auxilin-like clathrin uncoating factor SWA2
- Zuotin
- Mitochondrial DnaJ homolog 2
- J domain-containing protein 1
- ER-localized J domain-containing protein 5
- Pre-mRNA-splicing factor CEF1
- Mitochondrial import inner membrane translocase subunit TIM14
- DnaJ-like chaperone JEM1
- J-type co-chaperone JAC1, mitochondrial
Sequence:
MVKETEYYDILGIKPEATPTEIKKAYRRKAMETHPDKHPDDPDAQAKFQAVGEAYQVLSDPGLRSKYDQFGKEDAVPQQGFEDASEYFTAIFGGDGFKDWIGEFSLFKELNEATEMFGKEDEEGTAATETEKADESTDGGMVKHDTNKAESLKKDKLSKEQREKLMEMEKKRREDMMKQVDELAEKLNEKISRYLIAVKSNNLEEFTRKLDQEIEDLKLESFGLELLYLLARVYKTKANNFIMSKKTYGISKIFTGTRDNARSVKSAYNLLSTGLEAQKAMEKMSEVNTDELDQYERAKFESTMAGKALGVMWAMSKFELERKLKDVCNKILNDKKVPSKERIAKAKAMLFIAHKFASARRSPEEAEEARVFEELILGEQEKEHKKHTVAR