wanglab/gogpt-training-data huggingface dataset:
Protein: SAGA-associated factor 73 (73 kDa SAGA-associated factor) (SAGA histone acetyltransferase complex 73 kDa subunit) (P53165)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Functions as component of the transcription regulatory histone acetylation (HAT) complex SAGA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Histone acetyltransferase GCN5
- SAGA complex subunit SPT7
- SAGA complex subunit NGG1
- SAGA complex subunit SPT20
- SAGA complex/NuA4 acetyltransferase complex subunit TRA1
- SAGA complex subunit SGF11
- Ubiquitin carboxyl-terminal hydrolase 8
- SAGA complex subunit SPT3
- SAGA complex/transcription factor TFIID complex subunit TAF9
- SAGA complex/transcription factor TFIID complex subunit TAF10
Sequence:
MRSGDAEIKGIKPKVIEEYSLSQGSGPSNDSWKSLMSSAKDTPLQYDHMNRESLKKYFNPNAQLIEDPLDKPIQYRVCEKCGKPLALTAIVDHLENHCAGASGKSSTDPRDESTRETIRNGVESTGRNNNDDDNSNDNNNDDDDDDDNDDNEDDDDADDDDDNSNGANYKKNDSSFNPLKRSTSMESANTPNMDTKRSKTGTPQTFSSSIKKQKKVKQRNPTEKHLIDFNKQCGVELPEGGYCARSLTCKSHSMGAKRAVSGRSKPYDVLLADYHREHQTKIGAAAEKRAKQQELQKLQKQIQKEQKKHTQQQKQGQRSKQRNVNGGKSAKNGGKSTVHNGNNINEIGHVNLTPEEETTQVLNGVSRSFPLPLESTVLSSVRYRTKYFRMREMFASSFSVKPGYTSPGYGAIHSRVGCLDLDRTTDYKFRVRTPQPINHLTNQNLNPKQIQRLQQQRALQAQLLSQQQQQQQQQQQHHSPQAQAQASTQQPTQGMVPNHFPGGATNSSFNANVSSKQIQQQQQQQQHKSQDTGLTPLEIQSQQQKLRQQQLQQQKFEAAASYLANATKLMQESNQDSHLSGTHNNNSSKNGNNNLMTMKASISSPNTSVNSIQSPPSVNSVNGSGQGVSTGINVSGNNGRIEVGIGNSVNPYNGRIN
Protein: Runt-related transcription factor rnt-1 (G5EFQ5)
Organism: Caenorhabditis elegans
Function: Transcription factor (By similarity). Binds to regulatory DNA sequences in order to modulate transcription; negatively autoregulates its own expression, perhaps dependent upon CBF beta homolog bro-1. Promotes proliferation, and prevents differentiation, of seam cells, a stem cell-like lineage, acting in concert with bro-1. Required for controlling cell proliferation in the seam cells, perhaps by repressing expression of cyclin-dependent kinase inhibitor cki-1. Inhibition of seam cell differentiation is regulated by rnt-1 and bro-1, perhaps acting upstream of pop-1, by antagonizing pop-1 repressor function. Required for asymmetrical cell divisions in the lineage derived from a posterior embryonic seam cell, the T blast cell, and for asymmetric expression of zinc finger protein tlp-1. Regulates growth and male tail development. Involved in the oxidative stress response, perhaps downstream of the p38 MAP kinase pathway, and acting as part of a negative feedback loop via a transcriptional target gene, tyrosine-protein phosphatase vhp-1. Positively modulates dopaminergic signaling in a non-cell autonomous manner. May be involved in TGF-beta signaling.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00399, ECO:0000269|PubMed:16226243, ECO:0000269|PubMed:16236764, ECO:0000269|PubMed:31740621}. Note=High level of nuclear localization in interphase seam cells before the symmetric larval stage L2 divisions, but subsequently rnt-1 disappears during mitosis, and largely remains absent when the nuclei reform in telophase. {ECO:0000269|PubMed:31740621}.
Interaction partners:
- Core-binding factor subunit beta homolog bro-1 homolog)
- Zinc Finger and Homeobox
- G1/S-specific cyclin-D
- Tyrosine protein-kinase src-1
- RING-type domain-containing protein
- Protein pop-1
- Transcription factor unc-37
- Transcription factor elt-1
- Protein arginine N-methyltransferase 1
- Protein dbl-1
Sequence:
MTNVFHHVRNFIEQQPAPAKTLEKSSSPNILYTALPKHWRSNKSFQEPFYVVLLTPVPDNTEVSIWAGNDEKPCEEVRNEKAKVHRQVAKFNDLRFVGRSGRGRKFHLTIVIHSAPMMVATVKNVIKVTVDGPRDARIPKPQGSLKRQAEQQTIFPNDIIRTPGPPMPMTMIPPPWFPLPMTQTFPPSFFPLISPGPHPSISAALWKIHSESMKTPIKQKVEQENVSLNTSTCLSSPSIFITPTSDDRKLKRPSSPRSITKSSETSINLIQETPESVESKRRRNVSITSSNSSSPTIWRPF
Protein: Voltage-dependent N-type calcium channel subunit alpha (O89089)
Organism: Rattus norvegicus (Rat)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141, ECO:0000256|RuleBase:RU003808}.
Interaction partners:
Sequence:
MVRFGDELGGRYGGTGGGERARGGGAGGAGGPGQGGLPPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFVFHKGSYLRNGWNVMDFVVVLTGILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDAEPVGDFPCGKEAPARLCDSDTECREYWPGPNFGITNFDNILFAILTVFQCITMEGWTDILYNTNDAAGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYLEWIFKAEEVMLAEEDKNAEEKSPLDVLKRAATKKSRNDLIHAEEGEDRFVDLCAAGSPFARASLKSGKTESSSYFRRKEKMFRFLIRRMVKAQSFYWVVLCVVALNTLCVAMVHYNQPQRLTTALYFAEFVFLGLFLTEMSLKMYGLGPRSYFRSSFNCFDFGVIVGSIFEVVWAAIKPGTSFGISVLRALRLLRIFKVTKYWNSLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFQDETPTTNFDTFPAAILTVFQILTGEDWNAVMYHGIESQGGVSKGMFSSFYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEEEMEEAANQKLALQKAKEVAEVSPMSAANISIAARQQNSAKARSVWEQRASQLRLQNLRASCEALYSEMDPEERLRYASTRHVRPDMKTHMDRPLVVEPGRDGLRGPAGNKSKPEGTEATEGADPPRRHHRHRDRDKTSASTPAGGEQDRTDCPKAESTETGAREERARPRRSHSKEAPGADTQVRCERSRRHHRRGSPEEATEREPRRHRAHRHAQDSSKEGKEGTAPVLVPKGERRARHRGPRTGPRETENSEEPTRRHRAKHKVPPTLEPPEREVAEKESNVVEGDKETRNHQPKEPRCDLEAIAVTGVGSLHMLPSTCLQKVDEQPEDADNQRNVTRMGSQPSDPSTTVHVPVTLTGPPGEATVVPSANTDLEGQAEGKKEAEADDVLRRGPRPIVPYSSMFCLSPTNLLRRFCHYIVTMRYFEMVILVVIALSSIALAAEDPVRTDSFRNNALKYMDYIFTGVFTFEMVIKMIDLGLLLHPGAYFRDLWNILDFIVVSGALVAFAFSGSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVLNILIVYMLFMFIFAVIAVQLFKGKFFYCTDESKELERDCRGQYLDYEKEEVEAQPRQWKKYDFHYDNVLWALLTLFTVSTGEGWPMVLKHSVDATYEEQGPSPGFRMELSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKVMSECSLEKNERACIDFAISAKPLTRYMPQNKQSFQYKTWTFVVSPPFEYFIMAMIALNTVVLMMKFYDAPYEYELMLKCLNIVFTSMFSLECILKIIAFGVLNYFRDAWNVFDFVTVLGSITDILVTEIAETNNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDDGTSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLGNRACDPHANASECGSDFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFIRVWAEYDPAACGRISYNDMFEMLKHMSPPLGLGKKCPARVAYKRLVRMNMPISNEDMTVHFTSTLMALIRTALEIKLAPAGTKQHQCDAELRKEISSVWANLPQKTLDLLVPPHKPDEMTVGKVYAALMIFDFYKQNKTTRDQTHQAPGGLSQMGPVSLFHPLKATLEQTQPAVLRGARVFLRQKSATSLSNGGAIQTQESGIKESLSWGTQRTQDVLYEARAPLERGHSAEIPVGQPGALAVDVQMQNMTLRGPDGEPQPGLESQGRAASMPRLAAETQPAPNASPMKRSISTLAPRPHGTQLCNTVLDRPPPSQVSHHHHHRCHRRRDKKQRSLEKGPSLSVDTEGAPSTAAGSGLPHGEGSTGCRRERKQERGRSQERRQPSSSSSEKQRFYSCDRFGSREPPQPKPSLSSHPISPTAALEPGPHPQGSGSVNGSPLMSTSGASTPGRGGRRQLPQTPLTPRPSITYKTANSSPVHFAEGQSGLPAFSPGRLSRGLSEHNALLQKEPLSQPLASGSRIGSDPYLGQRLDSEASAHNLPEDTLTFEEAVATNSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSTGVRARHSYHHPDQDHWC
Protein: Protein SOSEKI 5 (AtSOK5) (Q9FJF5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: SOSEKI proteins (SOK1-5) locally interpret global polarity cues and can influence cell division orientation to coordinate cell polarization relative to body axes.
Subcellular location: Cell membrane {ECO:0000269|PubMed:30737509}; Peripheral membrane protein {ECO:0000269|PubMed:30737509}; Cytoplasmic side {ECO:0000269|PubMed:30737509}. Note=SOSEKI proteins integrate apical-basal and radial organismal axes to localize to polar cell edges. {ECO:0000269|PubMed:30737509}.
Interaction partners:
- Transcription factor PRE3
Sequence:
MSSRVFRATPDNNYLVPRRSKDQQDTSPDRNRIWSEPRLKPVVNRKVPVVYYLCRNGQLDHPHFIEVTLSSHDGLYLKDVINRLNDLRGKGMASLYSWSSKRSYKNGFVWHDLSEDDFIFPVQGQEYVLKGSEVLDSCLISNPRSLLETSSFRDPRSLNPDKNSGDDIPAVINRRRNQSWSSIDLSEYKVYKATESSAESTQRLAADASTQTDDRRRRRRPAKEEIEEVKSPASYENQSTELSRDEISPPPSDSSPETLENLIKADGRLILRPSESSTDHRTVESLSSGRMRASAVLMQLISCGTMSFKECGPVLLKDQGLALNGRSGCTITRGAEDNGEERVDKELKSFGRVQLEDKEYFSGSLIETKKELVPALKRSSSYNADRCSRMGPTTEKDEEEAVRAKCIPRKPKPVAKRNNGGQQ
Protein: Bifunctional polymyxin resistance protein ArnA (Polymyxin resistance protein PmrI) [Includes: UDP-4-amino-4-deoxy-L-arabinose formyltransferase (EC 2.1.2.13) (ArnAFT) (UDP-L-Ara4N formyltransferase); UDP-glucuronic acid oxidase, UDP-4-keto-hexauronic acid decarboxylating (EC 1.1.1.305) (ArnADH) (UDP-GlcUA decarboxylase) (UDP-glucuronic acid dehydrogenase)] (P77398)
Organism: Escherichia coli (strain K12)
Function: Bifunctional enzyme that catalyzes the oxidative decarboxylation of UDP-glucuronic acid (UDP-GlcUA) to UDP-4-keto-arabinose (UDP-Ara4O) and the addition of a formyl group to UDP-4-amino-4-deoxy-L-arabinose (UDP-L-Ara4N) to form UDP-L-4-formamido-arabinose (UDP-L-Ara4FN). The modified arabinose is attached to lipid A and is required for resistance to polymyxin and cationic antimicrobial peptides.
Interaction partners:
- Undecaprenyl-phosphate 4-deoxy-4-formamido-L-arabinose transferase
- UDP-4-amino-4-deoxy-L-arabinose--oxoglutarate aminotransferase aminotransferase)
- Probable 4-deoxy-4-formamido-L-arabinose-phosphoundecaprenol deformylase ArnD
- Undecaprenyl phosphate-alpha-4-amino-4-deoxy-L-arabinose arabinosyl transferase
- Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnE
- UDP-glucose 6-dehydrogenase
- Probable 4-amino-4-deoxy-L-arabinose-phosphoundecaprenol flippase subunit ArnF
- Ribosomal RNA small subunit methyltransferase B
- Small ribosomal subunit protein uS19
- Small ribosomal subunit protein uS3
Sequence:
MKTVVFAYHDMGCLGIEALLAAGYEISAIFTHTDNPGEKAFYGSVARLAAERGIPVYAPDNVNHPLWVERIAQLSPDVIFSFYYRHLIYDEILQLAPAGAFNLHGSLLPKYRGRAPLNWVLVNGETETGVTLHRMVKRADAGAIVAQLRIAIAPDDIAITLHHKLCHAARQLLEQTLPAIKHGNILEIAQRENEATCFGRRTPDDSFLEWHKPASVLHNMVRAVADPWPGAFSYVGNQKFTVWSSRVHPHASKAQPGSVISVAPLLIACGDGALEIVTGQAGDGITMQGSQLAQTLGLVQGSRLNSQPACTARRRTRVLILGVNGFIGNHLTERLLREDHYEVYGLDIGSDAISRFLNHPHFHFVEGDISIHSEWIEYHVKKCDVVLPLVAIATPIEYTRNPLRVFELDFEENLRIIRYCVKYRKRIIFPSTSEVYGMCSDKYFDEDHSNLIVGPVNKPRWIYSVSKQLLDRVIWAYGEKEGLQFTLFRPFNWMGPRLDNLNAARIGSSRAITQLILNLVEGSPIKLIDGGKQKRCFTDIRDGIEALYRIIENAGNRCDGEIINIGNPENEASIEELGEMLLASFEKHPLRHHFPPFAGFRVVESSSYYGKGYQDVEHRKPSIRNAHRCLDWEPKIDMQETIDETLDFFLRTVDLTDKPS
Protein: Vesicle-fusing ATPase (EC 3.6.4.6) (B4DGR3)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU367045}.
Interaction partners:
Sequence:
MAGRSMQAARCPTDELSLTNCAVVNEKDFQSGQHVIVRTSPNHRYTFTLKTHPSVVPGSIAFSLPQRKWAGLSIGQEIEVSLYTFDKAKQCIGTMTIEIDFLQKKSIDSNPYDTDKMAAEFIQQFNNQAFSVGLVVGNSQVAFEKAENSSLNLIGKAKTKENRQSIINPDWNFEKMGIGGLDKEFSDIFRRAFASRVFPPEIVEQMGCKHVKGILLYGPPGCGKTLLARQIGKMLNAREPKVVNGPEILNKYVGESEANIRKLFADAEEEQRRLGANSGLHIIIFDEIDAICKQRGSMAGSTGVHDTVVNQLLSKIDGVEQLNNILVIGMTNRPDLIDEALLRPGRLEVKMEIGLPDEKGRLQILHIHTARMRGHQLLSADVDIKELAVETKNFSGAELEGLVRAAQSTAMNRHIKASTKVEVDMEKAESLQVTRGDFLASLENDIKPAFGTNQEDYASYIMNGIIKWGDPVTRVLDDGELLVQQTKNSDRTPLVSVLLEGPPHSGKTALAAKIAEESNFPFIKICSPDKMIGFSETAKCQAMKKIFDDAYKSQLSCVVVDDIERLLDCVPIGPRFSNLVLQALLVLLKKAPPQGRKLLIIGTTSRKDVLQEMEMLNAFSTTIHVPNIATGEQLLEALELLGNFKDKERTTIAQQVKGKKVWIGIKKLLMLIEMSLQMDPEYRVRKFLALLREEGASPLDFD
Protein: Fe2OG dioxygenase domain-containing protein (Q54PP0)
Organism: Dictyostelium discoideum (Social amoeba)
Interaction partners:
Sequence:
MNRELKAVDVLECIPNNKLFAITIDDVFTEEECKEWIDLTEKTGYEPALVNIGYGQQQLMTDIRNNDRCIIDSVEMADKIYQRVKKFIPHTFNQKWEVVSLNERLRFLRYYVGQEFKKHQDGNYKRNNGETSFITLQLYLNNVEEGGSTKFFLKSGQNEIEIIPKPGKVLLFQHNIWHQGSPVTKGVKYVIRTDVILNIKIKKIKNLLQNFTPKHFSFFFFFFFLNFFFFFFFFFFFKIFIWFFFFFLNEKY
Protein: Serine/threonine-protein kinase LMTK2 (EC 2.7.11.1) (Apoptosis-associated tyrosine kinase 2) (Brain-enriched kinase) (hBREK) (CDK5/p35-regulated kinase) (CPRK) (Kinase/phosphatase/inhibitor 2) (Lemur tyrosine kinase 2) (Serine/threonine-protein kinase KPI-2) (Q8IWU2)
Organism: Homo sapiens (Human)
Function: Phosphorylates PPP1C, phosphorylase b and CFTR.
Subcellular location: Membrane {ECO:0000269|PubMed:23114966}; Multi-pass membrane protein {ECO:0000269|PubMed:23114966}.
Interaction partners:
- Serine/threonine-protein phosphatase PP1-gamma catalytic subunit
- Protein phosphatase inhibitor 2
- Unconventional myosin-VI
- Beta-microseminoprotein
Sequence:
MPGPPALRRRLLLLLLVLLIAGSAGAAPLPQTGAGEAPPAAEVSSSFVILCVCSLIILIVLIANCVSCCKDPEIDFKEFEDNFDDEIDFTPPAEDTPSVQSPAEVFTLSVPNISLPAPSQFQPSVEGLKSQVARHSLNYIQEIGNGWFGKVLLGEIYTGTSVARVIVKELKASANPKEQDTFLKNGEPYYILQHPNILQCVGQCVEAIPYLLVFEFCDLGDLKAYLRSEQEHMRGDSQTMLLQRMACEVAAGLAAMHKLHFLHSDLALRNCFLTSDLNVKVGDYGIGFSRYKEDYIETDDKKVFPLRWTAPELVTSFQDRLLTADQTKYSNIWSLGVTLWELFDNAAQPYSNLSNLDVLNQVIRERDTKLPKPQLEQPYSDRWYEVLQFCWLSPEKRPAAEDVHRLLTYLRLQSQRDSEVDFEQQWNALKPNTNSRDSSNNAAFPILDHFARDRLGREMEEVLTVTETSQGLSFEYVWEAAKHDHFDERSRGHLDEGLSYTSIFYPVEVFESSLSDPGPGKQDDSGQDVPLRVPGVVPVFDAHNLSVGSDYYIQLEEKSGSNLELDYPPALLTTDMDNPERTGPELSQLTALRSVELEESSTDEDFFQSSTDPKDSSLPGDLHVTSGPESPFNNIFNDVDKSEDLPSHQKIFDLMELNGVQADFKPATLSSSLDNPKESVITGHFEKEKPRKIFDSEPLCLSDNLMHQDNFDPLNVQELSENFLFLQEKNLLKGSLSSKEHINDLQTELKNAGFTEAMLETSCRNSLDTELQFAENKPGLSLLQENVSTKGDDTDVMLTGDTLSTSLQSSPEVQVPPTSFETEETPRRVPPDSLPTQGETQPTCLDVIVPEDCLHQDISPDAVTVPVEILSTDARTHSLDNRSQDSPGESEETLRLTESDSVLADDILASRVSVGSSLPELGQELHNKPFSEDHHSHRRLEKNLEAVETLNQLNSKDAAKEAGLVSALSSDSTSQDSLLEDSLSAPFPASEPSLETPDSLESVDVHEALLDSLGSHTPQKLVPPDKPADSGYETENLESPEWTLHPAPEGTADSEPATTGDGGHSGLPPNPVIVISDAGDGHRGTEVTPETFTAGSQGSYRDSAYFSDNDSEPEKRSEEVPGTSPSALVLVQEQPLPEPVLPEQSPAAQDSCLEARKSQPDESCLSALHNSSDLELRATPEPAQTGVPQQVHPTEDEASSPWSVLNAELSSGDDFETQDDRPCTLASTGTNTNELLAYTNSALDKSLSSHSEGPKLKEPDIEGKYLGKLGVSGMLDLSEDGMDADEEDENSDDSDEDLRAFNLHSLSSESEDETEHPVPIILSNEDGRHLRSLLKPTAANAPDPLPEDWKKEKKAVTFFDDVTVYLFDQETPTKELGPCGGEACGPDLSGPAPASGSPYLSRCINSESSTDEEGGGFEWDDDFSPDPFMSKTTSNLLSSKPSLQTSKYFSPPPPARSTEQSWPHSAPYSRFSISPANIASFSLTHLTDSDIEQGGSSEDGEKD
Protein: FMR1 autosomal homolog 1 (E7EU85)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000256|ARBA:ARBA00004331}.
Interaction partners:
Sequence:
MMKGEFYVIEYAACDATYNEIVTFERLRPVNQNKTVKKNTFFKCTVDVPEDLREACANENAHKDFKKAVGACRIFYHPETTQLMILSASEATVKRVNILSDMHLRSIRTKLMLMSRNEEATKHLECTKQLAAAFHEEFVVREDLMGLAIGTHGSNIQQARKVPGVTAIELDEDTGTFRIYGESADAVKKARGFLEFVEDFIQVPRNLVGKVIGKNGKVIQEIVDKSGVVRVRIEGDNENKLPREDGMVPFVFVGTKESIGNVQVLLEYHIAYLKEVEQLRMERLQIDEQLRQIGSRSYSGRGRGRRGPNYTSGYGTNSELSNPSETESERKDELSDWSLAGEDDRDSRHQRDSRRRPGGRGRSVSGGRGRGGPRGGKSSISSVLKDPDSNPYSLLDNTESDQTADTDASESHHSTNRRRRSRRRRTDEDAVLMDGMTESDTASVNENGLGKRCD
Protein: Peroxisomal isocitrate dehydrogenase [NADP] (EC 1.1.1.42) (Q9SLK0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: May be involved in response to oxidative stresses.
Subcellular location: Peroxisome {ECO:0000269|PubMed:17951448}.
Interaction partners:
- Aconitate hydratase 3, mitochondrial
- Aconitate hydratase 2, mitochondrial
- Aconitate hydratase 1
- 2-oxoglutarate dehydrogenase, mitochondrial
- 2-oxoglutarate dehydrogenase, mitochondrial
- Putative isocitrate dehydrogenase subunit-like 4
- Isocitrate dehydrogenase regulatory subunit 3, mitochondrial
- Isocitrate dehydrogenase catalytic subunit 5, mitochondrial
- Isocitrate dehydrogenase catalytic subunit 6, mitochondrial
- Isocitrate dehydrogenase regulatory subunit 1, mitochondrial
Sequence:
MEFEKIKVINPVVEMDGDEMTRVIWKFIKDKLIFPFLELDIKYFDLGLPNRDFTDDKVTIETAEATLKYNVAIKCATITPDEARVREFGLKKMWRSPNGTIRNILNGTVFREPIICRNIPRLVPGWTKPICIGRHAFGDQYRATDLIVNEPGKLKLVFEPSGSSQKTEFEVFNFTGGGVALAMYNTDESIRAFAESSMYTAYQKKWPLYLSTKNTILKIYDGRFKDIFQEVYEANWRSKYEAAGIWYEHRLIDDMVAYAMKSEGGYVWACKNYDGDVQSDFLAQGYGSLGMMTSVLVCPDGKTIEAEAAHGTVTRHYRVHQKGGETSTNSIASIFAWSRGLAHRAKLDSNAALLSYTEKLEAACMGTVESGKMTKDLALLIHGAKVRRDQYVNTEEFIDAVAWELKRRLLGNNSRL
Protein: Serine rich endogenous peptide 8 (AtSCOOP8) (Phytocytokine SCOOP8) (Precursor of serine rich endogenous peptide phytocytokine 8) (Q8GWN6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Brassicaceae-specific phytocytokine (plant endogenous peptide released into the apoplast) perceived by MIK2 in a BAK1/SERK3 and SERK4 coreceptors-dependent manner, that modulates various physiological and antimicrobial processes including growth prevention and reactive oxygen species (ROS) response regulation. Inhibits root growth.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:B3H7I1}. Secreted, extracellular space, apoplast {ECO:0000250|UniProtKB:B3H7I1}. Note=The precursor of SCOOP8, PROSCOOP8, accumulates at the plasma membrane and is proteolytically cleaved to release the SCOOP8 in the apoplasm. {ECO:0000250|UniProtKB:B3H7I1}.
Interaction partners:
Sequence:
MEEKSASQLGLVVFLLLFLLVPTHTESSLPSQQESLPVIGSSRRLMSTYKTNSNIDFEGSISGQAGGGQQNP
Protein: ESSS subunit of NADH:ubiquinone oxidoreductase (Complex I) protein (Expressed protein) (Q8L3S7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- NADH dehydrogenase 1 beta subcomplex subunit 7
- NADH dehydrogenase 1 beta subcomplex subunit 10-A
- NADH dehydrogenase 1 beta subcomplex subunit 2
- Excitatory amino acid transporter
- Probable NADH dehydrogenase 1 alpha subcomplex subunit 5
- Uncharacterized protein At2g27730
- NADH dehydrogenase iron-sulfur protein 1, mitochondrial
- NADH dehydrogenase 1 alpha subcomplex subunit 1
- NADH dehydrogenase 1 alpha subcomplex subunit 8-B
- NADH dehydrogenase flavoprotein 1, mitochondrial
Sequence:
MASTKPLIVAAKTLRNRIHFRSGSTSTGPSRWATPGHEERPKGYFMNRTPPPPGQSRKWEDWELPCYITSFLTIVILGVGLNAKPDLSIETWAHQKALERLEMEKLASAGDSSG
Protein: Glycosyl hydrolase, putative (Q4WXA7)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Interaction partners:
Sequence:
MGVLRLRVDGQTFRDPDNREITLRGINVAGEAKYPKKPDIPSYVSDGFFDADNVSFVGRPFSLDDAHTHFSRLRKWGYNTIRYVFTWEAIEHEGPGKYDDEWISFTIEVLRIAKQYGFYVFLDPHQDVWSRLSGGSGAPAWTLYAAGFDPRGFKKTEAALVQNTFDDPAEFPKMIWSTNYTRLVSQTMFTLFYGGRDFAPKAIIDGINIQDYLQGHFIAACRYFAQKIHEAGDIENEVVIGWESMNEPNRGLIGVQDISVIPPEQQLQLGTSPTAFQGMLTGSGRACEESTWAFGGFGPYQTGRELVDPEGETAWLPADYDDTRYGWVRDPGWKLGECLWAQHGVWDPSSDKLLRKDYFAKNPQTGEPLNYDKFTNTYFMEHYRAYRDALRSVWPEAIIFCQPPVMEVPPDLKGTVDDDPNMVHAVHYYDGITLLTKHWNRLYNVDVIGVLRGKYLTPAFAVKIGETAIRNCLRDQLKFLRDESLRYMGTHPLIFTEIGIPFDMDDRHAYKTGDYSGQVSAMDANHFAIEGSTANGFTLWLYTTSNNHEWGDNWNGEDLSIYSVDDLELPSGKLLAFENESQRDPQSPAYSESQRNTESYRVGPRDLKQALQAPSISSEISQSSQDKLGFRAAEAWVRPSPIITNGQILQYGFDLKSCVFSMRLLGEKKGLGQEAATEIFLPDFHFPDTHTVVAVSAGEWTIDYPEIHSVKFQRLRWWHPEGDHNIKIQGVKRKPGDPTVSGEELSYLEQCQGGGCSVM
Protein: Flotillin-like protein 3 (D2XNR0)
Organism: Medicago truncatula (Barrel medic) (Medicago tribuloides)
Function: May act as a scaffolding protein within caveolar membranes, functionally participating in formation of caveolae or caveolae-like vesicles (By similarity). May be involved in nodule formation.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. Membrane, caveola {ECO:0000250}.
Interaction partners:
Sequence:
MYRVAKASEYLAITGAGIDDIKLQKKAWIFPGQSCTVFDLSPVNYTFEVQAMSAEKLPFVLPAVFTIGPRVDDQESLLKYAKLISPHDRHSNHVNELVQGIIEGETRVLAASMTMEEVFRGTKQFKQEVFDKVQLELNQFGLLIYNANVKQLVDVPGHEYFSYLGQKTQMEAANQAKVDVAEAKMKGEIGSKLRVGQTLQNAAKIDAETKVIAMQRAGESEKQGIKVRTEVKVFENQREAEVAEANSELAKKKAAWTKAAQVAEVEAKKAVALREAELQGEVEKMNALTTTEKLKADLLSKASVQYETKVQEANWELYKKQKEAEAILFEKKAEAEAQKALADSTFYARKQEAEAELYAKKKEAEGIVTLGNAQGAYVSTLLNALGNNYTAVRDYLMINGGMFQEIAKINAEAVRGLEPKISIWTNGGDNSGGEGAMKEVAGVYKMLPPLFKTVHEQTGMLPPAWMGSLSDKSS
Protein: DNA-directed DNA polymerase (EC 2.7.7.7) (C1F6L4)
Organism: Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 / NCIMB 13165 / 161)
Interaction partners:
- UmuC domain-containing protein
- Beta sliding clamp
- DNA polymerase III subunit delta
- DNA polymerase III, delta prime subunit
- Uncharacterized protein
- Protein RecA
- DNA polymerase III subunit gamma/tau
Sequence:
MTERYVELHAASAFSFLEGGSNPESLTERAAALQMPAMALLDRNGLYGAARFHTSAQRHGVQANIGAEVAVPEFGARLTPPAWLPHLWPTEPVRLPLLCATRKGYQNLCQLISRYKLREPSKQEGAARVNELEQFAEGLICLTGGSEGPLAAALMQGGEAAGQKLLHRLTAIFGHQHVYVELQRHHDREQEWRNQAALRIAHKLRLPMVATNGVRYASERDREVLDLFTAIRHHTPLDRAGHLLSANSLRHLRSAREMAALFRDIPAAIENTIELSSRLAFQLSDLGYEFPRYPVPAGDCMDSFLRKRVQEGVALRYNSRHNHDLLARVHKQVERELSLIARLGFAGYFLIVWDIIRFCKQHDILVQGRGSAANSVVCYALEITAVDPVGMDLLFERFLNENRGEWPDIDLDLPSEEKREQAIQYVYQRYGELGAAMTANVITYRGKSAAREVGKALGFDADALQRLSGLVANFEWKGPTDSLAHSFRHAGFDPAQPRIARYLELCTRIQDMPRHLGQHSGGMVICQGQLNQVVPVERASMPGRTVVQWDKEDCADMGIIKVDLLGLGMMAVLKDCVELIPRHYGERIDLAQLPQDEAVYRTLQRADTVGMFQVESRAQMASLPRNMPAKFYDLVVQVAIIRPGPIVGKMMHPYMRRRQGKEPVTYPHPSLEPVLQRTLGVPLFQEQLLRIAMTVANFSGTEAEELRRAVGMRRSWERMKNLESKLRAGMAANGIAPATQEQIIQQISSFALYGFPESHAASFALIAYASAYLKVKYLAAFTCALLNNQPMGFYMPAVIVKDAQRHGLRVKPIDIQISAWPCTLEQEPDDSLSLRLGLGYARGLRQRTAEATLHARQENGPFSSAENLVARVPALSRKELALLARIGALNSLDQVAHRRDALWQIERAGKPEGPLFAQSNEALREQDVALPLMPMTTEERLVADYFGTGLTVGKHPMSYRRQELDHAGILTASALQQFQDGKLVRVAGCVIARQRPGTAKGFVFLSMEDETGIANIIVTPDLFERERLIVTRSKFLLVEGPLQNQDGVIHVKAQRLRSLSGQLLNLRSHDFH
Protein: GEO13347p1 (Seminal fluid protein 87B) (B4ZJA7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Seminal fluid protein 23F
- Seminal fluid protein 24Bb
- Seminal fluid protein 60F, isoform A
- Accessory gland-specific peptide 57Da
- Accessory gland-specific peptide 57Db
- Accessory gland-specific peptide 57Dc
- Seminal fluid protein 96F
- ACP24A4
- FI11009p
- Ejaculatory bulb-specific protein 2
Sequence:
MRFVFVFVLLSVLALSLVSAKEQSKTSSSPGRNNVGATVNPRLRPKRNILFNRPTIRGQVQRYIYGYPYHNGVPTYYKYPYYGYFRI
Protein: Sodium-dependent phosphate transport protein 1 (Na(+)/PI cotransporter 1) (Na/Pi-4) (Renal Na(+)-dependent phosphate cotransporter 1) (Renal sodium-dependent phosphate transport protein 1) (Renal sodium-phosphate transport protein 1) (Sodium/phosphate cotransporter 1) (Solute carrier family 17 member 1) (Q14916)
Organism: Homo sapiens (Human)
Function: Important for the resorption of phosphate by the kidney. May be involved in actively transporting phosphate into cells via Na(+) cotransport in the renal brush border membrane. Plays a role in urate transport in the kidney.
Subcellular location: Apical cell membrane {ECO:0000269|PubMed:25252215, ECO:0000269|PubMed:27906618}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Sodium-dependent phosphate transport protein 2A
- Solute carrier family 22 member 11
- Solute carrier family 22 member 12
- Sodium-dependent phosphate transport protein 2B
- Na
- Solute carrier family 2, facilitated glucose transporter member 9
- MFS-type transporter SLC18B1
- Broad substrate specificity ATP-binding cassette transporter ABCG2
- Chromaffin granule amine transporter
- Sodium-dependent phosphate transport protein 2C
Sequence:
MQMDNRLPPKKVPGFCSFRYGLSFLVHCCNVIITAQRACLNLTMVVMVNSTDPHGLPNTSTKKLLDNIKNPMYNWSPDIQGIILSSTSYGVIIIQVPVGYFSGIYSTKKMIGFALCLSSVLSLLIPPAAGIGVAWVVVCRAVQGAAQGIVATAQFEIYVKWAPPLERGRLTSMSTSGFLLGPFIVLLVTGVICESLGWPMVFYIFGACGCAVCLLWFVLFYDDPKDHPCISISEKEYITSSLVQQVSSSRQSLPIKAILKSLPVWAISTGSFTFFWSHNIMTLYTPMFINSMLHVNIKENGFLSSLPYLFAWICGNLAGQLSDFFLTRNILSVIAVRKLFTAAGFLLPAIFGVCLPYLSSTFYSIVIFLILAGATGSFCLGGVFINGLDIAPRYFGFIKACSTLTGMIGGLIASTLTGLILKQDPESAWFKTFILMAAINVTGLIFYLIVATAEIQDWAKEKQHTRL
Protein: Muskelin-like protein (Q8WSN1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MSSSSTSSPTDNSSHGSVALSSALNPSLNPVSGTNTSSQKPFSLSERLNFEIYRYSSYSPNYLPENVLVDCPNDQTSRWSAYTNSPPQFLTLKLRRPAIVKKIKFGKFEKSHVCNIKKFRVYGGLDDEHMVLLLEGGLKNDNVPEVFNLRCLTEDGSENLPILYLKIVPLLSWGPSFNFSIWYVELHGQDDPMYTSARMKNYKLARGGDHQAVSEALPPAGYLSAFGALQEQTNVQLEHPLISELHKCLVLQGDFEKAERFIVECIDEGLMDEYLHKQDYKHSWHMKHTESDIKPGNRGGHQLVVDAKRRLIYLYGGWDGYQDLSDLWVFNIEDDQWTLLCERSELSNGPTPRSCHKMVFDPISENVFMLGRYLDNSIRTSDYIKSDFYLYDTRAGNWMQICDDTSQVGGPQLVYDHQMCMDTDKRTIYVFGGKILTHSQCQCHGSDRTRYSGLFSYHIATNTWAQILVDCHHASASLADVMSIKSRITHCMVFHNKHRKLYIYGGQRGKEDLDEFLSYDVDTQAISVLNKEHPHHGTIAGNEAKFEPSSGYTLRATIDCERDEIYIFSSLSKVKDRRDIQHIDASNSFWVYSLRNHKWSRIYYCRHSGQDANSINNMNILGATEGDGTLEPCPRYAHQLVYDDVTNTHYLFGGNPGICQQQQLRLDDFWLLCLEKPKREEILKHCRFLVRKLRYEEMTRQDPLKAMQYLRHHIADVIDHSDAEQLNNFHKLASLLFKNHDGNLDRECNTPALCADADDLETDSDVSAKIKEELADGPATENLSLESNESMISSGISETASSPSSSSCTKRARTDCTPELKNKRAFLFNKLVQLMPPSMVQPERNLSDFVVM