wanglab/gogpt-training-data huggingface dataset:
Protein: High-affinity iron permease (A0A1D8PFV0)
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:
- Ferroxidase
- Ferroxidase
- Fet31p
- Siderophore transporter
- Fet99p
- Ferric/cupric reductase transmembrane component 1
- Fth1p
- Cu
- Cfl2p
- Fth2p
Sequence:
MVDVFNVQIFFIVFRESLEAIIVVSVLLAFVKQSMGGSSDPQLKKRLYRQIWLGAGLGVLVCLIIGCAFIGAFYGLGKDIWGNSEDLWEGIFCIIATVLITAMGIPMLRINKMKEKWRVKLAQALIKSPTNKKDRFKLGYLGKKYALFILPFITCLREGLEAVVFVGGVGLNSPATSFPIPVIVGLIAGIVVGALLYYFGSSMSMQIFLIISTCILYLIAAGLFSRGIWYFETNTYNKKTGGDASENGSGPGTYDISKSVWHVNCCNPETDNGWDIFNAILGWQNSATYGSVISYNIYWLFIICVLLLMVYEEKHGHLPFTKNLTLVQLNPMYHIKGKKKLELNKAEKDELFTKLQQQNFGQAAEVDETSSNKLIESKENK
Protein: Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 40 kDa form (EC 2.3.1.164) (Isopenicillin-N N-acyltransferase) [Cleaved into: Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 11 kDa subunit; Acyl-coenzyme A:6-aminopenicillanic-acid-acyltransferase 29 kDa subunit] (P21133)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Nonribosomal peptide synthetase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic. AatA catalyzes the exchange of the alpha-aminoadipyl side chain of isopenicillin N for phenylacetic acid to yield penicillin. This step occurs in the peroxisomal matrix and the penM and paaT transporters are involved in the isopenicillin N and phenylacetic acid import into the peroxisome, respectively (By similarity). The penicillin biosynthesis occurs via 3 enzymatic steps, the first corresponding to the production of the tripeptide N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine (LLD-ACV or ACV) by the NRPS acvA. The tripeptide ACV is then cyclized to isopenicillin N (IPN) by the isopenicillin N synthase ipnA that forms the beta-lactam nucleus. Finally, the alpha-aminoadipyl side chain is exchanged for phenylacetic acid by the isopenicillin N acyltransferase penDE to yield penicillin in the peroxisomal matrix (By similarity).
Subcellular location: Peroxisome matrix {ECO:0000250|UniProtKB:P15802}. Note=The unprocessed preprotein is translocated inside peroxisomes and regulates its self-processing. {ECO:0000250|UniProtKB:P15802}.
Interaction partners:
- Acetylglutamate kinase
- Isopenicillin N synthase
- Acyl-CoA:6-aminopenicillanic-acid-acyltransferase, putative
- N-
- argininosuccinate lyase
- Ornithine carbamoyltransferase, mitochondrial
- Arginine biosynthesis bifunctional protein ArgJ
- Arginase
- Hypothetical arginase family protein
- Argininosuccinate synthase
Sequence:
MLHVTCQGTPSEIGYHHGSAAKGEIAKAIDFATGLIHGKTKKTQAELEQLLRELEQVMKQRWPRYYEEICGIAKGAEREVSEIVMLNTRTEFAYGLVEARDGCTTVYCKTPNGALQGQNWDFFTATKENLIQLTICQPGLPTIKMITEAGIIGKVGFNSAGVAVNYNALHLHGLRPTGLPSHLALRMALESTSPSEAYEKIVSQGGMAASAFIMVGNAHEAYGLEFSPISLCKQVADTNGRIVHTNHCLLNHGPSAQELNPLPDSWSRHGRMEHLLSGFDGTKEAFAKLWEDEDNYPLSICRAYKEGKSRGSTLFNIVFDHVGRKATVRLGRPNNPDETFVMTFSNLDTKSAIQANI
Protein: Acyl-CoA Delta(11) desaturase (EC 1.14.19.5) (Acyl-CoA Delta-11 desaturase) (Delta(11)-desaturase) (Acyl-CoA Z/E11 desaturase) (Q8ISS3)
Organism: Choristoneura rosaceana (Oblique banded leafroller)
Function: Catalyzes the formation of Delta(11) fatty acyl precursors in the pheromone gland, with a preference for myristic acid.
Subcellular location: Membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MAPNVEDMESDLPESEEKLEKLVAPQAAPRKYQIIYTNLLTFGYWHIAGLYGLYLCFTSAKWQTIILALILNEMAILGITAGAHRLWAHRSYKATVPLQIILIIFNSLSFQNSAIHWIRDHRMHHKYSDTDGDPHNASRGFFYSHVGWLLVKKHPEVKKRAKTIDMSDIYSNPILRFQKKYAIPFIGMICFVLPTIIPMYFWGETLSNAWHITMLRYVFSLNSIFLVNSAAHLYGYRPYDKNILPAENKMTFIACLGENFHNYHHVFPWDYRASELGNIGMNWTAKFIDFFAWIGWAYDLKTASDENIKSRMKRTGDGTDVSGQKYSCESSEVLQ
Protein: Spanin, outer lipoprotein subunit (o-spanin) (Lysis protein Rz1) (Outer membrane lipoprotein Rz1) (Q37935)
Organism: Escherichia phage lambda (Bacteriophage lambda)
Function: Component of the spanin complex that disrupts the host outer membrane and participates in cell lysis during virus exit. The spanin complex conducts the final step in host lysis by disrupting the outer membrane after holin and endolysin action have permeabilized the inner membrane and degraded the host peptidoglycans. Host outer membrane disruption due to local fusion between the inner and outer membrane performed by the spanin complex.
Subcellular location: Host cell outer membrane {ECO:0000269|PubMed:18713319, ECO:0000269|PubMed:23387988}; Lipid-anchor {ECO:0000269|PubMed:18713319, ECO:0000269|PubMed:23387988}; Periplasmic side {ECO:0000269|PubMed:18713319, ECO:0000269|PubMed:23387988}.
Interaction partners:
Sequence:
MLKLKMMLCVMMLPLVVVGCTSKQSVSQCVKPPPPPAWIMQPPPDWQTPLNGIISPSERG
Protein: Protein TIFY 9 (Jasmonate ZIM domain-containing protein 10) (Protein JASMONATE-ASSOCIATED 1) (Protein JAZ10) (Q93ZM9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Repressor of jasmonate (JA) responses that lacks the entire Jas domain and possesses severe JA insensitivity and resistance to JA-induced degradation. Acts as an endogenous repressor of JA signal output in JA-stimulated cells. Modulator of JA-controlled growth inhibition in response to wounding.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00768, ECO:0000269|PubMed:17675405, ECO:0000269|PubMed:19151223}. Note=Isoform 1, isoform 2 and isoform 3 are localized to the nucleus. {ECO:0000269|PubMed:19151223}.
Interaction partners:
- Transcription factor MYC2
- Transcription factor MYC3
- Coronatine-insensitive protein 1
- AFP homolog 2
- Protein TIFY 5A
- Protein TIFY 11A
- Protein TIFY 7
- Protein TIFY 6B
- Protein TIFY 5B
- Transcription factor MYC4
Sequence:
MSKATIELDFLGLEKKQTNNAPKPKFQKFLDRRRSFRDIQGAISKIDPEIIKSLLASTGNNSDSSAKSRSVPSTPREDQPQIPISPVHASLARSSTELVSGTVPMTIFYNGSVSVFQVSRNKAGEIMKVANEAASKKDESSMETDLSVILPTTLRPKLFGQNLEGDLPIARRKSLQRFLEKRKERLVSTSPYYPTSA
Protein: Interleukin-1 (A3DTN3)
Organism: Anser anser (Domestic goose)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Lysosome {ECO:0000256|ARBA:ARBA00004371}. Secreted, extracellular exosome {ECO:0000256|ARBA:ARBA00004550}.
Interaction partners:
Sequence:
MAFVPDLDVLESSSLSEETFYGPSCLCLQKKPRLDSEHTTVDVQVTVRKGRGARSFRRAAVLVVAMTKLLRRPRSRDFADSDLSALLEEVFEPVTFQRLESSYAGAPAFRYTRSQSFDIFDINQKCFVLESPTQLVALHLQGPSSSQKVRLNIALYRPRGPRGSAGTGQMPVALGIKGYKLYMSCVMSGTEPTLQLEEADVMRDIDSVELTRFIFYRLDSPTECTTRFESAAFPGWFICTSLQPRQPVGITNQPDQVNIATYKLSGR
Protein: 6-hydroxycyclohex-1-ene-1-carbonyl-CoA dehydrogenase (EC 1.1.1.368) (O87871)
Organism: Thauera aromatica
Function: Involved in the central benzoyl-CoA catabolism. Catalyzes the oxidation of 6-hydroxycyclohex-1-ene-1-carbonyl-CoA to 6-oxocyclohex-1-ene-1-carbonyl-CoA. It is specific to NAD and is also able to oxidize 2-hydroxycyclohexane-1-carbonyl-CoA.
Interaction partners:
Sequence:
MAAKSSVSSWRSEMSSNPHRWMMTSPGAPMVRAEFEIGELSADQVVVAVAGCGVCHTDLGYYYDSVRTNHALPLALGHEISGRVVQAGANAAQWLGRAVIVPAVMPCGTCELCTSGHGTICRDQVMPGNDIQGGFASHVVVPARGLCPVDEARLAAAGLQLADVSVVADAVTTPYQAVLQAGVEPGDVAVVIGVGGVGGYAVQIANAFGASVVAIDVDPAKLEMMSKHGAALTLNAREISGRDLKKAIEAHAKANGLRLTRWKIFECSGTGAGQTSAYGLLTHGATLAVVGFTMDKVEVRLSNLMAFHARALGNWGCLPEYYPAALDLVLDKKIDLASFIERHPLDQIGEVFAAAHAHKLTRRAILTP
Protein: Biosynthetic arginine decarboxylase (ADC) (EC 4.1.1.19) (Q9HUX1)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Catalyzes the biosynthesis of agmatine from arginine.
Interaction partners:
- Agmatine deiminase
- Lysine decarboxylase LdcA
- Polyamine aminopropyltransferase 1
- Arginine--pyruvate transaminase AruH
- Arginine N-succinyltransferase subunit alpha
- Arginine N-succinyltransferase subunit beta
- ornithine decarboxylase
- Argininosuccinate lyase
- Arginine deiminase
Sequence:
MAARRTRKDDGSNWTVADSRGVYGIRHWGAGYFAINDGGNVEVRPQGADSTPIDLYELVGQLREAGLSLPLLVRFPDILQDRVRKLTGAFDANIERLEYQSRYTALYPIKVNQQEAVVENIIATENVSIGLEAGSKPELMAVLALAPKGGTIVCNGYKDREFIKLALMGQKLGHNVFIVIEKESEVQLVIEEAANVGVQPQVGLRVRLSSLASSKWADTGGEKAKFGLSAAQLLSVVERFRQAGLDQGVRLLHFHMGSQIANLADYQHGFKEAIRYYGELRALGLPVDHIDVGGGLGVDYDGTHSRNASSINYDIDDYAGVVVGMLKEFCDAQGLPHPHIFSESGRALTAHHAVLITQVTDVERHNDDVPKIVDLDEQPEIVRWLAELLGPTDAEMVTETYWRATHYIGDAAAQYADGKISLAQKALAEQCYFAICRRLHNQLKARQRSHRQVLDELNDKLADKYICNFSVFQSLPDTWAIGQVLPILPLHRLGEEPDRRAVLQDLTCDSDGKITQYVDEQSIETSLPVHEVKEGEDYLIGVFLVGAYQEILGDMHNLFGDTDSVNVYQRADGGIYHAGIETHDTIEDMLRYVHLSPEELMTLYRDKVAGAKLTARERNQYLDALRLGLTRSAYLS
Protein: ATP-dependent RNA helicase DHX15 (EC 3.6.4.13) (ATP-dependent RNA helicase #46) (DEAH box protein 15) (Splicing factor Prp43) (hPrp43) (O43143)
Organism: Homo sapiens (Human)
Function: RNA helicase involved in mRNA processing and antiviral innate immunity. Pre-mRNA processing factor involved in disassembly of spliceosomes after the release of mature mRNA. In cooperation with TFIP11 seem to be involved in the transition of the U2, U5 and U6 snRNP-containing IL complex to the snRNP-free IS complex leading to efficient debranching and turnover of excised introns. Plays a key role in antiviral innate immunity by promoting both MAVS-dependent signaling and NLRP6 inflammasome. Acts as an RNA virus sensor: recognizes and binds viral double stranded RNA (dsRNA) and activates the MAVS-dependent signaling to produce interferon-beta and interferon lambda-3 (IFNL3). Involved in intestinal antiviral innate immunity together with NLRP6: recognizes and binds viral dsRNA and promotes activation of the NLRP6 inflammasome in intestinal epithelial cells to restrict infection by enteric viruses. The NLRP6 inflammasome acts by promoting maturation and secretion of IL18 in the extracellular milieu. Also involved in antibacterial innate immunity by promoting Wnt-induced antimicrobial protein expression in Paneth cells (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:12458796}. Nucleus, nucleolus {ECO:0000269|PubMed:12458796}.
Interaction partners:
- Splicing factor 45
- Tuftelin-interacting protein 11
- Pre-mRNA-processing factor 17
- SURP and G-patch domain-containing protein 1
- U2 small nuclear ribonucleoprotein A'
- Pre-mRNA-processing factor 19
- 116 kDa U5 small nuclear ribonucleoprotein component
- Cell division cycle 5-like protein
- Small nuclear ribonucleoprotein F
- RNA-binding protein 10
Sequence:
MSKRHRLDLGEDYPSGKKRAGTDGKDRDRDRDREDRSKDRDRERDRGDREREREKEKEKELRASTNAMLISAGLPPLKASHSAHSTHSAHSTHSTHSAHSTHAGHAGHTSLPQCINPFTNLPHTPRYYDILKKRLQLPVWEYKDRFTDILVRHQSFVLVGETGSGKTTQIPQWCVEYMRSLPGPKRGVACTQPRRVAAMSVAQRVADEMDVMLGQEVGYSIRFEDCSSAKTILKYMTDGMLLREAMNDPLLERYGVIILDEAHERTLATDILMGVLKEVVRQRSDLKVIVMSATLDAGKFQIYFDNCPLLTIPGRTHPVEIFYTPEPERDYLEAAIRTVIQIHMCEEEEGDLLLFLTGQEEIDEACKRIKREVDDLGPEVGDIKIIPLYSTLPPQQQQRIFEPPPPKKQNGAIGRKVVVSTNIAETSLTIDGVVFVIDPGFAKQKVYNPRIRVESLLVTAISKASAQQRAGRAGRTRPGKCFRLYTEKAYKTEMQDNTYPEILRSNLGSVVLQLKKLGIDDLVHFDFMDPPAPETLMRALELLNYLAALNDDGDLTELGSMMAEFPLDPQLAKMVIASCDYNCSNEVLSITAMLSVPQCFVRPTEAKKAADEAKMRFAHIDGDHLTLLNVYHAFKQNHESVQWCYDNFINYRSLMSADNVRQQLSRIMDRFNLPRRSTDFTSRDYYINIRKALVTGYFMQVAHLERTGHYLTVKDNQVVQLHPSTVLDHKPEWVLYNEFVLTTKNYIRTCTDIKPEWLVKIAPQYYDMSNFPQCEAKRQLDRIIAKLQSKEYSQY
Protein: Calponin-1 (Basic calponin) (Calponin H1, smooth muscle) (P51911)
Organism: Homo sapiens (Human)
Function: Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity (By similarity).
Interaction partners:
- Myosin-11
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 5
- Calmodulin-like protein 6
- Calmodulin-like protein 4
- Actin, gamma-enteric smooth muscle
- Actin, aortic smooth muscle
- Caldesmon
- Myocardin
Sequence:
MSSAHFNRGPAYGLSAEVKNKLAQKYDHQREQELREWIEGVTGRRIGNNFMDGLKDGIILCEFINKLQPGSVKKINESTQNWHQLENIGNFIKAITKYGVKPHDIFEANDLFENTNHTQVQSTLLALASMAKTKGNKVNVGVKYAEKQERKFEPGKLREGRNIIGLQMGTNKFASQQGMTAYGTRRHLYDPKLGTDQPLDQATISLQMGTNKGASQAGMTAPGTKRQIFEPGLGMEHCDTLNVSLQMGSNKGASQRGMTVYGLPRQVYDPKYCLTPEYPELGEPAHNHHAHNYYNSA
Protein: Proheparin-binding EGF-like growth factor (A9JRW9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}. Secreted, extracellular space {ECO:0000256|ARBA:ARBA00004239}.
Interaction partners:
- Receptor protein-tyrosine kinase.
- Receptor protein-tyrosine kinase.
- Epidermal growth factor receptor precursor.
- Receptor protein-tyrosine kinase.
- Heparin-binding EGF-like growth factor b.
- Matrix metalloproteinase 2.
- Epidermal growth factor.
- Probetacellulin
- Epigen precursor)
Sequence:
MNFLTVLRLFVFTIVAVRGASIPLVFESERPAQTAVIDLLEALSEKRSTVDNKLVEYEEEDEEYYYDDDVEEDEEDEFSGDYGLPIVAFSSQPKDPSAVLNAEKLEGSKRKGLGRKKGKGKGKGKKRNPCLKKYKDFCIHGTCQYFRDLKGPSCICDQGYSGERCHDFSLPVKTNDGGYDRTTALAVVAVVLSSLCLTIIGLLLALRFHKQGAYNVENEEKIKLGAAPHH
Protein: Tumor protein p53 binding protein, 2 (A0A8I6A5P5)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MQPLNLYLVSGPRSQDAGVKRNGVKVPGEHRRKENGVNSPRLDLTLAELQEMASRQQQQIEAQQQMLATKEQRLKFLKQQDQRQQQQAAEQEKLKRLREIAESQEAKLKKVRALKGHVEQKRLSNGKLVEEIEQMNSLFQQKQRELVLAVSKVEELTRQLEMLKNGRIDGHHDNQSAVAELDRLYKELQLRNKLNQEQNAKLQQQRECLNKRNSEVAVMDKRVNELRDRLWKKKAALQQKENLPVSPDGNPPQQAVSAPSRVAAVGPYMQSSTMPRMPSRPELLGKPALPDSSLVMQSAEGPMKIQTLPNMRSGAASQSKGPKAHSASSDWNPSSTDLLPSQGSGSALDQVDEGEIALREKEKKVRPFSMFDTVDQCAPPPSFGTLRKNQSSEDILRDAQTVNKNVAKVPPPVPTKPKQINLPYFGQTAQSSSDVKPDGNPQQLPIAATSMGAKLKPAGPQARVLLSPSAPSGGQDQVLSPASKQESPPAAAVRPFTPQPSKDTFPPAFRKPQTVAASSIYSMYTQHQVPGKNFQQAVQSASTKTHPRGPHFSSVYGKPVIAAAQNPQQHPENIYSCSQGKPGSPEPETEPVSSVHESHENERIPRPLSPTKLLPFLSNPYRNQSDADLEALRKKLSNAPRPLKKRSSITEPEGPNGPNIQKLLYQRTTIAAMETISVPSYPSKSPSSVTVNPESPIEIPNPYLHVEPEKEAGSLVPEPLSPEDMGSASTENSDMPAPPPGLECVSEGVPDNSTTLQDNTEGTNPEAPHLLEVYLEEYPPYPPPPYPSGEPEVSEEDSARMRPPEVTGQVSLPPGKRTNLRKTGSERIAHGMRVKFNPLALLLDSSLEGEFDLVQRIIYEVDDPSLPNDEGITALHNAVCAGHTEIVKFLVQFGVNVNAADSDGWTPLHCAASCNNVQVCKFLVESGAAVFAMTYSDMQTAADKCEEMEEGYTQCSQFLYGVQEKMGIMNKGVIYALWDYQPQHDDELLLKEGDCMAVVRREDEDETEWWWARLNDKEGYVPRNLLGLYPRIKPRQRSLA
Protein: protein-serine/threonine phosphatase (EC 3.1.3.16) (F1LWM1)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Cofilin 2
- Cofilin-1
- Protein phosphatase 3 catalytic subunit alpha
- Serine/threonine-protein phosphatase 2B catalytic subunit beta isoform
- Serine/threonine-protein phosphatase
- Protein phosphatase Slingshot homolog 3
- protein-serine/threonine phosphatase
- Calcineurin subunit B type 1
- Calcineurin subunit B type 2
- LIM domain kinase 2
Sequence:
MDLFFLSDFCVFLRPTRYLCHSGVSSPRYLSESFFMVKGAALFLQQGNSPQGQRSLQHPHKHAGDLPQHLQVMINLLRCEDRIKLAVRLESVWTDRVRYMVVVYTSGRQDTEENILLGVDFSSKESKSCTIGMVLRLWSDTKIHLDGDGGFSVSTAGRMHIFKPVSVQAMWSALQVLHKACEVARRHNYFPGGVALIWATYYESCISSEQSCINEWNAMQDLESTRPDSPALFVDKPTEGERTERLIKAKLRSIMMSQDLENVTSKEIRNELEKQMNCNLKEFKEFIDNEMLLILGQMDKPSLIFDHLYLGSEWNASNLEELQGSGVDYILNVTREIDNFFPGLFAYHNIRVYDEETTDLLAHWNEAYQFINKAKRNHSKCLVHCKMGVSRSASTVIAYAMKEFGWPLEKAFNYVKQKRSITRPNAGFMRQLSEYEGILDASKQRHNKLWRQQPADDTIAEPSEFLPETLDGALDTQLPCLEDATHPGLPRSLPSGGPSLPCCFRRLSDPLLLPHRDGAGGLVHLEDLERDALLEDEAQPVEVRKLVPSSQEGDRLCEKDVKRKLEFGSPKARSGSLPQVEELEKDGSPRPGRWRRASTQLERGLLDQENLNNNNSKRSCPDDFERDAVFGILSKVKPPYTSCADCMYPAAGAPEAFMERHEDPSSSAICTQPTFLPHVTSSPMAHTSNRSRAPERPTSGPANTSPFLLPAGSRKPDVSGSGAGVAPEPPASLPEPSRETSKALQKSLLSKNSHCDKNAANTEAAAKEELSTKKDPKPSKDLRLLFSQEGEKPTANSYLMQHQESIIQLQKAGLVRKHTKELERLKSLPSDSPSTCRDSAASRLEASIPEEGQEPAHPALDSQAGTEEKPVGGASQKSPPPTLLLRLDHTSKDFSKDFLKSACYTPTPSSISSNLTRSSSSDSIHSVRGKPGLVKQRAQEIETRLRLAGLTVSSPLKRSHSLAKLGSLNFSTEDLSSEADTSTIADSQDAKCTLSSFLPEPQAAPRNPSATSKPSGKSAPENLKIPVRVNKS
Protein: Lupus La protein homolog (La autoantigen homolog) (La ribonucleoprotein) (P38656)
Organism: Rattus norvegicus (Rat)
Function: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- RNA-binding protein RO60
Sequence:
MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLETMIKFNRLNRLTTDFNVIVQALSKSKANLMEVSADKTKIRRSPSRPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLDDKGQILNIQMRRTLHKTFKGSIFAVFDSIQSAKKFVDTPGQKYKDTNLLILFKEDYFAKKNEERKQSKVEAKLKAKQEHEGRHKPGSTETRALEGKMGCLLKFSGDLDDQTCREDFHFLFSNHGEIKWIDFVRGAKEGIILFKEKAKDALEKARSANNGNLLLRNKKVTWKVLEGHAEKDAMKKITDDQQESLNKWKSKGGHAARRFKGSHVFTAARRFKGRGKGNRPAYAGAPKGRGQFQGRRTRFDDDDHRRGPVKRGIDGRDREEPASKHKKRENGARDK
Protein: 15-hydroxyprostaglandin dehydrogenase [NAD(+)] (EC 1.1.1.141) (EC 1.1.1.232) (Eicosanoid/docosanoid dehydrogenase [NAD(+)]) (Prostaglandin dehydrogenase 1) (D6RA83)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGIL
Protein: Mitogen-activated protein kinase kinase kinase 7 (EC 2.7.11.25) (P0C8E4)
Organism: Rattus norvegicus (Rat)
Function: Serine/threonine kinase which acts as an essential component of the MAP kinase signal transduction pathway. Plays an important role in the cascades of cellular responses evoked by changes in the environment. Mediates signal transduction of TRAF6, various cytokines including interleukin-1 (IL-1), transforming growth factor-beta (TGFB), TGFB-related factors like BMP2 and BMP4, toll-like receptors (TLR), tumor necrosis factor receptor CD40 and B-cell receptor (BCR). Ceramides are also able to activate MAP3K7/TAK1. Once activated, acts as an upstream activator of the MKK/JNK signal transduction cascade and the p38 MAPK signal transduction cascade through the phosphorylation and activation of several MAP kinase kinases like MAP2K1/MEK1, MAP2K3/MKK3, MAP2K6/MKK6 and MAP2K7/MKK7. These MAP2Ks in turn activate p38 MAPKs, c-jun N-terminal kinases (JNKs) and I-kappa-B kinase complex (IKK). Both p38 MAPK and JNK pathways control the transcription factors activator protein-1 (AP-1), while nuclear factor-kappa B is activated by IKK. MAP3K7 activates also IKBKB and MAPK8/JNK1 in response to TRAF6 signaling and mediates BMP2-induced apoptosis. In osmotic stress signaling, plays a major role in the activation of MAPK8/JNK1, but not that of NF-kappa-B (By similarity). Promotes TRIM5 capsid-specific restriction activity (By similarity). Phosphorylates RIPK1 at 'Ser-321' which positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Note=Although the majority of MAP3K7/TAK1 is found in the cytosol, when complexed with TAB1/MAP3K7IP1 and TAB2/MAP3K7IP2, it is also localized at the cell membrane. {ECO:0000250}.
Interaction partners:
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
- Myeloid differentiation primary response protein MyD88
- TNF receptor-associated factor 6
- NF-kappa-B essential modulator
- TGF-beta-activated kinase 1 and MAP3K7-binding protein 2
- Dual specificity mitogen-activated protein kinase kinase 4
- TGF-beta activated kinase 1
- Ubiquitin-conjugating enzyme E2 N
- RING-type E3 ubiquitin transferase
- RING-type E3 ubiquitin transferase
Sequence:
MSTASAASSSSSSSASEMIEAPSQVLNFEEIDYKEIEVEEVVGRGAFGVVCKAKWRAKDVAIKQIESESERKAFIVELRQLSRVNHPNIVKLYGACLNPVCLVMEYAEGGSLYNVLHGAEPLPYYTAAHAMSWCLQCSQGVAYLHSMQPKALIHRDLKPPNLLLVAGGTVLKICDFGTACDIQTHMTNNKGSAAWMAPEVFEGSNYSEKCDVFSWGIILWEVITRRKPFDEIGGPAFRIMWAVHNGTRPPLIKNLPKPIESLMTRCWSKDPSQRPSMEEIVKIMTHLMRYFPGADEPLQYPCQYSDEGQSNSATSTGSFMDIASTNTSNKSDTNMEQVPATNDTIKRLESKLLKNQAKQQSDSGRLSLGASRGSSVESLPPTSEGKRMSADMSEIEARIVATTAYTKPKRGHRKTASFGNILDVPEIVISGNGQPRRRSIQDLTVTGTEPGQVSSRSSSPSVRMITTSGPTSEKPARSLPWTPDDSTDTNGSDNSIPMAYLTLDHQLQPLAPCPNSKESMAVFEQHCKMAQEYMKVQTEIALLLQRKQELVAELDQDEKDQQNTSRLVQEHKKLLDENKSLSTYYQQCKKQLEVIRSQQQKRQGTS
Protein: DIOX_N domain-containing protein (O61907)
Organism: Caenorhabditis elegans
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Probable histone-binding protein lin-53
- Protein let-418
- Chromodomain-helicase-DNA-binding protein 3 homolog
- Transcription factor dcp-66
- Histone deacetylase 1
- Probable histone-binding protein rba-1
- Methyl-CpG binding protein 2/3 C-terminal domain-containing protein
- Histone deacetylase
- Egg-laying defective protein 27
- Putative histone deacetylase 2
Sequence:
MSSSSLSSTSTRVTYAVGDFVYFDDTSATDAPYQIRKIEELVKTEKGGVDARCVVYLRRRDIPQHLLKIADQAQRRFDNYYEVDKKKPENFTTKGFIVVNGASEAAPEAAPEATEASAETSETKVKEDTDDVAEKMEEDEECPAPVGQGRTSSTEEPSASDAPAATAKDKKEEKEAKENAKNLKETAEAEATKLIDWGDGGLPLGVDKLTPDQRLKLRQHEIFMTRQSEILPAAAIRGKCRVVLLGDGEEAQNYLPLDDTFYHSLVYDPNAQTLLADKGAIRVGEKYQAVVDEWMEPADREAKEAKVLAEKVKKEEEEAKLKAEAEEDTENDGLTIAEDEEMPELKNEEKEETKVEEEATTTDSEGEVGEVLVWHPHHALTDRDIDQYMIVARSVGLFARAIDGASAPKLPTLQLAAAFASRDVTIFHAHAILHQANYDVGQAVKYLVPVASRDTYPCQVDDSSGLQTKTLGGPILCRDQLEEWSTPEMNLFEDALDKVGKDFNEIRAEYLPWKSIRDIVEYYYLMKASNRYTDRKKNKPSAGGGSSTTTDEKFTNIYIPPFNKPIAASILPYNTSQTTLMNNDNPCENCGTLDALNWYQWGGVGDKKVLCSTCWIQWKKFAGLNQKHELERFDKTRPPPVEPVAPTPAASNGTPASQKAAATAAVNTLTPQQQQQQRAAAANMLMTLNSGDKQNLLNVAKEALARGQITQEQFLQLQKNFAQKIQAQIQQQIQQQQQRQAQTTPQVVATPRKKTTPATKPAIVFYTTICRRAVRRILPKSAFNLRKLSRRPNLAIDDEKILRAMIMLDKKHLLQSAQAAAGDKRSLIVESEFHKGITHLQHALTQAATGKRSAPQAVASGEPSAKMAKQQQQQLPTAFAASGSSSWTPIVAPSLEDVGNSLLAVNHAMKCGGDGGGCVSNNDAPILRQYLTNHQGPATRIDSVRELMRTRTDSRWFVVKDEDVKMRAGPRMKTKRRNLLTRHESRRIARHPCEFHQFLEPFCPIIYPFFTGPLQQSRTTES
Protein: Proline-rich protein 5-like (Protein observed with Rictor-2) (Protor-2) (A2AVJ5)
Organism: Mus musculus (Mouse)
Function: Associates with the mTORC2 complex that regulates cellular processes including survival and organization of the cytoskeleton (By similarity). Regulates the activity of the mTORC2 complex in a substrate-specific manner preventing for instance the specific phosphorylation of PKCs and thereby controlling cell migration. Plays a role in the stimulation of ZFP36-mediated mRNA decay of several ZFP36-associated mRNAs, such as TNF-alpha and GM-CSF, in response to stress. Required for ZFP36 localization to cytoplasmic stress granule (SG) and P-body (PB) in response to stress.
Interaction partners:
- Target of rapamycin complex 2 subunit MAPKAP1
- Proline-rich protein 5
- Rapamycin-insensitive companion of mTOR
- Target of rapamycin complex subunit LST8
- Serine/threonine-protein kinase mTOR
- Proline-rich AKT1 substrate 1
- Regulatory-associated protein of mTOR
- DEP domain-containing mTOR-interacting protein
- Telomere length regulation protein TEL2 homolog
- TELO2-interacting protein 1 homolog
Sequence:
MTRGLAPLLPIEFHKMGSFRRPRPRFMSSPVLSELPRFQAARQALQLSSNSAWNSVQTAVINVFKGGGLQSNELYALNESIRRLLKSELGSFITDYFQNQLLAKGLSFVEEKIKLCEGDNRIEVLAEVWDHFFTETLPTLQAIFYPVQGQELTIRQISLLGFRDLVLLKVKLGDVLLLAQSKLPSSVIQMLLILQSVHEPTGPSEGYLQLEELVKQVVSPFLSISGDRSCSGPTYSLARRHSRVRPKVTVLNYASLMTTVGRPLNEMVLTPLTEQEGEAYLEKCGSVRRHTVANAHSDIQLLAMATMMHSGLGEEAGGEDKHLLLPPSFPPPHRQCSSEPSILDSPDELELEDVASGSQEDSELNCASLS
Protein: Uncharacterized protein (Q57YI8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MSPWKKEEEVCGKPTQYNLQTCEYNWRSLPDTHFTFEAQNRRRRHIGILPGLQGTEKYEARKIPPMESPRADPSPPVWDARPPALPLQPLSQPTLNILPWSHEGLRQMIMANNMEAQHSYLRGV