wanglab/gogpt-training-data huggingface dataset:
Protein: Essential MCU regulator, mitochondrial (Single-pass membrane protein with aspartate-rich tail 1, mitochondrial) (Q9DB10)
Organism: Mus musculus (Mouse)
Function: Essential regulatory subunit of the mitochondrial calcium uniporter complex (uniplex), a complex that mediates calcium uptake into mitochondria. Required to bridge the calcium-sensing proteins MICU1 and MICU2 with the calcium-conducting subunit MCU. Plays a central role in regulating the uniplex complex response to intracellular calcium signaling. Acts by mediating activation of MCU and retention of MICU1 to the MCU pore, in order to ensure tight regulation of the uniplex complex and appropriate responses to intracellular calcium signaling (By similarity).
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:27001609}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q9H4I9}. Note=MAIP1 is required to assist sorting of EMRE/SMDT1 into mitochondrion by protecting EMRE/SMDT1 against protein degradation by YME1L1, thereby ensuring SMDT1/EMRE maturation by the mitochondrial processing peptidase (PMPCA and PMPCB). {ECO:0000250|UniProtKB:Q9H4I9}.
Interaction partners:
- Calcium uptake protein 1, mitochondrial
- Calcium uptake protein 2, mitochondrial
- Calcium uniporter protein
- Calcium uniporter regulatory subunit MCUb, mitochondrial
- Calcium uptake protein 3, mitochondrial
- Endothelial differentiation-related factor 1
- Mitochondrial calcium uniporter regulator 1
- Dynactin subunit 3
- Mitochondrial inner membrane m-AAA protease component AFG3L2
- NADH dehydrogenase 1 alpha subcomplex subunit 8
Sequence:
MASTAARRLAWVAVRPGALWSGPRGRRGGDVYTVPGSSGLSQVPSRSVIVTRSGAILPKPVKMSFGLLRVFSIVIPFLYVGTLISKNFAALLEEHDIFVPEDDDDDD
Protein: DNA polymerase alpha catalytic subunit (EC 2.7.7.7) (DNA polymerase I) (P28040)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Catalytic subunit of the DNA polymerase alpha complex (also known as the alpha DNA polymerase-primase complex) which plays an essential role in the initiation of DNA synthesis. During the S phase of the cell cycle, the DNA polymerase alpha complex (composed of a catalytic subunit pol1, an accessory subunit spb70/pol12 and two primase subunits, the catalytic subunit spp1/pri1 and the regulatory subunit spp2/pri2) is recruited to DNA at the replicative forks. The primase subunit of the polymerase alpha complex initiates DNA synthesis by oligomerising short RNA primers on both leading and lagging strands (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:10759889, ECO:0000269|PubMed:16823372}.
Interaction partners:
- DNA primase large subunit
- DNA primase small subunit
- DNA polymerase alpha subunit B
- Minichromosome loss protein 1
- DNA polymerase epsilon catalytic subunit A
- DNA polymerase epsilon subunit B
- Cell division control protein 45 homolog
- DNA replication licensing factor mcm4
- DNA polymerase epsilon subunit D
- DNA polymerase subunit delta-2
Sequence:
MRKRNAGIKPSQRFAELRALRQAGKTRASTYESKENEELYDNVSEEEYRKIVRQRLDEDDFVVDDNGAGYVDNGYDEWDQSHYSDEDDENEKGSSGRKRKKSKNVLAEPNQQIGAFFKANAIQPASRIANRKNNEKEDEFMAEILGSIDQDIPERLSTKKGNRSHTTSNAKRRSQKAASSISTTNVVSSDPKKYIPETVPSTPQPASSLPIPSSPPAALETEENVDSQPMELDEPELPVGSDAPIIDVEESIAMKPLMSHDQVDDTASLSKATISQQPLSPMTPLSSELDVSAFSEINSKIKNVDVPASSYSSPISKVSPSDVTEEDGSLFFFWMDYTEMYGSLCLFGKVYDKATKQYVSCFLKVDGIMRSLYFLPRPSSSSVSEDSIAAQTKDVYDEVANLLSKRGVKEWKSRVSKYKYAFELEDVPRTADYLEVIYSYSYPALPTDLTGSSFSHVFGTNTALFEQFVLSRRVMGPCWLKIQQPNFDAVKNASWCRVEIGCSSPQNISVSFEKNEITSKTPPMTVMSLAFRTLINKEQNKQEVVMISARIFENVDIEKGLPANDMPSYSFSLIRPLKQIFPNGFEKLARQHKSSIFCERSEVSLLNNFLNKVRTYDPDVYFGHDFEMCYSVLLSRLKERKIHNWSSIGRLRRSEWPRSFNRSSQQFVEKQIIAGRLMCDLSNDFGRSMIKAQSWSLSEIVLKELDIKRQDINQEKALQSWTDTAHGLLDYLVHCEIDTFFIAAVAFKIQMLQLSKNLTNIAGNSWARTLTGTRAERNEYILLHEFKKNGYIVPDKQQSIRRHAEAFGAEDGLQEESLGKKKDKYKGGLVFEPQKGLYETCILVMDFNSLYPSIIQEYNICFTTVDRSPSNSDSDDQIPDTPSASANQGIFPRLIANLVERRRQIKGLLKDNSATPTQRLQWDIQQQALKLTANSMYGCLGYTKSRFYARPLAVLITYKGREALMNTKELADQMGLQVIYGDTDSVMLNTNVTDKNHALRIGNEFKEKVNERYSKLEIDIDNVYQRMLLHAKKKYAALQLDSQGKPNLDVKGLDMKRREFCTLAKEASKFCLDQILSGELTETVIENIHSYLMDFSEKMRNGKFPANKFIIFNRLGKNPEDYPNGKTMPFVQVALKKKARGENVRVGDVIPFIIAGSDADGHPADRAYSPQEIMNTNSTLVIDYNYYLSHQILPPIERVIAPIEGTNRARLAECLGLDARKYYSHETSESSAFQRYESTLTDDQCFINVSPLLLKCPSCNATSFSLRSVKSLKETLYANTVECDCGYEYSDFTIILQFSSQLRDFINLYYEGILVCDDSSCGNRTRQMSVYGKRCCNKSCRGSVHFEYNDEQLYNQIKFLLKAVQTTTGATRNGIIRCNAINKNISRIMNKNAREFVDMGLIFSS
Protein: Serrate RNA effector molecule homolog (Arsenite-resistance protein 2) (Q99MR6)
Organism: Mus musculus (Mouse)
Function: Acts as a mediator between the cap-binding complex (CBC) and the primary microRNAs (miRNAs) processing machinery during cell proliferation. Contributes to the stability and delivery of capped primary miRNA transcripts to the primary miRNA processing complex containing DGCR8 and DROSHA, thereby playing a role in RNA-mediated gene silencing (RNAi) by miRNAs. Binds capped RNAs (m7GpppG-capped RNA); however interaction is probably mediated via its interaction with NCBP1/CBP80 component of the CBC complex. Involved in cell cycle progression at S phase. Does not directly confer arsenite resistance but rather modulates arsenic sensitivity. Independently of its activity on miRNAs, necessary and sufficient to promote neural stem cell self-renewal. Does so by directly binding SOX2 promoter and positively regulating its transcription.
Subcellular location: Nucleus, nucleoplasm. Cytoplasm. Note=Predominantly nuclear. Shuttles between the nucleus and the cytoplasm in a CRM1-dependent way.
Interaction partners:
- Nuclear cap-binding protein subunit 2
- Nuclear cap-binding protein subunit 1
- Phosphorylated adapter RNA export protein
- Spliceosome RNA helicase Ddx39b
- THO complex subunit 4
- Exosome RNA helicase MTR4
- RNA-binding protein 7
- RNA-binding protein 39
- ATP-dependent RNA helicase A
- RNA-binding protein 25
Sequence:
MGDSDDEYDRRRRDKFRRERSDYDRSRERDERRRGDDWNDREWDRGRERRSRGEYRDYDRNRRERFSPPRHELSPPQKRMRRDWDEHSSDPYHSGYDMPYAGGGGGPTYGPPQPWGHPDVHIMQHHVLPIQARLGSIAEIDLGVPPPIMKSFKEFLLSLDDSVDETEAVKRYNDYKLDFRRQQMQDFFLAHKDEEWFRSKYHPDEVGKRRQEARGALQNRLKVFLSLMESGWFDNLLLDIDKADAIVKMLDAAVIKMEGGTENDLRILEQEEEEEQAGKTGEASKKEEARAGPALGEGERKANDKDEKKEDGKQAENDSSNDDKTKKSEGDGDKEEKKEEAEKEAKKSKKRNRKQSGDDSFDEGSVSESESESEGGQAEEEKEEAEEALKEKEKPKEEEKEKPKDAAGLECKPRPLHKTCSLFMRNIAPNISRAEIISLCKRYPGFMRVALSEPQPERRFFRRGWVTFDRSVNIKEICWNLQNIRLRECELSPGVNRDLTRRVRNINGITQHKQIVRNDIKLAAKLIHTLDDRTQLWASEPGTPPVPTSLPSQNPILKNITDYLIEEVSAEEEELLGSSGGPPPEEPPKEGNPAEINVERDEKLIKVLDKLLLYLRIVHSLDYYNTCEYPNEDEMPNRCGIIHVRGPMPPNRISHGEVLEWQKTFEEKLTPLLSVRESLSEEEAQKMGRKDPEQEVEKFVTSNTQELGKDKWLCPLSGKKFKGPEFVRKHIFNKHAEKIEEVKKEVAFFNNFLTDAKRPALPEIKPAQPPGPAQILPPGLTPGLPYPHQTPQGLMPYGQPRPPILGYGAGAVRPAVPTGGPPYPHAPYGAGRGNYDAFRGQGGYPGKPRNRMVRGDPRAIVEYRDLDAPDDVDFF
Protein: LIM domain-containing protein C4F6.12 (O74398)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
- Cell division control protein 15
- Ingression protein fic1
- Septation protein imp2
- Probable Rho-GTPase-activating protein 7
- 1,3-beta-glucan synthase component bgs1
- Rho1 guanine nucleotide exchange factor 3
- Myosin regulatory light chain 1
- Uncharacterized protein P22H7.03
- Myosin type-2 heavy chain 1
- Cell division control protein 12
Sequence:
MHSPIPELPRFERRLTGPRAAPSSPVSTNGSPLNNLVRSRLSDGALNFTGGRIATPLPQPSLKTPESPLSKRNPTIKQNRVRFDLPDDELSRSNVSSPEKTLLTSASTSTFDSLKKELLPELPSLAYSDDDEFPSSPEELNSHVNYPDVRNVYDCHTGLQPLVDHDCIEDRQKTFASKQLPTLPLQKSSKLSNRRPALHSFHSAPANSLYPLPTPTSQLPSNLSSNNLFQSDSLKPSMVSSHTSTKPVLYRGNSEKSCHSCGGSLRAGRIISASGKKLHPQCFKCDTCSQNLEHVGFYYREGKFYCHLDYHEQFSPRCKHCKTPIEDQAVHINNDWFHENHHFCAGCSEVFNVNIPCIYRDDLYWCQTCYDNKYAVKCKKCRKPILGISVKGSDGEYHSQCWTCGACNALLGDEGYFMIENTPICRPCKAISVKFNLD
Protein: Inner membrane component of tripartite multidrug resistance system (E0SIF2)
Organism: Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937))
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Achromobactin siderophore NIS synthase
- Putative AcsD
Sequence:
MVSMGMTMPLTGYLGHRLGNKPLYLLGVALFISGSLLGMLADSISQVIAARTVQGIASGLMIPLSLTLIFSVYPKQERGGITGIWGAIVMLAPALGPLCGGILLEWFSWRALFVMNIPIGALALLMGLVVLPKTAPGERKPFDMTGYVLVSAGIGLLMIGAGRLHHAAALANPLNLLMLLAAAVCLIAFVRVELRKREPLLNLRIFQLHGYRLSVVIAVVQSVGMFECLVLLPMLVQMVMGYSAIWTGLALLCTALFASLFGKIGGSLLDRHGPSRVVGAGVLLTALATVGLGMAGVQTSIGVVFGWMMLRGVGLGLSYMPVTTAGLNVLPETLVTQGAAMNNISRRLVSSLAIVVASLYLEFRLAGSGLAHETVRAAAISETFIATGMLILLALPCALRFPTATDEASANALLAGESTLPAGTRESR
Protein: Glycine N-acyltransferase-like protein Keg1 (EC 2.3.1.13) (Acyl-CoA:glycine N-acyltransferase protein Keg1) (Kidney-expressed gene 1 protein) (Q9DCY0)
Organism: Mus musculus (Mouse)
Function: Acyltransferase which transfers the acyl group to the N-terminus of glycine. Can conjugate a multitude of substrates to form a variety of N-acylglycines (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Note=Also localizes in regions surrounding the centrosome. The centrosomal localization is dependent on microtubules (By similarity). {ECO:0000250}.
Interaction partners:
- Glycine N-acyltransferase
- Coagulation factor XIII B chain
- UDP-glucuronosyltransferase 3A2
Sequence:
MFCLQSSQALQVLENSLRKHLPESLKVYGTVFHINQGNPFKLKTLVDKWPDFNTVVIRPQEEDMTDDLDHYNNTYLVYSKDPKHCQEFLGSSEVINWKQHLQIQSSQSDLGKVIESLGATNLGKVKHKQCFLYMVCQTAKKLAPSLMDAKNLVVSRNKLTPLDQQLFKFASLDVTHAALVNSLWHFGGNEKSQKFIERCIFTFPSFCIMGPEGTPVSWTLMDHTGELRMGGTLPKYRRQSLIYHVASQQIQTLEKLGFPMYAHVDKANFTVQRMVGLLGQILLPCTWNQWNCVPL
Protein: FI05255p (Magu, isoform A) (Magu, isoform B) (Magu, isoform D) (Q0E9E0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- FI20169p1
- receptor protein serine/threonine kinase
Sequence:
MLARCVLFVTWLAVFIATGKSDDQLMKLPACAAKQGECDDNEGPVCGTDGQTYPTRCHLLRAQCGGHQVSLKYSGSCNACLEAVKFARRQQERDPGYFVPRCRKDGNFAAMQCYGNNGCWCSDSQGRPIADDNKQFRRKGKLRCRANRRDRRRLASHQIGYNPDTSASKGSSEAGSTAHRTCSKSDRSQFNTNLMRMFRNEAQSFFRQPSLSDSHILEWQFSKLDTNGNKLLDRQEIRELKKVLRRNVKPRRCGRTFGKYCDVTKDANLNWLEWSVCFTKEFHNRSAVVNLLASSAATAPPHSTHYSIHNTNVNGHHRGHTNTIGTGVNPHSYSEDASGSEEHEDNYEDSATGYGGEEDDSQGADLPSSRTHIPSLYMLNSKPETASQDLENDSNCWMDQSVTLEEQGHGGKSVLFVPQCLPDGRYQRIQCYSSTSTSYCWCVNEDTGKSIPGTSVKNKRPQCDESVAVRPMKGCTEPRKTQFLKELKAYLNTSLLPSSTTGSNSSMWKTDDERIATLSFVYLDKNKNKSWDRREWKNFRDLVTSASHLRRCGKKMPRYCDVNGDKKISLAEWLNCLQATPRESATTAKPAQSNETASPKFQGVNPVERYLKD
Protein: DNA-binding bromodomain-containing protein (Q8VY17)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cytochrome b561, DM13 and DOMON domain-containing protein At5g54830
- SWI/SNF complex subunit SWI3C
- Histone acetyltransferase subunit NuA4-domain protein
- Histone acetyltransferase of the MYST family 2
- Histone acetyltransferase of the MYST family 1
- At1g20670
- Polyadenylate-binding protein interacting protein
- At1g76380
- SWI/SNF complex subunit SWI3A
- Protein METABOLIC NETWORK MODULATOR 1
Sequence:
MSQIARRRRKGRPSKADLAARRSSSSPRESGYELRRGQRQRNVRYNFDFDDYFDEEEEDEVEEEKKRQKKLKQVLKLNQSRARADPPVKSRARVRHASDYEEEDEEDDEAEEEEEEVSEKRQVKKRKLNRQDEEEEEEEEKDYDVEEEEEEEEGHADSEEEDDKERKRRSASGNQCDHSSETTPILDKKSLELILDKLQKKDIYGVYAEPVDPEELPDYHDMIEHPMDFSTVRKKLANGSYSTLEELESDVLLICSNAMQYNSSDTVYYKQARTIQEMGKRKFEKARLKIKRAEKELKTDEKVKPDSSVKKQVRQPFSRNGLEAVGSDFSSGANLASGGASQNEPVSTQIGGHEKHSYTDVLFEGNTSLVDSLEKAEDLSSGKGLFGKCGRKLSVVEEDRRATYEDSDQQGDRSESIFTTFESEIKQFVAVGLHAEHAYGRSLARFAATLGPVAWKIASQRIEQALPADFKFGRGWVGEYEPLPTPVLLFETCTPKEPPKKASVFSKRKSNAATKTNETLFKTPLPAKEQQGSRPVRDGNHAFPFPASIGALSEGSPSFVATQVGNLKSMSQHEYRNPSQLDFVKPQNRIPQQVELNLPPPAEQTNSGSGCVLENQSFGKSDTVASYRSSSDMMRNMSSTDSEHYKHQMTTNGIFPGGLRNGKVSPGVNNRMFDLSTDFANQMSRTATSSQQPMRQQSQSHEEQAQIMRNFNERARTQHNSTYNHPKADAPPKISSPQSARSEDSGNASVAAARAWMSIGAGGNNKQTFENASNPKSSQISAESLYNPSREHFHQQAFKPRDAEETQFHPQRNGFPFQTFVHQPVHGMMNGGYQPFQNNRPIVFPQMAAPTSDFSRFHVQSQWRGGITPQVQLKQRQENFNLPPDLNIGVHSPDSPAKQSSGVRVDSQQPDLALQL
Protein: NLR family pyrin domain containing 5 (F1MT67)
Organism: Bos taurus (Bovine)
Interaction partners:
Sequence:
MPTRSVAANRRQERHHADPPKARHHRLPVGSCPRVSPVRLIRAQGPKKPSERRRSHWLRLPKTTFPFHLSSQPCIKMREAKIAPLSNYGLQWCFEQLGKEEFQTFKALLKEHASESAACSFPLVQVDRADAESLASLLHEHCRASLAWKTSTDIFEKMSLSALSEMARDEMKKYLLAEISEDSAPTKTDQGPSMKEVPGPREDPQDSRDYRIHVMTTFSTRLDTPQRFEEFASECPDAHALSGAFNPDSSGGFRPLTVVLHGPPGVGKSSLARRLLLFWAQGDLYKGLFSYVFLLRARDLQGSRETSFAELISKEWPDAPVPVEKVLSQPERLLIVVDGLEELELTFRDQDSSLLADWAERQPAPVLAHSLLKKVLLPECALLLTVQDAGLQRLQALLRSPRYLWVGGLSVENRMQLLLGGGKHCRRKTCAWHAGADHQEVLDKCQVPVVCALVREALELQGEPGKGLPVPGHTLTGLYATFVFQRLAPKDAGWRALSGEERGALKGLCRLAADGVWNAKFVFDGDDLGVHGLQGPELSALQQASILLPDGHCGRGHAFSHLSLQEFFAALFYVLRGVEGDGEGYPLFPQSTKSLTELRHIDLNVQLVQMKRFLFGLVSKEVMRALETLLGCPVAPVAKQQLLHWICLLGQHPAAAASPDLLEAFYCLFETQDDEFVRLALNGFQEVWLQLNRPMDLTVSSFCLRRCQHLQKVRLDVRGTPKDEFAEAWFGAPQGLKIKTLDEHWEDLCSVLSTHPNLRQLDLSGSVLSKEAMKTLCVKLRQPACKIQNLIFKGARVAPGLRHLWMTLIINRNITRLDLTGCRLREEDVRTACEALRHPQCALESLRLDRCGLTPASCREISQVLATSGSLKSLSLTGNKVVDQGVKSLCDALKVTPCTLQKLILGSCGLTAATCQDLASALIENQGLTHLSLSGDELGSKGMSLLCRAVKLSSCGLQKLALNACSLDVAGCGFLAFALMGNRHLTHLSLSMNPLEDPGMNLLCEVMMEPSCPLRDLDLVNCRLTASCCKSLSNVITRSPRLRSLDLAANALGDEGIAALCEGLKQKNTLTRLGLEACGLTSEGCKALSAALTCSRHLASLNLMRNDLGPRGMTTLCSAFMHPTSNLQTIGLWKEQYPARVRRLLEQVQRLKPHVVISDAWYTEEEEDGPCWRI
Protein: Histone-lysine N-methyltransferase KMT5B (Lysine-specific methyltransferase 5B) (Suppressor of variegation 4-20 homolog 1) (Su(var)4-20 homolog 1) (Suv4-20h1) ([histone H4]-N-methyl-L-lysine20 N-methyltransferase KMT5B) (EC 2.1.1.362) ([histone H4]-lysine20 N-methyltransferase KMT5B) (EC 2.1.1.361) (Q3U8K7)
Organism: Mus musculus (Mouse)
Function: Histone methyltransferase that specifically methylates monomethylated 'Lys-20' (H4K20me1) and dimethylated 'Lys-20' (H4K20me2) of histone H4 to produce respectively dimethylated 'Lys-20' (H4K20me2) and trimethylated 'Lys-20' (H4K20me3) and thus regulates transcription and maintenance of genome integrity. In vitro also methylates unmodified 'Lys-20' (H4K20me0) of histone H4 and nucleosomes (By similarity). H4 'Lys-20' trimethylation represents a specific tag for epigenetic transcriptional repression. Mainly functions in pericentric heterochromatin regions, thereby playing a central role in the establishment of constitutive heterochromatin in these regions. KMT5B is targeted to histone H3 via its interaction with RB1 family proteins (RB1, RBL1 and RBL2). Plays a role in myogenesis by regulating the expression of target genes, such as EID3. Facilitates TP53BP1 foci formation upon DNA damage and proficient non-homologous end-joining (NHEJ)-directed DNA repair by catalyzing the di- and trimethylation of 'Lys-20' of histone H4 (By similarity). May play a role in class switch reconbination by catalyzing the di- and trimethylation of 'Lys-20' of histone H4.
Subcellular location: Nucleus {ECO:0000269|PubMed:15145825}. Chromosome {ECO:0000269|PubMed:15145825}. Note=Associated with pericentric heterochromatin. CBX1 and CBX5 are required for the localization to pericentric heterochromatin.
Interaction partners:
- DNA
- N-lysine methyltransferase KMT5A
- Histone H4
- Histone-lysine N-methyltransferase SUV39H1
- Histone-lysine N-methyltransferase SUV39H2
- Histone-lysine N-methyltransferase SETD2
- Protein arginine N-methyltransferase 5
Sequence:
MKWLGDSKNMVVNGRRNGGKLSNDHQQNQSKLQQHSGKDTLKTGRNAVERRSSRCHGNSGFEGQSRYVPSSGMSAKELCENDDLATSLVLDPYLGFQTHKMNTSAFPSRSSRHISKADSFSHNNPVRFRPIKGRQEELKEVIERFKKDEHLEKAFKCLTSGEWARHYFLNKNKMQEKLFKEHVFIYLRMFATDSGFEILPCNRYSSEQNGAKIVATKEWKRNDKIELLVGCIAELSEIEENMLLRHGENDFSVMYSTRKNCAQLWLGPAAFINHDCRPNCKFVSTGRDTACVKALRDIEPGEEISCYYGDGFFGENNEFCECYTCERRGTGAFKSRVGLPAPAPVINSKYGLRETDKRLNRLKKLGDSSKNSDSQSVSSNTDADTTQEKDNATSNRKSSVGVKKSSKSRALTRPSMPRVPAASNSTSPKLVHTNNPRVPKKLRKPAKPLLSKIRLRNHCKRLDQKSASRKLEMGSLVLKEPKVVLYKNLPIKKEREPEGPAHAAVGSGCLTRHAAREHRQNHGRGAHSQGDSLPCTYTTRRSLRTRTGLKETTDIKLEPSPLDGYKNGILEPCPDSGQQPTPEVLEELAPETAHREEASQECPKNDSCLSRKKFRQVKPVKHLAKTEDCSPEHSFPGKDGLPDLPGSHPDQGEPSGTVRVPVSHTDSAPSPVGCSVVAPDSFTKDSFRTAQSKKKRRVTRYDAQLILENSSGIPKLTLRRRHDSSSKTNDHESDGVNSSKISIKLSKDHDSDSNLYVAKLSNGVSAGPGSSSTKLKIQLKRDEESRGPCAEGLHENGVCCSDPLSLLESQMEVDDYSQYEEDSTDESSSSEGEEEEEDCEDDFDDDFIPLPPAKRLRLIVGKDSIDIDISSRRREDQSLRLNA
Protein: Fungal lipase-type domain-containing protein (Q583Z4)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Phospholipid:diacylglycerol acyltransferase-like protein
- Acyltransferase
- Phosphatidic acid phosphatase protein, putative
- Phosphatidic acid phosphatase, putative
- Monoglyceride lipase, putative
- Lipase-like protein, putative
- Monoglyceride lipase, putative
- Phosphatidic acid phosphatase alpha, putative
- Lipin, putative
- Long-chain-fatty acid-CoA ligase protein, putative
Sequence:
MQGDTKTMGKKKTVSSLNETRERRRLDIGKVRDVWNTFQTAMWHVCLPNELVMCFDPLLRCIFALYYLPPVALVVAITHSALARIVWVLVTPVAQEMEKQPYDASRIVTLALGLYQIIICMLPFTTLSIAVATLGHKALNCFMESMVDSWCTYEQRDYPLLAARLRFMMEDRWRCCTFLVVLFLLGTLVLSGFHTDLLVAWPDREGNVALNVWLIIFIDLTFVVVSAFTCSPPGLRLLNSKKDTADGKDGSFLEYFFDTWWRKRVFYIRYATGYMVIALGVFTTYHDGPLRALSMLLETLMYLLIPHVMVHAVLSISIVAVNFHRSVRWLSHHRAAVPHTIAFILPYEGVLLYSMYYFRHHWMTVCLLVGVSVLLIYRSIDIAREFEVTEAGSVLWKREDDGTVAPPDLAKVLEEAHENKSRHLNTVSLGVSGDMERMRLISDGKEIPLQRVVIERIGESRSLSKKAVFLAYAFPRVLHAQKPNYLGGKHFRTGRLLLRTITSILLTFFALLVAGVILQAAFPELRKWPVRLRISEGGEILTIDHIVVRMHLLSRNASANPLSPPVTSAMTPAHAAFQWGNTTAFNTDWYASLCAREFHGASVWEVSLLALATYLSTEEEVRQMLHFMNTHMETDWIMRERHGMDCVAVDSSTKPTEWNGYFDFYSAKHDLSVVAIRGTDMTSAIDFLIDFNMFFEVVLYHLLSNFVPGAGILPSHLIADLIGLASLRSDGNFQYGTWESLIAESKADDKNNKLQCVSNNYRRDFFADVYNHIRYIGSRSKRPKHVILTGHSLGGAVASIVGAKMGIQAVGFGAPGITLARKKFNVDLRSINKHVGNIISSHDIFPMIGGNVGEQHRIECLATTRELCHAMEFLVGALWRSCGSIRSRFPSMGSVL
Protein: Riparin-2.1 (P86127)
Organism: Crinia riparia (Streambank froglet) (Flinders Ranges froglet)
Function: Has antibacterial activity against the Gram-positive bacterium L.lactis (MIC=25 uM). Lacks antibacterial activity against the Gram-negative bacteria E.cloacae and E.coli, and against the Gram-positive bacteria B.cereus, E.faecalis, L.innocua, M.luteus, S.aureus, S.epidermidis and S.uberis. Does not inhibit the formation of NO by neuronal nitric oxide synthase.
Subcellular location: Secreted {ECO:0000269|PubMed:16470724}.
Interaction partners:
Sequence:
IIEKLVNTALGLLSGL
Protein: Peroxidase (DmPO) (EC 1.11.1.7) (Chorion peroxidase) (Q01603)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in the chorion hardening process, through protein cross-linking mediated by the formation of di- and tri-tyrosine bonds.
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Uncharacterized protein
- RH49821p
- Zye
Sequence:
MIRARDLLLLALLGFISSALGLKVSSGYHIVHNQPQSSFPNYHGFSYLQGSAPYVIGNSLPTSPAPQNPFSSPASPPVSAYGYSFPTAGRVSCAAPPAVCEKTAYRTLDGSCNHLEQPGLGVANSKYGRLLTPKYADGISAPTRSVTGDELPSARLVSLVAFGEQDVPDPEFTLHNMQWGQIMTHDMSMQAGGTQSKKHPTRCCTDDGRLIGLDTAHKTCFAIIVPPHDPAYSQVGTECLNFVRTLTDRDSNCQYQGGPAEQLTVVTSYLDLSLVYGNSIQQNSDIREFQGGRMIVEERNGAKWLPLSRNVTGDCDAVDASEVCYRSGDVRVNQNPGLAILQTILLREHNRIADALSALNPHYDDRTLFQEARKINIAQYQQISYYEWLPIFLGGENMLKNRLIYKAPSGSYINDFDPNIDPSVLNEHATAAFRYFHSQIEGRLDLLSELRQVLGSLTLSDWFNRPGIIEVGDNFDSLTRGHATQPEELTDINFDRQIKHFLFRRNMPFGSDLRSLDIQRNRDHGLASYNDMREFCGLRRAHSWEGYGDLISPPILEKLKSLYPSHEDVDLTVGASLEAHVAGALAGPTFLCILTEQFYRTRVGDRFFFENGDKLTGFTPDQLEELRKASMARLLCDNGNHISSMQPEAFRTVSHSNPIIPCSNIPQVDLTKWIDQKLYATVDPSHYGKK
Protein: Sodium/potassium-transporting ATPase subunit alpha (Q7ZYK8)
Organism: Xenopus laevis (African clawed frog)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Sodium/potassium-transporting ATPase subunit beta
- Sodium/potassium-transporting ATPase subunit beta
- Sodium/potassium-transporting ATPase subunit beta
- Sodium/potassium-transporting ATPase subunit beta
- Sodium/potassium-transporting ATPase subunit beta
- Sodium/potassium-transporting ATPase subunit beta
- Sodium/potassium-transporting ATPase subunit beta
- Zinc finger protein 574
- FXYD domain-containing ion transport regulator
- FXYD domain-containing ion transport regulator
Sequence:
MGYGRSDSYRVATTQDNKDEKSPKKGKGVPKKEMDDLKKEVAMTEHKMSVEEVCRKYNTDCVQGLTLSKAAEILERDGPNALTPPPTTPEWIKFCRQLFGGFSILLWIGAILCFLAYSIQKGVEDDPAGDNLYLGIVLAAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALIIREGEKMQVNAEEVVVGDLVEIKGGDRVPADLRIISSHGCKVDNSSLTGESEPQTRSPDCTHDNPLETRNVTFFSTNCVEGTARGVVVATGDRTVMGRIATLASGLEVGKTPIAKEIEHFIHLITGVAVFLGISFFILSLVLGYSWLEAVIFLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHEADTTEDQSGASFDKSSQTWLALAQIAALCNRAVFKAGNDNIPVLKRDVAGDASESALLKCIELSCGSVKAIREKNKKVAEIPFNSTNKYQLSIHETEDPNDNRYLLVMKGAPERILDVCSTILIQGKEQPLDDELKEAFQNAYLELGGLGERVLGFCHFYFPEELYPKGFAFDTEDQNFSTENMCFVGLMSMIDPPRAAVPDAVGKCRSAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEDIAARLNIPVSQVNPRDAKACVIHGTDLKDMPAEKIDEILQNHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALKKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSIAYTLTSNIPEITPFLLFIMANIPLPLGTITILCIDLGTDMVPAISLAYEAAESDIMKRQPRNPRTDKLVNERLISMAYGQIGMIQALGGFFAYFVILAENGFLPSHLVGIRLTWDDRSVNDLEDSYGQQWTYEQRKIVEFTCHTAFFVSIVVVQWADVIICKTRRNSVFQQGMKNKILIFGLFEETALAAFLSYCPGMDIALRMYPLKPSWWFCAFPYSFLIFIYDEIRKLILRRHPGGWVEKESYY
Protein: Serine/threonine-protein acetyltransferase YopJ (EC 2.3.1.-) (Virulence factor YopJ) (A0A0N9NCU6)
Organism: Yersinia pseudotuberculosis
Function: Serine/threonine-protein acetyltransferase translocated into infected cells, which inhibits the host immune response and induces cell death by mediating acetylation of target proteins. Inhibits the MAPK and NF-kappa-B signaling pathways by acetylating protein-kinases such as MAP2K1, MAP2K6, MAP3K7/TAK1 and I-kappa-B kinase (CHUK/IKKA and IKBKB) on serine and threonine residues critical for their activation by phosphorylation, thereby preventing protein-kinase activation. Promotes pyroptosis, a programmed cell death, in host cells by mediating acetylation of MAP3K7/TAK1: MAP3K7/TAK1 inactivation triggers activation of caspase-8 (CASP8), followed by CASP8-dependent cleavage of gasdermin-D (GSDMD) and induction of pyroptosis. Also able to induce intestinal barrier dysfunction by acetylating and inhibiting host protein-kinases RIPK2/RICK and MAP3K7/TAK1, thereby promoting cell death (By similarity).
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0DUD0}. Note=Secreted via type III secretion system (T3SS). {ECO:0000250|UniProtKB:P0DUD0}.
Interaction partners:
Sequence:
MIGPISQINISGGLSEKETSSLISNEELKNIITQLETDISDGSWFHKNYSRMDVEVMPALVIQANNKYPEMNLNLVTSPLDLSIEIKNVIENGVRSSRFIINMGEGGIHFSVIDYKHINGKTSLILFEPANFNSMGPAMLAIRTKTAIERYQLPDCHFSMVEMDIQRSSSECGIFSFALAKKLYIERDSLLKIHEDNIKGILSDGENPLPHDKLDPYLPVTFYKHTQGKKRLNEYLNTNPQGVGTVVNKKNETIVNRFDNNKSIVDGKELSVSVHKKRIAEYKTLLKV
Protein: Transmembrane protein 186 (Q9CR76)
Organism: Mus musculus (Mouse)
Function: As part of the MCIA complex, required for efficient assembly of the mitochondrial complex I.
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q96B77}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q96B77}.
Interaction partners:
- NADH-ubiquinone oxidoreductase chain 3
- Evolutionarily conserved signaling intermediate in Toll pathway, mitochondrial
- Complex I intermediate-associated protein 30, mitochondrial
- Complex I assembly factor TMEM126B, mitochondrial
- Complex I assembly factor ACAD9, mitochondrial
- Distal membrane-arm assembly complex protein 2
- FAD-dependent oxidoreductase domain-containing protein 1
- Transmembrane protein 70
Sequence:
MAFLLRVVPRLQGPTAWRRPLQGLWCCSGQGDSKRWVGSRSPHSREKSPGTETETFHTIYRFRAIRAIGFLSRLKLAQTAVTVVALPPGFYCYSQGLMTLSSLCLLGGVASFALAMLCWMSHFFRRLVGILYVNESGTLLRVAHLTFWGWRQDTYCAVSDMIPLSESQERVQDVFVRIQQYSGKQTFYLTLRYGRILDRERFAQVFGTLATLKNSK
Protein: Two component system response regulator (Two-component response regulator) (A0A0H3NKV1)
Organism: Salmonella typhimurium (strain SL1344)
Interaction partners:
Sequence:
MKEYKILLVDDHEIIINGIMNALLPWPHFKIVEHVKNGLEVYNACCAYEPDILILDLSLPGINGLDIIPQLHQRWPAMNILVYTAYQQEYMTIKTLAAGANGYVLKSSSQQVLLAALQTVAVNKRYIDPTLNREAILAELNADTTNHQLLTLRERQVLKLIDEGYTNHGISEKLHISIKTVETHRMNMMRKLQVHKVTELLNCARRMRLIEY
Protein: ERCC excision repair 1, endonuclease non-catalytic subunit (A0A8I6A2U2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MDPGKDEENRPQPSGPPTRKKFVIPLEEDEAPSSGAKPLFKSSRNPTPTAASTHSAPLTYAEYAIAQPPGGAGATVPTGSEPATGDSPSQTLKAGTKSSSIIVSPRQRGNPVLKFVRSVPWEFGEVTPDYVLGQSTCALFLSLRYHNLHPDYIHERLQSLGKNFALRVLLVQVDVKDPQQALKELAKICILADCTLVLAWSAEEAGRYLETYKAYEQKPADLLMEKLEQNFLSRVRMRILSFCTS