wanglab/gogpt-training-data huggingface dataset:
Protein: cGMP-inhibited 3',5'-cyclic phosphodiesterase 3B (EC 3.1.4.17) (CGIPDE1) (Cyclic GMP-inhibited phosphodiesterase B) (CGI-PDE B) (Q61409)
Organism: Mus musculus (Mouse)
Function: Cyclic nucleotide phosphodiesterase with a dual-specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Regulates angiogenesis by inhibiting the cAMP-dependent guanine nucleotide exchange factor RAPGEF3 and downstream phosphatidylinositol 3-kinase gamma-mediated signaling (By similarity). Controls cardiac contractility by reducing cAMP concentration in cardiocytes.
Subcellular location: Membrane {ECO:0000269|PubMed:10454575}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- RAC-alpha serine/threonine-protein kinase
- Adenosine kinase
- RAC-beta serine/threonine-protein kinase
- Inosine triphosphate pyrophosphatase
- cGMP-inhibited 3',5'-cyclic phosphodiesterase 3A
- Hypoxanthine-guanine phosphoribosyltransferase
- GTP:AMP phosphotransferase AK3, mitochondrial
Sequence:
MRKDERERDAPAMRSPPPPPASAASPPESLRNGYVKSCVSPLRQDPPRSFFFHLCRFCNVEPPAASLRAGARLSLGVLAAFVLAALLGARPERWAAAAAGLRTLLSACSLSLSPLFSIACAFFFLTCFLTRAQRGPGRGAGSWWLLALPACCYLGDFAAWQWWSWLRGEPAAAGRLCLVLSCVGLLTLAPRVRLRHGVLVLLFAGLVWWVSFSGLGALPPALRPLLSCLVGGAGCLLALGLDHFFHVRGASPPPRSASTAEEKVPVIRPRRRSSCVSLGESAAGYYGSGKMFRRPSLPCISREQMILWDWDLKQWCKPHYQNSGGGNGVDLSVLNEARNMVSDLLIDPSLPPQVISSLRSISSLMGAFSGSCRPKINSFTPFPGFYPCSEVEDPVEKGDRKLHKGLSGRTSFPTPQLRRSSGASSLLTNEHCSRWDRSSGKRSYQELSVSSHGCHLNGPFSSNLFTIPKQRSSSVSLTHHAGLRRAGALPSHSLLNSSSHVPVSAGSLTNRSPIGFPDTTDFLTKPNIILHRSLGSVSSAADFHQYLRNSDSNLCSSCGHQILKYVSTCEPDGTDHPSEKSGEEDSSVFSKEPLNIVETQEEETMKKACRELFLEGDSHLMEEAQQPNIDQEVSLDPMLVEDYDSLIEKMNNWNFQIFELVEKMGEKSGRILSQVMYTLFQDTGLLETFKIPTQEFMNYFRALENGYRDIPYHNRVHATDVLHAVWYLTTRPIPGLPQIHNNHETETKADSDGRLGSGQIAYISSKSCCIPDMSYGCLSSNIPALELMALYVAAAMHDYDHPGRTNAFLVATNAPQAVLYNDRSVLENHHAASAWNLYLSRPEYNFLLNLDHMEFKRFRFLVIEAILATDLKKHFDFLAEFNAKANDVNSNGIEWSSENDRLLVCQVCIKLADINGPAKDRDLHLRWTEGIVNEFYEQGDEEAALGLPISPFMDRSSPQLAKLQESFITHIVGPLCNSYDAAGLLPGQWIETEEGDDTESDDDDDDDDGDGGEELDSDDEETEDNLNPKPQRRKGRRRIFCQLMHHLTENHKIWKEIIEEEEEKCKAEGNKLQVDNASLPQADEIQVIEEADEEEEQMFE
Protein: COP9 signalosome subunit 3 (C9JLV5)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MASALEQFVNSVRQLSAQGQMTQLCELINKSGELLAKNLSHLDTVLGALDVQEHSLGVLAVLFVKFSMPSVPDFETLFSQVQLFISTCNGEHIRYATDTFAGLCHQLTNALVERKQPLRGIGILKQAIDKMQMNTNQLTSIHADLCQLCLLAKCFKPALPYLDVDMMDICKENGAYDAKHFLCYYYYGGMIYTGLKNFERALYFYEQAITTPAMAVSHIMLESYKKYILVSLILLGKVQQLPKYTSQIVGRFIKRQSLAMLARLVLNSWPQAVLLRLPPRVLGLQPLSNAYHELAQVYSTNNPSELRNLVNKHSETFT
Protein: Zinc finger protein 100 (Q8IYN0)
Organism: Homo sapiens (Human)
Function: May be involved in transcriptional regulation.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MDDPRYGMCPLKGASGCPGAERSLLVQSYFEKGPLTFRDVAIEFSLEEWQCLDSAQQGLYRKVMLENYRNLVFLAGIALTKPDLITCLEQGKEPWNIKRHEMVAKPPVICSHFPQDLWAEQDIKDSFQEAILKKYGKYGHDNLQLQKGCKSVDECKVHKEHDNKLNQCLITTQSNIFQCDPSAKVFHTFSNSNRHKIRHTRKKPFKCKKCEKSFCMLLHLTQHKRFHITENSYQCKDCGKAFNWFSTLTTHRRIHTGEKPYKCEECGKAFNRSSHLTTHKIIHTGEKPYRCEECGKAFNRSSHLTTHKRIHTGVKPYKCTECGKAFNRSSHLTTHRIIHTGEKPYKCEECGKAFNQSSTLTTHKITHAGEKPYKCEECGKAFYRFSYLTKHKTSHTGEKFYKCEECGKGFNWSSALTKHKRIHTGEKPYKCEECGKAFNESSNLTTHKMIHTGEKPYKCDECGKAFNRSSQLTAHKMIHTGEKPYKCEECGKAFNRSSTLTKHKITHTGEKSYKWEECGKDFNQSLSLIKQNNSYWRETLQM
Protein: CAST (Q25B55)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell projection, axon {ECO:0000256|ARBA:ARBA00004489}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Synapse {ECO:0000256|ARBA:ARBA00034103}.
Interaction partners:
Sequence:
MGSPYYRDMDEPTSPAGAGHHRSRSASRPPMAHAMDYPRTRYQSLDRGGLVDPHDREFIPIREPRDRSRDRSLERGLYLEDELYGRSARQSPSAMGGYNTGMGPTSDRAYLGDLQHQNTDLQRELGDLKRELELTNQKLGSSMHSIKTFWSPELKKERAPRKEESAKYSLINDQLKLLSTENQKQAMLVRQLEEELRLRMRQPNLEMRQQMEAIYAENDHLQREISILRETVKDLECRVETQKQTLIARDESIKKLLEMLQAKGMGKEEERQMFQQMQAMAQKQLDEFRLEIQRRDQEILAMAAKMKTLEEQHQDYQRHIAVLKESLCAKEEHYNMLQTDVEEMRARLEEKNRLIEKKTQGTLQTVQERNRLTSELTELKDHMDIKDRKISVLQRKIENLEDLLKEKDNQVDMARARLSAMQAHHSSSEGALTSLEEAIGDKEKQMAQLRDQRDRAEHEKQEERDLHEREVADYKIKLRAAESEVEKLQTRPERAVTERERLEIKLEASQSELGKSKAELEKATCEMGRSSADWESTKQRTARLELENERLKHDLERSQNVQKLMFETGKISTTFGRTTMTTSQELDRAQERADKASAELRRTQAELRVTQSDAERAREEAAALQEKLEKSQGEVYRLKAKLENAQGEQESLRQELEKAQSGVSRIHADRDRAFSEVEKIKEEMERTQATLGKSQLQHEKLQNSLDKAQNEVDHLQDKLDKACTENRRLVLEKEKLTYDYDNLQSQLDKALGQAARMQKERETLSLDTDRIREKLEKTQVQLGRIQKERDQFSDELETLKERSESAQTLLMKAARDREAMQTDLEVLKERYEKSHAIQQKLQMERDDAVTEVEILKEKLDKALYASQKLIDEKDTSNKEFEKMLEKYDRAQNEIYRLQSRCDTAEADRARLEVEAERSGLAASKAREDLRKLQDESTRLQEACDRAALQLSRAKECEDNARSELEHSRDRFDKLQTDIRRAQGEKEHFQSELERVTYELERAHAAQTKASASVEAAKEEAAHYAVELEKMRDRYEKSQVELRKLQDTDTFGRETRRLKEENERLREKLDKTLMELETIRGKSQYESESFEKYKDKYEKIEMEVQNMESKLHETSLQLELSKGEVAKMLANQEKQRSELERAHIEREKARDKHEKLLKEVDRLRLQQSSVSPGDPVRASTSSSSALSAGERQEIDRLRDRLEKALQSRDATELEAGRLAKELEKAQMHLAKQQENTESTRIEFERMGAELGRLHDRLEKAEAEREALRQANRSGGAGAAPHPQLEKHVQKLESDVKQLAMEREQLVLQLEKSQEILMNFQKELQNAEAELQKTREENRKLRNGHQVPPVAAPPAGPSPAEFQAMQKEIQTLQQKLQESERALQAAGPQQAQAAAAAGASREEIEQWRKVIEQEKSRADMADKAAQEMHKRIQLMDQHIKDQHAQMQKMQQQMQQQQQAAQQAVQQAAQQQQSAAGAGGADPKELEKVRGELQAACTERDRFQQQLELLVTELEKSKMSNQEQAKQLQTAQQQVQQLQQQVQQLQQQMQQLQQAASAGAGATDVQRQQLEQQQKQLEEVRKQIDNQAKATEGERKIIDEQRKQIDAKRKDIEEKEKKMAEFDVQLRKRKEQMDQLEKSLQTQGGGAAAAGELNKKLMDTQRQLEACVKELQNTKEEHKKAATETERLLQLVQMSQEEQNAKEKTIMDLQQALKIAQAKVKQAQTQQQQQQDAGPAGFLKSFF
Protein: Adhesion G protein-coupled receptor L1 (Calcium-independent alpha-latrotoxin receptor 1) (CIRL-1) (Latrophilin-1) (O88917)
Organism: Rattus norvegicus (Rat)
Function: Calcium-independent receptor of high affinity for alpha-latrotoxin, an excitatory neurotoxin present in black widow spider venom which triggers massive exocytosis from neurons and neuroendocrine cells. Receptor probably implicated in the regulation of exocytosis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:21724987, ECO:0000269|PubMed:22333914}; Multi-pass membrane protein {ECO:0000269|PubMed:21724987, ECO:0000269|PubMed:22333914}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane. Cell projection, axon. Cell projection, growth cone. Synapse. Presynaptic cell membrane. Synapse, synaptosome. Note=Colocalizes with TENM2 on the cell surface, across intercellular junctions and on nerve terminals near synaptic clefts.
Interaction partners:
- Teneurin-2
- Teneurin-4
- Teneurin-3
- Netrin receptor UNC5D
- Netrin receptor UNC5C
- Netrin receptor UNC5A
- Unc-5 family C-terminal like
- Vascular endothelial growth factor A
- Vascular endothelial growth factor B
- SUZ RNA-binding domain-containing
Sequence:
MARLAAALWSLCVTTVLVTSATQGLSRAGLPFGLMRRELACEGYPIELRCPGSDVIMVENANYGRTDDKICDADPFQMENVQCYLPDAFKIMSQRCNNRTQCVVVAGSDAFPDPCPGTYKYLEVQYDCVPYKVEQKVFVCPGTLQKVLEPTSTHESEHQSGAWCKDPLQAGDRIYVMPWIPYRTDTLTEYASWEDYVAARHTTTYRLPNRVDGTGFVVYDGAVFYNKERTRNIVKYDLRTRIKSGETVINTANYHDTSPYRWGGKTDIDLAVDENGLWVIYATEGNNGRLVVSQLNPYTLRFEGTWETGYDKRSASNAFMVCGVLYVLRSVYVDDDSEAAGNRVDYAFNTNANREEPVSLAFPNPYQFVSSVDYNPRDNQLYVWNNYFVVRYSLEFGPPDPSAGPATSPPLSTTTTARPTPLTSTASPAATTPLRRAPLTTHPVGAINQLGPDLPPATAPAPSTRRPPAPNLHVSPELFCEPREVRRVQWPATQQGMLVERPCPKGTRGIASFQCLPALGLWNPRGPDLSNCTSPWVNQVAQKIKSGENAANIASELARHTRGSIYAGDVSSSVKLMEQLLDILDAQLQALRPIERESAGKNYNKMHKRERTCKDYIKAVVETVDNLLRPEALESWKDMNATEQVHTATMLLDVLEEGAFLLADNVREPARFLAAKQNVVLEVTVLSTEGQVQELVFPQEYASESSIQLSANTIKQNSRNGVVKVVFILYNNLGLFLSTENATVKLAGEAGTGGPGGASLVVNSQVIAASINKESSRVFLMDPVIFTVAHLEAKNHFNANCSFWNYSERSMLGYWSTQGCRLVESNKTHTTCACSHLTNFAVLMAHREIYQGRINELLLSVITWVGIVISLVCLAICISTFCFLRGLQTDRNTIHKNLCINLFLAELLFLVGIDKTQYEVACPIFAGLLHYFFLAAFSWLCLEGVHLYLLLVEVFESEYSRTKYYYLGGYCFPALVVGIAAAIDYRSYGTEKACWLRVDNYFIWSFIGPVSFVIVVNLVFLMVTLHKMIRSSSVLKPDSSRLDNIKSWALGAIALLFLLGLTWAFGLLFINKESVVMAYLFTTFNAFQGVFIFVFHCALQKKVHKEYSKCLRHSYCCIRSPPGGAHGSLKTSAMRSNTRYYTGTQVPGQGRHIHQVSLGPRGRSALPESQKDPGGQSGPGDPLTFGLCPSRIRRMWNDTVRKQTESSFMAGDINSTPTLNRGTMGNHLLTNPVLQPRGGTSPYNTLIAESVGFNPSSPPVFNSPGSYREPKHPLGGREACGMDTLPLNGNFNNSYSLRSGDFPPGDGGPEPPRGRNLADAAAFEKMIISELVHNNLRGASGGAKGPPPEPPVPPVPGVSEDEAGGPGGADRAEIELLYKALEEPLLLPRAQSVLYQSDLDESESCTAEDGATSRPLSSPPGRDSLYASGANLRDSPSYPDSSPEGPNEALPPPPPAPPGPPEIYYTSRPPALVARNPLQGYYQVRRPSHEGYLAAPSLEGPGPDGDGQMQLVTSL
Protein: SCAN domain-containing protein 1 (Q571L0)
Organism: Mus musculus (Mouse)
Subcellular location: Nucleus {ECO:0000256|PROSITE-ProRule:PRU00187}.
Interaction partners:
Sequence:
PARVPGPCPSAALSYLLPMQTQARRRTAKQRGTPTAVVMAAPQPSQDPQSPAAPPEQQEGAGDCAAPSPDSGSSPAPELPGAPAALNTAPYADAVLRPGASRPGPETFRQRFRQFRYQDAAGPREAFRQLRELSRQWLRPDIRTKEQIVEMLVQEQLQAILPEAARARRLRRRADVRITG
Protein: Protein sly1 homolog (Q24179)
Organism: Drosophila melanogaster (Fruit fly)
Function: Non-vital for development.
Subcellular location: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}.
Interaction partners:
- BET1 homolog
- Syntaxin-5
- Probable Golgi SNAP receptor complex member 2
- LD34211p
- Golgi SNAP receptor complex member 1
- Secretory 22, isoform B
- Alpha-soluble NSF attachment protein
- Syntaxin-18
- General vesicular transport factor p115
- Vesicle-fusing ATPase 2
Sequence:
MLTLRERQINAIKQMLNLNSQQPKALAAEPVWKILIYDRVGQDIISPIISIKELRELGVTLHVQLHSDRDSIPDVPAIYFCLPTDENLDRIQQDFSSGLYDVYHLNFLAPITRSKIENLAAAALHAGCVANIHRVYDQYVNFISLEDDFFILKHQQSDQLSYYAINRANTRDEEMEALMDSIVDSLFALFVTLGNVPIIRCPRNSAAEMVARKLEKKLRENLWDARANLFHMDATQAGGGVFSFQRPVLLLLDRNMDLATPLHHTWSYQALVHDVLDLGLNLVYVEDETASAGARKKPKACDLDRNDRFWMTHKGSPFPTVAEAIQEELESYRNSEEEIKRLKTSMGIEGESDIAFSLVNDTTARLTNAVNSLPQLMEKKRLIDMHTKIATAILNFIKARRLDSFFEIEEKVMSKQTLDRPLLDLLRDGEFGQAEDKLRLYIIYFICAQQLPESEQERLKEALQAAGCDLTALAYVQRWKGIMNRSPSISQATQYEGGGTKTVSMFTKLVSQGSSFVMEGVKNLVVKRHNLPVTKITEQVMECRSNAETDDYLYLDPKLLKGGEVLPKNRAPFQDAVVFMVGGGNYIEYQNLVDFIKQKQTSNVQRRIIYGASTLTNARQFLKELSALGGEIQSPTATS
Protein: E3 ubiquitin-protein ligase SH3RF2 (EC 2.3.2.27) (Heart protein phosphatase 1-binding protein) (HEPP1) (POSH-eliminating RING protein) (Protein phosphatase 1 regulatory subunit 39) (RING finger protein 158) (RING-type E3 ubiquitin transferase SH3RF2) (SH3 domain-containing RING finger protein 2) (Q8TEC5)
Organism: Homo sapiens (Human)
Function: Has E3 ubiquitin-protein ligase activity. Acts as an anti-apoptotic regulator of the JNK pathway by ubiquitinating and promoting the degradation of SH3RF1, a scaffold protein that is required for pro-apoptotic JNK activation. Facilitates TNF-alpha-mediated recruitment of adapter proteins TRADD and RIPK1 to TNFRSF1A and regulates PAK4 protein stability via inhibition of its ubiquitin-mediated proteasomal degradation. Inhibits PPP1CA phosphatase activity.
Subcellular location: Nucleus {ECO:0000269|PubMed:24130170}.
Interaction partners:
Sequence:
MDDLTLLDLLECPVCFEKLDVTAKVLPCQHTFCKPCLQRVFKAHKELRCPECRTPVFSNIEALPANLLLVRLLDGVRSGQSSGRGGSFRRPGTMTLQDGRKSRTNPRRLQASPFRLVPNVRIHMDGVPRAKALCNYRGQNPGDLRFNKGDIILLRRQLDENWYQGEINGISGNFPASSVEVIKQLPQPPPLCRALYNFDLRGKDKSENQDCLTFLKDDIITVISRVDENWAEGKLGDKVGIFPILFVEPNLTARHLLEKNKGRQSSRTKNLSLVSSSSRGNTSTLRRGPGSRRKVPGQFSITTALNTLNRMVHSPSGRHMVEISTPVLISSSNPSVITQPMEKADVPSSCVGQVSTYHPAPVSPGHSTAVVSLPGSQQHLSANMFVALHSYSAHGPDELDLQKGEGVRVLGKCQDGWLRGVSLVTGRVGIFPNNYVIPIFRKTSSFPDSRSPGLYTTWTLSTSSVSSQGSISEGDPRQSRPFKSVFVPTAIVNPVRSTAGPGTLGQGSLRKGRSSMRKNGSLQRPLQSGIPTLVVGSLRRSPTMVLRPQQFQFYQPQGIPSSPSAVVVEMGSKPALTGEPALTCISRGSEAWIHSAASSLIMEDKEIPIKSEPLPKPPASAPPSILVKPENSRNGIEKQVKTVRFQNYSPPPTKHYTSHPTSGKPEQPATLKASQPEAASLGPEMTVLFAHRSGCHSGQQTDLRRKSALGKATTLVSTASGTQTVFPSK
Protein: Secreted aspartic protease 6 (ACP 6) (Aspartate protease 6) (EC 3.4.23.24) (Candidapepsin-6) (Q5AC08)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Secreted aspartic peptidases (SAPs) are a group of ten acidic hydrolases considered as key virulence factors. These enzymes supply the fungus with nutrient amino acids as well as are able to degrade the selected host's proteins involved in the immune defense. During infection, plays an important role in penetration into deeper tissues and interaction with host defense. Activates host systemic immunity and induces host inflammatory cytokine production in a proteolytic activity-independent way. Contributes to corneal pathogenicity. Moreover, acts toward human hemoglobin though limited proteolysis to generate a variety of antimicrobial hemocidins, enabling to compete with the other microorganisms of the same physiological niche using the microbicidal peptides generated from the host protein.
Subcellular location: Secreted {ECO:0000250|UniProtKB:P0CY27}.
Interaction partners:
- Hyphal wall protein 1
- Agglutinin-like protein 3
Sequence:
MLLKNILSVLAFALLIDAAPVKRSPGFVTLDFNVKRSLVDPDDPTVESKRSPLFLDLDPTKIPVDDTGRNDGVDKRGPVAVKLDNEIITYSADITVGSNNQKLSVIVDTGSSDLWIPDSKAICIPKWRGDRGDFCKNNGSYSPAASSTSKNLNTRFEIKYADGSYAKGNLYQDTVGIGGASVKNQLFANVWSTSAHKGILGIGFQANEATRTPYDNLPISLKKQGIIAKNAYSLFLNSPEASSGQIIFGGIDKAKYSGSLVELPITSDRTLSVGLRSVNVMGRNVNVNAGVLLDSGTTISYFTPSIARSIIYALGGQVHFDSAGNKAYVADCKTSGTVDFQFDKNLKISVPASEFLYQLYYTNGKPYPKCEIRVRESEDNILGDNFMRSAYIVYDLDDKKISMAQVKYTSESNIVAIN
Protein: Lipoxygenase (EC 1.13.11.-) (Q9FSE5)
Organism: Oryza sativa (Rice)
Interaction partners:
Sequence:
MLTATQTLAPAVLSRSHGAPSSFSSQPRRTAAAASRVSCTRVGALSEVVNGELVVGDQEQTTDDLLTRHKNVVADYTLSATVTVSLKQDDSTPQKVADMVNRDWLFLDFFSSHIEGMHTEPQLARYSHMDGKGSFIYEASFSIPSSLDAVGAVQVVNRYSSEVYISDIDVHLCGGRHQWTDITFHCNSWIDYNPNDQRFFFPLKSYLPSQTPRGVKNLRKEELRAIRGDGRGERKEWERIYDYDVYNDLGDPDNDPATRRPVLGGRGRPYPRRCRTGRRRCRTDPSSESPPAKDGAGIYVPRDEAFTERKAGAFATKKALSALSAFTTAQRVSGDRRRGFPSLAAIDALYEDGYKNRPSSSQQEADNLEGYFREVLQKQVKLLLKGEKEEFKEELRKVFKFQTPEIHDKDKLAWFRDEEFARQTLAGMNPLSIQLVRDTDFPIFSKLDEETYGPGDSLITKELIEEQINGVMTAEEAVEKKKLFMLDYHDVLLPFVHAVRELDDTTLYASRTLFFLTEDGTLRPIAIELTRPKSPNTPQWRQVFTPGSSVAASWLWQLAKTHVLAHDTGYHQLVSHWLRTHCCVEPYVIAANRRLSQMHPIYRLLHPHFRFTMEINAQARGMLINANGIIESAFAPGKLCMELSSAVYDKFWRFDMEALPADLIRRGMAIECEDGKLELTIEDYPYANDGLLIWDSIKEWVSDYVNHYYQLASDIHMDKELQGWWNEVRTKGHPDKEEGWPELNCHGSLVEVLTTIIWVASGHHAAVNFGQYPYAGYFPNRPTIARRNMPTEGQACSHDGMQPTFVEDPVRVLLDTFPSQYQTTLVLPVLNLLSSHSPGEEYMGTHAESAWMADREVRAAFGRFNERMMSIAEMIDCRNKDPERKNRQGPGVVPYVLLKPSYGDPKDMTSVMEMGIPNSISI
Protein: V-type proton ATPase subunit a (Q86M57)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGSLFRSEEMALCQLFLQSEAAYACVSELGELGLVQFRDLNPDVNAFQRKFVNEVRRCDEMERKLRYLEKEIKKDGIPMLDTGESPEAPQPREMIDLEATFEKLENELREVNQNAEALKRNFLELTELKHILRKTQVFFDEMADNQNEDEQAQLLGEEGVRASQPGQNLKLGFVAGVILRERLPAFERMLWRACRGNVFLRRAMIETPLEDPTNGDQVHKSVFIIFFQGDQLKTRVKKICEGFRATLYPCPEAPADRREMAMGVMTRIEDLNTVLGQTQDHRHRVLVAAAKNLKNWFVKVRKIKAIYHTLNLFNLDVTQKCLIAECWVPLLDIETIQLALRRGTERSGSSVPPILNRMQTFENPPTYNRTNKFTKAFQALIDAYGVASYREMNPAPYTIITFPFLFAVMFGDLGHGAIMALFGLWMIRKEKGLAAQKTDNEIWNIFFGGRYIIFLMGVFSMYTGLIYNDIFSKSLNIFGSHWHLSYNKSTVMENKFLQLSPKGDYEGAPYPFGMDPIWQVAGANKIIFHNAYKMKISIIFGVIHMIFGVVMSWHNHTYFRNRISLLYEFIPQLVLLLLLFFYMVLLMFIKWIKFAATNDKPYSEACAPSILITFIDMVLFNTPKPPPENCETYMFMGQHFIQVLFVLVAVGCIPVMLLAKPLLIMQARKQANVQPIAGATSDAEAGGVSNSGSHGGGGGHEEEEELSEIFIHQSIDTIEYVLGSVSHTASYLRLWALSLAHAQLAEVLWTMVLSIGLKQEGPVGGIVLTCVFAFWAILTVGILVLMEGLSAFLHTLRLHWVEFQSKFYKGQGYAFQPFSFDAIIENGAAAAEE
Protein: Large ribosomal subunit protein eL36B (60S ribosomal protein L36-B) (L39) (YL39) (O14455)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Large ribosomal subunit protein uL10
- Large ribosomal subunit protein eL30
- Large ribosomal subunit protein uL3
- Large ribosomal subunit protein eL33A
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein eL32
- Large ribosomal subunit protein eL39
- Large ribosomal subunit protein eL27A
- Large ribosomal subunit protein uL13A
- Large ribosomal subunit protein uL22A
Sequence:
MAVKTGIAIGLNKGKKVTQMTPAPKISYKKGAASNRTKFVRSLVREIAGLSPYERRLIDLIRNSGEKRARKVAKKRLGSFTRAKAKVEEMNNIIAASRRH
Protein: DNA-directed RNA polymerase III subunit 2 (DNA-directed RNA polymerase III subunit RPC2) (DNA polymerase I subunit C2) (EC 2.7.7.6) (Nuclear RNA polymerase C2) (F4KD38)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Second largest core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Proposed to contribute to the polymerase catalytic activity and forms the polymerase active center together with the largest subunit. Pol III is composed of mobile elements and NRPC2 is part of the core element with the central large cleft and probably a clamp element that moves to open and close the cleft.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:P22276}.
Interaction partners:
- DNA-directed RNA polymerase III subunit RPC3
- RNApolymerase 14 kDa subunit
- SIN-like family protein
- DNA-directed RNA polymerase subunit
- DNA-directed RNA polymerases II, IV and V subunit 6A
- DNA-directed RNA polymerase III subunit RPC9
- DNA-directed RNA polymerases II and V subunit 6B
- DNA-directed RNA polymerase III subunit 1
- DNA-directed RNA polymerase III subunit RPC6
- DNA-directed RNA polymerases I and III subunit RPAC1
Sequence:
MGLDQEDLDLTNDDHFIDKEKLSAPIKSTADKFQLVPEFLKVRGLVKQHLDSFNYFINVGIHKIVKANSRITSTVDPSIYLRFKKVRVGEPSIINVNTVENINPHMCRLADMTYAAPIFVNIEYVHGSHGNKAKSAKDNVIIGRMPIMLRSCRCVLHGKDEEELARLGECPLDPGGYFIIKGTEKVLLIQEQLSKNRIIIDSDKKGNINASVTSSTEMTKSKTVIQMEKEKIYLFLHRFVKKIPIIIVLKAMGMESDQEIVQMVGRDPRFSASLLPSIEECVSEGVNTQKQALDYLEAKVKKISYGTPPEKDGRALSILRDLFLAHVPVPDNNFRQKCFYVGVMLRRMIEAMLNKDAMDDKDYVGNKRLELSGQLISLLFEDLFKTMLSEAIKNVDHILNKPIRASRFDFSQCLNKDSRYSISLGLERTLSTGNFDIKRFRMHRKGMTQVLTRLSFIGSMGFITKISPQFEKSRKVSGPRSLQPSQWGMLCPCDTPEGESCGLVKNLALMTHVTTDEEEGPLVAMCYKLGVTDLEVLSAEELHTPDSFLVILNGLILGKHSRPQYFANSLRRLRRAGKIGEFVSVFTNEKQHCVYVASDVGRVCRPLVIADKGISRVKQHHMKELQDGVRTFDDFIRDGLIEYLDVNEENNALIALYESDGTTELDEGAEAAKADTTHIEIEPFTILGVVAGLIPYPHHNQSPRNTYQCAMGKQAMGNIAYNQLNRMDTLLYLLVYPQRPLLTTRTIELVGYDKLGAGQNATVAVMSFSGYDIEDAIVMNKSSLDRGFGRCIVMKKIVAMSQKYDNCTADRILIPQRTGPDAEKMQILDDDGLATPGEIIRPNDIYINKQVPVDTVTKFTSALSDSQYRPAREYFKGPEGETQVVDRVALCSDKKGQLCIKYIIRHTRRPELGDKFSSRHGQKGVCGIIIQQEDFPFSELGICPDLIMNPHGFPSRMTVGKMIELLGSKAGVSCGRFHYGSAFGERSGHADKVETISATLVEKGFSYSGKDLLYSGISGEPVEAYIFMGPIYYQKLKHMVLDKMHARGSGPRVMMTRQPTEGKSKNGGLRVGEMERDCLIAYGASMLIYERLMISSDPFEVQVCRACGLLGYYNYKLKKAVCTTCKNGDNIATMKLPYACKLLFQELQSMNVVPRLKLTEA
Protein: Alveolarin (P84760)
Organism: Polyporus alveolaris (Hexagonal-pored polypore) (Neofavolus alveolaris)
Function: Antifungal activity. Inhibits mycelial growth of F.cinera, F.oxysporum, M.arachidicola and P.piricola. Lacks protease, ribonuclease, deoxyribonuclease and hemagglutinating activity.
Interaction partners:
Sequence:
GVCDMADLA
Protein: Bromodomain PHD finger transcription factor (A0A8I6GLB4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MRGRRGRPPKQPAAPAAERCAPAPPPPPPPPPPPPPPPPPPPASGPIGGLRSRHRGSSRGRWAAAQAEVAPKTRLSSPRGGGRRKQPPPPPASASSASGPGRGGRGGGGGRTGGGGGHLARTTSARRAVNKVVYDDHESEDDDEEEDMVSEEDEEEEEDGDAEETQDSEDDEEDDMEEDDDDSDYPEEMEDDDDDASYCTESSFRSHSTYSSTPGRRKPRVHRPRSPILEEKDIPPLEFPKSSEDLMVPNEHIMNVIAIYEVVRNFGNVLRLSPFCFEDFCAALVSQEQCTLMAEMHVALLKAVLREEDTSNTTFGPADLKDSVNSTLYFIDGMTWPEVLRVYCESDKEYHHVLPYQEAEDYPYGPVESKIKVLQFLVDQFLTTNIAREELMSEGVIQYDDHCRVCHKLGDLLCCETCSAVYHLECVKPPLEEVPEDEWQCEVCVAHKVPGVTDCVAEVQKNKPYVRHEPIGYDRSRRKYWFLNRRLIIEEDTENENEKKVWYYSTKVQLAELIDCLDKDYWEAELCRVLEDIREEMQQHMDVTEDLTNKARGSNKSFLAAANEEILDSLRIKRGEDIDCDQNPEDTEKDKNEGENDSSKGAEKSREESEDQSPDKDADGKVLEEEPGQGKPEEDSHKTCDSSNTSATTASSQPNLENCSSSSSSSELTSSQSDSAKAADDPDIGERDSHTPVSVQEEIGDFRLDKSNGEVSESPGTGKGTSGSTRIITRLRNPESKLSQLKSQQVAAAAHEANKLFKEGKEVLVVNSQGEVSRLSTKKEVVMKGNINNYFKLGQEGKYRVYHNQYSTNSFALNKHQHREDHDKRRHLAHKFCLTPAGEFKWNGSVHGSKVLTISTLRLTITQLESNIPSSFLHPNWASHRANWIKAVQMCSKPREFALALAILECAVKPVVMLPIWRESLGHTRLHRMTSIEREEKEKVKKKEKKQEEEETMQQATWVKYTFPVRHQVTGYGGWSWISKTHVYRFLPKLPGNTNVNYRKPLEGVKNNMDENKDESDKRKSPRSPKKMKTECDSEKGEARDADSTAGATAGTMELSKLPEKEEHDVKELLDPDNDKPFKEEPMEIDDSVKTESHMNSEESAQVDVVNVSEGFHLRTSYKKKTKSSKLDGLLERRIRQFTLEEKQRLEKLKLESGVKGAGKPPTGAVKSSSEPPVSTKADEGHQGDLLRQEQRSTPSQAGTADLGLGASQSDPLVLGISPPSLSTGKPDPKGQVLDDVSIQSPGPACQGQNSVESDLDARISEATSKGLELSQTKTKVTDSLTDDSKPTSADEGSTLICKSKKPLPQDDCSTAVSSSSKSTLPAPVPKSPRDRDARAFPKAMDLDGRLGGDSEYNSTLENNSGTMYMRDSSEEDMVVQNSNDTTSKRFITPDQGMESTEPTKCQLVSKSTENCDNRLQGKVTEANGKKLGQHQKPEERAVNRCADQVSLRHSADRKNSEARESEKRGQKANKFQINGKDSKAKGYLKGPGMKDVSDGKVMSGAVEPKVNNINKVIPGNIKSLAGKESAVKPFVNGDIIMEEFSEQNTSETNSYSLSSSDAKGNHQDGLHTLPSTKDSASTQVIIPPAPCPDRNSLNQVEDMETEGPEVKKVTPSPITTGEDSNLGKDVMDENGLPSSKDENVNGESQRKTVITEVTTMTSTVATESKTVIKVAKGDKQTVVSSTENCARSTVTTTTTTVTKLSTPSPDSDVDTVSVKEQSKTVVTTTVTDSLSTAGSTLVTSMTVSREYSTRDRVKLMKFSRPKKTRSGTALPSYRKFVTKSSKKSIFVLPNDDLKKLARKGGIREVPCFNYNAKPALDIWPYPSPRPTFGITWRYRLQTVKSLAGVSLMLRLLWASLRWDDMAAKAPPGGGSTRTETSETEITTTEIIKRRDVGPYGIRSEYCIRKIICPIGVPEAPKETPTPQRKGLRSSALRPKRPETPKQTGPVVIESWVAEEELELWEIRAFAERVEKEKAQAVEQQTKKRLEQQKPAVIAASTTSPTNSTSSTVSPAQKVMVAPLSGSVTPGTKMVLATKVGSPATVTFQQNKNFHQTFATWVKQGQSNSGVVQVQQKVLGIIPSTAGPSQQTFTSFQPRTATVTIRPNTSASAGTTTTSQVITGPQIRPGMTVIRAPLQQPALGKAVIRTPVTMQPGAPQQVVTQIIRGQPVSTAISASSTASSAPVQKGLTPGAAAGTLQPSAPHSPRPQQGQVKLTMAQLTQLTQGHGGNQGLTVVIQGQGQTTGQLQLIPQGMTVLPGPGQQLMQAAMPNGTVQRFLFTPLSTPVTAVSSSSSSSSTNATATGSGEQKQSKLSPQTQVQPATTLAPTQSSSVSPAEAQPQPAQPAAQPQPQPQPPAQPEVQTQPAASSHVPSETQPSQAQSSKPLVATQCQPQSSVQGQSPVRVQSPPLTRIRPSTPSQVTPGQQPQVQTTASQPIPIPPPTSLQAPSQGQPQSQPQVQSSTQTLSSGQTLNQVTVPSPSRPQPQTQQPQPQVIAVPQLQQVQVLSQIQSQVVAQIQAQQGGAPQQIKLQLPVHVQQNSAAQAQHAQSVLTVQAASVREQLQRVQQLRDQQQKKKQQIEMEREHTLQASNQSEIIQKQVVMKHNAVIEHLKQKKTMTPAEREENQRMIVCNQVMKYILDKIDKEEKQAAKKRKREESVEQKRSKQNASKLSALLFKHKEQLKAEILKKRALLDKELQMQVQEELKRDLKMKREREMAQVVQANAAAGPTPSVPAPVPAPAPAPAAPPAPPSPPPSTHSLPPAGHPTAPLPVTSQKRKREEEKDSKSKKKKMISTTSKEAKKDTRLYCICKTPYDESKFYIGCDRCQNWFHGRCVGILQSEAELIDEYVCPQCQSTEDAMTVLTPLTEKDYEGLKRVLRSLQAHKMAWPFLEPVDPNDAPDYYGVIKEPMDLATMEERIQKRYYEKLTEFVADMTKIFDNCRYYNPSDSPFYQCAEVLESFFVQKLKGFKASRSHNNKLQSTAP
Protein: 3-aminoacrylate deaminase RutC (3-AA deaminase) (EC 3.5.-.-) (P0AFQ5)
Organism: Escherichia coli (strain K12)
Function: Involved in pyrimidine catabolism. Catalyzes the deamination of 3-aminoacrylate to malonic semialdehyde, a reaction that can also occur spontaneously. RutC may facilitate the reaction and modulate the metabolic fitness, rather than catalyzing essential functions. In vitro, can also deaminate 2-aminoacrylate.
Interaction partners:
- Putative carbamate hydrolase RutD
- Ureidoacrylate amidohydrolase RutB
- Probable malonic semialdehyde reductase RutE
- Pyrimidine monooxygenase RutA
- FMN reductase RutF
- Putative pyrimidine permease RutG
- NADP-dependent 3-hydroxy acid dehydrogenase YdfG
- RutC family protein YoaB
Sequence:
MPKSVIIPAGSSAPLAPFVPGTLADGVVYVSGTLAFDQHNNVLFADDPKAQTRHVLETIRKVIETAGGTMADVTFNSIFITDWKNYAAINEIYAEFFPGDKPARFCIQCGLVKPDALVEIATIAHIAK