wanglab/gogpt-training-data huggingface dataset:
Protein: Large ribosomal subunit protein eL36 (60S ribosomal protein L36) (P47964)
Organism: Mus musculus (Mouse)
Function: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9Y3U8}. Cytoplasm {ECO:0000269|PubMed:36517592}. Note=Detected on cytosolic polysomes. {ECO:0000250|UniProtKB:Q2YGT9, ECO:0000250|UniProtKB:Q9Y3U8}.
Interaction partners:
- Small ribosomal subunit protein eS25
- Large ribosomal subunit protein eL19
- Large ribosomal subunit protein uL2
- Large ribosomal subunit protein uL5
- Large ribosomal subunit protein uL24
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS10
- Small ribosomal subunit protein uS15
- Large ribosomal subunit protein eL18
- Small ribosomal subunit protein eS28
Sequence:
MALRYPMAVGLNKGHKVTKNVSKPRHSRRRGRLTKHTKFVRDMIREVCGFAPYERRAMELLKVSKDKRALKFIKKRVGTHIRAKRKREELSNVLAAMRKAAAKKD
Protein: Phosphatidic acid phosphohydrolase 1 (PAP1) (EC 3.1.3.4) (Protein SMP2) (P32567)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Mg(2+)-dependent phosphatidate (PA) phosphatase which catalyzes the dephosphorylation of PA to yield diacylglycerol. Required for de novo lipid synthesis and formation of lipid droplets. Controls transcription of phospholipid biosynthetic genes and nuclear structure by regulating the amount of membrane present at the nuclear envelope. Involved in plasmid maintenance, in respiration and in cell proliferation.
Subcellular location: Cytoplasm. Nucleus membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Peripheral membrane protein.
Interaction partners:
- CTP-dependent diacylglycerol kinase 1
- Diacylglycerol O-acyltransferase 1
- Lipid phosphate phosphatase 1
- Diacylglycerol pyrophosphate phosphatase 1
- Phospholipid:diacylglycerol acyltransferase
- Phosphatidate cytidylyltransferase
- Sporulation-specific protein SPO7
- Nuclear envelope morphology protein 1
- Glycerol-3-phosphate O-acyltransferase 1
- Triacylglycerol lipase 4
Sequence:
MQYVGRALGSVSKTWSSINPATLSGAIDVIVVEHPDGRLSCSPFHVRFGKFQILKPSQKKVQVFINEKLSNMPMKLSDSGEAYFVFEMGDQVTDVPDELLVSPVMSATSSPPQSPETSILEGGTEGEGEGENENKKKEKKVLEEPDFLDINDTGDSGSKNSETTGSLSPTESSTTTPPDSVEERKLVEQRTKNFQQKLNKKLTEIHIPSKLDNNGDLLLDTEGYKPNKNMMHDTDIQLKQLLKDEFGNDSDISSFIKEDKNGNIKIVNPYEHLTDLSPPGTPPTMATSGSVLGLDAMESGSTLNSLSSSPSGSDTEDETSFSKEQSSKSEKTSKKGTAGSGETEKRYIRTIRLTNDQLKCLNLTYGENDLKFSVDHGKAIVTSKLFVWRWDVPIVISDIDGTITKSDALGHVLAMIGKDWTHLGVAKLFSEISRNGYNILYLTARSAGQADSTRSYLRSIEQNGSKLPNGPVILSPDRTMAALRREVILKKPEVFKIACLNDIRSLYFEDSDNEVDTEEKSTPFFAGFGNRITDALSYRTVGIPSSRIFTINTEGEVHMELLELAGYRSSYIHINELVDHFFPPVSLDSVDLRTNTSMVPGSPPNRTLDNFDSEITSGRKTLFRGNQEEKFTDVNFWRDPLVDIDNLSDISNDDSDNIDEDTDVSQQSNISRNRANSVKTAKVTKAPQRNVSGSTNNNEVLAASSDVENASDLVSSHSSSGSTPNKSTMSKGDIGKQIYLELGSPLASPKLRYLDDMDDEDSNYNRTKSRRASSAAATSIDKEFKKLSVSKAGAPTRIVSKINVSNDVHSLGNSDTESRREQSVNETGRNQLPHNSMDDKDLDSRVSDEFDDDEFDEDEFED
Protein: Inverted formin-2 (HBEBP2-binding protein C) (Q27J81)
Organism: Homo sapiens (Human)
Function: Severs actin filaments and accelerates their polymerization and depolymerization.
Subcellular location: Cytoplasm, perinuclear region {ECO:0000269|PubMed:20023659}.
Interaction partners:
- Alpha-actinin-4
- Nephrin
- CD2-associated protein
- Podocin
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
- Short transient receptor potential channel 6
- Cell division control protein 42 homolog
- Speckle-type POZ protein
- Apolipoprotein L1
- Wilms tumor protein
Sequence:
MSVKEGAQRKWAALKEKLGPQDSDPTEANLESADPELCIRLLQMPSVVNYSGLRKRLEGSDGGWMVQFLEQSGLDLLLEALARLSGRGVARISDALLQLTCVSCVRAVMNSRQGIEYILSNQGYVRQLSQALDTSNVMVKKQVFELLAALCIYSPEGHVLTLDALDHYKTVCSQQYRFSIVMNELSGSDNVPYVVTLLSVINAVILGPEDLRARTQLRNEFIGLQLLDVLARLRDLEDADLLIQLEAFEEAKAEDEEELLRVSGGVDMSSHQEVFASLFHKVSCSPVSAQLLSVLQGLLHLEPTLRSSQLLWEALESLVNRAVLLASDAQECTLEEVVERLLSVKGRPRPSPLVKAHKSVQANLDQSQRGSSPQNTTTPKPSVEGQQPAAAAACEPVDHAQSESILKVSQPRALEQQASTPPPPPPPPLLPGSSAEPPPPPPPPPLPSVGAKALPTAPPPPPLPGLGAMAPPAPPLPPPLPGSCEFLPPPPPPLPGLGCPPPPPPLLPGMGWGPPPPPPPLLPCTCSPPVAGGMEEVIVAQVDHGLGSAWVPSHRRVNPPTLRMKKLNWQKLPSNVAREHNSMWASLSSPDAEAVEPDFSSIERLFSFPAAKPKEPTMVAPRARKEPKEITFLDAKKSLNLNIFLKQFKCSNEEVAAMIRAGDTTKFDVEVLKQLLKLLPEKHEIENLRAFTEERAKLASADHFYLLLLAIPCYQLRIECMLLCEGAAAVLDMVRPKAQLVLAACESLLTSRQLPIFCQLILRIGNFLNYGSHTGDADGFKISTLLKLTETKSQQNRVTLLHHVLEEAEKSHPDLLQLPRDLEQPSQAAGINLEIIRSEASSNLKKLLETERKVSASVAEVQEQYTERLQASISAFRALDELFEAIEQKQRELADYLCEDAQQLSLEDTFSTMKAFRDLFLRALKENKDRKEQAAKAERRKQQLAEEEARRPRGEDGKPVRKGPGKQEEVCVIDALLADIRKGFQLRKTARGRGDTDGGSKAASMDPPRATEPVATSNPAGDPVGSTRCPASEPGLDATTASESRGWDLVDAVTPGPQPTLEQLEEGGPRPLERRSSWYVDASDVLTTEDPQCPQPLEGAWPVTLGDAQALKPLKFSSNQPPAAGSSRQDAKDPTSLLGVLQAEADSTSEGLEDAVHSRGARPPAAGPGGDEDEDEEDTAPESALDTSLDKSFSEDAVTDSSGSGTLPRARGRASKGTGKRRKKRPSRSQEEVPPDSDDNKTKKLCVIQ
Protein: Alpha-amylase 3, chloroplastic (AtAMY3) (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) (Q94A41)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Possesses endoamylolytic activity in vitro, but seems not required for breakdown of transitory starch in leaves. May be involved in the determination of the final structure of glucans by shortening long linear phospho-oligosaccharides in the chloroplast stroma. Can act on both soluble and insoluble glucan substrates to release small linear and branched malto-oligosaccharides. Works synergistically with beta-amylase toward efficient starch degradation. Has activity against p-nitrophenyl maltoheptaoside (BPNP-G7), amylopectin and beta-limit dextrin. Involved in stress-induced starch degradation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:15637061, ECO:0000269|PubMed:21294843}.
Interaction partners:
- Alpha-glucan phosphorylase 1
- Isoamylase 3, chloroplastic
- Alpha-glucan phosphorylase 2, cytosolic
- 4-alpha-glucanotransferase DPE2
- 4-alpha-glucanotransferase DPE1, chloroplastic/amyloplastic
- Isoamylase 1, chloroplastic
- Isoamylase 2, chloroplastic
- 1,4-alpha-glucan-branching enzyme 3, chloroplastic/amyloplastic
- alpha-D-xyloside xylohydrolase
- 1,4-alpha-glucan-branching enzyme 2-1, chloroplastic/amyloplastic
Sequence:
MSTVPIESLLHHSYLRHNSKVNRGNRSFIPISLNLRSHFTSNKLLHSIGKSVGVSSMNKSPVAIRATSSDTAVVETAQSDDVIFKEIFPVQRIEKAEGKIYVRLKEVKEKNWELSVGCSIPGKWILHWGVSYVGDTGSEWDQPPEDMRPPGSIAIKDYAIETPLKKLSEGDSFFEVAINLNLESSVAALNFVLKDEETGAWYQHKGRDFKVPLVDDVPDNGNLIGAKKGFGALGQLSNIPLKQDKSSAETDSIEERKGLQEFYEEMPISKRVADDNSVSVTARKCPETSKNIVSIETDLPGDVTVHWGVCKNGTKKWEIPSEPYPEETSLFKNKALRTRLQRKDDGNGSFGLFSLDGKLEGLCFVLKLNENTWLNYRGEDFYVPFLTSSSSPVETEAAQVSKPKRKTDKEVSASGFTKEIITEIRNLAIDISSHKNQKTNVKEVQENILQEIEKLAAEAYSIFRSTTPAFSEEGVLEAEADKPDIKISSGTGSGFEILCQGFNWESNKSGRWYLELQEKADELASLGFTVLWLPPPTESVSPEGYMPKDLYNLNSRYGTIDELKDTVKKFHKVGIKVLGDAVLNHRCAHFKNQNGVWNLFGGRLNWDDRAVVADDPHFQGRGNKSSGDNFHAAPNIDHSQDFVRKDIKEWLCWMMEEVGYDGWRLDFVRGFWGGYVKDYMDASKPYFAVGEYWDSLSYTYGEMDYNQDAHRQRIVDWINATSGAAGAFDVTTKGILHTALQKCEYWRLSDPKGKPPGVVGWWPSRAVTFIENHDTGSTQGHWRFPEGKEMQGYAYILTHPGTPAVFFDHIFSDYHSEIAALLSLRNRQKLHCRSEVNIDKSERDVYAAIIDEKVAMKIGPGHYEPPNGSQNWSVAVEGRDYKVWETS
Protein: Protein PALE CRESS, chloroplastic (Q39089)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Required for the differentiation of chloroplast from proplastids or etioplasts, probably by modulating some chloroplast-encoded genes expression and mRNA maturation. Involved in leaf-cells differentiation.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:10350211, ECO:0000269|PubMed:9648738}. Plastid, chromoplast {ECO:0000269|PubMed:10350211}. Plastid, etioplast {ECO:0000269|PubMed:10350211}. Plastid, amyloplast {ECO:0000269|PubMed:10350211}. Note=Present in thin tubular projections emanating from plastids and often connecting organelles each other. {ECO:0000269|PubMed:10350211}.
Interaction partners:
- Phytoene synthase 1, chloroplastic
- Expressed protein family protein)
- Adenylylsulfatase HINT3
- Ubiquitin carboxyl-terminal hydrolase-related protein
- Lycopene beta cyclase, chloroplastic
- 1-deoxy-D-xylulose-5-phosphate synthase, chloroplastic
- 15-cis-phytoene desaturase, chloroplastic/chromoplastic
- Probable E3 ubiquitin-protein ligase ARI5
- UDP-glycosyltransferase 79B7
- Protein RFT1 homolog
Sequence:
MAATSLVLTCASPLFSSPRVISATKKLTTELSISTAKFRRRCSGNNDEVLLEGMPPEYYDDEWQARQREKTKELRRMQREEEEEEERKIEEYREIGTRLKEFPEQDLRKARKLVSSFIRAAEEVEERIEEAAEKGELDELVLMIIWNRLDLARRDDEKDAIRSLDLLYRRVETEILKRQASPAMKLLNDLLNMHDGFEDDAWLKDCRKRMAETFPREDPFSILMPPGFDIDMHQGQLRPPIETETDNTLLRVDFVREVDALLQEVRIEEDATTGSKGEGLDPEAIALKFKQQEKQRTIRQIEAILDLALNLKW
Protein: Cytosolic phospholipase A2 beta (cPLA2-beta) (EC 3.1.1.4) (Lysophospholipase A1 group IVB) (EC 3.1.1.5) (Phospholipase A2 group IVB) (P0C869)
Organism: Homo sapiens (Human)
Function: Calcium-dependent phospholipase A1 and A2 and lysophospholipase that may play a role in membrane phospholipid remodeling.
Subcellular location: [Isoform 3]: Cytoplasm, cytosol {ECO:0000269|PubMed:16617059}. Mitochondrion membrane {ECO:0000269|PubMed:16617059}; Peripheral membrane protein. Early endosome membrane {ECO:0000269|PubMed:16617059}; Peripheral membrane protein. Note=Translocates to membrane vesicles in a calcium-dependent fashion. {ECO:0000269|PubMed:16617059}.; SUBCELLULAR LOCATION: [Isoform 5]: Cytoplasm, cytosol {ECO:0000269|PubMed:16617059}.
Interaction partners:
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- Mitogen-activated protein kinase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Guanine nucleotide-binding protein G
- Mitogen-activated protein kinase 3
- Guanine nucleotide-binding protein G
- Phospholipase A2 group V
- X-box-binding protein 1
- Patatin-like phospholipase domain-containing protein 7
- Polyunsaturated fatty acid lipoxygenase ALOX15B
Sequence:
MAVAEVSRTCLLTVRVLQAHRLPSKDLVTPSDCYVTLWLPTACSHRLQTRTVKNSSSPVWNQSFHFRIHRQLKNVMELKVFDQDLVTGDDPVLSVLFDAGTLRAGEFRRESFSLSPQGEGRLEVEFRLQSLADRGEWLVSNGVLVARELSCLHVQLEETGDQKSSEHRVQLVVPGSCEGPQEASVGTGTFRFHCPACWEQELSIRLQDAPEEQLKAPLSALPSGQVVRLVFPTSQEPLMRVELKKEAGLRELAVRLGFGPCAEEQAFLSRRKQVVAAALRQALQLDGDLQEDEIPVVAIMATGGGIRAMTSLYGQLAGLKELGLLDCVSYITGASGSTWALANLYEDPEWSQKDLAGPTELLKTQVTKNKLGVLAPSQLQRYRQELAERARLGYPSCFTNLWALINEALLHDEPHDHKLSDQREALSHGQNPLPIYCALNTKGQSLTTFEFGEWCEFSPYEVGFPKYGAFIPSELFGSEFFMGQLMKRLPESRICFLEGIWSNLYAANLQDSLYWASEPSQFWDRWVRNQANLDKEQVPLLKIEEPPSTAGRIAEFFTDLLTWRPLAQATHNFLRGLHFHKDYFQHPHFSTWKATTLDGLPNQLTPSEPHLCLLDVGYLINTSCLPLLQPTRDVDLILSLDYNLHGAFQQLQLLGRFCQEQGIPFPPISPSPEEQLQPRECHTFSDPTCPGAPAVLHFPLVSDSFREYSAPGVRRTPEEAAAGEVNLSSSDSPYHYTKVTYSQEDVDKLLHLTHYNVCNNQEQLLEALRQAVQRRRQRRPH
Protein: Vinculin (Metavinculin) (P12003)
Organism: Gallus gallus (Chicken)
Function: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion.
Subcellular location: Cell membrane {ECO:0000269|PubMed:20584916}; Peripheral membrane protein {ECO:0000305|PubMed:20584916}; Cytoplasmic side {ECO:0000305|PubMed:20584916}. Cell junction, adherens junction {ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20584916}. Cell junction, focal adhesion {ECO:0000269|PubMed:20086044}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P85972}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:Q64727}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q64727}; Cytoplasmic side {ECO:0000250|UniProtKB:Q64727}. Cell projection, podosome {ECO:0000250|UniProtKB:Q64727}. Note=Recruitment to cell-cell junctions occurs in a myosin II-dependent manner (PubMed:20584916). Interaction with CTNNB1 is necessary for its localization to the cell-cell junctions (PubMed:20086044). {ECO:0000269|PubMed:20086044, ECO:0000269|PubMed:20584916}.
Interaction partners:
- Actin, cytoplasmic 1
- Talin 2.
- Talin-1
- Uncharacterized protein.
- Zyxin
- Focal adhesion kinase 1
- Uncharacterized protein.
- Filamin B
- Proto-oncogene tyrosine-protein kinase Src
- WH1 domain-containing protein.
Sequence:
MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVSAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVRAAQMLQADPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNTKSQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALALIDSKMNQAKGWLRDPNAPPGDAGEQAIRQILDEAGKAGELCAGKERREILGTCKTLGQMTDQLADLRARGQGATPMAMQKAQQVSQGLDLLTAKVENAARKLEAMTNSKQAIAKKIDAAQNWLADPNGGSEGEEHIRGIMSEARKVAELCEEPKERDDILRSLGEISALTAKLSDLRRHGKGDSPEARALAKQIATSLQNLQSKTNRAVANTRPVKAAVHLEGKIEQAQRWIDNPTVDDRGVGQAAIRGLVAEGRRLANVMMGPYRQDLLAKCDRVDQLAAQLADLAARGEGESPQARAIAAQLQDSLKDLKARMQEAMTQEVSDVFSDTTTPIKLLAVAATAPSDTPNREEVFEERAANFENHAARLGATAEKAAAVGTANKTTVEGIQATVKSARELTPQVVSAARILLRNPGNQAAYEHFETMKNQWIDNVEKMTGLVDEAIDTKSLLDASEEAIKKDLDKCKVAMANMQPQMLVAGATSIARRANRILLVAKREVENSEDPKFREAVKAASDELSKTISPMVMDAKAVAGNISDPGLQKSFLDSGYRILGAVAKVREAFQPQEPDFPPPPPDLEHLHLTDELAPPKPPLPEGEVPPPRPPPPEEKDEEFPEQKAGEAINQPMMMAARQLHDEARKWSSKPVTVINEAAEAGVDIDEEDDADVEFSLPSDIEDDYEPELLLMPTNQPVNQPILAAAQSLHREATKWSSKGNDIIAAAKRMALLMAEMSRLVRGGSGNKRALIQCAKDIAKASDEVTRLAKEVAKQCTDKRIRTNLLQVCERIPTISTQLKILSTVKATMLGRTNISDEESEQATEMLVHNAQNLMQSVKETVREAEAASIKIRTDAGFTLRWVRKTPWYQ
Protein: DNA polymerase I (POL I) (EC 2.7.7.7) (P00582)
Organism: Escherichia coli (strain K12)
Function: In addition to polymerase activity, this DNA polymerase exhibits 3'-5' and 5'-3' exonuclease activity. It is able to utilize nicked circular duplex DNA as a template and can unwind the parental DNA strand from its template.
Interaction partners:
- Beta sliding clamp
- Protein RecA
- DNA polymerase II
- DNA mismatch repair protein MutL
- Formamidopyrimidine-DNA glycosylase
- Nuclease SbcCD subunit D
- Exodeoxyribonuclease III
- DNA polymerase IV
- UvrABC system protein A
- DNA helicase II
Sequence:
MVQIPQNPLILVDGSSYLYRAYHAFPPLTNSAGEPTGAMYGVLNMLRSLIMQYKPTHAAVVFDAKGKTFRDELFEHYKSHRPPMPDDLRAQIEPLHAMVKAMGLPLLAVSGVEADDVIGTLAREAEKAGRPVLISTGDKDMAQLVTPNITLINTMTNTILGPEEVVNKYGVPPELIIDFLALMGDSSDNIPGVPGVGEKTAQALLQGLGGLDTLYAEPEKIAGLSFRGAKTMAAKLEQNKEVAYLSYQLATIKTDVELELTCEQLEVQQPAAEELLGLFKKYEFKRWTADVEAGKWLQAKGAKPAAKPQETSVADEAPEVTATVISYDNYVTILDEETLKAWIAKLEKAPVFAFDTETDSLDNISANLVGLSFAIEPGVAAYIPVAHDYLDAPDQISRERALELLKPLLEDEKALKVGQNLKYDRGILANYGIELRGIAFDTMLESYILNSVAGRHDMDSLAERWLKHKTITFEEIAGKGKNQLTFNQIALEEAGRYAAEDADVTLQLHLKMWPDLQKHKGPLNVFENIEMPLVPVLSRIERNGVKIDPKVLHNHSEELTLRLAELEKKAHEIAGEEFNLSSTKQLQTILFEKQGIKPLKKTPGGAPSTSEEVLEELALDYPLPKVILEYRGLAKLKSTYTDKLPLMINPKTGRVHTSYHQAVTATGRLSSTDPNLQNIPVRNEEGRRIRQAFIAPEDYVIVSADYSQIELRIMAHLSRDKGLLTAFAEGKDIHRATAAEVFGLPLETVTSEQRRSAKAINFGLIYGMSAFGLARQLNIPRKEAQKYMDLYFERYPGVLEYMERTRAQAKEQGYVETLDGRRLYLPDIKSSNGARRAAAERAAINAPMQGTAADIIKRAMIAVDAWLQAEQPRVRMIMQVHDELVFEVHKDDVDAVAKQIHQLMENCTRLDVPLLVEVGSGENWDQAH
Protein: Tuberculin related peptide (P96277)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Interaction partners:
- Cell envelope integrity protein Cei
- Uncharacterized protein Rv1351
- DUF3263 domain-containing protein
- Putative glutamate--cysteine ligase 2
- Superoxide dismutase
- Lon N-terminal domain-containing protein
- Probable conserved transmembrane protein
- Probable conserved lipoprotein LppL
- Uncharacterized protein Rv1109c
- DUF402 domain-containing protein
Sequence:
MLVTVGSMNERVPDSSGLPLRAMVMVLLFLGVVFLLLVWQALGSSPNSEDDSSAISTMTTTTAAPTSTSVKPAAPRAEVRVYNISGTEGAAARTADRLKAAGFTVTDVGNLSLPDVAATTVYYTEVEGERATADAVGRTLGAAVELRLPELSDQPPGVIVVVTG
Protein: Small conductance calcium-activated potassium channel protein 3 (SK3) (SKCa 3) (SKCa3) (KCa2.3) (P70605)
Organism: Rattus norvegicus (Rat)
Function: Forms a voltage-independent potassium channel activated by intracellular calcium. Activation is followed by membrane hyperpolarization. Thought to regulate neuronal excitability by contributing to the slow component of synaptic afterhyperpolarization.
Subcellular location: Cell membrane {ECO:0000269|PubMed:11245600, ECO:0000269|PubMed:14559917}; Multi-pass membrane protein. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000250|UniProtKB:P58391}.
Interaction partners:
- Calcium-activated potassium channel subunit alpha-1
- Calcium-activated potassium channel subunit beta-4
- Calcium-activated potassium channel subunit beta-1
- Calcium-activated potassium channel subunit beta-2
- Potassium channel subfamily U member 1
- Intermediate conductance calcium-activated potassium channel protein 4
- Small conductance calcium-activated potassium channel protein 2
- Protein kinase C gamma type
- Small conductance calcium-activated potassium channel protein 1
- Protein kinase C beta type
Sequence:
MDTSGHFHDSGVGDLDEDPKCPCPSSGDEQQQQQQPPPPSAPPAVPQQPPGPLLQPQPPQLQQQQQQQQQQQQQQQQQQQAPLHPLPQLAQLQSQLVHPGLLHSSPTAFRAPNSANSTAILHPSSRQGSQLNLNDHLLGHSPSSTATSGPGGGSRHRQASPLVHRRDSNPFTEIAMSSCKYSGGVMKPLSRLSASRRNLIEAEPEGQPLQLFSPSNPPEIIISSREDNHAHQTLLHHPNATHNHQHAGTTAGSTTFPKANKRKNQNIGYKLGHRRALFEKRKRLSDYALIFGMFGIVVMVIETELSWGLYSKDSMFSLALKCLISLSTIILLGLIIAYHTREVQLFVIDNGADDWRIAMTYERILYISLEMLVCAIHPIPGEYKFFWTARLAFSYTPSRAEADVDIILSIPMFLRLYLIARVMLLHSKLFTDASSRSIGALNKINFNTRFVMKTLMTICPGTVLLVFSISLWIIAAWTVRVCERYHDQQDVTSNFLGAMWLISITFLSIGYGDMVPHTYCGKGVCLLTGIMGAGCTALVVAVVARKLELTKAEKHVHNFMMDTQLTKRIKNAAANVLRETWLIYKHTKLLKKIDHAKVRKHQRKFLQAIHQLRGVKMEQRKLSDQANTLVDLSKMQNVMYDLITELNDRSEDLEKQIGSLESKLEHLTASFNSLPLLIADTLRQQQQQLLTAFVEARGISVAVGTSHAPPSDSPIGISSTSFPTPYTSSSSC
Protein: NAD(P)H-quinone oxidoreductase chain 4, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase, chain 4) (NADH-plastoquinone oxidoreductase chain 4) (P0C324)
Organism: Oryza sativa subsp. indica (Rice)
Subcellular location: Plastid, chloroplast thylakoid membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- NAD
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- NAD
- 4Fe-4S ferredoxin-type domain-containing protein
Sequence:
MSSFPWLTILVVLPIFAGSLIFFLPHRGNKIVRWYTMSICLLEFLLMTYAFCYHFQLEDPLIQLKEDSKWIDVFNFHWRLGIDGLSLGSILLTGFMTTLATLAAWPVTRNSRLFYFLMLAMYSGQIGLFSSRDLLLFFIMWELELIPVYLLLSMWGGKRRLYSATKFILYTAGGSIFFLIGVLGMGLYGSNEPRLDLERLINQSYPATLEILFYFGFLIAYAVKLPIIPLHTWLPDTHGEAHYSTCMLLAGILLKMGAYGLIRINMELLPHAHYLFSPWLVIIGAMQIIYAASTSLGQRNFKKRIAYSSVSHMGFIIIGIGSITNIGLNGAILQILSHGFIGATLFFLAGTACDRMRLVYLEELGGVSIPMPKIFTMFSSFSMASLALPGMSGFVAELVVFFGLITSPKFLLMPKMLITFVMAIGMILTPIYLLSMLRQMFYGYKLFHVPNENFEDSGPRELFLLICIFLPVIGIGIYPDFVLSLSVDRVEALLSNYYPK
Protein: Protein TAR1 (Transcript antisense to ribosomal RNA protein 1) (Q8TGM6)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: May be involved in mtDNA stability or mitochondrial gene expression regulation at the post-transcriptional level.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12414727}.
Interaction partners:
- Uncharacterized protein YLR154C-G
- Uncharacterized protein YLR157C-C
- Putative uncharacterized protein YLR154W-B
- Putative uncharacterized protein ART3
- Putative uncharacterized protein YLR154W-F
Sequence:
MRDSPTHKEQRAQNTMSDQMPFPFNNFTYFFTLFSKFFSSFHHCTCSLSVSRQYLALDGIYHPLRAAFPNNSTLRRHFTKNRTPRHTGFSPSMTSCSKEHRQGTAPKLPSPNYNSGTEGTRFQI
Protein: Flagellar biosynthetic protein FliR (P35537)
Organism: Bacillus subtilis (strain 168)
Function: Role in flagellar biosynthesis.
Subcellular location: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Bacterial flagellum basal body {ECO:0000250}.
Interaction partners:
- Flagellar biosynthetic protein FlhB
- Flagellar biosynthetic protein FliQ
- Flagellar biosynthetic protein FliP
- Flagellar biosynthesis protein FlhA
- Flagellum-specific ATP synthase
- Flagellar motor switch protein FliM
- Flagellar M-ring protein
- FlaA locus uncharacterized protein YlxG
- Flagellar biosynthetic protein FliZ
- Flagellar motor switch phosphatase FliY
Sequence:
MNSIIDLFPAFLLVFIRISAFFVTIPLFGHRNVPAVHRIGFAFFLAVICFSTIDKPPSLEIDEHYMLLAFKEALVGLCLGLIAYMMIAAVQIAGSFIDFQMGFSIANVIDPQTGAQSPLIGQFIYTMALLFMLSVNAHHLLLDGIYYSFQYISVDQAFPNFGDEKFAYFIAKSFNAMFIIAFQMSAPVVASLFLVDLALGIVARTVPQLNVFVVGLPLKIAVSFIMLIVCMSVIFVVVRNVFSLTIETMRNLLALVGVS
Protein: E3 ubiquitin-protein ligase PUB24 (EC 2.3.2.27) (Plant U-box protein 24) (RING-type E3 ubiquitin transferase PUB24) (U-box domain-containing protein 24) (Q9SF15)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: E3 ubiquitin-protein ligase that acts as negative regulator of the immunity triggered by the pathogen-associated molecular patterns (PAMPs), in association with PUB22 and PUB23.
Interaction partners:
- Exocyst complex component EXO70B2
- RING-H2 finger protein ATL40
- Squamosa promoter-binding-like protein 11
Sequence:
MDQEEEEIEIPNYFICPISLEIMKDPVTTVSGITYDRQNIVKWLEKVPSCPVTKQPLPLDSDLTPNHMLRRLIQHWCVENETRGVVRISTPRVPPGKLNVVEEIKNLKKFGQEALGREETLQKLEVLAMDGNNRRLMCECGVHKSLILFVVKCTSEDEDGRRRIKGLDESLRLLHLIGIPSNDAKTILMENDRVMESLTWVLHQEDFLSKAYTIVLLRNLTEYTSSHIVERLNPEIFKGIIGFLKDVVNSVNRTSPTVRETVQSSSRPSLGKTEPSKLDHSLVIKQAVTAALMILLETSSWSRNRSLLVDLGAVSELIELEISYTGEKRITELMLGVLSRLCCCANGRAEILAHRGGIAVVTKRLLRVSPAADDRAISILTTVSKFSPENMVVEEMVNVGTVEKLCSVLGMDCGLNLKEKAKEILKDHFDEWKKFPCIDITLLTKLLSISPKGPKI
Protein: GMP reductase 1 (GMPR 1) (EC 1.7.1.7) (Guanosine 5'-monophosphate oxidoreductase 1) (Guanosine monophosphate reductase 1) (P36959)
Organism: Homo sapiens (Human)
Function: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.
Interaction partners:
- GMP synthase
- Bifunctional purine biosynthesis protein ATIC
- Adenylosuccinate synthetase isozyme 2
- Adenylosuccinate synthetase isozyme 1
- AMP deaminase 3
- Adenine phosphoribosyltransferase
- 5'-nucleotidase
- AMP deaminase 2
- AMP deaminase 1
- Hypoxanthine-guanine phosphoribosyltransferase
Sequence:
MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFS
Protein: U3 small nucleolar ribonucleoprotein protein mpp10 (O13910)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the U3 small nucleolar ribonucleoprotein. Required for the early cleavages at sites A0, A1 and A2 during 18S ribosomal pre-RNA processing (By similarity).
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
- Uncharacterized protein C57A7.06
- rRNA biogenesis protein rrp5
- U3 small nucleolar RNA-associated protein 21 homolog
- Probable nucleolar complex protein 14
- Ribosome biogenesis protein bms1
- Uncharacterized protein C3B8.09
- U3 small nucleolar RNA-associated protein 22
- U3 small nucleolar RNA-associated protein 10
- rRNA 2'-O-methyltransferase fibrillarin
- Probable U3 small nucleolar RNA-associated protein 18
Sequence:
MTELINSEPTLFLFPNKEDSKQLVEKAIEVFSNIKIPSTSPIQTIVTKGLDNWQIYNQLALAAKYALDDLPQVDVENEDEEEDSITSFQDEDDETSHQELSDNSEMNNRDDADDEFLGFSGPENLEDVDESSAEDVSGDEAEIMNEEGQQIEQKKDAFGLNDGFFDIDNFNKQTLALEEEAVEEGVLGDEDDGIDLLMDPDENMEDSEDESNGPQADSIMYEDFFGPKTAAGRRELKKKKAESKRKRTSKPDFKNDVQQNVIEENNESSDNEYATFDRVKKDLFASDEEDDVSADQLSSYERDKARLTQQIRELEAENVAKKSWTMMGEATSKGRPSNSLLDVDLEFETGAKPVPVQTEETTETLEDLIKNRIISKTFDDVPKRAPVAVTEFRPSELFELNENKSQRSLAEEYEEEFLKKSNADTYKSEADKKKEKEHEEIKALFSEVSRTLDSLASWHYVPPPPESTVEIVSNAPTLAMEDVQPTAASDTMALAPQEVYKPSNENREGETITRSGIAISSTEMDHQQKQARRRRVRRKHAEKRKQMAEKRRNSGTEQVVRQLSKSNVEVIGKGGERKKVASNSNKYHPIVSSNQLKL
Protein: Combgap, isoform B (A1Z9M3)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MCAAQNPPPFGYTWGFADNGNRAAESVLEISPNINYTVSGESMPYLLSTDGSLAVQKDVKGLTAGGKNNVVRRMFVVNDPSFPPGTQRVITAGGASTVVKKQDNNQQVLSLDKNYLLVDPATAAAAAAAAGGDSGLAHHHTLTNGSIVDAKTGQTVLTAGSAAAKSHFSSIGALHLTQEECNEILIKRAIAAGHHQTHTITAADGSHHHASGGTPSDILPGISVQVQKVIQGLEDNEDSQGEAPNLKLEPGTLELSPKTELQESMHFSETDATIKKERPYSCDECGKSFLLKHHLTTHARVHTGERPHICTHCGKSFAHKHCLNTHLLLHSTERPYQCQECKKSFTLKHHLLTHSRVHSRERPFVCQECGRAFPLKRHLVTHSKFHAGERPYVCEECGESFAQENHLIMHSRFHGSLNPFVCAECGASFPRKFQLVNHGRIHGKIPHSCTVCGKEFLQKRTLVSHMRRVHTGEQAHPCVSCGEGFLTKAELHQHVRTAHNGVNPNTSSATIIANQQLQQAHHHQAGQQTHPQTITVVSNPGNSTLLTVSTTDANGVARPQFVCRECGSAFNSREALALHLRLHTGDKSLMTDLCALTAALPGHFLSTASLNPGTVVTANPNLVGQSPVPVQIISSTGQVMSQTTLVQAANSTHPQAVVTAVPTMPVHGQQQHLQHVAQQQQQQQQQQQQQQQHVVSVAPANKPKSHFCASCGKGFAAKHGLMQHNRRHPNGGCTVRTHVCECGKAFFQKNHLMLHQRQHLETKPAISQQQVC