wanglab/gogpt-training-data huggingface dataset:
Protein: Alpha/beta-Hydrolases superfamily protein (F4J010)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Glycerophosphodiester phosphodiesterase GDPD1, chloroplastic
- Glycerophosphodiester phosphodiesterase GDPD6
- Glycerophosphodiester phosphodiesterase GDPD2
- Glycerophosphodiester phosphodiesterase GDPD5
- Glycerophosphodiester phosphodiesterase GDPD3
- Alpha/beta-Hydrolases superfamily protein
- Phospholipase A
- Lecithin-cholesterol acyltransferase-like 4
- Phospholipase A
- Alpha/beta-Hydrolases superfamily protein
Sequence:
MSYSRQSMGSGSRSTRGYEFGRTYVVRPKGKHQATIVWLHGLGDNGSRILACSLITTSHFGSVSFCSSSQLLESLPLPNIKWICPTAPSRPVSLLGGFPCTAWFDVGEISEDLHDDIEGLDASAAHIANLLSAEPTDVKVGIGGFSMGAAIALYSTTCYALGRYGTGHAYTINLRATVGLSGWLPGWRSLRSKIESSNEVARRAASIPILLAHGTSDDVVPYRFGEKSAHSLAMAGFRQTMFKPYEGLGHYTVPKEMDEVVHWLVSRLGLEGSR
Protein: Volume-regulated anion channel subunit LRRC8C (Factor for adipocyte differentiation 158) (Leucine-rich repeat-containing protein 8C) (Q8TDW0)
Organism: Homo sapiens (Human)
Function: Non-essential component of the volume-regulated anion channel (VRAC, also named VSOAC channel), an anion channel required to maintain a constant cell volume in response to extracellular or intracellular osmotic changes. The VRAC channel conducts iodide better than chloride and can also conduct organic osmolytes like taurine. Plays a redundant role in the efflux of amino acids, such as aspartate and glutamate, in response to osmotic stress. The VRAC channel also mediates transport of immunoreactive cyclic dinucleotide GMP-AMP (2'-3'-cGAMP), an immune messenger produced in response to DNA virus in the cytosol. Channel activity requires LRRC8A plus at least one other family member (LRRC8B, LRRC8C, LRRC8D or LRRC8E); channel characteristics depend on the precise subunit composition.
Subcellular location: Cell membrane {ECO:0000269|PubMed:24790029, ECO:0000269|PubMed:28193731}; Multi-pass membrane protein {ECO:0000305}. Endoplasmic reticulum membrane {ECO:0000305|PubMed:24790029}. Note=In the absence of LRRC8A, resides primarily in a cytoplasmic compartment, probably the endoplasmic reticulum. Requires LRRC8A for expression at the cell membrane. {ECO:0000269|PubMed:24790029}.
Interaction partners:
- Volume-regulated anion channel subunit LRRC8A
- Volume-regulated anion channel subunit LRRC8B
Sequence:
MIPVTEFRQFSEQQPAFRVLKPWWDVFTDYLSVAMLMIGVFGCTLQVMQDKIICLPKRVQPAQNHSSLSNVSQAVASTTPLPPPKPSPANPITVEMKGLKTDLDLQQYSFINQMCYERALHWYAKYFPYLVLIHTLVFMLCSNFWFKFPGSSSKIEHFISILGKCFDSPWTTRALSEVSGEDSEEKDNRKNNMNRSNTIQSGPEDSLVNSQSLKSIPEKFVVDKSTAGALDKKEGEQAKALFEKVKKFRLHVEEGDILYAMYVRQTVLKVIKFLIIIAYNSALVSKVQFTVDCNVDIQDMTGYKNFSCNHTMAHLFSKLSFCYLCFVSIYGLTCLYTLYWLFYRSLREYSFEYVRQETGIDDIPDVKNDFAFMLHMIDQYDPLYSKRFAVFLSEVSENKLKQLNLNNEWTPDKLRQKLQTNAHNRLELPLIMLSGLPDTVFEITELQSLKLEIIKNVMIPATIAQLDNLQELSLHQCSVKIHSAALSFLKENLKVLSVKFDDMRELPPWMYGLRNLEELYLVGSLSHDISRNVTLESLRDLKSLKILSIKSNVSKIPQAVVDVSSHLQKMCIHNDGTKLVMLNNLKKMTNLTELELVHCDLERIPHAVFSLLSLQELDLKENNLKSIEEIVSFQHLRKLTVLKLWHNSITYIPEHIKKLTSLERLSFSHNKIEVLPSHLFLCNKIRYLDLSYNDIRFIPPEIGVLQSLQYFSITCNKVESLPDELYFCKKLKTLKIGKNSLSVLSPKIGNLLFLSYLDVKGNHFEILPPELGDCRALKRAGLVVEDALFETLPSDVREQMKTE
Protein: Pentraxin family member (A3KPH5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Secreted {ECO:0000256|RuleBase:RU362112}.
Interaction partners:
Sequence:
MLGFIFTLLILTPAAAEVGLGGKVLLFPTQSATSYVKLTPDKLLSLSAFTLCMRVATELQGGREVILFAYRTSEVDELNVWRENDGRLSMYIQSSSDAARFYLPPLSTFQTHLCVSWESATGLTAFWVDGRRSLYQIYKKDASVRPGGTVLLGQDPDSYVGSFDANQCFIGEITDVKLWDYVLSEIQIKALYSNQDPLVPAGNVFDWDTVKYDVVGNVTVANDNL
Protein: MIF4G domain-containing protein B (Q5EAQ1)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Functions in replication-dependent translation of histone mRNAs which differ from other eukaryotic mRNAs in that they do not end with a poly-A tail but a stem-loop. May participate in circularizing those mRNAs specifically enhancing their translation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
Interaction partners:
- Stem-loop-binding protein.
- DEAD/H
- Polyadenylate-binding protein-interacting protein 1
Sequence:
MENSSKEDYKIQSFDLETQKLLKTALKDPGSVDLEKVSSVIVDQSLKDQVFSREAGRICYTIVQAEAKQTNGSVFRRNLLNRLQQEFKAREETRKRSTQEWVCLVSFICNIFDYLKVNNMPMVALVHPVYDCLFRLAQSDALKNEEEVDCLVLQLHRIGDQLEKMNVQLMDELFNLLRDGFLLQEDLSSMGRLLLLEILEFRAGGWKLSDTAQKYYYSEVTD
Protein: Secretogranin-1 (Chromogranin-B) (CgB) (Secretogranin I) (SgI) [Cleaved into: PE-11; Peptide SR-17; Peptide HQ-34; Peptide KR-11; CCB peptide] (Q9GLG4)
Organism: Sus scrofa (Pig)
Function: Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides.
Subcellular location: Secreted. Note=Neuroendocrine and endocrine secretory granules.
Interaction partners:
- Chromogranin-A
- Secretogranin-2
- Secretogranin-3
- Neuroendocrine protein 7B2
- P/Homo B domain-containing protein
Sequence:
MQPAVLLGFLGATVVAAVSSMPVDNRNHNEEMVAHCIIEVLSNALSKSNAPPITPECRQVLKKGGKEVKDEEKGANENTRFEVRLLRDPADTSETQRPSGGREGAEAPSEDTQGPPGADVEGGGHSREGAGKPRGGPYSSDNPVAKEGKTRHSEKSEGQDREEEEGEKYQKRERGEEGSEERHLQEPGETQTAFLNQGNRATAKKKEEFESRYDAHSAGGPAKTHSRERSSQESGEETGSQDAAPGEPESPPEGQEAPEESQEDASLEVDKRRWRPRHHHGRSRPDRAPQEGSPPPEERGHPREESEESVLGLASPGGQRTRHPTHYPASEEEAEHGEEVRSSSSVQAPGDLVGARYGGRGGAEHRAARRPGEESPEQDRRVGASSELRNKGPGHSEESEEERGDEGQRHHRAWAGGPRADAPPDPAEEEQFWGEAHRPVPESQVDEARRHPQAKLRNYLNRGEENGEEGAPGRWQQPEDLQGPGEHAAEARLPGKPYAAHRIPEKKRLGELLNPYYVPPQWESSHFERKDNVGDNFLEGEDANGVTLNEKTFFPEYSYDWWEKKPFEEDVNWGYEERNLAPKLDLKRQYDRVAELDQLLHYRKKSAEFPDFYDSGEHLSPRHAAESEKERAGQGVLTEEEEKELENLAAMDLELQKIAEKFSGNRRG
Protein: Kin of IRRE-like protein 1 (Kin of irregular chiasm-like protein 1) (Nephrin-like protein 1) (Q6X936)
Organism: Rattus norvegicus (Rat)
Function: Required for proper function of the glomerular filtration barrier. It is involved in the maintenance of a stable podocyte architecture with interdigitating foot processes connected by specialized cell-cell junctions, known as the slit diaphragm (By similarity). It is a signaling protein that needs the presence of TEC kinases to fully trans-activate the transcription factor AP-1 (By similarity).
Subcellular location: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Predominantly located at podocyte slit diaphragm. {ECO:0000269|PubMed:12865409}.
Interaction partners:
- Nephrin
- CD2-associated protein
- Podocin
- Tight junction protein ZO-1
- FAT atypical cadherin 1
- Tyrosine-protein kinase Fyn
Sequence:
MTLENRSTCLMTCQSSLLPKKPRFLSQKMWAPHLVVAYLIFVTLALALPGTQTRFSQEPADQTVVAGHRAVLPCVLLNYSGIVQWTKDGLALGMGQGLKAWPRYRVVGSADAGQYNLEITDAELSDDASYECQATEAALRSRRAKLTVLIPPEDTRIDGGPVILLQAGTPYNLTCRAFNAKPAATIIWFRDGTQQEGAVTSTELLKDGKRETTISQLLIQPTDLDIGRVFTCRSMNEAIPNGKETSIELDVHHPPTVTLSIEPQTVLEGERVIFTCQATANPEILGYRWAKGGFLIEDAHESRYETNVDYSFFTEPVSCEVYNKVGSTNVSTLVNVHFAPRIVVYPKPTTTDIGSDVTLTCVWVGNPPLTLTWTKKDSNMVLSNSNQLLLKSVTQADAGTYTCRAIVPRIGVAEREVPLYVNGPPIISSEAVQFAVRGDGGKVECFIGSTPPPDRIAWAWKENFLEVGTLERYTVERTNSGSGVLSTLTINNVMEADFQTHYNCTAWNSFGPGTAIIQLEEREVLPVGIIAGATIGAGILLVFSFAALVFFLYRRRKGSRKDVTLRKLDIKVETVNREPLTMHSDREDDTTSISTATRVMKAIYSSFKDDVDLKQDLHCDTIETREEYEMKDPTNGYYNVRAHEDRPSSRAVLYADYRAPGPTRFDGRPSSRLSHSSGYAQLNTYSRAPASDYGTEPTPSGPSAPGGTDTTSQLSYENYEKFNSHPFPGAAGYPTYRLGYPQAPPSGLERTPYEAYDPIGKYATATRFSYTSQHSDYGQRFQQRMQTHV
Protein: Neutral ceramidase 3 (AtNCER3) (N-CDase 3) (NCDase 3) (EC 3.5.1.23) (Acylsphingosine deacylase 3) (N-acylsphingosine amidohydrolase 3) (F4KHQ8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes the sphingolipid ceramide into sphingosine and free fatty acid (By similarity). Promotes oxidative stress resistance.
Subcellular location: Secreted {ECO:0000250|UniProtKB:Q9VA70}. Endoplasmic reticulum {ECO:0000250|UniProtKB:F4HQM3}. Golgi apparatus {ECO:0000250|UniProtKB:Q0JL46}.
Interaction partners:
- Non-lysosomal glucosylceramidase
- Alkaline ceramidase
- Non-lysosomal glucosylceramidase
- Non-lysosomal glucosylceramidase
- Non-lysosomal glucosylceramidase
- Ceramide kinase
- Sphingosine kinase 1
- Sphingosine kinase 2
- Sphinganine C4-monooxygenase 2
- Sphinganine C4-monooxygenase 1
Sequence:
MTRWSMSMHCTLFLLFLLRLTCIFSDSDYLMGLGSYDITGPAADVNMMGYANMEQVASGVHFRLRARAFIVAEPYKKRIAFVNLDAGMASQLVTIKVIERLKQRYGELYTEENVAISGTHTHAGPGGYLQYILYLVTSLGFVHQSFNALVDGIEQSIIQAHENLRPGSILINKGELLDAGVNRSPSAYLNNPAHERSKYEYDVDKEMTLVKFVDDQWGPVARIMEDWFERENGCRSVDVESPRRVSSIISDPYDQDLMEMASSLLSTGGKTVTRMSSVARRVRSRFRHADKPRFVSAFCQTNCGDVSPNVLGAFCIDTGLPCEFNQSTCGGKNEQCYGRGPGYPDEFESTRIIGERQFKKAADLFTKASEEIQGKVDYRHAYVDFSQLEVTINGQNGGSEVVKTCPAAMGFGFAAGTTDGPGAFDFKQGDDQGNPFWRLVRNLLKNPTEEQVRCQRPKPILLDTGEMKQPYDWAPSILPVQILRIGQLVILCVPGEFTTMAGRRLRDAVKTVLKEGSNGREFSVVIAGLTNSYSQYIATFEEYQVQRYEGASTLYGPHTLSGYIQEFKKLANDLLSAQTTDPGPQPPDLLHKQISLLTPVVADMTPIGTAFGDVTSDVPRLSKFRKGADIVRVQFRSANPRNDLMTEGTFALVERWLEGRETWVPVYDDDDFCLRFKWSRPFKLSTQSTATIEWRIPETASPGVYRITHFGSAKTPISSIHHFSGSSSAFVVY
Protein: Uridine kinase (EC 2.7.1.48) (Cytidine monophosphokinase) (Uridine monophosphokinase) (P0A8F4)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm.
Interaction partners:
- Uracil phosphoribosyltransferase
- Uridine phosphorylase
- Cytidylate kinase
- Cytidine deaminase
- Uridylate kinase
- 5'/3'-nucleotidase SurE
- Protein UshA
- Pyrimidine-specific ribonucleoside hydrolase RihB
- Orotidine 5'-phosphate decarboxylase
- Pyrimidine 5'-nucleotidase YjjG
Sequence:
MTDQSHQCVIIGIAGASASGKSLIASTLYRELREQVGDEHIGVIPEDCYYKDQSHLSMEERVKTNYDHPSAMDHSLLLEHLQALKRGSAIDLPVYSYVEHTRMKETVTVEPKKVIILEGILLLTDARLRDELNFSIFVDTPLDICLMRRIKRDVNERGRSMDSVMAQYQKTVRPMFLQFIEPSKQYADIIVPRGGKNRIAIDILKAKISQFFE
Protein: Fatty acyl CoA synthetase 2 (EC 6.2.1.3) (Q9U403)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MNTASALNEIEVAVLQLMDEANSRESAPNEDIVQLRSKGSQNEAIPQTETENMSAIYRRAGVSGEEHTRLCREWYYGVNMPQKFMAICKKGGSRRAFAYRVLSNISKEVLRDQNGLERSYDITYFKETCYINYRVLWENIESFGRGLVELGISPNSRVAIYEETRWEWLATIYGIWSQNMVATTVYANLGEDALAYALRETGSRAIICNATNVPTLVRLVQSNRIPPLVIIYIGQLPPDTKSTHCRIISWLHVVDNGRLSDEPLRIPTDNDQVAFIMYTSGTTGDPKGVIHTHGSLISGVTACADYVNELIGPYEEGESYCAYLPLAHIFEFGVVNIFLARGSFVGFGNPRTLLDTYTRPHGDYREYKPVFTIGVPRVYDTIKKTVESQLAPRGTLQRRIFEHAFQTRLRALKKGEETPYWNRLIFSPFRSMLGGKMKTMLSAGGPLSAPTQTFLHVVFGIMPQGWGLTETVCVGTKQVAGDMEPAAAGKQERTCEMRLLDVEGYKHTDEPDPRGEILLRGPFLFKGYYKQEELTKEVLDEDGWFHTGDVGSIGPNGTLRIIGRVKALAKNVLGEYVAMEALESMYAHNSLSMPNGVCVLVHPDRPYICALVLTDEAKVVAFTREHGLKGKYPEVLQDPEFQKKATASFQETARASDRQKFEIVRHVRLLSDEWTPENGVLTAAGKLKRRVIDEKYTDTIVSLFVEEC
Protein: Microtubule-associated protein 2 (MAP-2) (P20357)
Organism: Mus musculus (Mouse)
Function: The exact function of MAP2 is unknown but MAPs may stabilize the microtubules against depolymerization. They also seem to have a stiffening effect on microtubules.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:17984326}.
Interaction partners:
- Tubulin beta-3 chain
- Disks large homolog 4
- Synaptophysin
- Neurofilament light polypeptide
- Synapsin-1
- Glial fibrillary acidic protein
- RNA binding protein fox-1 homolog 3
- Neuromodulin
- Nestin
- Neuronal migration protein doublecortin
Sequence:
MADERKDEGKAPHWTSASLTEAAAHPHSPEMKDQGGAGEGLSRNANGFPYREEEEGAFGEHRSQGTYSDTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKGEQEKEAQHKDQPAALPLAAEETANLPPSPPPSPASEQTATVEEDLLTASKMEFPEQEKFPSSFAEPLDKGEMEFKMPSKPGEDFEHAALVPDTSKTPQDKKDLQGMEGEKLPPVPFAQTFGTNLEDRKQSTEPSIVMPSIGLSAEPPAPKEPKDWFIEMPTESKKDEWGLAAPISPGPLTPMREKDVLEDIPRWEGKQFDSPMPSPFHGGSFTLPLDTMKNERVSEGPRPFAPVFFQSDDKVSLQDPSALATSKESSKDEEPLKDKADKVADVSISEVTTLLGNVHSPVVEGYVGENISGEVKVTTDQEKKETSAPSVQEPTLTETEPQTKLDEKSTVSIEEAVAKKEESFKLRDDKTGVIQTSTEQSFSKEDQKGQEHTIDELKQDSFPISLEQAVTDAAMTSKTLGKVTSEPEAVSERREIQGLFEEKTADKNKLEGAGSATIAEVEMPFYEDKSGMSKYFETSALKEDMTRSTELGSDYYELSDSRGSAQESLDTISPKNQHDEKELQAKASQPSPPAQEAGYSTLAQSYTPDHPSELPEEPSSPQERMFTIDPKVYGEKRDLHSKNKDDLTLSRSLGLGGRSAIEQRSMSINLPMSCLDSIALGFNFGRGHDLSPLASDILTNTSGSMDEGDDYLPPTTPAVEKMPCFPIESKEEEDKAEQAKVTGGQTIQVETSSESPFPAKEYYKNGTVMAPDLPEMLDLAGTRSRLASVSADAEVARRKSVPSEAMLAESSTSLPPVADESPVTVKPDSQLEDMGYCVFNKYTVPLPSPVQDSENLSGESGSFYEGTDDKVRRDLATDLSLIEVKLAAAGRVKDEFTAEKEASPPTSADKSRLSREFDHDRKANDKLDTVLEKSEEHIDSKEHAKESEEMGGKVELFGLGITYDQASTKELITTKDTSPEKTEKGLSSVPEVAEVEPTTKADQGLDFAATKAEPSQLDIKVSDFGQMASGMNVDAGKAIELKFEVAQELTLSSEAPQEADSFMGVESGHIKEGGKVNETEVKEKVTKPDLVHQEAVDKEESYESSGEHESLTMESLKPDEGKKETSPETSLIQDEVALKLSVEIPCPPPVSEADLSTDEKGEVQMEFIQLPKEESTETPDIPAIPSDVTQPQPEAIVSEPAEVPSEEEEIEAGGEYDKLLFRSDTLQISDLLVSESREEFVETCPGELKGVVESVVTIEDDFITVVQTTTDEGESGSHSVRFAAPAQPEEERRPRPHDEELEIEMAAEAQAEPKDGSPDAPATPEKEEVAFSEYKTETYDDYKDETTIDDSIMDADSLWVDTQDDDRSILTEQLETIPKEERAEKDARRPSLEKHRKEKPFKTGRGRISTPERKVAKKEPSTVSRDEVRRKKAVYKKAELAKKSEVQAHSPSRKLILKPAIKYTRPTHLSCVKRKTTAASGDLAQAPGAFKQAKDKVTDGISKSPEKRSSLPRPSSILPPRRGVSGDREENSFSLNSSISSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPGTPKSGILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVQIVTKKIDLSHVTSKCGSLKNIRHRPGGGRVKIESVKLDFKEKAQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPSRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL
Protein: DNA-binding protein (F4JXC7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DCD
- Uncharacterized protein At5g48340
- F-box/kelch-repeat protein At1g64840
- Glycosyltransferase
- Vacuolar protein sorting-associated protein 35C
- AT4g33380/F17M5_140
- Tubulin beta-6 chain
Sequence:
MSYESKGFWVMKNNEHTSEEDSVYDHSTRDDSKRPHPWFVDSSRSEMFPNKKQAVQDPVVGLGKSNVGLPLWESSSVFQSVSNQFMDRLLGAEMPPRPLLFGDRDRTEGCSHHHQNKSIAESYMEDTSVELSISNGVEVAGGCFGGDGNRKLPVSRVKETMSTHVALEGHSQRKIESSSIQACSRENESSYINFALAGHPYGNEDSQGITFGEINDEHGVGSTSNVVGNYQSYVQDPIGTLDIVYDQETGSSQTSSGVVSEQQVAKPSLGSLPKTKAEAKSSKKEASTSFPSNVRSLISTGMLDGVPVKYVSVSREELRGVIKGSGYLCGCQTCDFTKVLNAYAFERHAGCKTKHPNNHIYFENGKTIYQIVQELRNTPESILFDVIQTVFGSPINQKAFRIWKESFQAATRELQRIYGKEERSF
Protein: Sterol carrier protein 2 (SCP-2) (Acetyl-CoA C-myristoyltransferase) (EC 2.3.1.155) (Non-specific lipid-transfer protein) (NSL-TP) (Propanoyl-CoA C-acyltransferase) (EC 2.3.1.176) (SCP-2/3-oxoacyl-CoA thiolase) (SCP-2/thiolase) (EC 2.3.1.16) (SCP-chi) (SCPX) (Sterol carrier protein X) (SCP-X) (P07857)
Organism: Bos taurus (Bovine)
Function: Plays a crucial role in the peroxisomal oxidation of branched-chain fatty acids. Catalyzes the last step of the peroxisomal beta-oxidation of branched chain fatty acids and the side chain of the bile acid intermediates di- and trihydroxycoprostanic acids (DHCA and THCA) (By similarity). Also active with medium and long straight chain 3-oxoacyl-CoAs. Stimulates the microsomal conversion of 7-dehydrocholesterol to cholesterol and transfers phosphatidylcholine and 7-dehydrocholesterol between membrances, in vitro (By similarity). Isoforms SCP2 and SCPx cooperate in peroxisomal oxidation of certain naturally occurring tetramethyl-branched fatty acyl-CoAs (By similarity).
Subcellular location: [Isoform SCP2]: Peroxisome {ECO:0000250|UniProtKB:P32020}. Cytoplasm {ECO:0000250|UniProtKB:P22307}. Mitochondrion {ECO:0000250|UniProtKB:P22307}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P32020}. Mitochondrion {ECO:0000250|UniProtKB:P32020}.; SUBCELLULAR LOCATION: [Isoform SCPx]: Peroxisome {ECO:0000250|UniProtKB:P11915}.
Interaction partners:
- Peroxisomal targeting signal 1 receptor
- Peroxisomal acyl-coenzyme A oxidase 1
- Acyl-coenzyme A oxidase
- Acetyl-CoA acyltransferase 1
- PEX5-related protein
- Peroxisomal multifunctional enzyme type 2
- Enoyl-CoA delta isomerase 2
- Bile acid-CoA:amino acid N-acyltransferase
- long-chain-fatty-acid--CoA ligase
- Peroxisomal bifunctional enzyme
Sequence:
MSLVASQSPLRNRVFVVGVGMTKFTKPGVENRDYPDLAKEAGQKALADAQIPYSAVEQACIGYVYGDSTSGQRAIYHSLGLTGIPIINVNNNCSTGSTALFMARQLIQGGLADCVLALGFEKMVKGPIAVNIQDKANPIDKHIEVMVNKYGLSPSPVAPQMFGNAGKEHMEKYGTTLEHFAKIGWKNHKHSVNNPYSQFQKEYSLDEVMTSRKIFDFLTVLQCCPTSDGAAAAILASEAFVQKHNLKPKAVEILAQEMVTDMPSSFEGKSIIKMVGFDMSKEAARRCYEKSGLRPSDIDVIELHDCFSANELITYEALGLCPEGQGGKLVERGDNTYGGKWVINPSGGLISKGHPLGATGLAQCVELCWHLRGEAGKRQVPGAKVALQHNIGIGGAVVVTLYKMGFPEAARTHQIEAAPTSSSVDGFKANLVFKEIEKKLEDEGEQFVKKIGGIFAFKVKDGPGGKEATWVVDVKNGKGSVLPNSDKKADCTITMADSDLLALMTGKMNPQTAFFQGKLKINGNMGLAMKLQNLQLQPGKAKL
Protein: Large subunit ribosomal protein L36a, isoform CRA_a (RCG38013, isoform CRA_c) (Rpl36a protein) (B2RYQ8)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MVNVPKTRRTFCKKCGKHQPHKVTQYKKGKDSLYAQGKRRYDRKQSGYGGQTKPIFRKKAKTTKKIVLRLECVEPNCRSKRMLAIKRCKHFELGGDKKRKGQVIQF
Protein: Lysosome membrane protein 2-C (Lysosome membrane protein II-3) (LIMP II-3) (Q55FQ9)
Organism: Dictyostelium discoideum (Social amoeba)
Function: May act as a lysosomal receptor (By similarity). May be involved role in macropinocytosis and fluid phase exocytosis.
Subcellular location: Lysosome membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Note=Localizes to membranes of endolysosomal vesicles and macropinosomes. {ECO:0000269|PubMed:11489884}.
Interaction partners:
Sequence:
MVANNKGLLIAGLLLSVIGAALFVISLALLPSVLNVATNNAIVDAVIVDSFKSQRYNDWAGQKSVDNYFKQYYYLWNLTNPNEVLNGKNCNFEKIGPFNYKYEWNNSKVSFSDDGNLINYIQSKSYKWIEGEDSLNPFTVSTTNFNPAYLGLLSTLSKNSITLGMTAEDLLYTLASAPQTKQFLEYLSSDNFTMIAYFYNGPKYFNQQYQLLLSTINNNLTTTPTIYFLEQWSNSTIIPTNGNSSLWDNMLISYGLDSPSGISLQSALEILNPMNQYSLLNSTNGISYWINAVFNGPNSNSYQILEQELGINQAQLTLVMIWWLKGFNDQYTMSQLLKQCEIESIELLGVCQFITTIPLGYKSISQFNITNLPWLEPIEIPIAMGTNLTISTNEAQSNLFNDSIDDSLLTIHGLGLFLEQMSTNSNNFTKWNLTNNDAMTMIGYFLSYIPNTTGYSIKSVQSFYNTSGLIVTRTANEWLWDCQDDLLDYLGIDQQCSFQQNNTIFKPSTVYTGKKDLSLTNQYQQFQEQSTLTIWNGTVNVTGFVENGQMAPLVQDNLPQSLTIFEENILRPLSLVHSSSSSVMGVSTQRYYLPNQSFPIDPVFNNSINGFANLTGLFNGVPIYVSLWDMYGVPIEYSSLYINGLNQTYENAEIPLDLEPITGNTLYYNLKLQINLQIPSNANSLWFSSLGNWTNIFSPTNSNSFGIFYPSLKIGQTATASTNDINLLKQQFKQIQTVKIAPVVVVSIFGGILLIAGLVMAINGFRKTFYNNNQYNGYNIIN
Protein: Sm-like protein LSM2 (AtLSM2) (U6 snRNA-associated Sm-like protein LSM2) (Q1H595)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Component of LSM protein complexes, which are involved in RNA processing. Component of the cytoplasmic LSM1-LSM7 complex which is involved in mRNA degradation by promoting decapping and leading to accurate 5'-3' mRNA decay. The cytoplasmic LSM1-LSM7 complex regulates developmental gene expression by the decapping of specific development-related transcripts. Component of the nuclear LSM2-LSM8 complex which is involved splicing nuclear mRNAs. LSM2-LSM8 binds directly to the U6 small nuclear RNAs (snRNAs) and is essential for accurate splicing of selected development-related mRNAs through the stabilization of the spliceosomal U6 snRNA. Plays a critical role in the regulation of development-related gene expression.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:23221597}. Nucleus {ECO:0000269|PubMed:23221597}.
Interaction partners:
- Sm-like protein LSM6A
- Sm-like protein LSM3A
- Small nuclear ribonucleoprotein Sm D2
- Sm-like protein LSM1A
- Sm-like protein LSM7
- Sm-like protein LSM36B
- Sm-like protein LSM4
- Sm-like protein LSM5
- Sm-like protein LSM8
- Sm-like protein LSM3B
Sequence:
MLFFSYFKDLVGQEVTVELKNDLAIRGTLHSVDQYLNIKLENTRVVDQDKYPHMLSVRNCFIRGSVVRYVQLPKDGVDVDLLHDAARREARGG
Protein: Parvalbumin (A0A060X840)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
- Protein kinase domain-containing protein
- Protein kinase domain-containing protein
- Protein kinase domain-containing protein
- Guanylate kinase-like domain-containing protein
- Peripheral plasma membrane protein CASK
- Protein kinase domain-containing protein
- Guanylate kinase-like domain-containing protein
- Protein kinase domain-containing protein
- Protein kinase domain-containing protein
- Myosin motor domain-containing protein
Sequence:
MSFAGLNDADVAAALAACAAADSFNHKAFFAKVGLASKSNDDVKKAFYVIDQDKSGFIEEDELKLFLQNFSASARALTDAETKAFLADGDKDGDGMIGVDEFAAMIKG
Protein: Nascent polypeptide-associated complex subunit alpha (NAC-alpha) (Alpha-NAC) (P87147)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the nascent polypeptide-associated complex (NAC), a dynamic component of the ribosomal exit tunnel, protecting the emerging polypeptides from interaction with other cytoplasmic proteins to ensure appropriate nascent protein targeting. The NAC complex also promotes mitochondrial protein import by enhancing productive ribosome interactions with the outer mitochondrial membrane and blocks the inappropriate interaction of ribosomes translating non-secretory nascent polypeptides with translocation sites in the membrane of the endoplasmic reticulum. Ucp15 may also be involved in transcription regulation (By similarity).
Subcellular location: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Note=Predominantly cytoplasmic, may also transiently localize to the nucleus. {ECO:0000250}.
Interaction partners:
- Nascent polypeptide-associated complex subunit beta
- Large ribosomal subunit protein eL14
- Elongation factor 1-gamma
- Large ribosomal subunit protein eL13
- Large ribosomal subunit protein eL8
- Large ribosomal subunit protein eL18A
- Large ribosomal subunit protein eL31
- Large ribosomal subunit protein eL6
- Large ribosomal subunit protein uL29
- Large ribosomal subunit protein uL24
Sequence:
MSVESQPVEKISELPAGSTTVVHAEKAQKLIQKLGLKRVEGITRVAMRRPKNILLIINEPIVYKSSNNAYIVLGKVTVEDMAAQARAFNESQKQATETKEEAAITEESGDAQPADTAKIEESFEQEKAVDETGVDAKDIELVMAQANVSRAKAVTALKENNSDVVNAIMSLTM
Protein: Mitogen-activated protein kinase pmk-1 (EC 2.7.11.24) (Stress-activated protein kinase pmk-1) (p38 MAP kinase 1) (Q17446)
Organism: Caenorhabditis elegans
Function: Serine/threonine kinase which responds to activation by environmental stress and pro-inflammatory cytokines by phosphorylating downstream targets. As part of a MAP kinase signaling pathway, plays a role in modulation of lifespan and immunity. Phosphorylates skn-1 which probably regulates skn-1 nuclear translocation in response to oxidative stress. Probably by activating skn-1, involved in the up-regulation of gcs-1 and glutathione-S-transferase gst-4 expression upon bacteria infection. Up-regulates expression of gcs-1 in intestinal cells upon arsenite treatment. Functions downstream of the MAPKK sek-1 and the MAPKKK nsy-1 as the MAP kinase which regulates pathogen resistance and responses to oxidative stress. Required for expression of antimicrobial peptide nlp-29 in response to fungal infection or physical injury. Involved in resistance to the nematotoxic C.cinerea galectin (Cgl2). May play a redundant role with other MAP kinases in susceptibility to anoxia, downstream of tir-1/nsy-1. Phosphorylates transcription factor rnt-1 during oxidative stress which results in rnt-1 stabilization in the intestine. Phosphorylates transcription factor atf-7 during pathogen infection resulting in modulation of target genes. Probably downstream of nsy-1 and sek-1, involved in germline apoptosis induced by heavy metals, such as Cu(2+).
Subcellular location: Nucleus {ECO:0000269|PubMed:20369020}. Note=Accumulates in nucleus in response to heavy metals, such as cadmium. {ECO:0000269|PubMed:20369020}.
Interaction partners:
- Protein skinhead-1
- Tyrosine-protein phosphatase vhp-1
- Forkhead box protein O
- MAP kinase-activated protein kinase mak-2
- Dual specificity mitogen-activated protein kinase kinase sek-1
- Transcription factor atf-7
- NAD
- Dual specificity mitogen-activated protein kinase kinase mek-1
- Dual specificity protein phosphatase lip-1
- Putative ribosomal protein S6 kinase alpha-2
Sequence:
MFPQTTMDHILHPTPREGYYVVELNRSVWVVPNYYINLTPIGTGAYGTVCAAECTRSGTRVAIKKFNRPFQSIIHARRTYRELRLLRCMCHENIIDLLDVFTPNENVNDIEDVYFVSMLMGADLSNILKIQRLNDDHIQFLVYQILRGLKYIHSADIIHRDLKPSNIAVNEDCELKILDFGLARQTDSEMTGYVATRWYRAPEIMLNWMHYTQTVDVWSVGCILAELITGKTLFPGSDHIDQLTRIMSVTGTPDEEFLKKISSEEARNYIRNLPKMTRRDFKRLFAQATPQAIDLLEKMLHLDPDRRPTAKEAMEHEYLAAYHDETDEPIAEEMDLNDDVRADTIDEWKKIIWEEISDFQKNVAFADEEEDEEKMES