wanglab/gogpt-training-data huggingface dataset:
Protein: Mitogen-activated protein kinase kinase kinase 20 (EC 2.7.11.25) (Leucine zipper- and sterile alpha motif kinase ZAK) (Leucine zipper- and sterile alpha motif-containing kinase) (MLK-like mitogen-activated protein triple kinase) (Mitogen-activated protein kinase kinase kinase MLT) (Mixed lineage kinase-related kinase) (MLK-related kinase) (MRK) (Sterile alpha motif- and leucine zipper-containing kinase AZK) (Q9ESL4)
Organism: Mus musculus (Mouse)
Function: Stress-activated component of a protein kinase signal transduction cascade that promotes programmed cell death in response to various stress, such as ribosomal stress, osmotic shock and ionizing radiation. Acts by catalyzing phosphorylation of MAP kinase kinases, leading to activation of the JNK (MAPK8/JNK1, MAPK9/JNK2 and/or MAPK10/JNK3) and MAP kinase p38 (MAPK11, MAPK12, MAPK13 and/or MAPK14) pathways. Activates JNK through phosphorylation of MAP2K4/MKK4 and MAP2K7/MKK7, and MAP kinase p38 gamma (MAPK12) via phosphorylation of MAP2K3/MKK3 and MAP2K6/MKK6. Involved in stress associated with adrenergic stimulation: contributes to cardiac decompensation during periods of acute cardiac stress (By similarity). May be involved in regulation of S and G2 cell cycle checkpoint by mediating phosphorylation of CHEK2 (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:11042189}. Nucleus {ECO:0000269|PubMed:11042189}. Note=Appears to shuttle between nucleus and cytoplasm. {ECO:0000269|PubMed:11042189}.
Interaction partners:
- Dual specificity mitogen-activated protein kinase kinase 7
- Dual specificity mitogen-activated protein kinase kinase 3
- Serine/threonine-protein kinase N1
Sequence:
MSSLGASFVQIKFDDLQFFENCGGGSFGSVYRAKWISQDKEVAVKKLLKIEKEAEILSVLSHRNIIQFYGVILEPPNYGIVTEYASLGSLYDYINSNRSEEMDMEHIMTWATDVAKGMHYLHMEAPVKVIHRDLKSRNVVIAADGVLKICDFGASRFHNHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKNERLTIPSSCPRSFAELLHQCWEADAKKRPSFKQIISILESMSNDTNLPDQCNSFLHNKAEWRCEIEATLERLKKLERDLSFKEQELKERERRLKMWEQKLTEQSNTPLLPSFEIGAWTEDDVYFWVQQLVRKGESSVEMSGYASLFKENNITGKRLLLLEEEDLKDMGIVSKGHIIHFKSAIEKLTHDYLNLFHFPPLIKDSGGEPEENEEKIVNLELVFGFHLKPGTGPQDCKWKMYMEMDGDEVAITYIKDVTFNTSLPDAEILKMTKPPFVMEKWIVGIAEDQTVECTVTYENDVRTPKLTKHVHSIQWDRTKPQDEVKAVQLAIQTLFSSSEGNPGSRSDSSADCQWLDTLRMRQIASHTSLQRSQSNPILGSPFFPYFANQDSYAAAVRRTQTPVKYQQITPSINPSRSSSPTQYGLSRNFSSLNLSSRDSGFSSLNDSSSERGRYSDRSRNKYYRGSVSLNSSPKGRYGGKSQHSTPSRERYSGKFYRLPQSALNTHQSPDFKRSPNDHDRRVPRTIPGMPLHPETASKAGEEESRVSEGGWTKVEYRKKTHRQLSAKTSKERTRGNYRGRRNF
Protein: Probable importin c550.11 (O59809)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Active in protein import into the nucleus.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus envelope {ECO:0000269|PubMed:16823372}.
Interaction partners:
- GTP-binding nuclear protein spi1
- Importin subunit beta-1
- Probable importin subunit beta-4
- Exportin-1
- Importin subunit beta-2
- Protein argonaute
- Exportin-T
- Ran-specific GTPase-activating protein 1
- Importin subunit beta-3
- Uncharacterized protein C11G11.07
Sequence:
MSLVEHFDATLSADPNTRTKAELSLKQLEKEPSFVLAVLQLLSSQEISLPTQQAAVIYLKNRVSRSWSSIDDAPSPLDIPEEQKALFRQNILPVLLQSPMSTRSHLMAILNIILSTDFPEYWPGFSEYTSNLVHSTERCEVYAGLICFHELAKVYRWRLDDRQRDIGPLVAALFPTILQLGQGLINLEDNDSAEMLRLILKTFKSVIALELPPELLANDMILSWIQLLLAVVQKPLPESLMSLEPEVRQSHVWHKCKKWAYYSLNRIFTRYGEPSSLVGDSANKYRAFAKNFITNVVPNILETYIQQTILWTQGQLWLSPRVLYFLGCFYEECVKPKSTWALLKPHLQLLIGSFVFPQLCMSEEDEELWELDPVEFIHKYIDIYDDFNSADVAASRFLVKLASKRKKYTFMGILSFASDILNQYAASPPNEKNPRQKEGALRMVAAVSNSILSKNSPVAGMMQDFLVAHVMPEFTSPVGYLRSRACEMINRFSEIDWSDKSQLLNAYQAVLNCLQDNDLPVRIQAALALQPLMRHLEVHDVMTAHVPIIMQNLLFLANEVDIDALSSCMEEFVSSFSHELTPFASQLAKQLRNTFVKLMQETMDESTTVDDFDSLVDDKSIAAIGILNTLSTMILSLENTVDVLREIEAILLPMINFVLDNNIFDVYAELFEIIDGCTFASKEISPIMWGVYEKLQKVLKESGIEFVEEATPALSNFITYGGKEFASRPDYIAVMVDIIMQVFNSEHLAVNDRVSACKLTELLMLNYRGLLDQYVPAFIEVAGNLLLVTEKPTSQTYRVFLLEVIINALYYNPSMSLGVLEMHQWTLPFFALWFENIPSFTRVHDKKLSLVAILSVISLGAQQVAVAIQDSWGNIMKVMITLLNTLPEALAARAELEKEYDGETFNLSGSGWNDGIDWEADDDEGVDDFAVEYGGPDLGGEISADVVDDFDEFEHFQGNYLLDEDPLFHTLLDQVDPFSLFQEFMVHLKDNSPVTLQDLVKNLEASEQQSLQRLVTEKPSTLAVASDKT
Protein: Paraneoplastic antigen Ma3 (Q9UL41)
Organism: Homo sapiens (Human)
Subcellular location: Nucleus, nucleolus {ECO:0000250}.
Interaction partners:
Sequence:
MPLTLLQDWCRGEHLNTRRCMLILGIPEDCGEDEFEETLQEACRHLGRYRVIGRMFRREENAQAILLELAQDIDYALLPREIPGKGGPWEVIVKPRNSDGEFLNRLNRFLEEERRTVSDMNRVLGSDTNCSAPRVTISPEFWTWAQTLGAAVQPLLEQMLYRELRVFSGNTISIPGALAFDAWLEHTTEMLQMWQVPEGEKRRRLMECLRGPALQVVSGLRASNASITVEECLAALQQVFGPVESHKIAQVKLCKAYQEAGEKVSSFVLRLEPLLQRAVENNVVSRRNVNQTRLKRVLSGATLPDKLRDKLKLMKQRRKPPGFLALVKLLREEEEWEATLGPDRESLEGLEVAPRPPARITGVGAVPLPASGNSFDARPSQGYRRRRGRGQHRRGGVARAGSRGSRKRKRHTFCYSCGEDGHIRVQCINPSNLLLVKQKKQAAVESGNGNWAWDKSHPKSKAK
Protein: POU domain class 2-associating factor 1 (B-cell-specific coactivator OBF-1) (BOB-1) (OCA-B) (OCT-binding factor 1) (Q16633)
Organism: Homo sapiens (Human)
Function: Transcriptional coactivator that specifically associates with either POU2F1/OCT1 or POU2F2/OCT2. It boosts the POU2F1/OCT1 mediated promoter activity and to a lesser extent, that of POU2F2/OCT2. It recognizes the POU domains of POU2F1/OCT1 and POU2F2/OCT2. It is essential for the response of B-cells to antigens and required for the formation of germinal centers. Regulates IL6 expression in B cells as POU2F2/OCT2 coactivator (By similarity).
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- POU domain, class 2, transcription factor 1
- B-cell antigen receptor complex-associated protein alpha chain
- Marginal zone B- and B1-cell-specific protein
- B-lymphocyte antigen CD20
- Paired box protein Pax-5
- POU domain, class 2, transcription factor 2
- Transcription factor Spi-B
- Immunoglobulin J chain
- Tumor necrosis factor receptor superfamily member 17
- Tyrosine-protein kinase SYK
Sequence:
MLWQKPTAPEQAPAPARPYQGVRVKEPVKELLRRKRGHASSGAAPAPTAVVLPHQPLATYTTVGPSCLDMEGSVSAVTEEAALCAGWLSQPTPATLQPLAPWTPYTEYVPHEAVSCPYSADMYVQPVCPSYTVVGPSSVLTYASPPLITNVTTRSSATPAVGPPLEGPEHQAPLTYFPWPQPLSTLPTSTLQYQPPAPALPGPQFVQLPISIPEPVLQDMEDPRRAASSLTIDKLLLEEEDSDAYALNHTLSVEGF
Protein: 6-phosphofructo-2-kinase/fructose-2, 6-biphosphatase, putative (EC 2.7.1.105, EC 3.1.3.46) (Q57WN9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MDCLVCSGRLPVQTAFNRMAAIQEEIARIDDQLATLYLTENMAATSPKEAPTDESIDQTIAHMLAVELCQLSASGDTVGIRVLLSGGADCNCVDYHGRTPLHLACLMGHVTVARVLLEFGADVTATDKEGKTPMDLAVRSDTREIVELLMSHCICDSSGGARSPPQELDGVLGEGLQEDSPLTATHPDFSSLPRPMMGSLIVIMVGLPARGKMYTARQIQRYFQWNGLQSSIFTYDNYVHQLAPRQPASCDITQDVDMELRVAKAIAHDMTHFIHQEDGVAVLAGSNVTSVRRMALFNAVMETGHIRQGRVVFVEVINTVSERIRNNVLLAKEMVTGASDRFVEEYYEKMEQLEAVYTSLDPVVDKDLTYIRVENGEVFSLNNISGWMPSRLAYMLHNLNPCSHNIYLTRSGEYIDLVDQRIGGNSPLTERGRAYGRAIFEYFRREHGAERFVVMSSCAVRCTETVHYFDKRNELSQDPYFASGSTSPAVNCRVSYLPTLDDINRGDCEGMLLSDVRRTMPGTLRNILDDPYLTAWPNGECTHQVFNARLEPLIHDIQASDHSVLVVSHLHLLQGLYSYFVCKDGNVIAPQNAYTIDIPLECVVKIRRVGDNRVAEIIDLSHEVDRIAQLYHGGAQRHCRRTEDFNKL
Protein: Terpineol synthase, chloroplastic (EC 4.2.3.111) (1,8-cineol synthase, chloroplastic) (EC 4.2.3.108) (Alpha-pinene synthase) (EC 4.2.3.-) (Beta-myrcene synthase) (EC 4.2.3.15) (Limonene synthase) (EC 4.2.3.-) (Sabinene synthase) (EC 4.2.3.-) (H2ELN1)
Organism: Nicotiana langsdorffii (Langsdorff's tobacco)
Function: Monoterpene synthase (TPS) involved in the biosynthesis of monoterpene natural products of the 'cineole cassette', volatile compounds present in floral scent. Catalyzes the conversion of (2E)-geranyl diphosphate (GPP) into alpha-terpineol and, as minor products, sabinene, beta-myrcene, limonene, alpha-pinene and 1,8-cineole.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
RRSGNYQPTMWDFEYIQSIHNDYAGDKYMKRFNELKEEMKKMIMAEGSQELEKLELIDNLQRLGVSYHFKHEIMQILSSIKQHSTPADSLYATALKFRLLREHGFHISQEIFDGLSETHTKDTKGMLYLYEASFLATEGESELEQAWTEKHLREYLKNKNIDQNVAKLVHRALELPLHWRMLRLEARWFISFYKKRQDMIPLLLELAILDFNIVQAAHIQDLKYVARWWKETGLAENLPFARDRLVENFFWTIGVNFLPQYGYSRRIETKVNALVTAIDDVYDVFGTLDELQCFTDAIQRWNTDELDNLPDNMKMCYFALDDFINEVACDALIVPYLRNAWTDLCKSYLIEAKWYFSKYIPTMEEYMDNAWISISAPVILVHAYFLIANPVNKEALHYLRNYHDIIRWSALILRLANDLGTSSDELKRGDVPKSIQCYMNEKKVSEEEARQHIRLLISETWKKLNEAHNVAAHPFPKMFVKSAMNLARMAQCMYQHGDGHGGQNSETQNRIMALLFESIPPA
Protein: Probable diacyglycerol O-acyltransferase tgs2 (TGS2) (Diacylglycerol O-acyltransferase) (DGAT) (EC 2.3.1.20) (Long-chain-alcohol O-fatty-acyltransferase) (EC 2.3.1.75) (Probable triacylglycerol synthase tgs2) (Wax ester synthase/acyl-CoA:diacylglycerol acyltransferase) (Wax synthase) (WS) (P9WKC7)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Function: Catalyzes the terminal and only committed step in triacylglycerol synthesis by using diacylglycerol and fatty acyl CoA as substrates. Required for storage lipid synthesis.
Interaction partners:
- Possible multi-functional enzyme with acyl-CoA-reductase activity AcrA1
- Uncharacterized oxidoreductase Rv1543
- Triacylglycerol lipase
- Nudix hydrolase domain-containing protein
- Diacylglycerol kinase
Sequence:
MDLMMPNDSMFLFIESREHPMHVGGLSLFEPPQGAGPEFVREFTERLVANDEFQPMFRKHPATIGGGIARVAWAYDDDIDIDYHVRRSALPSPGRVRDLLELTSRLHTSLLDRHRPLWELHVVEGLNDGRFAMYTKMHHALIDGVSAMKLAQRTLSADPDDAEVRAIWNLPPRPRTRPPSDGSSLLDALFKMAGSVVGLAPSTLKLARAALLEQQLTLPFAAPHSMFNVKVGGARRCAAQSWSLDRIKSVKQAAGVTVNDAVLAMCAGALRYYLIERNALPDRPLIAMVPVSLRSKEDADAGGNLVGSVLCNLATHVDDPAQRIQTISASMDGNKKVLSELPQLQVLALSALNMAPLTLAGVPGFLSAVPPPFNIVISNVPGPVDPLYYGTARLDGSYPLSNIPDGQALNITLVNNAGNLDFGLVGCRRSVPHLQRLLAHLESSLKDLEQAVGI
Protein: Receptor-type tyrosine-protein phosphatase H (R-PTP-H) (EC 3.1.3.48) (Stomach cancer-associated protein tyrosine phosphatase 1) (SAP-1) (E9Q0N2)
Organism: Mus musculus (Mouse)
Function: Protein phosphatase that may contribute to contact inhibition of cell growth and motility by mediating the dephosphorylation of focal adhesion-associated substrates and thus negatively regulating integrin-promoted signaling processes. Induces apoptotic cell death by at least two distinct mechanisms: inhibition of cell survival signaling mediated by PI 3-kinase, Akt, and ILK and activation of a caspase-dependent proapoptotic pathway. Inhibits the basal activity of LCK and its activation in response to TCR stimulation and TCR-induced activation of MAP kinase and surface expression of CD69. Inhibits TCR-induced tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal activity of DOK1 and its CD2-induced tyrosine phosphorylation. Induces dephosphorylation of BCAR1, focal adhesion kinase and SRC. Reduces migratory activity of Jurkat cells (By similarity). Reduces tyrosine phosphorylation of CEACAM20 and thereby contributes to suppress the intestinal immune response.
Subcellular location: Cell projection, microvillus membrane {ECO:0000269|PubMed:19170756, ECO:0000269|PubMed:26195794}; Single-pass type I membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250|UniProtKB:Q9HD43}. Apical cell membrane {ECO:0000269|PubMed:19170756, ECO:0000269|PubMed:26195794}; Single-pass type I membrane protein {ECO:0000305}. Note=Colocalizes with CEACAM20 at the apical brush border of intestinal cells. {ECO:0000269|PubMed:26195794}.
Interaction partners:
Sequence:
MARAGGNCGVWRSLVLLGLYGCSVVRAAGTSVTVDRHAPASSYEFSMWVEKDGVSSSPQIPVTTAAPNPVRNLRVEGQNNISISLSWEPPDQSSLQGLTYWTQCSRHGGQTETRNTTDTSVTVDGLDPGSSYECSVWVEKDGLYSKNETLNTSTAPNPVRNLRVEGQNNISISLSWEPPDQPSLQGLTYWAQCSRHGGQTETRNTADTSVTVDGLDPGSSYECSVWVEKDGVYSTNETLNTSTAPNPVRNLRVEGQNNISISLSWEPPDQPSLQGLTYWAQCSRHGGQTETRNTTDTSITVDGLDPGSSYECSVWVEKDGVYSTNETLSNTTAPNPVRNLRVKSQNNFSISLSWEPPDQPSLQGLIYWAQCSRHGGQTETRNTTDTSVTVDGLDPGFLYKCSVWVEKDGVYSTNETLNTSTVPISASNPVRNLRVEGQNNFSISLSWEPPDQSSLQGLTYWAQCSRHGGQTETRNTADTSVTVDGLDPGSSYECSVWVEKDGVYSTNETLNTSTVPAAVNITSCISTSGGYGVLLTWSCPSGGYESFEVKVGRKWRSENGSLCGKGVTVSDLEPAQSYTATVTTVFKDLKAQSLSTTCHTESAAIIAGAIVGILLLFILVGLLIVFLKRRRKKRQPKEVPKDLVCSCPGDILAKDFADHVRENEKDSNCGFAEEYQQLALEGQGQSQITASALENRSKNRYRNVLPYDWSRVPLQPLQEEPGSDYINASFMPGLWSPKEFIATQGPLPNTVGDFWRMVWEQQSHTLVMLTNCMESGRVKCEHYWPLDAQPCIHGQLQVMLISEEASENWTVRHLQLFHMKEQQTLSLRQFHYLAWPDHGVPYSPDPLLAFRKMLRQWMDQTTDGGPPIVHCSAGVGRTGTLIALDVLLRQLECEGLVGPFSFVKKMRESRPLMVQTEAQYVFLHQCILKSLQKPAPALVPEEAMYENVASLVYENASAIMAHESEFSASGC
Protein: PML nuclear body scaffold (A0A8I6AC37)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
MPPPEEPSEDHEHSQSPAEQAIKEEFQFLRCPGCQTQAKCPKLLPCLHTLCSGCLEAPGLQCPICQAPGSANANAEALDNVFFESLQRRLAVFRQIVDAQAACTRCKELADFWCFECEQLMCGKCFDAHQWYLKHEARPLAELRDNSVREFLDSTRKSNIFCSNTNHRTPAQTNVIMQSPFILEEMTDPHSTIPPQRSACLLPTNSKPLQVYFIYCRGCAKPLCCECALLDRNHSHLQCEIGKEIQQLHEELGTMTQALEEQGRTFDSAHAQMHSAIGQLDDARSDTEKQIRARVRQVIEHVQAQERELLEAVNVRYQRDYQEIAGQLGHLEAVLQRIRTGGALVKRMKLYASEQEVLDMHGFLRKALCRLRQEEPQNHKVQLRTSGFEEFKLCLQDLVSFITQRTDVAVAGRASPEAASTHPEAASAQPEAASTHPEAASAQPEAASAHPESASTPGNSTDLEQPKEVQRAQAQAMELSKTQPVAMVKSVPGAHPVPVYAFSMQGPTYREEASQTVSPMKRKCCHIDCCRKIIKMESTDENEDRLSTSSPEQPRPSTSKAISPPHPDGTSSTESTIPEKETPLPNNNHVASDAGETEERIVVISSSEDSDAENLPSHELDDSSSESSSIQLEGPNSLKALDESLAEPHLEDRTLVFFDLKIDNETQKISQLAAVNRESKFRVLIQPEAFSVYSKAVSLESGLQHFLSFLNSMHRPLLACPRLWGPGLPIFFQALNDINKLWEFQDAISGFLAVLPLIQERIPSASSFKLRNLAKTYLARNMSERSALAAVLAMRDLCCLLEVSPGLQLAQHIYSFSSLQCFASLQPLIQAQVLPQPEARLLALHNVSFLELLTAYRSNRQEGLKKYVHYLSLQTTPSSASTQIAQFLQALSAYMDGQLEGHIPAGAEGTALSLSGRAENKGCLA
Protein: 1-phosphatidylinositol 4-kinase (EC 2.7.1.67) (Q49GP4)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MCPVDIRGVFQLDERRRDAVIALGIFLVESELQHKDAIVPYLLVLLKGLPRVQWIEESSERKGREALPIAENFSFCLVTVLSDVAQMDESMRIQILEAVMNLIQVLQETCQNIEGQDKEYLCKYTVPCLLGVVRAFGRYSNTEEPLLSKLFPRIVPQPPGTGDGAEVTRRRSFNDFRSILPSSLLTVCQSDTLRRKTSSTSSISQQASPERAGLPPSSPSDPSAHYFEAASYLPDGSAVDPDYYFSTISSSFSVSPLFTGSNNKEFTVPLDLLRQLLQMVEQFVSESFMKTLDQAMTEVLEINPTAYLYYKTFSDPLYVAIFKMLRDSLYYMKDLQVSFVKEVHDFVLEQFSSSQSELQRILHDVEYLHSELNPLKLRCQANAACVDLMVWAVTEEQGAENLCTKLSEKLQSKTSSKVIIAHMPLLICCLQGLGRLCERFPVVAHSVTMSLRDFLVVPSPVLVKLYKYHSQYTTGAGEIKIHVTNEHSQSTFSSHSSKKSQPSMYEQLRDISINNICRCLKAGLTMDSVIVEAFLASLSNRLYISQENDKDAHLIPDHTIRALGHIAVALRDTPRVMEPILQILQQKFCQPPSQLDVLIIDQLGCMVITGNQYIYQEVWNLFQQISVKASSMVYSTKDYKDHGYRHCSLAVINALANIAANLQTEQMVDELLVNLLELFVQLGLEGKRASERASEKGPALKASSSAGNLGVLIPVIAVLTKRLPAIKEAKPRLQKLFRDFWLYSVVMGFAVEGSGLWPEEWYEGVCEIATKSPLLTFPSGEPLRSELQYNSALKNDTVTPAELNDLRGTIINLLDPPPEVAALINKLDFAMSTYLLSVYRLEYMRVLRSQESDRFQVMFRYFEDRAIQKDKSGMMQCVIAVGDKVFDVFLQMMADKAKTKAHEEELESHAQFLLVNFNHIHKRIRRVADKYLSGLAETFPHLLWSGRVLRTMLDILQTLSLSLSADIHKDQPYYDIPDTPYRITVPDTYEARESIVKDFAARCGEILKEAMKWAPSVTKSHLQEYLNKHQNWVSGLSQHTGLAMATESILHFAGYNRQSTSLGTTQLTERPACVKKDYSNFMASLNLRNRYAGEVAGMIHFSEATRSTSDLNKLMIRQMNEALDGGQPEAFTEALFKMAALLISSREWDPLLLHHLCWSPLKMFTENGMETAIACWEWLLAGRTGVEVPFMREMAGAWQMTVDLKMGLFSDAQLEADPLAASEESQPIPCPPDVTPHYIWIEFLVQRFEIAKYSSADQVEIFGSLLQRSLSLNVGSPKSSLNRHVAAIGPRFRLLTLGLSLLHSDVVTNATIRNVLREKIYSTAFDYFSVASKFPTQGDKRLREDISIMIRFYASILSDKKYLGASLLVPPDNQDPSLNSLSVMNATDPRNNMDMTVGSRQQSAQGWINTYPLSSGMSTTSKKSGMSKKSNRGTQLHKYYMKRRTLLLALLASEIERLSTWYNPLSTQELAIPTEQSVETSISNWRSKYINLTEKQWKDNVNLAWSIAPYLALQLPARFKNADAIVAEVTRLVRLDPGAVSDVPEAVKFLVTWHTIDADSPELSHILCWAHADPPTGLSYFSSMYPPHPLTAQYGVKVLRSFPPDTILFYIPQIVQALRYDKMGYVREYILWAAQKSQLLAHQFIWNMKTNIFLDEEGHQKDPDIGELLEQMVEEITHSLSGPAKDFYQREFDFFNKITNVSAIIKPVPKGDERKRACLKALSEIKVQPGCYLPSNPEAIVLDIDYKSGTPMQSAAKAPYLAKFKVKRCGVSELEKEGLRCPSDSQDEGDESSLMAQRVCWQAAIFKVGDDCRQDMLALQIIGLFKNIFQLVGLDLFVFPYRVVATAPGCGVIECIPDCKSRDQLGRQTDFGMYDYFRNQYGDESTLAFQKARYNFIRSMAAYSLLLFLLQIKDRHNGNIMLDSKGHLIHIDFGFMFESSPGGNLGWEPDIKLTDEMVMIMGGKMEATPFKWFMEMCVRGYLAVRPYMDAVVSLVTLMLDTGLPCFRGQTIKLLKQRFNPNMSEKEAAAFMIKVIERCFLSSRSKTYDMLQYYQNQIPY
Protein: Glycine receptor subunit beta (Glycine receptor 58 kDa subunit) (P48167)
Organism: Homo sapiens (Human)
Function: Glycine receptors are ligand-gated chloride channels. GLRB does not form ligand-gated ion channels by itself, but is part of heteromeric ligand-gated chloride channels. Channel opening is triggered by extracellular glycine. Heteropentameric channels composed of GLRB and GLRA1 are activated by lower glycine levels than homopentameric GLRA1. Plays an important role in the down-regulation of neuronal excitability. Contributes to the generation of inhibitory postsynaptic currents.
Subcellular location: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P48168}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415}. Synapse {ECO:0000250|UniProtKB:P48168}. Cell projection, dendrite {ECO:0000250|UniProtKB:P48168}. Cell membrane {ECO:0000269|PubMed:11929858, ECO:0000269|PubMed:12684523, ECO:0000269|PubMed:15302677, ECO:0000269|PubMed:16144831, ECO:0000269|PubMed:22973015, ECO:0000269|PubMed:23238346, ECO:0000269|PubMed:25445488, ECO:0000269|PubMed:35526563, ECO:0000269|PubMed:8717357}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P23415}. Cytoplasm {ECO:0000269|PubMed:12684523, ECO:0000269|PubMed:35526563}. Note=Retained in the cytoplasm upon heterologous expression by itself. Coexpression with GPHN promotes expression at the cell membrane (PubMed:12684523). Coexpression with GLRA1, GLRA2 or GLRA3 promotes expression at the cell membrane. {ECO:0000250|UniProtKB:P20781, ECO:0000269|PubMed:12684523}.
Interaction partners:
- Gephyrin
- Glycine receptor subunit alpha-3
- Sodium- and chloride-dependent glycine transporter 2
- Rho guanine nucleotide exchange factor 9
- Glycine receptor subunit alpha-1
- Neurobeachin
Sequence:
MKFLLTTAFLILISLWVEEAYSKEKSSKKGKGKKKQYLCPSQQSAEDLARVPANSTSNILNRLLVSYDPRIRPNFKGIPVDVVVNIFINSFGSIQETTMDYRVNIFLRQKWNDPRLKLPSDFRGSDALTVDPTMYKCLWKPDLFFANEKSANFHDVTQENILLFIFRDGDVLVSMRLSITLSCPLDLTLFPMDTQRCKMQLESFGYTTDDLRFIWQSGDPVQLEKIALPQFDIKKEDIEYGNCTKYYKGTGYYTCVEVIFTLRRQVGFYMMGVYAPTLLIVVLSWLSFWINPDASAARVPLGIFSVLSLASECTTLAAELPKVSYVKALDVWLIACLLFGFASLVEYAVVQVMLNNPKRVEAEKARIAKAEQADGKGGNVAKKNTVNGTGTPVHISTLQVGETRCKKVCTSKSDLRSNDFSIVGSLPRDFELSNYDCYGKPIEVNNGLGKSQAKNNKKPPPAKPVIPTAAKRIDLYARALFPFCFLFFNVIYWSIYL
Protein: RH74701p (Q0E985)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Ribosome biogenesis protein BOP1 homolog
- Putative rRNA methyltransferase
- Nucleolar GTP-binding protein 1
- Ribosome biogenesis protein WDR12 homolog
- Probable ribosome biogenesis protein RLP24
- Probable rRNA-processing protein EBP2 homolog
- LD11307p
- FI01826p
- RRM domain-containing protein
- Nucleolar complex protein 3
Sequence:
MVRKHKGTLAVIEKIYQDIPAFSDIFTEESFYMFAFCFVCATILVAFILSRFITIKPVDF
Protein: Propionyl-CoA carboxylase alpha chain, mitochondrial (PCCase subunit alpha) (EC 6.4.1.3) (Propanoyl-CoA:carbon dioxide ligase subunit alpha) (Q91ZA3)
Organism: Mus musculus (Mouse)
Function: This is one of the 2 subunits of the biotin-dependent propionyl-CoA carboxylase (PCC), a mitochondrial enzyme involved in the catabolism of odd chain fatty acids, branched-chain amino acids isoleucine, threonine, methionine, and valine and other metabolites. Propionyl-CoA carboxylase catalyzes the carboxylation of propionyl-CoA/propanoyl-CoA to D-methylmalonyl-CoA/(S)-methylmalonyl-CoA (By similarity). Within the holoenzyme, the alpha subunit catalyzes the ATP-dependent carboxylation of the biotin carried by the biotin carboxyl carrier (BCC) domain, while the beta subunit then transfers the carboxyl group from carboxylated biotin to propionyl-CoA (By similarity). Propionyl-CoA carboxylase also significantly acts on butyryl-CoA/butanoyl-CoA, which is converted to ethylmalonyl-CoA/(2S)-ethylmalonyl-CoA (By similarity). Other alternative minor substrates include (2E)-butenoyl-CoA/crotonoyl-CoA (By similarity).
Subcellular location: Mitochondrion matrix {ECO:0000250|UniProtKB:P05165}.
Interaction partners:
- Propionyl-CoA carboxylase beta chain, mitochondrial
- Methylcrotonoyl-CoA carboxylase beta chain, mitochondrial
- Methylmalonyl-CoA epimerase, mitochondrial
- Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- 3-ketoacyl-CoA thiolase, mitochondrial
- Short-chain specific acyl-CoA dehydrogenase, mitochondrial
- Acyl-CoA synthetase short-chain family member 3, mitochondrial
- Ethylmalonyl-CoA decarboxylase
- Trifunctional enzyme subunit beta, mitochondrial
Sequence:
MAGQWVRTVALLAARRHWRRSSQQQLLGTLKHAPVYSYQCLVVSRSLSSVEYEPKEKTFDKILIANRGEIACRVIKTCKKMGIKTVAIHSDVDASSVHVKMADEAVCVGPAPTSKSYLNMDAIMEAIKKTRAQAVHPGYGFLSENKEFAKRLAAEDVTFIGPDTHAIQAMGDKIESKLLAKRAKVNTIPGFDGVVKDADEAVRIAREIGYPVMIKASAGGGGKGMRIAWDDEETRDGFRFSSQEAASSFGDDRLLIEKFIDNPRHIEIQVLGDKHGNALWLNERECSIQRRNQKVVEEAPSIFLDPETRQAMGEQAVALAKAVKYSSAGTVEFLVDSQKNFYFLEMNTRLQVEHPVTECITGLDLVQEMILVAKGYPLRHKQEDIPISGWAVECRVYAEDPYKSFGLPSIGRLSQYQEPIHLPGVRVDSGIQPGSDISIYYDPMISKLVTYGSDRAEALKRMEDALDNYVIRGVTHNIPLLREVIINTRFVKGDISTKFLSDVYPDGFKGHTLTLSERNQLLAIASSVFVASQLRAQRFQEHSRVPVIRPDVAKWELSVKLHDEDHTVVASNNGPAFTVEVDGSKLNVTSTWNLASPLLSVNVDGTQRTVQCLSREAGGNMSIQFLGTVYKVHILTKLAAELNKFMLEKVPKDTSSTLCSPMPGVVVAVSVKPGDMVAEGQEICVIEAMKMQNSMTAGKMGKVKLVHCKAGDTVGEGDLLVELE
Protein: Short chain dehydrogenase prhI (EC 1.1.1.-) (Paraherquonin biosynthesis cluster protein I) (A0A1E1FFP5)
Organism: Penicillium brasilianum
Function: Short chain dehydrogenase; part of the gene cluster that mediates the biosynthesis of paraherquonin, a meroterpenoid with a unique, highly congested hexacyclic molecular architecture. The first step of the pathway is the synthesis of 3,5-dimethylorsellinic acid (DMOA) by the polyketide synthase prhL (By similarity). Synthesis of DMOA is followed by farnesylation by the prenyltransferase prhE, methylesterification by the methyl-transferase prhM, epoxidation of the prenyl chain by the flavin-dependent monooxygenase prhF, and cyclization of the farnesyl moiety by the terpene cyclase prhH, to yield the tetracyclic intermediate, protoaustinoid A (By similarity). The short chain dehydrogenase prhI then oxidizes the C-3 alcohol group of the terpene cyclase product to transform protoaustinoid A into protoaustinoid B. The FAD-binding monooxygenase prhJ catalyzes the oxidation of protoaustinoid B into preaustinoid A which is further oxidized into preaustinoid A1 by FAD-binding monooxygenase phrK. Finally, prhA leads to berkeleydione via the berkeleyone B intermediate. PrhA is a multifunctional dioxygenase that first desaturates at C5-C6 to form berkeleyone B, followed by rearrangement of the A/B-ring to form the cycloheptadiene moiety in berkeleydione. Berkeleydione serves as the key intermediate for the biosynthesis of paraherquonin as well as many other meroterpenoids (Probable). The cytochrome P450 monooxygenases prhB, prhD, and prhN, as well as the isomerase prhC, are probably involved in the late stage of paraherquonin biosynthesis, after the production of berkeleydione (Probable). Especially prhC might be a multifunctional enzyme that catalyzes the D-ring expansion via intramolecular methoxy rearrangement, as well as the hydrolysis of the expanded D-ring (Probable).
Subcellular location: Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MYNIQDHVVIITGSSSGIGLAASTLALASGAKVFGIDISNSPTSVTANPNYTFFAADLSHPESAKKAIAACIAAYGNRIDGLLNIAGVMDLNQSADTVTDDMWDRCIAINLTAPVKLMREVIPIMRLRGKGSIVNVGSKASMSGAVSGIAYTASKHGLVGATKNVAWRFKHEGIRCNIVCPGGVAATGIRDGVDSTQFDSEALEMMSVIHQAHASDHAKGLGLQPEDLAHSLLYFLSDLSKGISGAVIPVDNAWSTI