wanglab/gogpt-training-data huggingface dataset:
Protein: Major DNA-binding protein (Q2HRD3)
Organism: Human herpesvirus 8 type P (isolate GK18) (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Function: Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation. Promotes viral DNA recombination by performing strand-transfer, characterized by the ability to transfer a DNA strand from a linear duplex to a complementary single-stranded DNA circle. Can also catalyze the renaturation of complementary single strands. Additionally, reorganizes the host cell nucleus, leading to the formation of prereplicative sites and replication compartments. This process is driven by the protein which can form double-helical filaments in the absence of DNA.
Subcellular location: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04007}. Note=In the absence of DNA replication, found in the nuclear framework-associated structures (prereplicative sites). As viral DNA replication proceeds, it migrates to globular intranuclear structures (replication compartments). {ECO:0000255|HAMAP-Rule:MF_04007}.
Interaction partners:
Sequence:
MALKGPQTLEENIGSAAPTGPCGYLYAYVTHNFPIGEASLLGNGYPEAKVFSLPLLHGLTVESDFPLNVKAVHKKIDATTASVKLTSYHREAIVFHNTHLFQPIFQGKGLEKLCRESRELFGFSTFVEQQHKGTLWSPEACPQLPCANEIFMAVIVTEGFKERLYGGKLVPVPSQTTPVHIGEHQAFKIPLYDEDLFGPSRAQELCRFYNPDISRYLHDSIFTGIAQALRVKDVSTVIQASERQFVHDQYKIPKLVQAKDFPQCASRGTDGSTLMVIDSLVAELGMSYGLSFIEGPQDSCEVLNYDTWPIFENCETPDARLRALEVWHAEQALHIGAQLFAANSVLYLTRVAKLPQKNQRGDANMYNSFYLQHGLGYLSEATVKENGASAFKGVPVSALDGSSYTLQHLAYASSFSPHLLARMCYYLQFLPHHKNTNSQSYNVVDYVGTAAPSQMCDLCQGQCPAVCINTLFYRMKDRFPPVLSNVKRDPYVITGTAGTYNDLEILGNFATFREREEEGNPVEDAPKYTYWQLCQNITEKLASMGISEGGDALRTLIVDIPSFVKVFKGIDSTVEAELLKFINCMIKNNYNFRENIKSVHHILQFACNVYWQAPCPVFLTLYYKSLLTVIQDICLTSCMMYEQDNPAVGIVPSEWLKMHFQTMWTNFKGACFDKGAITGGELKIVHQSMFCDLFDTDAAIGGMFAPARMQVRIARAMLMVPKTIKIKNRIIFSNSTGAESIQAGFMKPASQRDSYIVGGPYMKFLNALHKTLFPSTKTSALYLWHKIGQTTKNPILPGVSGEHLTELCNYVKASSQAFEEINVLDLVPDTLTSYAKIKLNSSILRACGQTQFYATTLSCLSPVTQLVPAEEYPHVLGPVGLSSPDEYRVKVAGRSVTIVQSTLKQAVSTNGRLRPIITVPLVVNKYTGSNGNTNVFHCANLGYFSGRGVDRNLRPESVPFKKNNVSSMLRKRHVIMTPLVDRLVKRIVGINSGEFEAEAVKRSVQNVLEDRDNPNLPKTVVLELVKHLGSSCASLTEEDVIYYLGPYAVLGDEVLSLLSTVGQAGVPWTAEGVASVIQDIIDDCELQFVGPEEPCLIQGQSVVEELFPSPGVPSLTVGKKRKIASLLSDLDL
Protein: Negative cofactor 2 complex subunit beta (NC2 complex subunit beta) (O14348)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Transcription regulator complex subunit bur6
- TATA-box-binding protein
- DNA polymerase epsilon subunit D
- TATA-binding protein-associated factor mot1
- SAGA complex subunit Sgf29
- SAGA complex subunit Ada2
- Histone acetyltransferase gcn5
Sequence:
MNDGFADDELSLPKATVQKMVSDILPVDLTFTKEARDLLIECCVEFIHLVSSEANEICEKEAKKTIAAEHIIKALENLEFKEYIAEALEVAAEHKEQQKNREKKSSKFEQSGVSRDELLRQQEELLSRARERFKNQNIAHDNHTTTAIPVPTASETETKEN
Protein: Neutrophil antibiotic peptide NP-2 (RatNP-2) (Neutrophil defensin 2) (Q62715)
Organism: Rattus norvegicus (Rat)
Function: Active in vitro against S.aureus, fungi, Gram-positive and Gram-negative bacteria and to a lesser extent against an enveloped virus.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MRTLTLLTALLLLALHTQAKSPQGTAEEAPDQEQLVMEDQDISISFGGDKGTALQDADVKAGVTCYCRSTRCGFRERLSGACGYRGRIYRLCCR
Protein: Cytosolic phospholipase A2 (cPLA2) (Phospholipase A2 group IVA) [Includes: Phospholipase A2 (EC 3.1.1.4) (Phosphatidylcholine 2-acylhydrolase); Lysophospholipase (EC 3.1.1.5)] (P50393)
Organism: Rattus norvegicus (Rat)
Function: Has primarily calcium-dependent phospholipase and lysophospholipase activities, with a major role in membrane lipid remodeling and biosynthesis of lipid mediators of the inflammatory response (By similarity). Plays an important role in embryo implantation and parturition through its ability to trigger prostanoid production (By similarity). Preferentially hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity). Selectively hydrolyzes sn-2 arachidonoyl group from membrane phospholipids, providing the precursor for eicosanoid biosynthesis via the cyclooxygenase pathway. In an alternative pathway of eicosanoid biosynthesis, hydrolyzes sn-2 fatty acyl chain of eicosanoid lysophopholipids to release free bioactive eicosanoids. Hydrolyzes the ester bond of the fatty acyl group attached at sn-1 position of phospholipids (phospholipase A1 activity) only if an ether linkage rather than an ester linkage is present at the sn-2 position. This hydrolysis is not stereospecific. Has calcium-independent phospholipase A2 and lysophospholipase activities in the presence of phosphoinositides. Has O-acyltransferase activity. Catalyzes the transfer of fatty acyl chains from phospholipids to a primary hydroxyl group of glycerol (sn-1 or sn-3), potentially contributing to monoacylglycerol synthesis (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P47712}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P47712}. Nucleus envelope {ECO:0000250|UniProtKB:P47712}. Note=Translocates to intracellular membranes in a calcium-dependent way. {ECO:0000250|UniProtKB:P47712}.
Interaction partners:
- Polyunsaturated fatty acid lipoxygenase ALOX15
- Polyunsaturated fatty acid 5-lipoxygenase
- Prostaglandin G/H synthase 2
- Mitogen-activated protein kinase 3
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-1
- Phospholipase A and acyltransferase 3
- Arachidonate 12-lipoxygenase, 12R-type
- Polyunsaturated fatty acid lipoxygenase ALOX15B
- Protein kinase C beta type
Sequence:
MSFIDPYQHIIVEHQYSHKFTVVVLRATKVTKGTFGDMLDTPDPYVELFISTTPDSRKRTRHFNNDINPVWNETFEFILDPNQENVLEITLMDANYVMDETLGTATFPVSSMKVGEKKEVPFIFNQVTEMILEMSLEVCSCPDLRFSMALCDQEKTFRRQRKENIKENMKKLLGPKKSEGLYSTRDVPVVAILGSGGGFRAMVGFSGVMKALYESGILDCATYVAGLSGSTWYMSTLYSHPDFPEKGPEEINEELMKNVSHNPLLLLTPQKVKRYVESLWKKKSSGQPVTFTDIFGMLIGETLIQNRMSTTLSSLKEKVSAARCPLPLFTCLHVKPDVSELMFADWVEFSPYEIGMAKYGTFMTPDLFGSKFFMGTVVKKYEENPLHFLMGVWGSAFSILFNRVLGVSGSQNKGSTMEEELENITAKHIVSNDSSDSDDEAQGPKGTENEDAEREYQNDNQASWVHRMLMALVSDSALFNTREGRAGKEHNFMLGLNLNTSYPLSPLRDFSPQDSFDDDELDAAVADPDEFERIYEPLDVKSKKIHVVDSGLTFNLPYPLILRPQRGVDLIISFDFSARPSDTSPPFKELLLAEKWAKMNKLPFPKIDPYVFDREGLKECYVFKPKNPDVEKDCPTIIHFVLANINFRKYKAPGVLRETKEEKEIADFDIFDDPESPFSTFNFQYPNQAFKRLHDLMYFNTLNNIDVIKDAIVESIEYRRQNPSRCSVSLSNVEARKFFNKEFLSKPTAESI
Protein: Adenosine deaminase (EC 3.5.4.4) (S-methyl-5'-thioadenosine deaminase) (EC 3.5.4.31) (A0A1Y3DYH2)
Organism: Plasmodium knowlesi
Function: Catalyzes the hydrolytic deamination of adenosine to produce inosine. Unlike mammalian adenosine deaminases, also catalyzes the deamination of 5'-methylthioadenosine (MTA), a by-product of polyamine biosynthesis, to produce 5'-methylthioinosine (MTI). Plays an essential role in the purine salvage pathway which allows the parasite to use host cell purines for the synthesis of nucleic acids (Probable).
Interaction partners:
Sequence:
MNILQEPIDFLKKDELKNIDLSQMDKKERYKIWKRIPKCELHCHLDLCFSADFFLSCVRKYNLQPNLSDEEVLDYYLFAKGGKSLGEFVEKAIRVADIFQDYEMIEDLAKHAVFNKYKEGVVLMEFRYSPTFVAFKHNLDIELIHQAIVKGIKEVVELLDHKIDVTLLCIGDTGHRAADIKASADFCLKHKADFVGFDHGGHEVDLKPYKEIFDYVKEGGMHLTVHAGEDVTLPNLNTLYSAIQVLKVERIGHGIRVSESQELIDMVKENNILLEVCPISNVLLKNAKSFDTHPIRKLYDAGVKVSVSSDDPGMFLTNINDDYEKLYTHLHFTLEDFMKMNEWALEKSFIGCDIKEKIKKLYF
Protein: Endonuclease SceI small subunit (EC 3.1.21.-) (Endo.SceI 50 kDa subunit) (Maturase-like RF3 protein) (P12294)
Organism: Saccharomyces cerevisiae (Baker's yeast)
Function: Catalytic component of endonuclease SceI (Endo.SceI), which cleaves specifically at multiple sites on mitochondrial DNA and produces double-stranded breaks.
Subcellular location: Mitochondrion.
Interaction partners:
Sequence:
MKKQNLNSILLMYINYIINYFNNIHKNQLKKDWIMEYEYMYKFLMNNMTCFIKWDNNKILLLLDMYYNVLYNYHKQRTPMSNKRLMNSKNIMDYKLLYTYFYILNKMKMEMDNYNNNNNNISLKYNELLKNIMNNLNYKTSNIETNLSNNFYLMDKYLINKYMKYLDMLNMIPNNYMFNNINYKGKLNIKTVLDLNNNEFYDYLSGLIEGDGYIGPGGITITNHANDVLNTIFINKRIKNSILVEKWMDTLKDNPYFVNAFSINIKTNLAKEKIFTNIYNKLYSDYKINQINNHIPYYNYLKINNKLPIKNIMDIKNNYWLAGFTAADGSFLSSMYNPKDTLLFKNMRPSYVISQVETRKELIYLIQESFDLSISNVKKVGNRKLKDFKLFTRTTDELMKFIYYFDKFLPLHDNKQFNYIKFRFNTFIKSYNWNNRVFGLVLSEYINNIKIDNYDYYYYNKYINMHNARKPKGYIK
Protein: propanoyl-CoA C-acyltransferase (EC 2.3.1.176) (Propanoyl-CoA C-acyltransferase) (O33332)
Organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- Probable fatty oxidation protein FadB
- Probable acyl-CoA dehydrogenase FadE21
- Probable acyl-CoA dehydrogenase FadE4
- Probable acyl-CoA dehydrogenase FadE23
- Probable acyl-CoA dehydrogenase FadE13
- Acyl-CoA dehydrogenase FadE7
- Propanal dehydrogenase
- Probable acyl-CoA dehydrogenase FadE1
- Probable acyl-CoA dehydrogenase FadE2
- Steroid 3-ketoacyl-CoA thiolase
Sequence:
MPNQGSSNKVYVIGVGMTKFEKPGRREGWDYPDMARESGTKALRDAGIDYREVEQGYVGYVYGESTSGQRALYELGMTGIPIVNVNNNCSTGSTALYLGAQAIRGGLADCVLALGFEKMQPGALGGGADDRESPLGRHVKALAEIDEFGFPVAPWMFGAAGREHMKKYGTTAEHFAKIGYKNHKHSVNNPYAQFQDEYTLDDILASKMISDPLTKLQCSPTSDGSAAVVLASEDYLANHNLAGRAVEIVGQAMTTDFASTFDGSARNIIGYDMTVQAAQRVYQQSGLGPKDFGVIELHDCFSANELLLYEALGLCGPGEAPELIDDNQTTYGGRWVVNPSGGLISKGHPLGATGLAQCAELTWQLRGTAEARQVDNVTAALQHNIGLGGAAVVTAYQRAER
Protein: Trophinin (Q8BSK0)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
GALSTSASFGGVLNGSAGFGGALNTNATFGGVLNGSAGFGGAMNTNATFGGALNSNAGFGGAISTSTNFGGALNNSAGFGGAMNTSASFGGALNNSAGFGGAISTNATFGGALNNSAGFGGAISTNATFGGALNNSAGFGGAISTSASFGGTLNNSASFGGAINTSASFGGVLNNSAGFGGAINTSANFGGALTNSAGFGGAISTSASFGGALNNSAGFGGAISTSASFGGALNNSAGFGGAISTNASFGGAISNSPDFGGAFSTSVGFGGTLNTTDFGSTHSNSISFGSAPTTSVSFGGSHSTNLCFGGAPSTSLCFGSASNTNLCFGGSNSTNCFSGATSANFNEGHSISFGNGLSTSAGFGNGLGTSAGFGSSLGTSTGFGGSLGPSASFNGGLGTSTGFGGGLGTSTDFSGGLNHNADFNGGLGNSAGFNGGLNTNTDFGGELGTSAGFGDGLGSSTSFGAGLVTSDGFAGNLGTNTGFGGTLGTGAGFSVSLNNGNGFGNGPNASFNRGLNTIIGFGSGSNTSNGFTGEPNTGSSFSNGPSSIVGFSGGPSTGAGFCSGPSTGGFGGGPSTGPGFGGPSTGPGFGGPSTGGGFGGPNTGGGFGGPSTGGGFGGPSTGGGFGGPSTGGGFGGPSTAAGFGSGLSTSTGFGGGLNTSAGFSGGPPSTGTGFGGGASSHGGCGFPYG
Protein: Increased recombination centers protein 22-2 (Q59XW9)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Function: Is probably involved in a pathway contributing to genomic integrity.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
Interaction partners:
Sequence:
MKLSTIFTAFAATIATVAGYETTGSKQTVDILIDYIIKETPELSQNDVANWENGDTVTLQYVVNNNEESEITVVGVTGQFKNPINNEIVTNLTTGKVGPIAVPPGEAIKFDQKINVDLIPANYELIPHVFIAQDSLIKVIPCRGQLATIVDAAVSFFDPRLIFLELVLLITFAGLIYVGYEIWGKQYFKGVAPVKAKKVSAAKASSPVATGPSTTSATGYDTNWIPESHLKQKKTKKVN
Protein: Arginine/agmatine antiporter (P60066)
Organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Function: Major component of the acid-resistance (AR) system allowing enteric pathogens to survive the acidic environment in the stomach (Probable). Exchanges extracellular arginine for its intracellular decarboxylation product agmatine (Agm) thereby expelling intracellular protons. Probably undergoes several conformational states in order to translocate the substrate across the membrane; keeps the substrate accessible to only 1 side of the membrane at a time by opening and closing 3 membrane-internal gates (By similarity).
Subcellular location: Cell inner membrane {ECO:0000305|PubMed:19578361}; Multi-pass membrane protein {ECO:0000269|PubMed:19578361}.
Interaction partners:
- Transcriptional activator of adiA
- Arginine decarboxylase
Sequence:
MSSDADAHKVGLIPVTLMVSGNIMGSGVFLLPANLAATGGIAIYGWLVTIIGALALSMVYAKMSSLDPSPGGSYAYARRCFGPFLGYQTNVLYWLACWIGNIAMVVIGVGYLSYFFPILKDPLVLTLTCVAVLWIFVLLNIVGPKMITRVQAVATVLALVPIVGIAVFGWFWFKGETYMAAWNVSGMNTFGAIQSTLNVTLWSFIGVESASVAAGVVKNPKRNVPIATIGGVLIAAVCYVLSTTAIMGMIPNAALRVSASPFGDAARMALGDTAGAIVSFCAAAGCLGSLGGWTLLAGQTAKAAADDGLFPPIFARVNKAGTPVAGLLIVGVLMTIFQFSSMSPNAAKEFGLVSSVSVIFTLVPYLYTCAALLLLGHGHFGKARPLYLLITFVAFVYCIWAVIGSGAKEVMWSFVTLMVITALYALNYNRIHKNPYPLDAPVKQD
Protein: Large ribosomal subunit protein bL9m (39S ribosomal protein L9, mitochondrial) (L9mt) (MRP-L9) (Q9VF89)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q9BYD2}.
Interaction partners:
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein uL18
- Small ribosomal subunit protein uS13
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL32m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein bL20m
Sequence:
MLKNIYVTPLNLLKSATSLQQQVRTTFVLKRKYDPPLHKTNEKPRRMRAKNFIYELVDDTLVKKRPNIEVVLKTFVEGVGDKGDVVSMKPHFVYNKLLLPGLAAYNTPENVAKYAKTEAEKSTVKHSSPYAQRTVNMLETIVLAVVMNKDEPWVLEPWHIKASLRKTGFYCREECITLPKERIEGPDLKKENKDFYCTVTINKLEQARLKCRLHHWSTDPSERLPYVLEHWKLQSEPLLDVCSPEKTP
Protein: Multidrug resistance protein pgp-1 (EC 7.6.2.2) (P-glycoprotein A) (P-glycoprotein-related protein 1) (P34712)
Organism: Caenorhabditis elegans
Function: Energy-dependent efflux pump responsible for decreased drug accumulation in multidrug-resistant cells.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
Sequence:
MLRNGSLRQSLRTLDSFSLAPEDVLKTAIKTVEDYEGDNIDSNGEIKITRDAKEEVVNKVSIPQLYRYTTTLEKLLLFIGTLVAVITGAGLPLMSILQGKVSQAFINEQIVINNNGSTFLPTGQNYTKTDFEHDVMNVVWSYAAMTVGMWAAGQITVTCYLYVAEQMNNRLRREFVKSILRQEISWFDTNHSGTLATKLFDNLERVKEGTGDKIGMAFQYLSQFITGFIVAFTHSWQLTLVMLAVTPIQALCGFAIAKSMSTFAIRETLRYAKAGKVVEETISSIRTVVSLNGLRYELERYSTAVEEAKKAGVLKGLFLGISFGAMQASNFISFALAFYIGVGWVHDGSLNFGDMLTTFSSVMMGSMALGLAGPQLAVLGTAQGAASGIYEVLDRKPVIDSSSKAGRKDMKIKGDITVENVHFTYPSRPDVPILRGMNLRVNAGQTVALVGSSGCGKSTIISLLLRYYDVLKGKITIDGVDVRDINLEFLRKNVAVVSQEPALFNCTIEENISLGKEGITREEMVAACKMANAEKFIKTLPNGYNTLVGDRGTQLSGGQKQRIAIARALVRNPKILLLDEATSALDAESEGIVQQALDKAAKGRTTIIIAHRLSTIRNADLIISCKNGQVVEVGDHRALMAQQGLYYDLVTAQTFTDAVDSAAEGKFSRENSVARQTSEHEGLSRQASEMDDIMNRVRSSTIGSITNGPVIDEKEERIGKDALSRLKQELEENNAQKTNLFEILYHARPHALSLFIGMSTATIGGFIYPTYSVFFTSFMNVFAGNPADFLSQGHFWALMFLVLAAAQGICSFLMTFFMGIASESLTRDLRNKLFRNVLSQHIGFFDSPQNASGKISTRLATDVPNLRTAIDFRFSTVITTLVSMVAGIGLAFFYGWQMALLIIAILPIVAFGQYLRGRRFTGKNVKSASEFADSGKIAIEAIENVRTVQALAREDTFYENFCEKLDIPHKEAIKEAFIQGLSYGCASSVLYLLNTCAYRMGLALIITDPPTMQPMRVLRVMYAITISTSTLGFATSYFPEYAKATFAGGIIFGMLRKISKIDSLSLAGEKKKLYGKVIFKNVRFAYPERPEIEILKGLSFSVEPGQTLALVGPSGCGKSTVVALLERFYDTLGGEIFIDGSEIKTLNPEHTRSQIAIVSQEPTLFDCSIAENIIYGLDPSSVTMAQVEEAARLANIHNFIAELPEGFETRVGDRGTQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEKVVQEALDRAREGRTCIVIAHRLNTVMNADCIAVVSNGTIIEKGTHTQLMSEKGAYYKLTQKQMTEKK
Protein: Uncharacterized protein At3g52710 (Uncharacterized protein F3C22_110) (Q9LXJ3)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Probable LRR receptor-like serine/threonine-protein kinase At1g56140
- AT4g30240/F9N11_90
- DNA-directed RNA polymerase II subunit 7
- DnaJ heat shock amino-terminal domain protein
- Stress-response A/B barrel domain-containing protein UP3
Sequence:
MPQVVASACTGGSDRKISCETLADDNEDSPHNSKIRPVSISAVDFPPESYSLSKEAQLEWLNDNAFFERKESQKGNSSAPISNPNTNPNSSSHRISLKSKASIIRLPKPQKTCFNEAKKRRNCRIARTLMIPKRIGSRLKSDPTLSEPCSPKVSCIGRVRSKRDRSRRMQRQKSGRTNSFKDKPVPVKKPGFFASFRAIFRTGGGCKDLSASGAHAPRRDVVVSPPRVSVRRSTDIRGRLPPGDVGKSSPQRNSTGSRRSIDGGEPVLPGLGGMTRFTSGRRPDLLVEV
Protein: Acyl-CoA synthetase X1 L (EC 6.2.1.3) (Q9VDU4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
Interaction partners:
- Peptidyl-prolyl cis-trans isomerase
Sequence:
MPYTPENSYDNDQKIWSGEPVVKYFDPDLSIGEIIFHEMRRHPQLTAQISATEGTVLTRGELLANAMRLASYMRSLGLLQSDIVGIIGRNTTHMLAVAYACFFNGIAFHSLNITYDRDTIEKIYKVTRPSIIFCDGDEFEKVRSATAELDVKIVTMRNHPLDSIKIDEVVATPIEENFQPAKLEKGNDQTLAILCSSGTTGTPKAVTITNSRHILAGNYHLTTADVQYSHNTLDWITGLLTTITSGVFSTTRIIADNAFDPAFALRIIEEYKVTWTIQPPSSMALMINCPDFETCDMSSLRCYMFGGSRAALEVQKGIRSRLSHDCLQFVYGFTELGAMATINCHFDEKTGSVGQLVNGLKMKIINDDGESLGPDEIGEVCIMNNQHWSGYYGNEVETRNMRDSLGWYHSGDLGYMDRDGFLYIMDRKKEMLKYQNIMYYPNDIESVISEMPQVAEVCVFGIWSNIFGDEAAAAVVKKLGSELEAQDVVDYVRSRTDSKYKQLNGGAVIVDDLQRSANGKTNRMANKAYFLHLKNRS
Protein: Ubiquitin-related modifier 1 (Q9P3U9)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a sulfur carrier required for 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Serves as sulfur donor in tRNA 2-thiolation reaction by being thiocarboxylated (-COSH) at its C-terminus by the MOCS3 homolog UBA4. The sulfur is then transferred to tRNA to form 2-thiolation of mcm(5)S(2)U. Prior mcm(5) tRNA modification by the elongator complex is required for 2-thiolation. Also acts as a ubiquitin-like protein (UBL) that is covalently conjugated via an isopeptide bond to lysine residues of target proteins such as AHP1. The thiocarboxylated form serves as substrate for conjugation and oxidative stress specifically induces the formation of UBL-protein conjugates.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03048}.
Interaction partners:
- Adenylyltransferase and sulfurtransferase uba4
- Cytoplasmic tRNA 2-thiolation protein 1
- Cytoplasmic tRNA 2-thiolation protein 2
- Multifunctional methyltransferase subunit trm112
- Probable 3-mercaptopyruvate sulfurtransferase
- Elongator complex protein 3
- Elongator complex protein 1
- DNA replication licensing factor mcm5
- Putative tRNA pseudouridine synthase C25B8.05
- Protein kti12
Sequence:
MAIKVELLGGLDLLFNKQKALSLSLSNLGSTKLGSLIDYMAQIIEKPSQKDLFILNGTVRPGIIVLVNDQDWELLEKEEYNLEEGDEVVFVSTLHGG
Protein: Metallothionein-4 (MT-4) (Metallothionein D) (Q8I9B4)
Organism: Drosophila melanogaster (Fruit fly)
Function: This protein binds cations of several transition elements. Thought to be involved in metal ion homeostasis (By similarity).
Interaction partners:
- GEO10380p1
- Metallothionein-1
- Metal response element-binding transcription Factor-1, isoform C
Sequence:
MGCKACGTNCQCSATKCGDNCACSQQCQCSCKNGPKDKCCSTKN
Protein: Sodium/potassium-transporting ATPase subunit alpha (Q6VYM4)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Subcellular location: Cell membrane {ECO:0000256|RuleBase:RU362084}; Multi-pass membrane protein {ECO:0000256|RuleBase:RU362084}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MGLVKGKDDYKLAATSEDDGKKKSEKQVKKAKEKMDKDDLKKEVDLDDHKLTLDELNRKYGTDLARGLSSVRAKEILLRDGPNTLTPPRTTPEWVKFCKQLFGGFCMLLWIGAVLCFIAHIIQVTSEEEPTNANLYLGLVLAVVVIITGCFSYYQEAKSSKIMDSFKNLVPQQALVVRDGEKKNINTEEVVVGDIVEVKGGDRIPADLRIVSASGCKVDNSSLTGESEPQTRSPDFSNDNPLETRNIAFFSTNCVEGTARGIVINTGDHTIMGRIAALAMSLESGQTPLGIEIDHFIEIITGVSVFFGVTFLILSVILGYGWLPSIIFLIGIIVANVPEGLLATVTVCLTLTAKRMAKKNCLVKNLEAVETLGSTSTICSDKTGTLTQNRMTVAHMWFDNQIHDADTTENQSGTSFDKSSATWAALARVAGLCNRAVFLAEQNNVPILKRDVSGDASETALLKCIELCCGSVKDMREKYSKVVEIPFNSTNKYQLSIHENNMAGESNHLLVMKGAPERILDSCSTILLQGKEHPLDDEIKESFQKAYEALGGLGERVLGFCHFQLPDDQFPEGFDFDCEDVNFPTENLCFVGLMSMIDPPRAAVPDAVGKCRCAGIKVIMVTGDHPITAKAIAKGVGIISEGNETVEEIAARLKIPVSEVNPRDAKACVVHGGELKDMTPEELDDILKHHTEIVFARTSPQQKLIIVEGCQRQGAIVAVTGDGVNDSPALRKADIGVAMGIAGSDVSKQAADMILLDDNFASIVTGVEEGRLIFDNLKKSITYTLSSKIPEMTPFLFLLLANIPLALGTVTILCIDLGTDMIPAISLAYEQAENDIMKRQPRNPKTDRLVNERLISVAYGQFGVMLAAAGFFTYFVIMAENGFYPMDLLGIRLDWENQYINDLEDSYGQQWTYESRKIIEFSCHTAYFAAVVIAQWAVLIVCKTRKNSFFQQGLMKNRVLIFGLCSESALALFLSYCPGMDIAIRMDPLKPFWWVCAFPYTLLIFIYDEVRKYIMRRNSGGWVYQETYY
Protein: Sodium- and chloride-dependent betaine transporter (BGT-1) (Na(+)/Cl(-) betaine/GABA transporter) (Solute carrier family 6 member 12) (P48065)
Organism: Homo sapiens (Human)
Function: Transports betaine and GABA. May have a role in regulation of GABAergic transmission in the brain through the reuptake of GABA into presynaptic terminals, as well as in osmotic regulation.
Subcellular location: Basolateral cell membrane {ECO:0000250|UniProtKB:P31651}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P31651}; Multi-pass membrane protein {ECO:0000255}. Note=In kidney, locates in basolateral membranes of renal medulla. In liver, locates in hepatocytes cell membrane. {ECO:0000250|UniProtKB:P31651}.
Interaction partners:
- Sodium/myo-inositol cotransporter
- Putative protein CASTOR3P
- Aldo-keto reductase family 1 member B1
- Nuclear factor of activated T-cells 5
Sequence:
MDGKVAVQECGPPAVSWVPEEGEKLDQEDEDQVKDRGQWTNKMEFVLSVAGEIIGLGNVWRFPYLCYKNGGGAFFIPYFIFFFVCGIPVFFLEVALGQYTSQGSVTAWRKICPLFQGIGLASVVIESYLNVYYIIILAWALFYLFSSFTSELPWTTCNNFWNTEHCTDFLNHSGAGTVTPFENFTSPVMEFWERRVLGITSGIHDLGSLRWELALCLLLAWVICYFCIWKGVKSTGKVVYFTATFPYLMLVILLIRGVTLPGAYQGIIYYLKPDLFRLKDPQVWMDAGTQIFFSFAICQGCLTALGSYNKYHNNCYKDCIALCFLNSATSFVAGFVVFSILGFMSQEQGVPISEVAESGPGLAFIAFPKAVTMMPLSQLWSCLFFIMLIFLGLDSQFVCVECLVTASIDMFPRQLRKSGRRELLILTIAVMCYLIGLFLVTEGGMYIFQLFDYYASSGICLLFLSLFEVVCISWVYGADRFYDNIEDMIGYRPWPLVKISWLFLTPGLCLATFLFSLSKYTPLKYNNVYVYPPWGYSIGWFLALSSMVCVPLFVVITLLKTRGPFRKRLRQLITPDSSLPQPKQHPCLDGSAGRNFGPSPTREGLIAGEKETHL
Protein: Recombining binding protein suppressor of hairless (CBF-1) (J kappa-recombination signal-binding protein) (RBP-J kappa) (RBP-J) (RBP-JK) (Renal carcinoma antigen NY-REN-30) (Q06330)
Organism: Homo sapiens (Human)
Function: Transcriptional regulator that plays a central role in Notch signaling, a signaling pathway involved in cell-cell communication that regulates a broad spectrum of cell-fate determinations. Acts as a transcriptional repressor when it is not associated with Notch proteins. When associated with some NICD product of Notch proteins (Notch intracellular domain), it acts as a transcriptional activator that activates transcription of Notch target genes. Probably represses or activates transcription via the recruitment of chromatin remodeling complexes containing histone deacetylase or histone acetylase proteins, respectively. Specifically binds to the immunoglobulin kappa-type J segment recombination signal sequence. Binds specifically to methylated DNA. Binds to the oxygen responsive element of COX4I2 and activates its transcription under hypoxia conditions (4% oxygen). Negatively regulates the phagocyte oxidative burst in response to bacterial infection by repressing transcription of NADPH oxidase subunits (By similarity).
Subcellular location: Nucleus. Cytoplasm. Note=Mainly nuclear, upon interaction with RITA/C12orf52, translocates to the cytoplasm, down-regulating the Notch signaling pathway.
Interaction partners:
- Mastermind-like protein 3
- Mastermind-like protein 1
- Mastermind-like protein 2
- Neurogenic locus notch homolog protein 1
- Nuclear receptor corepressor 2
- Neurogenic locus notch homolog protein 2
- Neurogenic locus notch homolog protein 3
- Histone acetyltransferase KAT2B
- Corepressor interacting with RBPJ 1
- Neurogenic locus notch homolog protein 4
Sequence:
MDHTEGSPAEEPPAHAPSPGKFGERPPPKRLTREAMRNYLKERGDQTVLILHAKVAQKSYGNEKRFFCPPPCVYLMGSGWKKKKEQMERDGCSEQESQPCAFIGIGNSDQEMQQLNLEGKNYCTAKTLYISDSDKRKHFMLSVKMFYGNSDDIGVFLSKRIKVISKPSKKKQSLKNADLCIASGTKVALFNRLRSQTVSTRYLHVEGGNFHASSQQWGAFFIHLLDDDESEGEEFTVRDGYIHYGQTVKLVCSVTGMALPRLIIRKVDKQTALLDADDPVSQLHKCAFYLKDTERMYLCLSQERIIQFQATPCPKEPNKEMINDGASWTIISTDKAEYTFYEGMGPVLAPVTPVPVVESLQLNGGGDVAMLELTGQNFTPNLRVWFGDVEAETMYRCGESMLCVVPDISAFREGWRWVRQPVQVPVTLVRNDGIIYSTSLTFTYTPEPGPRPHCSAAGAILRANSSQVPPNESNTNSEGSYTNASTNSTSVTSSTATVVS