wanglab/gogpt-training-data huggingface dataset:
Protein: RE69557p (SLC22A family member) (Q9VNX2)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MAASEAPPADPAVEVAPPAKDSEDVTLDAILKHLGQFGRFQLIIFLLICLPMMFHAMFSVTYVFTAATVTHRCSVEECDLPGSNYYEPHTNWSIPKNGKDLDSCNRYTNSELPQWNHSVDICSADHFTKNKEACAHNEFVFRDDEVTISNDFGIFCDDEWKLSMVGTINNLGQFFGIPIGGFVADRYGRSFSIALGGILGAVLGVIRSFSPSYGWFLVFEFLDNMTSSTLYSTCFVIGIELVGPKRRVLACSVITVFYAVGEVLLAMSAKAFHDWRILLRITYGPSLILLAYFWILPESVRWLLSQGKEERAKNILRRAAHVNKRELPESVLDKLVLANRDKLQQSSESRFPIREAFKNFKWRIANCSLCWIVHVLVYYGLSLNVVLLDGDKYNNFAYIALVEIPGFFMPLLIMDRFGRRYSLCGLMLASGLCCIGTIFTGADQPVLQLVLFLVGKLTITASFQVLYFFASEIYPTNLRNSLLSFCSMMGRFGSMLAPQTPLLAKYYANAPAMLFAGAAIVSGLLTLFFPETTNVVLPTTVQEADAIGVKKQSKSKDLDLVVTATQAQ
Protein: Stage II sporulation protein SB (Antidote protein SpoIISB) (Antitoxin SpoIISB) (O34800)
Organism: Bacillus subtilis (strain 168)
Function: Antitoxin component of a type II toxin-antitoxin (TA) system. Antitoxin that binds cognate toxin SpoIISA and neutralizes its toxic activity; unlike most antitoxins it does not seem to be highly labile upon expression in E.coli.
Interaction partners:
- Stage II sporulation protein SA
- Uncharacterized protein YcgB
- Putative ATP-dependent DNA helicase YjcD
- Uncharacterized protein YitR
Sequence:
MERAFQNRCEPRAAKPFKILKKRSTTSVASYQVSPHTARIFKENERLIDEYKRKKA
Protein: Type II inositol 1,4,5-trisphosphate 5-phosphatase (EC 3.1.3.36) (Inositol polyphosphate-5-phosphatase B) (Phosphoinositide 5-phosphatase) (5PTase) (Q8K337)
Organism: Mus musculus (Mouse)
Function: Hydrolyzes phosphatidylinositol 4,5-bisphosphate (PtIns(4,5)P2) and the signaling molecule phosphatidylinositol 1,4,5-trisphosphate (PtIns(1,4,5)P3), and thereby modulates cellular signaling events.
Subcellular location: Cytoplasm, cytosol {ECO:0000269|PubMed:9525932}. Endoplasmic reticulum-Golgi intermediate compartment {ECO:0000250|UniProtKB:P32019}. Early endosome membrane {ECO:0000250|UniProtKB:P32019}. Membrane {ECO:0000250|UniProtKB:P32019}; Peripheral membrane protein {ECO:0000250|UniProtKB:P32019}; Cytoplasmic side {ECO:0000250|UniProtKB:P32019}. Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:9525932}.
Interaction partners:
- Phosphatidylinositol-3-phosphatase SAC1
- Inositol polyphosphate 5-phosphatase OCRL
- Inositol polyphosphate-4-phosphatase type I A
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Phosphatidylinositide phosphatase SAC2
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
Sequence:
MDQSVAIQETLVEGEYCVIAVQGVLCKGDSRQSRLLGLVRYRLENDAQEHALFLYTHRRMAITGDDVSLDQIVPLSKDFMLEEVSPDGELYILGSDVTVQLNTAELKLVFQLPFGSHTRTFLQEVARACPGFDPETRDPEFEWLSRHTCAEPDAESPKPREWNSDPGTRSGFAPIGGSRHQSRNARRGLEDVLPRGPGYILLWGGAAEEPEFLLAEEMHEGGPVRGRRPLAGRRDEALEEADWEMSAGGGSRERDCAGVSNVDSSRPNGRGPDQPSGARCPEKPENSLTRQNKSKSDMSEKVRSATVTVSDKAHILSVQKFGLRDTIVRSHLVQKEENYTYIQNFRFFVGTYNVNGQSPKECLRPWLSHSALAPDVYCVGFQELDLSKEAFFFHDTPKEEEWFKAVSESLHPDAKYAKVKFVRLVGIMLLLYVKQEHAAYISEVEAETVGTGIMGRMGNKGGVAIRFQLHNTSICVVNSHLAAHTEEYERRNQDYRDICSRMQFPQVDPSQPPLTINKHDVILWLGDLNYRIEELDVGKVKKLVEEKAFQTLYAHDQLKIQVAARTIFDGFTEGEITFQPTYKYDTGSDDWDTSEKCRAPAWCDRILWKGKNITQLSYQSHMALKTSDHKPVSSVFDIGVRVVNEELYRKTLEEIVRSLDKMENANIPSVTLSKREFCFENVKYMQLQTESFTIHNSQVPCQFEFINKPDEESYCKQWLTARPSKGFLLPDSHVEIELELFVNKSTATKLNSGKDTIEDILVLHLERGKDYFLSVSGNYLPSCFGSPIHTLCYMREPILDLPLKTVSDLTLMSVQTADDRSQLENPMEIPKELWMMVDYLYRNAVQQEDLFQQPGLRPEFDHIRDCLDTGMIDQLCANNHSVAEALLLFLESLPEPVICYSAYHSCLECSGNYAASKQIILTLPSFHKNVFNYLMAFLQELLKNSANNHLDENILASIFGSLLLRNPARHQKLDMAEKKKAQEFIHQFLCGPL
Protein: SCP domain-containing protein (Q9VHJ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
Sequence:
MNLLWAIVIVAELKCHTGHTVFRTRWPTYVQKKHYNIPVKPPDYCNADICPANKKHITCGFKFWSTKCGRNHEGVRMSDYRYDIVRNVNNFRRKLEWGLGNLPRAVKFKNIKWDDELSVMAMRVSNQCLQHTFSPCVNTFLYKDVGESSDFVKVQNTSKGFNVISFLNMWFEYHKMMKPSYVNNFPNIAPQDRLIIFANLIYEKNKKMGCGMVKSGQGRFLTCLFDKKIKPNQKLYTTRLNDPFRTNRKTNETESIQSNSSSTEAIVNLNTAYK
Protein: Alpha trans-inducing protein (Alpha-TIF) (G8HBG2)
Organism: Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1)
Subcellular location: Host nucleus {ECO:0000256|ARBA:ARBA00004147}. Virion tegument {ECO:0000256|ARBA:ARBA00004535}.
Interaction partners:
Sequence:
MDLLVDELFADMNADGASPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSALPTNADLYRECKFLSTLPSDVVEWGDAYVPERTQIDIRAHGDVAFPTLPATRDGLGLYYEALSRFFHAELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRDRDLGEMLRATIADRYYRETARLARVLFLHLYLFLTREILWAAYAEQMMRPDLFDCLCCDLESWRQLAGLFQPFMFVNGALTVRGVPIEARRLRELNHIREHLNLPLVRSAATEEPGAPLTTPPTLHGNQARASGYFMVLIRAKLDSYSSFTTSPSEAVMREHAYSRARTKNNYGSTIEGLLDLPDDDAPEEAGLAAPRLSFLPAGHTRRLSTAPPTDVSLGDELHLDGEDVAMAHADALDDFDLDMLGDGDSPGPGFTPHDSAPYGALDMADFEFEQMFTDALGIDEYGG
Protein: Cleavage and polyadenylation specificity factor subunit, putative (Q581U7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Cleavage and polyadenylation specificity factor-like protein, putative
- C3H1-type domain-containing protein
- Uncharacterized protein
- Cleavage and polyadenylation specificity factor 30 kDa subunit
- Cleavage and polyadenylation specificity factor subunit 2
- Nucleic acid binding protein, putative
- Uncharacterized protein
- Uncharacterized protein
- Cleavage stimulation factor 50 kDa subunit
- RNA-binding protein, putative
Sequence:
MFSHAAYSAPGVHVLDSSSPRHLAAGPQPAAAPPSTDEVEILPIGSGGEVGRSCVVVRYKGRSVMLDCGNHPAKSGLDSLPFFDSIRCDEIDLVLITHFHLDHCGALPYFCEQTSFRGRIFMTSATKAFYKMVMNDFLRIGASAEDIVNNEWLQSTIEKIETVEYHEEVTVNGIHFQPFNAGHVLGAALFMVDIAGMKLLYTGDFSRVPDRHLLGAEVPPYSPDILIAESTNGIRELESREERESLFTTWVHDVVKGGGRCLVPVFALGRAQELLLILEEYWEAHKELQHIPIYYASSLAQRCMKLYQTFVSAMNDRVKKQHENHRNPFVFKYIQSLLDTRSFEDTGPCVVLASPGMLQSGISLELFERWCGDKRNGIIVAGYCVDGTIAKDILSKPREITKPDGKVLPLRMRTIQSVSFSAHSDGRQTRDFIQALPKTKHVILVHGNVGAMGQLKNKLQQDFADRGVQVYATKNQEAIRIPFSVQRTAKVLGTLARNPPRDGEFISGVLLMSGHHTYSVVHPTDIPHFTDLDVAQIQQAIVLPLPRYKSPHEVLEMLKRYFAQSQMFSDVTPHEQQKQEGGDAANAIGGGQEQECAGNATQITVSKDVWVDVQQSTRSQTTVTVNWTSSHHNDLLADVTCIALIKLMQQEHAASSADALPVDVCGNDRLFRLKCFHHMMSQFYPSVVTNLGTGVCTVELEDGQHATITGCIEIDLQGNTKSSYSSTEVERLKTVLKRVYLTLFPIPVDQGWCDCGMIHGAEPAPIDEGA
Protein: Serotonin N-acetyltransferase (EC 2.3.1.87) (Aralkylamine N-acetyltransferase) (Q6V7J8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Acetylserotonin O-methyltransferase
- Acetylserotonin O-methyltransferase
- Aromatic-L-amino-acid decarboxylase
- Indoleamine 2,3-dioxygenase 1.
- Amine oxidase [flavin-containing]
- Amine oxidase.
- Serotonin N-acetyltransferase
- Melatonin receptor type 1C
- Melatonin receptor type 1B-B
- Tryptophan hydroxylase 1
Sequence:
MSVVSALPFLKPIHARVPISPGRQRRHTLPASEFRSLNAEDAISVFEIEREAFISVSGECPLHLDEVRHFLTLCPELSLGWFEQGRLVAFIIGSLWDQDRLTADALTLHKPHGTTVHIHVLAVHRTFRQQGKGSILLWRYLQYLRCLPYVRRAVLMCEDFLVPFYQKSGFKGQGPSEIIVGSLTFIEMYYPIRGHAFVRRNSGC
Protein: GTP-binding protein GEM (GTP-binding mitogen-induced T-cell protein) (RAS-like protein KIR) (P55040)
Organism: Homo sapiens (Human)
Function: Could be a regulatory protein, possibly participating in receptor-mediated signal transduction at the plasma membrane. Has guanine nucleotide-binding activity but undetectable intrinsic GTPase activity.
Subcellular location: Cell membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Kinesin-like protein KIF9
Sequence:
MTLNNVTMRQGTVGMQPQQQRWSIPADGRHLMVQKEPHQYSHRNRHSATPEDHCRRSWSSDSTDSVISSESGNTYYRVVLIGEQGVGKSTLANIFAGVHDSMDSDCEVLGEDTYERTLMVDGESATIILLDMWENKGENEWLHDHCMQVGDAYLIVYSITDRASFEKASELRIQLRRARQTEDIPIILVGNKSDLVRCREVSVSEGRACAVVFDCKFIETSAAVQHNVKELFEGIVRQVRLRRDSKEKNERRLAYQKRKESMPRKARRFWGKIVAKNNKNMAFKLKSKSCHDLSVL
Protein: Protein PLASTID TRANSCRIPTIONALLY ACTIVE 12, chloroplastic (pTAC12) (Plastid-encoded RNA polymerase-associated protein 5) (PEP-associated protein 5) (Protein HEMERA) (F4IHY7)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in plastid gene expression. Required in the nucleus for the initiation of photomorphogenesis mediated by phytochromes (PHYs) (e.g. PHYA and PHYB) by mediating PHYs localization to photobodies, especially in response to red and far-red light, and implicating phytochrome nuclear bodies as sites of proteolysis for PHYs and PIFs proteins (e.g. PIF1 and PIF3). Acts downstream of PHYs and upstream of DET1.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:16326926, ECO:0000269|PubMed:20603003}. Nucleus {ECO:0000269|PubMed:20603003, ECO:0000269|PubMed:22895253}. Note=Localizes to subnuclear domains in the nucleolus and in the nucleoplasm, and in chloroplasts. {ECO:0000269|PubMed:20603003}.
Interaction partners:
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 14
- PLASTID TRANSCRIPTIONALLY ACTIVE protein 6, chloroplastic
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 7
- Plastid transcriptionally active 3
- Protein PLASTID TRANSCRIPTIONALLY ACTIVE 10
- Pentatricopeptide repeat-containing protein At1g74850, chloroplastic
- Fructokinase-like 2, chloroplastic
- Protein PLASTID REDOX INSENSITIVE 2
- Fructokinase-like 1, chloroplastic
- Thioredoxin-like protein CITRX, chloroplastic
Sequence:
MASISTTTWLYRGQVCTDSGKSSNCIVQRRVKCGFPLKTLHAGITSRDRSLRHCIKCKKEDGDGDVSEGSKKSEEGFEYVTVERHPYHSYMDSTSGKLEPASGARASIPGEDYWPEGTSSRVRAARAPQPAGESSSFPSYGKNPGSRRKKNRKATEENVTVETNDEVSDSEDSSEEEENDSSDGFVTYKNEFEREEEETGFELDKKLGRPHPFIDPTKKKQIEKTLTSDESWWNWRKPEKEQWSRWQRRRPDVETVFLKAMAETGQVKLYGEEPTLTETSLYRARRHLFKEERLQAERERLAKEGPMAFYSEWVKAWKRDTSREAVQKHFEETGEDENTQLIEMFSHQTDREYRIMMGTDIRIKRDPLAMRMREDQIKQIWGGDPVYPTINYIQDPNAVMDFRGPDFHEPTPNMLSYLKENGKVISREMHEALLTKEKTEQLEVPDMDDAMAQAVDIGENDDDEDDADVEKDDEKVPRNWSVLKETPELRTAKPKPKKEGRMSLDEAVDDAENLTDFLMDFEEETDP
Protein: Cysteine/Histidine-rich C1 domain family protein (Q9LT63)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- PHD finger protein MALE MEIOCYTE DEATH 1
- Chromatin remodeling protein SHL
- PHD finger protein ALFIN-LIKE 5
- PHD finger protein MALE STERILITY 1
- Chromatin remodeling protein EBS
- Protein OBERON 1
- Protein OBERON 2
- PHD finger protein ALFIN-LIKE 7
- Sister chromatid cohesion protein SCC2
- Protein ENHANCED DOWNY MILDEW 2
Sequence:
MDTATFPVFKFRGHAHDLFIVNTPFHQCAACDRRTAVGYGVGYICNECDFSIHHICAFLFNIPEIFDHPSHDGHCLKLLTTGAPHHTDPNCHLCGKYTKSILYHCSDCKLNLDIDCISHHIFAASKDHLLVSWHHHPIQICYTDICEFCNGVNELGCHCLQCGFRIHLTCVPVFDSPEITHPSHVRLPLKLLTDGAPNYTDPRCHICGEDTQHLLYHCDICKFNLDLRCAAKSPPPIALSNLKVHEHTLTLMPRLISFVCDACGTEGDRSPYICVQCDFMIFHQKCAQLPRVIHVNHHDHRISYKYPLGPGEWRCGVCWEEIDWSYGAYPCSLCPNYAIHSLCATRKDVWDGKELDEVPEEVEDIEPFKRNDDNTITHFAHEHNLMSLGKDGEEGSYCGACARPISSYTFYKCSRSDCSFILHETCANLRKKKRHFLSPEQLVISQWKNYGNFPKWCDACLLVCSEGFVYGVMFDLVCSSIDVPFIHESHPHHLLYLKLQDGHFKTCQSCGIDHTKVVIGCLKCNYFLDFHCATLPLTVSLPRYDDHPLTLCYGEKASGKYWCDICERETNPETWFYTGLESGVTLHILCVLGDIRYAKPGGNICEGFELQLNSSSTRPICLNCKCRCPGTFFINFVGYGEDHDGYNVFFCSFYCLKHVIFRYSNDYHIMCPPWVKKLELKT
Protein: Acyl-coenzyme A oxidase 4, peroxisomal (AOX 4) (EC 1.3.3.6) (G6p) (Short-chain acyl-CoA oxidase) (AtCX4) (AtG6) (SAOX) (Q96329)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the desaturation of short-chain acyl-CoAs to 2-trans-enoyl-CoAs. Active on butyryl-CoA (C4), hexanoyl-CoA (C6), and octanoyl-CoA (C8). Has no activity as acyl-CoA dehydrogenase or on crotonyl-CoA (an unsaturated C4:1 carbocyclic ester) or glutaryl-CoA (a dicarboxylic ester). Peroxisomal fatty acid beta-oxidation is essential for embryo development. Acts as a suppressor of transcriptional silencing. Required for nuclear histone acetylation and DNA demethylation at some endogenous genomic loci.
Subcellular location: Glyoxysome {ECO:0000269|PubMed:10212254}. Peroxisome {ECO:0000269|PubMed:10212254, ECO:0000269|PubMed:31064880}.
Interaction partners:
- Peroxisomal fatty acid beta-oxidation multifunctional protein MFP2
- Probable enoyl-CoA hydratase 1, peroxisomal
- 3-ketoacyl-CoA thiolase 2, peroxisomal
- 3-ketoacyl-CoA thiolase 1, peroxisomal
- Peroxisomal fatty acid beta-oxidation multifunctional protein AIM1
- 3-ketoacyl-CoA thiolase 5, peroxisomal
- Probable acyl-CoA dehydrogenase IBR3
- Acetyl-CoA acetyltransferase 1
- Acetyl-CoA acetyltransferase 2
- Electron transfer flavoprotein subunit alpha, mitochondrial
Sequence:
MAVLSSADRASNEKKVKSSYFDLPPMEMSVAFPQATPASTFPPCTSDYYHFNDLLTPEEQAIRKKVRECMEKEVAPIMTEYWEKAEFPFHITPKLGAMGVAGGSIKGYGCPGLSITANAIATAEIARVDASCSTFILVHSSLGMLTIALCGSEAQKEKYLPSLAQLNTVACWALTEPDNGSDASGLGTTATKVEGGWKINGQKRWIGNSTFADLLIIFARNTTTNQINGFIVKKDAPGLKATKIPNKIGLRMVQNGDILLQNVFVPDEDRLPGVNSFQDTSKVLAVSRVMVAWQPIGISMGIYDMCHRYLKERKQFGAPLAAFQLNQQKLVQMLGNVQAMFLMGWRLCKLYETGQMTPGQASLGKAWISSKARETASLGRELLGGNGILADFLVAKAFCDLEPIYTYEGTYDINTLVTGREVTGIASFKPATRSRL
Protein: Putative arginine N-methyltransferase, type III (Q4QIZ0)
Organism: Leishmania major
Interaction partners:
- Putative arginine N-methyltransferase, type II
- Histone H4
- Histone H4
- Histone H4
Sequence:
MPPKQTSAGGAKKKTSTAATRNNRHAHPQADIGFLPPGAKYPAEASWNHHEHQQRNSASYNKQGDRDRNKDFDYRFEQHIFVPPRLRRVPAALVEAVNDFHYAMMNDLPRNEFYYNMLKKHIVPGESGVLEIGAGSGLLSMMAAKLNAKWVVAVEGSSEMASLARSNIATNRLQDKVKVLNMLSTELKPCDLPEPPSILVSEIFGTLLLGESALDYIADARQRLLPKTAKILPQHGVQYAVPIECETLGQICAVSSWNGIDLSHVMALQDTTSVVFTKQYGFRMSSVPFRRLADPIPLLTINFAETKRSTFKKVFPVEVPATASGTAHAWLFYWISTDGEEVMSTAPEDTLHNFSRDMQWGQALQLIDAGTNSHTPTALSMSAGEFYKFDCALSSDRVVMSLKYTGSSSAAALLKADANEAEKRRETESEQQWLPPSE
Protein: 4-amino-5-hydroxymethyl-2-methylpyrimidine phosphate synthase THI11 (HMP-P synthase) (Hydroxymethylpyrimidine phosphate synthase) (EC 2.-.-.-) (Thiamine biosynthesis protein 11) (Thiamine pyrimidine synthase) (P47183)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for the formation of the pyrimidine heterocycle in the thiamine biosynthesis pathway. Catalyzes the formation of hydroxymethylpyrimidine phosphate (HMP-P) from histidine and pyridoxal phosphate (PLP). The protein uses PLP and the active site histidine to form HMP-P, generating an inactive enzyme. The enzyme can only undergo a single turnover, which suggests it is a suicide enzyme.
Interaction partners:
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI20
- Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase THI21
- Thiamine thiazole synthase
- Putative pyridoxal kinase BUD16
- Pyridoxamine 5'-phosphate oxidase
- Thiamine biosynthetic bifunctional enzyme
- Probable pyridoxal 5'-phosphate synthase subunit SNZ2
- Thiamine transporter
- Uncharacterized protein YGR017W
- Putative pyridoxal kinase BUD17
Sequence:
MSTDKITFLLNWQPTPYHIPIFLAQTKGYFKEQGLDIAILEPTNPSDVTELIGSGKVDMGLKAMIHTLAAKARGFPVTSVASLLDEPFTGVLYLKGSGITEDFQSLKGKKIGYVGEFGKIQIDELTKHYGMKPEDYTAVRCGMNVAKYIIEDKIDAGIGIECMQQVELEEYLAKQGRPASDAKMLRIDKLACLGCCCFCTVLYICNDEFLKKNPEKVRKFLKAIKKATDYVLADPVKAWKEYIDFKPQLNNDLSYKQYQRCYAYFSSSLYNVHRDWKKVTGYGKRLAILPPDYVSNYTNEYLSWPEPEEVSDPLEAQRLMAIHQEKCRQEGTFKRLALPA
Protein: Lysophospholipase 1 (EC 3.1.1.5) (Phospholipase B 1) (Q8TG07)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Catalyzes the release of fatty acids from lysophospholipids. Phospholipase B may well contribute to pathogenicity by abetting the fungus in damaging and traversing host cell membranes, processes which likely increase the rapidity of disseminated infection (By similarity).
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- Lysophospholipase 2
- Candida glabrata strain CBS138 chromosome J complete sequence
- Lysophospholipase NTE1
- Lysophospholipase
- Candida glabrata strain CBS138 chromosome L complete sequence
- Patatin-like phospholipase domain-containing protein
- Candida glabrata strain CBS138 chromosome G complete sequence
- Candida glabrata strain CBS138 chromosome A complete sequence
- Candida glabrata strain CBS138 chromosome H complete sequence
- Candida glabrata strain CBS138 chromosome M complete sequence
Sequence:
MQLQDLVVTVSLLAAFNGGVEAWSPTNSYVPANVTCPNDINLLRNATGLSQSEIDWLKKRDVNTREALESFLKRVTSNFTSNSSASNLIDQLFSTNSSNIPKIGIAASGGGYRAMLSGAGMVSAMDNRTDGANEHGLGGLLQAATYLAGLSGGNWLTTTLSWNNWTSVQDIVDSQDNDSAIWDISHSIVSPGGINIFKTGSRWDHISDAVEDKQKAGFNVSLADVWGRALSYQFFPTLYRGGVAYLWSDLRESDVFKNAEMPMPISVADGRYPGTAVIDLNSTVFEYSPFELGSWDPSLSAFTDVQYLGTKVSDGKPAEEGKCIAGFDNVGFLMGTSSTLFNQFLLRINDTSIPKFIRNLATHFLKDLSEDYDDIAVYAPNPFRDADYVNNNRSKSLSESEYLFLVDGGEDGQNVPLVPLIQQERDLDIVFALDNSADTEENWPDGASLMHTYRRQFGFQGQGVTFPSVPGTDTFVNLGLNKKPTFFGCDARNMTDLEYIPPLIVYIPNSRHSYNGNTSTFKLSYSEKERLGVIRNGFEAATMNNLTADSNFAGCIGCAIMRRKQQALNLTLPKECETCFTNYCWNGTIDNTPAKGVTASNDFDNASGSAAADMAEQDASGAASASSSSRKKNAAVSVDVNAKTLFAIITAMTAVFQLI
Protein: Histone deacetylase RPD3 (EC 3.5.1.98) (Transcriptional regulatory protein RPD3) (P32561)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalytic component of the RPD3 histone deacetylase (HDAC) complexes RPD3C(L) and RPD3C(S) responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation plays an important role in transcriptional regulation, cell cycle progression, DNA damage response, osmotic stress response and developmental events. Is involved in rDNA and telomere silencing and in double strand breaks repair. Required for both full transcription repression and activation of many genes including cell type-specific genes (STE6, TY2 and HO), cell differentiation-specific genes (SPO13), genes that respond to external signals (PHO5) and TRK2. The RPD3 complexes regulate also chromosomal replication timing.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Chromatin modification-related protein EAF3
- Transcriptional regulatory protein UME6
- Transcriptional regulatory protein RCO1
- Transcriptional regulatory protein PHO23
- Transcriptional regulatory protein SIN3
- Transcriptional regulatory protein SDS3
- Transcriptional regulatory protein UME1
- Transcriptional regulatory protein SAP30
- Histone deacetylase complex subunit CTI6
- Transcriptional regulatory protein RXT2
Sequence:
MVYEATPFDPITVKPSDKRRVAYFYDADVGNYAYGAGHPMKPHRIRMAHSLIMNYGLYKKMEIYRAKPATKQEMCQFHTDEYIDFLSRVTPDNLEMFKRESVKFNVGDDCPVFDGLYEYCSISGGGSMEGAARLNRGKCDVAVNYAGGLHHAKKSEASGFCYLNDIVLGIIELLRYHPRVLYIDIDVHHGDGVEEAFYTTDRVMTCSFHKYGEFFPGTGELRDIGVGAGKNYAVNVPLRDGIDDATYRSVFEPVIKKIMEWYQPSAVVLQCGGDSLSGDRLGCFNLSMEGHANCVNYVKSFGIPMMVVGGGGYTMRNVARTWCFETGLLNNVVLDKDLPYNEYYEYYGPDYKLSVRPSNMFNVNTPEYLDKVMTNIFANLENTKYAPSVQLNHTPRDAEDLGDVEEDSAEAKDTKGGSQYARDLHVEHDNEFY
Protein: Cytoplasmic alpha-amylase (EC 3.2.1.1) (1,4-alpha-D-glucan glucanohydrolase) (P26612)
Organism: Escherichia coli (strain K12)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:1400215}.
Interaction partners:
- Glycogen debranching enzyme
- 1,4-alpha-glucan branching enzyme GlgB
- Periplasmic alpha-amylase
- Maltodextrin glucosidase
- Glycogen phosphorylase
- 4-alpha-glucanotransferase
- Maltodextrin phosphorylase
- Flagellar protein FliT
Sequence:
MRNPTLLQCFHWYYPEGGKLWPELAERADGFNDIGINMVWLPPAYKGASGGYSVGYDSYDLFDLGEFDQKGSIPTKYGDKAQLLAAIDALKRNDIAVLLDVVVNHKMGADEKEAIRVQRVNADDRTQIDEEIIECEGWTRYTFPARAGQYSQFIWDFKCFSGIDHIENPDEDGIFKIVNDYTGEGWNDQVDDELGNFDYLMGENIDFRNHAVTEEIKYWARWVMEQTQCDGFRLDAVKHIPAWFYKEWIEHVQEVAPKPLFIVAEYWSHEVDKLQTYIDQVEGKTMLFDAPLQMKFHEASRMGRDYDMTQIFTGTLVEADPFHAVTLVANHDTQPLQALEAPVEPWFKPLAYALILLRENGVPSVFYPDLYGAHYEDVGGDGQTYPIDMPIIEQLDELILARQRFAHGVQTLFFDHPNCIAFSRSGTDEFPGCVVVMSNGDDGEKTIHLGENYGNKTWRDFLGNRQERVVTDENGEATFFCNGGSVSVWVIEEVI
Protein: Insulin receptor-related protein (IRR) (EC 2.7.10.1) (IR-related receptor) [Cleaved into: Insulin receptor-related protein alpha chain; Insulin receptor-related protein beta chain] (P14616)
Organism: Homo sapiens (Human)
Function: Receptor with tyrosine-protein kinase activity. Functions as a pH sensing receptor which is activated by increased extracellular pH. Activates an intracellular signaling pathway that involves IRS1 and AKT1/PKB.
Subcellular location: Membrane; Single-pass type I membrane protein.
Interaction partners:
- Insulin receptor
- Insulin
- Insulin-like growth factor 1 receptor
- Growth factor receptor-bound protein 2
- Tyrosine-protein phosphatase non-receptor type 1
- Son of sevenless homolog 2
- Son of sevenless homolog 1
- Insulin-like growth factor 1
- Insulin receptor substrate 1
- Phosphatidylinositol 3-kinase regulatory subunit alpha
Sequence:
MAVPSLWPWGACLPVIFLSLGFGLDTVEVCPSLDIRSEVAELRQLENCSVVEGHLQILLMFTATGEDFRGLSFPRLTQVTDYLLLFRVYGLESLRDLFPNLAVIRGTRLFLGYALVIFEMPHLRDVALPALGAVLRGAVRVEKNQELCHLSTIDWGLLQPAPGANHIVGNKLGEECADVCPGVLGAAGEPCAKTTFSGHTDYRCWTSSHCQRVCPCPHGMACTARGECCHTECLGGCSQPEDPRACVACRHLYFQGACLWACPPGTYQYESWRCVTAERCASLHSVPGRASTFGIHQGSCLAQCPSGFTRNSSSIFCHKCEGLCPKECKVGTKTIDSIQAAQDLVGCTHVEGSLILNLRQGYNLEPQLQHSLGLVETITGFLKIKHSFALVSLGFFKNLKLIRGDAMVDGNYTLYVLDNQNLQQLGSWVAAGLTIPVGKIYFAFNPRLCLEHIYRLEEVTGTRGRQNKAEINPRTNGDRAACQTRTLRFVSNVTEADRILLRWERYEPLEARDLLSFIVYYKESPFQNATEHVGPDACGTQSWNLLDVELPLSRTQEPGVTLASLKPWTQYAVFVRAITLTTEEDSPHQGAQSPIVYLRTLPAAPTVPQDVISTSNSSSHLLVRWKPPTQRNGNLTYYLVLWQRLAEDGDLYLNDYCHRGLRLPTSNNDPRFDGEDGDPEAEMESDCCPCQHPPPGQVLPPLEAQEASFQKKFENFLHNAITIPISPWKVTSINKSPQRDSGRHRRAAGPLRLGGNSSDFEIQEDKVPRERAVLSGLRHFTEYRIDIHACNHAAHTVGCSAATFVFARTMPHREADGIPGKVAWEASSKNSVLLRWLEPPDPNGLILKYEIKYRRLGEEATVLCVSRLRYAKFGGVHLALLPPGNYSARVRATSLAGNGSWTDSVAFYILGPEEEDAGGLHVLLTATPVGLTLLIVLAALGFFYGKKRNRTLYASVNPEYFSASDMYVPDEWEVPREQISIIRELGQGSFGMVYEGLARGLEAGEESTPVALKTVNELASPRECIEFLKEASVMKAFKCHHVVRLLGVVSQGQPTLVIMELMTRGDLKSHLRSLRPEAENNPGLPQPALGEMIQMAGEIADGMAYLAANKFVHRDLAARNCMVSQDFTVKIGDFGMTRDVYETDYYRKGGKGLLPVRWMAPESLKDGIFTTHSDVWSFGVVLWEIVTLAEQPYQGLSNEQVLKFVMDGGVLEELEGCPLQLQELMSRCWQPNPRLRPSFTHILDSIQEELRPSFRLLSFYYSPECRGARGSLPTTDAEPDSSPTPRDCSPQNGGPGH
Protein: ELAV-like protein (Q6P105)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Glial fibrillary acidic protein
- Neurogenin-1
- Melanocyte inducing transcription factor a isoform 1
- Neurogenic differentiation factor 1
- Histone H2B
- Histone H2B 3
- Brain-type fatty acid-binding protein
- DnaJ homolog subfamily C member 2
- Vesicular glutamate transporter 2.1
- Insulin gene enhancer protein isl-2b
Sequence:
MVTIISTMETQVSNGPSGTSLPNGPVISTNGATDDSKTNLIVNYLPQNMTQEEFKSLFGSIGEIESCKLVRDKITGQSLGYGFVNYVDPNDADKAINTLNGLKLQTKTIKVSYARPSSASIRDANLYVSGLPKTMSQKDMEQLFSQYGRIITSRILVDQVTAGISRGVGFIRFDKRNEAEEAIKGLNGQKPLGAAEPITVKFANNPSQKTGQALLTQLYQTAARRYTGPLHHQTQRFRLDNLLNASYGVKRFSPITIDSMTSLAGVNLTGPTGAGWCIFVYNLSPEADESVLWQLFGPFGAVTNVKVIRDFTTNKCKGFGFVTMTNYDEAAMAIASLNGYRLGDRVLQVSFKTSKQHKA
Protein: Aldose 1-epimerase (EC 5.1.3.3) (Galactose mutarotase) (Type-1 mutarotase) (P0A9C3)
Organism: Escherichia coli (strain K12)
Function: Mutarotase converts alpha-aldose to the beta-anomer. It is active on D-glucose, L-arabinose, D-xylose, D-galactose, maltose and lactose.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Galactokinase
- UDP-glucose 4-epimerase
- Galactose-1-phosphate uridylyltransferase
- Beta-galactosidase
- Glucokinase
- Alpha-D-glucose 1-phosphate phosphatase YihX
- Evolved beta-galactosidase subunit alpha
- Glucose-1-phosphatase
- Alpha-galactosidase
- Evolved beta-galactosidase subunit beta
Sequence:
MLNETPALAPDGQPYRLLTLRNNAGMVVTLMDWGATLLSARIPLSDGSVREALLGCASPECYQDQAAFLGASIGRYANRIANSRYTFDGETVTLSPSQGVNQLHGGPEGFDKRRWQIVNQNDRQVLFALSSDDGDQGFPGNLGATVQYRLTDDNRISITYRATVDKPCPVNMTNHVYFNLDGEQSDVRNHKLQILADEYLPVDEGGIPHDGLKSVAGTSFDFRSAKIIASEFLADDDQRKVKGYDHAFLLQAKGDGKKVAAHVWSADEKLQLKVYTTAPALQFYSGNFLGGTPSRGTEPYADWQGLALESEFLPDSPNHPEWPQPDCFLRPGEEYSSLTEYQFIAE