wanglab/gogpt-training-data huggingface dataset:
Protein: L-glutamyl-[BtrI acyl-carrier protein] decarboxylase (EC 4.1.1.95) (Butirosin biosynthesis protein K) (Q2L4H3)
Organism: Niallia circulans (Bacillus circulans)
Function: Pyridoxal phosphate-dependent decarboxylase that catalyzes 1 step in the biosynthesis of the side chain of the aminoglycoside antibiotics in the biosynthetic pathway of butirosin. Able to decarboxylate L-ornithine, L-arginine, L-lysine, but not L-glutamate or any D-amino acids. Has low activity with substrates not bound to an acyl-carrier protein.
Interaction partners:
Sequence:
MNLDQAEITALTKRFETPFYLYDGDFIEAHYRQLRSRTNPAIQFYLSLKANNNIHLAKLFRQWGLGVEVASAGELALARHAGFSAENIIFSGPGKKRSELEIAVQSGIYCIIAESVEELFYIEELAEKENKTARVAIRINPDKSFGSTAIKMGGVPRQFGMDESMLDAVMDAVRSLQFTKFIGIHVYTGTQNLNTDSIIESMKYTVDLGRNIYERYGIVCECINLGGGFGVPYFSHEKALDIGKITRTVSDYVQEARDTRFPQTTFIIESGRYLLAQAAVYVTEVLYRKASKGEVFVIVDGGMHHHAASTFRGRSMRSNYPMEYIPVREDSGRRELEKVTIAGPLCTPEDCLGKDVHVPALYPGDLVCVLNSGAYGLSFSPVHFLGHPTPIEILKRNGSYELIRRKGTADDIVATQLQTESNLLFVDK
Protein: Protein transport protein SEC22 (O97323)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004163}; Single-pass type IV membrane protein {ECO:0000256|ARBA:ARBA00004163}. Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004394}.
Interaction partners:
- Syntaxin, Qa-SNARE family
- Protein transport protein BOS1, putative
- BET1-like protein, putative
- Protein transport protein SEC23
- Syntaxin, Qa-SNARE family
- Sec1 family protein, putative
- Protein transport protein Sec24A
- Alpha-soluble NSF attachment protein, putative
- SNARE protein, putative
- Syntaxin, Qa-SNARE family
Sequence:
MCDVVLLCRVSDGMTLVETNSETKSISHKLELKKLCKKLYSFPNLSTVTSNNFNYHFLIENGIAYIAVFPVTYPKKLAFLFLNDICKQFNEELMIQYGTHSIDYRSIIETIEKPYSFIKFDRKITKIKQEYKDPRSNIAIKKLNESLNEVSSIMKKNIDDILMRGENLEDVGRKAFNLKYESEKFKKVSRVLNLKYALYQYGILASIVIFFFLIIIFKNYF
Protein: Proline dehydrogenase 1, mitochondrial (EC 1.5.5.2) (Proline oxidase) (Q9WU79)
Organism: Mus musculus (Mouse)
Function: Converts proline to delta-1-pyrroline-5-carboxylate.
Subcellular location: Mitochondrion matrix.
Interaction partners:
- Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
- Pyrroline-5-carboxylate reductase 3
- Pyrroline-5-carboxylate reductase 2
- Pyrroline-5-carboxylate reductase 1, mitochondrial
- Prolyl 4-hydroxylase subunit alpha-2
- Prolyl 4-hydroxylase subunit alpha-1
- Prolyl 4-hydroxylase subunit alpha-3
- Cytosol aminopeptidase
- Catechol O-methyltransferase
- Ornithine aminotransferase, mitochondrial
Sequence:
MALKRVFLLRSVAPRVAALSTKPQAQEQPPASPEALRGCGAAKAVRPPVPAVDFTNTQEAYRSRRSWELVRNLLVLRLCASPVLLAHHEQLFQVARKLLGQRMFERLMKMTFYGHFVAGEDQESIRPLIRHNKAFGVGFILDYGVEEDLSPEEAERKEMESCTSEAERDGSGANKREKQYQVHPAFGDRRDGVISARTYFYANEAKCDNYMENLLQCIKASGGASDGGFSAIKLTALGRPQFLLQFSDVLTRWRRFFHQMAAEQGQAGRAAVDTKLEVAVLQDSIAKMGIASRAEIEGWFTPETLGVSGTVDLLDWNSLIDSRTRLSRHLVVPNVQTGQLEPLLSRFTEEEEQQMKRMLQRMDVLAKKAKEAGVRLMIDAEQSYFQPAISRLTLEMQRRFNVDKPFIFNTFQCYLKDAYDNVTLDMELARREGWCFGAKLVRGAYMAQERVRAAEIGYEDPINPTYEATNAMYHRCLNYVLEELKHSTKAEVMVASHNEDTVHFTLCRMKEIGLHPADGQVCFGQLLGMCDQISFPLGQAGFPVYKYVPYGPVMEVLPYLSRRALENSSIMKGAQRERQLLWQELRRRLRTGSLFHHPA
Protein: Cadherin domain-containing protein (Q3TVS7)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004251}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004251}.
Interaction partners:
Sequence:
MLRMRTTGWARGWCLGCCLLLPLCFSLAAAKQLLRYRLAEEGPADVRIGNVASDLGIVTGSGEVTFSLESGSEYLKIDNLTGELSTSERRIDREKLPQCQMIFDENECFLDFEVSVIGPSQSWVDLFEGRVIVLDINDNTPTFPSPVLTLTVEENRPVGTLYLLPTATDRDFGRNGIERYELLQEPGGGGGSGEGRRLGPADSAPYPGGGGNSASGGGSGGSKRRLDAPEGGGGTSPSGRSSVFELQVADTPDGEKQPQLIVKGALDREQRDSYELTLRVRDGGDPPRSSQAILRVLITDVNDNSPRFEKSVYEADLAENSAPGTPILQLRATDLDVGVNGQIEYVFGAATESVRRLLRLDETSGWLSVLHRIDREEVNQLRFTVMARDRGQPPKTDKATVVLNIKDENDNVPSIEIRKIGRIPLKDGVANVAEDVLVDTPIALVQVSDRDQGENGVVTCTVVGDVPFQLKPASDTEGDQNKKKYFLHTSAPLDYETTREFNVVIVAVDSGSPSLSSNNSLVVKVGDTNDNPPVFGQSVVEVYFPENNIPGERVATVLATDADSGKNAEIAYSLDSSVMGTFAIDPDSGDILVNTVLDREQTDRYEFKVNAKDKGIPVLQGSTTVIVQVADKNDNDPKFMQDVFTFYVKENLQPNSPVGMVTVMDADKGRNAEMSLYIEENSNIFSIENDTGTIYSTMSFDREHQTTYTFRVKAVDGGDPPRSATATVSLFVMDENDNAPTVTLPRNISYTLLPPSSNVRTVVATVLATDSDDGINADLNYSIVGGNPFKLFEIDSTSGVVSLVGKLTQKHYGLHRLVVQVNDSGQPSQSTTTLVHVFVNESVSNATVIDSQIVRSLHTPLTQDIAGDPSYEISKQRLSIVIGVVAGIMTVILIILIVMMARYCRSKNKNGYEAGKKDHEDFFTPQQHDKSKKPKKDKKNKKSKQPLYSSIVTVEASKPNGQRYDSVNEKLSDSPCMGRYRSVNGGPGSPDLARHYKSSSPLPTVQLHPQSPTAGKKHQAVQDLPPANTFVGAGDNISIGSDHCSEYSCQTSNKYSKQMRVHPYITVFG
Protein: AT5g58640/mzn1_90 (Selenoprotein, Rdx type) (Q8W1E5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDRAQLILLGLPIFLFCSDLFNLFTPPPPKPQPHRPHQPPHIPHQHRPNAIIPETLDFPSQKTSGLGGAIGYGNTVEINFCVSCSYKGTAVTMKKMLETAFPGLDVILANYPPPAPKRLLAKVVPVVQMGVIGMIVAGDRILPMIGITNPPAWFHSLRANRFGSMASTWLIGNFLQSYLQSSGAFEVHCNGEPVFSKLKEGRFPGEIELRDLISKTLTRPSILTGSSY
Protein: 1,3-beta-glucanosyltransferase (EC 2.4.1.-) (G8B692)
Organism: Candida parapsilosis (strain CDC 317 / ATCC MYA-4646) (Yeast) (Monilia parapsilosis)
Subcellular location: Cell envelope {ECO:0000256|ARBA:ARBA00004196}. Cell membrane {ECO:0000256|RuleBase:RU361209}; Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU361209}. Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004589}.
Interaction partners:
Sequence:
MLFKSLLTYISLVSTVLAIPAIEVQGNAFWNTETGKRFYIRGVDYQPGGSSELEDPLADTKVCERDIPYFQELGINTIRVYSVDNTKDHDECMDKLAEAGIYVILDVNTPHSSITRSNSECSYNSDYLQEVFASAQMFAQYNNTLGFFAGNEVINDGASLDSAPYVKAVVRDLKTFIKNRGFRTIPVGYSAASVDEYRLASGLYFNCGDDEMARIDMYGINDYSWCGDASMTTSQYSQQMKDFKNFTVPLFFSEFGCNAKKPRPFTEIEAIYSTDMSSVFSGGLVYEYSEEDNEYGLVKLGDDDDDDDVTPNQDFKNLKNEFNKTENPSGDGGASKDLTGGNNCPSKSSLWNVTEEIPDTPGGAIKYLKGVAEPTGHGFDAYVQGNCHGNNDVDDSGNYTSSVGASTRDASATSSSAQSSSGSSSSSSGSTSSGSKENQGVVAATTSVTGVVGLLALIAGFVVV
Protein: Beta-sarcoglycan (Q3ZB93)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane, sarcolemma {ECO:0000256|ARBA:ARBA00004274}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004274}. Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
- Dystrophin
- Delta-sarcoglycan)
- Alpha-sarcoglycan
- Dystroglycan 1
- Gamma-sarcoglycan
Sequence:
MASEQEISNAPMKKSMREKAIERRSANKEHNSNFKAGYVPIEEERLHKTGLRGRKGIFAIGIIILLFLLALINLIITLVIWTVIRIGPGGCESMEFHESGLLRFKQKADMGIVHPLHKSTVGGRKDQDLVITGNNNPVVFRQGNTKLSVEEDKTSIVSDLGISFTDPRTQNTFFSTDFDTHEFHLPKEVKVLNVKKASTERITSNASSDLTIKGDGKAIIRGNEGVYIMGKTVEFSMGGGIELKAENSIILNGSVMISPSRIPNSSLGGDLYFNDGLERYKLCMCADGTLFRVQVKYSNMGCQTSDNPCGAAH
Protein: Sentan (Protein S100-A1-like) (S100 calcium-binding protein A1-like) (Q8C9X1)
Organism: Mus musculus (Mouse)
Function: May be a component of the linker structure that bridges the ciliary membrane and peripheral singlet microtubules.
Subcellular location: Cell projection, cilium {ECO:0000269|PubMed:18829862}. Note=Expressed exclusively at the cilium tip where it localizes between the cell membrane and peripheral A-subfibers.
Interaction partners:
- Protein FAM216B
- Low density lipoprotein receptor class A domain containing 1
Sequence:
MGGCMHSTWDHALHSRGEPRPSEAPASISAPSKMPKSVSISKQLASIKALKKGSDLEKAIATIALVFRNASDPDGKLGKATAKKLLQTQFKKFTEREETKPKYQDILSELDEHTENKLDFEDFVILLLSLAIMSDLLRNMWNENTMK
Protein: Polypeptide N-acetylgalactosaminyltransferase 6 (EC 2.4.1.41) (Polypeptide GalNAc transferase 6) (GalNAc-T6) (pp-GaNTase 6) (Protein-UDP acetylgalactosaminyltransferase 6) (UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 6) (Q8NCL4)
Organism: Homo sapiens (Human)
Function: Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. May participate in synthesis of oncofetal fibronectin. Has activity toward MUC1A, MUC2, EA2 and fibronectin peptides. Glycosylates FGF23.
Subcellular location: Golgi apparatus membrane {ECO:0000250|UniProtKB:Q14435}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q14435}.
Interaction partners:
- Beta-1,3-galactosyl-O-glycosyl-glycoprotein beta-1,6-N-acetylglucosaminyltransferase
- Alpha-N-acetylgalactosaminide alpha-2,6-sialyltransferase 1
- Acetylgalactosaminyl-O-glycosyl-glycoprotein beta-1,3-N-acetylglucosaminyltransferase
- Glycoprotein-N-acetylgalactosamine 3-beta-galactosyltransferase 1
- Beta-1,4 N-acetylgalactosaminyltransferase 1
- C1GALT1-specific chaperone 1
Sequence:
MRLLRRRHMPLRLAMVGCAFVLFLFLLHRDVSSREEATEKPWLKSLVSRKDHVLDLMLEAMNNLRDSMPKLQIRAPEAQQTLFSINQSCLPGFYTPAELKPFWERPPQDPNAPGADGKAFQKSKWTPLETQEKEEGYKKHCFNAFASDRISLQRSLGPDTRPPECVDQKFRRCPPLATTSVIIVFHNEAWSTLLRTVYSVLHTTPAILLKEIILVDDASTEEHLKEKLEQYVKQLQVVRVVRQEERKGLITARLLGASVAQAEVLTFLDAHCECFHGWLEPLLARIAEDKTVVVSPDIVTIDLNTFEFAKPVQRGRVHSRGNFDWSLTFGWETLPPHEKQRRKDETYPIKSPTFAGGLFSISKSYFEHIGTYDNQMEIWGGENVEMSFRVWQCGGQLEIIPCSVVGHVFRTKSPHTFPKGTSVIARNQVRLAEVWMDSYKKIFYRRNLQAAKMAQEKSFGDISERLQLREQLHCHNFSWYLHNVYPEMFVPDLTPTFYGAIKNLGTNQCLDVGENNRGGKPLIMYSCHGLGGNQYFEYTTQRDLRHNIAKQLCLHVSKGALGLGSCHFTGKNSQVPKDEEWELAQDQLIRNSGSGTCLTSQDKKPAMAPCNPSDPHQLWLFV
Protein: Klrc1 protein (A6H5Z4)
Organism: Mus musculus (Mouse)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
Sequence:
MSNERVTYAELKVAKNSRNQHRKPRGPRSSISVIEQEIIYSDFSFQNPSQEQPWICRNCPCKGFPSPPEKLIAGTLGLICFVLIVAVVVITTVATPYTEAKAQINSSMTRTHRDINYTLSSAQPCPHCPKEWISYSHNCYFIGMERKSWNDSLGSCISKNCSLLHIDSEEEQDFLQSLSLISWTGILRKGRGQPWVWKEDSIFKPKIAEILHDECNCAMMSASGLTADNCTTLHPYLCKCKFPI
Protein: Cell division protein kinase 5 (A0A090N7W4)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MQKYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLHDVLHSDKKLTLVFEFCDQDLKKYFDSCNGDLDPEIVKSFLFQLLKGLGFCHSRNVLHRDLKPQNLLINRNGELKLADFGLARAFGIPVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLKRIFRLLGTPTEEQWPSMTKLPDYKPYPMYPATTSLVNVVPKLNATGRDLLQNLLKCNPVQRISAEEALQHPYFSDFCPP
Protein: Omega-hydroxyceramide transacylase (EC 2.3.1.296) (Patatin-like phospholipase domain-containing protein 1) (Q3V1D5)
Organism: Mus musculus (Mouse)
Function: Omega-hydroxyceramide transacylase involved in the synthesis of omega-O-acylceramides (esterified omega-hydroxyacyl-sphingosine; EOS), which are extremely hydrophobic lipids involved in skin barrier formation. Catalyzes the last step of the synthesis of omega-O-acylceramides by transferring linoleic acid from triglycerides to an omega-hydroxyceramide. Omega-O-acylceramides, are required for the biogenesis of lipid lamellae in the stratum corneum and the formation of the cornified lipid envelope which are essential for the epidermis barrier function. These lipids also play a role in keratinocyte differentiation. May also act on omega-hydroxylated ultra-long chain fatty acids (omega-OH ULCFA) and acylglucosylceramides (GlcEOS).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q8N8W4}.
Interaction partners:
- 1-acylglycerol-3-phosphate O-acyltransferase ABHD5
- Magnesium transporter NIPA4
- Lipase member N
- Ceramide synthase 3
- Hydroperoxide isomerase ALOXE3
- Calcium-independent phospholipase A2-gamma
- Protein-glutamine gamma-glutamyltransferase K
- Glucosylceramide transporter ABCA12
Sequence:
MDEQVFKGDPDTPHSISFSGSGFLSYYQAGAVDALRDLAPRMLDTAHRFAGTSAGAVIAALVVCGIEMEKYLRVLNMGLAEVKKFFLGPLSPSCKMVQMMRQFLYDVLPEDSYKFATGKLHVSLTRVTDGENVVVSEYRSKEELIEALYCSCFVPVYCGFIPPTYRGERYIDGGFTSMQPCSFWTDSITISTFSSQQDICPRDCPTIFHDFRMFNFSFQFSLENITRMTHALFPPDLVILQEYYYRGYNDAVSYLRRLNAAYLDSPSKRVIFPRVEVYCQIEVALGHEPPPPSLQNLPALRRSPADSSQTHAQGSPKKDRKDSHSSAAPSVQTPESGCKESVESPVSLRVSISKQPSVSPLSPAQPVPVMRPTGPRDSCPINVQTPNPERGVKGALDSATERGMKDALASATDEQSTTTLPPVLLPAADSRGSKTGSSVPIGSPESPRLLLRSSQGATASRATLGLPPLSPSTPPAGPPVEDLGPERPTATGSPALSQLTGSAAPGTGKKAPHKPLLVEGPGEDSNTAKTMFKRKQKTNATRECFHRNAQSKKPASKLKSAPCPLNFPVLPKRVWVTYKPHPSRIQDYSYPEGVSGQNS
Protein: O-glycoside alpha-1,2-mannosyltransferase homolog 3 (EC 2.4.1.-) (O74546)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Probable mannosyltransferase involved in O-glycosylation of cell wall and secreted proteins.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}. Golgi apparatus membrane {ECO:0000269|PubMed:16823372}; Single-pass type II membrane protein {ECO:0000269|PubMed:16823372}.
Interaction partners:
- ERAD-associated E3 ubiquitin-protein ligase hrd1
Sequence:
MGIPKSSIYFCILLFCIISFYLQSSKDGPKELKVKYVFLKKATAKQRGESSLTDSDYFPKQPNMNATLFMLCRNRDIKDALVSIQSVEDRFNHRYHYPWTFMNDAPFTKEFITATSKMVSGDATYVQLNNEEWGIPINIDLNRMLKSIRDMTDDKVIYGFSLSYRIMCRFNSGFFYRNKALSHYDYYWRVEPGVEYSCDIPYDPFRKLSDENKAYGFVISMTDYYETLPSLWNVTRDFIHQNPQYLAQNNSLDFIVNDHQGLSGDYNLCHFWSNFEIANLNFFRSPAYTDYFAHLDKNYGFFYERWGDAPVHSLAASLFLNKSQIHYFEDFGYYHLPWYHCPTDVQSHATARCLCDPTGTIDYLPFSCAIKWLENINS
Protein: Transcription factor 7-like 1 (HMG box transcription factor 3) (TCF-3) (Q9HCS4)
Organism: Homo sapiens (Human)
Function: Participates in the Wnt signaling pathway. Binds to DNA and acts as a repressor in the absence of CTNNB1, and as an activator in its presence. Necessary for the terminal differentiation of epidermal cells, the formation of keratohyalin granules and the development of the barrier function of the epidermis (By similarity). Down-regulates NQO1, leading to increased mitomycin c resistance.
Subcellular location: Nucleus.
Interaction partners:
- Catenin beta-1
- C-terminal-binding protein 1
- Transcription factor 7-like 2
- Junction plakoglobin
- Telomerase reverse transcriptase
- C-terminal-binding protein 2
- Serine/threonine-protein kinase NLK
- Transcription factor SOX-17
- Histone acetyltransferase p300
- Transcription factor 7
Sequence:
MPQLGGGGGGGGGGSGGGGGSSAGAAGGGDDLGANDELIPFQDEGGEEQEPSSDSASAQRDLDEVKSSLVNESENQSSSSDSEAERRPQPVRDTFQKPRDYFAEVRRPQDSAFFKGPPYPGYPFLMIPDLSSPYLSNGPLSPGGARTYLQMKWPLLDVPSSATVKDTRSPSPAHLSNKVPVVQHPHHMHPLTPLITYSNDHFSPGSPPTHLSPEIDPKTGIPRPPHPSELSPYYPLSPGAVGQIPHPLGWLVPQQGQPMYSLPPGGFRHPYPALAMNASMSSLVSSRFSPHMVAPAHPGLPTSGIPHPAIVSPIVKQEPAPPSLSPAVSVKSPVTVKKEEEKKPHVKKPLNAFMLYMKEMRAKVVAECTLKESAAINQILGRKWHNLSREEQAKYYELARKERQLHSQLYPTWSARDNYGKKKKRKREKQLSQTQSQQQVQEAEGALASKSKKPCVQYLPPEKPCDSPASSHGSMLDSPATPSAALASPAAPAATHSEQAQPLSLTTKPETRAQLALHSAAFLSAKAAASSSGQMGSQPPLLSRPLPLGSMPTALLASPPSFPATLHAHQALPVLQAQPLSLVTKSAH
Protein: Alpha-amylase-related protein (EC 3.2.1.1) (O18408)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Secreted {ECO:0000305}.
Interaction partners:
- 1,4-alpha-glucan branching enzyme
- Glycogen phosphorylase
- Glycogen debranching enzyme
- Alpha-amylase B
- alpha-glucosidase
- alpha-glucosidase
- Maltase A1
- Cytochrome c oxidase subunit 2
- alpha-glucosidase
- alpha-glucosidase
Sequence:
MFKFALTLTLCLAGSLSLAQHNPHWWGNRNTIVHLFEWKWSDIAQECESFLGPRGFAGVQVSPVNENILSAGRPWWERYQPISYKLTTRSGNEEEFGDMVRRCNDVGVRIYVDVLLNHMSGDFDGVAVGTAGTEAEPSKKSFPGVPYTAQDFHPTCEITDWNDRFQVQQCELVGLKDLDQSSDWVRSKLIEFLDHLIELGVAGFRVDAAKHMASEDLEYIYSSLSNLNIDHGFPHNSRPFIFQEVIDHGHETVSRDEYKDLGAVTEFRFSEEIGNAFRGNNALKWLQSWGTDWGFLPSGQALTFVDNHDNQRDAGAVLNYKSPRQYKMATAFHLAYPYGISRVMSSFAFDDHDTPPPQDAQERIISPEFDADGACVNGWICEHRWRQIYAMVGFKNAVRDTEITGWWDNGDNQISFCRGNKGFLAINNNLYDLSQDLNTCLPAGTYCDVISGSLIDGSCTGKSVTVNENGYGYIHIGSDDFDGVLALHVDAKV
Protein: Putative aliphatic sulfonates-binding protein (P75853)
Organism: Escherichia coli (strain K12)
Function: Part of a binding-protein-dependent transport system for aliphatic sulfonates. Putative binding protein.
Subcellular location: Periplasm {ECO:0000305}.
Interaction partners:
- FMN reductase
- Alkanesulfonate monooxygenase
- Putative aliphatic sulfonates transport permease protein SsuC
- Aliphatic sulfonates import ATP-binding protein SsuB
- Taurine transport system permease protein TauC
- Taurine-binding periplasmic protein
- Taurine import ATP-binding protein TauB
- Alpha-ketoglutarate-dependent taurine dioxygenase
- Probable ABC transporter permease protein YphD
- Thiosulfate-binding protein
Sequence:
MRNIIKLALAGLLSVSTFAVAAESSPEALRIGYQKGSIGMVLAKSHQLLEKRYPESKISWVEFPAGPQMLEALNVGSIDLGSTGDIPPIFAQAAGADLVYVGVEPPKPKAEVILVAENSPIKTVADLKGHKVAFQKGSSSHNLLLRALRQAGLKFTDIQPTYLTPADARAAFQQGNVDAWAIWDPYYSAALLQGGVRVLKDGTDLNQTGSFYLAARPYAEKNGAFIQGVLATFSEADALTRSQREQSIALLAKTMGLPAPVIASYLDHRPPTTIKPVNAEVAALQQQTADLFYENRLVPKKVDIRQRIWQPTQLEGKQL
Protein: RE41896p (Q86P35)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
VHSRLESPAPRIQNFKFVYGNRVRVCVSCVRAGWPAGPLFRALDFAQKLISSERKLSHYVITPKSPLLHNKLQKYKMGSIYGLLPLLLLLCRLHDGGSKFVSPTRHTDLSSTIIIVEDAKACFRRVLAGKRIAPHFVRRSISCERVEECMRECGRERRFMCEGFNYRLDPSGHGQGDCELVEMPLAQMDLYSSPDRRDANLLRHPDYDYYERDRNAPSSCRRSACQDCSKGPVSSQPVYFKPSGGAGGYGDRDRDRDRDRDHYRPHSNTAVDHYRGPSGPPGSSSYEHRPPYSSEFHGSHSSSSSASSYEFSSHGSGSSSGSSSGYFGHTPPSSYGGDHPYVDRHDSPHYRPGRPDRWETLPSSSGYDSSAYRPPRPETDRIDKYRPPYRPGSDYSPYRPPSRPSHNYLDRDGAGPPGPPGSNKKPNKFVPYLIGGEDNWGHYGGSYGGSSKHSSSSSSSYWGLTESQRRKDQHDFNYFQLGAPHRESNSVLSYPGSGYEDDYPRRRNDYRQQWTRRAGPDECSAKTSEGFRLHKTAVRHAYNVPTLTECERLCSDPRPSFVCHTFSYRYNQAGRDNCMLCDRPINMLDYYVDIEPDRDYDIYSMADDMDVCRQPPPRRHDTAGPSTAISDPRNAQCFFRAIDATRFFKSIVRDSLTVRSVGECEMECTRSTKFTCRAFAFRYGQQRHAGVIDNCQLSDWPVRDMDKERHLILDAAFDIFERASYGHGCEIQPIVDEKHKKLCYLGYGSPARLLPPAIKKVISVPSEIACKKECIRFRETTPFKCFAFSYGSHASSFNCELSDLDQTELKQDVHYAHTKDRDFWLFAWNPFDWTCRDKVNTIGGSRVNNDRRMDIFREPGDVAWRHYTVSGKPCRRSSPCAKNLITGFYSCETDASEVGSWDYCCKADHPCGYSKGFDYPWCFVGDESDQWRKCSDRYFPGKNGTQPTHSHLGLPSAKEKQKHPHPHHSQPATAASSEYSQHPPRPGGLQSLSDFAAARLWPVTYLYSEGPPNATEFSNFVDCNKESC
Protein: Sugar transport protein 6 (Hexose transporter 6) (Q9SFG0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Mediates an active uptake of hexoses, probably by sugar/hydrogen symport. Can transport glucose, 3-O-methylglucose, mannose, fructose and galactose, and, to a lower extent, xylose and ribulose.
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Protein FANTASTIC FOUR 4
- Germin-like protein subfamily 2 member 3
- Sucrose transport protein SUC9
- Protein trichome birefringence-like 10
Sequence:
MAVVVSNANAPAFEAKMTVYVFICVMIAAVGGLIFGYDIGISGGVSAMDDFLKEFFPAVWERKKHVHENNYCKYDNQFLQLFTSSLYLAALVASFVASATCSKLGRRPTMQFASIFFLIGVGLTAGAVNLVMLIIGRLFLGFGVGFGNQAVPLFLSEIAPAQLRGGLNIVFQLMVTIGILIANIVNYFTATVHPYGWRIALGGAGIPAVILLFGSLLIIETPTSLIERNKNEEGKEALRKIRGVDDINDEYESIVHACDIASQVKDPYRKLLKPASRPPFIIGMLLQLFQQFTGINAIMFYAPVLFQTVGFGSDAALLSAVITGSINVLATFVGIYLVDRTGRRFLLLQSSVHMLICQLIIGIILAKDLGVTGTLGRPQALVVVIFVCVYVMGFAWSWGPLGWLIPSETFPLETRSAGFAVAVSCNMFFTFVIAQAFLSMLCGMRSGIFFFFSGWIIVMGLFAFFFIPETKGIAIDDMRESVWKPHWFWKRYMLPEDDHHDIEKRNA
Protein: Rap1 GTPase-GDP dissociation stimulator 1 (A0A0G2K1D2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Cytoplasm, cytosol {ECO:0000256|ARBA:ARBA00004514}. Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00004240}. Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
Interaction partners:
- Transforming protein RhoA
- RSA-14-44 protein.
Sequence:
MDNLSDALKKLKITAADKTEGSLEGCLDCLLQALAQNNAETSEKIQGSGILQLFANLLTPQASCTAKVANIIAEVAKNEFMRIPCVDAGLISPLVQLLNSKDQEVLLQTGRALGNICYDSHEGRSAVDQAGGAQIVIDHLRSLCGRADPANEKLLTVFCGMLMNYSNENDSLQAQLINMGVIPTLVKLLGIHCHNAALTEMCLVAFGNLAELESSKEQFASTNIAEELVKLFKKQIEHDKREMIFEVLAPLAENDAIKLQLVEAGLVECLLEIVQQKVDSTKEDDLAELKTASDLMVLLLLGDESMQKLFEGGKGSVFQRVLSWIPSNSQQLQLAGALAIANFARNDGNCIHMVDNGIVEKLMDLLDRHVEDGNVTVQHAALSALRNLAIPVVNKAKMLSAGVTETVLKFLKSEMPPVQFKLLGTLRMLIDAQAEAAEQLGKNAKLVERLVEWCEAKDHAGVMGESNRLLSALIRHSKSKDVIKTIVQSGGIKHLVTMATSEHVIMQNEALVALALIAALELGPAEKDLASAQLVQILHRLLADERSAPEIKYNSMVLICALMGSEALHKEVQDLAFLDVVSKLRSHENKSVAQQASLTEQRLTVQS
Protein: Protein cornichon homolog 2 (CNIH-2) (Cornichon family AMPA receptor auxiliary protein 2) (Cornichon-like protein) (Q6PI25)
Organism: Homo sapiens (Human)
Function: Regulates the trafficking and gating properties of AMPA-selective glutamate receptors (AMPARs). Promotes their targeting to the cell membrane and synapses and modulates their gating properties by regulating their rates of activation, deactivation and desensitization. Blocks CACNG8-mediated resensitization of AMPA receptors.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Postsynaptic cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Postsynaptic density {ECO:0000250}. Note=Also localizes to the cell membrane of extrasynaptic sites (dendritic shafts, spines of pyramidal cells). {ECO:0000250}.
Interaction partners:
- Glutamate receptor 1
- Glutamate receptor 2
- Voltage-dependent calcium channel gamma-8 subunit
- Glutamate receptor 3
- Protein shisa-9
- Glutamate receptor 4
- Voltage-dependent calcium channel gamma-2 subunit
- Voltage-dependent calcium channel gamma-7 subunit
- Cytosolic 5'-nucleotidase 1A
- Disks large homolog 4
Sequence:
MAFTFAAFCYMLTLVLCASLIFFVIWHIIAFDELRTDFKNPIDQGNPARARERLKNIERICCLLRKLVVPEYSIHGLFCLMFLCAAEWVTLGLNIPLLFYHLWRYFHRPADGSEVMYDAVSIMNADILNYCQKESWCKLAFYLLSFFYYLYSMVYTLVSF
Protein: Large ribosomal subunit protein mL49 (39S ribosomal protein L49, mitochondrial) (L49mt) (MRP-L49) (Q5EA71)
Organism: Bos taurus (Bovine)
Subcellular location: Mitochondrion {ECO:0000250|UniProtKB:Q13405}.
Interaction partners:
- Small ribosomal subunit protein mS29
- Ribosomal protein
- Large ribosomal subunit protein uL4m
- Large ribosomal subunit protein mL43
- Large ribosomal subunit protein mL40
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein bL19m
- Small ribosomal subunit protein uS12m
- Large ribosomal subunit protein uL15m
- Large ribosomal subunit protein mL64
Sequence:
MAAATFWFVLRGWRTGVPPGCGLRRLSQTQGTPDYPRFLESVDEYRFVERLLPPTSIPKPPKHEHYPTPCGWQPPRDPPPNLPYFVRRSRMHNIPVYRDITHGNRQMTVIRKVEGDIWALQKDVEDFLSPLLGKTPITQVNEVTGTLRIKGYFDQQLKAWLLEKGF
Protein: Leucine-rich repeat-containing protein 19 (Q9H756)
Organism: Homo sapiens (Human)
Function: Pathogen-recognition receptor which mediates the activation of TRAF2- and TRAF6 NF-kappa-B signaling pathways and induces the expression of pro-inflammatory cytokines. In kidney, prevents infection by uropathogenic bacteria by inducing the production of cytokines, chemokines and antimicrobial substances. In gut, involved in host-microbiota interactions, plays a critical role in promoting the recruitment of immune cells and intestinal inflammation (By similarity).
Subcellular location: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MKVTGITILFWPLSMILLSDKIQSSKREVQCNFTEKNYTLIPADIKKDVTILDLSYNQITLNGTDTRVLQTYFLLTELYLIENKVTILHNNGFGNLSSLEILNICRNSIYVIQQGAFLGLNKLKQLYLCQNKIEQLNADVFVPLRSLKLLNLQGNLISYLDVPPLFHLELITLYGNLWNCSCSLFNLQNWLNTSNVTLENENITMCSYPNSLQSYNIKTVPHKAECHSKFPSSVTEDLYIHFQPISNSIFNSSSNNLTRNSEHEPLGKSWAFLVGVVVTVLTTSLLIFIAIKCPIWYNILLSYNHHRLEEHEAETYEDGFTGNPSSLSQIPETNSEETTVIFEQLHSFVVDDDGFIEDKYIDIHELCEEN
Protein: CTP synthase (EC 6.3.4.2) (Cytidine 5'-triphosphate synthase) (Cytidine triphosphate synthetase) (CTP synthetase) (CTPS) (UTP--ammonia ligase) (P0A7E5)
Organism: Escherichia coli (strain K12)
Function: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:32507415}. Note=Localizes to the cytoophidium, a subcellular filamentary structure where CTP synthase is compartmentalized. Many cells form cytoophidia which are observed in stationary phase. {ECO:0000269|PubMed:32507415}.
Interaction partners:
- DNA-directed RNA polymerase subunit beta
- Large ribosomal subunit protein uL2
- GMP synthase
- Elongation factor G
- Small ribosomal subunit protein uS2
- Nucleoside diphosphate kinase
- Large ribosomal subunit protein uL13
- Nucleoside triphosphate pyrophosphohydrolase
- dCTP deaminase
- Large ribosomal subunit protein uL14
Sequence:
MTTNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPIQHGEVFVTEDGAETDLDLGHYERFIRTKMSRRNNFTTGRIYSDVLRKERRGDYLGATVQVIPHITNAIKERVLEGGEGHDVVLVEIGGTVGDIESLPFLEAIRQMAVEIGREHTLFMHLTLVPYMAASGEVKTKPTQHSVKELLSIGIQPDILICRSDRAVPANERAKIALFCNVPEKAVISLKDVDSIYKIPGLLKSQGLDDYICKRFSLNCPEANLSEWEQVIFEEANPVSEVTIGMVGKYIELPDAYKSVIEALKHGGLKNRVSVNIKLIDSQDVETRGVEILKGLDAILVPGGFGYRGVEGMITTARFARENNIPYLGICLGMQVALIDYARHVANMENANSTEFVPDCKYPVVALITEWRDENGNVEVRSEKSDLGGTMRLGAQQCQLVDDSLVRQLYNAPTIVERHRHRYEVNNMLLKQIEDAGLRVAGRSGDDQLVEIIEVPNHPWFVACQFHPEFTSTPRDGHPLFAGFVKAASEFQKRQAK