wanglab/gogpt-training-data huggingface dataset:
Protein: E3 ubiquitin-protein transferase RMND5A (EC 2.3.2.27) (P44CTLH) (Protein RMD5 homolog A) (Q9H871)
Organism: Homo sapiens (Human)
Function: Core component of the CTLH E3 ubiquitin-protein ligase complex that selectively accepts ubiquitin from UBE2H and mediates ubiquitination and subsequent proteasomal degradation of the transcription factor HBP1. MAEA and RMND5A are both required for catalytic activity of the CTLH E3 ubiquitin-protein ligase complex. Catalytic activity of the complex is required for normal cell proliferation. The CTLH E3 ubiquitin-protein ligase complex is not required for the degradation of enzymes involved in gluconeogenesis, such as FBP1.
Subcellular location: Nucleus, nucleoplasm {ECO:0000269|PubMed:17467196, ECO:0000269|PubMed:24143168, ECO:0000269|PubMed:25793641}. Cytoplasm {ECO:0000269|PubMed:17467196, ECO:0000269|PubMed:24143168, ECO:0000269|PubMed:25793641}.
Interaction partners:
- Glucose-induced degradation protein 8 homolog
- Ran-binding protein 9
- WD repeat-containing protein 26
- Armadillo repeat-containing protein 8
- Glucose-induced degradation protein 4 homolog
- Muskelin
- Ran-binding protein 10
- E3 ubiquitin-protein transferase MAEA
- Protein yippee-like 5
- Zinc finger MYND domain-containing protein 19
Sequence:
MDQCVTVERELEKVLHKFSGYGQLCERGLEELIDYTGGLKHEILQSHGQDAELSGTLSLVLTQCCKRIKDTVQKLASDHKDIHSSVSRVGKAIDKNFDSDISSVGIDGCWQADSQRLLNEVMVEHFFRQGMLDVAEELCQESGLSVDPSQKEPFVELNRILEALKVRVLRPALEWAVSNREMLIAQNSSLEFKLHRLYFISLLMGGTTNQREALQYAKNFQPFALNHQKDIQVLMGSLVYLRQGIENSPYVHLLDANQWADICDIFTRDACALLGLSVESPLSVSFSAGCVALPALINIKAVIEQRQCTGVWNQKDELPIEVDLGKKCWYHSIFACPILRQQTTDNNPPMKLVCGHIISRDALNKMFNGSKLKCPYCPMEQSPGDAKQIFF
Protein: Zeatin O-xylosyltransferase (EC 2.4.2.40) (Zeatin O-beta-D-xylosyltransferase) (P56725)
Organism: Phaseolus vulgaris (Kidney bean) (French bean)
Function: Utilizes UDP-xylose as the sugar donor and catalyzes the formation of o-xylosylzeatin from zeatin. Does not act on UDP-glucose.
Interaction partners:
Sequence:
MALNDETKVVVLLLPFPVQGHLNPFLQLSHLIAAQNIAVHYVGTVTHIRQAKLRYHNATSNIHFHAFEVPPYVSPPPNPEDDFPSHLIPSFEASAHLREPVGKLLQSLSSQAKRVVLINDSLMASVAQDAANFSNVERYCFQVFSALNTAGDFWEQMGKPPLADFHFPDIPSLQGCISAQFTDFLTAQNEFRKFNNGDIYNTSRVIEGPYVELLERFNGGKEVWALGPFTPLAVEKKDSIGFSHPCMEWLDKQEPSSVIYVSFGTTTALRDEQIQELATGLEQSKQKFIWVLRDADKGDIFDGSEAKRYELPEGFEERVEGMGLVVRDWAPQMEILSHSSTGGFMSHCGWNSCLESLTRGVPMATWAMHSDQPRNAVLVTDVLKVGLIVKDWEQRKSLVSASVIENAVRRLMETKEGDEIRKRAVKLKDEIHRSMDEGGVSRMEMASFIAHISR
Protein: Ubiquitin carboxyl-terminal hydrolase 14 (EC 3.4.19.12) (Deubiquitinating enzyme 14) (Glucose-induced degradation protein 6) (Ubiquitin thioesterase 14) (Ubiquitin-specific-processing protease 14) (P38237)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1). Accelerates proteasomal breakdown of ubiquitinated proteins as it disassembles free ubiquitin chains that would compete with ubiquitinated proteins to bind to the proteasome.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}.
Interaction partners:
- Polyubiquitin
- Ubiquitin carboxyl-terminal hydrolase 15
- Ubiquitin carboxyl-terminal hydrolase 6
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin carboxyl-terminal hydrolase 2
- OTU domain-containing protein 2
- Ubiquitin carboxyl-terminal hydrolase RPN11
- Ubiquitin thioesterase OTU1
- Ubiquitin-ribosomal protein eL40A fusion protein
- Ubiquitin carboxyl-terminal hydrolase 3
Sequence:
MAEAVLENVNVPAVVSKDECIYCFESPYNEPLALNASPKHSLNICLNCFQATCNRHVPLHIRVTEYACDTIHSNYLTIAKVEKPKQENVEENNNNKKIKLQVIETSEDDTHNTIWSLQRFNGENVPRTVLSKSTDSDISSTALEKIEKILKAKSQDFEDKKNSWVLEISTCPHTENFQIPSKPENTVNLNQCSSCDLTQNLWLCLHCGNIGCGREQIGIDGHSHALDHYRSNNNHPLAIKLGSLSSSTYDLYCYACDDETRFPDNVNLGSALQIYGINIQEKIADEKTLVQLQVEQNENWQFRMVDSSGKEFEKLSASKNYGCGLINLGNSCYLNSVIQSLVNGGVPNWSLDFLGSKFPLDVVYPDNNLKCQWIKLLNAMKCEPELYPNGIKPTTFKKCIGQNHQEFSSNRQQDAMEFLTFLLDLLDKKFFSSSSSGIPNPNDLVRFMMEDRLQCNICGKVKYSYEPTEAIQIPLEENDEPQDMLERIKAYFEGQTIEFKCANCKEKVTANKKPGFKSLPQTLILNPIRIRLQNWIPVKTSNELSLPGLIDRDDMLDVSSYLSQGFDPQTENLLPDEDENRSSFTPNQCSISQLIEMGFTQNASVRALFNTGNQDAESAMNWLFQHMDDPDLNDPFVPPPNVPKKDKREVDEVSLTSMLSMGLNPNLCRKALILNNGDVNRSVEWVFNNMDDDGTFPEPEVPNEEQQQKKDLGYSTAKPYALTAVICHKGNSVHSGHYVVFIRKLVADKWKWVLYNDEKLVAADSIEDMKKNGYIYFYTRC
Protein: DNA mismatch repair protein MSH5 (OsMSH5) (MutS protein homolog 5) (Q6L4V0)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Involved in meiotic recombination. Required for reciprocal recombination and proper segregation of homologous chromosomes at meiosis. Promotes homologous recombination through facilitating chiasma formation during prophase I. Involved in the control of class I crossover (interference-sensitive crossover) formation.
Subcellular location: Nucleus {ECO:0000269|PubMed:23220939}. Chromosome {ECO:0000269|PubMed:23220939}. Note=Detected in punctuate foci onto the chromosomes during the early meiotic prophase I. {ECO:0000269|PubMed:23220939}.
Interaction partners:
- Os01g0958900 protein
- Exonuclease 1
- Os09g0407600 protein
- Os01g0180600 protein.
- Os04g0507000 protein
- Os02g0592300 protein.
- DNA mismatch repair protein MSH3
- Os09g0551900 protein
- Proliferating cell nuclear antigen
- Flap endonuclease GEN-like 1
Sequence:
MDEEEEEEMSEREVDSQVHMACVMQGRRVGIAYYDSSMHQLFVLEIWEDITEDFPLIDLVKYQSKPSTIYTSTKTDEALLLALQRNDCNDEAPAVKLMKSSTFSYEQAWHRLMYLKVAAMDEGLSVKERICFLNSMMDLGSDVQVRAAGGLLAILDNERLLDTLDQMEGGASIAIDSVAQISLDKFLKLDATAHEALQIFQVDKHPSYMGIGRAKEGFSVFGMLNKCVTPMGKHLLRTWFLRPIIDIDVINNRLNTISFFLCCEDVMSALRGTLKSVRDIPHMLKKFNSPSSFCTSSDWHAFLKCICSLLHINKIFEVGISEHLAIKLQHMNIDLVGKANSSITEELDYVSDLVVGVIDVQRGKEKGYDTLVKDGLCEELDELRMVYEELPDFLEQVSANEIASFPFSFECRKAPLIVYVHQIGYLMCFFDEKISDALLIGLPDFEFAFSEEGEERRFYYHTQKTRELDNLLGDIYHKILDMERAIIRDLVCRVCQFIPQLTKAVNFAAELDCILSLAIVARQNNYVRPILTEDSILEIQNGRHALQEMTVDTFVPNDTKIRSSGRINIITGPNYSGKSIYIKQVALVVFLAHIGSFVPADSAIVGLTDRIFCAMGSKSMTSEQSTFMIDLHQVGTMLRHATSRSLCLLDEFGKGTLTEDGIGLLGGTISHFTDYDCPPKVLLSTHLTQIFTESYLPQSEHIKCYTMSVLNPDEQTDNEDVIFLYRLVPGQALLSFGLHCAQLAGVPSEVVQRAVTVLGDIHSKRPIRRMVWEKLAAKDQQYQDAVTKLLAFDPHKGDLVNFFQEVFPS
Protein: Lysine--tRNA ligase (EC 6.1.1.6) (Lysyl-tRNA synthetase) (Q8IDJ8)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Proline--tRNA ligase
- lysine--tRNA ligase
- tRNA import protein tRIP
- glutamate--tRNA ligase
- glutamine--tRNA ligase
- isoleucine--tRNA ligase
- leucine--tRNA ligase
- Elongation factor 1-gamma, putative
- Proline--tRNA ligase, putative
- ATP synthase subunit alpha
Sequence:
MTSKSFLLSFLKYKHVNTYIFEKSFSKILKNTKKHIDCHLKSCFVTMNEKKEHVLEGEKNKRVVNASKDKKKEEEGEVDPRLYFENRSKFIQDQKDKGINPYPHKFERTISIPEFIEKYKDLGNGEHLEDTILNITGRIMRVSASGQKLRFFDLVGDGEKIQVLANYSFHNHEKGNFAECYDKIRRGDIVGIVGFPGKSKKGELSIFPKETILLSACLHMLPMKYGLKDTEIRYRQRYLDLLINESSRHTFVTRTKIINFLRNFLNERGFFEVETPMMNLIAGGANARPFITHHNDLDLDLYLRIATELPLKMLIVGGIDKVYEIGKVFRNEGIDNTHNPEFTSCEFYWAYADYNDLIKWSEDFFSQLVYHLFGTYKISYNKDGPENQPIEIDFTPPYPKVSIVEEIEKVTNTILEQPFDSNETIEKMINIIKEHKIELPNPPTAAKLLDQLASHFIENKYNDKPFFIVEHPQIMSPLAKYHRTKPGLTERLEMFICGKEVLNAYTELNDPFKQKECFKLQQKDREKGDTEAAQLDSAFCTSLEYGLPPTGGLGLGIDRITMFLTNKNSIKDVILFPTMRPAN
Protein: TRAF-type zinc finger domain-containing protein 1 (Protein FLN29) (Q99MM4)
Organism: Rattus norvegicus (Rat)
Function: Negative feedback regulator that controls excessive innate immune responses. Regulates both Toll-like receptor 4 (TLR4) and DDX58/RIG1-like helicases (RLH) pathways. May inhibit the LTR pathway by direct interaction with TRAF6 and attenuation of NF-kappa-B activation. May negatively regulate the RLH pathway downstream from MAVS and upstream of NF-kappa-B and IRF3 (By similarity).
Interaction partners:
Sequence:
MAEFPDDQAARLCDNCKKEIPVFNFTIHEIHCQRNIGVCPVCKEPFPKSDMDIHVATEHCQVTCKCNKKLEKRQLKQHVETECPLRLAVCQHCDLELSVVKLKEHEDYCGARTELCGSCGRNVLVKELQTHPAVCGRVEEEKRSEAAVPPEAYDEPWSQDRIWIASQLLRQIEALDPPMRLPGRPLRAFEADPFYSRTASQRGVTAHFPIQNNLFEEQERQERNRSHQSPKDSAENSAHLDFMLALSLQNEGQASSMVEQGFWESVPEADPARAGPTSLGDIKGAADETLLPCEFCEELYPEELLIDHQTSCNPSHALRSLNTGSSSIRGVEDPGAIFQNFLQQATSNQLDTLMGLSSSAAVEDSIIIPCEFCGVQLEEEVLFHHQDQCDQRPATANHRAMEGIPTQDSQPEDRSPELSRRRVKHQGDLSSGYMDDVKQESVKGSTYSLSPNRTMNNVSTCNRLLNSSGPRSDCQRSPPGVLKLNNSGSQDIRGRIRGSQNGPIASAHAPVIHSIRNLYPENLAPSFPHGSPGRFGASEGSRSSRVTPTAASYHSRAAKAKPPKQQGAGDAEEEEE
Protein: Flagellar protofilament ribbon protein (Q9M6B1)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000256|ARBA:ARBA00004611}.
Interaction partners:
Sequence:
MGRLVAQVPNEDPERLKRVLDAKWRTIGVDKETLELQAQEKKDREQAEKDRDEAFARLTAYFDDQLTLMQQEADQIRKAYNHDTEAFRQQQQLKHTRREWDINRPDAKQLDMPGRVGDDDNRLGPSSLQKFDGEDLTSGDRKKAQIEQSVNWWAEQTAIRDALRAAEKEAETAHAELVKYQDLLQQTAKSEEAAVRREVARATADYNKRLAEEKRLREYAAKQADLAANMAEMEATITSSFMTEDPNMAASSMSAYRVRKDHYKGMTETEKQAILDAQLAQMEEKKARRAQEQLENMMYARTQHDIQRALQEQAQRVDDFKKAQMARASEILKKQQEEKAERDKHLASLYRNKMAPEFFTQFGTSHR
Protein: Potassium-transporting ATPase KdpF subunit (ATP phosphohydrolase [potassium-transporting] F chain) (Potassium-binding and translocating subunit F) (Potassium-translocating ATPase F chain) (P36937)
Organism: Escherichia coli (strain K12)
Function: Part of the high-affinity ATP-driven potassium transport (or Kdp) system, which catalyzes the hydrolysis of ATP coupled with the electrogenic transport of potassium into the cytoplasm. This subunit may be involved in stabilization of the complex.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378, ECO:0000305|PubMed:10608856}; Single-pass membrane protein {ECO:0000269|PubMed:28636601, ECO:0000269|PubMed:30478378}.
Interaction partners:
- Potassium-transporting ATPase ATP-binding subunit
- Potassium-transporting ATPase potassium-binding subunit
- Potassium-transporting ATPase KdpC subunit
- Sensor protein KdpD
- KDP operon transcriptional regulatory protein KdpE
- Spermidine/putrescine transport system permease protein PotC
- Putrescine transport system permease protein PotI
- ATP-dependent lipid A-core flippase
- sn-glycerol-3-phosphate transport system permease protein UgpA
- Maltose/maltodextrin transport system permease protein MalF
Sequence:
MSAGVITGVLLVFLLLGYLVYALINAEAF
Protein: Sodium- and chloride-dependent neutral and basic amino acid transporter B(0+) (Amino acid transporter ATB0+) (Solute carrier family 6 member 14) (Q9UN76)
Organism: Homo sapiens (Human)
Function: Amino acid transporter that plays an important role in the absorption of amino acids in the intestinal tract. Mediates the uptake of a broad range of neutral and cationic amino acids (with the exception of proline) in a Na(+)/Cl(-)-dependent manner. Transports non-alpha-amino acids such as beta-alanine with low affinity, and has a higher affinity for dipolar and cationic amino acids such as leucine and lysine. Can also transport carnitine, butirylcarnitine and propionylcarnitine coupled to the transmembrane gradients of Na(+) and Cl(-).
Subcellular location: Membrane {ECO:0000305|PubMed:10446133}; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:Q9JMA9}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Neutral amino acid transporter B
Sequence:
MDKLKCPSFFKCREKEKVSASSENFHVGENDENQDRGNWSKKSDYLLSMIGYAVGLGNVWRFPYLTYSNGGGAFLIPYAIMLALAGLPLFFLECSLGQFASLGPVSVWRILPLFQGVGITMVLISIFVTIYYNVIIAYSLYYMFASFQSELPWKNCSSWSDKNCSRSPIVTHCNVSTVNKGIQEIIQMNKSWVDINNFTCINGSEIYQPGQLPSEQYWNKVALQRSSGMNETGVIVWYLALCLLLAWLIVGAALFKGIKSSGKVVYFTALFPYVVLLILLVRGATLEGASKGISYYIGAQSNFTKLKEAEVWKDAATQIFYSLSVAWGGLVALSSYNKFKNNCFSDAIVVCLTNCLTSVFAGFAIFSILGHMAHISGKEVSQVVKSGFDLAFIAYPEALAQLPGGPFWSILFFFMLLTLGLDSQFASIETITTTIQDLFPKVMKKMRVPITLGCCLVLFLLGLVCVTQAGIYWVHLIDHFCAGWGILIAAILELVGIIWIYGGNRFIEDTEMMIGAKRWIFWLWWRACWFVITPILLIAIFIWSLVQFHRPNYGAIPYPDWGVALGWCMIVFCIIWIPIMAIIKIIQAKGNIFQRLISCCRPASNWGPYLEQHRGERYKDMVDPKKEADHEIPTVSGSRKPE
Protein: Ficolin-3 (Collagen/fibrinogen domain-containing lectin 3 p35) (Collagen/fibrinogen domain-containing protein 3) (Hakata antigen) (O75636)
Organism: Homo sapiens (Human)
Function: May function in innate immunity through activation of the lectin complement pathway. Calcium-dependent and GlcNAc-binding lectin. Has affinity with GalNAc, GlcNAc, D-fucose, as mono/oligosaccharide and lipopolysaccharides from S.typhimurium and S.minnesota.
Subcellular location: Secreted. Note=Found in blood plasma, bronchus, alveolus and bile duct.
Interaction partners:
- MBL associated serine protease 1
- Mannan-binding lectin serine protease 2
- Mannose-binding protein C
- Ficolin-2
- Collectin-11
- Collectin-10
- Ficolin-1
- Complement C3
- Complement C1s subcomponent
- Killer cell immunoglobulin-like receptor 3DL1
Sequence:
MDLLWILPSLWLLLLGGPACLKTQEHPSCPGPRELEASKVVLLPSCPGAPGSPGEKGAPGPQGPPGPPGKMGPKGEPGDPVNLLRCQEGPRNCRELLSQGATLSGWYHLCLPEGRALPVFCDMDTEGGGWLVFQRRQDGSVDFFRSWSSYRAGFGNQESEFWLGNENLHQLTLQGNWELRVELEDFNGNRTFAHYATFRLLGEVDHYQLALGKFSEGTAGDSLSLHSGRPFTTYDADHDSSNSNCAVIVHGAWWYASCYRSNLNGRYAVSEAAAHKYGIDWASGRGVGHPYRRVRMMLR
Protein: Adenosine receptor A2a (P30543)
Organism: Rattus norvegicus (Rat)
Function: Receptor for adenosine (By similarity). The activity of this receptor is mediated by G proteins which activate adenylyl cyclase.
Subcellular location: Cell membrane {ECO:0000269|PubMed:16339847, ECO:0000269|PubMed:23994616}; Multi-pass membrane protein {ECO:0000269|PubMed:16339847}. Note=Colocalizes with GAS2L2 at neuronal processes. {ECO:0000269|PubMed:23994616}.
Interaction partners:
- D
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Adenosine receptor A2b
- Guanine nucleotide-binding protein G
- Pro-opiomelanocortin
- Pituitary adenylate cyclase-activating polypeptide
- Adenosine receptor A1
- Pro-glucagon
- BDNF/NT-3 growth factors receptor
Sequence:
MGSSVYITVELAIAVLAILGNVLVCWAVWINSNLQNVTNFFVVSLAAADIAVGVLAIPFAITISTGFCAACHGCLFFACFVLVLTQSSIFSLLAIAIDRYIAIRIPLRYNGLVTGVRAKGIIAICWVLSFAIGLTPMLGWNNCSQKDGNSTKTCGEGRVTCLFEDVVPMNYMVYYNFFAFVLLPLLLMLAIYLRIFLAARRQLKQMESQPLPGERTRSTLQKEVHAAKSLAIIVGLFALCWLPLHIINCFTFFCSTCRHAPPWLMYLAIILSHSNSVVNPFIYAYRIREFRQTFRKIIRTHVLRRQEPFQAGGSSAWALAAHSTEGEQVSLRLNGHPLGVWANGSATHSGRRPNGYTLGLGGGGSAQGSPRDVELPTQERQEGQEHPGLRGHLVQARVGASSWSSEFAPS
Protein: Prefoldin subunit 3 (HIBBJ46) (von Hippel-Lindau-binding protein 1) (VBP-1) (VHL-binding protein 1) (P61758)
Organism: Homo sapiens (Human)
Function: Binds specifically to cytosolic chaperonin (c-CPN) and transfers target proteins to it. Binds to nascent polypeptide chain and promotes folding in an environment in which there are many competing pathways for nonnative proteins.
Subcellular location: Cytoplasm. Nucleus. Note=In complex with VHL can translocate to the nucleus.
Interaction partners:
- Prefoldin subunit 6
- Prefoldin subunit 2
- Prefoldin subunit 5
- Prefoldin subunit 4
- Prefoldin subunit 1
- T-complex protein 1 subunit theta
- T-complex protein 1 subunit zeta
- T-complex protein 1 subunit beta
- T-complex protein 1 subunit delta
- T-complex protein 1 subunit alpha
Sequence:
MAAVKDSCGKGEMATGNGRRLHLGIPEAVFVEDVDSFMKQPGNETADTVLKKLDEQYQKYKFMELNLAQKKRRLKGQIPEIKQTLEILKYMQKKKESTNSMETRFLLADNLYCKASVPPTDKVCLWLGANVMLEYDIDEAQALLEKNLSTATKNLDSLEEDLDFLRDQFTTTEVNMARVYNWDVKRRNKDDSTKNKA
Protein: Cellular tumor antigen p53 (Tumor suppressor p53) (E7EMR6)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}. Nucleus, PML body {ECO:0000256|ARBA:ARBA00004322}.
Interaction partners:
Sequence:
MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQ
Protein: Teg12 (B7T1D7)
Organism: uncultured soil bacterium
Interaction partners:
Sequence:
MNGIRWIASYPKAGNTWVRCMLAAYITGKAPQVWNDIDAESLTLEAMLRFGDLPPAEPMEPVLVKTHLKADVPVLGLYGEATAKVLYLVRNPRDMLLSSMRMASISRDDVEKSRDFARKFIANEGLGWNALGAGGGVGLGSWPENVRSWTESSSDRFPNADVLTMRYEDLKGDPVARFSEIVEFLDLGGPVDIEDIRRAVAASTLERMRELEKRSEQQGGGSPIRHGDARMMKGGPGGARPQFVGEGRYDQSLSFLGEDIESDYQELLHGDSGFALYAKQYGYAG
Protein: ACP53C14A (Q6GUT9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MHLIRIALLLSFLALCQKSQVQAAISSELDHYLRCLEVVTDAGALMIENSITAISLLSDCVDFQPKIKLTGSILRFIRVAHQFGKKAIYDRPECLVQTFTTGVGLIRPIIAKFDSLRCFDE
Protein: Alpha-ketoglutarate-dependent dioxygenase AlkB (EC 1.14.11.33) (Alkylated DNA repair protein AlkB) (DNA oxidative demethylase AlkB) (P05050)
Organism: Escherichia coli (strain K12)
Function: Dioxygenase that repairs alkylated DNA and RNA containing 3-methylcytosine or 1-methyladenine by oxidative demethylation. Has highest activity towards 3-methylcytosine. Has lower activity towards alkylated DNA containing ethenoadenine, and no detectable activity towards 1-methylguanine or 3-methylthymine. Accepts double-stranded and single-stranded substrates. Requires molecular oxygen, alpha-ketoglutarate and iron. Provides extensive resistance to alkylating agents such as MMS and DMS (SN2 agents), but not to MMNG and MNU (SN1 agents).
Interaction partners:
- Bifunctional transcriptional activator/DNA repair enzyme Ada
- DNA-3-methyladenine glycosylase 2
- Putative acyl-CoA dehydrogenase AidB
- ABC transporter ATP-binding/permease protein YojI
- Methylated-DNA--protein-cysteine methyltransferase
Sequence:
MLDLFADAEPWQEPLAAGAVILRRFAFNAAEQLIRDINDVASQSPFRQMVTPGGYTMSVAMTNCGHLGWTTHRQGYLYSPIDPQTNKPWPAMPQSFHNLCQRAATAAGYPDFQPDACLINRYAPGAKLSLHQDKDEPDLRAPIVSVSLGLPAIFQFGGLKRNDPLKRLLLEHGDVVVWGGESRLFYHGIQPLKAGFHPLTIDCRYNLTFRQAGKKE
Protein: Lipolysis-stimulated lipoprotein receptor (Lipolysis-stimulated remnant receptor) (Q9WU74)
Organism: Rattus norvegicus (Rat)
Function: Probable role in the clearance of triglyceride-rich lipoprotein from blood. Binds chylomicrons, LDL and VLDL in presence of free fatty acids and allows their subsequent uptake in the cells. Maintains epithelial barrier function by recruiting MARVELD2/tricellulin to tricellular tight junctions (By similarity).
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:Q99KG5}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q99KG5}. Note=Located at tricellular contacts. {ECO:0000250|UniProtKB:Q99KG5}.
Interaction partners:
- MARVEL domain containing 2
- Apolipoprotein B-100
Sequence:
MAPAAGACAGAPDSHPATVVFVCLFLIIFCPDPASAIQVTVSDPYHVVILFQPVTLPCTYQMSNTLTVPIVIWKYKSFCRDRIADAFSPASVDNQLNAQLAAGNPGYNPYVECQDSVRTVRVVATKQGNAVTLGDYYQGRRITITGNADLTFEQTAWGDSGVYYCSVVSAQDLDGNNEAYAELIVLGRTSEAPELLPGFRAGPLEDWLFVVVVCLASLLLFLLLGICWCQCCPHTCCCYVRCPCCPDKCCCPEALYAAGKAATSGVPSIYAPSIYTHLSPAKTPPPPPAMIPMGPPYGYPGDFDRHSSVGGHSSQVPLLRDVDGSVSSEVRSGYRIQANQQDDSMRVLYYMEKELANFDPSRPGPPNGRVERAMSEVTSLHEDDWRSRPSRAPALTPIRDEEWNRHSPQSPRTWEQEPLQEQPRGGWGSGRPRARSVDALDDINRPGSTESGRSSPPSSGRRGRAYAPPRSRSRDDLYDPDDPRDLPHSRDPHYYDDIRSRDPRADPRSRQRSRDPRDAGFRSRDPQYDGRLLEEALKKKGSGERRRVYREEEEEEEGQYPPAPPPYSETDSQASRERRLKKNLALSRESLVV
Protein: Caspase 1b (W0TYK3)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
LEGSKASDKMIARVQERDPGLYDKMGLAPTPSSPQLSQQEEQPVSSVLTPSTNDFKKDILQRKGSEIYPPMDKSGRKRLALLINNVEFDDKNMLRRGAEKDEEDVERLLRDLGYDVVKHRNLSGQEMDEAVKAFSKREEHLLSDSVFVVMMSHGELGAIMGVHYKKGDPNLDIFPINNIFTHLNTENCKALINKPKVILIQACRGGKDGSVWV
Protein: Uncharacterized protein (Q5B4F5)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Interaction partners:
- Uncharacterized protein
Sequence:
MKASVITALTWAACTMAGPIGLRDVAGEDCTCEIETVTITVPAPTEVGTIGGPTNPPGTATWSEPAEPNPNTNTGTATGTVTATATATATETWTNTVTATGTATGPATVPPTSAPTPCDDEECHGTGHLIQDLGPQVNRALTVTGADGERFLVQVNEDVYNLLSGRVSLSDSIGEIVGDAATIGDLIADLGPIIDCILTIVGEDSHILLVRLAPEVADLLRGTGVTLGLDAINNPIGGLLGSLTGGLLTRDEAQPLTVTGQSGHDLPVALDGVVGNTLRENNVSGPIGTVIAAAISVTQLLQHPLAQDSEDLIVVIGRDTGALLIRLAPGVARLLDGLLPGIATPVGRIIAVIGDSL
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (E9PC69)
Organism: Homo sapiens (Human)
Subcellular location: Cell projection, dendrite {ECO:0000256|ARBA:ARBA00004279}. Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MSSARTPLPTLNERDTEQPTLGHLDSKPSSKSNMIRGRNSATSADEQPHIGNYRLLKTIGKGNFAKVKLARHILTGKEVAVKIIDKTQLNSSSLQKLFREVRIMKVLNHPNIVKLFEVIETEKTLYLVMEYASGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKFIVHRDLKAENLLLDADMNIKIADFGFSNEFTFGNKLDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLILNPSKRGTLEQIMKDRWMNVGHEDDELKPYVEPLPDYKDPRRTELMVSMGYTREEIQDSLVGQRYNEVMATYLLLGYKSSELEGDTITLKPRPSADLTNSSAPSPSHKVQRSVSANPKQRRFSDQAGPAIPTSNSYSKKTQSNNAENKRPEEDRESGRKASSTAKVPASPLPGLERKKTTPTPSTNSVLSTSTNRSRNSPLLERASLGQASIQNGKDSLTMPGSRASTASASAAVSAARPRQHQKSMSASVHPNKASGLPPTESNCEVPRPSTAPQRVPVASPSAHNISSSGGAPDRTNFPRGVSSRSTFHAGQLRQVRDQQNLPYGVTPASPSGHSQGRRGASGSIFSKFTSKFVRRNLNEPESKDRVETLRPHVVGSGGNDKEKEEFREAKPRSLRFTWSMKTTSSMEPNEMMREIRKVLDANSCQSELHEKYMLLCMHGTPGHEDFVQWEMEVCKLPRLSLNGVRFKRISGTSMAFKNIASKIANELKL
Protein: Potassium voltage-gated channel subfamily KQT member 3 (KQT-like 3) (Potassium channel subunit alpha KvLQT3) (Voltage-gated potassium channel subunit Kv7.3) (Q8K3F6)
Organism: Mus musculus (Mouse)
Function: Associates with KCNQ2 or KCNQ5 to form a potassium channel with essentially identical properties to the channel underlying the native M-current, a slowly activating and deactivating potassium conductance which plays a critical role in determining the subthreshold electrical excitability of neurons as well as the responsiveness to synaptic inputs. Therefore, it is important in the regulation of neuronal excitability. KCNQ2-KCNQ3 channel is selectively permeable to other cations besides potassium, in decreasing order of affinity K(+) > Rb(+) > Cs(+) > Na(+). Associates with Na(+)-coupled myo-inositol symporter SLC5A3 forming a coregulatory complex that alters ion selectivity, increasing Na(+) and Cs(+) permeation relative to K(+) permeation.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O43525}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Potassium voltage-gated channel subfamily KQT member 2
- Potassium voltage-gated channel subfamily KQT member 5
- Potassium voltage-gated channel subfamily KQT member 4
- Potassium voltage-gated channel subfamily KQT member 1
- Inward rectifier potassium channel 4
- Inward rectifier potassium channel 2
- ATP-sensitive inward rectifier potassium channel 12
- ATP-sensitive inward rectifier potassium channel 14
- Ubiquitin-like protein FUBI
- Ankyrin-3
Sequence:
MGLKARRAAGAAGGGGGEGGGGGGGAANPAGGDSAVAGDEERKVGLAPGDVEQVTLALGAGADKDGTLLLEGGGREEGQRRTPQGIGLLAKTPLSRPVKRNNAKYRRIQTLIYDALERPRGWALLYHALVFLIVLGCLILAVLTTFKEYETVSGDWLLLLETFAIFIFGAEFALRIWAAGCCCRYKGWRGRLKFARKPLCMLDIFVLIASVPVVAVGNQGNVLATSLRSLRFLQILRMLRMDRRGGTWKLLGSAICAHSKELITAWYIGFLTLILSSFLVYLVEKDVPEMDAQGEEMKEEFETYADALWWGLITLATIGYGDKTPKTWEGRLIAATFSLIGVSFFALPAGILGSGLALKVQEQHRQKHFEKRRKPAAELIQAAWRYYATNPNRLDLVATWRFYESVVSFPFFRKEQLEAAASQKLGLLDRVRLSNPRGSNTKGKLFTPLNVDAIEESPSKEPKPVGLNNKERFRTAFRMKAYAFWQSSEDAGTGDPMAEDRGYGNDFLIEDMIPTLKAAIRAVRILQFRLYKKKFKETLRPYDVKDVIEQYSAGHLDMLSRIKYLQTRIDMIFTPGPPSTPKHKKSQKGSAFTYPSQQSPRNEPYVARAATSETEDQSMMGKFVKVERQVHDMGKKLDFLVDMHMQHMERLQVHVTEYYPTKGASSPAEGEKKEDNRYSDLKTIICNYSETGPPDPPYSFHQVPIDRVGPYGFFAHDPVKLTRGGPSSTKAQANLPSSGSTYAERPTVLPILTLLDSCVSYHSQTELQGPYSDHISPRQRRSITRDSDTPLSLMSVNHEELERSPSGFSISQDRDDYVFGPSGGSSWMREKRYLAEGETDTDTDPFTPSGSMPMSSTGDGISDSIWTPSNKPT