wanglab/gogpt-training-data huggingface dataset:
Protein: Outer mitochondrial transmembrane helix translocase (EC 7.4.2.-) (Mitochondrial sorting of proteins) (Tat-binding homolog 4) (P28737)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Outer mitochondrial translocase required to remove mislocalized tail-anchored transmembrane proteins on mitochondria. Specifically recognizes and binds exposed hydrophobic surfaces of mistargeted tail-anchored transmembrane proteins. Acts as a dislocase that mediates the ATP-dependent extraction of mistargeted tail-anchored transmembrane proteins from the mitochondrion outer membrane. Able to unfold protein substrates by processive threading through its central pore. Once extracted from the mitochondrion outer membrane, substrate proteins are then transferred to the endoplasmic reticulum, where they are ubiquitinated and degraded by the proteasome. Also mediates extraction of excess tail-anchored proteins from the peroxisomal membrane. In normal conditions, MSP1 translocase activity is inhibited by PEX3 at peroxisomes; only catalyzes removal of excess tail-anchored proteins.
Subcellular location: Mitochondrion outer membrane {ECO:0000269|PubMed:24843043, ECO:0000269|PubMed:28906250, ECO:0000269|PubMed:31445887, ECO:0000269|PubMed:8226973, ECO:0000305|PubMed:24821790}; Single-pass membrane protein {ECO:0000255}. Peroxisome membrane {ECO:0000269|PubMed:24821790, ECO:0000269|PubMed:24843043, ECO:0000269|PubMed:28906250}; Single-pass membrane protein {ECO:0000255}.
Interaction partners:
- ATPase GET3
- Mitochondrial import receptor subunit TOM70
- Meiosis-specific APC/C activator protein AMA1
- Uncharacterized protein YBL039W-B
- Nuclear protein localization protein 4
- Mitofusin FZO1
- Peroxisomal biogenesis factor 3
- Peroxisomal membrane protein import receptor PEX19
- Ubiquitin fusion degradation protein 1
- Mitochondrial fission 1 protein
Sequence:
MSRKFDLKTITDLSVLVGTGISLYYLVSRLLNDVESGPLSGKSRESKAKQSLQWEKLVKRSPALAEVTLDAYERTILSSIVTPDEINITFQDIGGLDPLISDLHESVIYPLMMPEVYSNSPLLQAPSGVLLYGPPGCGKTMLAKALAKESGANFISIRMSSIMDKWYGESNKIVDAMFSLANKLQPCIIFIDEIDSFLRERSSTDHEVTATLKAEFMTLWDGLLNNGRVMIIGATNRINDIDDAFLRRLPKRFLVSLPGSDQRYKILSVLLKDTKLDEDEFDLQLIADNTKGFSGSDLKELCREAALDAAKEYIKQKRQLIDSGTIDVNDTSSLKIRPLKTKDFTKKLRMDATSTLSSQPLD
Protein: 4-oxobutanoate dehydrogenase (Q39Q67)
Organism: Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15)
Interaction partners:
- succinate dehydrogenase
- succinate dehydrogenase
- Succinate dehydrogenase/fumarate reductase, iron-sulfur protein
- Succinate dehydrogenase/fumarate reductase, type E, iron-sulfur protein
- Phosphoenolpyruvate carboxykinase
- citrate synthase
- citrate synthase
- Methionyl-tRNA formyltransferase
- Succinate dehydrogenase/fumarate reductase, cytochrome b558 subunit
- Succinate dehydrogenase/fumarate reductase, type E, CCG domain pair subunit
Sequence:
MMILKNSSLLKQQCYLDGHWCCADGGATIDVTNPATGEILGVVPKMGTQETRRAIEAANGALDGWKARTAKERSAILRRWFELIMENLEDLAVIMTAEQGKPLAESRGEIAYAASFIEWFAEEGKRIYGDTIPSYARDKRIVVIKEPIGVCAAITPWNFPAAMITRKAGPALAAGCTMVVKPATATPFSALALALIGEQAGIPAGVFSVITGSSKEIGDEMTGNPIVRKLTFTGSTEVGKQLTAQCAGTMKKVSMELGGNAPFIVFDDADLDAAVEGAIASKYRNTGQTCVCTNRILVQESVYEAFSAKLVAAVSKMTVGDGLKGEVQQGPLIDMTALEKVEEHIADAVAKGARVVLGGKRHALGGTFFEPTIITDVTPGMLVAREETFGPLAPLFKFSTDEEAIRMANDTEFGLASYFYSRDIRRVWKVSEALEYGMVGINTGLISSEVAPFGGVKESGVGREGSKYGIEEFVEVKYLCMGGI
Protein: Testis tissue sperm-binding protein Li 48e (Transmembrane emp24 protein transport domain containing 3, isoform CRA_a) (A0A140VKD1)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004115}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004115}. Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000256|ARBA:ARBA00004151}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004151}. Golgi apparatus, cis-Golgi network membrane {ECO:0000256|ARBA:ARBA00004619}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00004619}. Membrane {ECO:0000256|RuleBase:RU003827}; Single-pass type I membrane protein {ECO:0000256|RuleBase:RU003827}.
Interaction partners:
Sequence:
MGSTVPRSASVLLLLLLLRRAEQPCGAELTFELPDNAKQCFHEEVEQGVKFSLDYQVITGGHYDVDCYVEDPQGNTIYRETKKQYDSFTYRAEVKGVYQFCFSNEFSTFSHKTVYFDFQVGDEPPILPDMGNRVTALTQMESACVTIHEALKTVIDSQTHYRLREAQDRARAEDLNSRVSYWSVGETIALFVVSFSQVLLLKSFFTEKRPISRAVHS
Protein: PDZ and LIM domain protein 7 (LIM mineralization protein) (LMP) (Q679P3)
Organism: Gallus gallus (Chicken)
Function: May function as a scaffold on which the coordinated assembly of proteins can occur. May play a role as an adapter that, via its PDZ domain, localizes LIM-binding proteins to actin filaments of both skeletal muscle and nonmuscle tissues. May be involved in bone formation (By similarity).
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:15302601}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:15302601}. Note=Colocalizes with TPM2 near the Z line in muscle (By similarity). Colocalizes with TBX4 and TBX5 to actin filaments. {ECO:0000250}.
Interaction partners:
- T-Box protein 4
- T-box transcription factor TBX5
- Unconventional myosin-Va
- Unconventional myosin-VI
Sequence:
MESYKVMLNGPAPWGFRLQGGKDFSMPLSISRLTPGGKAAQAGVGVGDWVLYIDGESTGTMTHIEAQNRIRACGDRLCLTLSRAQNHLGKPQKDSLPCSEPPKYNFAPSTALNKTARPFGASSPPNPRPGLVTKPVTYVPLAPACTPQHNGQVSVPDPSPGAAMKTEPGLAPRTPAATPGPTSRPPWAVDPSFAERYAPDKTSTVLSKHSQPATPTPMQNRSSIVQAAQQAPESPGRTPLCYKCNKIIRGRYLVALGHYYHPEEFTCCQCRKVLDEGGFFEEKGSIFCPKCYDTRYAPSCAKCKKKITGEVMHALKMTWHVQCFTCAACKTPIRNRAFYMEEGQPYCERDYEKMFGTKCRGCDFKIDAGDRFLEALGFSWHDTCFVCAICQTNLEGKTFYSKKDKPLCKSHAFSHV
Protein: DnaJ protein P58IPK homolog (AtP58IPK) (Chaperone protein dnaJ 36) (AtDjA36) (AtJ36) (Q9LYW9)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays an important positive role in viral symptom development and is required for viral multiplication and pathogenesis.
Subcellular location: Endoplasmic reticulum lumen {ECO:0000305|PubMed:18718935}.
Interaction partners:
- DnaJ protein ERDJ3B
- Heat shock 70 kDa protein BIP1
- Heat shock 70 kDa protein BIP3
- Heat shock 70 kDa protein BIP2
- Heat shock 70 kDa protein 17
- Eukaryotic translation initiation factor 2 subunit alpha
- Heat shock 70 kDa protein 4
- Small ribosomal subunit protein mS75
- Endoplasmin homolog
- bZIP transcription factor 28
Sequence:
MDLFRVWSGMDFLAWRGMAYTLLLLNFVFACQLLLLQPLVSALDGQSVDAAELFERASQSIKVKRYSDALDDLNAAIEADPALSEAYFKRASVLRHFCRYEDSENSYQKYLEFKSGDSNAEKELSQLHQAKSALETASTLYESKDIAKALEFVDKVVLVFSPACSKAKLLKVKLLMVSKDYSGAISETGYILKEDENNLEALLLRGRAYYYLADHDIAQRHYQKGLRLDPEHSELKKAYFGLKKLLKKTKSAEDNANKGKLRVSAEEYKEAIALDPEHTANNVHLYLGLCKVSVRLGRGKDGLNSCNEALNIDAELIEALHQRGEAKLLLEDWEGAVEDLKQAAQNSQDMEIHESLGKAEKALKMSKRKDWYKILGISRTASISEIKKAYKKLALQWHPDKNVGNREEAENKFREIAAAYEILGDDDKRARFDRGEDLEDMGGGGGGGYNPFHGGGGGGQQYTFHFEGGFPGGGGGFGGFGF
Protein: Ig lambda-1 chain V region (P01723)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MAWISLILSLLALSSGGAISQAVVTQESALTTSPGETVTLTCRSSTGAVTTSNYANWVQEKPDHLFTGLIGGTNNRAPGVPARFSGSLIGDKAALTITGAQTEDEAIYFCALWYSNH
Protein: RtSox23 (O57396)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Interaction partners:
Sequence:
MVEPSPPALHLHANGDVSMVGIGCDRRQESGGEGGGAKAEPCSSPACDWSGHQPMARPESRQLTPPLSRSPSEGSLGKEQFQSPVGMKGGNRGSDHRPEGHKQPTVSEVMPTIEKLLSVDWREKLLEISFLGGNHLKGTPESLAEKELQLLLMINQLSGLREQLLGAHSEQRNMATLLLEKQQQQMELARQQQEQIAKQQQQLIQQQHKINLLQQQIQQVNMPYVMIPAFHPNNQQPVTSDTQMTMPLQPIPCKPVDYPMHLLQNLHSAPMKRPSGTFRQEASQPLNLTSKPKGMDIGNIPSPQSFELGTLTLQGGYRPRDNHRDSPSRPALNLGFLGEGDVVTQAIHDAQQLLRSHGPGGRERERERESTARMEYKVAGHSNRLPPPDRGEDGQTLQTNEDHHSSDSEGPLSAPGVGVFAEVRSPPSSVHIKRPMNAFMVWAKDERRRILQAFPDMHNSSISKILGTRWKSMSNQEKQPYYEEQARLSRQHLERYPDYKYKPRPKRTCIVEGRRLRVGEYKAMMKNRRQEQRGAYPHSQSEPQQLHYTPGEGQYPGGGGAVSMATVPFTPRYWSTTCREGWRLR
Protein: Minor fimbrium anchoring subunit Mfa2 (Minor fimbrial antigen 2) (B2RHG2)
Organism: Porphyromonas gingivalis (strain ATCC 33277 / DSM 20709 / CIP 103683 / JCM 12257 / NCTC 11834 / 2561)
Function: Anchoring subunit of the minor fimbriae. Regulates fimbrial length. These filamentous pili are attached to the cell surface; they mediate biofilm formation, adhesion onto host cells and onto other bacteria that are part of the oral microbiome. Fimbriae of P.gingivalis are major virulence factors (Probable).
Subcellular location: Cell outer membrane {ECO:0000269|PubMed:19589838, ECO:0000269|PubMed:26437277, ECO:0000269|PubMed:27062925}; Lipid-anchor {ECO:0000305|PubMed:27062925}.
Interaction partners:
Sequence:
MNKRKHMDIRRLIISLPAIMALWGGLASCDKMIYDNYDDCPRGVYVNFYSQTECAENPSYPAEVARLNVYAFDKDGILRSANVFEDVQLSAAKEWLIPLEKDGLYTIFAWGNIDDHYNIGEIKIGETTKQQVLMRLKQDGKWATNIDGTTLWYATSPVVELKNMEDGADQYIHTRANLREYTNRVTVSVDSLPHPENYEIKLASSNGSYRFDGTVAKADSTYYPGETKVVGDSTCRAFFTTLKLESGHENTLSVTHKPTGREIFRTDLVGAILSSQYAQNINLRCINDFDIRLVAHHCNCPDDTYVVVQIWINGWLIHSYEIEL
Protein: Protein DWARF 53 (Q2RBP2)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Repressor of strigolactones (SL) signaling. Subjected to a negative feedback control of SL signaling. Suppresses the transcriptional activation activity of SPL14/IPA1 in SL signaling. Acts with SPL14/IPA1 to mediate the SL-regulated tiller development. Subject to a negative feedback regulation by SPL14/IPA1, which binds to D53 promoter to repress D53 gene expression.
Subcellular location: Nucleus {ECO:0000269|PubMed:24336200, ECO:0000269|PubMed:24336215}.
Interaction partners:
- Protein TPR1
- Os08g0432500 protein
Sequence:
MPTPVAAARQCLSPAAVPALDAAVASSRRRAHAQTTSLHLISSLLAPPAPPLLRDALARARSAAYSPRVQLKALDLCFAVSLDRLPSVSASSSSSGAADEPPVSNSLMAAIKRSQANQRRNPDTFHFYHQAATAQTPAAVKVELSHLVLAILDDPVVSRVFAEAGFRSGDIKLAILRPAPPMPLLGRLPTRTRPPPLFLCSFAAADDADVPSPAGNLAGAGEENCRRIAEILSRGRNPMLVGVGAASAADDFAAASPYRIIHVDPNTIDRSDLGVAAAMASATSGLIISIGDLKQLVPDEDAEAQEKGRRVVAEVTRVLETHSKVGRVWVMGWSATYETYLAFLSKFPLVDKDWDLQLLPITAVHAAATAGPAAAAAGLMPPATTVAAFSKPAASLMDSFVPFGGFLCDNYEENSLTANSCPQALRCQQCNDKYEQEVATIISASGITAEDHHQGGLPSLLQNGSMMGPNNGFDPVKARDDRMVLNSKILNLRKKWNEYCLRLHQDHQRINRDPYKPFPRYIGVPTDKERSANSSKGSESVGVQKDVIKPCAVSAVHSSSTARPISSPSVTNKRNEDLVLNLQARHSKSDENLQERGMQSQHGTLSNVDNPDDHVSPSSAAPVETDLVLGTPRECSSKGSSSTCSKRVEDSERSVHLVPKKVDDLNLKHPQLSVQPNSCSWSSINVGKTSHSTLHSVASGGFSAFGQWQKRSPLAAQNSDLSNYKLLVERLFKVVGRQEEALSAICESIVRCRSTESRRGPNRNDIWLCFHGSDSMAKKRIAVALAELMHGSKDNLIYLDLNLQDWDDSSFRGKTGIDCIVEQLSKKRQSVLFLDNIDRADCLVQDSLSDAIKSGRFQDMRGKVVDINDSIVVLSRSMIQGSKNGLEEGLSFSEEKILATRGHRLKILVEPGRAITSGCPSGKVVVSPRHFLTKIQASLCSGSISKRKLSISDDQEKLQESPSSSKRLHRTSSVPFDLNLPVDEDEPLDADDDSSSHENSYGNTEKSIDALLHSVDGSINFKPFDFDKLADDMLQEFSNILRKNLGSECMLEIDVGAMEQILAAAWKSEEDRKPVPTWLEQVFARSLDELKLKRKHVSSSTLRLVACEDTVPAVKGDGLGVLLPPRIILDC
Protein: Glucan 1,4-beta-glucosidase, putative, cel3B (EC 3.2.1.74) (B3PDN7)
Organism: Cellvibrio japonicus (strain Ueda107) (Pseudomonas fluorescens subsp. cellulosa)
Interaction partners:
- Glucanase
- 6-phospho-beta-glucosidase, putative, pbg4A
- Putative 1,4-beta-D-glucan glucohydrolase cel3D
- Glucan 1,4-beta-glucosidase, putative, cel3C
- Glucan 1,4-beta-glucosidase cel3A
- Endoglucanase A
- Glycoside hydrolase family 30, gly30A
- Glucan exo-1,3-beta glucosidase, putative, glu5A
- Alpha-glucosidase, putative, adg97B
- Endoglucanase
Sequence:
MLWPKVTSKVKKDPILEAKIDQLMARMSLEEKIGQMMQPEIRHLTPEDVKQYHVGSVLNGGGSVPNSNRYSKAADWLAMADAFYAASMDESDGKVAIPIMWGTDAVHGVGNIVGATLFPHNIGLGATQNPELIKEIGKVTATEIAVTGLDWDFSPTVAVARDDRWGRTYESYSEDPAIVRLYAAEMVAGLQGDADTASFLSITQVVATAKHFLGDGGTLNGIDRGDCSASESELLEIHAAGYYSAIEAGVQTVMASFNSWHGQHMHGHRYLLTDVLKEQMGFDGFIVGDWNGHGFVEGASVLNCPQAINAGLDMFMVPDPEWKTLYQNTLDQVRDGIIPLARVDDAVRRILRVKLRADLWGKGLPSSRPLAGRDELLGAAAHRAIARQAVRESLVMLKNKNNLLPLSPKSRVLVAGDGADNISKQTGGWSVNWQGTGNTMEDFPGATTLWMGIKAAVTAAGGDAELSPDGTYSSRPDVALVIFGEDPYAEMQGDIQHQLLKSGDTADLDLLRRLKADGIPVVALFITGRPMWVNRELNAADAFVVIWQPGTEGAGVADVLFARAEGGVNYPMGGRLTFSWPKRPDQGPLNVHDTNYDPLFPYGYGLRYGDKDILGDTLSEEGISMPQSTRVLELFNRRPMGNYVIALEGNRNDRQLMNGNLAKASTLTVTVVDRDVQEDARRAVWNGEGEGLVALSTPNRQVLSDYYESDAALFFDIKVDQAPEQQAFVRIGCGPSCHSDVDVTELLRSLEGKGWASIRVDLACYPEVETNFGLRRLPHELFALILEPFSLVANGKMDISFSRVYIEKNRAQHGTFGVVG
Protein: Beta-ureidopropionase (EC 3.5.1.6) (BUP-1) (Beta-alanine synthase) (N-carbamoyl-beta-alanine amidohydrolase) (Q9UBR1)
Organism: Homo sapiens (Human)
Function: Catalyzes a late step in pyrimidine degradation. Converts N-carbamoyl-beta-alanine (3-ureidopropanoate) into beta-alanine, ammonia and carbon dioxide. Likewise, converts N-carbamoyl-beta-aminoisobutyrate (3-ureidoisobutyrate) into beta-aminoisobutyrate, ammonia and carbon dioxide (Probable).
Subcellular location: Cytoplasm.
Interaction partners:
- Dihydropyrimidinase
- Dihydropyrimidine dehydrogenase [NADP
- 4-aminobutyrate aminotransferase, mitochondrial
- Alpha-aminoadipic semialdehyde dehydrogenase
- 4-trimethylaminobutyraldehyde dehydrogenase
- Alanine--glyoxylate aminotransferase 2, mitochondrial
- Cytosolic non-specific dipeptidase
- Beta-Ala-His dipeptidase
- Aldehyde dehydrogenase, mitochondrial
- Aldehyde dehydrogenase, dimeric NADP-preferring
Sequence:
MAGAEWKSLEECLEKHLPLPDLQEVKRVLYGKELRKLDLPREAFEAASREDFELQGYAFEAAEEQLRRPRIVHVGLVQNRIPLPANAPVAEQVSALHRRIKAIVEVAAMCGVNIICFQEAWTMPFAFCTREKLPWTEFAESAEDGPTTRFCQKLAKNHDMVVVSPILERDSEHGDVLWNTAVVISNSGAVLGKTRKNHIPRVGDFNESTYYMEGNLGHPVFQTQFGRIAVNICYGRHHPLNWLMYSINGAEIIFNPSATIGALSESLWPIEARNAAIANHCFTCAINRVGTEHFPNEFTSGDGKKAHQDFGYFYGSSYVAAPDSSRTPGLSRSRDGLLVAKLDLNLCQQVNDVWNFKMTGRYEMYARELAEAVKSNYSPTIVKE
Protein: Cholinergic receptor nicotinic alpha 1 subunit (A0A1B0GV17)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MKLGTWTYDGSVVAINPESDQPDLSNFMESGEWVIKESRGWKHSVTYSCCPDTPYLDITYHFVMQRLPLYFIVNVIIPCLLFSFLTGLVFYLPTDSGEKMTLSISVLLSLTVFLLVIVELIPSTSSAVPLIGKYMLFTMVFVIASIIITVIVINTHHRSPSTHVMPNWVRKVFIDTIPNIMFFSTMKRPSREKQDKKIFTEDIDISDISGKPGPPPMGFHSPLIKHPEVKSAIEGIKYIAETMKSDQESNNAAAEWKYVAMVMDHILLGVFMLVCIIGTLAVFAGRLIELNQQG
Protein: Desmin (P17661)
Organism: Homo sapiens (Human)
Function: Muscle-specific type III intermediate filament essential for proper muscular structure and function. Plays a crucial role in maintaining the structure of sarcomeres, inter-connecting the Z-disks and forming the myofibrils, linking them not only to the sarcolemmal cytoskeleton, but also to the nucleus and mitochondria, thus providing strength for the muscle fiber during activity. In adult striated muscle they form a fibrous network connecting myofibrils to each other and to the plasma membrane from the periphery of the Z-line structures. May act as a sarcomeric microtubule-anchoring protein: specifically associates with detyrosinated tubulin-alpha chains, leading to buckled microtubules and mechanical resistance to contraction. Contributes to the transcriptional regulation of the NKX2-5 gene in cardiac progenitor cells during a short period of cardiomyogenesis and in cardiac side population stem cells in the adult. Plays a role in maintaining an optimal conformation of nebulette (NEB) on heart muscle sarcomeres to bind and recruit cardiac alpha-actin (By similarity).
Subcellular location: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:24200904, ECO:0000269|PubMed:26724190, ECO:0000269|PubMed:30262925}. Cytoplasm {ECO:0000269|PubMed:25394388}. Cell membrane, sarcolemma {ECO:0000269|PubMed:25394388}. Nucleus {ECO:0000250|UniProtKB:P31001}. Cell tip {ECO:0000250|UniProtKB:P31001}. Nucleus envelope {ECO:0000250|UniProtKB:P31001}. Note=Localizes in the intercalated disks which occur at the Z line of cardiomyocytes (PubMed:24200904, PubMed:26724190). Localizes in the nucleus exclusively in differentiating cardiac progenitor cells and premature cardiomyocytes (By similarity). PKP2 is required for correct anchoring of DES at the cell tip and nuclear envelope (By similarity). {ECO:0000250|UniProtKB:P31001, ECO:0000269|PubMed:24200904, ECO:0000269|PubMed:26724190}.
Interaction partners:
- Vimentin
- Syncoilin
- Titin
- Telethonin
- Mastermind-like protein 1
- Plectin
- Dystrobrevin alpha
- Glial fibrillary acidic protein
- Synemin
- FH1/FH2 domain-containing protein 3
Sequence:
MSQAYSSSQRVSSYRRTFGGAPGFPLGSPLSSPVFPRAGFGSKGSSSSVTSRVYQVSRTSGGAGGLGSLRASRLGTTRTPSSYGAGELLDFSLADAVNQEFLTTRTNEKVELQELNDRFANYIEKVRFLEQQNAALAAEVNRLKGREPTRVAELYEEELRELRRQVEVLTNQRARVDVERDNLLDDLQRLKAKLQEEIQLKEEAENNLAAFRADVDAATLARIDLERRIESLNEEIAFLKKVHEEEIRELQAQLQEQQVQVEMDMSKPDLTAALRDIRAQYETIAAKNISEAEEWYKSKVSDLTQAANKNNDALRQAKQEMMEYRHQIQSYTCEIDALKGTNDSLMRQMRELEDRFASEASGYQDNIARLEEEIRHLKDEMARHLREYQDLLNVKMALDVEIATYRKLLEGEESRINLPIQTYSALNFRETSPEQRGSEVHTKKTVMIKTIETRDGEVVSEATQQQHEVL
Protein: Taste receptor type 2 member 30 (T2R30) (Taste receptor type 2 member 47) (T2R47) (P59541)
Organism: Homo sapiens (Human)
Function: Receptor that may play a role in the perception of bitterness and is gustducin-linked. May play a role in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate alpha gustducin, mediate PLC-beta-2 activation and lead to the gating of TRPM5 (By similarity).
Subcellular location: Membrane; Multi-pass membrane protein.
Interaction partners:
- Taste receptor type 1 member 2
- Guanine nucleotide-binding protein G
- Taste receptor type 1 member 3
Sequence:
MITFLPIIFSILIVVIFVIGNFANGFIALVNSIEWVKRQKISFVDQILTALAVSRVGLLWVLLLHWYATQLNPAFYSVEVRITAYNVWAVTNHFSSWLATSLSMFYLLRIANFSNLIFLRIKRRVKSVVLVILLGPLLFLVCHLFVINMDETVWTKEYEGNVTWKIKLRSAMYHSNMTLTMLANFVPLTLTLISFLLLICSLCKHLKKMQLHGKGSQDPSTKVHIKALQTVTSFLLLCAIYFLSMIISVCNFGRLEKQPVFMFCQAIIFSYPSTHPFILILGNKKLKQIFLSVLRHVRYWVKDRSLRLHRFTRGALCVF
Protein: Adenylosuccinate synthetase (AMPSase) (AdSS) (EC 6.3.4.4) (IMP--aspartate ligase) (Q3JZ68)
Organism: Streptococcus agalactiae serotype Ia (strain ATCC 27591 / A909 / CDC SS700)
Function: Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}.
Interaction partners:
Sequence:
MTSVVVVGTQWGDEGKGKITDFLSADAEVIARYQGGDNAGHTIVIDNKKFKLHLIPSGIFFKEKISVIGNGVVVNPKSLVKELAYLHGEGVTTDNLRISDRAHVILPYHIKLDQLQEDAKGDNKIGTTIKGIGPAYMDKAARVGIRIADLLDREVFAERLKINLAEKNRLFEKMYDSTPLEFDDIFEEYYEYGQQIKQYVTDTSVILNDALDAGKRVLFEGAQGVMLDIDQGTYPFVTSSNPVAGGVTIGSGVGPSKINKVVGVCKAYTSRVGDGPFPTELFDEVGDRIREIGKEYGTTTGRPRRVGWFDSVVMRHSRRVSGITNLSLNSIDVLSGLDTVKICVAYDLDGKRIDYYPASLEQLKRCKPIYEELPGWSEDITACRSLDGLPENARNYVRRVGELVGVRISTFSVGPGREQTNILESVWSNI
Protein: Sugar efflux transporter A (P31675)
Organism: Escherichia coli (strain K12)
Function: Involved in the efflux of sugars. The physiological role may be the detoxification of non-metabolizable sugar analogs. Can transport IPTG, lactose and glucose. Has broad substrate specificity, with preferences for glucosides or galactosides with alkyl or aryl substituents.
Subcellular location: Cell inner membrane; Multi-pass membrane protein.
Interaction partners:
- HTH-type transcriptional regulator SgrR
Sequence:
MIWIMTMARRMNGVYAAFMLVAFMMGVAGALQAPTLSLFLSREVGAQPFWIGLFYTVNAIAGIGVSLWLAKRSDSQGDRRKLIIFCCLMAIGNALLFAFNRHYLTLITCGVLLASLANTAMPQLFALAREYADNSAREVVMFSSVMRAQLSLAWVIGPPLAFMLALNYGFTVMFSIAAGIFTLSLVLIAFMLPSVARVELPSENALSMQGGWQDSNVRMLFVASTLMWTCNTMYIIDMPLWISSELGLPDKLAGFLMGTAAGLEIPAMILAGYYVKRYGKRRMMVIAVAAGVLFYTGLIFFNSRMALMTLQLFNAVFIGIVAGIGMLWFQDLMPGRAGAATTLFTNSISTGVILAGVIQGAIAQSWGHFAVYWVIAVISVVALFLTAKVKDV
Protein: Kynurenine 3-monooxygenase (EC 1.14.13.9) (Biosynthesis of nicotinic acid protein 4) (Kynurenine 3-hydroxylase) (P38169)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Catalyzes the hydroxylation of L-kynurenine (L-Kyn) to form 3-hydroxy-L-kynurenine (L-3OHKyn). Required for synthesis of quinolinic acid.
Subcellular location: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03018, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:16407407}.
Interaction partners:
- Kynureninase
- 3-hydroxyanthranilate 3,4-dioxygenase
- Kynurenine formamidase
- High-affinity nicotinic acid transporter
- Probable kynurenine--oxoglutarate transaminase BNA3
- Indoleamine 2,3-dioxygenase
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 1
- Nicotinamide/nicotinic acid mononucleotide adenylyltransferase 2
- Nicotinate-nucleotide pyrophosphorylase [carboxylating]
- Uridine nucleosidase
Sequence:
MSESVAIIGAGLVGCLAALAFSKEGYNVTLYDFRQDPRLDTTKNKNLKSINLAISARGIDALKSIDPDACEHILQDMIPMKGRMIHDLKGRQESQLYGLHGEAINSINRSVLNNSLLDELEKSTTELKFGHKLVKIEWTDDKQICHFAIGEDLKTPHTEKYDFVIGCDGAYSATRSQMQRKVEMDFSQEYMNLRYIELYIPPTEEFKPNYGGNFAIAPDHLHIWPRHKFMLIALANSDGSFTSTFFGSKDQISDLITSKSRVREFLIENFPDIINIMDLDDAVKRFITYPKESLVCVNCKPYDVPGGKAILLGDAAHAMVPFYGQGMNCGFEDVRILMALLKKHSGDRSRAFTEYTQTRHKDLVSITELAKRNYKEMSHDVTSKRFLLRKKLDALFSIIMKDKWIPLYTMISFRSDISYSRALERAGKQTRILKFLESLTLGMLSIGGYKLFKFLTRERS
Protein: Valerianol synthase TPS1G (EC 4.2.3.204) (Terpene synthase 1g) (ChTps1g) (A0A348AUW1)
Organism: Camellia hiemalis (Camellia)
Function: Terpene synthase that catalyzes the biosynthesis of the terpene valerianol, which is a volatile compound of floral scent.
Interaction partners:
Sequence:
MASSQVGDMVNGNAEPTRHLAKFPPSLWGDRFTSFTLDKQLSDKYGNEIEVLKEQVRSMVVAGGRKAVEQINLINVLERLGVSYHFEKEIEEQLEQLFAKFEDNEDYDLFTIALHFRIFRQHGYKMSCDVFNKFRDSNGEFKETVSNDVQGMLSLYEATYLKIRGEGFLDEAHAFTIAQLESLVGGPHLSSDLSEQVMHALKQSIHRGFPRLEAKHFISFYEKDASRNETLLRLAKLDFNQLQLSHREELCHIFRWWKELDLISKVPYARDRAVECFFWSTCAYYEPQHSVGRAVLTKIMLLLSVTDDTYDAYGTYDEVKLYTNAVQRWDVSAMDELPDYMKALYRALLNVYDEVERDLAKQGRAYGVHHSKEAFKEIVRSYEIEAEWFKEGYVVSFEEYMKNALVTSTGRLHTTSCFMGLEADVATTEAFEWILTKPKMVATSGAIGRLVDDVMSHDEEQERGHVATGLDCYMKQHGVSKQEAIVELYKMIENAWRDINEEMLKPTAISMKLLIRVLNLSRISDVVYKYVDGYTHPEIIKDHVISLFEDPIPM
Protein: Outer membrane OMP85 family protein (Q9SRL6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Mitochondrion outer membrane {ECO:0000256|ARBA:ARBA00004374}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004374}. Plastid, chloroplast outer membrane {ECO:0000256|ARBA:ARBA00024013}.
Interaction partners:
- Mitochondrial outer membrane import complex protein METAXIN
- Mitochondrial import receptor subunit TOM40-1
- Probable mitochondrial import receptor subunit TOM40-2
- Mitochondrial import receptor subunit TOM9-2
- Protein REDUCED CHLOROPLAST COVERAGE 1
- Mitochondrial import receptor subunit TOM9-1
- Geranylgeranyl transferase type-1 subunit beta
- RNA ligase/cyclic nucleotide phosphodiesterase family protein
- Rho GTPase-activating protein 3
Sequence:
MANPTENLDANPQIREPEAEEEVEELNGYEGDDGGEDDDGEDDDTESKSQTRESGSSVDRIKAESLFRRMRAAPVPVRVHDVIIGGNEKTKDHIIEAEVDAVREATTLQELLEASRVANSNLRALDIFDSVNITLDSGPPELPGTTNVVIDVVESKSPLTGQIGAYTRAEARSSSVEASLKYKNIFGYGDIWDGSIVYGCDNSAEVGLGMYLPRFRGLSTPFTSRLFLSTQDWLKFSSYKERSLGLSLGLFSSKYHELIYTIAWRNLIDPSQAAAVSIRRQLGHSLLSALKYTFRFDQRNSSLRPTNGYAFISTSQIGGLAPDSRSLRFLKQEVDLRYAVPFGFYNAAINFGVSGGVSFPWGSGYQNRPSSIPERFFLGGNSSPVCSLSGPSALWGFKTRGVGPSEPKRKGDSERDFVGGDAAVTAFADLSFDLPVRWLRERGIHGHVFACAGNMAKLSENEFRNFTAPKFLETFRTSVGAGIVLPTSLFRMELNYCHILKKQEHDQARSGVFLTFSASS
Protein: S1-like domain-containing protein C146.08c (Q9Y803)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Serine/threonine-protein kinase rio1
- Small ribosomal subunit protein eS30B
- Small ribosomal subunit protein eS30A
Sequence:
MSKKYGGQISFDPPARLEKDQVVAKVVQLKGSALFMVVENNGQELLVEMPPKYRNKIWVRRNGFVIVDKSEFLEKDNKIDGTILYVVQSPLKNWKKQIYWPKEFADESLNQNDSEESSSSEEEYDSD
Protein: Neprilysin-like 13 (Q9VCU3)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004401}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
Interaction partners:
- LP16634p
Sequence:
MRATRSAWLGFLLELLLLFEIQLCDVTEARQNHMNRMQMSGNFPDSREEQLVRQKIATDVQKYMNLSADPCTDFFEYACGQWGRYHKRQLRPDELSTAQQLMETKISEQLQQLLTQPLPPQHHPNGYSGASMTNVRKVRAFYESCVAVEANASERRRFLMKILKDNGGLRNVPNSNWQHNRQWVQTLGELRRNYGLDILLGLEIDLNLQTMKGNTIYFGEPKLTIIPAEHCNALATRGAQVRDEVYELVQQQVTENLRDWFGMDTGEAARFAGDIIRFEFELCKQMGEQDIQKPEEEFPPAIQAQIYGARSRTGQERLRRQKGGMTLTELTSEMGNHLDFKMLVEVILESQYPSQVYLRSPEYVKHVVRTVKANNRITVGGYILYVALNELNQPPEEAPSQRARQCVQVTQRLFPQVLGEMFQRHVQRDNAKHDLDAVFNDVIKALEEQFHVEWMDENDRRAARTRLSQYRVSLPDYQSLDLTDLQFQKSEDYWRRLEIALKYRSHQQFEALRGNDFGQDADGLDAFEVRAALSPRQQMVLVGWGLLQAPYYNYYYPKSLKYALLGHRLASALVQAFDDEGWNNHPQATAQWNEVTMSGYRNASECQRAQYSSYLYNEPGEFRNATRLREIIADGSGLNLAFNAYLAWLEQQDHKLRPLLAKETLSELNFTNTQLFFIYFAQTRCWAKDNQDAILDSMPLMQHTPERWDVNGPLSNSAEFGREFGCALGTPMNSGDKCLVY