wanglab/gogpt-training-data huggingface dataset:
Protein: Proteinase-activated receptor 1 (PAR-1) (Thrombin receptor) (P26824)
Organism: Rattus norvegicus (Rat)
Function: High affinity receptor for activated thrombin coupled to G proteins that stimulate phosphoinositide hydrolysis.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15145074}; Multi-pass membrane protein.
Interaction partners:
- Prothrombin
- Guanine nucleotide-binding protein subunit alpha-12
- Guanine nucleotide-binding protein subunit alpha-13
- Vitamin K-dependent protein C
- Guanine nucleotide-binding protein G
- Lysophosphatidic acid receptor 1
- Beta-arrestin-1
- Beta-arrestin-2
- Angiotensinogen
- Lysophosphatidic acid receptor 2
Sequence:
MGPRRLLLVAVGLSLCGPLLSSRVPMRQPESERMYATPYATPNPRSFFLRNPSEDTFEQFPLGDEEEKNESIPLEGRAVYLNKSRFPPMPPPPFISEDASGYLTSPWLTLFIPSVYTFVFIVSLPLNILAIAVFVFRMKVKKPAVVYMLHLAMADVLFVSVLPFKISYYFSGTDWQFGSGMCRFATAACYCNMYASIMLMTVISIDRFLAVVYPIQSLSWRTLGRANFTCVVIWVMAIMGVVPLLLKEQTTQVPGLNITTCHDVLNETLLHGFYSYYFSAFSAIFFLVPLIISTVCYTSIIRCLSSSAVANRSKKSRALFLSAAVFCIFIVCFGPTNVLLIVHYLLLSDSPGTETAYFAYLLCVCVTSVASCIDPLIYYYASSECQKHLYSILCCRESSDSNSCNSTGQLMPSKMDTCSSHLNNSIYKKLLA
Protein: SD08921p (Q8T9B4)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
Sequence:
MAETLVSIKRVQKYMQSDETNVMDMSVDLTEDFQGSNQETVHADGDEERDEAEDKLLGPPIATVNENAKLSEAGISISGLMAKWDVNSPDYSLNGVNLRVQPGTMLGIVGRTGSGKSSLIQAILGELPAESGEIKVNGSMSYASQEPWLFSGTVRQNILFGQPMDRRRYAKVVKKCALERDFELLPFKDKTIVGERGASLSGGQKARISLARAVYRETSIYLLDDPLSAVDTHVARHLFEQCMRGYLRERIVILATHQLQFLQHADQIVIMDKGRVSAVGTYESLRESGLDFASMLADPERDEQSEERSRSRSGSYTHSHSDQRRNSEQSLLSMADSCMDDLEAEQANNQERQEAGQIGLRLYSKYFKAGGGFFAFFVMMGFCVLSQGLASLGDYFLSYWVTKKGNVAYRADNNDTTRSEELEPRLSTWLRDIGLSVDAEMLDTYIFTVITVLTILVTVARSFLFFNLAMKASIRLHNSMFRGITRAAMYFFNTNPSGRILNRFSKDMGQVDEILPAVMMDVIQIFLALAGIVIVIAVVNPLFLIPTVVLGIIFYQLRTFYLKTSRDVKRMEAITRSPVYSHLAASLTGLSTIRAFGAQRVLEAEFDNYQDMHSSAFYMFISTSRAFGYWLDCFCVIYIAIITLSFFIFPPANGGDVGLAITQAMGMTGMVQWGMRQSAELENTMTAVERVVEYEDIEPEGALEAPADKKPPKSWPEQGKIVFDELSLRYTPDPKSENVLKSLSFVIKPKEKVGIVGRTGAGKSSLINALFRLSYNDGSVLIDKRDTSEMGLHDLRSKISIIPQEPVLFSGTMRYNLDPFDEYSDDKLWRSLEEVKLKEVVADLPSGLQSKITEGGTNFSVGQRQLVCLARAILRENRILVMDEATANVDPQTDGLIQTTIRNKFKECTVLTIAHRLHTIMDSDKVLVMDAGRAVEFGTPYELLTLADSKVFHGMVKQTGHATYESLLKIAQKAFENRQNHSLSS
Protein: Small ribosomal subunit protein uS14B (40S ribosomal protein S29-B) (S36) (YS29) (P41058)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains the ribosomal catalytic site termed the peptidyl transferase center (PTC), which catalyzes the formation of peptide bonds, thereby polymerizing the amino acids delivered by tRNAs into a polypeptide chain. The nascent polypeptides leave the ribosome through a tunnel in the LSU and interact with protein factors that function in enzymatic processing, targeting, and the membrane insertion of nascent chains at the exit of the ribosomal tunnel.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}.
Interaction partners:
- Small ribosomal subunit protein eS24A
- Small ribosomal subunit protein uS9A
- Small ribosomal subunit protein uS7
- Small ribosomal subunit protein uS12A
- Small ribosomal subunit protein uS15
- Small ribosomal subunit protein uS13A
- Small ribosomal subunit protein eS19A
- Small ribosomal subunit protein uS2A
- Small ribosomal subunit protein eS10B
- Small ribosomal subunit protein uS3
Sequence:
MAHENVWFSHPRRFGKGSRQCRVCSSHTGLVRKYDLNICRQCFREKANDIGFHKYR
Protein: Vacuolar protein sorting-associated protein 41 homolog (B2RB94)
Organism: Homo sapiens (Human)
Subcellular location: Endosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Late endosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Early endosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Lysosome membrane {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein {ECO:0000256|PIRNR:PIRNR028921}. Golgi apparatus, trans-Golgi network {ECO:0000256|ARBA:ARBA00004601, ECO:0000256|PIRNR:PIRNR028921}. Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000256|PIRNR:PIRNR028921}. Late endosome {ECO:0000256|ARBA:ARBA00004603}.
Interaction partners:
Sequence:
MAEAVEQETGSLEESTDESEEEESEEEPKLKYERLSNGVTEILQKDAASCMTVHDKFLALGTHYGKVYLLDVQGNITQKFDVSPVKINQISLDESVEHMGVCSEDGKVQVFGLYSGEEFHETFDCPIKIIAVHPHFVRSSCKQFVTGGKKLLLFERSWMNRWKSAVLHEGEGNIRSVKWRGHLIAWANNMGVKIFDIISKQRITNVPRDDISLRPDMYPCSLCWKDNVTLIIGWGTSVKVCSVKERHASEMRDLPSRYVEIVSQFETEFYISGLAPLCDQLVVLSYVKEISEKTEREYCARPRLDIIQPLSETCEEISSDALTVRGFQENECRDYHLEYSEGESLFYIVSPRDVVVAKERDQDDHIDWLLEKKKYEEALMAAEISQKNIKRHKILDIGLAYINHLVERGDYDIAARKCQKILGKNAALWEYEVYKFKEIGQLKAISPYLPRGDPVLKPLIYEMILHEFLESDYEGFATLIREWPGDLYNNSVIVQAVRDHLKKDSQNKTLLKTLAELYTYDKNYGNALEIYLTLRHKDVFQLIHKHNLFSSIKDKIVLLMDFDSEKAVDMLLDNEDKISIKKVVEELEDRPELQHVYLHKLFKRDHHKGQRYHEKQISLYAEYDRPNLLPFLRDSTHCPLEKALEICQQRNFVEETVYLLSRMGNSRSALKTIMEELHDVDKAIEFAKEQDDGELWEDLILYSIDKPPFITGLLNNIGTHVDPILLIHRIKEGMEIPNLRDSLVKILQDYNLQILLREGCKKILVADSLSLLKKMHRTQMKGVLVDEENICESCLSPILPSDAAKPFSVVVFHCRHMFHKECLPMPSMNSAAQFCNICSAKNRGPGSAILEMKK
Protein: Tumor susceptibility 101 (F5H442)
Organism: Homo sapiens (Human)
Subcellular location: Late endosome membrane {ECO:0000256|ARBA:ARBA00004633}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004633}.
Interaction partners:
Sequence:
MAVSESQLKKMVSKYKYRDLTVRETVNVITLYKDLKPVLDSYVFNDGSSRELMNLTGTIPVPYRGNTYNIPICLWLLDTYPYNPPICFVKPTSSMTIKTGKHVDANGKIYLPYLHEWKHPQSDLLGLIQVMIVVFGDEPPVFSRPISASYPPYQATGPPNTSYMPGMPGGISPYPSGYPPNPSGYPGCPYPPGGPYPATTSSQYPSQPPVTTVGPSRDGTISEDTIRASLISAVSDKLRWRMKEEMDRAQAELNALKRTEEDLKKGHQKLEEMVTRLDQEVAEVDKNIELLKKKDEELSSALEKMENQSENNDIDEVIIPTAPLYKQILNLYAEENAIEDTIFYLGEALRRGVIDLDVFLKTSVP
Protein: MICOS complex subunit MIC10 (Mitochondrial inner membrane organizing system protein 1) (Q5TGZ0)
Organism: Homo sapiens (Human)
Function: Component of the MICOS complex, a large protein complex of the mitochondrial inner membrane that plays crucial roles in the maintenance of crista junctions, inner membrane architecture, and formation of contact sites to the outer membrane.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:22114354}; Single-pass membrane protein {ECO:0000269|PubMed:22114354}. Note=The C-terminus is located in the intermembrane space (By similarity), while the location of the N-terminus has not been determined yet. As some programs predict the presence of 2 closely apposed membrane domains, it has been proposed that the protein may cross the membrane twice and that both termini may face the intermembrane space (PubMed:22114354). {ECO:0000250, ECO:0000269|PubMed:22114354}.
Interaction partners:
- MICOS complex subunit MIC19
- MICOS complex subunit MIC60
- MICOS complex subunit MIC25
- MICOS complex subunit MIC27
- MICOS complex subunit MIC26
- MICOS complex subunit MIC13
- Sorting and assembly machinery component 50 homolog
- Metaxin-2
- Metaxin-1
- DnaJ homolog subfamily C member 11
Sequence:
MSESELGRKWDRCLADAVVKIGTGFGLGIVFSLTFFKRRMWPLAFGSGMGLGMAYSNCQHDFQAPYLLHGKYVKEQEQ
Protein: Stress-activated protein kinase JNK (EC 2.7.11.24) (J3KNK1)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasm {ECO:0000256|RuleBase:RU368052}.
Interaction partners:
Sequence:
MSDSKCDSQFYSVQVADSTFTVLKRYQQLKPIGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKTLEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENASQARDLLSKMLVIDPDKRISVDEALRHPYITVWYDPAEAEAPPPQIYDAQLEEREHAIEEWKELIYKEVMDWEERSKNGVVKDQPSDAAVSSNATPSQSSSINDISSMSTEQTLASDTDSSLDASTGPLEGCR
Protein: Actin-related protein 2 (Protein WURM) (Q9LSD6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Functions as ATP-binding component of the Arp2/3 complex which is involved in regulation of actin polymerization and together with an activating nucleation-promoting factor (NPF) mediates the formation of branched actin networks. Seems to contact the pointed end of the daughter actin filament (By similarity). Arp2/3 complex plays a critical role in the control of cell morphogenesis via the modulation of cell polarity development. Involved in the control of cell morphogenesis in leaf epidermal pavement cells, root hairs, hypocotyls epidermal cells and trichomes, especially during rapid cell expansion. Regulates the directionality of cell expansion by regulating the actin organization, and thus the microtubules distribution and the fusion of small vacuoles.
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Actin-related protein 2/3 complex subunit 2A
- Actin-related protein 3
- Actin-related protein 2/3 complex subunit 3
- Actin-related protein 2/3 complex subunit 4
- Uncharacterized protein
- Actin-related protein 2/3 complex subunit 1A
- Actin-related protein 2/3 complex subunit 1B
- Actin-related protein 2/3 complex subunit 5A
- Actin-related protein 2/3 complex subunit 5B
- At4g14145
Sequence:
MDNKNVVVCDNGTGYVKCGFAGENFPTSVFPCVVGRPLLRYEESLMEQQVKDIVVGETCSELRHQLDINYPVHNGIVQNWDDMEHVWDHAFYNELKINPSDCKILLTDPPLNPSKNREKMIETMFEKYNFAGVFIQIQAVLTLYAQGLLTGLVIDSGDGVTHVVPVVDGYSFPHLTKRMNVAGRHITAYLVDLLSRRGYAMNKTADFETVREIKEKLCYISYDYKRESQLGLETTILVKNYTLPDGRVIKVGTERFQAPEALFTPELIDVEGDGMADMVFRCIQEMDIDNRMMLYQHIVLSGGSTMYPGLPSRLEKEIQDRYLDTVLKGNKDGLKKLRLRIEDPPRRKHMVYLGGAVLAGIMKDAPEFWINREDYMEEGINCLNKMSQA
Protein: Lactamase-like protein vrtG (EC 3.1.-.-) (Viridicatumtoxin synthesis protein G) (D7PHZ8)
Organism: Penicillium aethiopicum
Function: Lactamase-like protein; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system. The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyketide synthase vrtA. The aldolase vrtJ may be involved in the synthesis of the malonamate substrate for malonamoyl-CoA synthetase vrtB. The polyketide synthase vrtA then may utilize the malonamoyl-CoA starter unit, followed by sequential condensation of eight malonyl-CoA units to form the polyketide backbone. The cyclization of the last ring could be mediated by the lactamase-like protein vrtG. The proposed post-PKS tailoring steps are an hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase vrtE, a hydroxylation at C12a catalyzed by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase vrtF. VrtC is then proposed to catalyze the transfer of a geranyl group synthesized by vrtD to the aromatic C ring of the tetracyclic polyketide intermediate of viridicatumtoxin to yield previridicatumtoxin. Finally, the cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to afford viridicatumtoxin.
Interaction partners:
Sequence:
MATRIPFDESYWEEYLSGQEASLPALPAVTQLSPRVTRLLAGNPGIMQLQGTNTYLVGTGPARILIDTGEGRPVWHATLAEHLRTHHLTLEYILLTHWHGDHTGGIPDLIAHDPTLQSRIYKHHPDRGQRPIRDGQRFTVTGATVRAVFTPGHAIDHMCFLIEEEKALLTGDNVLGHGFAIVQDLAEYMASLARMAALGCERGYPAHGAVIENLPAKMQLYIHHNEVRVQQVITALASVVKLPGKRVGMTVPEIGRAIYGEVPREIVENAIVPFLSQVLWKLAEDRKVGFEPGEANKRRWFGLVTQQ
Protein: Putative ribosomal large subunit pseudouridine synthase SVR1, chloroplastic (EC 5.4.99.-) (Protein PIGMENT DEFECTIVE 328) (Protein SUPPRESSOR OF VARIEGATION 1) (Q8L960)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Responsible for synthesis of pseudouridine in chloroplastic 23S ribosomal RNA (Probable). Necessary for normal chloroplast rRNA processing and translation. Required for normal chloroplast development and maintenance. May function in other plastids, such as root amyloplasts.
Subcellular location: Plastid, chloroplast {ECO:0000269|PubMed:18599582}.
Interaction partners:
- Putative rRNA 2'-O-methyltransferase fibrillarin 3
- NOL1/NOP2/sun family protein / antitermination NusB domain-containing protein
- ATP-dependent Clp protease proteolytic subunit-related protein 1, chloroplastic
- H/ACA ribonucleoprotein complex subunit 4
- ATP-dependent zinc metalloprotease FTSH 2, chloroplastic
- Pentatricopeptide repeat-containing protein At4g16390, chloroplastic
- Probable histone H2A.2
- Probable protein phosphatase 2C 49
- Translation initiation factor IF3-2, chloroplastic
- Large ribosomal subunit protein bL35c
Sequence:
MASVAASSSISFAASFLKIKAFPLSPRFFPIRTLRCSVSSSSSEPIEFDISFAPPKPKPSSTHGGVTPQQLFIPWIVRSDDGTLKLQSQPPARLIHNLAIDATTQNPKKKDKSKKKQPQATSSSSATTTASSPASHSEVKPKLSKAARRFYNENFKEQPQRLSKVLAAAGVASRRTSEELIFDGKVTVNGILCNTPQTRVDPSRDIIYVNGNRIPKKLPPKVYFALNKPKGYICSSGEKEIKSAISLFDEYLSSWDKRNPGTPKPRLFTVGRLDVATTGLIVVTNDGDFAQKLSHPSSSLPKEYITTVVGDIHKRHLMAISEGTMVEGVHCVPDSVELMPKQHDIPRARLRIVVHEGRNHEVRELVKNAGLEVHSLKRVRIGGFRLPSDLGLGKHVELKQSELKALGWKN
Protein: Beta-1,6-galactofuranosyltransferase WbbI (EC 2.4.1.-) (D-Galf:alpha-D-Glc beta-1,6-galactofuranosyltransferase) (GalF transferase) (P37749)
Organism: Escherichia coli (strain K12)
Function: Involved in the transfer of galactofuranose (Galf) onto an alpha-D-gluco-configured acceptor substrate to form a beta-1,6-linkage. It uses n-octyl alpha-D-glucopyranoside as an acceptor substrate for the addition of galactofuranose from the donor substrate UDP-galactofuranose. It is not able to use beta-D-glucopyranoside isomers.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- Putative glycosyltransferase WbbK
- UDP-galactopyranose mutase
- Putative O-antigen polymerase
- Putative lipopolysaccharide biosynthesis O-acetyl transferase WbbJ
- Putative O-antigen transporter
- dTDP-4-dehydrorhamnose 3,5-epimerase
- Glucose-1-phosphate thymidylyltransferase 1
- dTDP-glucose 4,6-dehydratase 1
- dTDP-4-dehydrorhamnose reductase
- Uncharacterized protein YqeK
Sequence:
MYFLNDLNFSRRDAGFKARKDALDIASDYENISVVNIPLWGGVVQRIISSVKLSTFLCGLENKDVLIFNFPMAKPFWHILSFFHRLLKFRIVPLIHDIDELRGGGGSDSVRLATCDMVISHNPQMTKYLSKYMSQDKIKDIKIFDYLVSSDVEHRDVTDKQRGVIYAGNLSRHKCSFIYTEGCDFTLFGVNYENKDNPKYLGSFDAQSPEKINLPGMQFGLIWDGDSVETCSGAFGDYLKFNNPHKTSLYLSMELPVFIWDKAALADFIVDNRIGYAVGSIKEMQEIVDSMTIETYKQISENTKIISQKIRTGSYFRDVLEEVIDDLKTR
Protein: Ubiquitin-like modifier activating enzyme 7 (H3BKY9)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
XAAQCFLSEESLGRNRAEASQAQLAQLNEAVQISVHSGDITEDLLQGFQVVVLTDSKLEDQLKVGPLCHKHGVRFLMAETRGLVGAPYSQLMSFLSNFRHPH
Protein: C-type lectin domain family 2 member B (Activation-induced C-type lectin) (C-type lectin superfamily member 2) (IFN-alpha-2b-inducing-related protein 1) (Q92478)
Organism: Homo sapiens (Human)
Subcellular location: Cell membrane {ECO:0000269|PubMed:23929856, ECO:0000269|PubMed:29980609}; Single-pass type II membrane protein {ECO:0000305}. Golgi apparatus membrane {ECO:0000269|PubMed:23929856}. Note=Resting NK cells contain intracellular stores of CLEC2B associated with the Golgi complex. {ECO:0000269|PubMed:23929856}.
Interaction partners:
- Killer cell lectin-like receptor subfamily F member 1
- SLAM family member 6
- NKG2-F type II integral membrane protein
- Killer cell lectin-like receptor subfamily F member 2
- HLA class I histocompatibility antigen, alpha chain E
- Natural cytotoxicity triggering receptor 1
Sequence:
MMTKHKKCFIIVGVLITTNIITLIVKLTRDSQSLCPYDWIGFQNKCYYFSKEEGDWNSSKYNCSTQHADLTIIDNIEEMNFLRRYKCSSDHWIGLKMAKNRTGQWVDGATFTKSFGMRGSEGCAYLSDDGAATARCYTERKWICRKRIH
Protein: Polyadenylate-binding protein RBP47C (Poly(A)-binding protein RBP47C) (RNA-binding protein 47C) (AtRBP47C) (Q9SX79)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Heterogeneous nuclear ribonucleoprotein (hnRNP)-protein binding the poly(A) tail of mRNA and probably involved in some steps of pre-mRNA maturation.
Subcellular location: Nucleus {ECO:0000250}. Cytoplasmic granule {ECO:0000250}.
Interaction partners:
- AT3g17750/MIG5_4
- Large ribosomal subunit protein uL13y
- DEAD-box ATP-dependent RNA helicase 15
- Large ribosomal subunit protein eL15y
- Small ribosomal subunit protein eS27y
- Protein SHORT ROOT IN SALT MEDIUM 1
- Serine/arginine-rich splicing factor SC35
- Helicase-like transcription factor CHR28
- Large ribosomal subunit protein eL13z
Sequence:
MADVKIQSESESSDSHPVVDNQPPPPPPPPQQPAKEEENQPKTSPTPPPHWMRYPPTVIIPHQMMYAPPPFPPYHQYPNHHHLHHQSRGNKHQNAFNGENKTIWVGDLHHWMDEAYLNSSFASGDEREIVSVKVIRNKNNGLSEGYGFVEFESHDVADKVLREFNGTTMPNTDQPFRLNWASFSTGEKRLENNGPDLSIFVGDLSPDVSDNLLHETFSEKYPSVKAAKVVLDANTGRSKGYGFVRFGDENERTKAMTEMNGVKCSSRAMRIGPATPRKTNGYQQQGGYMPNGTLTRPEGDIMNTTIFVGGLDSSVTDEDLKQPFNEFGEIVSVKIPVGKGCGFVQFVNRPNAEEALEKLNGTVIGKQTVRLSWGRNPANKQPRDKYGNQWVDPYYGGQFYNGYGYMVPQPDPRMYPAAPYYPMYGGHQQQVS
Protein: sn-1-specific diacylglycerol lipase (EC 3.1.1.116) (B7Z150)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Eye-specific diacylglycerol kinase
Sequence:
MPGLVVFRRRWSVGSDDLVVPGAFLLTIHFICFVIVSVSLVIFEYNTRILSVKLLFYHLIGYLLILFFSICVEIGICVISMRGSILDAEARTSINIWIYLKSLVILFDIAWLAVGSVWLGHYYTTAPIDDPKKVYIAIIICNWALVVITLITIWCTFDAAGRSWVKMKKYQRSMRETESRFNYKRSNSMNRNWRQRKVMRAYQDSWDHRCRLLFCCMGSSERNRNSFTDIARLLSDFFRELDVVPSDVVAGLVLLRKFQRLEREAIVRQRKNGTYEFLSGVPITERTQFLALNDAKNYDFFQTVIHYMYFAQGAYGWPMYVIINRSKMWHLVPELKCFGCCCGTSDDTEVIQDNCCLCNYAALKKTLQLGDIDIVYATYHVDVGETPFFVAIDYTHRAVVISIRGTLSMKDILTDLNAEGEVLPLQPPRDDWLGHKGMVQAAIYIRNKLQEENLIERALQRNPDRQTHTFDLVLVGHSLGAGTAAILAILLKPEHPTLQCFSYSPPGGLLSMPAVEYSKSFITSVVLGKDVVPRIGLNQMEALRADLINAIQRSVDPKWKTISCSVICCGCGPEPTSVVNMSGQDTHINQYQEERGTARSTSAHPTDSSIALTLHQPLYPPGRIIHIVRHHPKPDEQKYDSGWRNVLKNREPVYQAIWADSTDFDEVLISPVMLQDHMPDKVLAALKKVVTTSGPRKPQRQTSNAFSTGSNEAAHDMDLEPPHCSGHSAPTDAMRFETRTDPGQMQNSMSQSQHCKRLSQSSYTNLSNCLVLTPTAQHKLCLETSFTNGSTPHQSGVQPNPRLTSAASSLLSSATTPYDISSALDDSLATVALRQSPSLISAETTATVIVNPEPDAEEIAIPQRLKAVAFDMALTPPPTLPERSMLGRQHSEKKPRSLPLAQVQALRRASDAGAVPGVDLLHDDWYGLAPLASPETLSEISSVSSRTSVPISLANSIERYLQHMGVGVGGPKVPLEDIFESQLHTPKVMRRAPKFSENLAGCAEDTRNLDQYKRLGRVFITFPRIFPDQSPAAHSLDSSDDSFESASAHSLQRLQLPHGANAVQSSKSADPLDGDPDATRQTQPAKKLTFSDSDILTDADCLRLCPHCPCDRDVQRGCCTRSEHGKCGTEISGGCGGAAMGLGSTDTSFYSASSSLEQFATPARQNGGTGASGNHLEEILIRPGVLESHFPVLGGGSAIETPALVAPASPSPLSNGKRPDVVGGRVRKRLSSEEFVFSRSEDLPSLVQIGDRCTGSPAGRRRAKGCVYPAGNSLRLDAAAAVASASASPTSISKFTRTRVAAGGLAAKQAAGNNESNV
Protein: 1,3-beta-galactosyl-N-acetylhexosamine phosphorylase Cphy3030 (EC 2.4.1.211) (D-galactosyl-1,4-L-rhamnose phosphorylase) (A9KQ75)
Organism: Lachnoclostridium phytofermentans (strain ATCC 700394 / DSM 18823 / ISDg) (Clostridium phytofermentans)
Function: Reversibly phosphorolyzes beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine to form alpha-D-galactopyranose 1-phosphate and acetyl-D-glucosamine. Active towards galacto-N-biose and lacto-N-biose. Does not phosphorolyze galacto-N-tetraose or lacto-N-tetraose. In the reverse reaction has activity toward N-acetyl-D-glucosamine and N-acetyl-D-galactosamine, but not L-rhamnose, D-glucose or D-galactose.
Interaction partners:
- Extracellular solute-binding protein family 1
- Extracellular solute-binding protein family 1
- Binding-protein-dependent transport systems inner membrane component
- Binding-protein-dependent transport systems inner membrane component
Sequence:
MSEKLTGRVTVPTDVDMIQETKEIAERWGADALRDCDGTDMPDELKKMPAKIYSTYYTTRKDNAWANANPDEVQQVYLMTEFYTAMSQGELRIPLMKHLYKDQLKPNTIHDIKRWWEVVDRTTGEPLVLDAWEYDENNQEVIILNPDHFHDYTVSFLAFIIWDPVHMYNFITNDWQDVEHQITYDVRQPKTQKYVIEKLKRWMKENPDSDVVRFTTFFHQFTLVFNEFAKEKFVDWFGYSASVSPYILEQFEKEVGYKFRPEYIIDQGYHNNTNRVPSKEFRDFQEFQQREVAKLMKVLVDICHDNDKEAMMFLGDHWIGTEPFGEYFKHVGLDAVVGSVGNGTTLRLISDIPGVKYTEGRFLPYFFPDVFHEGGDPIKEAKVNWVTARRAILRKPVDRIGYGGYLKLALDFPEFIQYIEEVCDEFRLLYDNMGGQSPYSHFKVGVLNSWGKIRSWGTHMVAHAIDYKQTYSYAGVLEALSGMPFDVEFISFEDVIKNPVILNECGVVINVGDAYTGPSGGAYWTNEKVSSAVKAFVAQGGGFIGVGEPSACEHQGRYFTLANVLGVNKEIGFSMSTDKYNWDEHSHFITEDSNESINFGEGMKNIYALDGAQILRKDGQDVQMAVNQFGDGRSVYISGIPYSFENSRMLYRAIFWAAGMEQEMKKWYSSNYNVEVNYYPATKKYCIVNNTYEPQETMIYDGLGREYSMKLKANDILWFTFLED
Protein: 4-trimethylaminobutyraldehyde dehydrogenase (TMABA-DH) (TMABADH) (EC 1.2.1.47) (Aldehyde dehydrogenase family 9 member A1) (EC 1.2.1.3) (Formaldehyde dehydrogenase) (EC 1.2.1.46) (Gamma-aminobutyraldehyde dehydrogenase) (EC 1.2.1.19) (Q9JLJ2)
Organism: Mus musculus (Mouse)
Function: Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine with high efficiency (in vitro). Can catalyze the irreversible oxidation of a broad range of aldehydes to the corresponding acids in an NAD-dependent reaction, but with low efficiency.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9JLJ3}. Cytoplasm {ECO:0000250|UniProtKB:P49189}.
Interaction partners:
- Gamma-butyrobetaine dioxygenase
- Alpha-aminoadipic semialdehyde dehydrogenase
- Hydroxyacyl-coenzyme A dehydrogenase, mitochondrial
- Aldo-keto reductase family 1 member A1
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- Peroxisomal bifunctional enzyme
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- Acetyl-coenzyme A synthetase, cytoplasmic
- Beta-ureidopropionase
- Aldehyde oxidase 3
Sequence:
MSTGTFVVSQPLNYRGGARVEPVDASGTEKAFEPATGRVIATFACSGEKEVNLAVENAKAAFKLWSKKSGLERCQVLLEAARIIKERKDEIATVETINNGKSIFEARLDVDTCWQCLEYYAGLAASMAGEHIQLPGGSFGYTRREPLGVCVGIGAWNYPFQIACWKSAPALACGNAMIFKPSPFTPVSALLLAEIYTKAGAPPGLFNVVQGGAATGQFLCHHREVAKISFTGSVPTGVKIMEMSAKGVKPITLELGGKSPLIIFSDCNMENAVKGALMANFLTQGQVCCNGTRVFVQKEIADKFINEVVKQTQKIKLGDPLLEDTRMGPLINAPHLERVLGFVKLAKEQGATVLCGGEVYVPEDPKLKHGYYMTPCILTNCRDDMTCVKEEIFGPVMSILTFGTEAEVLERANDTTFGLAAGVFTRDIQRAHRVAAELQAGTCYINNYNVSPVELPFGGYKKSGFGRENGRVTIEYYSQLKTVCVEMGDVESAF