wanglab/gogpt-training-data huggingface dataset:
Protein: Acylglycerol kinase, mitochondrial (hAGK) (EC 2.7.1.107) (EC 2.7.1.138) (EC 2.7.1.94) (Multiple substrate lipid kinase) (HsMuLK) (MuLK) (Multi-substrate lipid kinase) (Q53H12)
Organism: Homo sapiens (Human)
Function: Lipid kinase that can phosphorylate both monoacylglycerol and diacylglycerol to form lysophosphatidic acid (LPA) and phosphatidic acid (PA), respectively. Does not phosphorylate sphingosine. Phosphorylates ceramide (By similarity). Phosphorylates 1,2-dioleoylglycerol more rapidly than 2,3-dioleoylglycerol (By similarity). Independently of its lipid kinase activity, acts as a component of the TIM22 complex. The TIM22 complex mediates the import and insertion of multi-pass transmembrane proteins into the mitochondrial inner membrane by forming a twin-pore translocase that uses the membrane potential as the external driving force. In the TIM22 complex, required for the import of a subset of metabolite carriers into mitochondria, such as ANT1/SLC25A4 and SLC25A24, while it is not required for the import of TIMM23. Overexpression increases the formation and secretion of LPA, resulting in transactivation of EGFR and activation of the downstream MAPK signaling pathway, leading to increased cell growth.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:15939762, ECO:0000269|PubMed:16269826, ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726}; Peripheral membrane protein {ECO:0000269|PubMed:28712724}. Mitochondrion intermembrane space {ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726}. Note=Localizes in the mitochondrion intermembrane space, where it associates with the inner membrane (PubMed:28712724). It is unclear whether the N-terminal hydrophobic region forms a transmembrane region or associates with the membrane without crossing it (PubMed:28712724, PubMed:28712726). {ECO:0000269|PubMed:28712724, ECO:0000269|PubMed:28712726}.
Interaction partners:
- Mitochondrial import inner membrane translocase subunit Tim29
- Mitochondrial import inner membrane translocase subunit Tim10 B
- Mitochondrial import inner membrane translocase subunit Tim22
- Mitochondrial import inner membrane translocase subunit Tim9
- Mitochondrial import inner membrane translocase subunit Tim10
- Monoglyceride lipase
- Lysocardiolipin acyltransferase 1
- 1-acyl-sn-glycerol-3-phosphate acyltransferase beta
- Membrane-bound glycerophospholipid O-acyltransferase 2
- 1-acyl-sn-glycerol-3-phosphate acyltransferase gamma
Sequence:
MTVFFKTLRNHWKKTTAGLCLLTWGGHWLYGKHCDNLLRRAACQEAQVFGNQLIPPNAQVKKATVFLNPAACKGKARTLFEKNAAPILHLSGMDVTIVKTDYEGQAKKLLELMENTDVIIVAGGDGTLQEVVTGVLRRTDEATFSKIPIGFIPLGETSSLSHTLFAESGNKVQHITDATLAIVKGETVPLDVLQIKGEKEQPVFAMTGLRWGSFRDAGVKVSKYWYLGPLKIKAAHFFSTLKEWPQTHQASISYTGPTERPPNEPEETPVQRPSLYRRILRRLASYWAQPQDALSQEVSPEVWKDVQLSTIELSITTRNNQLDPTSKEDFLNICIEPDTISKGDFITIGSRKVRNPKLHVEGTECLQASQCTLLIPEGAGGSFSIDSEEYEAMPVEVKLLPRKLQFFCDPRKREQMLTSPTQ
Protein: PTPRF interacting protein alpha 1 (A0A2R8Y7R9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
XGGHGSGSPSQPDADSHFEQLMVSMLEERDRLLDTLRETQETLALTQGKLHEVGHERDSLQRQLNTALPQEFAALTKELNVCREQLLEREEEIAELKAERNNTRLLLEHLECLVSRHERSLRMTVVKRQAQSPAGVSSEVEVLKALKSLFEHHKALDEKVRERLRVALERCSLLEEELGATHKELMILKEQNNQKKTLTDGVLDINHEQENTPSTSGKRSSDGSLSHEEDLAKVIELQEIISKQSREQSQMKERLASLSSHVTELEEDLDTARKDLIKSEEMNTKLQRDVREAMAQKEDMEERITTLEKRYLAAQREATSVHDLNDKLENEIANKDSMHRQTEDKNRQLQERLELAEQKLQQTLRKAETLPEVEAELAQRVAALSKAEERHGNIEERLRQMEAQLEEKNQELQRARQREKMNEEHNKRLSDTVDKLLSESNERLQLHLKERMAALEDKNSLLREVESAKKQLEETQHDKDQLVLNIEALRAELDHMRLRGASLHHGRPHLGSVPDFRFPMADGHTDSYSTSAVLRRPQKGRLAALRDEPSKVQTLNEQDWERAQQASVLANVAQAFESDADVSDGEDDRDTLLSSVDLLSPSGQADAHTLAMMLQEQLDAINKEIRLIQEEKENTEQRAEEIESRVGSGSLDNLGRFRSMSSIPPYPASSLASSSPPGSGRSTPRRIPHSPAREVDRLGVMTLPSDLRKHRRKLPPSREEVRDDKTTIKCETSPPSSPRALRLDRLHKGALHTVSHEDIRDIRNSTGSQDGPVSNPSSSNSSQDSLHKAPKKKGIKSSIGRLFGKKEKGRPGQTGKEALGQAGVSETDNSSQDALGLSKLGGQAEKNRKLQKKHELLEEARRQGLPFAQWDGPTVVVWLELWVGMPAWYVAACRANVKSGAIMSALSDTEIQREIGISNPLHRLKLRLAIQEIMSLTSPSAPPTSRTTTGNVWLTHEEMETLAATPQTEDEEGSWAQTLAYGDMNHEWIGNEWLPSLGLPQYRSYFMECLVDARMLDHLTKKDLRGQLKMVDSFHRNSFQCGIMCLRRLNYDRKELERKREESQSEIKDVLVWSNDRVIRWILSIGLKEYANNLIESGVHGALLALDETFDFSALALLLQIPTQNTQARAVLEREFNNLLVMGTDRRFDEDDDKSFRRAPSWRKKFRPKDIRGLAAGSAETLPANFRVTSSMSSPSMQPKKMQMDGNVSGTQRLDSATVRTYSC
Protein: Non-ribosomal peptide synthetase (Q70AZ6)
Organism: Actinoplanes teichomyceticus
Interaction partners:
Sequence:
MTVDDTRAKPRSSVEDVWPLSPLQEGMLYHTALDGDGPDTYTVQTVYGIDGPLDAGRLRASWQALVDRHAALRACFRYVSGAQMVQVIQRDVELPWRETDLSGLPEDLADGEVARLAEQEMAERLRLEAAPLMKLHLIRLGPQRHRLVHTLHHVLVDGWSMPILHRELAAIYAAGGDASGLPPAVSYRDYLAWLGRQDKESARAAWRDALAGLDTPTTVAPADPARVPDIDTAMVELSPELTDDLLRLAHGHDLTLNTVVQGVWAVVLAQLAGRTDVVFGATASGRPAELAGVEAMVGLLLATLPVRVRLDGRQRVVDMLADLQRDQSALRAHQHLGLQEVQAVVGPGAVFDTLVIYENFPRTGLGGSADDGLVMRPVQKGRDSSHYPFTLVTGPGERMPVILYYDRGLFDQAAATSVLGAIVRVLERLVAEPGVLVGRLTLLGEAERAVVVGDWNATAGPVPGDSMVELFDRRVAAAPDTVAITDADGADLTYAEVDQASNRLAAHLADRGVRRGDRVGVAVERSADLPIVFLAIWKAGAAYVPVDVGYPAERIALILAGSAVSTVICTQATEAAVPQNVPQRATIVLDAPPTRAAVDACAGTAPTFRPSAADLAYVMYTSGSTGVPKGVAVPHGAVAGLAGDAGWRIGPGDGVLMHATHVFDPSLYEMWVPLATGGRVLVAAPGVVDAGGIRQAVARGATAVHLTAGTFRALAEASPDCFAGLREVGTGGDVVPAHTVAHLRRAQPQLRVRNTYGPTETTLCATWKPIEPGAQLGPELPIGRPMTNRRIYILDAFLRPVAPGVAGELYIAGTGLARGYLSRPDLTAERFVACPFLAGERMYRTGDLARWNRDGEVVFLGRADDQVKIRGYRVELAEVEAVLAAQPGVREAVVVAREDRPGERRLVGYVVSDAGELDTEQIRQQMARVLPGYMVPVAVIGLVSLPITANSKVDRRALPAPDLAGHASAKAPESATEKVLCALYAEILGVERVGVDDAFHDLGGSSALAMRLIARIREELGVDLPIRQLFSSPTPAGVARALAAKSRPALEAVTRPERVPLTARQLRAWLLARPSEETRGRHLSVALRLRGRLDVAALEAALRDVAARHEILRTTFPGDAQTVHQHIHDAAPVRLTPVPATEEDLPARLAERGEQLFDLTRDMPWRCELFALSEKEHVLSVTVHRIAADDDSMDVFFRDLAAAYGARRAGRAPERAPLALQFADYAIWEQRLLDGEREQDSLINDQITFWRNHLAGIDQETVLPFDRARPAIPSRRAGTVALRLDAGPHARLAEAVESAGADMPQLVQAALAMLLTRYGAGTDLVIGTTLPRDEDLIDLEPMIGPFARPFPVRTDLSADPTFLEVVARVQEAVREARQHLDVPFEKIPELLALPGSLSRHPVYQVGLQVREEDNGAWDAAELPALRTSVEPTGVEAIELDLAFALTERRNDDDDEDGIEGALHYAADLFDHDTAASLARRLVRVLEQVAEDPGRRISDLDILLDDAERGAPAIAPARWAGAVPAAVADLVAAGPLGALVLDEAQRPVAPGTVGDLWVTGPAVDADTGGRPSVPCPFGTPGHRMLHTGLLARKSPARTLVVVGERRGASASAKTGDYEVLLPLRAAGDRAPLFCIHASGGLSWNYGPLLRHLPPNQPVYGVQARGLARTEPLPGSVEEMAADYVEQIRTVQPTGPYHLLGWSLGGRIAQAMAVLLEADGEKVGLLALLAAYPVYMGRKATGTVTEEAARDEDALERRKQQELELAGQLVQGAGARSRLEAVMRNLWEVGPAHTASPFASDVLLFVASVDRPAHLPVSEAIASWKDFTGGTIEPHEIATNHYEMVQPAALAQIGAIVAEKLRSRPDA
Protein: Fgr14p (A0A1D8PSY7)
Organism: Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast)
Interaction partners:
- Fgr13p
- Fgr28p
Sequence:
MKRNESYINSLTIGSKNIGSHQSTDFKKLLDIFLKLIGEHSMIDIWFIQEIRFVSQEQFNYINKILKQHNAQLRMHHFEDLTGFLIHSPHAKLKFKIRDNDNHHTTHFEGRISILDITLITNEDITLINNYLHSGNMDAQMTLLKAFIKYIANLKKHTNHNIIYGGDYNHIMSLDDVQLPSDQTRYIISKKESEIIQLMSNFYKKWKLQDAFQIRNNLQPTNFHSNKSVKKRLDRIYIDSRIRRKLRNCRILEEFKQISTHKIIAMSFQIQKEPILKVGNPRYSIPQWMSQDENIIKDLNNNEQSSLTPFSNWNGIINRIKEKVIFYEKYQRYIRAYIPHAGNFPDEKMLKFRFRPSFNFSIITEMQTESGNTVQDTEIMINLATKFYQDLFLVEDRHLESFTFVEQFDKKIDDTDKVLLEKAFIEDNVYDHSLMINKKTAVGTDGISYQNLIELWPSLGESLIRAGNNILKYGTLPQQMSEVIITLIPKKSKTPIIENFRPISVISCAVRLLSSVIEKQLNPVLAKVIEKTQTGFLKERSISNSIYLLDMVLTRYQTSKTADAESAGFINLDFRKAFDSVHHDFILKVLQQVGFGPKATNFLMAITAKQKAKVSINNIEGPCFPLKRGVRQGNPISPLIFILILETFLARLSKEIEGIGVVNEVSSVAYTAYADDVIIFFKNKNDQERIQQLLEDFGRESGLYLNNNKTEVCYFNDIPEISFLPYVSKKLQLEKLTYLGVPMKKADEEFDPWTSFVLNLNAQIRMTPISDLPYQLIMKLMNIFIFSKLYYRDLHSPISTTAVSSIITTVQQRLPLYFKLQRLQTPNHLGGFGLMNPNHQVKGRRGKQIYLLYTQEDDLIIKFMRTKIQDILDNIAKDYYTMPTEPDKLIVYPWYLFGMGVSCHSSLQFRYLKERVYENLTKSEISWFEAWFQLVHYTGPPVETPIIIMSIEDYANLIIQPQTESIKLMSPNFEEQSLSEQTFHHTSRKLCPQAPIIPEGWGKHFDTIKSLTISDWTEFWKNMNKVQKQSVGSLQDYHLFILGYYSHYPFYPNYKKSEIHFCQLCNTGTDSIVHHIFECGETMELWSKHFNSQRTPQFIIGNKHLHKKDLYALNEYIKEVVQKVKRRRGSPILNQGERENVDAGTNVLV
Protein: Vacuolar protein sorting-associated protein 54 (Tumor antigen SLP-8p homolog) (Q5SPW0)
Organism: Mus musculus (Mouse)
Function: Acts as component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN). The GARP complex is required for the maintenance of the cycling of mannose 6-phosphate receptors between the TGN and endosomes, this cycling is necessary for proper lysosomal sorting of acid hydrolases such as CTSD. Within the GARP complex, required to tether the complex to the TGN. Not involved in endocytic recycling.
Subcellular location: Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:Q9P1Q0}. Membrane {ECO:0000250|UniProtKB:Q9JMK8}. Note=Associates with membranes in an EIPR1-independent manner. {ECO:0000250|UniProtKB:Q9JMK8}.
Interaction partners:
- Vacuolar protein sorting-associated protein 53 homolog
- Vacuolar protein sorting-associated protein 51 homolog
- Vacuolar protein sorting-associated protein 52 homolog
- EARP and GARP complex-interacting protein 1
- Syntaxin-16
- Syndetin
- Syntaxin-6
- Conserved oligomeric Golgi complex subunit 4
- Conserved oligomeric Golgi complex subunit 8
- Conserved oligomeric Golgi complex subunit 6
Sequence:
MASSHSSSPVPQGSSSDVFFKKEVDPTKHIRPVQSLPDVCPKEPTGDSHTLCVAPSLVTDQHRWTVYHSKVNLPAALNDPTLAKRESDFFTKTWGLDFVDTEVIPSLYLPQISKENFIAYQQEISQREKIHERCKNICPPKDTFDRTLLHIHDKSRTDLEQVPKIFMKPDFALDDSLTFNSVLPWSHFNTAGGKGSRDAASSKLLQEKLSHYLDIVEVNIAHQISLRSEAFFHAMTSQHELQDYLKKTTQAVKMLRDKIAQIDKVMCEGSLQILRLALTRNNCVKVYNKLKLMATVHQTQPTVQVLLSTSEFVGALDLIATTQEVLQQELQGIHSFRHLGSQLCELEKLIDKMMIAEFSTYSHSDLNRPLEGECQVLEEERLVSLVFGLLKQRKLNFLEIYGEEMIITAKNIIKERVINKVSQIEEIDTDVVVKLADQMRMLNFPQWIDLLKDIFSKFTVFLQRVKATLNIIHSVVLSVLEKSQRTRELEEIPQQRSAGKDSSLDTDVAYLTHEGWFISDAFSEGEPASAAVDTTSQRNTSPHSEPCSSDSVSEPECTTDSSSSKEQTSACAPPGGIEIIVSEDMRLTDLELGKLASNIQELLCNASDVCHDRAVKFLMSRAKDGFLEKLNSTEFIALSRLMETFIVDTEQICGRKSTSLLGALQSQANKFVNRFHEERRTKLSLLLDNERWKQADVPAEFQDLVDSIADGKIALPEKKPVVTEERKPADVLVVEGHQYAVVGTVLLLIRIILEYCQCVDNIPSVTTDMLTRLTDLLKYFNSRSCQLVLGAGALQVVGLKTITTKNLALSSRCLQLIVHYIPVIRAHFEARLPPKQWSMLRHFDHITKDYHDHIAEISAKLVAIMDSLFDKLLSKYEVKAPVPSPCFRNICKQMTKMHEAIFDLLPEEQTQMLFLRINASYKLHLKKQLSHLNVINDGGPQNGLVTADVAFYTGNLQALKGLKDLDLNMAEIWEQKR
Protein: Xyloglucan endotransglucosylase/hydrolase (EC 2.4.1.207) (B2KL33)
Organism: Gossypium hirsutum (Upland cotton) (Gossypium mexicanum)
Subcellular location: Secreted, cell wall {ECO:0000256|RuleBase:RU361120}. Secreted, extracellular space, apoplast {ECO:0000256|RuleBase:RU361120}.
Interaction partners:
Sequence:
MGMGLRNGFLLILSCVVTLSLSVWGRPATFLEDFRITWSDSHIRQIDGGRAIQLVLDQNSGCGFASKRQYLFGRVSMKIKLIPGDSAGTVTAFYMNSVTDAVRDELDFEFLGNRTGQPYTVQTNIYAHGKGDREQRVNLWFDPAADFHTYSIMWNHHQIVFYIDEVPIRVYKNNEARNIPYPKLQPMGVYSTLWEADDWATRGGLEKIDWTKAPFLAYYKDFDIEGCPVPGPVNCATNSRNWWEGTAYQALNAMEAKRYRWVRMNHVIYDYCTDKSRYPVTPPECMSII
Protein: Guanine nucleotide-binding protein alpha-1 subunit (GP1-alpha) (P27584)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Implicated in the mating and sporulation pathway. Probably coupled to mating-factor receptors. May act in concert with Ras1.
Interaction partners:
- Regulator of G-protein signaling 1
- Guanine nucleotide-binding protein subunit beta
- Guanine nucleotide-binding protein negative regulator 1
- Protein kinase byr2
- Pheromone P-factor receptor
- Mitogen-activated protein kinase spk1
- Ras-like protein 1
- Protein kinase byr1
- Adenylate cyclase
- Uncharacterized protein C16E9.15
Sequence:
MGCMSSKYADTSGGEVIQKKLSDTQTSNSSTTGSQNARVPVLENWLNIVLRGKPQNVESSGVRVKGNSTSGGNDIKVLLLGAGDSGKTTIMKQMRLLYSPGFSQVVRKQYRVMIFENIISSLCLLLEAMDNSNVSLLPENEKYRAVILRKHTSQPNEPFSPEIYEAVHALTLDTKLRTVQSCGTNLSLLDNFYYYQDHIDRIFDPQYIPSDQDILHCRIKTTGISEETFLLNRHHYRFFDVGGQRSERRKWIHCFENVTALLFLVSLAGYDQCLVEDNSGNQMQEALLLWDSICNSSWFSESAMILFLNKLDLFKRKVHISPIQKHFPDYQEVGSTPTFVQTQCPLADNAVRSGMYYFYLKFESLNRIASRSCYCHFTTATDTSLLQRVMVSVQDTIMSNNLQSLMF
Protein: HL08167p (Hyperkinetic, isoform D) (Hyperkinetic, isoform G) (Q9W2W9)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
Interaction partners:
Sequence:
MCRAPIASLDCMEEFSGTGGHLDFGRSISLGSNPALPLRHGSTPTPGLRYKNLGKSGLRISNVGLGTWPVFSPGVSDDQAEAILKLAIESGINLFDISEAHSETEIGKILQRAGWKRTAYVITTKVYWSTKSEERGLSRKHIIECVRASLQRLQLQYIDIVIIHKADPMCPMEVVRAMSYVIQQGWAMYWGTARWSQVEIMEAYTNCRQFNCITPIVEQSEYHMFCREKCELYLPEMYNKIGVGLMAWGPLSMALSDTQNGDKLFLPKGSFKTKSFSWTEDEINRNAALSPQGSWGKDRIDEGRRHCDRLRDLAALAEKLGCSPTQLSIAWSLKHEPVQCLLLGATSAEQLHQSLQSLQLLPRLSSSVMLELERILENKPVRPPMISTLALR
Protein: GH08870p (Genderblind, isoform A) (Genderblind, isoform B) (Genderblind, isoform C) (SD19826p) (Q9VB75)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- alpha-glucosidase
- Amino acid transporter protein JHI-21
- LD25378p
Sequence:
MPAADELQSPSSEMVLLTPSSGNPPSSIAQPAANPAEKAQCREGSAESDSSRVVIKKQLGLLEGVAIILGIIFGSGIFVSPKGVIREVESVGASLVIWVLCGLLSMIGALCYAELGTAIPKSGGDYAYIFEAYGSLPAFLYLWDAMMIFVPTTNAIMGLTFASYVLEPFFGGACEIPKIALQLLAAITICFLTYLNSYYMKVTTKMQNVIMFTKIAALVLIILVGLVWMMMGNVENFTRPFDNTETDPGKMSVAFYSGIFSYAGWNYLNFMTEELRDPYRNLPRAIYISLPLVTGIYVLANVAYLAVLSPSEMIASNAIAVTFGDKILGVFSLIIPLMVAISAFGGLSVHIMTSSRICFVGARNGHMPAILSHISVKSYTPLPSLVFLCFLSIVMLVVSDVYVLITYASIVESFFIMLSVSAVLYFRYTRPCMERPIKVAMWIPALFVIVCAFLVVVPIYVAPYEVGMGVLITIIGIPFYYVGVVWKNKPKWVQSTIDSVTFTCQKLFMSAKEEKED
Protein: Mechanosensory abnormality protein 6 (O01811)
Organism: Caenorhabditis elegans
Function: Subunit of an amiloride-sensitive cation channel (degenerin channel complex) permeable for sodium, potassium, lithium and N-methylglucamine, and required for mechanosensory transduction (touch sensitivity). Interacts with degenerin channel proteins and stabilizes the channel. Plays a role in mechanosensory transduction (touch sensitivity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:12478294}; Single-pass membrane protein {ECO:0000269|PubMed:12478294}. Cell projection, axon {ECO:0000269|PubMed:12478294}. Note=Co-localizes with mec-4 in puncta along the axons of touch cell receptor neurons and in muscles. {ECO:0000269|PubMed:12478294}.
Interaction partners:
- Degenerin mec-10
- Mechanosensory protein 2
- Degenerin mec-4
- Band 7 domain-containing protein
- Band 7 domain-containing protein
- MEC-5
- Kunitz/Bovine pancreatic trypsin inhibitor domain protein
- Papilin
- Tubulin alpha-3 chain
- Tubulin beta-1 chain
Sequence:
MGLQSAAAHFINRFIIWITIFMVACFLLRLLVVLDLNKRVYNHTPGPCRVLTDNYKGTAGMTYVESQKRVYITLGYGRAHDLKTKTGIAFYKTNRTDGRSQQEMYDLIEMTINWNGYEYKKEFIPTGIDSYSSSNGRVLLYVINAHPNHQCIHFFQIVESSKLNHRKAICDPSFSSLQDIAVVGPDRLFVTNMAAFGRGWAQILEFSLQTGQGAVYYYDGSKLSTAASSLIAPTGIGYDAKRRILYVGSMIRESIFAYKVAKDTTLELLYEMMLLTSPIGVFVESKTGDIWIAAHPVIHESAWHYTHPENQNIHSPSQILRIRIQEEGNSWVTTEPYANDGATISASSSVVFTDEQMLIGSSFGRLLHCDLTHSYIT
Protein: SNAP receptor-like protein (G0S236)
Organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719) (Thermochaetoides thermophila)
Interaction partners:
- Small conjugating protein ligase-like protein
- Synaptobrevin homolog YKT6
- Putative vesicle transport V-snare protein
- Vesicular-fusion protein sec17-like protein
- Protein transport protein SEC22
- V-SNARE coiled-coil homology domain-containing protein
- Probable vacuolar protein sorting-associated protein 16 homolog
- t-SNARE affecting a late Golgi compartment protein 1
- Golgi SNAP receptor complex member 1
- t-SNARE coiled-coil homology domain-containing protein
Sequence:
MSFDQLSSLEAGRRRGPTTSSRYTDDPEFARLSQDLMNKLFRLNGNNQRLAGEIGHLGTRRDTPRVRERVHELIEESRDMFKQVGEGVKKIQAWEDVTPTQRYMQQKLSREFQTSLAEFQSLQRQALEKQKASVSAARASFESEHHAPSATGAPEQHQLLQQQQELTHLAPQDEVDFQEALILEREEEIRNIEQGVSDLNVLFQQVAQLVAEQGEVLDTIERNVEAVGDDTRGADRELRAAARYQKRARSRMCCLLMILTVILTIILLAIFVG
Protein: Adenylate kinase, putative (EC 2.7.4.3) (Q57U69)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Adenylosuccinate lyase
- Adenosine kinase
- Adenosine kinase
- adenine phosphoribosyltransferase
- adenine phosphoribosyltransferase
- Pyruvate kinase
- Phosphodiesterase
Sequence:
MSTGQLSADAVKYLEEKRVTYLLEELFHDVLRNLPENPLEFLLKALERKTTLHLIIVGPPGSGKQTQARRIAKRYDAVHVRAQDIFLNEVKRRTPEGEIIERCMRDGEQVPSHISSELVIRRLREDDVVKRGWVLDGFPQTRSQALRLQTAGLSPLLFIMLDVGNEVSVKRCAGRRYEPITRNIYHIEYLPAPSGMHLELMSPDDESRAAVASRWKYFDARRGELVGCYEPMYVRIDGDRPFDTVFAEVCEQVDSRFVSV
Protein: Sorting nexin 2B (B9DFS6)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Plays a role in vesicular protein sorting. Acts at the crossroads between the secretory and endocytic pathways. Is involved in the endosome to vacuole protein transport and, as component of the membrane-associated retromer complex, is also involved in endosome-to-Golgi retrograde transport.
Subcellular location: Cytoplasm. Endosome membrane; Peripheral membrane protein; Cytoplasmic side. Prevacuolar compartment membrane; Peripheral membrane protein; Cytoplasmic side. Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein 35C
- Vacuolar protein sorting-associated protein 35A
- Vacuolar protein sorting-associated protein 35B
- Vacuolar protein sorting-associated protein 26B
- Vacuolar protein sorting-associated protein 26A
- Sorting nexin 2A
- Sorting nexin 1
- Biogenesis of lysosome-related organelles complex 1 subunit 1
- Biogenesis of lysosome-related organelles complex 1 subunit 2
Sequence:
MMGSENDEESHLHSSKEEMEKLFLREDGDPLTKSNVNGDKSNSNYRSAMSTLFDSRHPSIVVTPADSDPLFAPPSYYSESRSPRSKPNGGDRVSSYLEPPSYADVIFSPFDDISEINGSEDGHSQSSDSLSRSPSSLSSDYIKITVSNPQKEQEATNSMIPGGSTYITYQITTRTNLSDYGGSEFSVRRRFRDIVTLADRLAESYRGFCIPPRPDKSIVESQVMQKQEFVEQRRVALEKYLRRLVAHPVIRNSDELKVFLQAQGKLPLATSTDVASRMLDGAVKLPKQLFGEGGGASSVEVVQPGRGGRDFLRMFKELRQSVSNDWGGSKPPVVEEDKEFLEKKEKMYDLEQQIINASQQAESLVKAQQDMGETMGELGLAFIKLTKFENEEAVFNSQRARANDMKNLATSAVKASRFYRELNSQTVKHLDTLHDYLGLMMAVQGAFADRSSALLTVQTLLSELSSLEARAEKLEVASSKVFGGDKSRIKKIEELKETIKVTEDSKNVAIREYEQIKENNWSEVERLDRERRADFLNMMKGFVANQVGYAEKIANVWTKVAEETRQYDRESS
Protein: Cardiolipin synthase (CMP-forming) (CLS) (EC 2.7.8.41) (Protein GCD10 homolog) (Q9UJA2)
Organism: Homo sapiens (Human)
Function: Catalyzes the synthesis of cardiolipin (CL) (diphosphatidylglycerol) by specifically transferring a phosphatidyl group from CDP-diacylglycerol to phosphatidylglycerol (PG). CL is a key phospholipid in mitochondrial membranes and plays important roles in maintaining the functional integrity and dynamics of mitochondria under both optimal and stress conditions.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:16547353, ECO:0000305|PubMed:16547353}; Multi-pass membrane protein {ECO:0000269|PubMed:16547353}.
Interaction partners:
- Phosphatidate cytidylyltransferase 1
- Phosphatidate cytidylyltransferase 2
- CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase, mitochondrial
- Tafazzin
- Lysocardiolipin acyltransferase 1
- CDP-diacylglycerol--inositol 3-phosphatidyltransferase
- Acyl-CoA:lysophosphatidylglycerol acyltransferase 1
- Lysophosphatidylcholine acyltransferase 1
- Lysophosphatidylcholine acyltransferase 2
- Lysophospholipid acyltransferase LPCAT4
Sequence:
MLALRVARGSWGALRGAAWAPGTRPSKRRACWALLPPVPCCLGCLAERWRLRPAALGLRLPGIGQRNHCSGAGKAAPRPAAGAGAAAEAPGGQWGPASTPSLYENPWTIPNMLSMTRIGLAPVLGYLIIEEDFNIALGVFALAGLTDLLDGFIARNWANQRSALGSALDPLADKILISILYVSLTYADLIPVPLTYMIISRDVMLIAAVFYVRYRTLPTPRTLAKYFNPCYATARLKPTFISKVNTAVQLILVAASLAAPVFNYADSIYLQILWCFTAFTTAASAYSYYHYGRKTVQVIKD
Protein: Transcription factor MYB11 (Myb-related protein 11) (AtMYB11) (Protein PRODUCTION OF FLAVONOL GLYCOSIDES 2) (Q9LZK4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Modulates overall growth by reducing the proliferation activity of meristematic cells and delaying development. Flavonol-specific transcription activator involved in the regulation of several genes of flavonoid biosynthesis. Activates the expression of CHS, CHI, F3H and FLS1. Confers tolerance to UV-B.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00625}.
Interaction partners:
- Flavonol synthase/flavanone 3-hydroxylase
- Naringenin,2-oxoglutarate 3-dioxygenase
- Transcription factor TT8
- Dihydroflavonol 4-reductase
- Flavonoid 3'-monooxygenase
- Protein TRANSPARENT TESTA GLABRA 1
- Anthocyanidin 3-O-glucoside 2'''-O-xylosyltransferase
- Chalcone synthase
- Leucoanthocyanidin dioxygenase
- Transcription factor EGL1
Sequence:
MGRAPCCEKVGIKKGRWTAEEDRTLSDYIQSNGEGSWRSLPKNAGLKRCGKSCRLRWINYLRSDIKRGNITPEEEDVIVKLHSTLGTRWSTIASNLPGRTDNEIKNYWNSHLSRKLHGYFRKPTVANTVENAPPPPKRRPGRTSRSAMKPKFILNPKNHKTPNSFKANKSDIVLPTTTIENGEGDKEDALMVLSSSSLSGAEEPGLGPCGYGDDGDCNPSINGDDGALCLNDDIFDSCFLLDDSHAVHVSSCESNNVKNSEPYGGMSVGHKNIETMADDFVDWDFVWREGQTLWDEKEDLDSVLSRLLDGEEMESEIRQRDSNDFGEPLDIDEENKMAAWLLS
Protein: Protein NipSnap homolog 2 (NipSnap2) (Glioblastoma-amplified sequence) (O75323)
Organism: Homo sapiens (Human)
Function: May act as a positive regulator of L-type calcium channels.
Subcellular location: Mitochondrion matrix {ECO:0000269|PubMed:30982665}.
Interaction partners:
- Sequestosome-1
- Gamma-aminobutyric acid receptor-associated protein-like 2
- GABA type A receptor associated protein like 1
- Gamma-aminobutyric acid receptor-associated protein
- Next to BRCA1 gene 1 protein
- Protein NipSnap homolog 1
Sequence:
MAARVLRARGAAWAGGLLQRAAPCSLLPRLRTWTSSSNRSREDSWLKSLFVRKVDPRKDAHSNLLAKKETSNLYKLQFHNVKPECLEAYNKICQEVLPKIHEDKHYPCTLVGTWNTWYGEQDQAVHLWRYEGGYPALTEVMNKLRENKEFLEFRKARSDMLLSRKNQLLLEFSFWNEPVPRSGPNIYELRSYQLRPGTMIEWGNYWARAIRFRQDGNEAVGGFFSQIGQLYMVHHLWAYRDLQTREDIRNAAWHKHGWEELVYYTVPLIQEMESRIMIPLKTSPLQ
Protein: PAT complex subunit CCDC47 (Coiled-coil domain-containing protein 47) (Q8SZL8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Rough endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00034697}; Single-pass type I membrane protein {ECO:0000256|ARBA:ARBA00034697}.
Interaction partners:
Sequence:
MRPVFAFLLLALICFASTKSESDFEEDDSDDFAEFDDGNFYAEPAAKNADSFSGGAGSSHGESRDDPPAKEPRKQAQNQESDEEDGLVEDDDEFEHFQDEEEFEGYDGGDSKDPPIDQKVEPKLNIPNIPLHFRTHWDSYWMEMLMVAGLLAYFANFFAGKAKNARLAQLWFSTHRALLDENFALVGDDGKAENENPGLIKESESLYTLWCSGRTCCEGMLVELKMIKRQDLVSLVAGLMRPQLDQAHIKIELTRGVMDAFVFAVGTKKTITKLFKEYTDLSKFCSLVGKPEDRYNVPTGFGVPSEIPEATSAILESRIITALNKYQSYIDYLHISDQFSGPIQQEEGGTLKQPETKAVLLAGFNLPKHAEMETIKPLLLLIFYLMERLKTYRMSKEGKAKSDKNRQRVEEEFLKSTHAARAEAAAQRREDKRKQEKERILADEDPEKQRRWEAKEQKRQAKRNAPKMKRLAVKSL
Protein: Alanine--glyoxylate aminotransferase 2, mitochondrial (AGT 2) (EC 2.6.1.44) ((R)-3-amino-2-methylpropionate--pyruvate transaminase) (EC 2.6.1.40) (Beta-ALAAT II) (Beta-alanine-pyruvate aminotransferase) (EC 2.6.1.18) (D-3-aminoisobutyrate-pyruvate aminotransferase) (D-AIBAT) (D-beta-aminoisobutyrate-pyruvate aminotransferase) (Q64565)
Organism: Rattus norvegicus (Rat)
Function: Can metabolize asymmetric dimethylarginine (ADMA) via transamination to alpha-keto-delta-(NN-dimethylguanidino) valeric acid (DMGV). ADMA is a potent inhibitor of nitric-oxide (NO) synthase, and this activity provides mechanism through which the kidney regulates blood pressure (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:2123486, ECO:0000269|PubMed:2393662}.
Interaction partners:
- Alanine--glyoxylate aminotransferase
- D-amino-acid oxidase
- Alpha-aminoadipic semialdehyde dehydrogenase
- 4-aminobutyrate aminotransferase, mitochondrial
- Glycine amidinotransferase, mitochondrial
- Aldehyde dehydrogenase, mitochondrial
- 4-trimethylaminobutyraldehyde dehydrogenase
- 3-hydroxyisobutyrate dehydrogenase, mitochondrial
- Aldehyde dehydrogenase family 3 member A2
- Aldehyde dehydrogenase X, mitochondrial
Sequence:
MSLAWRTLQKAFYLETSLRILQMRPSLSCASRIYVPKLTLHTKHNMPPCDFSPEKYQSLAYNHVLEIHKQHLSPVNTAYFQKPLLLHQGHMEWLFDSEGNRYLDFFSGIVTVGVGHCHPKVTAVAKKQMDRLWHTSSVFFHSPMHEYAERLSALLPEPLKVIFLVNSGSEANDLAMVMARAYSNHTDIISFRGAYHGCSPYTLGLTNVGIYKMKVPSTIACQSTMCPDVFRGPWGGSHCRDSPVQTVRKCSCAPDGCQAKERYIEQFKDTLNTSVATSIAGFFAEPIQGVNGVVQYPKEFLKEAFALVRERGGVCIADEVQTGFGRLGSHFWGFQTHDTMPDIVTMAKGIGNGFPMAAVVTTPEIASSLAKHLHHFSTFGGSPLACAIGSAVLEVIEEENLQRNSQEVGTYMLLKFAKLRDEFDIVGDVRGKGLMVGIEMVQDKISRQPLPKTEVNQIHEDCKDMGLLVGRGGNFSQTFRIAPPMRVTKLEVDFAFEVFRSALTQHMERRAK