wanglab/gogpt-training-data huggingface dataset:
Protein: Nucleolar protein 56 (Q580Z5)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus, nucleolus {ECO:0000256|ARBA:ARBA00004604}.
Interaction partners:
- HEAT repeat-containing protein 1
- H/ACA ribonucleoprotein complex subunit 2
- BING4 C-terminal domain-containing protein
- Bms1-type G domain-containing protein
- KRR1 small subunit processome component
- Periodic tryptophan protein 2, putative
- Uncharacterized protein
- Nucleolar RNA binding protein, putative
- U3 small nucleolar ribonucleoprotein protein MPP10, putative
- DDB1- and CUL4-associated factor 13
Sequence:
MSKTLYLLYEGPTGYALFKVLTTEEIGAGDVALQKDLQTFATFSPWVKLLSFAPYQSPENALEDAVCINESIVSPFLNNFLTSVLSKKATKGEANWELGVSDPKLGSAIHDELKFAVLCNENVVEMCRCLRLHAEKLLPEHQEKDILRAQCGLGHAFSRNKVKFNVHRSDNMIIQSSALTEHMDKGVNLLGMRVKEWYGWHFPELAKEVPEPLKYSKVALLIGSRSTLEERDTEEVTQQIAEILEGDEALAARVYEKAVTSMGGDMAEVDWSNIRRFMKRVVSLGDYRESLQQYLVDKMMLVAPNLTELMGQNIGAKLISKAGSLTNLAKSPASTIQILGAEKALFRALKKRKGNTPKYGLIFHSTFIQRAAKEHRGKISRYLANKAALACRIDCFMDAPPQVFGEKLREQVEARLNFFDTGNKPPSNRVAMEEALEQYKKIIRRRAKKQRTAQSAEAEGEREEVSETPKQKRSRREVPQESA
Protein: ATP-binding cassette, sub-family C (CFTR/MRP), member 8 (ATP-binding cassette, sub-family C member 8) (B2RUS7)
Organism: Mus musculus (Mouse)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004370}.
Interaction partners:
- ATP-sensitive inward rectifier potassium channel 11
- ATP-sensitive inward rectifier potassium channel 8
- Rap guanine nucleotide exchange factor 4
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
- ATP-binding cassette sub-family C member 9
- Transient receptor potential cation channel subfamily M member 4
- Rap guanine nucleotide exchange factor 3
- Hexokinase-4
- Proton-coupled zinc antiporter SLC30A8
Sequence:
MPLAFCGTENHSAAYRVDQGVLNNGCFVDALNVVPHVFLLFITFPILFIGWGSQSSKVHIHHSTWLHFPGHNLRWILTFMLLFVLVCEIAEGILSDGVTESRHLHLYMPAGMAFMAAITSVVYYHNIETSNFPKLLIALLIYWTLAFITKTIKFVKFYDHAIGFSQLRFCLTGLLVILYGMLLLVEINVIRVRRYIFFKTPREVKPPEDLQDLGVRFLQPFVNLLSKGTYWWMNAFIKTAHRKPIDLRAIGKLPIAMRALTNYQRLCAAFDAQARKDTQSQQGARAIWRALCHAFGRRLVLSSTFRILADLLGFAGPLCIFGIVDHLGKENHVFQPKTQFLGVYFVSSQEFLGNAYVLAVLLFLALLLQRTFLQASYYVAIETGINLRGAIQTKIYNKIMHLSTSNLSMGEMTAGQICNLVAIDTNQLMWFFFLCPNLWAMPVQIIVGVILLYYILGVSALIGAAVIILLAPVQYFVATKLSQAQRSTLEYSNERLKQTNEMLRGIKLLKLYAWENIFCSRVEMTRRKEMTSLRAFAVYTSISIFMNTAIPIAAVLITFVGHVSFFKESDFSPSVAFASLSLFHILVTPLFLLSSVVRSTVKALVSVQKLSEFLSSAEIREEQCAPREPAPQGQAGKYQAVPLKVVNRKRPAREEVRDLLGPLQRLTPSMDGDADNFCVQIIGGFFTWTPDGIPTLSNITIRIPRGQLTMIVGQVGCGKSSLLLATLGEMQRVSGAVFWNSSLPDSEGEDPRYCLRTSNPERETAADSDARSRGPVAYASQKPWLLNATVEENITFESPFNKQRYKMVIEACSLQPDIDILPHGDQTQIGERGINLSGGQRQRISVARALYQHTNVVFLDDPFSALDVHLSDHLMQAGILELLRDDKRTVVLVTHKLQYLPHADWIIAMKDGTIQREGTLKDFQRSECQLFEHWKTLMNRQDQELEKETVMERKAPEPSQGLPRAMSSRDGLLLDEDEEEEEAAESEEDDNLSSVLHQRAKIPWRACTKYLSSAGVLLLSLLVFSQLLKHMVLVAIDYWLAKWTDSALVLSPAARNCSLSQECALDQSVYAMVFTVLCSLGIALCLVTSVTVEWTGLKVAKRLHRSLLNRIILAPMRFFETTPLGSILNRFSSDCNTIDQHIPSTLECLSRSTLLCVSALTVISYVTPVFLVALLPLAVVCYFIQKYFRVASRDLQQLDDTTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNNIASLFLTAANRWLEVRMEYIGACVVLIAAATSISNSLHRELSAGLVGLGLTYALMVSNYLNWMVRNLADMEIQLGAVKRIHTLLKTEAESYEGLLAPSLIPKNWPDQGKIQIQNLSVRYDSSLKPVLKHVNALIAPGQKIGICGRTGSGKSSFSLAFFRMVDMFEGRIIIDGIDIAKLPLHTLRSRLSIILQDPVLFSGTIRFNLDPEKKCSDSTLWEALEIAQLKLVVKALPGGLDAIITEGGENFSQGQRQLFCLARAFVRKTSIFIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVHTILSADLVMVLKRGAILEFDKPEKLLSQKDSVFASFVRADK
Protein: Hydroxyacid-oxoacid transhydrogenase, mitochondrial (HOT) (EC 1.1.99.24) (Alcohol dehydrogenase iron-containing protein 1) (ADHFe1) (Q8R0N6)
Organism: Mus musculus (Mouse)
Function: Catalyzes the cofactor-independent reversible oxidation of gamma-hydroxybutyrate (GHB) to succinic semialdehyde (SSA) coupled to reduction of 2-ketoglutarate (2-KG) to D-2-hydroxyglutarate (D-2-HG). L-3-hydroxybutyrate (L-3-OHB) is also a substrate for HOT when using 2-KG as hydrogen acceptor, resulting in the formation of D-2-HG (By similarity).
Subcellular location: Mitochondrion {ECO:0000269|PubMed:17559793}.
Interaction partners:
- Methylmalonate-semialdehyde/malonate-semialdehyde dehydrogenase [acylating], mitochondrial
- 3-hydroxyisobutyryl-CoA hydrolase, mitochondrial
- All-trans-retinol dehydrogenase [NAD
- All-trans-retinol dehydrogenase [NAD
- Alcohol dehydrogenase 6A
- Alcohol dehydrogenase 1
- L-2-hydroxyglutarate dehydrogenase, mitochondrial
- Alcohol dehydrogenase class-3
Sequence:
MAAAARARVTHLLRHLQSTACQCPTHSHTYSQAPGPSGKTADYAFEMAVSNIRYGAGVTKEVGMDLQNMGAKNVCLMTDKNLSQLPPVQIVMDSLSKNGISFQVYDDVRVEPTDGSFMDAIEFAKKGAFDAYVAVGGGSTMDTCKAANLYASSPHSEFLDYVNAPIGKGKPVTVPLKPLIAVPTTSGTGSETTGVAIFDYEHLKVKTGIASRAIKPTLGLVDPLHTLHMPCQVVANSGFDVLCHALESYTAIPYSMRSPCPSNPIQRPAYQGSNPISDIWAVHALQIVAKYLKRAVRNPDDLEARSKMHLASAFAGIGFGNAGVHLCHGMSYPISGLVKTYKAKEYNVDHPLVPHGLSVVLTSPAVFTFTAQMFPERHLETAGILGANIRTARIQDAGLVLADALRKFLFDLNVDDGLAALGYSKDDIPSLVKGTLPQERVTKLAPRAQSEEDLSALFEASMKLY
Protein: Vacuolar protein sorting-associated protein 17 (Q9URW7)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Plays a role in vesicular protein sorting. Required for the endosome-to-Golgi retrieval of the vacuolar protein sorting receptor pep1/vps10. Component of the membrane-associated retromer complex which is essential in endosome-to-Golgi retrograde transport. The vps29-vps26-vps35 subcomplex may be involved in cargo selection.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Vacuolar protein sorting-associated protein 29
- Vacuolar protein sorting-associated protein vps5
- Vacuolar protein sorting-associated protein 35
- Vacuolar protein sorting-associated protein 26
- Sorting nexin-3
- Vacuolar protein sorting/targeting protein 10
- Sorting nexin-4
Sequence:
MSSQHSTDDLMNSHVFSGGFSTLDDKGFQDVPIHTDMPGSISVEPSSEDANVGSVNGNINETPVFEADRLIAEATMNPSAASSTTGENSISQTGSGPFLRIRIVDIEAENSKDPVIKMNVQTTLPAYRSKLYKNVRRTHAEFKKFAKYLISTHPECLIPAVPEAKTSVSSGIKEDLIYLKSGLQSWLNYVSTNPNLLYDPELQLFVESDYGYSPLINTGNPTSGLKRKALKQFPLPPDPCQALANLRPIVKSFYKNAKDAEIKLEKLVNRKQSLALTHADLGQSLIDYSVEEQHNGLANALNRVGKMLQAISDVRIMQSSKQLVTLADSLCYASDNAFVVKEILSNRHILMRDLISSKNQTNSYLSAANRLQDSPKISKARTDDALQALEVARVHEKLLSDKVDFVTLNLVKESKTYTKKTSVSLQKAIREYVEKEAYYERRLLSIMESIRPHIRNIDPFGGLSRLGREEYPRRLSNPPPSQKTNQDAWTNRKRPGYSSSFDGSSQSTFNPSNNDGAHNTSENADELVEPPIGNERLDPKSVANLLNAI
Protein: Ribosome-recycling factor, mitochondrial (RRF) (Ribosome-releasing factor, mitochondrial) (P38771)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Necessary for protein synthesis in mitochondria. Functions as a ribosome recycling factor in mitochondria.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:12853640}.
Interaction partners:
- Large ribosomal subunit protein bL17m
- Small ribosomal subunit protein uS2m
- Small ribosomal subunit protein uS9m
- Small ribosomal subunit protein bS6m
- Large ribosomal subunit protein bL32m
- Small ribosomal subunit protein bS16m
- Large ribosomal subunit protein bL19m
- Large ribosomal subunit protein uL23
- Large ribosomal subunit protein bL27m
- Large ribosomal subunit protein uL18
Sequence:
MILTTARLNCRPVTVPRLFNRSFSQSFIILKKKSSTPTEKVEEDEIDVNELLKKAETQFKKTLEIQKQKMNEIKQGNFNPKVFNSLVFKNNRKFTDIATTSLKGKNALLITVFDPKDVKTVISGVLAANLNLTPERVPNNDLQLKVSLPPPTTESRLKVAKDLKRVFEEYKQSSLKDSLGTIRGSILKEFKSFKKDDAVRKAERDLEKLHKDYVNKLHDQFQKVEKSIVK
Protein: Glucose transporter, putative (Q584F8)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MIEGSRNSSAVKKRLVAKPLEECAPLNLLGAEDVMGALHTSSVSFFTWGILQTVIVHCFAGALFGYGIGFVGPYYTLYKMGSDCMTVTTQSTCPMFIPEKCTWKDNACKFVVDNCSGQLKEACGASSSSSVSQTCYWNHKTNVCQPMAGFTALQNGIFAGAFIFGGCIGSLISAPLLSVSGHRITFLLCGFVGTVGGALTHFATYTDSYMLLVAGRFLTGVSAGVLCVSSPAYVEETAPIQHRQLVGVFFQIACTFGILSASAMGLGLAQRSFSTQHDMQQRQQMFCLPGTIIALLMMFISGPMRESVVWMEQRHLSRPGEQDDLVTFAEGRVSYGTVISSDPKPGWGGVKGQLLTALVLCIAQQLTGMNAIMNYAPIITDRMGLEPLFGNFVVMAWNFITVLTSIPISSRAHADRAYVVALLLASLSCLLVAVAVLPFFGFSSNLKVKLSATGILLFITFFELGMGSFFWTLSQGIFPPNFRHRGSSFTVLVHFLINIVINVGFPLAVEWLSGGPSGNQDVGMGIAFLFFGIVGLLSTAYLHRHLRLWQSS
Protein: Mannosyl-oligosaccharide glucosidase (EC 3.2.1.106) (Glucosidase I) (A0A3B3IRW2)
Organism: Homo sapiens (Human)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU369107}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004648, ECO:0000256|RuleBase:RU369107}.
Interaction partners:
Sequence:
MVKSRLNSWFQHRPPGAPPERYLGLPGSLKWEDRGPSGQGQGQFLIQQVTLKIPISIEFVFESGSAQAGGNQALPRLAGSLLTQALESHAEGFRERFEKTFQLKEKGLSSGEQVLGQAALSGLLGGIGYFYGQGLVLPDIGVEGSEQKVDPALFPPVPLFTAVPSRSFFPRGFLWDEGFHQLVVQRWDPSLTREALGHWLGLLNADGWIGREQILGDEARARVPPEFLVQRAVHANPPTLLLPVAHMLEVGDPDDLAFLRKALPRLHAWFSWLHQSQAGPLPLSYRWRGRDPALPTLLNPKTLPSGLDDYPRASHPSVTERHLDLRCWVALGARVLTRLAEHLGEAEVAAELGPLAASLEAAESLDELHWAPELGVFADFGNHTKAVQLKPRPPQGLVRVVGRPQPQLQYVDALGYVSLFPLLLRLLDPTSSRLGPLLDILADSRHLWSPFGLRSLAASSSFYGQRNSEHDPPYWRGAVWLNVNYLALGALHHYGHLEGPHQARAAKLHGELRANVVGNVWRQYQATGFLWEQYSDRDGRGMGCRPFHGWTSLVLLAMAEDY
Protein: Solute carrier family 25, member 27 (A0A8I6ALR4)
Organism: Rattus norvegicus (Rat)
Subcellular location: Mitochondrion inner membrane {ECO:0000256|ARBA:ARBA00004448}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004448}.
Interaction partners:
Sequence:
MILEGFVGLSECFGGFPPLRLFSISLATFPLDLTKTRLQMQGEAALAKLGDGAMESAPYRGMMRTALGIVQEEGFLKLWQGVTPAIYRHVVYSGGRMVTYEHLREVVFGKSEDEHYPLWKSVIGGMMAGVIGQFLANPTDLVKVQMQMEGKRRLEGKPLRFRGVHHAFAKILAEGGIRGLWAGWIPNIQRAALVNMGDLTTYDTVKHYLVLNTALEDNIATHGLSSLCSGLVASILGTPADVIKSRIMNQPRDKQGRGLLYKSSTDCVIQAVQGEGFLSLYKGFLPSWLRMEDTLLHRDCDLQGATLYPSLETGVLSDSSFYLRAICLVQSHETNH
Protein: Aldehyde dehydrogenase family 3 member B3 (EC 1.2.1.3) (J3QMK6)
Organism: Mus musculus (Mouse)
Function: Oxidizes medium and long chain aldehydes into non-toxic fatty acids.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25286108}; Lipid-anchor {ECO:0000305|PubMed:25286108}.
Interaction partners:
- All-trans-retinol dehydrogenase [NAD
- Aldo-keto reductase family 1 member A1
- Alcohol dehydrogenase class-3
- All-trans-retinol dehydrogenase [NAD
- Alcohol dehydrogenase 1
- Acetyl-coenzyme A synthetase, cytoplasmic
- Acetyl-coenzyme A synthetase 2-like, mitochondrial
- 4-aminobutyrate aminotransferase, mitochondrial
- Catechol O-methyltransferase
- Amine oxidase [flavin-containing] B
Sequence:
MSTKGKHPRADQGTDPFEEKLQRLKEAFNTGKTKTAKFRAEQLQSLGRFLQDNSKQLHDALDGDLGKSGFESDMSEIILCENEVDLALKNLQTWMKDEPVSTNLLTKLSTAFIRKEPFGLVLIIAPWNYPVNLMIIPLVGAIAAGNCVVLKPSEISKNTEKVLAELLPQYLDQSCFAVMLGGPEETGQLLEHKFDYIFFTGSPRVGKIVMTAAAKHLTPITLELGGKNPCYVDDNCDPQTVANRVAWFRYFNAGQTCVAPDYILCSQEMQEQLVPALQNAITRFYGDNPQTSPNLGRIINQKHFKRLQGLLGCGRVAIGGQSDEGERYIAPTVLVDVQETEPVMQEEIFGPILPLVTVRSLDEAIEFMNQREKPLALYAYSNNAEVIKQVLARTSSGGFCGNDGFMYMTLSSLPFGGVGSSGMGRYHGKFSFDTFSNQRACLLSCPGMEKLNGLRYPPYSPRRQQLLRWAIGSESCTLL
Protein: WD repeat-containing protein 36 (T-cell activation WD repeat-containing protein) (TA-WDRP) (Q8NI36)
Organism: Homo sapiens (Human)
Function: Involved in the nucleolar processing of SSU 18S rRNA. Involved in T-cell activation and highly coregulated with IL2.
Subcellular location: Nucleus, nucleolus {ECO:0000269|PubMed:21051332, ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:34516797}.
Interaction partners:
- U3 small nucleolar RNA-associated protein 15 homolog
- WD repeat-containing protein 75
- U3 small nucleolar RNA-associated protein 4 homolog
- HEAT repeat-containing protein 1
- U3 small nucleolar RNA-associated protein 6 homolog
- Nucleolar protein 56
- DDB1- and CUL4-associated factor 13
- Bystin
- Neuroguidin
- KRR1 small subunit processome component homolog
Sequence:
MCCTEGSLRKRDSQRAPEAVLCLQLWQRTVPLDTLKGLGTCFPSGPELRGAGIAAAMERASERRTASALFAGFRALGLFSNDIPHVVRFSALKRRFYVTTCVGKSFHTYDVQKLSLVAVSNSVPQDICCMAADGRLVFAAYGNVFSAFARNKEIVHTFKGHKAEIHFLQPFGDHIISVDTDGILIIWHIYSEEEYLQLTFDKSVFKISAILHPSTYLNKILLGSEQGSLQLWNVKSNKLLYTFPGWKVGVTALQQAPAVDVVAIGLMSGQVIIHNIKFNETLMKFRQDWGPITSISFRTDGHPVMAAGSPCGHIGLWDLEDKKLINQMRNAHSTAIAGLTFLHREPLLVTNGADNALRIWIFDGPTGEGRLLRFRMGHSAPLTNIRYYGQNGQQILSASQDGTLQSFSTVHEKFNKSLGHGLINKKRVKRKGLQNTMSVRLPPITKFAAEEARESDWDGIIACHQGKLSCSTWNYQKSTIGAYFLKPKELKKDDITATAVDITSCGNFAVIGLSSGTVDVYNMQSGIHRGSFGKDQAHKGSVRGVAVDGLNQLTVTTGSEGLLKFWNFKNKILIHSVSLSSSPNIMLLHRDSGILGLALDDFSISVLDIETRKIVREFSGHQGQINDMAFSPDGRWLISAAMDCSIRTWDLPSGCLIDCFLLDSAPLNVSMSPTGDFLATSHVDHLGIYLWSNISLYSVVSLRPLPADYVPSIVMLPGTCQTQDVEVSEETVEPSDELIEYDSPEQLNEQLVTLSLLPESRWKNLLNLDVIKKKNKPKEPPKVPKSAPFFIPTIPGLVPRYAAPEQNNDPQQSKVVNLGVLAQKSDFCLKLEEGLVNNKYDTALNLLKESGPSGIETELRSLSPDCGGSIEVMQSFLKMIGMMLDRKRDFELAQAYLALFLKLHLKMLPSEPVLLEEITNLSSQVEENWTHLQSLFNQSMCILNYLKSALL
Protein: Diacylglycerol kinase beta (DAG kinase beta) (EC 2.7.1.107) (90 kDa diacylglycerol kinase) (Diglyceride kinase beta) (DGK-beta) (P49621)
Organism: Rattus norvegicus (Rat)
Function: Diacylglycerol kinase that converts diacylglycerol/DAG into phosphatidic acid/phosphatidate/PA and regulates the respective levels of these two bioactive lipids. Thereby, acts as a central switch between the signaling pathways activated by these second messengers with different cellular targets and opposite effects in numerous biological processes (Probable). Has a higher activity with long-chain diacylglycerols like 1,2-di-(9Z-octadecenoyl)-sn-glycerol compared to 1,2-didecanoyl-sn-glycerol. Specifically expressed in brain, it regulates neuron-specific morphological changes including neurite branching and neurite spine formation (By similarity).
Subcellular location: Postsynaptic cell membrane {ECO:0000305|PubMed:7689223}; Peripheral membrane protein {ECO:0000305|PubMed:7689223}. Cell membrane {ECO:0000305|PubMed:7689223}; Peripheral membrane protein {ECO:0000305|PubMed:7689223}. Cytoplasm {ECO:0000305|PubMed:7689223}. Note=Translocation to the plasma membrane is induced by phorbol esters. {ECO:0000250|UniProtKB:Q9Y6T7}.
Interaction partners:
- Lipoprotein lipase
- Glycerol-3-phosphate dehydrogenase, mitochondrial
- Dihydroxyacetone phosphate acyltransferase
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase epsilon-1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Phospholipase D2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase gamma-2
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3
- 1-acyl-sn-glycerol-3-phosphate acyltransferase
Sequence:
MTNQEKWAHLSPSEFSQLQKYAEYSTKKLKDVLEEFHGNGVLAKYNPEGKQDILNQTIDFEGFKLFMKTFLEAELPDDFTAHLFMSFSNKFPHSSPNVKSKPALLSGGLRMNKGAITPPRSSPANTCFPEVIHLKDIVCYLSLLERGRPEDKLEFMFRLYDTDGNGFLDSSELENIIGQMMHVAEYLEWDVTELNPILHEMMEEIDYDRDGTVSLEEWIQGGMTTIPLLVLLGLENNVKDDGQHVWRLKHFNKPAYCNLCLNMLIGVGKQGLCCSFCKYTVHERCARAPPSCIKTYVKSKKNTDVMHHYWVEGNCPTKCDKCHKTVKCYQGLTGLHCVWCQTTLHNKCASHLKPECDCGPLKDHILPPTTICPVVLTMPTAGTSVPEERQSTAKKEKGSSQQPNKVTDKNKMQRANSVTMDGQGLQITPIPGTHPLLVFVNPKSGGKQGERIYRKFQYLLNPRQVYSLSGNGPMPGLHFFRDVPDFRVLACGGDGTVGWILDCIEKANVVKHPPVAILPLGTGNDLARCLRWGGGYEGENLMKILKDIESSTEIMLDRWKFEVTPNDKDEKGDPVPYSIINNYFSIGVDASIAHRFHIMREKHPEKFNSRMKNKFWYFEFGTSETFSATCKKLHESVEIECDGVQIDLINISLQGIAILNIPSMHGGSNLWGESKKKRSHRRIEKKGSDKRPTLTDAKELKFASQDLSDQLLEVVGLEGAMEMGQIYTGLKSAGRRLAQCSSVVIRTSKSLPMQIDGEPWMQTPCTIKITHKNQAPMLMGPPPKTGLFCSLIKRTRNRSKE
Protein: Alpha/beta hydrolase domain-containing protein 17C (Abhydrolase domain-containing protein 17C) (EC 3.1.2.22) (B5DFK7)
Organism: Rattus norvegicus (Rat)
Function: Hydrolyzes fatty acids from S-acylated cysteine residues in proteins. Has depalmitoylating activity towards DLG4/PSD95.
Subcellular location: Recycling endosome membrane {ECO:0000269|PubMed:27307232}; Lipid-anchor {ECO:0000269|PubMed:27307232}; Cytoplasmic side {ECO:0000269|PubMed:27307232}. Cell projection, dendritic spine {ECO:0000269|PubMed:27307232}. Postsynaptic density membrane {ECO:0000269|PubMed:27307232}.
Interaction partners:
- Acyl-protein thioesterase 1
- GTPase NRas
Sequence:
MPEPGPRMNGFSLGELCWLFCCPPCPSRIAAKLAFLPPEPTYTVLAPEQRAPAPAATPAPAPAAQPAPAEEGAGPGACSLHLSERADWQYSQRELDAVEVFFSRTARDNRLGCMFVRCAPSSRYTLLFSHGNAVDLGQMCSFYIGLGSRINCNIFSYDYSGYGVSSGKPSEKNLYADIDAAWQALRTRYGVSPENIILYGQSIGTVPTVDLASRYECAAVILHSPLMSGLRVAFPDTRKTYCFDAFPSIDKISKVTSPVLVIHGTEDEVIDFSHGLAMYERCPRAVEPLWVEGAGHNDIELYAQYLERLKQFISHELPNS
Protein: Kune-kune (SD14923p1) (A1Z6H0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Neurexin-4
- Contactin
- Lachesin
- LD42595p
- UPAR/Ly6 domain-containing protein crim
- UPAR/Ly6 domain-containing protein crok
- Neuroglian
- GH16267p
- Parkin coregulated gene protein homolog
Sequence:
MGASNRILQVALCASVFSLICFVIAFSTPYWLVTDGRLQNPRFTNLGLWEVCFNNFQDIHRFFDNSFNGCLWVFEEEYYIIHDFLLPGFYISVQLFATLCFVMCLVVIPLTVAFLRTSRDDDRYMVLLLAIGSCQVVGSVFGFIAVVIFGAKGDSRDWMPGWQNNDMGWSFALGVVGAVLLLPSGVLYLVEARRERYKRLNEISNREISEYGDEYYQNQGPSAVLPTAPSPYQSYFASEPSRPRRPQQSSASNSAVQGGIQTDI
Protein: G protein-activated inward rectifier potassium channel 3 (GIRK-3) (Inward rectifier K(+) channel Kir3.3) (Potassium channel, inwardly rectifying subfamily J member 9) (Q92806)
Organism: Homo sapiens (Human)
Function: This receptor is controlled by G proteins. Inward rectifier potassium channels are characterized by a greater tendency to allow potassium to flow into the cell rather than out of it. Their voltage dependence is regulated by the concentration of extracellular potassium; as external potassium is raised, the voltage range of the channel opening shifts to more positive voltages. The inward rectification is mainly due to the blockage of outward current by internal magnesium (By similarity).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- G protein-activated inward rectifier potassium channel 2
- G protein-activated inward rectifier potassium channel 1
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid type B receptor subunit 1
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- G protein-activated inward rectifier potassium channel 4
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase catalytic subunit alpha
Sequence:
MAQENAAFSPGQEEPPRRRGRQRYVEKDGRCNVQQGNVRETYRYLTDLFTTLVDLQWRLSLLFFVLAYALTWLFFGAIWWLIAYGRGDLEHLEDTAWTPCVNNLNGFVAAFLFSIETETTIGYGHRVITDQCPEGIVLLLLQAILGSMVNAFMVGCMFVKISQPNKRAATLVFSSHAVVSLRDGRLCLMFRVGDLRSSHIVEASIRAKLIRSRQTLEGEFIPLHQTDLSVGFDTGDDRLFLVSPLVISHEIDAASPFWEASRRALERDDFEIVVILEGMVEATGMTCQARSSYLVDEVLWGHRFTSVLTLEDGFYEVDYASFHETFEVPTPSCSARELAEAAARLDAHLYWSIPSRLDEKVEEEGAGEGAGGEAGADKEQNGCLPPPESESKV
Protein: Palmitoyltransferase (EC 2.3.1.225) (Q9VKN8)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MVFIRDPCGIACLVVTYGAVLYADYVVIRWIILTTMPGSLWMSFHVVLFNTVVFLLAMSHSKAVFSDPGTVPLPANRLDFSDLHTTNKNNPPPGNGHSSEWTVCTRCETYRPPRAHHCRICKRCIRRMDHHCPWINNCVGERNQKYFLQFLIYVALLSLYSIALIVGSWVWPCEECSQNVIETQLRMIHSVILMLVSALFGLFVTAIMVDQLHAILYDETAVEAIQQKGTYRPNRRKYQLLADVFGRGHPALWLLPCTSLNHASRYHDTPLLSHEV
Protein: Derlin (Q4WDG5)
Organism: Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata)
Subcellular location: Endoplasmic reticulum membrane {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363059}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004477, ECO:0000256|RuleBase:RU363059}.
Interaction partners:
- Ubiquitin-protein ligase Sel1/Ubx2, putative
- RING-type E3 ubiquitin transferase
- Protein OS-9 homolog
- Cell division control protein Cdc48
- Nuclear protein localization protein 4
- Ubiquitin fusion degradation protein 1
- Endoplasmic reticulum-Golgi intermediate compartment protein
- UBX domain protein, putative
- Protein png1
- SH3 domain protein
Sequence:
MAAIWGNGGQGGQFPLEQWFYEMPPVTRWWTVATVATSVLVQCHILTPFQLFYSFRAVYFKSQYWRLLTTFLYFGPLNLDLLFHVFFLQRYSRLLEESSGRSPAHFSWLLFYAMTSLLLISPFLSLPFLGTALSSSLVYIWSRRNPDTRLSFLGILVFTAPYLPWVLMAFSLVVHGIVPKDEICGIVVGHIWYFFNDVYPSLHGGHRPLDPPRWWRRIFDPRAAAGEAQRTDTDNVNRDFAAAAAPEVR
Protein: VOC domain-containing protein (Q9A2Y2)
Organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15) (Caulobacter crescentus)
Interaction partners:
Sequence:
MREDGKIDYIEWPGGDLPATKAFYSAAFGWTFADYGPDYVAFEGQGTDGGFAKPQEGSSDRPLVILYAHDLEAMLDKVTAAGGVITAPIFSFPGGRRFHFTDPSGNELGVWSATGVE
Protein: H(+)-exporting diphosphatase (EC 7.1.3.1) (Q8IKR1)
Organism: Plasmodium falciparum (isolate 3D7)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004127}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004127}.
Interaction partners:
Sequence:
MDLFYVFLFLPPTIGLIFSIIECIWVSNINIKGPEDKVEKLEDGDNPVEKMKEIASYIAVGANAFLKKEFQYLAVFIIVFSILLGFFVNSFTAVSFVLGCLTSILCGYIGMKIAVYANVRTTNETWKSLDKGFQVTLNAGTVMGFSLVSFGIIALGLLIFVYKTYVFKNTIPDNQIYKIIAGFGLGGSSIALFSRVGGGIYTKAADVGADLSGKNEYGIPEDDIRNPACIADNVGDNVGDMAGMGADLFGSLAESLCAALVIGSSVISIGEGSPGNAFHCILFPLLFVSFSVICSMITFYIITYSVKINDKKDVEKSLKYLLLLSTVLQSLAILAIGYVCFPSLVKYNYLKDIHRWKIIVPALVGLWSGLIIGFTTEFYTSYSFSPVQEIAHTQKVSAATGIIYGLSLGYKSTFIPIICLSATLGISYGLCDIYGIALAAVGMLSTLCICLTIDAYGPISDNAGGIAEMAGLPSEVRERTDILDAAGNTTAAIGKGFAIGSAALVAFALFGAYASSANLRHVNILNSWVIIGLLIGAMLPYLFSALTMKSVAIAANSVLNECLEQFPLILEGKQKPDYEKCIKISTDASLRQMIVPGLISVFSPLIIGMLMGKYATAGLLIGIILSGIQLAFSSTNSGGAWDNAKKYIESGALGKEHCKGSNAHKNSVIGDTVGDPLKDTSGPSLNILIKLSAITSLVFANVIATKFTSTRGGPIWL
Protein: Dynein light chain (Q4W5W8)
Organism: Vicia faba (Broad bean) (Faba vulgaris)
Interaction partners:
Sequence:
MAHRSSRRRNTAPPESTPPTAPAAPTIPAKQPRPTIFSPSPSHYTKANSDLIQATKSSFLVKPFQSLNLGSKKTKHSQTKHVDSRLHTKSMTTSAIFESSKPNKTHNTKNIVLTPKLEKESIFLTSKKTHKEKPLKPGSELERWKLQGLLKNEKKESCKGCVVEDVKDEKSRKLAVVEEGDVVKERVSVSMGQSGGGGGGGRRKSLCGSMVDLGDFFAINGAKMVSADMPPFMQIHAVDCARKAFDSMEKFTSKTLASSLKKEFDGVYGPAWHCIVGTSFGSFVTHSVGGFLYFSMDQKLYILLFKTAVQKAD
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (EC 3.1.4.11) (PLC-154) (Phosphoinositide phospholipase C-beta-1) (Phospholipase C-beta-1) (PLC-beta-1) (P10894)
Organism: Bos taurus (Bovine)
Function: Catalyzes the hydrolysis of 1-phosphatidylinositol 4,5-bisphosphate into diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) and mediates intracellular signaling downstream of G protein-coupled receptors. Regulates the function of the endothelial barrier.
Subcellular location: Nucleus membrane {ECO:0000250|UniProtKB:Q9Z1B3}. Cytoplasm {ECO:0000250|UniProtKB:P10687}. Note=Colocalizes with the adrenergic receptors, ADREN1A and ADREN1B, at the nuclear membrane of cardiac myocytes. {ECO:0000250|UniProtKB:Q9Z1B3}.
Interaction partners:
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein subunit alpha-14
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Protein kinase C alpha type
- Guanine nucleotide binding protein
- Guanine nucleotide-binding protein subunit alpha
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-4
- Inositol polyphosphate 1-phosphatase
- cGMP-dependent protein kinase 1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
Sequence:
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWEDDSTVVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGKHAKAPKDPKLRELLDVGNIGRLEHRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLAKKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLDKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSVFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKKRNRSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTVDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPIWEEEPIVFKKVVLPSLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLMLPALFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETPSEAPSEARPTPAENGVNHTTSLTPKPPSQALHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYLRRRAALEKTAKKDNKKKSEPSSPDHVSSTIEQDLAALDAEMTQKLVDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKPKLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHSSAPPLMTSDSGKLNQKPPSSEELEGENPGKEFDTPL