wanglab/gogpt-training-data huggingface dataset:
Protein: U2 small nuclear ribonucleoprotein auxiliary factor 35 kDa subunit-related protein 2 (CCCH type zinc finger, RNA-binding motif and serine/arginine rich protein 2) (U2(RNU2) small nuclear RNA auxiliary factor 1-like 2) (U2AF35-related protein) (URP) (Q62377)
Organism: Mus musculus (Mouse)
Function: Pre-mRNA-binding protein required for splicing of both U2- and U12-type introns. Selectively interacts with the 3'-splice site of U2- and U12-type pre-mRNAs and promotes different steps in U2 and U12 intron splicing. Recruited to U12 pre-mRNAs in an ATP-dependent manner and is required for assembly of the prespliceosome, a precursor to other spliceosomal complexes. For U2-type introns, it is selectively and specifically required for the second step of splicing (By similarity).
Subcellular location: Nucleus {ECO:0000250}.
Interaction partners:
- Splicing factor U2AF 65 kDa subunit
- Serine/arginine-rich splicing factor 2
- Serine/arginine-rich splicing factor 1
- Splicing factor 3B subunit 1
- Serine/arginine-rich splicing factor 7
- Splicing factor U2AF 35 kDa subunit
- PHD finger-like domain-containing protein 5A
- RNA-binding region-containing protein 3
- U11/U12 small nuclear ribonucleoprotein 48 kDa protein
- Splicing factor 3B subunit 3
Sequence:
METAGATADATAGPQKLSRKKYLALRKKERRKRRRQALARLREAELAQKEEEEDPLAEEKRLEEERLLEEERQRLHEEWLLREEKAQEEFRAKKKKEEEARKRKEELERKLKAEWEEQQRKEREEEEQKRQEKREREEAVQKMLDQAENELENGGTWQNPEPPMDIRVLEKDRANCPFYSKTGACRFGDRCSRKHNFPTSSPTLLIKGMFTTFGMEQCRRDDYDPDSSLEFSEEEIYQQFLDFYYDVLPEFKSVGKVIQFKVSCNLEPHLRGNVYVQYQSEEDCQAAFSVFNGRWYAGRQLQCEFCPVTRWKMAICGLFEVQQCPRGKHCNFLHVFRNPNNEYRDANRDLYPSPDWTSSSFGKNSERRERASHYDEYYGRSRRRRRSPSPDFYKRNGESDRKSSSRHRVKKSHRYGMKSRERRSSPSRRRKDHSPGPWEPEQEEPPQQESQSQPQPQPQSDP
Protein: A-kinase anchor protein 14 (AKAP-14) (A-kinase anchor protein 28 kDa) (AKAP 28) (Protein kinase A-anchoring protein 14) (PRKA14) (Q86UN6)
Organism: Homo sapiens (Human)
Function: Binds to type II regulatory subunits of protein kinase A and anchors/targets them.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- cAMP-dependent protein kinase catalytic subunit alpha
- cAMP-dependent protein kinase catalytic subunit beta
- cAMP-dependent protein kinase type II-alpha regulatory subunit
- cAMP-dependent protein kinase type II-beta regulatory subunit
- cAMP-dependent protein kinase catalytic subunit gamma
- Sperm surface protein Sp17
- A-kinase anchor protein 4
- Dynein axonemal assembly factor 6
- EF-hand calcium-binding domain-containing protein 7
- A-kinase anchor protein 1, mitochondrial
Sequence:
MSETQNSTSQKAMDEDNKAASQTMPNTQDKNYEDELTQVALALVEDVINYAVKIVEEERNPLKNIKWMTHGEFTVEKGLKQIDEYFSKCVSKKCWAHGVEFVERKDLIHSFLYIYYVHWSISTADLPVARISAGTYFTMKVSKTKPPDAPIVVSYVGDHQALVHRPGMVRFRENWQKNLTDAKYSFMESFPFLFNRV
Protein: Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR3 (EC 3.1.3.95) (Myotubularin homologous protein 1) (ceMTMH1) (Myotubularin-related protein 3) (ceMTM3) (Phosphatidylinositol-3,5-bisphosphate 3-phosphatase) (Phosphatidylinositol-3-phosphate phosphatase) (Q22712)
Organism: Caenorhabditis elegans
Function: Preferentially dephosphorylates phosphatidylinositol 3-phosphate (PI3P), and has some activity towards phosphatidylinositol 3,5-bisphosphate (PI35P). May also dephosphorylate proteins phosphorylated on Ser, Thr, and Tyr residues (By similarity). Positively regulates autophagy and is recruited to autophagosomes by PI3P where it catalyzes PI3P turnover to promote autophagosome maturation. Thought to have a role in maintenance of muscle function. Involved in locomotion and lifespan determination.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:25124690}. Membrane {ECO:0000250|UniProtKB:Q13615}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q13615}.
Interaction partners:
- SAC domain-containing protein
- Phosphatidylinositol 3-kinase piki-1
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase mtm-1
- Phosphatidylinositol 3-kinase catalytic subunit type 3
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR6
- Phosphatidylinositol-3-phosphatase SAC1
- Phosphatidylinositol-4,5-bisphosphate 4-phosphatase
- Phosphoinositide 3-kinase adapter subunit
- 1-phosphatidylinositol 4-kinase
- SAC domain-containing protein
Sequence:
MTVTSSAAIDIGGGGGGRRSDRLDSDRTSEDMSFIASPANESFQIGASFVDVQNESSGSIDTATATLHELNYTFGMPPVTEESENMPQNYETVVELLPGEERAPINKLTEFPIEGGSLFVTNFRIVVILKDKEVEEALRFLVFPLQDIEQIDLAIPAFIHLSLKIGRMFTICFKTAEDAALVHKILYTAFQRLNRPISSIYTSRPQDWTSKNTDNPMQSLNAFAWKFSEAVDELDRDGKLPSWLLRADSVAQEITHIDFNRLGMSEHFQISSVNENFEVCPTYPEKIIVPKGITDDDIRKGAPYRSIGRFPAVIWRCRKTRAVLMRSSQPQVGILSWRNPTDEKIIEEAVKASRIEGEEKKQFIIMDARGYTSAFANRARSGGFENTEYYQQAKLEFLGLPNIHAVRGSFNNVRTMLHNLGPNEQLLTSLQTTGWLLNLSNLLVNAANCADHLSKGHSVLVHCSDGWDRTTQVTTLAKIMLDEYYRTVKGFEELIRRDWIAFGHKLYDRQLVAFGNWGTSDERSPVFLQFLEAVRHLQREQPTLFQFTHAYLIKLAKHAYSGLFGSFLFNSHKERREAMEKCKGTLVDIWRFIGPHNEEYVNQSFDEHYTGAVKPVNVSVINLRVWHEVFADEEEHYTQIFSPKEERPLSGCTTPMNTSTSTNLVKSKSSESINSLNVDGSAKESSQQHPTCSTTPSDNTNSLPMSTSFIQQSLYQPKVRGVAAIDRDGVIRFEDDEQAMLRKKNKLRAEEIRRKDEKIEELRRRAVLDTNKVSPGQRQSYSESDVETTGTLERVMSDVSMVDPVNELPHFKPNTTWEGESGHCAYCKKEFNKLSVYVEDRQHHCRNCGRVVCEDCSKNRFSVIEEGKSVQKRACDSCYDSMHETDLKLSSSSTTTTSSSTKIENDSNVPGLDNNSDNVSENVSENAIPDIIVEEKEAEDPIKEAESPSKETKCPKTLRNFISFSPKSSMRKNKVHSRDPLKSIDEGSSSQQAESDDVLDVNEQPL
Protein: Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha isoform X1 (Phosphatidylinositol-4-phosphate 3-kinase, catalytic subunit type 2 alpha) (F6NMW9)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
Sequence:
MAHISSGNGFKFDRPASPGVVRPKGIVGKEEALRMEVEAFDKIKREKRHTLPVTASSVNPLPNPTAQTSSSRPEKDLIVFCESETQKKEQKDNFEDIDLENLTKEELEKLLLDDSFGANKMTRPSSLLGCNLSASYPGGHAFNPSSFHWTPTPTHAQTPIFPSAPFAKPPCSFQNGFSPAMSPFIPPTPFLSFTPIQPPAALVYSQPAVTPEMAKLFDKIASTSEYLKNGRSSSMETESASVKSLEPLPLPSEPPNISRFEWLDLDPLNKRKEVEVEETPAVSSCPFIEESGKAKDPWDAVLQDEHETVDNGSPTAEEKSKATQPRRASTGAAVTKSQSLSISANSTNQSTGKQVNKGSTNVLSKYSALQEKEAQNLEVVAFCEDISKLRSKFPHDDLSTNPGYVLSPVITQRDAGGDNGGSVKVSIEISDSQQPVTFTCDVTSPVDLLIMQALCWVHDDLNQVDINSYVLKVCGQEEVLQNKHSLGSHEYVQNCRKWESEIKLQLLFLSTMRRDLARTAEDDISPIDLEKYLGLVERPFKEAVTREGLAEYLEGFHKQVNLCLQNENNQYKTVDNVVQSVKNLCCALDEVETPAITDAVKRLKRSVNLPRTRSPEAGATSSGGSANGYSSPVEESLAVLTDAVYELAKLYLQSFCPISPGFMIEEHKEDERDSKEASGTTEHLQFTLFAVHGIPATWVSSFEKYYLMCALTHNNRNLFKPVQSKKVGTYKSFFYHIKWDELINFPISVSLLPLEAMLSLSLYGVLSQNANNSPDSNKQRKGPELLGKVSMPLFDFRRVLSRGSKLLSLWTSPQALQPGAAGKGRNPTEKIILQVDFPSPAVDVLYVGPQENGCPNPQSLDPLDQDDRSEIEKLCARASTFGLSRADRQLLWDQRYYCREYEYSLPKILASAPSWDWGSMGEIHALLHHWPALSPVSALELLESKFADTEVRKVAVSWIQSSSDDELADYLPQLVQAVKFECHLNNALVKFLLSRALGNVNIAHYLYWLLRDAVQDPAFGQRYERILCVLLCLCGTGLRAELEKQTRLVQLLGALAEKVRQASSSTRQVVLLEGLERVQSFFQKNSCRLPISPSLVAKELNIKVCSFFNSNAVPLKIALVNADPLGDEINVMFKVGEDLRQDMLALQMIRIMDRIWLQEGLDLRIVNFKCISTGKDKGMVELVPSSETLRKIQVEYGVTGSFKDKPLAEWLRKYNPAEDEYEKASENFIYTCAGCCVATYILGICDRHNDNIMLRSTGHMFHIDFGKFLGHAQMIGSFKRDRAPFVLTSDMAYVINGGERPTSRFQLFVDLCSQAYNLIRKHSNLFLNLLSLMTQSGLPELTGVQDLKYVYDALQPQTTDAEATIFFTRLIESSLGSVATKFNFFIHNLAQLRFSGLPSNDEPILSFAPRTYTMKQDGKIRDASVFSFQKRYNPDKHYTYVIRILREGQSEPQFVFRTFDEFQELHNKLTILFQLWKLPGFPSKMVLGRTHIKDVASKRKVELNSYVHNLMRSSTEVAQCDLIYTFFHPIARDDKTEGVDTLSKTPDMPPVSPTTGRVEGEVKLSVSYRNSTLFIMVMHIKDLMSNDGADPNPYVKTYLLPDPHKTSKRKTKIARKTRNPTFNEMLVYSGYSKETLKQRELQLSVLSAESLRENCYLGGITLCLKDFDLSRETVKWYKLTTVPYF
Protein: Pterin-4-alpha-carbinolamine dehydratase (PHS) (EC 4.2.1.96) (4-alpha-hydroxy-tetrahydropterin dehydratase) (Dimerization cofactor of hepatocyte nuclear factor 1-alpha) (DCoH) (Dimerization cofactor of HNF1) (Phenylalanine hydroxylase-stimulating protein) (Pterin carbinolamine dehydratase) (PCD) (P61458)
Organism: Mus musculus (Mouse)
Function: Involved in tetrahydrobiopterin biosynthesis. Seems to both prevent the formation of 7-pterins and accelerate the formation of quinonoid-BH2. Coactivator for HNF1A-dependent transcription. Regulates the dimerization of homeodomain protein HNF1A and enhances its transcriptional activity (By similarity). Also acts as a coactivator for HNF1B-dependent transcription (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:P61459}. Nucleus {ECO:0000250|UniProtKB:P61459}. Note=Recruited to the nucleus through the interaction with HNF1B. {ECO:0000250|UniProtKB:P35680}.
Interaction partners:
- Phenylalanine-4-hydroxylase
- Dihydropteridine reductase
- Tyrosine 3-monooxygenase
- Hepatocyte nuclear factor 1-alpha
- Tryptophan 5-hydroxylase 1
- Tryptophan 5-hydroxylase 2
- Pterin-4-alpha-carbinolamine dehydratase 2
- Hepatocyte nuclear factor 1-beta
- Homogentisate 1,2-dioxygenase
Sequence:
MAGKAHRLSAEERDQLLPNLRAVGWNEVEGRDAIFKQFHFKDFNRAFGFMTRVALQAEKLDHHPEWFNVYNKVHITLSTHECAGLSERDINLASFIEQVAVSMT
Protein: CAP, isoform V (A0A0B4K6W0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell junction {ECO:0000256|ARBA:ARBA00004282}.
Interaction partners:
Sequence:
MPNNRNRNRNRNRNKRNRNQNQNQNPSQNQNENHQQQAEGAEDREEQQDFQTQIAVAQSSSFVDDNGNSGSVSNGPTENSEEVTNTLEKTEKKEEIFEQPATVIQKEADSDAEMGAKNSKHRKEKSDKQASNGKSEEQVRPPPTIIRRPPGSPRQAKVIVHRIVREEDTANGKAQSPEPPKAVESKEQHMEVEDSKKEKPEAQQEIETKEERENEPSPKELPESSHLSEDAQQKHVEVEENQQVYDEVDYSKDETTDNNPQQEQHDSKEPEQYVLQLEKAMEFVENAHQQHVAAVQSYQKQRDTEQNAQQQEQNEAQHLQESTKAHQQNIAVPQILVDPKKREEGLAQQLHHDVKEEPILNNAQQQNDDTAPKSPKEVTIKVQFQTEDPYSQQPPPQKPTSKVIIHQIHVETTDEEQNAKPTFEEVSSTTGSLAGTLSPPPRYLVESPKNVSSGQFSNFSRNVQIQEMELNSDFSSGEFNSLQSPLVCEVDSESEGSVVLGPERSPSDQQVPSSSRVEQHEQVRQKRAQYRNALESHFMPQLLNPRYLDSILEENEWRNSTASSGGSDQTGIRTPKLNETFPRSQLDFSRRHKRREEAPSPLKLETKLLEESTDLESCTRLQSALSPQSEDAELVYLSSSASSSVSDLMELELEQAAALAERALVDLDTDASRLIARPDDEMSSTSTTTADRSETEAETETETEREGEQSRESTPVNANPTLASSQSSLLSAATPTPTPTPTPADREQLAKDTNVSGGSTVSFGAASPLAATREEFVRNMDKVRELIEMTRREQEQGELPRSPSPPPVPPPPASVPPYSPESSSFHLASLQLKRQESNDSHCSDSTTHSQCTAINLASPPPPPTAQPPTPPLRQKPAPPPVPQPVSPPAPPTPQSEPELSVADSVANANADVDADADTDTEAIKKLRLLCTEQLASMPYGEQVLEELASVAQNISDQSQNKMPYPMPQLPHIKELQLNANESKSSSAWLGLPTQSDPKLLVCLSPGQRDLVNNQTQPDDLLDAHQKFVERRGYHELSKAQVLEQDHQQQQSEMLKTAAMMRELRKSLSPPAPPVPPPPVPVKSAETAAKATAHENAKRDDASEQKQKIAACESSSLENKPRRAADLGAQQSAEQRQSSSTTTSSHKATTETMSSDTAKFPTLDSMESELARMFPQHKGDIFEEQRKRFSNIEFPSHQPVSQTKRYSNIETSSYESKKRMENGQVVYDVSTSSHEKKEQGDPPKDQPVPPVPPPPIMSATKLNGNTFIDGDVAPKNSQPSRESGSGSGNGTYEEFRQRAKAAADAFGEQREQQNGLDQDRVFKDFDRLSQQMHAELQSTREKREKSASMYDLSGFTRPASGHPRLDELQQRRHAHMQELEREIERSAKSRQERMSSVPRQMEATPPRTHEIPIELEPRSRRAESLCNLNEPPPRPHTTVGHYNHPVVQDDWSRYANDLGYSENIARPFAREVEICYQRQNQRTPHCIRAPRLSASTNDLSSSSQYSYDTFNAYGGRRTHAPMLNQAQQQQRPHYGSCYSMIERDPNPRYISTTSRRGVSPAPPPVATPQQQQVPPPAYDRQQRRSSLPRELHEQQLKYILSKEEELKFEVERLQQERRRLMEEMQRAPVLPAPQRRESYRPAAKLPTLSEDEVFRQQMAEEWMNKVAEREERRQHKIIRISKIEDEHDHSAVDKATISDEFLDRVKERRHKLSMPADSDWESGAESQPQPAAQSQPESDVEAPPVRILEGQAEANLRQLPRHLREFAKFSTSEQLPDGAQMERHEEQERREEATDNAHSSATKKTSIVKTYKVSRLPPSVQVYKVKHEYMSEPETGSDRPRKMAQLGRRQYDGIGPVTNDGMPIILRSEVKEPHQHEWYKRLYQTIHKQKNGDDFVIRYKCPRARPSYKSNGYVSEPEPNYDSDYSTVRYRTQNPHRVQSVSSAVNVRNLNQDEKLYGTMPNPIKSAQNSYKNQPGRIENYTTGHSSVSEKEKKEWWDEVMDIFNGNLEQSKLSPLYTEGNLSRALAKESGYTSDSNLVFRKKEVPVSSPLSPVEQKQAYKSLQAGGEPPLLGFRKPAPEKPRDLDPNAPPIPPQPPVKGLSSYDFPYSTDTVDGSDVNIHFKTPIRHEQRQNLSEEELAIRQAEHMQKLYHEERRRKYLQELQDMNSRRHTDNFTPSQKSPIALNRYDDFPTDVTLKSLVGPKTVARALFNFQGQTSKELSFRKGDTIYIRRQIDANWYEGEHNAMIGLLPASYVEIVSRDGARTPSKRPSEGQARAKYNFQAQSGIELSLNKGELVTLTRRVDGNWFEGKIANRKGIFPCSYVEVLTDIGAEDIAARTTTVITSQSTTNLRPNLDVLRTNINNEFNTLTQNGAQPPNGILKETRTLHKTDALHVDTSSEPLAYRALYKYRPQNSDELELLEGDVVHVLEKCDDGWFVGTSQRTGCFGTFPGNYVERA
Protein: Heterogeneous nuclear ribonucleoprotein A1 (H0YH80)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALSKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF
Protein: DNA-directed RNA polymerases II, IV and V subunit 11 (DNA-directed RNA polymerase II 13.6 kDa polypeptide) (DNA-directed RNA polymerase II subunit J) (DNA-directed RNA polymerase II subunit RPB11) (RNA polymerase II subunit B11) (Q38859)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription machinery. It is composed of mobile elements that move relative to each other. NRPB11 is part of the core element with the central large cleft. Component of RNA polymerases IV and V which mediate short-interfering RNAs (siRNA) accumulation and subsequent RNA-directed DNA methylation-dependent (RdDM) transcriptional gene silencing (TGS) of endogenous repeated sequences, including transposable elements.
Subcellular location: Nucleus.
Interaction partners:
- DNA-directed RNA polymerases II, IV and V subunit 8B
- DNA-directed RNA polymerase subunit 10-like protein
- DNA-directed RNA polymerase V subunit 5A
- DNA-directed RNA polymerase IV subunit 1
- DNA-directed RNA polymerases II, IV and V subunit 3
- DNA-directed RNA polymerases II, IV and V subunit 12
- DNA-directed RNA polymerase II subunit 7
- DNA-directed RNA polymerases IV and V subunit 3B
- DNA-directed RNA polymerases II, IV and V subunit 9A
- DNA-directed RNA polymerase V subunit 7
Sequence:
MNAPERYERFVVPEGTKKVSYDRDTKIINAASFTVEREDHTIGNIVRMQLHRDENVLFAGYQLPHPLKYKIIVRIHTTSQSSPMQAYNQAINDLDKELDYLKNQFEAEVAKFSNQF
Protein: Zinc finger CCCH-type containing 18 (H3BRH3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
KSKKEDGVKEEKRKRDSSTQPPKSAKPPAGGKSSQQPSTPQQAPPGQPQQGTFVAHKEIKLTLLNKAADKGSRKRYEPSDKDRQSPPPAKRPNTSPDRGSRDRKSGGRLGSPKPERQRGQNSKAPAAPADRKRQLSPQSKSSSKVTSVPGKASDPGAASTKSGKASTLSRREELLKQLKAVEDAIARKRAKIPGKA
Protein: Mesaconyl-CoA hydratase (EC 4.2.1.148) (2-methylfumaryl-CoA hydratase) (Beta-methylmalyl-CoA dehydratase) (Q3IZ78)
Organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter sphaeroides)
Function: Involved in the ethylmalonyl-CoA pathway for acetate assimilation. Catalyzes the reversible hydration of mesaconyl-CoA (2-methylfumaryl-CoA) to yield beta-methylmalyl-CoA ((2R,3S)-beta-methylmalyl-CoA).
Interaction partners:
- 
- L-malyl-CoA/beta-methylmalyl-CoA lyase
- (3S)-malyl-CoA thioesterase ((3S)-malyl-CoA thiolesterase)
- Ethylmalonyl-CoA mutase
- Crotonyl-CoA carboxylase/reductase
- 3-hydroxyacyl-CoA dehydrogenase
- Conserved small protein
- 3-hydroxyacyl-CoA dehydrogenase
- Membrane protein
Sequence:
MKTNAGRFFEDYRLGETIAHAVPRTVSGGERALYHALYPARHALSSSDEFARACGLPAAPVDELMAFHLVFGKTVPDISLNAVANLGYAEGRWLKPVFPGDTLRAESTVIGLKENSNGASGVVWVRTRGLNQQGEAVLSYVRWVMVRKRDTAAPAPAPTVPELAGSVAASDLVIPEGLSFTDYDLTLAGEPHRWGDYAVGEKIDHVDGVTVEESEHMLATRLWQNTAKVHFDATNRPDGRRLIYGGHVISLARTLSFNGLANAQMIVALNAGAHANPCFAGDTVRAWSEVLDKAETADPGVGALRLRLVAMKHGTEPFVTRSEDGKYLPGVLLDLDYWALVPR
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-1 (EC 3.1.4.11) (PLC-154) (Phosphoinositide phospholipase C-beta-1) (Phospholipase C-I) (PLC-I) (Phospholipase C-beta-1) (PLC-beta-1) (Q9NQ66)
Organism: Homo sapiens (Human)
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 G
- Guanine nucleotide-binding protein subunit alpha-11
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Guanine nucleotide-binding protein subunit alpha-14
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-15
- Protein kinase C alpha type
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR2
- Calcium/calmodulin-dependent protein kinase type II subunit alpha
Sequence:
MAGAQPGVHALQLKPVCVSDSLKKGTKFVKWDDDSTIVTPIILRTDPQGFFFYWTDQNKETELLDLSLVKDARCGRHAKAPKDPKLRELLDVGNIGRLEQRMITVVYGPDLVNISHLNLVAFQEEVAKEWTNEVFSLATNLLAQNMSRDAFLEKAYTKLKLQVTPEGRIPLKNIYRLFSADRKRVETALEACSLPSSRNDSIPQEDFTPEVYRVFLNNLCPRPEIDNIFSEFGAKSKPYLTVDQMMDFINLKQRDPRLNEILYPPLKQEQVQVLIEKYEPNNSLARKGQISVDGFMRYLSGEENGVVSPEKLDLNEDMSQPLSHYFINSSHNTYLTAGQLAGNSSVEMYRQVLLSGCRCVELDCWKGRTAEEEPVITHGFTMTTEISFKEVIEAIAECAFKTSPFPILLSFENHVDSPKQQAKMAEYCRLIFGDALLMEPLEKYPLESGVPLPSPMDLMYKILVKNKKKSHKSSEGSGKKKLSEQASNTYSDSSSMFEPSSPGAGEADTESDDDDDDDDCKKSSMDEGTAGSEAMATEEMSNLVNYIQPVKFESFEISKKRNKSFEMSSFVETKGLEQLTKSPVEFVEYNKMQLSRIYPKGTRVDSSNYMPQLFWNAGCQMVALNFQTMDLAMQINMGMYEYNGKSGYRLKPEFMRRPDKHFDPFTEGIVDGIVANTLSVKIISGQFLSDKKVGTYVEVDMFGLPVDTRRKAFKTKTSQGNAVNPVWEEEPIVFKKVVLPTLACLRIAVYEEGGKFIGHRILPVQAIRPGYHYICLRNERNQPLTLPAVFVYIEVKDYVPDTYADVIEALSNPIRYVNLMEQRAKQLAALTLEDEEEVKKEADPGETPSEAPSEARTTPAENGVNHTTTLTPKPPSQALHSQPAPGSVKAPAKTEDLIQSVLTEVEAQTIEELKQQKSFVKLQKKHYKEMKDLVKRHHKKTTDLIKEHTTKYNEIQNDYLRRRAALEKSAKKDSKKKSEPSSPDHGSSTIEQDLAALDAEMTQKLIDLKDKQQQQLLNLRQEQYYSEKYQKREHIKLLIQKLTDVAEECQNNQLKKLKEICEKEKKELKKKMDKKRQEKITEAKSKDKSQMEEEKTEMIRSYIQEVVQYIKRLEEAQSKRQEKLVEKHKEIRQQILDEKPKLQVELEQEYQDKFKRLPLEILEFVQEAMKGKISEDSNHGSAPLSLSSDPGKVNHKTPSSEELGGDIPGKEFDTPL
Protein: Cilia- and flagella-associated protein 100 (Flagella-associated protein 100) (Modifier of inner arms 1 protein) (Mia1p) (A8I4E9)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: As part of MIA, a complex associated with the outer doublet microtubules of the axoneme, may play a role in ciliary/flagellar motility by regulating the assembly and the activity of axonemal inner dynein arm.
Subcellular location: Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000269|PubMed:23569216}. Note=Localizes to the outer doublet microtubules of the axoneme. {ECO:0000269|PubMed:23569216}.
Interaction partners:
Sequence:
MPIYDEASVPGTAAGRSTTDVGATAGANPFNIPADEEIFRFREEERARKEQDKLIAQTMRVADKTTFAAQMQATATADARTLLRELRPPKGPKATTTLAASSVGTLDRRKEKENMADFIAKKREIFLLQMSLDTKRAEIKKLEERARQREEALKKSEQMLEEDALRFDAFLKENDEKVQEAIKKAEAEAKAKQDKVLEIKRLNTATAALRSELNKYEEQLEDCRRYKEFLDSITPPEWFEQQAAKLQRRKDALVAEWQSQCEALKQRREAALAAKTAAESDYANARTQQQAERAERAIKESVAALKEIMKEKEPQPPNLDFEMDPEDEEMYFQEPGQLLAVYKQLEESNLFYIQNAQETEEALEELRQKLRDTKTRMDAEAQGLQGQVSTLQASIVAAREKAKRLKDRTLENEGAFTLSMGSSNAPTSSVTGSSGPGGPVNLKELGDKVREVYVRCGFDADASISTLQMLTNIEMKLEEYLNLAEGMTPDYVDGAEKAREKDRRKVARDEKLSTQHREHEARMARALERAAAPVFKKTGKPLMFRSAPPQRKKVVQADDRNDEEAELEAYLAQDMI
Protein: EGF-containing fibulin-like extracellular matrix protein 1 (Fibulin-3) (FIBL-3) (T16 protein) (O35568)
Organism: Rattus norvegicus (Rat)
Function: Binds EGFR, the EGF receptor, inducing EGFR autophosphorylation and the activation of downstream signaling pathways. May play a role in cell adhesion and migration. May function as a negative regulator of chondrocyte differentiation. In the olfactory epithelium, it may regulate glial cell migration, differentiation and the ability of glial cells to support neuronal neurite outgrowth.
Subcellular location: Secreted, extracellular space {ECO:0000269|PubMed:18803302}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:18803302}. Note=Localizes to the lamina propria underneath the olfactory epithelium. {ECO:0000269|PubMed:18803302}.
Interaction partners:
- Metalloproteinase inhibitor 3
Sequence:
MLQTVFLTMLTLALVKSQVTEETITYTQCTDGYEWDPVRQQCKDIDECDIVPDACKGGMKCVNHYGGYLCLPKTAQIIVNNEQPQQETPAAEASSGAATGTIAARSMATSGVIPGGGFIASATAVAGPEVQTGRNNFVIRRNPADPQRIPSNPSHRIQCAAGYEQSEHNVCQDIDECTSGTHNCRLDQVCINLRGSFTCHCLPGYQKRGEQCVDIDECSVPPYCHQGCVNTPGSFYCQCNPGFQLAANNYTCVDINECDASNQCAQQCYNILGSFICQCNQGYELSSDRLNCEDIDECRTSSYLCQYQCVNEPGKFSCMCPQGYQVVRSRTCQDINECETTNECREDEMCWNYHGGFRCYPQNPCQDPYVLTSENRCVCPVSNTMCRDVPQSIVYKYMNIRSDRSVPSDIFQIQATTIYANTINTFRIKSGNENGEFYLRQTSPVSAMLVLVKSLTGPREHIVGLEMLTVSSIGTFRTSSVLRLTIIVGPFSF
Protein: Ankyrin repeat-containing protein P1E11.10 (Q9UU77)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- 5'-3' exoribonuclease 2
Sequence:
MSTTTPNIWIAASDGKTDVVLKHLDSGISPNAADENGYTPIHAAVSYGHSDLLKILVERGGDINIRDQDGETPLFVCEKLEIAHDLINQYNADTTVKNNDGLIAAQVIEANGEFPELAKYLYSFTDLEPKDVNTLPNDTKIEYAKLMTEQEMDEEAGQPLLDQKAKAEIDRILALRDTGVNVDDELRKILTGALSGHFERNVRPRSN
Protein: Cytochrome c peroxidase, mitochondrial (EC 1.11.1.5) (Q4Q3K2)
Organism: Leishmania major
Subcellular location: Mitochondrion intermembrane space {ECO:0000256|ARBA:ARBA00004569}. Mitochondrion matrix {ECO:0000256|ARBA:ARBA00004305}.
Interaction partners:
- Cytochrome c
- L-gulonolactone oxidase
- Superoxide dismutase
- Trypanothione reductase
- non-specific serine/threonine protein kinase
Sequence:
MSGTSRRAKGLFTGIAVGTFVSGAMFVSCASARVEEPPFDIRALRADIEDMISEKLELGPSLIRLAWHEAASYDCFKKDGSPNSASMRFKPECLYAGNKGLDIPRKALETLKKKYPQISYADLWVLAAYVAIEYMGGPTIPFCWGRVDAKDGSVCGPDGRLPDGSKTQSHVREVFRRLGFNDQETVALIGAHTCGECHIEFSGYHGPWTHDKNGFDNSFFTQLLDEDWVLNPKVEQMQLMDRATTKLMMLPSDVCLLLDPSYRKYVELYAKDNDRFNKDFANAFKKLTELGTRNLHKAPASES
Protein: Ligand-gated ion channel pHCl-A (Q5D6W1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004236}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
FDESSSDKEILDLLLEKKRYDKRLLPPVNDEDFCCGLQSPDMATNQNARRPHNRGTLTVNVNVLLLSLASPDESSLKYEVEFLLNQQWNDPRLQYGNKSHYDFLNALHHHDSIWTPDTYFIMHGDFKDPIIPMHFALRIFRNGTITYAMRRHLILSCQGSLHIFPFDDPKCSFSMESISYEEAQIKYVWKNDEDTLRKSPSLTTLNAYLIKNQTTACDQNSWRGNYSCLRVDLIFTRDRAFYFTTVFIPGIILVTSSFITFWLEWNAVPARSMIGVTTMLNFFTTSNGFRSTLPVVSNLTAMNVWDGVCMCFIYASLLEFVCVNYVGRKRPLHNVVYRPGENPVTQRLPAVLSRIGVILASPLPGEKRQNAGAPNEIVACTTCGGSNSPCTHSANNGCATETCFVQVRKKEPPHPIRVAKTIDVIARITFPTAYAIFLIFFFVHYKGFS
Protein: Mitochondrial import receptor subunit TOM40 homolog 1 (dtom40) (Male sterile protein 15) (Translocase of outer membrane 40 kDa subunit homolog 1) (Q9U4L6)
Organism: Drosophila melanogaster (Fruit fly)
Function: Channel-forming protein essential for import of protein precursors into mitochondria.
Subcellular location: Mitochondrion outer membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}.
Interaction partners:
- FI03495p
- LD34461p
- Mitochondrial import receptor subunit TOM7 homolog
- Metaxin-1 homolog
- Mitochondrial import receptor subunit TOM22 homolog
- TOMM20-like protein 1
- SAM50-like protein CG7639
- Serine/threonine-protein kinase Pink1, mitochondrial
- Voltage-dependent anion-selective channel
- Mitochondrial import inner membrane translocase subunit Tim10
Sequence:
MGNVLAASSGAPGSGASNLGLGLQEPAPLPSNSGSLTESSSSAEGLDSLAAAKDAALENPGTVEELHKKCKDIQAITFEGAKIMLNKGLSNHFQVSHTINMSNVVPSGYRFGATYVGTKEFSPTEAFPVLLGDIDPAGNLNANVIHQFSARLRCKFASQIQESKVVASQLTTDYRGSDYTLSLTVANPSIFTNSGVVVGQYLQSVTPALALGSELAYQFGPNVPGRQIAIMSVVGRYTAGSSVWSGTLGQSGLHVCYYQKASDQLQIGAEVETSLRMQESVATLAYQIDLPKANLVFRGGIDSNWQIFGVLEKRLAPLPFTLALSGRMNHVKNNFRLGCGLMIG
Protein: Melatonin receptor type 1B (Mel-1B-R) (Mel1b receptor) (Q8CIQ6)
Organism: Mus musculus (Mouse)
Function: High affinity receptor for melatonin. The activity of this receptor is mediated by pertussis toxin sensitive G proteins that inhibits adenylate cyclase activity (By similarity).
Subcellular location: Cell membrane; Multi-pass membrane protein.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-4
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Melatonin-related receptor
- Guanine nucleotide-binding protein G
Sequence:
MPENSSIPNCCEASGLAARPSWSGSAGARPPVTARAPWVAPMLSTVVVVTTAVDFVGNLLVILSVLRNRKLRNAGNLFVVSLALADLVIALYPYPLILVAIIRDGWVLGEAHCKASAFVMGLSVIGSVFNITAIAINRYCCICHSTTYHRVCSHWYTPIYISLVWLLTLVALVPNFFVGSLEYDPRIYSCTFIQTASTQYTAAVVAIHFLLPMAVVSFCYLRIWVLVLQARRKAKATRKLRLRPSDLRSFLTMFAVFVVFAICWAPLNCIGLAVAINPEAMALQVPEGLFVTSYFLAYFNSCLNAIVYGLLNQNFRREYKRILLAIWNTRRCIQHASKHCLTEERQGPTPPAARATVPVKEGAL