wanglab/gogpt-training-data huggingface dataset:
Protein: 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 (EC 3.1.4.11) (Phosphoinositide phospholipase C-beta-3) (Phospholipase C-beta-3) (PLC-beta-3) (Q01970)
Organism: Homo sapiens (Human)
Function: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:29122926}. Membrane {ECO:0000250|UniProtKB:Q99JE6}. Nucleus {ECO:0000250|UniProtKB:P51432}. Note=And particulate fractions. {ECO:0000250|UniProtKB:Q99JE6}.
Interaction partners:
- Guanine nucleotide-binding protein G
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR1
- Inositol 1,4,5-trisphosphate-gated calcium channel ITPR3
- Guanine nucleotide-binding protein subunit alpha-11
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein subunit alpha-15
- Guanine nucleotide-binding protein subunit alpha-14
- Protein kinase C alpha type
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
Sequence:
MAGAQPGVHALQLEPPTVVETLRRGSKFIKWDEETSSRNLVTLRVDPNGFFLYWTGPNMEVDTLDISSIRDTRTGRYARLPKDPKIREVLGFGGPDARLEEKLMTVVSGPDPVNTVFLNFMAVQDDTAKVWSEELFKLAMNILAQNASRNTFLRKAYTKLKLQVNQDGRIPVKNILKMFSADKKRVETALESCGLKFNRSESIRPDEFSLEIFERFLNKLCLRPDIDKILLEIGAKGKPYLTLEQLMDFINQKQRDPRLNEVLYPPLRPSQARLLIEKYEPNQQFLERDQMSMEGFSRYLGGEENGILPLEALDLSTDMTQPLSAYFINSSHNTYLTAGQLAGTSSVEMYRQALLWGCRCVELDVWKGRPPEEEPFITHGFTMTTEVPLRDVLEAIAETAFKTSPYPVILSFENHVDSAKQQAKMAEYCRSIFGDALLIEPLDKYPLAPGVPLPSPQDLMGRILVKNKKRHRPSAGGPDSAGRKRPLEQSNSALSESSAATEPSSPQLGSPSSDSCPGLSNGEEVGLEKPSLEPQKSLGDEGLNRGPYVLGPADREDEEEDEEEEEQTDPKKPTTDEGTASSEVNATEEMSTLVNYIEPVKFKSFEAARKRNKCFEMSSFVETKAMEQLTKSPMEFVEYNKQQLSRIYPKGTRVDSSNYMPQLFWNVGCQLVALNFQTLDVAMQLNAGVFEYNGRSGYLLKPEFMRRPDKSFDPFTEVIVDGIVANALRVKVISGQFLSDRKVGIYVEVDMFGLPVDTRRKYRTRTSQGNSFNPVWDEEPFDFPKVVLPTLASLRIAAFEEGGKFVGHRILPVSAIRSGYHYVCLRNEANQPLCLPALLIYTEASDYIPDDHQDYAEALINPIKHVSLMDQRARQLAALIGESEAQAGQETCQDTQSQQLGSQPSSNPTPSPLDASPRRPPGPTTSPASTSLSSPGQRDDLIASILSEVAPTPLDELRGHKALVKLRSRQERDLRELRKKHQRKAVTLTRRLLDGLAQAQAEGRCRLRPGALGGAADVEDTKEGEDEAKRYQEFQNRQVQSLLELREAQVDAEAQRRLEHLRQALQRLREVVLDANTTQFKRLKEMNEREKKELQKILDRKRHNSISEAKMRDKHKKEAELTEINRRHITESVNSIRRLEEAQKQRHDRLVAGQQQVLQQLAEEEPKLLAQLAQECQEQRARLPQEIRRSLLGEMPEGLGDGPLVACASNGHAPGSSGHLSGADSESQEENTQL
Protein: Negative regulator of pleiotropic drug resistance STB5 (Q6FQY1)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Function: Transcription factor that negatively regulates pleiotropic drug resistance genes, including the ABC transporter genes CDR1, PDH1, and YOR1.
Subcellular location: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00227}.
Interaction partners:
- RNA polymerase II holoenzyme cyclin-like subunit
- Serine/threonine-protein kinase SSN3
- Mediator of RNA polymerase II transcription subunit 14
- Mediator of RNA polymerase II transcription subunit 10
- Mediator of RNA polymerase II transcription subunit 6
- Mediator of RNA polymerase II transcription subunit 17
- Mediator of RNA polymerase II transcription subunit 31
- Mediator of RNA polymerase II transcription subunit 7
- Candida glabrata strain CBS138 chromosome L complete sequence
- Mediator of RNA polymerase II transcription subunit 21
Sequence:
MSGPDKGSDSGQTANDPKQKKARNGQMETYSCARCRKLKKKCPRQLPECSNCLKAREPCNYPGRAPRRTKKELRDAIMKGEVLPSMRRKHRKIEKELKTADLRHLESVDDRPVNQVMGGSMPPLGAYRGGEQQYNNGPPISGIDGNDSINRGKAQSVGSYQILPPQRKSKLVLDQNPKFVHSQSSALKTNEYPVPIMSPHIANQVYPEGVSSLISALNTMNDNVSANTPIALSYLQLQKLHQEQQQIQQQQIQQQQQHQHLVQQHLQHVRADATSILPPVTSQTVYTPIPGPRTSQIPFGFTHGYTASAPPPLMQPYSMPTSPFESREKQQQFDNIQYHPVYKIPPIAARQSPIDEIIGIENGSISIDAGSITREVVNSRMKGPHSTSWVNEDGSPKPIKKSLLEKFVSAYFEHNHRLFPMVDKVTFLKKLATINSFESIEMLAVNNPELPKTFIFEIYMIMAIGCTTLQRAGKLTTDEGHLYEHLAYLAMRNFRDILHQQDITTLRCLILLGIYSFFEPKGVSSWTISGIAMRLAIELGLNRPLTAKEMGDMSAVEVESRYRVFWSAYCFERVVATSLGRVSAIDDEDIGIPLPRALYDSEKEDIEVTNLIISLRKMGGKIYKEVHSLSAGRKDITMEQKQLIIQKLRKELDDIYEEECEKRRLKGKSRSSKRFEKSKESDSDRGVTEEDVKSGNENLIGLLASDDVSMTEHGQSIDNTLESTPLPTTIPTTIVNDSVDQHSTLENIPTSATSKDQIETIITKPTANIMNDQTDSDPLPKVDNKPISNNEEGPKSLKEGNSEQNPSENISPEDVTLTKTDNSENKESSLRSNSNISFHISNVWLEMRYTQLQILLYRPSALIPKPPIESLTVLGEFCLAAWRHTYTLYKEKLLPLNWITLFRTLTICNTILYCLCQWSIDLVASTIEIQQCVEILQHFGEKWVFAMKCADVFQNISNTIVEISLSQGQDPNIDKLTRELFGASNAYLEILNENNVDVSWEDRFR
Protein: Inactive protein-arginine deiminase type-6 (Arginine deiminase-like protein) (Egg and embryo abundant PAD) (ePAD) (P75) (Peptidylarginine deiminase VI) (Protein-arginine deiminase type VI) (Protein-arginine deiminase type-6) (Q8K3V4)
Organism: Mus musculus (Mouse)
Function: Catalyzes the deimination of arginine residues of proteins (By similarity). In oocytes, is released during cortical reaction and plays a role in preimplantation cleavage and early embryonic development. May be involved in cytoskeletal reorganization in the egg and early embryo.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:12654293}. Nucleus {ECO:0000269|PubMed:12654293}. Cytoplasmic vesicle, secretory vesicle, Cortical granule {ECO:0000269|PubMed:16137333}. Note=Predominantly cytoplasmic (oocyte cytoplasmic sheets), also nuclear. Released extracellularly during the cortical reaction, and remains associated with the blastomeres surfaces as a peripheral membrane protein until the blastocyst stage of development (PubMed:16137333). {ECO:0000269|PubMed:16137333}.
Interaction partners:
- Oocyte-expressed protein homolog
- Transducin-like enhancer protein 6
- KH domain-containing protein 3
- NACHT, LRR and PYD domains-containing protein 5
- 14-3-3 protein sigma
- Zinc finger BED domain-containing protein 3
Sequence:
MSFQNSLSLSLVNPTHALCMVGMEITLDISKCAPDKCKSFTIRGSPRILIHISSSVIAGKEDTVVWRSMNHPTVALVRMVAPSPTVDEDKVLVSYFCPDQEVPTATAVLFLTGIEISLEADIYRDGQLDMPSDKQAKKKWMWGMNGWGAILLVNCSPNAVGQPDEQSFQEGPREIQNLSQMNVTVEGPTSILQNYQLILHTSEEEAKKTRVYWSQRGSSAYELVVGPNKPVYLLPTFENRRKEAFYVEATEFPSPSFSGLISLSLSLVEKAHDECIPEIPLYKDTVMFRVAPYIFMPSTQMPLEVYLCRELQLQGFVDSVTKLSEKSKVQVVKVYEDPNRQSKWLQDEMAFCYTQAPHKTVSLILDTPRVSKLEDFPMKYTLTPGSGYLIRQTEDHRVASLDSIGNLMVSPPVKAQGKDYPLGRVLIGGSFYPSSEGRDMNKGLREFVYAQQVQAPVELFSDWLMTGHMDQFMCFVPTNDKNNDQKDFRLLLASPSACFELFEQKQKEGYGNVTLFEDIGAEQLLSNGRESKTISQILADKSFREQNTYVEKCISLNRTLLKTELGLEDKDIILIPQLFCLEQLTNVPSNQQSTKLFARPYFPDMLQIIVLGKNLGIPKPFGPKINGTCCLEEKVCGLLEPLGLKCTFIDDFDCYLANIGDVCASAIINRVPFAFKWWKMTP
Protein: Aminopeptidase (EC 3.4.11.-) (Q6FUY4)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
Sequence:
MFPKLSLKTVASSFARLPATSFLKVTKAPIATSIVNGRSFFTDTKYKCGKCERQKEISKTIRIKFANMNSENREVLPTNVTPIHYNLSLEPNFETFKFHGLEEINLKVNDKTNDVITLNSIEIDIHSAKLDDVEPKQTKFDHDKQTVEFVFPEGTLAKSNDPTLKLDFTGILNDNMAGFYRAKYQDKKTGETKYMATTQMEPTDARRAFPCFDEPNLKATFGITLISDPSLTHLSNMDVKNETISESKKVTTFNDTPKMSTYLVAFIVAELNYVENKEFRIPVRVYATPGDEHLGQYAADLTAKTLAFFEKTFGIKYPLPKMDNVAVHEFSAGAMENWGLVTYRVVDLLLDEENSSLDRIQRVAEVVQHELAHQWFGNLVTMDWWEGLWLNEGFATWMSWYSCNEFQPSWNVWQQYVTDTLQHALSLDALRSSHPIEVPVKRADEINQIFDAISYSKGASLLRMISKWLGEDVFIKGVSNYLNNFKYGNAKTDDLWDALAKASGKDVRGVMNIWTKKVGFPVISIEENGSEIQFTQNRYLTTGDVKPEEDETLYPVFLALKTKSGVDNSLVLSERSKAVTIDDSSFYKVNTDQSGIFITAYPEDRWEKFGKQSDLLSVEDRTGLVADAKALSSSGYINTTSFFKLISNWKDEKSFVVWDQIIISLASLKAAWLFESPEVKDALEAFSRNLVADKAKTLGWEFKESDSFATQRLKVALFGAACAARDEVVEKAALDMFEKYVSGDKKAIPALIKPSVFNAVARKGGKDNYEKIFNIYKNPVSTDEKLAALRTLGRFKEADLLDRTLGYLFDGTVLNQDIYIPMQGMRAHKEGVTALWKWLQENWDEIARRLPPGLSMLGSVVAISTSGFSSLEAVDEIKTFFNTKSTKGFDQSLAQSLDTITSKAQWVDRDRESISKYLSDNGYM
Protein: At5g62340 (Plant invertase/pectin methylesterase inhibitor superfamily protein) (Similarity to ripening-related protein) (Q9LVA5)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
- Cell wall / vacuolar inhibitor of fructosidase 1
Sequence:
MAKQYQALFLLFSVFYLFSSVLTTATVNPAGTTTKALNFIQSSCKSTTYQSLCVETLSVYANTIKTSPRHLLDAAITVSLNQALSTKLFISHLRKSQFQILQDCAPSTDTFSTDCECSVQALQEVVNCNSWTDCLFHVKNAEVCAISGESHSVENTCSSPFADPGKISARGRISDAVRKSLHTRFSKLRQEINNAKMLFEAFPNKH
Protein: Rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma (EC 3.1.4.35) (M0R4R9)
Organism: Rattus norvegicus (Rat)
Interaction partners:
- G protein subunit alpha transducin 1
- G protein subunit alpha transducin 2
- Phosphodiesterase
- Phosphodiesterase
- Guanine nucleotide-binding protein subunit gamma
- Guanine nucleotide-binding protein G
- Guanylate kinase
- Regulator of G-protein signaling 9
- Hypoxanthine-guanine phosphoribosyltransferase
- GMP synthase
Sequence:
MNLEPPKSEIRSATRVMGGPVTPRKGPPKFKQRQTRQFKSKPPKKGVQGFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII
Protein: Cysteine-serine-rich nuclear protein 1b (Cysteine/serine-rich nuclear protein 1b isoform X1) (E9QH67)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- Muscle segment homeobox 1a.
- Arrestin domain-containing 1b.
- Gadd45b protein
Sequence:
MSGVLKRKYEEVAEDPCYSSSSPSSLSSSAYSEWDSDGESCYSDTLDSTPSNPSSPATSLNTTSILKKAKRTRRGNVQFDQVTVFFFPRCQGFTSVPSRGGCTLGMMQRHSAQRRYTLAEFAIAQRHLRREKLKNRMREEKLEALKLKLTKNGTQESEEAEKLTVDDIPEDEIDLSGVNVDDGSFLHPYPSKKRYAILKAAGVKKIDREEKRQLHELRTSREDCGCDCQGFCEPETCSCSLAGIKCQMDHSSFPCGCTKDGCGNTQGRIEFNSSRVHTHYIHTIMKLELEKRLEEHTTETPPETHPDSSSLNQPAEISSTPDMPTFHFNSELLSTGENSCSSDMTDSSSSSGQSEDSESVENVPSEQSPLDVDENGLTRILSFSDTDNEDCSIRERNDNCDYQQKKSEGSMGYGIFSTEDDKLNMSQTDNSRTAMSELLDENANQGNGLFHSSFIPHTPSPSIDHSASYMDLSLSSESDLEFFDGFPCLGPSSLYNSLKEYEHVDNFFQFQLPTYPSLPQAVDPGTCLLESLIGLSDSVPEPPTTFTDNQMLEDAMKLSVMESLKV
Protein: Peptidyl-prolyl cis-trans isomerase FKBP62 (PPIase FKBP62) (EC 5.2.1.8) (70 kDa peptidyl-prolyl isomerase) (FK506-binding protein 62) (AtFKBP62) (Immunophilin FKBP62) (Peptidylprolyl isomerase ROF1) (Protein ROTAMASE FKBP 1) (Rotamase) (Q38931)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides (By similarity). Co-chaperone that positively modulates thermotolerance by interacting with HSP90.1 and increasing the HSFA2-mediated accumulation of chaperones of the small-HSPs family.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:19366428}. Nucleus {ECO:0000269|PubMed:19366428}. Note=Relocalization from the cytoplasm into the nucleus is induced by heat shock and in association with HSFA2.
Interaction partners:
- Heat shock protein 90-1
- Heat stress transcription factor A-2
- Heat shock 70 kDa protein 4
- Heat shock protein 90-6, mitochondrial
- Chaperone protein ClpB1
- Protein HEAT-STRESS-ASSOCIATED 32
- Peptidyl-prolyl cis-trans isomerase CYP18-1
- Heat shock 70 kDa protein 5
- Prefoldin subunit 2
- Multiprotein-bridging factor 1c
Sequence:
MDANFEMPPVGGMNDDDDMDFGDGASFLKVGEEKEIQQGLKKKLLKEGEGYETPENGDEVEVHYTGTLLDGTKFDSSRDRATPFKFTLGQGQVIKGWDIGIKTMKKGENAVFTIPAELAYGESGSPPTIPANATLQFDVELLKWDSVKDICKDGGVFKKILAVGEKWENPKDLDEVLVKFEAKLEDGTVVGKSDGVEFTVKDGHFCPALTKAVKTMKKGEKVLLTVKPQYGFGEKGKPASAGEGAVPPNATLEINLELVSWKTVSEVTDDNKVVKKVLKEGDGYERPNEGAVVKVKLIGKLQDGTVFLKKGHGENEEPFEFKTDEEQVVDGLDRAVMKMKKGEVALVTIDPEYAFGSNESQQELAVVPPNSTVTYEVDLLTFDKERESWDMNTEEKIEAASKKKEEGNSKFKGGKYSLASKRYEKAVKFIEYDTSFSEEEKKQAKALKVACNLNDAACKLKLKDYKQAEKLCTKVLELESTNVKALYRRAQAYMELSDLDLAEFDVKKALEIDPNNREVKLEQKRLKEKMKEFNKKEAKFYGNMFAKLSKE
Protein: Phosphatidylinositol 3-kinase regulatory subunit alpha (PI3-kinase regulatory subunit alpha) (PI3K regulatory subunit alpha) (PtdIns-3-kinase regulatory subunit alpha) (Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha) (PI3-kinase subunit p85-alpha) (PtdIns-3-kinase regulatory subunit p85-alpha) (P23727)
Organism: Bos taurus (Bovine)
Function: Binds to activated (phosphorylated) protein-Tyr kinases, through its SH2 domain, and acts as an adapter, mediating the association of the p110 catalytic unit to the plasma membrane. Necessary for the insulin-stimulated increase in glucose uptake and glycogen synthesis in insulin-sensitive tissues. Plays an important role in signaling in response to FGFR1, FGFR2, FGFR3, FGFR4, KITLG/SCF, KIT, PDGFRA and PDGFRB. Likewise, plays a role in ITGB2 signaling. Modulates the cellular response to ER stress by promoting nuclear translocation of XBP1 in a ER stress- and/or insulin-dependent manner during metabolic overloading in the liver and hence plays a role in glucose tolerance improvement (By similarity).
Interaction partners:
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit beta isoform
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform
- Platelet-derived growth factor receptor beta
- Phosphatidylinositol-4,5-bisphosphate 3-kinase catalytic subunit gamma
- Receptor protein-tyrosine kinase
- Phosphatidylinositol 3-kinase regulatory subunit beta
- E3 ubiquitin-protein ligase CBL
- non-specific serine/threonine protein kinase
Sequence:
MSAEGYQYRALYDYKKEREEDIDLHLGDILTVNKGSLVALGFSDGQEAKPEEIGWLNGYNETTGERGDFPGTYVEYIGRKKISPPTPKPRPPRPLPVAPGPSKTEADSEQQASTLPDLAEQFAPPDVAPPLLIKLVEAIEKKGLECSTLYRTQSSSNPAELRQLLDCDTASLDLEMFDVHVLADAFKRYLLDLPNPVIPVAVSSELISLAPEVQSSEEYIQLLKKLIRSPSIPHQYWLTLQYLLKHFFKLSQTSSKNLLNARVLSELFSPLLFRFPAASSENTEHLIKIIEILISTEWNERQPAPALPPKPPKPTTVANNGMNNNMSLQDAEWYWGDISREEVNEKLRDTADGTFLVRDASTKMHGDYTLTLRKGGNNKLIKIFHRDGKYGFSDPLTFNSVVELINHYRNESLAQYNPKLDVKLLYPVSKYQQDQVVKEDNIEAVGKKLHEYNTQFQEKSREYDRLYEDYTRTSQEIQMKRTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKREGNETEIQRIMHNYEKLKSRISEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYLMWLTQKGVRQKKLNEWLGNENTEDQYSLVEDDEDLPHHDEKTWNVGSSNRNKAENLLRGKRDGTFLVRESSKQGCYACSVVVDGEVKHCVINKTATGYGFAEPYNLYSSLKELVLHYQHTSLVQHNDSLNVTLAYPVYAQQRR
Protein: Dynein light chain 1, cytoplasmic (8 kDa dynein light chain) (DLC8) (Dynein light chain LC8-type 1) (Protein inhibitor of neuronal nitric oxide synthase) (PIN) (P63167)
Organism: Homo sapiens (Human)
Function: Acts as one of several non-catalytic accessory components of the cytoplasmic dynein 1 complex that are thought to be involved in linking dynein to cargos and to adapter proteins that regulate dynein function. Cytoplasmic dynein 1 acts as a motor for the intracellular retrograde motility of vesicles and organelles along microtubules. May play a role in changing or maintaining the spatial distribution of cytoskeletal structures.
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:14654843}. Chromosome {ECO:0000269|PubMed:37696958}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:20921139}. Nucleus {ECO:0000269|PubMed:15891768}. Mitochondrion {ECO:0000269|PubMed:18084006}. Note=Upon induction of apoptosis translocates together with BCL2L11 to mitochondria (PubMed:18084006). Recruited to DNA double-strand breaks (DSBs) by TP53BP1 when phosphorylated at Ser-88 (PubMed:37696958). {ECO:0000269|PubMed:18084006, ECO:0000269|PubMed:37696958}.
Interaction partners:
- Bcl-2-like protein 11
- Cytoplasmic dynein 2 heavy chain 1
- Cytoplasmic dynein 1 intermediate chain 2
- Cytoplasmic dynein 2 intermediate chain 1
- Cytoplasmic dynein 1 intermediate chain 1
- Cytoplasmic dynein 2 intermediate chain 2
- Dynein light chain roadblock-type 1
- Cytoplasmic dynein 1 heavy chain 1
- Cytoplasmic dynein 2 light intermediate chain 1
- Striatin-4
Sequence:
MCDRKAVIKNADMSEEMQQDSVECATQALEKYNIEKDIAAHIKKEFDKKYNPTWHCIVGRNFGSYVTHETKHFIYFYLGQVAILLFKSG
Protein: Galanin receptor type 1 (GAL1-R) (GALR-1) (P47211)
Organism: Homo sapiens (Human)
Function: Receptor for the hormone galanin. The activity of this receptor is mediated by G proteins that inhibit adenylate cyclase activity.
Subcellular location: Cell membrane {ECO:0000269|PubMed:26365466}; Multi-pass membrane protein.
Interaction partners:
- Galanin peptides
- Galanin receptor type 2
- Galanin-like peptide
- Galanin receptor type 3
- Guanine nucleotide-binding protein G
- 5-hydroxytryptamine receptor 1A
- Guanine nucleotide-binding protein G
- Mu-type opioid receptor
- Guanine nucleotide-binding protein G
- Free fatty acid receptor 1
Sequence:
MELAVGNLSEGNASWPEPPAPEPGPLFGIGVENFVTLVVFGLIFALGVLGNSLVITVLARSKPGKPRSTTNLFILNLSIADLAYLLFCIPFQATVYALPTWVLGAFICKFIHYFFTVSMLVSIFTLAAMSVDRYVAIVHSRRSSSLRVSRNALLGVGCIWALSIAMASPVAYHQGLFHPRASNQTFCWEQWPDPRHKKAYVVCTFVFGYLLPLLLICFCYAKVLNHLHKKLKNMSKKSEASKKKTAQTVLVVVVVFGISWLPHHIIHLWAEFGVFPLTPASFLFRITAHCLAYSNSSVNPIIYAFLSENFRKAYKQVFKCHIRKDSHLSDTKESKSRIDTPPSTNCTHV
Protein: Homeobox protein vent1 (Vent-1) (Q28ET4)
Organism: Xenopus tropicalis (Western clawed frog) (Silurana tropicalis)
Function: Transcriptional repressor. Cooperates with vent2 in a ventral signaling pathway downstream of bmp4, which antagonizes the Spemann organizer and dorsal mesoderm formation, and leads to ventral mesoderm formation. Acts downstream of bmp4 to repress transcription of foxa4-B/XFD-1'. Binds to DNA with preference for the target sequence 5'-CTATT[T/C]G-3'. Also binds 5'-TGCATTTTG-3' at a lower frequency, and occasionally 5'-TTGATC-3'. Binds to the homeobox 2 (HBX2) repressor element in the promoter of the myf5 gene (By similarity). Cooperates with vent2 to repress myf5 expression in the ventral domain.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
Sequence:
MVQQGFSIDLILARNREEAPDGKDSVSSRPHIPCAPQPLAPTKYAKEIPRRKDGQEQGEITSFQCSSEEARNRQFSNPSLPALHRSSGSSDEFSPAGSEDDGTESSGRNSQENDTEHRSKSPKSDLQRRLRTAFTPQQITRLEQAFNKQRYLGASERKKLATSLQLSEIQVKTWFQNRRMKLKRQIQDQQHSMVPPPVCYPQTFSYYPGGFPVPLNSGSFYQPPAHPFQAPQHSFIPQPLHHHMRMSAHQEQFPPLFGAQYM
Protein: RAB5B, member RAS oncogene family (A0A8I6AII6)
Organism: Rattus norvegicus (Rat)
Interaction partners:
Sequence:
TSGRGARPNGQPQASKICQFKLVLLGESAVGKSSLVLRFVKGQFHEYQESTIGAAFLTQSVCLDDTTVKFEIWDTAGQERYHSLAPMYYRGAQAAIVVYDITNQETFARAKTWVKELQRQASPSIVIALAGNKADLANKRMVEYEEAQAYADDNSLLFMETSAKTAMNVNDLFLAIAKKLPKSEPQNPGGAAGRSRGVDLHEQAQQNKSQCCSN
Protein: FI18160p1 (Nuclear fallout, isoform A) (Nuclear fallout, isoform C) (Q9VUD7)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cleavage furrow {ECO:0000256|ARBA:ARBA00004626}. Midbody {ECO:0000256|ARBA:ARBA00004214}. Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004654}; Peripheral membrane protein {ECO:0000256|ARBA:ARBA00004654}.
Interaction partners:
Sequence:
MAPMPRIQLPNGNSSIKASTNDFLFAETMSGDSSPTPSSPPSSTAGVAKSQCSSLSDGESFEGYGENEYPTQLREARSSNSNGSHNMSNHINNNSNISVGNNSGHNHSGHSNDGNNNLNGSTGVELDLAPHVGSSTPQDDDELNIMPRDNWARRSLRRTPTSSGRRQISSNALASQLYRSSSFNSSGRSSNCDTTEDMYSDISLENRHDYDYRLELLQRKVDDLSDTQNIAEDRTTRTKTEYAVLQARYHMLEEQYRESELRAEERLAEEQKRHREILARVEREASLQNENCQMKIRATEIEATALREEAARLRVLCDKQANDLHRTEEQLELARDQIGVLQQEHEEQAQALRRHEQEKKSTEELMLELGRELQRAREESGARAMPTTSPESIRLEELHQELEEMRQKNRTLEEQNEELQATMLTNQATMLTNGVEQGRHLLNGTLNSLAQELEEMSQAQLQQAFQEKEDENVRLKHYIDTILLNIVENYPQLLEVKPMERK
Protein: Ras-related protein Rab-7a (EC 3.6.5.2) (Q95UJ0)
Organism: Paramecium octaurelia
Function: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endosomal migration and positioning, and endosome-lysosome transport through different protein-protein interaction cascades (By similarity). Involved in lipophagy, a cytosolic lipase-independent autophagic pathway (By similarity). Plays a role in phagocyte formation and acidification.
Subcellular location: Cytoplasmic vesicle, phagosome membrane {ECO:0000269|PubMed:12799062, ECO:0000269|PubMed:22030555}; Peripheral membrane protein {ECO:0000269|PubMed:12799062, ECO:0000269|PubMed:22030555}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cytoplasmic vesicle, autophagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lipid droplet {ECO:0000250|UniProtKB:P51150}. Cytoplasmic vesicle {ECO:0000250|UniProtKB:P51150}.
Interaction partners:
Sequence:
MASQKKQLFKIIILGDSGVGKTSLMNQYVNARFTQQYRATVGADFMAKEVMIDDRMVTLQIWDTAGQERFQSLGGAFYRGADCCVLVYDITNPKSFDSLDSWRDEFLMQGQPKDPEHFPFVVLGNKLDKATERKVQESKAQQWCKSHGNIQFFEVSAKDATNIEQAFQDIAKAAASQEKDEEIFFPTTVTLTKQSQKPQAKQGGCC
Protein: Probable cGMP 3',5'-cyclic phosphodiesterase subunit delta (DmPrBP) (Q9VLJ0)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Nucleus {ECO:0000269|PubMed:18503409}. Cytoplasm {ECO:0000269|PubMed:18503409}. Note=Expressed predominantly in the nucleus, with less intense staining in the cytoplasm.
Interaction partners:
- ADP-ribosylation factor-like protein 2
- ADP-ribosylation factor-like protein 3
- Guanylate kinase
- Inosine triphosphate pyrophosphatase
- Adenine phosphoribosyltransferase
- nucleoside diphosphate phosphatase
- GMP synthase
- Apyrase
- Protein unc-119 homolog
- Ras-like protein 1
Sequence:
MGSDDQSAGDRIQKGFQINYMILRDADSGKIIWQENKDFSAPDQEHEARVPVKILDMRAVSREINFSTIESMENFRLDQKVLFKGRIMEEWFFEMGFVGANTTNTWQSTIEAAPESQMMPAKVLNGNVTIQTSFYDNETLITKSVVRLYYI
Protein: Leucine-rich repeat protein (LRRP) (Q38FQ7)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
- Elongation factor Ts, mitochondrial
- phenylalanine--tRNA ligase
- Small ribosomal subunit protein uS4
- U3 small nucleolar ribonucleoprotein protein IMP3, putative
- Centromere/microtubule binding protein cbf5, putative
- Tetratricopeptide repeat domain 5
- CTP synthase
- Ribosomal protein
- rRNA biogenesis protein, putative
- Plastid-encoded RNA polymerase subunit alpha
Sequence:
MVDLLRSSLSQLNDGAELPYNGSSDIERRLLSGSVDDEEPGPSELSPAPQLLELGDLLGSRSGGFSSAPSLTVLMSAAEVEVAKSVHVALSISSTMEWAILYRQLRQRLCIGQVRQVDFSDVSLDNVQWSWLCQTMLPAMPNLVSLRLVRMGVTDRKLAELLRHSLAYAVGRKPGPSARRVDLPTVRGILPPLGEKTISSSDDLVPRRNEILSASRNGVRGYGPLRGLRILDLSENHLTHRSATLIGKLLLWSADTLDELRLMGNNLQDYGFQILSIYISRLRLASLRGEPHLFPPNLVRLYAQLVEREKVVGSQPYLQEEVQSPTYCPSFLGDCKTPTDDAGARKDSSGDEYPSIHLGVSLLDVRKCQASPRGISELLAAASAAHRLSTVLFSGNSAPTSLRSEPKQLGKRCGIQDAAGDPNASDDVVTTPPSTESKKVGDSSSTGSLLPSSACRFSNFAELKHPCMLTTVNLGGVPLSTLCTPLCCRNLFLNLLFCCPRLSVLDLSGTFDAAQLPAVAIRQIQFGNEQVLADNDIFQQSFNHEAEKLVDASVFALEKLMFDRQVCVGNIMCELFAHAALNAQRRHCPAPTAFRRLKEIHLEGTGISDAAVKGLTASVRTVVLTGVLAELTLLNVADNFLTSRGCVCLLHAFVIEWPLSVSSVEVVSLQQSRGIACGNIKAFEEVNRAALNAVKRRKEEQRRKSHVPSLLVHFGAYGAAVQTRSSNEEITLKGPRTDWKGATISHMCDRAPKPAAKRVCRSLGTSIGIIVSSSQCDEQHQEQLHTEKFLSETLLYAHQLDSVASMELRTARVDEYADVGEAQQWTPRCLHTESSLLQRLIADGSPPENMWFSTYNGPPQHEDSEVQCRSCASQVTVLPSSLGVEFGHLLGSREVTHDQDSGFLSKESVASLNDQSGGDDNDKRQGRGVTESGGVVHVSSQLIPEGGDILPHFHSPTRHAEPPHGTTTTALQAKKKRTIPNRVGRSSSTLQRKLKFRNKRNIIMRYYHRAGDTICRGWTLLRRDDAVGEHARARLEKDLLMCLQPPDGYCDDAVVESVTLLVDTSSSRSPTDDDKTSCDSGYINAEGNTSRLLVVSNESRSTLEKRLRSCVSQVDGGTAFPRFTKVMQVYGVDMVEVARGVLNAAPSHRRAYLGSVTAESFVHTHHGREDQLLEDLNDLLVGAADMPDEEQCAVTSPISSSARGRLKLKTGEAQISGGSVCFSAEEASLSNMEGAVSGERIRKRAKGSKGRDEEGETLHSNHGLSNGQINVKPASTLPKKTVAEGAIPHPIEPVPPSLDMSPRSVSSGLHGVNAEGERSVRSPSSPSGRTKAHLFVLPHREGSILCCGWRLLSRSDKVGEMARRELEADVLSFLQDTLEGKANPNLSNGNEGAGAKLSLRTERSSSAVISVRMVFDSSPPGMQLRVVTSFPHAAVSSGLVDLQQKEGEAAFPRFAGMFSTKATYNTVSSIEKHLQQRDTTGQVRPRVLEKYRTISALVHCFHDDEDGLLMELMLPGLKSLDAFVEAPSTAAKAQERTRKDSGKTTKGTISEDIHPSLPHADKEVESTKKPRRSGEGVDMGAREPAESRRVPRIELMNHALAVGPQKAPVATAQSAANNEASPPSTISSLSSSVNRQFDLVSQLPNEANGAPSVAQDSTEDNDESIATSMESVFAEKLRRLQYLSYNAIAHGALLLDRRQRHKNRICKGKWGRVCVTVAVEWDVFLVVYFVKHSAFRVSSRKSLVLVHPIASGVRCSVEVGGNAANDTHTSGNDVVIHVERHYDPETLGLTTSELEQRLQQLILTTVRKKEGAPSMCSNRNSQMNMAAGENSVISRHSSISAVGSAEHSNGSMFLTLMPTAAQLLNRQVTMRVTLKSAAKARRAVTAIHEAGERAVSMIRDTINEQRRQAAAAAARSLHT
Protein: UDP glucuronosyltransferase 5 family, polypeptide B2 (E7EZQ8)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Aldehyde oxidase 6
- Xanthine dehydrogenase/oxidase
- Aromatase
- Cytochrome P450, family 3, subfamily A, polypeptide 65
Sequence:
MNGQWFQVIWPITLTLLLPSVPVAQCGKVLVFPVDGSHWVNMNILVEALSAKGHDVTVMRTASSCYIKEFSPHYTSINLKSKGGYNKEVLEQFASRIMHILRDGSTWGHLKLQADMWQSFLKIFEAEREMIVNMIEDQQLMQSLKDAKYDLILTDPNMFGGVILGHYLKLPMVYNVRWAGYNEAHFSIAPSPLSYVPMPSLELSDRMSFLQRVYNVVMYIFIEIGAALVISPINDALAERFIGPGTSFLSLVQGADLWLHRVDFVFEYPRPTMPNVIYMAGFQCKPSKPLPQDLEDFVQSSGDHGVIIMSLGTLIDKLPDDVAEAIAEAFAELPQKIIWRYKGKRPSALGNNTLIMDWMPQNDLLGHPKTRAFVAHGGTNGIQEAIYHGVPIIGFGLIFDQPDNLSKMRVRGAAKNVDFATMNKESFLTTVKEVLYDPSYRENMQRLSRLHKDVPVKPLDNAIFWIEFVMRHKGAAHLRTESYKMPWYSYHSVDVILVLISAVSLIILSIYAVIRYFCCRICMRKTKIKHE