wanglab/gogpt-training-data huggingface dataset:
Protein: Phosphatidylinositol 3-kinase C2 domain-containing subunit gamma (PI3K-C2-gamma) (PtdIns-3-kinase C2 subunit gamma) (EC 2.7.1.137) (EC 2.7.1.154) (Phosphoinositide 3-kinase-C2-gamma) (O70167)
Organism: Mus musculus (Mouse)
Function: Generates phosphatidylinositol 3-phosphate (PtdIns3P) and phosphatidylinositol 3,4-bisphosphate (PtdIns(3,4)P2) that act as second messengers. May play a role in SDF1A-stimulated chemotaxis.
Subcellular location: Membrane {ECO:0000269|PubMed:9514948}; Peripheral membrane protein {ECO:0000269|PubMed:9514948}.
Interaction partners:
- Phosphatidylinositol-4-phosphate 3-kinase catalytic subunit type 2 beta
- Phosphatidylinositol 3-kinase regulatory subunit beta
- Phosphatidylinositol 3-kinase regulatory subunit alpha
- Phosphatidylinositol 4-phosphate 3-kinase C2 domain-containing subunit alpha
- Type II inositol 3,4-bisphosphate 4-phosphatase
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Phosphatidylinositol 4-phosphate 5-kinase type-1 alpha
- Phosphatidylinositol 3-kinase regulatory subunit gamma
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Inositol polyphosphate-4-phosphatase type I A
Sequence:
MAYSWQTEPNRTEPQEDGSDTQQFHHTNQHLSSRQVRLGFDQLVEEINNKTPLSESEKEEDTYFVPDAPNLGSKWPSIYETHPRYFSEFTSQSPDSSQLRFGKLSAIGFNPAVLPTHQLIHEGASWRNPSGKYHGIEYPRFDALPPSSTGQGECNPQGQSGTKHHNYCGEHEGNLPHHHSSYSIDSIPNREKRRSGDVNLVEPSLEFSKDSFLPRTSENVSVESTEPIGCPIEIVEVPQGSNKNLASFCNKVKKIRESYHASDINSNSGKIWAITTAYPSRLFADTKFRVKISIDNSAQLLLLMPHANYLVKDLIAEILLLCANEPLSPKEYLLSVCGSEEFLQMDHSLGSHKIFQKNKSVIQLHLQKNRDTPGKLSRKSEDDHSPFHLNQLLEFTHIWKISRQCLSTVMKKYNLHVEHLLKPQKDMEEKHLSSMVSGNQHTSQPHVNNVLEEVKNICSVLGCIETKQVSDAVKELNLILQRPSQNFHQNSETSKKGFIERVTAELSRSIYQLIDVYCSSFCTDFQPVHTPGGVSHVHAGLQSHLSFTVCSLHNVPETWAHSYKAFSFSCWLTYAGKKLCQVKSCRPLPVTKSFSLLVNWNEIINFPLEIKSLPRESMLVIKLFGIDSATHSTNLLAWTCLPLFPRQESVLGSRLFSVTLQSEPPIEMIAPGVWDGSQPSPLTLQIDFPDAGWEYLKPESEENRTDHEEPPRECLKHIAKLSQKKSPLLLSEEKRRYLWFYRLYCNNENSSLPLVLGSAPGWDEETVSEMHAILRRWTFSHPWEALGLLTSRFPDQDIREVAVQQLDTLLTDELLDCLPQLVQAVKFEWNLESPLVELLPRRPLQSIRVAHCLYWLLRDAQGEAYFKSWYQELLAALQFCAGEALNEELSKEQKLVKLLGDIGEKVKSASDPQRKDVLKKEIGSLEEFFKDIKTCHLPLNPALCIKGIDRDACSYFTSNASPLKITFINANPMGKNISVIFKAGDDLRQDMLALQIIQVMDNAWLQEGLDMQMITYGCLSTGRAQGFIEMVPDAVTLAKIHLHSGLIGPLKENTIKKWFSQHNHLKEDYEKALRNFFYSCAGWCVVTFILGVCDRHNDNIMLTKSGHMFHIDFGKFLGHAQTFGGIKRDRAPFIFTSEMEYFITEGGKNIQHFQDFVELCCRAYNIVRKHSQLILSLLEMMLHAGLPELRGIEDLKYVHNNLRPQDTDLEATSHFTKKIKESLECFPVKLNNLIHTLAQMPALSLAKPAPQTLLQESCILNKTRTIQRVTILGFSKTHSNLYLMEVTCSDNRRSLTKKSFEQFYRLHSQMQKQFSSLALPEFPHWWHLPFTDSDHKRIRDLSHYVEQVLRGSYEVANSDCVLSFFLSEHIQPTLEDSPFVDPGENSLDKSPKVQLLMTYEDSRLTILVKHLKNIHLPDGSVPSAHVEIYLLPHPSEVRRKKTKCVPKCTDPTYNEIVVYDEVLGLQGHVLMLIVKSKTVFVGAVNIQLCSVPLNEEKWYPLGNSII
Protein: Importin subunit alpha (Q9UB78)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MTSMEQNRLQNFKNKGKDQDEMRRRRNEVTVELRKNKREETILKRRNVPNLDSNTDEEEQLSSSIDLKKLAKAAADATKPEQQLAAVQAARKLLSLDKNPPINDLIQSDILPILVECLKQHNHTMLQFEAAWALTNIASGTSAQTNEVVAAGAVPLFLQLLNSPAPNVCEQAVWALGNIIGDGPFLRDFVIKHGVVQPLLSFIKPDIPITFLRNVTWVIVNLCRNKDPAPPTATIHEILPALNVLIHHTDTNILVDTVWAISYLTDGGNDQIQMVIESGVVPKLIPLLGNSEVKVQTAALRAVGNIVTGSDEQTQVVLNYDALSYFPGLLSHPKEKIRKEAVWFLSNITAGNQSQVQAVINVGLLPKIIENLSKGEFQTQKEAAWAISNLTISGNREQVFTLIKEGVIPPFCDLLSCQDTQVINVVLDGLNNMLKVADSHVEAVANCIEECEGLAKIERLQSHENVEIYKLAYEIIDQYFTDEGEQTNMAPSSDGAQYNFDPHADRLTMNSFNF
Protein: Factor in the germline alpha (FIGalpha) (Transcription factor FIGa) (O55208)
Organism: Mus musculus (Mouse)
Function: Germ-line specific transcription factor implicated in postnatal oocyte-specific gene expression. Plays a key regulatory role in the expression of multiple oocyte-specific genes, including those that initiate folliculogenesis and those that encode the zona pellucida (ZP1, ZP2 and ZP3) required for fertilization and early embryonic survival. Essential for oocytes to survive and form primordial follicles. The persistence of FIGLA in adult females suggests that it may regulate additional pathways that are essential for normal ovarian development. Binds to the E-box (5'-CANNTG-3') of the ZPs (ZP1, ZP2, ZP3) promoters.
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Homeobox protein NOBOX
- Bone morphogenetic protein 15
- Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 1
- LIM/homeobox protein Lhx8
- Growth/differentiation factor 9
- Zona pellucida sperm-binding protein 1
- Zona pellucida sperm-binding protein 3
- Zona pellucida sperm-binding protein 2
- Spermatogenesis- and oogenesis-specific basic helix-loop-helix-containing protein 2
- Deleted in azoospermia-like
Sequence:
MDTAPASPEPFLVTPQAEVLEELIQAQMGPLPRLAAICRLKRLPSGGYSTTDDLHLVLERRRVANAKERERIKNLNRGFAKLKALVPFLPQSRKPSKVDILKGATEYIQILGCVLEEAKVSEKQSPEEQTHSGRPSDPHVSSTRELLGNATQPTSCASGLKKEEEGPWAYAGHSEPLYSYHQSTVPETRSYFTH
Protein: Tryptase gamma (EC 3.4.21.-) (Serine protease 31) (Transmembrane tryptase) [Cleaved into: Tryptase gamma light chain; Tryptase gamma heavy chain] (Q9NRR2)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MALGACGLLLLLAVPGVSLRTLQPGCGRPQVSDAGGRIVGGHAAPAGAWPWQASLRLRRVHVCGGSLLSPQWVLTAAHCFSGSLNSSDYQVHLGELEITLSPHFSTVRQIILHSSPSGQPGTSGDIALVELSVPVTLSSRILPVCLPEASDDFCPGIRCWVTGWGYTREGEPLPPPYSLREVKVSVVDTETCRRDYPGPGGSILQPDMLCARGPGDACQDDSGGPLVCQVNGAWVQAGTVSWGEGCGRPNRPGVYTRVPAYVNWIRRHITASGGSESGYPRLPLLAGFFLPGLFLLLVSCVLLAKCLLHPSADGTPFPAPD
Protein: Competence protein A (Q4QNA6)
Organism: Haemophilus influenzae (strain 86-028NP)
Interaction partners:
Sequence:
MQFSLKNYRTLQIGIHRKQGYFDFVWFDDLEQPQSYQIFVNDRDFKNRFLQQLKTQYQGKTFPLQFVASIPAHLTWSKVLMLPQVLNAQECHQQCKFVIEKELPISLNELWFDYRSTSLKQGFRLDVTAIRKSTAQTYLQDFQPFKINVLDVASNAILRAFQYLLNEQVRSENTLFLFQEDDYCLAICERSQQSQILQSHENLTALYEQFTERFEGQLEQVFVYQIPSSHTPLPENWQRVETELPFIALGNALWQKDLHQQKVGG
Protein: LONg (Q18530)
Organism: Caenorhabditis elegans
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004609}; Lipid-anchor, GPI-anchor {ECO:0000256|ARBA:ARBA00004609}.
Interaction partners:
- GlyPicaN
- Probable syndecan
- Heparan-sulfate 6-O-sulfotransferase
- Heparan sulfate 2-O-sulfotransferase hst-2
- Sulfotransferase domain-containing protein
- Sulfotransferase domain-containing protein
- Protein dbl-1
- Protein lon-1
- D-glucuronyl C5-epimerase
- Serine/threonine-protein kinase receptor sma-6
Sequence:
MVFRWLILFVLLYRSVLPAEEVVVVDILTNSTSLEEPTEEYTCDCNTDDLIQKGNYTLTVEVKNMQVRLVEPFRDAIAFTTGEKKHLLDFIRFVTLREVRSTYPLLLNYTDFLNSFDEMIGTFRNILTTENAISLTGIKYEVSTAVQKFLSAILPDMFLCLSVGKCRTVPLDYHNCMMASTKHWSVYLGNTPNKMAMTISEAIYRYRKVEFLLVDMHKQLMNAHNLTLSHECLQEYVHTLPCNCTMAGITPCHTSCSNSMEKCFGKFSREWAAKLHLMRNMTSTKKSFLDEFLSLKKTIFSVIRIFIERKSYVYAEHVFNSCGPLGEMIIHPSKHSVHFQSPGPFVSRGDGAVRELQLSAKTWDRLGRKICDHSGVVLNPTMCYDGTKVISIDHDLLPITKDVRPRPMMDWIEKKNEKKANVEGSASNPLWDDEDSEDFDGSGSGMPPVIDRNPVKAIIQEDHPKNIDLSTNPKGPSVIVTEKEIQPDGSTTSSILICVIIVAVIKLF
Protein: K10 (VIRF-4) (F5H9D8)
Organism: Human herpesvirus 8 (HHV-8) (Kaposi's sarcoma-associated herpesvirus)
Interaction partners:
Sequence:
MPKAGGSEWATLWIIDALENNKFPYFSWFDRNNLLFAAPAPLPAGSDIPPGWYSVYHAFDEECDRVYGPSPVVGQTVYGRFGRLLRGTRRAVVRNDLRYSDTFGGSYVVWQLVRTPFKNCTYCYGAAYGPEKLQRFIQCLLSPPMQTTATRRSDTREQSYEEAGAAAPAPPKAPSGLRGRPRKSNRYYNVGDITTEQKAACSVWIPVNEGASTSGMGSSGTRQVTQASSFTWRVPGDPPAPSTLTGPSDPHSSGAGLPGTAPPKPQHETRLAGTVSGVSGVAQTPGDTGQLAPPMRDGSRLPSTSPWIPACFPWGDLPVTGWWPQGASGLPEKVHPPTTGQFDPLSPRWTYTGIPSSQLNPAAPSWIPPHAQAGTFVGEFSQGAPLAPQGLLPQSGQCASAWLPRRETGAEGACGASTEGRAPQGAASERVYPFEPQPPSAPAPGYAKPSCYNWSPLAEPPATRPIRAPVWHPPVGHAVVPEVRTPLWIPWSSGGAPNQGLSHTQGGASATPSAGAPPTPEVAERQEPSSSGIPYVCQGDNMATGYRRVTTSSGALEVEIIDLTGDSDTPSTTVASTPLPVSGPRVFQPTVLYSAPEPAVNPEVSHLPTELERRECVCPGSGERPRVPLVSTYAGDRYAVGGYGPEQSLVPPPLGLPLTLSNLQGEDICTWEEGLGNILSELQEEPSSSTRQATDRRRPRSRSPHGRRTPVSHSGPEKPPSKMFFDPPDSQRVSFVVEIFVYGNLRGTLRREGDAGEAMLCSWPVGDTLGHLCQSFVPELLRIPRLTVPSPEQMEILNRVFEGLGHGFPIFCSMSGIYSRNATQVEGWWFGNPNSRYERILRSFSPRVPQQLFNTARYLATTAAIPQTPLSVNPVTCGTVFFGASPASTENFQNVPLTVKIFIGSIWDSLH
Protein: Transmembrane protein 171 (Q8WVE6)
Organism: Homo sapiens (Human)
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSPAAAAEPDGDQQDRHVSKLIFCFFVFGAVLLCVGVLLSIFGFQACQYKPLPDCPMVLKVAGPACAVVGLGAVILARSRAQLQLRAGLQRGQQMDPDRAFICGESRQFAQCLIFGFLFLTSGMLISVLGIWVPGCGSNWAQEPLNETDTGDSEPRMCGFLSLQIMGPLIVLVGLCFFVVAHVKKRNTLNAGQDASEREEGQIQIMEPVQVTVGDSVIIFPPPPPPYFPESSASAVAESPGTNSLLPNENPPSYYSIFNYGRTPTSEGAASERDCESIYTISGTNSSSEASHTPHLPSELPPRYEEKENAAATFLPLSSEPSPP
Protein: Serine/threonine-protein kinase pim-2 (EC 2.7.11.1) (Pim-2h) (Q9P1W9)
Organism: Homo sapiens (Human)
Function: Proto-oncogene with serine/threonine kinase activity involved in cell survival and cell proliferation. Exerts its oncogenic activity through: the regulation of MYC transcriptional activity, the regulation of cell cycle progression, the regulation of cap-dependent protein translation and through survival signaling by phosphorylation of a pro-apoptotic protein, BAD. Phosphorylation of MYC leads to an increase of MYC protein stability and thereby an increase transcriptional activity. The stabilization of MYC exerted by PIM2 might explain partly the strong synergism between these 2 oncogenes in tumorigenesis. Regulates cap-dependent protein translation in a mammalian target of rapamycin complex 1 (mTORC1)-independent manner and in parallel to the PI3K-Akt pathway. Mediates survival signaling through phosphorylation of BAD, which induces release of the anti-apoptotic protein Bcl-X(L)/BCL2L1. Promotes cell survival in response to a variety of proliferative signals via positive regulation of the I-kappa-B kinase/NF-kappa-B cascade; this process requires phosphorylation of MAP3K8/COT. Promotes growth factor-independent proliferation by phosphorylation of cell cycle factors such as CDKN1A and CDKN1B. Involved in the positive regulation of chondrocyte survival and autophagy in the epiphyseal growth plate.
Interaction partners:
- Serine/threonine-protein kinase pim-1
Sequence:
MLTKPLQGPPAPPGTPTPPPGGKDREAFEAEYRLGPLLGKGGFGTVFAGHRLTDRLQVAIKVIPRNRVLGWSPLSDSVTCPLEVALLWKVGAGGGHPGVIRLLDWFETQEGFMLVLERPLPAQDLFDYITEKGPLGEGPSRCFFGQVVAAIQHCHSRGVVHRDIKDENILIDLRRGCAKLIDFGSGALLHDEPYTDFDGTRVYSPPEWISRHQYHALPATVWSLGILLYDMVCGDIPFERDQEILEAELHFPAHVSPDCCALIRRCLAPKPSSRPSLEEILLDPWMQTPAEDVPLNPSKGGPAPLAWSLLP
Protein: Slit homolog 1 protein (Slt-1) (G5EFX6)
Organism: Caenorhabditis elegans
Function: Functions as a ligand for sax-3 receptor during larval development. Acts via the sax-3/Robo receptor to direct ventral axon guidance and guidance at the midline during embryonic development.
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Protein sax-3
- Protein eva-1
- Netrin unc-6
- Netrin receptor unc-40
- Ig-like domain-containing protein
- Netrin receptor unc-5
- Ig-like domain-containing protein
- E3 ubiquitin-protein ligase TRIM9
- UNC-34
- LONg
Sequence:
MLICFIFILLIPESATCPAECVCVDRTVSCVGQQLTEVPQNIPNDTIRLDLQDNEITKIGPNDFSSLMNLKALQLMDNQIVTIHNQSFSSLVFLQKLRLSRNRIRHLPDNVFQNNLKLTHLDLSENDITVVSDAQLQGPEFLEVLNLDKNHIFCLENNVISSWVSLEVLTLNGNRLTTFEEPSNARFRQLDLFNNPWNCDCRLRWMRKWLEKAEGQNKTVCATPLNLQGSSIEILQDKFMTCSGNRKRRYKKTCETAEICPLPCTCTGTTVDCRDSGLTYVPTNLPPSTTEIRLEQNQISSIPSHSFKNLKNLTRLDLSKNIITEIQPKAFLGLHNLHTLVLYGNNITDLKSDTFEGLGSLQLLLLNANQLTCIRRGTFDHVPKLSMLSLYDNDIKSISEVTFQNLTSLSTLHLAKNPLICDCNLQWLAQINLQKNIETSGARCEQPKRLRKKKFATLPPNKFKCKGSESFVSMYADSCFIDSICPTQCDCYGTTVDCNKRGLNTIPTSIPRFATQLLLSGNNISTVDLNSNIHVLENLEVLDLSNNHITFINDKSFEKLSKLRELRLNDNKLHHFSSMVLDEQSNLEILDLSGNNIQCFSSIFFNKATRIREIKVIGNDLLCDCRILPLMSWLRSNSSHSIDIPPCQQFQYSDNESDKQRCAAFPEETCSDDSNLCPPKCSCLDRVVRCSNKNLTSFPSRIPFDTTELYLDANYINEIPAHDLNRLYSLTKLDLSHNRLISLENNTFSNLTRLSTLIISYNKLRCLQPLAFNGLNALRILSLHGNDISFLPQSAFSNLTSITHIAVGSNSLYCDCNMAWFSKWIKSKFIEAGIARCEYPNTVSNQLLLTAQPYQFTCDSKVPTKLATKCDLCLNSPCKNNAICETTSSRKYTCNCTPGFYGVHCENQIDACYGSPCLNNATCKVAQAGRFNCYCNKGFEGDYCEKNIDDCVNSKCENGGKCVDLINSYRCDCPMEYEGKHCEDKLEYCTKKLNPCENNGKCIPINGSYSCMCSPGFTGNNCETNIDDCKNVECQNGGSCVDGILSYDCLCRPGYAGQYCEIPPMMDMEYQKTDACQQSACGQGECVASQNSSDFTCKCHEGFSGPSCDRQMSVGFKNPGAYLALDPLASDGTITMTLRTTSKIGILLYYGDDHFVSAELYDGRVKLVYYIGNFPASHMYSSVKVNDGLPHRISIRTSERKCFLQIDKNPVQIVENSGKSDQLITKGKEMLYIGGLPIEKSQDAKRRFHVKNSESLKGCISSITINEVPINLQQALENVNTEQSCSATVNFCAGIDCGNGKCTNNALSPKGYMCQCDSHFSGEHCDEKRIKCDKQKFRRHHIENECRSVDRIKIAECNGYCGGEQNCCTAVKKKQRKVKMICKNGTTKISTVHIIRQCQCEPTKSVLSEK
Protein: Protein SPIRAL1-like 3 (Q9S7P8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts redundantly with SPR1 in maintaining the cortical microtubules organization essential for anisotropic cell growth.
Interaction partners:
- At2g40070
- Protein SMALL AUXIN UP-REGULATED RNA 54
- Kinesin-like protein KIN-5A
- Jacalin-related lectin 34
- 65-kDa microtubule-associated protein 1
- Tubulin beta-6 chain
- Protodermal factor 1
- Microtubule-associated protein TORTIFOLIA1
Sequence:
MGKARGVNNGVNESSLGYLFGSGQPSSAAAATMGTTTTTTTTTTTDGTGGRPITTTTTTVTDNKKTSAGVRGSPNNYFRSEGQNCGNFLTDRPSTKVHAAPGGGSSLDYLFGGPSPAGSGNK
Protein: Mitogen-activated protein kinase kinase kinase kinase 5 (EC 2.7.11.1) (Kinase homologous to SPS1/STE20) (KHS) (MAPK/ERK kinase kinase kinase 5) (MEK kinase kinase 5) (MEKKK 5) (Q9Y4K4)
Organism: Homo sapiens (Human)
Function: May play a role in the response to environmental stress. Appears to act upstream of the JUN N-terminal pathway.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:9038372}.
Interaction partners:
- Growth factor receptor-bound protein 2
- Adapter molecule crk
- Crk-like protein
Sequence:
MEAPLRPAADILRRNPQQDYELVQRVGSGTYGDVYKARNVHTGELAAVKIIKLEPGDDFSLIQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHTKGKMHRDIKGANILLTDHGDVKLADFGVAAKITATIAKRKSFIGTPYWMAPEVAAVEKNGGYNQLCDIWAVGITAIELGELQPPMFDLHPMRALFLMSKSNFQPPKLKDKTKWSSTFHNFVKIALTKNPKKRPTAERLLTHTFVAQPGLSRALAVELLDKVNNPDNHAHYTEADDDDFEPHAIIRHTIRSTNRNARAERTASEINFDKLQFEPPLRKETEARDEMGLSSDPNFMLQWNPFVDGANTGKSTSKRAIPPPLPPKPRISSYPEDNFPDEEKASTIKHCPDSESRAPQILRRQSSPSCGPVAETSSIGNGDGISKLMSENTEGSAQAPQLPRKKDKRDFPKPAINGLPPTPKVLMGACFSKVFDGCPLKINCATSWIHPDTKDQYIIFGTEDGIYTLNLNELHEATMEQLFPRKCTWLYVINNTLMSLSEGKTFQLYSHNLIALFEHAKKPGLAAHIQTHRFPDRILPRKFALTTKIPDTKGCHKCCIVRNPYTGHKYLCGALQSGIVLLQWYEPMQKFMLIKHFDFPLPSPLNVFEMLVIPEQEYPMVCVAISKGTESNQVVQFETINLNSASSWFTEIGAGSQQLDSIHVTQLERDTVLVCLDKFVKIVNLQGKLKSSKKLASELSFDFRIESVVCLQDSVLAFWKHGMQGKSFKSDEVTQEISDETRVFRLLGSDRVVVLESRPTENPTAHSNLYILAGHENSY
Protein: Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1C (Cam-PDE 1C) (EC 3.1.4.17) (Q63421)
Organism: Rattus norvegicus (Rat)
Function: Calmodulin-dependent cyclic nucleotide phosphodiesterase with a dual specificity for the second messengers cAMP and cGMP, which are key regulators of many important physiological processes. Has a high affinity for both cAMP and cGMP. Modulates the amplitude and duration of the cAMP signal in sensory cilia in response to odorant stimulation, hence contributing to the generation of action potentials. Regulates smooth muscle cell proliferation. Regulates the stability of growth factor receptors, including PDGFRB (By similarity).
Subcellular location: Lysosome {ECO:0000250|UniProtKB:Q64338}.
Interaction partners:
- Calmodulin-1
- Calmodulin-like protein 3
- Calmodulin-like protein 4
- Phosphodiesterase
- Dual specificity calcium/calmodulin-dependent 3',5'-cyclic nucleotide phosphodiesterase 1B
- Guanine nucleotide-binding protein G
- Adenosine kinase
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 3
- Ectonucleotide pyrophosphatase/phosphodiesterase family member 1
- Adenine phosphoribosyltransferase
Sequence:
MTDTSHKKEGFKKCRSATFSIDGYSFTIVANEAGDKNARPLARFSRSKSQNCLWNSLIDGLTGNVKEKPRPTIVQDTRPPEEILADELPQLDSPEALVKTSFRLRSLVKQLERGEASVVDLKKNLEYAATVLESVYIDETRRLLDTEDELSDIQSDAVPSEVRDWLASTFTRQMGMMLRRSDEKPRFKSIVHAVQAGIFVERMYRRTSNMVGLSYPPAVIDALKDVDTWSFDVFSLNEASGDHALKFIFYELLTRYDLISRFKIPISALVSFVEALEVGYSKHKNPYHNLMHAADVTQTVHYLLYKTGVANWLTELEIFAIIFSAAIHDYEHTGTTNNFHIQTRSDPAILYNDRSVLENHHLSAAYRLLQEDEEMNILVNLSKDDWREFRTLVIEMVMATDMSCHFQQIKAMKTALQQPEAIEKPKALSLMLHTADISHPAKAWDLHHRWTMSLLEEFFRQGDREAELGLPFSPLCDRKSTMVAQSQVGFIDFIVEPTFTVLTDMTEKIVSPLIDETSQTGGTGQRRSSLNSINSSDAKRSGVKSSGSEGSAPINNSVIPVDYKSFKATWTEVVQINRERWRAKVPKEEKAKKEAEEKARLAAEEKQKEMEAKSQAEQGTTSKAEKKTSGETKGQVNGTRTSKGDNPRGKNSKGDKAGEKQQNGDLKDGKNKADKKDHSNTGNESKKADGTKKRSHGSPAPSTSSTSRLTLPVIKPPLRHFKRPAYASSSYAPSVPKKTDDHPVRYKMLDQRIKIKKIQNISHHWNKK
Protein: Tripartite motif-containing protein 26 (EC 2.3.2.27) (Zinc finger protein 173) (Q99PN3)
Organism: Mus musculus (Mouse)
Function: E3 ubiquitin-protein ligase which regulates the IFN-beta production and antiviral response downstream of various DNA-encoded pattern-recognition receptors (PRRs). Promotes nuclear IRF3 ubiquitination and proteasomal degradation. Bridges together TBK1 and NEMO during the innate response to viral infection leading to the activation of TBK1.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q12899}. Nucleus {ECO:0000250|UniProtKB:Q12899}. Note=Viral infection mediates TRIM26 nuclear translocation. {ECO:0000250|UniProtKB:Q12899}.
Interaction partners:
- PHD finger protein 20
- E3 ubiquitin-protein ligase RNF26
Sequence:
MAVSAPLRSLEEEVTCSICLDYLRDPVTIDCGHVFCRSCTSDIRPISGNRPVCPLCKKPFKKENIRPVWQLASLVENIERLKVDNGRQPGELAREPQDMKLCERHQEKLHYYCEDDGKLLCVMCRESREHRPHTAVLVEKAALPHREKILNHLNTLRRDRDKIQGFQAKGEADILAALTKLQEQRQYIVAEFKQGHQFLKKREQHLLDQLATLEQLLTEGREKFKTRGVSELDRLTLVISELEGKARQPAAELMQDVCTTQDTKDFANKYPRKKFWIGKAIPHMVKRKAGEFSDKLLSLQRGLRQFQGKLLRDLEYKTVSVTLDPQSASGYLHLSEDWKCVTYTGQYQSDCLLPQQFDCEPGVLGSKGFTWGKVYWEVELEREGWSEDEEEGEEEEEGEEEEEDEEVGYGDGYEDWETDEEDESLGEEEEEEEEEEEEVQESCMVGVAKDSVKRKGDLSLRPEDGVWALRLSPSGIWANTSPEAQLFPVLRPRRVGIALDYEGGTVTFTNAESQELIYTFTTTFTRRLVPFLWLKWPGARLLLRP
Protein: Uncharacterized protein (Q4GYD1)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MIKNASPLHPYNIDAPMGTSLWRIGRSSQHRPSPECHTTVPDVVATVATDSMDSHHNSTEEKPSCCPRLRTPVRGDDYDGLFSHAWWRCSNCVHDPGLLAYGLHRTAALSSFQAAQQQTTCAARLNGCSHHANLGGNDCGGSYNFVRGCCGKFGCGHLPCRATAHGSVAEGVNPMRYWPQTNEYHSYNYPHAAGRAHEASELAPSGKPTTRAWYQVPCDTSELHPLSQPYNISERPSTPQCDAATASGGVEAPDWLTSRARARYEQSRSRSPVCTPCRSSPVLGGDVEGARGEAFAIHRFSCQLESLQRRLDALEAECVVKSGVMHGRPPPHGVGEMGSVYTADECPSNRSTAVAPTPSTPATPPPLPPEPKMSPMDSASHEGTTMKSPPYRQVWPHSTPSSPTAGASDNGGGITLERLMRAVRSARERARQQDCQTAASSNA
Protein: Rho GTPase activating protein at 5A, isoform A (Q9W4A9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Cdc42 homolog
- Ras-related protein Rac1
- Asperous, isoform A
Sequence:
MPRNTEAGAGNANTGGSGGVGGAPEPSSPVQKVWKPELYKLQLEAPAPCPLRCQRTLPLPPAKSTAEAVEANNLAGRLYGSEYHGLMGHLEAEQLLANARDGSYFVRRSPQSDGYYTLSLRFNKRPKHYKLLYKPGVGHYLRGQDKRFDTVHDMVADGLINFHMQLHASPIIQQINQQTKNCYQQSPYMTLNGRKLRALSNELGKAAAKESKESPAEEKEQKQEEPPPPAVDPMPLVYEKPHHFKVHTFKGLNWCEFCANFLWGFTAQGVKCEACGFVAHSKCSELVPPKCVPDLKRIRGVFGTDLTTMVQLEPHHQIPFVVRRCVEEVEARGMLQEGIYRVSGFADEIEALKLALDREGEKTDMSETAYGNVNVIAGTLKLYLRLLPVPLITFQAYPSFMAAGRTGKQAEQRQLMAEAVRRLPPAHHSCLQYMLEHLKRVASHYAVNKMNEHNLATVFAPTLIATPQHMTNLTEEIFMLSSLITHCKTIFATS
Protein: Four and a half LIM domains 1 (Q5JXI8)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MAEKFDCHYCRDPLQGKKYVQKDGHHCCLKCFDKFCANTCVECRKPIGADSKEVHYKNRFWHDTCFRCAKCLHPLANETFVAKDNKILCNKCTTREDSPKCKGCFKAIVAGDQNVEYKGTVWHKDCFTCSNCKQVIGTGSFFPKGEDFYCVTCHETKFAKHCVKCNKAITSGGITYQDQPWHADCFVCVTCSKKLAGQRFTAVEDQYYCVDCYKNFVAKKCAGCKNPITGFGKGSSVVAYEGQSWHDYCFHCKKCSV
Protein: Phenazine-1-carboxylate N-methyltransferase (EC 2.1.1.327) (Q9HWH2)
Organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Function: Involved in the biosynthesis of pyocyanine, a blue-pigmented phenazine derivative, which plays a role in virulence. Converts phenazine-1-carboxylate (PCA) to 5-methylphenazine-1-carboxylate (5-methyl-PCA).
Interaction partners:
- 5-methylphenazine-1-carboxylate 1-monooxygenase
- Phenazine biosynthesis protein PhzA1
- Phenazine biosynthesis protein PhzB1
- Phenazine biosynthesis protein PhzD1
- Trans-2,3-dihydro-3-hydroxyanthranilate isomerase
- asparagine synthase
- Probable pyridoxamine 5'-phosphate oxidase
- Phenazine biosynthesis protein PhzA2
- Phospho-2-dehydro-3-deoxyheptonate aldolase
- Elastase
Sequence:
MNNSNLAAARNLIQVVTGEWKSRCVYVATRLGLADLIESGIDSDETLAAAVGSDAERIHRLMRLLVAFEIFQGDTRDGYANTPTSHLLRDVEGSFRDMVLFYGEEFHAAWTPACEALLSGTPGFELAFGEDFYSYLKRCPDAGRRFLLAMKASNLAFHEIPRLLDFRGRSFVDVGGGSGELTKAILQAEPSARGVMLDREGSLGVARDNLSSLLAGERVSLVGGDMLQEVPSNGDIYLLSRIIGDLDEAASLRLLGNCREAMAGDGRVVVIERTISASEPSPMSVLWDVHLFMACAGRHRTTEEVVDLLGRGGFAVERIVDLPMETRMIVAARA
Protein: Endolysin gp144 (EC 4.2.2.n1) (Lysis protein) (Q8SD18)
Organism: Pseudomonas phage phiKZ
Interaction partners:
Sequence:
MKVLRKGDRGDEVCQLQTLLNLCGYDVGKPDGIFGNNTFNQVVKFQKDNCLDSDGIVGKNTWAELFSKYSPPIPYKTIPMPTANKSRAAATPVMNAVENATGVRSQLLLTFASIESAFDYEIKAKTSSATGWFQFLTGTWKTMIENYGMKYGVLTDPTGALRKDPRISALMGAELIKENMNILRPVLKREPTDTDLYLAHFFGPGAARRFLTTGQNELAATHFPKEAQANPSIFYNKDGSPKTIQEVYNLMDGKVAAHRK
Protein: MIP27520p (Peritrophin A, isoform C) (E3CTR7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MQRFQVCSVLILAWIACGHALAVGSPECPEKYGVQAYAHTENCDQFFLCTNGTLTLETCENGLLFDGKGAVHNHCNYNWAVDCKGRQWDPTPISTPACEYQFGLYAVSKDCSTTYIKCAHGEPHEQDCDAGLAYDERIHGCNWPDQLLEHCNPEGEI
Protein: Putative coatomer subunit alpha (Alpha-coat protein) (Alpha-COP) (Q96WV5)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity).
Subcellular location: Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein; Cytoplasmic side.
Interaction partners:
- Probable coatomer subunit epsilon
- Probable coatomer subunit beta'
- Coatomer subunit beta
- Coatomer subunit delta
- Probable coatomer subunit gamma
- Probable coatomer subunit zeta
- ADP-ribosylation factor GTPase-activating protein glo3
- Protein transport protein sec31
- Probable clathrin heavy chain
- ADP-ribosylation factor 1
Sequence:
MEMLTKFESRSSRAKGVAFHPTQPWILTSLHNGRIQLWDYRMGTLLDRFDGHDGPVRGIAFHPTQPLFVSGGDDYKVNVWNYKSRKLLFSLCGHMDYVRVCTFHHEYPWILSCSDDQTIRIWNWQSRNCIAILTGHSHYVMCAAFHPSEDLIVSASLDQTVRVWDISGLRMKNAAPVSMSLEDQLAQAHNSISNDLFGSTDAIVKFVLEGHDRGVNWCAFHPTLPLILSAGDDRLVKLWRMTASKAWEVDTCRGHFNNVSCCLFHPHQELILSASEDKTIRVWDLNRRTAVQTFRRDNDRFWFITVHPKLNLFAAAHDSGVMVFKLERERPAHALNINTLLYVNKEKSIVSYDLLRAQSTTVASVKHLGSAWLPPRSLSYNPAEKVALLTSSADNGVYELVNVSSRSNSLPLKDNIKGPGDDAIFVARNRFAVFSRSDQTIEIKDLSNKVTKTIQLPEKTRDIFFAGMGHVLLSTATQVHLFDLQQKKIVSSFNANRVKYVVWSNDNSQAALLGKHYVYIVKKNLELITSIHETIRIKSAVWVENNVLLYATLDHLKYALMSGDTGVIKTLESTLYLVKAKGNMVFALNRAAEPVSFEIDPTEYLFKLALLRKDYEQVLHLIQNSNLVGQAIIAYLQKKGYPEIALQFVEDPSTRFELALECGNLETALELARTIDRPEVWSRLASDAMSYGNHKIAEITFQKLRYFEKLSFLYLITGNAEKLQKMAIIAEKRNDTLSLFQNSLYLNEVESRINILEQAGMYPIAYLTAKSNGLEEKAQQILSHCNKTEEEIKLPSLGSAFTTPVPVNETYTHNWPLLDTSHSTFEKSLQERMEQLAIERQEEQESEEEYEEVEQSLMDVVDEMSDLAESVPEEEVDGWEVEDLAPEEAVNDVVDDASAFVGADEIFLWKRNSPLAADHIAAGDFESAMKILNKQVGAINFSPLKTRFLEIYTASRVYLPTISGLDPLVSYVRRNAETAERSQALPFITRNLASIKSHELHEAYRLVKANKILEAQICFRSIIYLALTTVANSEEEADEISALIDECCRYIVALSCELERRRLGEEDTKRALELSYYFASADLQPMHSIIALRLAINASHKLKNYKSASFLGNKLLQLAESGPAAEAANRAITLGDRNPHDAFEIEYDPHVEMRICPKTLTPVYSGDDFDVCSVCGAVYHKGYVNEVCTVCDVGGIGQKGTGRRFFA
Protein: Somatotropin-2 (Growth hormone 2) (P20332)
Organism: Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri)
Function: Growth hormone plays an important role in growth control and is involved in the regulation of several anabolic processes. Implicated as an osmoregulatory substance important for seawater adaptation.
Subcellular location: Secreted.
Interaction partners:
Sequence:
MGQVFLLMPVLLVSCFLGQGAAMENQRLFNIAVNRVQHLHLLAQKMFNDFEGTLLPDERRQLNKIFLLDFCNSDSIVSPIDKQETQKSSVLKLLHISFRLIESWEYPSQTLTISNSLMVRNSNQISEKLSDLKVGINLLIKGSQDGVLSLDDNDSQHLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCRKYLEANCTL
Protein: Uncharacterized protein C83.12 (O94696)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Interaction partners:
Sequence:
MKRVNFTISGHGYILIKPNYPDHFNYRLPADMKFYKCVLTINYISVSSMSGPFTGPYEKYSSGYFSEFGPQHLFSINRYHGLRFSRQSSQEYDSVGHILYSPITYYVSGAEHVTMDSIDQRREFQDSIYTHDSSDSENIMSDSSQSECDYADLMINLDKLI