wanglab/gogpt-training-data huggingface dataset:
Protein: Type 1 phosphatidylinositol 4,5-bisphosphate 4-phosphatase (Type 1 PtdIns-4,5-P2 4-Ptase) (EC 3.1.3.78) (PtdIns-4,5-P2 4-Ptase I) (Transmembrane protein 55B) (Q86T03)
Organism: Homo sapiens (Human)
Function: Catalyzes the hydrolysis of phosphatidylinositol-4,5-bisphosphate (PtdIns-4,5-P2) to phosphatidylinositol-4-phosphate (PtdIns-4-P). Does not hydrolyze phosphatidylinositol 3,4,5-trisphosphate, phosphatidylinositol 3,4-bisphosphate, inositol 3,5-bisphosphate, inositol 3,4-bisphosphate, phosphatidylinositol 5-monophosphate, phosphatidylinositol 4-monophosphate and phosphatidylinositol 3-monophosphate. Regulates lysosomal positioning by recruiting JIP4 to lysosomal membranes, thus inducing retrograde transport of lysosomes along microtubules. Contributes to assembly of the V-ATPase complex in lipid rafts of the lysosomal membrane and to subsequent amino acid-dependent activation of mTORC1. May play a role in the regulation of cellular cholesterol metabolism.
Subcellular location: Late endosome membrane {ECO:0000269|PubMed:16365287}; Multi-pass membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:16365287}; Multi-pass membrane protein {ECO:0000255}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q3TWL2}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:Q3TWL2}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- C-Jun-amino-terminal kinase-interacting protein 4
- Phosphatidylinositol 5-phosphate 4-kinase type-2 alpha
- Phosphatidylinositol-3,5-bisphosphate 3-phosphatase MTMR4
- 1-phosphatidylinositol 3-phosphate 5-kinase
- Phosphatidylinositol 5-phosphate 4-kinase type-2 gamma
- Myotubularin
- Phosphatidylinositol 5-phosphate 4-kinase type-2 beta
- Phosphatidylinositol polyphosphate 5-phosphatase type IV
- Phosphatidylinositol 4-phosphate 5-kinase type-1 beta
- Inositol polyphosphate 5-phosphatase OCRL
Sequence:
MAADGERSPLLSEPIDGGAGGNGLVGPGGSGAGPGGGLTPSAPPYGAAFPPFPEGHPAVLPGEDPPPYSPLTSPDSGSAPMITCRVCQSLINVEGKMHQHVVKCGVCNEATPIKNAPPGKKYVRCPCNCLLICKVTSQRIACPRPYCKRIINLGPVHPGPLSPEPQPMGVRVICGHCKNTFLWTEFTDRTLARCPHCRKVSSIGRRYPRKRCICCFLLGLLLAVTATGLAFGTWKHARRYGGIYAAWAFVILLAVLCLGRALYWACMKVSHPVQNFS
Protein: Acyl-lipid 8-desaturase (EC 1.14.19.-) (Delta-8 desaturase) (A4KDP1)
Organism: Rebecca salina (Marine microalga) (Pavlova salina)
Function: Fatty acid desaturase that introduces a cis double bond at the 8-position in 20-carbon polyunsaturated fatty acids incorporated in a glycerolipid that contain a Delta(8) double bond to yield (20:4(8,11,14,17)).
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MGRGGDSSGQAHPAAELAVPSDRAEVSNADSKALHIVLYGKRVDVTKFQRTHPGGSKVFRIFQDRDATEQFESYHSKRAIKMMEGMLKKSEDAPADTPLPSQSPMGKDFKAMIERHVAAGYYDPCPLDELFKLSLVLLPTFAGMYMLKAGVGSPLCGALMVSFGWYLDGWLAHDYLHHSVFKGSVARTVGWNNAAGYFLGFVQGYAVEWWRARHNTHHVCTNEDGSDPDIKTAPLLIYVRNKPSIAKRLNAFQRYQQYYYVPVMAILDLYWRLESIAYVAMRLPKMLPQALALVAHYAIVAWVFAGNYHLLPLVTVLRGFGTGITVFATHYGEDILDADQVRHMTLVEQTALTSRNISGGWLVNVLTGFISLQTEHHLFPMMPTGNLMTIQPEVRAFFKKHGLEYREGNLIECVRQNIRALAFEHLL
Protein: DNA-directed RNA polymerase II subunit RPB4 (RNA polymerase II subunit B4) (B32) (DNA-directed RNA polymerase II 32 kDa polypeptide) (P20433)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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. RPB4 is part of a subcomplex with RPB7 that binds to a pocket formed by RPB1, RPB2 and RPB6 at the base of the clamp element. The RBP4-RPB7 subcomplex seems to lock the clamp via RPB7 in the closed conformation thus preventing double-stranded DNA to enter the active site cleft. The RPB4-RPB7 subcomplex binds single-stranded DNA and RNA. The RPB4-RPB7 subcomplex is necessary for promoter-directed transcription initiation but is not required for recruitment of Pol II to active preinitiation complexes and seems to be dispensable for transcription elongation and termination. The RPB4-RPB7 subcomplex recruits FCP1 to Pol II. Involved in DNA repair of damage in the transcribed strand. RPB4 is dispensable under optimal growth conditions, but becomes essential during heat or cold shock and under nutrient depletion. Suppresses the RBP9-mediated transcription-coupled repair (TCR) subpathway of nucleotide excision repair (NER) but facilitates the RAD26-mediated TCR subpathway. Under stress conditions only, involved in mRNA export to the cytoplasm. Involved in mRNA decay. Promotes or enhances the deadenylation process of specific mRNAs and may recruit PAT1 and the LSM1-7 complex to these mRNAs, thus stimulating their decapping and further decay.
Subcellular location: Nucleus. Cytoplasm. Cytoplasm, P-body. Note=Seems to shuttle between nucleus and cytoplasm in a complex with RPB7.
Interaction partners:
- DNA-directed RNA polymerase II subunit RPB7
- DNA-directed RNA polymerases I, II, and III subunit RPABC5
- DNA-directed RNA polymerase II subunit RPB11
- DNA-directed RNA polymerase II subunit RPB1
- DNA-directed RNA polymerases I, II, and III subunit RPABC4
- RNA polymerase II subunit B1 CTD phosphatase RTR1
- DNA-directed RNA polymerases I, II, and III subunit RPABC1
- Transcription initiation factor IIB
- DNA-directed RNA polymerase II subunit RPB9
- DNA-directed RNA polymerases I, II, and III subunit RPABC3
Sequence:
MNVSTSTFQTRRRRLKKVEEEENAATLQLGQEFQLKQINHQGEEEELIALNLSEARLVIKEALVERRRAFKRSQKKHKKKHLKHENANDETTAVEDEDDDLDEDDVNADDDDFMHSETREKELESIDVLLEQTTGGNNKDLKNTMQYLTNFSRFRDQETVGAVIQLLKSTGLHPFEVAQLGSLACDTADEAKTLIPSLNNKISDDELERILKELSNLETLY
Protein: Candida glabrata strain CBS138 chromosome G complete sequence (Q6FT65)
Organism: Candida glabrata (strain ATCC 2001 / BCRC 20586 / JCM 3761 / NBRC 0622 / NRRL Y-65 / CBS 138) (Yeast) (Nakaseomyces glabratus)
Interaction partners:
- L1c
- Large ribosomal subunit protein uL3
- 60S ribosomal protein L27
- L2
- Candida glabrata strain CBS138 chromosome H complete sequence
- 40S ribosomal protein S26
- 60S ribosomal protein L29
- Candida glabrata strain CBS138 chromosome F complete sequence
- Large ribosomal subunit protein eL31
- Ribosomal protein L37
Sequence:
MGRMHSSGKGISSSAIPYSRNAPAWFKTSTESVIEQIIKYARKGLTPSQIGVLLRDAHGVTQARVITGNKIMRILKSNGLAPEIPEDLYYLIKKAVSVRKHLERNRKDKDAKFRLILIESRIHRLARYYRTVAVLPPNWKYESATASALVN
Protein: Ferritin (Q6NZ44)
Organism: Homo sapiens (Human)
Subcellular location: Cytoplasmic vesicle, autophagosome {ECO:0000256|ARBA:ARBA00004419}.
Interaction partners:
Sequence:
MTTASTSQVRQNYHQDSEAAINRQINLELYASYVYLSMSYYFDRDDVALKNFAKYFLHQSHEEREHAEKLMKLQNQRGGRIFLQDIKEPDCDDWESGQNAMECALHLEKNVNQSLLELHKLATDKNDPHLCDFIETHYLNEQVKAIKELGDHVTNLRKMGAPESGLAEYLFDKHTLGDSDNES
Protein: Inactive peptidyl-prolyl cis-trans isomerase shutdown (Q9W1I9)
Organism: Drosophila melanogaster (Fruit fly)
Function: Co-chaperone required during oogenesis to repress transposable elements and prevent their mobilization, which is essential for the germline integrity. Acts via the piRNA metabolic process, which mediates the repression of transposable elements during meiosis by forming complexes composed of piRNAs and Piwi proteins and govern the methylation and subsequent repression of transposons. Acts as a co-chaperone via its interaction with Hsp83/HSP90 and is required for the biogenesis of all three piRNA major populations.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:10978289, ECO:0000269|PubMed:22902557}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:22902557}. Note=Localizes to the cytoplasm but is enriched in the perinuclear meiotic nuage (also known as germline granule or P granule), a germline-specific membraneless ribonucleoprotein biocondensate involved in post-transcriptional regulation of transposons and mRNAs (PubMed:22902557). Also enriched in Yb bodies (PubMed:22902557). {ECO:0000269|PubMed:22902557}.
Interaction partners:
- Protein vreteno
- Putative ATP-dependent RNA helicase SoYb
- Probable RNA helicase armi
- GH09064p
- Mitochondrial cardiolipin hydrolase
- Protein aubergine
- Tudor domain-containing protein krimp
- Protein piwi
- Putative ATP-dependent RNA helicase BoYb
- Probable ATP-dependent RNA helicase spindle-E
Sequence:
MEENFEPYTPQLLKNPLSYSDLVKKGVEFEVDNSQQNHARDLGLDSDSDSDYEDALDVDGEELRSPWTYSFDELRALMSEIDENIYKRITRTGHVDREAVPNKARVSVRYSGYWEGETAPFDSSLLRGSKFVFETGQGTVVEGLEVAVRSMRPYEQAEFIISYKLLFGELGCPPRIKPKADALFKVEVIDYSLIGDAKGIDAIPQEDRDKFCVVYPKAVDLHLHGKDSVKLGRYQSAATAFERAVSSLNYCRMANDEEERKQTELLTTLNQNLMIVYNKMNKPKRACIMMKALRHLTMGNPSCKALFQEGRALAALGEYNLARNAYLQAQAKQPANKEISDEIISMNKRISKYEEASRDIWARAFSLKNSKSDVRKTPAQLEKEAKEQDFNDKMEDLIRRFKNTSDQQVSFSRKSYSNAQFDATCKLAKEHNLKLTLSPIQEDVLTLSKPDVKFA
Protein: Spermatogenesis-associated protein 25 (Testis-specific gene 23 protein) (Q9DA57)
Organism: Mus musculus (Mouse)
Function: May play a role in spermatogenesis.
Subcellular location: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}.
Interaction partners:
Sequence:
MSYFVSPQSHLGLLPSGQGGAASSGSSLGLYSPAEPVVVAPGGLGPLSQKAEQVAPAAQAWGPTLAVPEARGCSGGVSWETPRRKEHNRYCPKLPPMRPLESLGWADPCSRSRAPYLGGPSRPRPLLLCGLSPGVLPISSEAGGKEAASQPDICILTLAMMIAGIPTVPVPGLREEDLIRAAQAFMMAHPEPEGAVEGVQWEQAHAHAHMASGQMPLVRSRRGSCL
Protein: Small monomeric GTPase (O17599)
Organism: Caenorhabditis elegans
Subcellular location: Recycling endosome membrane {ECO:0000256|ARBA:ARBA00004523}; Lipid-anchor {ECO:0000256|ARBA:ARBA00004523}; Cytoplasmic side {ECO:0000256|ARBA:ARBA00004523}.
Interaction partners:
- F-BAR domain-containing protein
- Rap guanine nucleotide exchange factor 1
- Protein shank
- Rap guanine nucleotide exchange factor
Sequence:
MREFKVVVLGSGGVGKSALTVQFVSSTFIEKYDPTIEDFYRKEIEVDGQPSVLEILDTAGTEQFSSMRDLYIKNGQGFVVVYSITSQQTFHDIRNMKEQIVRVKGSENVPILLVGNKCDLSHQRQVRSEEGLALAESWSCPFTECSAKNNQNVNVTFAEIVREMNYVQNKSRQSKSCCSLM
Protein: Rabaptin-5-associated exchange factor for Rab5 (SD03358p) (Q9W0H9)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- LD23155p
- Ras-related protein Rab5
- Ras-related protein Rab-21
- LD47384p
- LD44910p
- Ubiquitin-ribosomal protein eS31 fusion protein
- Ubiquitin-ribosomal protein eL40 fusion protein
- Vacuolar fusion protein MON1 homolog
- GH17761p
- Polyubiquitin
Sequence:
MSTAARPPSLRLGQQDLKCRSGCGFYGTPQNEGLCSMCFREKFNDKQRKLKQTGGETGPGSSSSVATLDRRSPQHAHLQGKVEQQVRKPSDKEQDNLGTLQKKKFTAVLQKTLQAGAQKITQQRGHVPDPTEGQFLLQLRQLRIPDDGKRKLKLEIQRLDSDIRKYMNGNGGKNINELSDLVQNAYTKVSDIVHNDPSFEIATNEDRDSAIDFFEKVVMTQNHKFLFSPYFTTDEDSDVKVQKRIRQLSWITAKHLDCSIDEVNSEARDLVYNAISELVGIDSYYSPQEKLQCTWRCCRHIFELLKRATGGPASADDFLPALIFVVLKANPVRLHSNINFVTRFTNASRLMSGESGYYFTNLCSAIAFIENLNGESLGVSSEEFEALMSGQQPYSTPWESALLACESLHLISENMKRMEMLQKRNALISSGITSFEKELIDFQREVTERVDTVIAKAPLNLLPIKTPAFLIGQARAHLLNESEAGHYQANMLHGGSLTSQSLTAAGGLVKPAAASKESGLSLKDTSMSSMGRLSPLQQNVQPADHLFASPIFNYTAFDAVSLLEEPVPDANTDVLMLGSEFQGGLTNINYDFDLSDQSGENSTADESKLNLDEFDPLAQKGLVAKPPPPLPETSLLDSTTDSLIDSEVPGTAVLLPSPLKPEVSNYRGFSNFDIPSISCNTGDFSSLGQDGADAPK
Protein: E3 ubiquitin-protein ligase Nedd-4 (DNedd4) (EC 2.3.2.26) (HECT-type E3 ubiquitin transferase NEDD4) (Q9VVI3)
Organism: Drosophila melanogaster (Fruit fly)
Function: Essential E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Down-regulates Notch/N signaling pathway by promoting Notch ubiquitination, endocytosis and degradation.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:15620649}.
Interaction partners:
- E3 ubiquitin-protein ligase Su
- E3 ubiquitin-protein ligase CBL
- GH01161p
- Protein commissureless 1
- E3 ubiquitin-protein ligase Smurf1
- Mothers against decapentaplegic homolog
- E3 ubiquitin-protein ligase NRDP1
- E3 ubiquitin-protein ligase NRDP1
- Mothers against decapentaplegic homolog
- Nedd4 family interacting protein
Sequence:
MSARSSGLVAAAALPVPSSSSSVAGGDVPRPPPRRRAASVAGQQQTRQEFGNGYTPRRSLAAVNDSGDSCHLRIVVLTGQSLAKKDIFGASDPYVRIDLNTINGDINIDSVLTKTKKKTLNPTWNEEFIFRVKPSEHKLVFQVFDENRLTRDDFLGMVELTLVNLPTEQEGRTIGEQSYTLRPRRSVGAKSRIKGTLRIYHAFIRETREQSEPSSGNSDGEWEHVEATNAGETSAQPHPFPTGGHDALPAGWEERQDANGRTYYVNHTARTTQWDRPTVLNSHSSQSTDDQLASDFQRRFHISVDDTESGRSADSISHNSIEDNNNAAGLAYTPKTAATSSAPPNTPTNNNGILAQIAMQYRAEEDQDPTVDHTSFVYNSLRHPVAHRQPEISATSLQNDLRPVREAPGVPDIAITNPFTRRAAGNMAGGAGWQQERRRQQMQLHIQQHQQRQQQQQQNRILLDVDHRQQEPQHRGQRHQQQHRPSNEDTDHTDSHNPSDISAPSTRRNSEEDNAAVPPMEQNTGGEEEPLPPRWSMQVAPNGRTFFIDHASRRTTWIDPRNGRASPMPNQTRRVEDDLGPLPEGWEERVHTDGRVFYIDHNTRTTQWEDPRLSNPNIAGQAVPYSRDYKQKYEYFKSHIRKPTNVPNKFEIRIRRTSILEDSYRIISSVTKTDLLKTKLWVEFEGETGLDYGGLAREWFYLLSKEMFNPYYGLFEYSAMDNYTLQINNGSGLCNEEHLSYFKFIGRIAGMAVYHGKLLDAFFIRPFYKMMLQKPIDLKDMESVDTEYYNSLMWIKENDPRILELTFCLDEDVFGQKSQHELKPGGANIDVTNENKDEYIKLVIEWRFVARVKEQMSSFLDGFGSIIPLNLIKIFDEHELELLMCGIQNIDVKDWRENTLYKGDYHMNHIIIQWFWRAVLSFSNEMRSRLLQFVTGTSRVPMNGFKELYGSNGPQMFTIEKWGTPNNFPRAHTCFNRLDLPPYEGYLQLKDKLIKAIEGSQGFAGVD
Protein: CCN family member 3 (Cellular communication network factor 3) (Nephroblastoma-overexpressed gene protein homolog) (Protein NOV homolog) (NovH) (Q9QZQ5)
Organism: Rattus norvegicus (Rat)
Function: Immediate-early protein playing a role in various cellular processes including proliferation, adhesion, migration, differentiation and survival. Acts by binding to integrins or membrane receptors such as NOTCH1. Essential regulator of hematopoietic stem and progenitor cell function. Inhibits myogenic differentiation through the activation of Notch-signaling pathway. Inhibits vascular smooth muscle cells proliferation by increasing expression of cell-cycle regulators such as CDKN2B or CDKN1A independently of TGFB1 signaling. Ligand of integrins ITGAV:ITGB3 and ITGA5:ITGB1, acts directly upon endothelial cells to stimulate pro-angiogenic activities and induces angiogenesis. In endothelial cells, supports cell adhesion, induces directed cell migration (chemotaxis) and promotes cell survival. Also plays a role in cutaneous wound healing acting as integrin receptor ligand. Supports skin fibroblast adhesion through ITGA5:ITGB1 and ITGA6:ITGB1 and induces fibroblast chemotaxis through ITGAV:ITGB5. Seems to enhance bFGF-induced DNA synthesis in fibroblasts (By similarity). Involved in bone regeneration as a negative regulator (By similarity). Enhances the articular chondrocytic phenotype, whereas it repressed the one representing endochondral ossification. Impairs pancreatic beta-cell function, inhibits beta-cell proliferation and insulin secretion (By similarity). Plays a role as negative regulator of endothelial pro-inflammatory activation reducing monocyte adhesion, its anti-inflammatory effects occur secondary to the inhibition of NF-kappaB signaling pathway (By similarity). Contributes to the control and coordination of inflammatory processes in atherosclerosis (By similarity). Attenuates inflammatory pain through regulation of IL1B- and TNF-induced MMP9, MMP2 and CCL2 expression. Inhibits MMP9 expression through ITGB1 engagement.
Subcellular location: Secreted {ECO:0000269|PubMed:15213231}. Cytoplasm {ECO:0000269|PubMed:15213231, ECO:0000269|PubMed:22353423}. Cell junction, gap junction {ECO:0000269|PubMed:15213231}. Note=Localizes at the gap junction in presence of GJA1. {ECO:0000269|PubMed:15213231}.
Interaction partners:
- Neurogenic locus notch homolog protein 1
Sequence:
MSVFLRKQCLCLGFLLLHLLNQVSATLRCPSRCPSQCPSISPTCAPGVRSVLDGCSCCPVCARQRGESCSEMRPCDQSSGLYCDRSADPNNETGICMVPEGDNCVFDGVIYRNGEKFEPNCQYHCTCRDGQIGCVPRCQLDVLLPGPDCPAPKKVAVPGECCEKWTCGSEEKGTLGGLALPAYRPEATVGVELSDSSINCIEQTTEWSACSKSCGMGLSTRVTNRNLQCEMVKQTRLCMVRPCEQEPGEATDMKGKKCLRTKKSLKSIHLQFKNCTSLYTYKPRFCGICSDGRCCTPFNTKTIQVEFQCLPGQIIKKPVMVIGTCTCHSNCPQNNEAFLQELELKTSRGEM
Protein: GTP-binding protein 8 (Q9CY28)
Organism: Mus musculus (Mouse)
Interaction partners:
- Mitochondrial ribosome-associated GTPase 1
- 5-taurinomethyluridine-[tRNA] synthase subunit GTPB3, mitochondrial
- Mitochondrial assembly of ribosomal large subunit protein 1
- rRNA methyltransferase 3, mitochondrial
- Large ribosomal subunit protein bL17m
- Large ribosomal subunit protein bL21m
- Large ribosomal subunit protein uL3m
- Large ribosomal subunit protein uL14
- Large ribosomal subunit protein uL13m
- Large ribosomal subunit protein uL24m
Sequence:
MAAARLSHRMGRLLEKAPALGPWTRVYSTSPAFAEVLRLPQKQLTKVVYPLRELGQHLAADSGPGLIEQRLFDPSLEDIGRAESIFEATARNRIEYLSSAVRLDHAPSLQQPEVCFIGRSNVGKSSLIKALFSLAPDVEVRISKKPGHTKKMNFFKVGKHFTLVDMPGYGYRAPEDFVDMVETYLKERNNLKRTFLLVDSVVGITKLDNIAIEMCEEFALPYVMILTKIDKSSKGYLLKQVLQIQKFVNTQTQGCFPQLFPISAVTNSGVHLLKCFIADITGSLK
Protein: Cation transporter, putative (Q384C9)
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:
MLGANLGINFHTDDDHGDHGDHEGHEGHDMGGCAPAAGSYSMGLHIAAIFILLIASFLGTVLPIAGNYVPRFKLPPFLIVVSKCISTGVVMSVAVLTLLNHSLHSFMEKCIPHGLSMEVYSAFGLLFMLISALLMHSFDSAMDLLLEGWAVRKEEEKLADGAPQVADSVPTAAALPPTQCGMKRCTAQPGVSCETNGCCQSSPGPAYGATGCCGSRGEAAALLTGARRVMALALMEFGLVVHSIFLGLSVGIASDSRTKVLLVALSFHQFFEGLALGARLAEASLKAKLELFLAILFSISVPVGTAIGAVTMRDGGKSITGSSYVTMSAIVNAIGAGILLYIGFVLLLVDFPTDLRIYAGVGTPNRFVRRIAMFVALWVGFGVMALLSKWH
Protein: Polymerase/histidinol phosphatase-like protein (F4JXF0)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MGFFDLSIPYNEPPRSGGKEIAGGKTLRLKLATKAMELGYVGIAHNRSIKGVMSDKDSCTIPLLTLGSLIKVAPRLASSVGFHRDLLGVPRTTPFRQYTRLTVHVESNAQCQSLNSGNPILKSYDIIAVRPMNQNAFDYACEKAEVDLISIDFTDKMLFRLKHPMVKAAIQRGIYFEIKYSDILMDAQTRRQVISNAKLLVDWTRGKNLIISSGAPSVTELRGPNDVINLMFLLGLSAERARAAISKNCRNMIAKVLKKKRFHKEAVRVELLSAGDTFSLEQPLSEDCMKWDRLSSGEGDMLLDDLAKAFDATNVVAHKSSKAIDFTSVLDGLPKHGFRVKDIVGTESVTQPSAAKVIDTQVHSSNQVSELRMATASSDDNLREIETISQIDMLMSEDDNKVEPTTNVLKEEAFALRKCSASHGQGILVQNQTATPFTLTRCTKSEAASDVSMNIESTSEGGSMSPSKSDHGIPQSPVEVNNMGNAAFEEEASVDENSKERATTGHASNDEMHITESGHHASIDDEKHIPEPEHLTSIADEMKIDCSSEANHDEYMEVTMEDQMHETGDSKIILPNLSSETTDLLSESGKSLSPDAVVQDHDEASRLESDETKLEEEASVPNHNTFEITMEDNKVEELTIEDEKVEKTETEASHQAQVQSSENNNDTKSGKTQAKRSRVRLPQLRPFKPFLLQSRFKRISKKRKH
Protein: CREB (Q9W618)
Organism: Taeniopygia guttata (Zebra finch) (Poephila guttata)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MTMESGAENQQSGDAAGTEAETQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETAAPAIATVTVPTPIYQTSSGQYIAITQGGAIQLSNNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD
Protein: N-myc proto-oncogene protein (Class E basic helix-loop-helix protein 37) (bHLHe37) (P04198)
Organism: Homo sapiens (Human)
Function: Positively regulates the transcription of MYCNOS in neuroblastoma cells.
Subcellular location: Nucleus.
Interaction partners:
- Aurora kinase A
- Protein max
- N-myc-interactor
- Histone-lysine N-methyltransferase EZH2
- Protein NDRG1
- Myc proto-oncogene protein
- ALK tyrosine kinase receptor
- Histone deacetylase 1
- Transcription factor E2F1
- Bromodomain-containing protein 4
Sequence:
MPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELILKRCLPIHQQHNYAAPSPYVESEDAPPQKKIKSEASPRPLKSVIPPKAKSLSPRNSDSEDSERRRNHNILERQRRNDLRSSFLTLRDHVPELVKNEKAAKVVILKKATEYVHSLQAEEHQLLLEKEKLQARQQQLLKKIEHARTC
Protein: Transcription factor TCP9 (O64647)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000305}.
Interaction partners:
- Transcription factor TCP4
- Transcription factor TCP3
- Transcription factor TCP12
- Transcription factor TCP17
Sequence:
MATIQKLEEVAGKDQTLRAVDLTIINGVRNVETSRPFQVNPTVSLEPKAEPVMPSFSMSLAPPSSTGPPLKRASTKDRHTKVEGRGRRIRMPATCAARIFQLTRELGHKSDGETIRWLLENAEPAIIAATGTGTVPAIAMSVNGTLKIPTTTNADSDMGENLMKKKRKRPSNSEYIDISDAVSASSGLAPIATTTTIQPPQALASSTVAQQLLPQGMYPMWAIPSNAMIPTVGAFFLIPQIAGPSNQPQLLAFPAAAASPSSYVAAVQQASTMARPPPLQVVPSSGFVSVSDVSGSNLSRATSVMAPSSSSGVTTGSSSSIATTTTHTLRDFSLEIYEKQELHQFMSTTTARSSNH
Protein: Methionine synthase reductase (MSR) (EC 1.16.1.8) (Aquacobalamin reductase) (AqCbl reductase) (Q8C1A3)
Organism: Mus musculus (Mouse)
Function: Key enzyme in methionine and folate homeostasis responsible for the reactivation of methionine synthase (MTR/MS) activity by catalyzing the reductive methylation of MTR-bound cob(II)alamin. Cobalamin (vitamin B12) forms a complex with MTR to serve as an intermediary in methyl transfer reactions that cycles between MTR-bound methylcob(III)alamin and MTR bound-cob(I)alamin forms, and occasional oxidative escape of the cob(I)alamin intermediate during the catalytic cycle leads to the inactive cob(II)alamin species. The processing of cobalamin in the cytosol occurs in a multiprotein complex composed of at least MMACHC, MMADHC, MTRR and MTR which may contribute to shuttle safely and efficiently cobalamin towards MTR in order to produce methionine (By similarity). Also necessary for the utilization of methyl groups from the folate cycle, thereby affecting transgenerational epigenetic inheritance. Also acts as a molecular chaperone for methionine synthase by stabilizing apoMTR and incorporating methylcob(III)alamin into apoMTR to form the holoenzyme. Also serves as an aquacob(III)alamin reductase by reducing aquacob(III)alamin to cob(II)alamin; this reduction leads to stimulation of the conversion of apoMTR and aquacob(III)alamin to MTR holoenzyme (By similarity).
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9UBK8}.
Interaction partners:
- Methionine synthase
- Methylenetetrahydrofolate reductase
- Cytochrome P450, family 4, subfamily a, polypeptide 31
- Cobalamin trafficking protein CblD
- Cyanocobalamin reductase / alkylcobalamin dealkylase
- Cystathionine beta-synthase
- C-1-tetrahydrofolate synthase, cytoplasmic
- Betaine--homocysteine S-methyltransferase 1
- Cytochrome P450 3A11
- Serine hydroxymethyltransferase, cytosolic
Sequence:
MRRFLLLYATQRGQAKAIAEEISEQAVSHGFSADLHCISESEKYDLKTETGPLVMVVSTTGTGDPPDTARKFVKEIHNKTLPTDYFAHLRYGLLGLGDSEYTYFCNGGKVIDKRLQELGAQRFYDTGHADDCVGLELVVEPWIDGLWAALTKHFKSLGGQENMSDTLSRASDAPLSTAMKPELLHIQSQVELLRLEDVGERDSELREQNETNRGQQGRIEDFDSSLVHSVPPLSQSSLSIPAVPPEYLEVHLQESLGQEENQASVPSGDPSFQVPISKAIRLTTNDAVKSTLLLELDISKIEFSHQPGDSFNVTCPNSDREVEELLQRLQLADKRAHRVILKIKTDTKKKGAALPAHVPEGRSLQFILTWCLEIRAVPKKAFLRALAEHTSSATEKRRLQELCSKQGAADYNRFIRDASVCLLDLLLTFPSCQPPLSLLLEHLPKLQPRPYSCASSSLRHPDKLHFVFNIVEFPPSTTAASPRKGVCTGWLATLVAPFLQPNTDVSNADSGDTLAPEIRISPRATNAFHLPEDPSAPIIMVGPGTGVAPFVGFLQHREKLQEQHPDGKFGAMWLFFGCRHKDRDYLFREELRHFLKTGVLTHLKVSFSRDAAPDGEEAPAKYVQDNLQRHSQQVARTLLQENGYIYVCGDAKNMAKDVNDTLIGIISNEAGVDKLEAMKTLATLKQEKRYLQDIWS
Protein: Calmodulin 4 (F4IEU4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MADQLTDEQISEFKEAFSLFDKDGDDSISDSGDSCGCITTKELGTVMRSLGQNPTEAELQDMINEVDADGNGTIDFPEFLNLMAKKMKDTDSEEELKEAFRVFDKDQNGFISAAELRHVMTNLGEKLTDEEVEEMIREADVDGDGQINYEEFVKIMMAK
Protein: Acyl-lipid omega-13 desaturase (CrDES) (EC 1.14.19.12) (Omega13 fatty acid desaturase) (Q2HWK7)
Organism: Chlamydomonas reinhardtii (Chlamydomonas smithii)
Function: Front-end desaturase having a omega-13 desaturase activity for omega-9 unsaturated C18/C20 fatty acids. Strong substrate preferences for linoleic acid and alpha-linolenic acid for the production of pinolenic and coniferonic acids respectively. No desaturase activity for dihomo gamma-linolenic acid and eicosatertraenoic acid.
Subcellular location: Membrane {ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
Sequence:
MCRPTDSDSGPALPSIPHQYWIIHGATYDLASYIKSHPGGDEAILLGRGRDCTELFEQYHVLNNKHLRVLERFRVTLPAAKVATNNLKEDMVSTISAFEGEEADAAAVVGIQQPAAPARVAHQSDPFYEDIKAMVRAHGNTKMSAPFVILHCLHVVGLIWSMKLWWQGAFISAFILPYFLWVLCAAMVHDGGHFAHSKRPLVNKLLTHTGALFTNSVGCWYLQHNILHHSYTNLVGKDGDLDSHHPYMRIHPEQSMLPANIHHAVRFFSHLIMYNFAHIGLTMISPLSYFRGVAAQKKGTADAKQAQDAQTVAQYHSTVMLQLVTVGAFYITPFLRFDFSRALLLTLLPTFMMSVAFMVIAQVSHIQMDAEAPSADLEKLHWARRMALTSVDYSQESTLWAYLTIGLNMQSLHHIVPGVSYSQLPRLYPAYRAICEKHGIKLLERRNLAHAFWTHLQTLWVLSKTHSFVEVARKLA