wanglab/gogpt-training-data huggingface dataset:
Protein: Membrane-associated progesterone receptor component 1 (mPR) (Dap1) (IZA) (O00264)
Organism: Homo sapiens (Human)
Function: Component of a progesterone-binding protein complex. Binds progesterone. Has many reported cellular functions (heme homeostasis, interaction with CYPs). Required for the maintenance of uterine histoarchitecture and normal female reproductive lifespan (By similarity). Intracellular heme chaperone. Regulates heme synthesis via interactions with FECH and acts as a heme donor for at least some hemoproteins.
Subcellular location: Microsome membrane {ECO:0000250|UniProtKB:Q95250}; Single-pass membrane protein {ECO:0000255}. Smooth endoplasmic reticulum membrane {ECO:0000303|PubMed:28396637}; Single-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000250|UniProtKB:O55022}; Single-pass membrane protein {ECO:0000305}; Extracellular side {ECO:0000250|UniProtKB:O55022}. Secreted {ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. Note=Localized at cell membrane, probably in lipid rafts, in serum-starved conditions. {ECO:0000269|PubMed:30443021}.
Interaction partners:
- Sigma intracellular receptor 2
- Insulin-induced gene 1 protein
- Ferrochelatase, mitochondrial
- Progesterone receptor
- SERPINE1 mRNA-binding protein 1
- Membrane progestin receptor alpha
- Lanosterol 14-alpha demethylase
- Membrane progestin receptor beta
- Cytochrome P450 1A2
- Cytochrome b5
Sequence:
MAAEDVVATGADPSDLESGGLLHEIFTSPLNLLLLGLCIFLLYKIVRGDQPAASGDSDDDEPPPLPRLKRRDFTPAELRRFDGVQDPRILMAINGKVFDVTKGRKFYGPEGPYGVFAGRDASRGLATFCLDKEALKDEYDDLSDLTAAQQETLSDWESQFTFKYHHVGKLLKEGEEPTVYSDEEEPKDESARKND
Protein: Dynamin-related protein 3B (Dynamin-like protein 2b) (Q8LFT2)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Involved in the control of mitochondrial and peroxisomal division and morphology.
Subcellular location: Mitochondrion {ECO:0000269|PubMed:14988495}. Peroxisome {ECO:0000269|PubMed:18785999, ECO:0000269|PubMed:20179140}.
Interaction partners:
- Mitochondrial fission 1 protein A
- Mitochondrial fission 1 protein B
- Dynamin
- Mitochondrial fission protein ELM1
- Clathrin heavy chain 1
- Clathrin heavy chain 2
- Probable transmembrane GTPase FZO-like, chloroplastic
- Plastid division protein PDV1
- Peroxisomal and mitochondrial division factor 1
- Peroxisomal and mitochondrial division factor 2
Sequence:
MSVDDLPPSSASAVTPLGSSVIPIVNKLQDIFAQLGSQSTIALPQVAVVGSQSSGKSSVLEALVGRDFLPRGNDICTRRPLRLQLVQTKPSSDGGSDEEWGEFLHHDPVRRIYDFSEIRREIEAETNRVSGENKGVSDIPIGLKIFSPNVLDISLVDLPGITKVPVGDQPSDIEARIRTMILTYIKEPSCLILAVSPANTDLANSDALQIAGNADPDGHRTIGVITKLDIMDRGTDARNHLLGKTIPLRLGYVGVVNRSQEDILMNRSIKDALVAEEKFFRSRPVYSGLTDRLGVPQLAKKLNQVLVQHIKALLPSLKSRINNALFATAKEYESYGDITESRGGQGALLLSFITKYCEAYSSTLEGKSKEMSTSELSGGARILYIFQSVFVKSLEEVDPCEDLTADDIRTAIQNATGPRSALFVPDVPFEVLVRRQISRLLDPSLQCARFIFDELVKISHQCMMKELQRFPVLQKRMDEVIGNFLREGLEPSQAMIRDLIEMEMDYINTSHPNFIGGTKAVEQAMQTVKSSRIPHPVARPRDTVEPERTASSGSQIKTRSFLGRQANGIITDQAVPTAADAERPAPAGSTSWSGFSSIFRGSDGQAAAKNNLLNKPFSETTQEVYQNLSTIYLKEPPTILKSSETHSEQESVEIEITKLLLKSYYDIVRKNVEDLVPKAIMHFLVNYTKRELHNVFIEKLYRENLIEELLKEPDELAIKRKRTQETLRILQQANRTLDELPLEAESVERGYKIGSEAKHEELPGTRRSRTETNGNGRLHM
Protein: BBSome complex member BBS4 (Bardet-Biedl syndrome 4 protein homolog) (Q8C1Z7)
Organism: Mus musculus (Mouse)
Function: The BBSome complex is thought to function as a coat complex required for sorting of specific membrane proteins to the primary cilia. The BBSome complex is required for ciliogenesis but is dispensable for centriolar satellite function. This ciliogenic function is mediated in part by the Rab8 GDP/GTP exchange factor, which localizes to the basal body and contacts the BBSome. Rab8(GTP) enters the primary cilium and promotes extension of the ciliary membrane. Firstly the BBSome associates with the ciliary membrane and binds to RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the Rab8-GTP localizes to the cilium and promotes docking and fusion of carrier vesicles to the base of the ciliary membrane. The BBSome complex, together with the LTZL1, controls SMO ciliary trafficking and contributes to the sonic hedgehog (SHH) pathway regulation. Required for proper BBSome complex assembly and its ciliary localization. Required for microtubule anchoring at the centrosome but not for microtubule nucleation. May be required for the dynein-mediated transport of pericentriolar proteins to the centrosome (By similarity).
Subcellular location: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection, cilium membrane {ECO:0000250}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriolar satellite {ECO:0000250}. Cell projection, cilium, flagellum {ECO:0000269|PubMed:15107855, ECO:0000269|PubMed:22072986}. Cell projection, cilium {ECO:0000269|PubMed:23943788}. Note=Localizes to the pericentriolar material. Centrosomal localization requires dynein (By similarity). Localizes to the connecting cilium of photoreceptor cells (PubMed:23943788).
Interaction partners:
- Protein PTHB1
- BBSome complex member BBS7
- BBSome complex member BBS1
- BBSome complex member BBS2
- BBSome complex member BBS5
- Tetratricopeptide repeat protein 8
- Pericentriolar material 1 protein
- BBSome interacting protein 1
- Leucine zipper transcription factor-like protein 1
- BBSome complex assembly protein BBS10
Sequence:
MAEVKLGMKTQVPASVESQKPRSKKAPDFPIVEKQNWLIHLHYIRKDYEACKAVIKEQLQETQGLCEYAIYVQALIFRLEGNIQESLELFQTCAVLSPQCADNLKQVARSLFLLGKHKAATEVYNEAAKLNQKDWEICHNLGVCYTYLKQFNKAQDQLHSALQLNKHDLTYIMLGKIHLLQGDLDKAIEIYKKAVEFSPENTELLTTLGLLYLQLGVYQKAFEHLGNALTYDPANYKAILAAGSMMQTHGDFDVALTKYRVVACAIPESPPLWNNIGMCFFGKKKYVAAISCLKRANYLAPFDWKILYNLGLVHLTMQQYASAFHFLSAAINFQPKMGELYMLLAVALTNLEDIENARRAYVEAVRLDKCNPLVNLNYAVLLYNQGEKKSALAQYQEMEKKVNFLKDNSPLEFDSEMVEMAQKLGAALQVGEALVWTKPVKDPKTKHRTNSGSKSATLQQPLGSIQALGQAMSSAAAYRKILSGAVGAQLPKPPSLPLEPEPEPTVEASPTEASEQKKEK
Protein: Excisionase (Gene product 36) (Gp36) (Q05246)
Organism: Mycobacterium phage L5 (Mycobacteriophage L5)
Function: Excisionase and integrase are necessary for the excision of prophage from the host genome by site-specific recombination at the att site.
Interaction partners:
Sequence:
MPPRASIQETADYLGVSTKTVRNYIADGRLKAVRLGPRLIRVERESVEELMRPIGK
Protein: ANKRD12 protein (Q6PG48)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPKSGFTKPIQSENSDSDSNMVEKPYGRKSKDKIASYSKTPKIERSDVSKEMKEKSSMKRKLPFTISPSRNEERDSDTDSDPGHTSENWGERLISSYRTYSEKEGPEKKKTKKEAGNKKSTPVSILFGYPLSERKQMALLMQMTARDNSPDSTPNHPSQTTPAQKKTPSSSSRQKDKVNKRNERGETPLHMAAIRGDVKQVKELISLGANVNVKDFAGWTPLHEACNVGYYDVAKILIAAGADVNTQGLDDDTPLHDSASSGHRDIVKLLLRHGGNPFQANKHGERPVDVAETEELELLLKREVPLSDDDESYTGSSYQFAGNAKLSGAS
Protein: ABC transporter G family member 31 (ABC transporter ABCG.31) (AtABCG31) (Pleiotropic drug resistance protein 3) (AtPDR3) (Q7PC88)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Together with ABCG25, export abscisic acid (ABA) from the endosperm to deliver it to the embryo via ABCG30 and ABCG40-mediated import to suppress radicle extension and subsequent embryonic growth. Together with ABCG9, involved in pollen coat deposition of steryl glycosides required for pollen fitness. May be a general defense protein (By similarity).
Subcellular location: Cell membrane {ECO:0000269|PubMed:24474628, ECO:0000269|PubMed:26334616}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Protein DETOXIFICATION 50
- Protein NRT1/ PTR FAMILY 4.6
Sequence:
MAAASNGSEYFEFDVETGRESFARPSNAETVEQDEEDLRWAAIGRLPSQRQGTHNAILRRSQTQTQTSGYADGNVVQTIDVKKLDRADREMLVRQALATSDQDNFKLLSAIKERLDRVGMEVPKIEVRFENLNIEADVQAGTRALPTLVNVSRDFFERCLSSLRIIKPRKHKLNILKDISGIIKPGRMTLLLGPPGSGKSTLLLALAGKLDKSLKKTGNITYNGENLNKFHVKRTSAYISQTDNHIAELTVRETLDFAARCQGASEGFAGYMKDLTRLEKERGIRPSSEIDAFMKAASVKGEKHSVSTDYVLKVLGLDVCSDTMVGNDMMRGVSGGQRKRVTTGEMTVGPRKTLFMDEISTGLDSSTTFQIVKCIRNFVHLMDATVLMALLQPAPETFDLFDDLILLSEGYMVYQGPREDVIAFFESLGFRLPPRKGVADFLQEVTSKKDQAQYWADPSKPYQFIPVSDIAAAFRNSKYGHAADSKLAAPFDKKSADPSALCRTKFAISGWENLKVCFVRELLLIKRHKFLYTFRTCQVGFVGLVTATVFLKTRLHPTSEQFGNEYLSCLFFGLVHMMFNGFSELPLMISRLPVFYKQRDNSFHPAWSWSIASWLLRVPYSVLEAVVWSGVVYFTVGLAPSAGRFFRYMLLLFSVHQMALGLFRMMASLARDMVIANTFGSAAILIVFLLGGFVIPKADIKPWWVWGFWVSPLSYGQRAIAVNEFTATRWMTPSAISDTTIGLNLLKLRSFPTNDYWYWIGIAVLIGYAILFNNVVTLALAYLNPLRKARAVVLDDPNEETALVADANQVISEKKGMILPFKPLTMTFHNVNYYVDMPKEMRSQGVPETRLQLLSNVSGVFSPGVLTALVGSSGAGKTTLMDVLAGRKTGGYTEGDIRISGHPKEQQTFARISGYVEQNDIHSPQVTVEESLWFSASLRLPKEITKEQKKEFVEQVMRLVELDTLRYALVGLPGTTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAFDELLLMKRGGQVIYGGKLGTHSQVLVDYFQGINGVPPISSGYNPATWMLEVTTPALEEKYNMEFADLYKKSDQFREVEANIKQLSVPPEGSEPISFTSRYSQNQLSQFLLCLWKQNLVYWRSPEYNLVRLVFTTIAAFILGTVFWDIGSKRTSSQDLITVMGALYSACLFLGVSNASSVQPIVSIERTVFYREKAAGMYAPIPYAAAQGLVEIPYILTQTILYGVITYFTIGFERTFSKFVLYLVFMFLTFTYFTFYGMMAVGLTPNQHLAAVISSAFYSLWNLLSGFLVQKPLIPVWWIWFYYICPVAWTLQGVILSQLGDVESMINEPLFHGTVKEFIEYYFGYKPNMIGVSAAVLVGFCALFFSAFALSVKYLNFQRR
Protein: Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-3 (P63214)
Organism: Bos taurus (Bovine)
Function: Guanine nucleotide-binding proteins (G proteins) are involved as a modulator or transducer in various transmembrane signaling systems. The beta and gamma chains are required for the GTPase activity, for replacement of GDP by GTP, and for G protein-effector interaction.
Subcellular location: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}.
Interaction partners:
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein subunit beta-5
- Guanine nucleotide-binding protein G
- Guanine nucleotide-binding protein G
- GNB4 protein
- Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein
- C-C chemokine receptor type 5
- C-X-C chemokine receptor type 4
- 5-hydroxytryptamine receptor 7
- Neuroendocrine secretory protein 55
Sequence:
MKGETPVNSTMSIGQARKMVEQLKIEASLCRIKVSKAAADLMTYCDAHACEDPLITPVPTSENPFREKKFFCALL
Protein: Elongator complex protein 4 (Q9USP1)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Component of the elongator complex, a multiprotein complex which is required for multiple tRNA modifications, including mcm5U (5-methoxycarbonylmethyl uridine), mcm5s2U (5-methoxycarbonylmethyl-2-thiouridine), and ncm5U (5-carbamoylmethyl uridine). The elongator complex catalyzes formation of carboxymethyluridine in the wobble base at position 34 in tRNAs.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}.
Interaction partners:
- Elongator complex protein 3
- Elongator complex protein 1
- Elongator complex protein 5
- Elongator complex protein 2
- Elongator complex protein 6 homolog
- Cytoplasmic tRNA 2-thiolation protein 1
- Adenylyltransferase and sulfurtransferase uba4
- Protein kti12
- Diphthamide biosynthesis protein 3
- Ubiquitin-related modifier 1
Sequence:
MSFKRKAAPQIAPTNLPTGVRLSSKDARWITSSGSSSFDYYLSGGIPMKSLLVIEEDSMDYASVLLKFFAAEGLKQDHVIWLGPSIGEMWFRQLPGDSDRPNKNENSAGEDNHSSPPSKNPQQERMKIAWRYEQVSKTKAPTLDMIPPGYTHSFDLSKNLIVKSDMKYAVSPFPLETGSNPYAPVIESLTRFLSTLTPGTVCRLVLPSILSPAFYSIRATHPQHFIRFIHTLSSLIKCTTSVHLICMCSVPSTLFSRDCEQIFWLENLASAVFSLHPFPVKETVNGLVTQPLGLFRIHKLPLALPFTNHANSNEAGDLSFTVSKRRFTIEPWVLPPLDDEQKDTKISNTNPQKQPVKSLDF
Protein: Cytochrome b-c1 complex subunit 10 (Complex III subunit 10) (Complex III subunit XI) (Ubiquinol-cytochrome c reductase complex 6.4 kDa protein) (Q9CPX8)
Organism: Mus musculus (Mouse)
Function: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III, CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to transfer electrons derived from NADH and succinate to molecular oxygen, creating an electrochemical gradient over the inner membrane that drives transmembrane transport and the ATP synthase. The cytochrome b-c1 complex catalyzes electron transfer from ubiquinol to cytochrome c, linking this redox reaction to translocation of protons across the mitochondrial inner membrane, with protons being carried across the membrane as hydrogens on the quinol. In the process called Q cycle, 2 protons are consumed from the matrix, 4 protons are released into the intermembrane space and 2 electrons are passed to cytochrome c. QCR10 has a role in CIII assembly and RIP1 stability.
Subcellular location: Mitochondrion inner membrane {ECO:0000269|PubMed:34616041, ECO:0000269|PubMed:38575788}; Single-pass membrane protein {ECO:0000269|PubMed:34616041}.
Interaction partners:
- Cytochrome b-c1 complex subunit 2, mitochondrial
- Cytochrome b-c1 complex subunit 1, mitochondrial
- Cytochrome b-c1 complex subunit Rieske, mitochondrial
- Cytochrome b-c1 complex subunit 9
- Cytochrome c1, heme protein, mitochondrial
- Cytochrome b-c1 complex subunit 6, mitochondrial
- Cytochrome c oxidase subunit 5A, mitochondrial
- Cytochrome b-c1 complex subunit 8
- Cytochrome b-c1 complex subunit 7
- Cytochrome c oxidase subunit 7C, mitochondrial
Sequence:
MLSRFLGPRYRELARNWIPTAGMWGTVGAVGLVWATDWRLILDWVPYINGKFKKDD
Protein: Patatin-like phospholipase domain-containing protein 7 (EC 3.1.1.-) (EC 3.1.1.5) (Neuropathy target esterase-related esterase) (NRE) (NTE-related esterase) (A2AJ88)
Organism: Mus musculus (Mouse)
Function: Lysophospholipase which preferentially deacylates unsaturated lysophosphatidylcholine (C18:1), generating glycerophosphocholine. Can also deacylate, to a lesser extent, lysophosphatidylethanolamine (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid (C16:0).
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}; Single-pass type III membrane protein {ECO:0000269|PubMed:28887301}. Lipid droplet {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 3]: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22326266}; Single-pass type III membrane protein {ECO:0000305}.
Interaction partners:
- Phosphatidylcholine-sterol acyltransferase
- Lysosomal phospholipase A and acyltransferase
- Phospholipase A and acyltransferase 3
- Patatin-like phospholipase domain-containing protein 6
- Glycerophosphocholine phosphodiesterase GPCPD1
- Membrane-bound glycerophospholipid O-acyltransferase 2
- Lysophospholipid acyltransferase LPCAT4
- Acyl-protein thioesterase 1
- Membrane-bound glycerophospholipid O-acyltransferase 1
- Phospholipase B1, membrane-associated
Sequence:
MQNEEDACLEAGYCLGTTLSSWRLHFMEEQSQSTMLMGIGIGALLTLAFVGITFFFVYRRVRRLRRAEPTPQYRFRKRDKVMFYGRKIMRKVTTLPHTLVGNTSAPRQRVRKRTKVLSLAKRILRFKKEYPTLQPKEPPPSLLEADLTEFDVKNSHLPSEVLYMLKNVRVLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVHSLLSILDVITGHTAPYKTVSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVVQIIMVRLQRVTFLALHNYLGLTTELFNPESQAIPLLSVASVAGRAKRQMSYGPEEQLERSLRPSEFSSSDHGSSCVTVSGPLLKRSCSVPLPSNHGEVDELRQSQGSGSNTSAFQESHEGATSDLGMAYNRARILPHSDEQLGNSLASKSKKSVVAETPSAIFHYSENFRDETGACGKTDAIFRAATKDLLTLMKLDDPSLLDGRVAFLHVPAGTLVSKQGDQDVNILFVVSGMLHVYQQKIDSLEDTCLFLTHPGEMVGQLAVLTGEPLMFTIRANRDCSFLSISKAHFYEIMRKRPDVVLGVAHTVVKRMSSFVRQIDFALDWMEVEAGRAIYRQGDKSDCTYIVLSGRLRSVIRKDDGKKRLAGEYGRGDLVGVVETLTHQARATTVHAVRDSELAKLPAGALTSIKRRYPQVVTRLIHLLGEKILGSLQQGSATGHQLGFNTASSKWDLGNPPGNLSTVAALPASEDVPLTAFALELQHALSAIGPVLLLTSDNIKQRLGSAALDSIHEYRLSSWLGQQEDIHRIVLYQADGTLTPWTQRCIRQADCILIVGLGEQEPAVGELEQMLESTAVRAQKQLILLHKEDGPVPSRTVEWLNMRSWCSGHLHLCCPRRVFSKRSLPKLVEMYTRVFQRPPDRHSDFSRLARMLTGNAIALVLGGGGARGCAQVGILRALAECGVPVDIIGGTSIGAFMGALFAEERSYSQTRIRAKQWAEGMTSMMKTILDLTYPITSMFSGTGFNSSISNIFKDRQIEDLWLPYFAITTDITASAMRVHTDGSLWRYVRASMSLSGYMPPLCDPKDGHLLMDGGYINNLPADVARSMGAKVVIAIDVGSRDETDLTNYGDALSGWWLLWKRWNPLATKVKVLNMAEIQTRLAYVCCVRQLEMVKNSDYCEYLRPPIDSYRTLDFGKFDEICEVGYQHGRTVFDIWVRSGVLEKMLQDQQGTSKRKDCGVFTCPNSSFTDLAEIVSRIEPAKVAAVDDESDYQTEYEEELPAIPKETYADFQSTGIELDSDSEYEPSMLQGPPSLTSPEQSQDSFPWLPNQDDQGPRLEHPS
Protein: Telomere length regulator taz1 (P79005)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Regulates telomere length and function. Required for the repression of telomere-adjacent gene expression and for normal meiosis or sporulation. It may be a negative regulator of the telomere-replicating enzyme, telomerase, or may protect against activation of telomerase-independent pathways of telomere elongation. It may be involved in the interactions between chromosomes and spindle proteins, disruption of these interactions would lead to defective meiosis.
Subcellular location: Cytoplasm. Nucleus. Chromosome, telomere.
Interaction partners:
- DNA-binding protein rap1
- Protection of telomeres protein poz1
- Coiled-coil quantitatively-enriched protein 1
- Protection of telomeres protein tpz1
- Telomerase reverse transcriptase
- Telomere length regulator protein rif1
- Protein ten1
- Protein stn1
- Protection of telomeres protein 1
- Telomeric DNA-binding factor trf1
Sequence:
MISVQSTETIQKVLENEGDQQFDKEVVQNSDSNIETGQISDSLTKAVEERAETESSSNLSNFTTSESESSKPAYCFNSHSQNMAEGSISIPVISHSMNVENEVSTAEGQDSRTGESENDQNAMIVRSIWDIEKASLLVNDCQNIANMAEQKVMMVSAIFSESSKDIVNPESFSERLGKETVKDLYEFNEQLTTKYGLEFRTIFFSYIRKYDAYWCLFEDLEKPLKSIQFFTGLIDLLDNTNKHLTLRSIVLDALLSADEEDSFYGDALVLFEELVIRYFGTDSNPSIDASEFILSCLPYTSLDALNVVCGQVWKSQKICDFLKSTIGNTSNSPLQLRASFPAFVNAVIHFLLEFKNVRRLERKDLSVKGMLYDSDSQQILNRLRERVSGSTAQSADEASGHESDASEDTFSERTLGLNSIDNTEISEVVSLGLVSSALDKITGLLSADNLSETVSQARDFSHTLSKSLKSRAKSLSQKEAANRSKLIAKRGDNLRREASLSSEQDDLSEDFPPVRESDEQESRSGGRSSAMRVSIERSAARSGTRRSQGNPYEGYRTRRKWTDEEENELYEMISQHGCCWSKIIHIQKLENGPLKTFGPTQIKDKARLIKARFMKQNRLQELYSKSLNWKNVTVGQAYCELHKIPYIEATPPLLREELVNYQS
Protein: Probable transcriptional regulator (Q746J7)
Organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
Interaction partners:
Sequence:
MTSSGVYTIAEVEAMTGLSAEVLRQWERRYGFPKPRRTPGGHRLYSAEDVEALKTIKRWLEEGATPKAAIRRYLAQEVRPEDLGTGLLEALLRGDLAGAEALFRRGLRFWGPEGVLEHLLLPVLREVGEAWHRGEIGVAEEHLASTFLRARLQELLDLAGFPPGPPVLVTTPPGERHEIGAMLAAYHLRRKGVPALYLGPDTPLPDLRALARRLGAGAVVLSAVLSEPLRALPDGALKDLAPRVFLGGQGAGPEEARRLGAEYMEDLKGLAEALWLPRGPEKEAI
Protein: Acyl-CoA desaturase (EC 1.14.19.1) (Q5AY99)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
- Acyl-CoA desaturase
- Elongation of fatty acids protein
- Elongation of fatty acids protein
- Very-long-chain 3-oxoacyl-CoA reductase
- very-long-chain enoyl-CoA reductase
- Bifunctional oelate/linoleic acid delta desaturase
- Oleate delta-12 desaturase
- Very-long-chain
- Membrane-tethered transcription factor
- Uncharacterized protein
Sequence:
MSAPTADIRARAPEAKKVHIADTAINRHNWYKHVNWLNVFLIIGIPLYGCIQAFWVPLQLKTAIWAVIYYFFTGLGITAGYHRLWAHCSYSATLPLRIWLAAVGGGAVEGSIRWWARDHRAHHRYTDTDKDPYSVRKGLLYSHLGWMVMKQNPKRIGRTDISDLNEDPVVVWQHRNYLKVVFTMGLAVPMLVAGLGWGDWLGGFVYAGILRIFFVQQATFCVNSLAHWLGDQPFDDRNSPRDHVITALVTLGEGYHNFHHEFPSDYRNAIEWHQYDPTKWSIWAWKQLGLAYDLKKFRANEIEKGRVQQLQKKLDRKRATLDWGTPLDQLPVMEWDDYVEQAKNGRGLVAIAGVVHDVTDFIKDHPGGKAMISSGIGKDATAMFNGGVYYHSNAAHNLLSTMRVGVIRGGCEVEIWKRAQKENVEYVRDGSGQRVIRAGEQPTKIPEPIPTADAA
Protein: Geraniol synthase, chloroplastic (ObGES) (EC 3.1.7.11) (Q6USK1)
Organism: Ocimum basilicum (Sweet basil)
Function: Monoterpene synthase that catalyzes the formation of geraniol from geranyl diphosphate.
Subcellular location: Plastid, chloroplast {ECO:0000255}.
Interaction partners:
Sequence:
MSCARITVTLPYRSAKTSIQRGITHYPALIRPRFSACTPLASAMPLSSTPLINGDNSQRKNTRQHMEESSSKRREYLLEETTRKLQRNDTESVEKLKLIDNIQQLGIGYYFEDAINAVLRSPFSTGEEDLFTAALRFRLLRHNGIEISPEIFLKFKDERGKFDESDTLGLLSLYEASNLGVAGEEILEEAMEFAEARLRRSLSEPAAPLHGEVAQALDVPRHLRMARLEARRFIEQYGKQSDHDGDLLELAILDYNQVQAQHQSELTEIIRWWKELGLVDKLSFGRDRPLECFLWTVGLLPEPKYSSVRIELAKAISILLVIDDIFDTYGEMDDLILFTDAIRRWDLEAMEGLPEYMKICYMALYNTTNEVCYKVLRDTGRIVLLNLKSTWIDMIEGFMEEAKWFNGGSAPKLEEYIENGVSTAGAYMAFAHIFFLIGEGVTHQNSQLFTQKPYPKVFSAAGRILRLWDDLGTAKEEQERGDLASCVQLFMKEKSLTEEEARSRILEEIKGLWRDLNGELVYNKNLPLSIIKVALNMARASQVVYKHDQDTYFSSVDNYVDALFFTQ
Protein: FACT complex subunit SSRP1 (Chromatin-specific transcription elongation factor 80 kDa subunit) (Facilitates chromatin transcription complex 80 kDa subunit) (FACT 80 kDa subunit) (FACTp80) (Facilitates chromatin transcription complex subunit SSRP1) (Recombination signal sequence recognition protein 1) (Structure-specific recognition protein 1) (hSSRP1) (T160) (Q08945)
Organism: Homo sapiens (Human)
Function: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II. The FACT complex is probably also involved in phosphorylation of 'Ser-392' of p53/TP53 via its association with CK2 (casein kinase II). Binds specifically to double-stranded DNA and at low levels to DNA modified by the antitumor agent cisplatin. May potentiate cisplatin-induced cell death by blocking replication and repair of modified DNA. Also acts as a transcriptional coactivator for p63/TP63.
Subcellular location: Nucleus {ECO:0000269|PubMed:10421373, ECO:0000269|PubMed:22002106}. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Chromosome {ECO:0000269|PubMed:10421373}. Note=Colocalizes with RNA polymerase II on chromatin. Recruited to actively transcribed loci. {ECO:0000250|UniProtKB:Q05344}.
Interaction partners:
- FACT complex subunit SPT16
- Transcription elongation factor SPT6
- RNA polymerase-associated protein RTF1 homolog
- RNA polymerase-associated protein LEO1
- Histone H3.1
- RNA polymerase-associated protein CTR9 homolog
- Transcription elongation factor SPT5
- Histone H4
- RNA polymerase II-associated factor 1 homolog
- DNA-directed RNA polymerase II subunit RPB1
Sequence:
MAETLEFNDVYQEVKGSMNDGRLRLSRQGIIFKNSKTGKVDNIQAGELTEGIWRRVALGHGLKLLTKNGHVYKYDGFRESEFEKLSDFFKTHYRLELMEKDLCVKGWNWGTVKFGGQLLSFDIGDQPVFEIPLSNVSQCTTGKNEVTLEFHQNDDAEVSLMEVRFYVPPTQEDGVDPVEAFAQNVLSKADVIQATGDAICIFRELQCLTPRGRYDIRIYPTFLHLHGKTFDYKIPYTTVLRLFLLPHKDQRQMFFVISLDPPIKQGQTRYHFLILLFSKDEDISLTLNMNEEEVEKRFEGRLTKNMSGSLYEMVSRVMKALVNRKITVPGNFQGHSGAQCITCSYKASSGLLYPLERGFIYVHKPPVHIRFDEISFVNFARGTTTTRSFDFEIETKQGTQYTFSSIEREEYGKLFDFVNAKKLNIKNRGLKEGMNPSYDEYADSDEDQHDAYLERMKEEGKIREENANDSSDDSGEETDESFNPGEEEEDVAEEFDSNASASSSSNEGDSDRDEKKRKQLKKAKMAKDRKSRKKPVEVKKGKDPNAPKRPMSAYMLWLNASREKIKSDHPGISITDLSKKAGEIWKGMSKEKKEEWDRKAEDARRDYEKAMKEYEGGRGESSKRDKSKKKKKVKVKMEKKSTPSRGSSSKSSSRQLSESFKSKEFVSSDESSSGENKSKKKRRRSEDSEEEELASTPPSSEDSASGSDE