wanglab/gogpt-training-data huggingface dataset:
Protein: Auxin-responsive protein SAUR36 (Protein RESPONSE TO AUXINS AND GIBBERELLINS 1) (Protein SENESCENCE-ASSOCIATED GENE 201) (Protein SMALL AUXIN UP RNA 36) (O22150)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Acts a positive regulator of leaf senescence and may mediate auxin-induced leaf senescence. Plays a role in the regulation of seed germination by gibberellins and abscisic acid (ABA). Plays a role in the regulation of light-dependent hypocotyl elongation.
Interaction partners:
- Auxin-responsive protein SAUR76
- Auxin-responsive protein SAUR61
- Auxin-responsive protein SAUR62
- Auxin-responsive protein SAUR63
- At5g50760
Sequence:
MRKIIGFRIGRRVSRWIFRKTRIQRSGYNRIHSTQQACMLMRPLAKLKSWGQRLKQSFRRRSTRRSAYIPVDHKKADPVPRGHLAIYVGQKDGDCHRVLVPIVYFNHPLFGELLREAEKEYGFCHEGGITIPCLYSDFERVKTRIASGSSSRVFPWGRHCRN
Protein: Meiotic drive suppressor wtf21 (O74474)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Acts as a suppressor component of the dual wtf meiotic drive system, and can suppress but not confer meiotic drive by compatible poisons (By similarity). Wtf meiotic drive systems promote unequal transmission of alleles from the parental zygote to progeny spores by encoding a poison and an antidote from the same locus; the poison is trans-acting and forms toxic aggregates in all spores within an ascus, wherease the antidote is spore-specific and targets aggregates for degradation by the vacuole (By similarity). Meiotic drive by wtf systems therefore lead to poisoning of all progeny that do not inherit the dual poison/antidote allele, or express a compatible antidote (By similarity).
Subcellular location: Spore membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:A0A218N034, ECO:0000255}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Wtf element wtf14
Sequence:
MKNNYTSLKSPLDEEDELKTDHEIDLEKGPLPEYDSEEEGALPPYSDHALVNNPPNTHRENNPSRSTDNSSPFLIKLLISFTPIYVLNVLAICYLTYKDAFFKDYGAAEWTLFGFWCLVCTLALIFLTYFYETWVKAVKVTVISLAKCVKVISIGLFNIRREMMIIIWILWLIICCILFVYIKSGDLILNKALICSTCTISAVLLLIVSSVCIPFWTFERTLAKLAKVLLLQSGIVLVLNGTMFLRGKHFERIGCEIEASVLFIMGNVLFLCEMECPGALIRTRNSIRNGIAFILGGIGNAMMGLANAIRGANDNNDIPLGEMDVESEV
Protein: Serine/threonine-protein kinase VRK1 (EC 2.7.11.1) (Serine/threonine-protein kinase 51PK) (Vaccinia-related kinase 1) (Q80X41)
Organism: Mus musculus (Mouse)
Function: Serine/threonine kinase involved in cell cycle, nuclear condensation and transcription regulation. Involved in Golgi disassembly during the cell cycle: following phosphorylation by PLK3 during mitosis, required to induce Golgi fragmentation (By similarity). Phosphorylates 'Thr-18' of p53/TP53 and may thereby prevent the interaction between p53/TP53 and MDM2 (By similarity). Phosphorylates KAT5 in response to DNA damage, promoting KAT5 association with chromatin and histone acetyltransferase activity. Phosphorylates BANF1: disrupts its ability to bind DNA, reduces its binding to LEM domain-containing proteins and causes its relocalization from the nucleus to the cytoplasm (By similarity). Phosphorylates ATF2 which activates its transcriptional activity (By similarity).
Subcellular location: Nucleus {ECO:0000269|PubMed:14645249, ECO:0000269|PubMed:9521809}. Cytoplasm {ECO:0000250|UniProtKB:Q99986}. Nucleus, Cajal body {ECO:0000250|UniProtKB:Q99986}. Note=Enriched on chromatin during mitotic chromatin condensation. {ECO:0000250|UniProtKB:Q99986}.
Interaction partners:
- Ankyrin repeat and LEM domain-containing protein 2
- Barrier-to-autointegration factor
- Barrier-to-autointegration factor-like protein
Sequence:
MPRVKAAQAGRPGPAKRRLAEQFAAGEVLTDMSRKEWKLGLPIGQGGFGCIYLADTNSSKPVGSDAPCVVKVEPSDNGPLFTELKFYQRAAKPEQIQKWIRTHKLKYLGVPKYWGSGLHDKNGKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLSLRILDILEYIHEHEYVHGDIKASNLLLSHKNPDQVYLVDYGLAYRYCPDGVHKEYKEDPKRCHDGTLEFTSIDAHKGVAPSRRGDLEILGYCMIQWLSGCLPWEDNLKDPNYVRDSKIRYRDNVAALMEKCFPEKNKPGEIAKYMESVKLLEYTEKPLYQNLRDILLQGLKAIGSKDDGKLDFSAVENGSVKTRPASKKRKKEAEESAVCAVEDMECSDTQVQEAAQTRSVESQGAIHGSMSQPAAGCSSSDSSRRQQHLGLEQDMLRLDRRGSRTRKKAQK
Protein: DNA polymerase catalytic subunit (EC 2.7.7.7) (P08546)
Organism: Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5)
Function: Replicates viral genomic DNA in the late phase of lytic infection, producing long concatemeric DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein (By similarity).
Subcellular location: Host nucleus {ECO:0000250}. Note=the protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs. {ECO:0000250}.
Interaction partners:
Sequence:
MFFNPYLSGGVTGGAVAGGRRQRSQPGSAQGSGKRPPQKQFLQIVPRGVMFDGQTGLIKHKTGRLPLMFYREIKHLLSHDMVWPCPWRETLVGRVVGPIRFHTYDQTDAVLFFDSPENVSPRYRQHLVPSGNVLRFFGATEHGYSICVNVFGQRSYFYCEYSDTDRLREVIASVGELVPEPRTPYAVSVTPATKTSIYGYGTRPVPDLQCVSISNWTMARKIGEYLLEQGFPVYEVRVDPLTRLVIDRRITTFGWCSVNRYDWRQQGRASTCDIEVDCDVSDLVAVPDDSSWPRYRCLSFDIECMSGEGGFPCAEKSDDIVIQISCVCYETGGNTAVDQGIPNGNDGRGCTSEGVIFGHSGLHLFTIGTCGQVGPDVDVYEFPSEYELLLGFMLFFQRYAPAFVTGYNINSFDLKYILTRLEYLYKVDSQRFCKLPTAQGGRFFLHSPAVGFKRQYAAAFPSASHNNPASTAATKVYIAGSVVIDMYPVCMAKTNSPNYKLNTMAELYLRQRKDDLSYKDIPRCFVANAEGRAQVGRYCLQDAVLVRDLFNTINFHYEAGAIARLAKIPLRRVIFDGQQIRIYTSLLDECACRDFILPNHYSKGTTVPETNSVAVSPNAAIISTAAVPGDAGSVAAMFQMSPPLQSAPSSQDGVSPGSGSNSSSSVGVFSVGSGSSGGVGVSNDNHGAGGTAAVSYQGATVFEPEVGYYNDPVAVFDFASLYPSIIMAHNLCYSTLLVPGGEYPVDPADVYSVTLENGVTHRFVRASVRVSVLSELLNKWVSQRRAVRECMRECQDPVRRMLLDKEQMALKVTCNAFYGFTGVVNGMMPCLPIAASITRIGRDMLERTARFIKDNFSEPCFLHNFFNQEDYVVGTREGDSEESSALPEGLETSSGGSNERRVEARVIYGDTDSVFVRFRGLTPQALVARGPSLAHYVTACLFVEPVKLEFEKVFVSLMMICKKRYIGKVEGASGLSMKGVDLVRKTACEFVKGVTRDVLSLLFEDREVSEAAVRLSRLSLDEVKKYGVPRGFWRILRRLVQARDDLYLHRVRVEDLVLSSVLSKDISLYRQSNLPHIAVIKRLAARSEELPSVGDRVFYVLTAPGVRTAPQGSSDNGDSVTAGVVSRSDAIDGTDDDADGGGVEESNRRGGEPAKKRARKPPSAVCNYEVAEDPSYVREHGVPIHADKYFEQVLKAVTNVLSPVFPGGETARKDKFLHMVLPRRLHLEPAFLPYSVKAHECC
Protein: Uncharacterized protein (Q4GZ71)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Interaction partners:
Sequence:
MGGAPSREATVVYSYLRGTYEIGLIPLTSAFFGRPSGRGEHEGENVLRGHFLQMREDLFAACTLPTRNKVLSWTEIVPNRFTGEDLDAFLEIVDKRLYPTNAAMVADKNSPLLPVPCAVCLVCKDGRERRGSFRWRGRNIVIIGYFGCMDEKLDAAFKTEKRTPRQGMYSITAAVFPSIGDRTFDRVLALAPVMLRGQFVGSVLQLRRGGGEFATPLSERGEMVDVSSEAPSLGAGIGGVVGQSDGLIHEDSAVDSAFEMFVERVSQMSVFVEVVSDNYSSLKSLVENVAFIQIHTQAEPKQCTLDLPPIVQNAFNRTTTASSCEKKADAEGHHAEKSPPQRSSAMEQGSSCCTVQGVSCSLERDDLTDLSSVEPEGSSHLSKVPTEDGGSFHFCTEIVRVHFNERYVSLAIQWLSSFFRKPTLLENGYWVHYCLKKEEEVIRRILCHRDTIVSGWRTSHPELANQYMGDGTDKLLEHVRILQHELQQARKAAEEPTLRKKASTPPTLPCPNTTSMAVLAPPPPPHVMPYAVPPLPSPVYFVQQQPVGNPMFVSLLPFQQVQQVPQVQQIPQFQQVPQIQPLQQISHVQQIPQLQQTQPVQSISHVQQISHVQPIHQVQQISHVQPMPLYHLQPPELQQPSVCYLPFGDGGALPPSYVIPSSLS
Protein: 58 protein (P88995)
Organism: Murid herpesvirus 4 (MuHV-4) (Murine gammaherpesvirus 68)
Interaction partners:
Sequence:
MKSHWSDVFLPLIVGGMSAVPFIWCLIFRTLYLPIECDWRCWIFVYGSMIWHITMFMSLLFKHKHGMIGWFKLCSAVAICLIIVLALLEQYCPYEMYIVPVIFIINIVLLSTWVPMALISTYMCNRIYARLLELGFLAAIIGYYVMLQIGAQESPAFWIPIPVLHIGGVYALLHFRTRPCFLHSVEKRHSIYYFGNNKYTVYPCETIVRMCSPEISLMIILIMMLAIGFPILAYYVKIVQGMQYFYMFLMLGPMVGGLIFDSKIVGTFFMMLALVTMIFAGIAPVWFPLMAERTFVISLILANFSAGCFLECMRVKLRRAINGVYFVYLVTVLYNLLVALIMIAVSM
Protein: K(+)-stimulated pyrophosphate-energized sodium pump (EC 7.2.3.1) (Membrane-bound sodium-translocating pyrophosphatase) (Pyrophosphate-energized inorganic pyrophosphatase) (Na(+)-PPase) (Tm-PPase) (Q9S5X0)
Organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)
Function: Sodium pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for Na(+) movement across the membrane.
Subcellular location: Cell inner membrane {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000305|PubMed:16182234}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01129, ECO:0000269|PubMed:16182234}.
Interaction partners:
- Adenosylhomocysteinase
- Hypothetical protein
- Redox-sensing transcriptional repressor Rex 1
- Reverse gyrase
- Conserved hypothetical protein
- Leucine--tRNA ligase
Sequence:
MYVAALFFLIPLVALGFAAANFAAVVRKPEGTERMKEISSYIRSGADSFLAHETKAIFKVAIVIAILLMIFTTWQTGVAFLLGAVMSASAGIVGMKMATRANVRVAEAARTTKKIGPALKVAYQGGSVMGLSVGGFALLGLVLVYLIFGKWMGQVDNLNIYTNWLGINFVPFAMTVSGYALGCSIIAMFDRVGGGVYTKAADMAADLVGKTELNLPEDDPRNPATIADNVGDNVGDVAGLGADLLESFVGAIVSSIILASYMFPIYVQKIGENLVHQVPKETIQALISYPIFFALVGLGCSMLGILYVIVKKPSDNPQRELNISLWTSALLTVVLTAFLTYFYLKDLQGLDVVGFRFGAISPWFSAIIGIFSGILIGFWAEYYTSYRYKPTQFLSKSSIEGTGMVISNGLSLGMKSVFPPTLTLVLGILFADYFAGLYGVAIAALGMLSFVATSVSVDSYGPIADNAGGISEMCELDPEVRKITDHLDAVGNTTAAIGKGFAIGSAIFAALSLFASYMFSQISPSDIGKPPSLVLLLNMLDARVIAGALLGAAITYYFSGYLISAVTKAAMKMVDEIRRQAREIPGLLEGKAKPDYNRCIEITSDNALKQMGYPAFIAILTPLVTGFLLGAEFVGGVLIGTVLSGAMLAILTANSGGAWDNAKKYLEAGNLEGYGKGSEPHKALVIGDTVGDPLKDTVGPSLDILIKIMSVVSVIAVSIFKHVHLF
Protein: HDAC6 (Histone deacetylase 6, isoform D (EC 3.5.1.98)) (Histone deacetylase HDA2) (Q9XYX1)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MLKNQGCGSQESVTDIFQNAVNSKSLVRKPTALIYDESMSQHCCLWDKEHYECPERFTRVLERCRELNLTERCLELPSRSATKDEILRLHTEEHFERLKETSGIRDDERMEELSSRYDSIYIHPSTFELSLLASGSTIELVDHLVAGKAQNGMAIIRPPGHHAMKAEYNGYCFFNNVALATQHALDVHKLQRILIIDYDVHHGQGTQRFFYNDPRVVYFSIHRFEHGSFWPHLHESDYHAIGSGAGTGYNFNVPLNATGMTNGDYLAIFQQLLLPVALEFQPELIIVSAGYDAALGCPEGEMEVTPACYPHLLNPLLRLADARVAVVLEGGYCLDSLAEGAALTLRSLLGDPCPPLVETVPLPRAELAQALLSCIAVHRPHWRCLQLQQTYDCVELQDRDKEEDLHTVLRHWIGGPPPMDRYPTRDTAIPLPPEKLTSNAARLQVLRAETKLSVPSFKVCYAYDAQMLLHCNLNDTGHPEQPSRIQHIHKMHDDYGLLKQMKQLSPRAATTDEVCLAHTRAHVNTVRRLLGREPKELHDAAGIYNSVYLHPRTFDCATLAAGLVLQAVDSVLRGESRSGICNVRPPGHHAEQDHPHGFCIFNNVAIAAQYAIRDFGLERVLIVDWDVHHGNGTQHIFESNPKVLYISLHRYEHGSFFPKGPDGNFDVVGKGAGRGFNVNIPWNKKGMGDLEYALAFQQLIMPIAYEFNPQLVLVSAGFDAAIGDPLGGCKVTAEGYGMLTHWLSALASGRIIVCLEGGYNVNSISYAMTMCTKTLLGDPVPTPQLGATALQKPPTVAFQSCVESLQQCLQVQRNHWRSLEFVGRRLPRDPVVGENNNEDFLTASLRHLNISNDDATAAAGGLAGDRPDCGDERPSGSKPKVKH
Protein: GID complex subunit 7 (Glucose-induced degradation protein 7) (P25569)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for the adaptation to the presence of glucose in the growth medium; mediates the degradation of enzymes involved in gluconeogenesis when cells are shifted to glucose-containing medium. Required for proteasome-dependent catabolite degradation of fructose-1,6-bisphosphatase (FBP1).
Subcellular location: Nucleus {ECO:0000269|PubMed:14562095}. Cytoplasm {ECO:0000269|PubMed:14562095}.
Interaction partners:
- GID complex subunit 5
- GID complex subunit 1
- GID complex subunit 8
- E3 ubiquitin-protein ligase RMD5
- GID complex subunit 9
- GID complex substrate-recognition subunit 4
- GID complex substrate-recognition subunit 10
- Protein yippee-like MOH1
- Ubiquitin fusion degradation protein 4
- Ubiquitin-conjugating enzyme E2-24 kDa
Sequence:
MSHTNKIAYVLNNDTEETASPSSVGCFDKKQLTKLLIHTLKELGYDSAANQLLLESGGYQNESNHIQTFFKLIKTGQFHLINWQIVCSLPLAHSSPLRSEWLQRLLIPTPTPATTSLFDHMLLQLQYLQQLMSSVNSSTCSDAEIATLRNYVEIMILVNRQIFLEFFHPVTNSASHKGPHTALPVLYLRKILKNFIEIWDSLLVSNDQFLNEENIFNPETTLRELSTYLTNPKLTAQLNLERDHLIDAISKYIDPNELVPKGRLLHLLKQAIKYQQSQDIFNIIDPDDDASFSSPPHRINLLQDNFSHDLTVTFQEWKTIQDTTDEIWFLTFSPNGKYLASATSESSRGYFITVYDVEQDFKIYKTCVSLSQSVLYLMFSPDSRYLVACPFSEDVTIYDMNATSLPDASATDSFLLYPSTRLSPMDSFKLDTTTYPDDTESSASSSSRPANANSNQSRVWCCDAFHTAERAGWMVVGSPDREAIVHSLTTKESLFSLKGRTCIALGHDENISGRKSIDPAKVLYKPTSSNGNWQYVEDDETFPRVHDVKISYDDKYVLLMTHQGVIDVYDFSGFPSKEELSKQTVDPKNFLIPRIARLDVGKNMTCISLPLNTTHQGFHRQQISESQHLVLVSLQDNELQMWDYKENILIQKYFGQKQQHFIIRSCFAYGNKLVMSGSEDGKIYIWDRIRGNLVSVLSGHSTVMSNSTKPMGKNCNVVASNPADKEMFASGGDDGKIKIWKISRN
Protein: Microperfuranone synthase (EC 2.3.1.-) (Nonribosomal peptide synthase micA) (Q5B7T4)
Organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans)
Function: Microperfuranone synthase is the only protein required for the biosynthesis of the secondary metabolite microperfuranone from phenylpyruvic acid (PPA). Several steps for the microperfuranione biosynthesis have been proposed. These steps include the activation of PPA, by the micA adenylation (A) domain to AMP-phenylpyruvic acid followed by loading of the PPA unit to the thiolation and peptide carrier (T) domain and eventually transferring to the thioesterase (TE) domain. After loading another PPA unit onto the T domain, aldol condensation establishes the carbon-carbon bond between the alpha- and beta-carbon of the two PPA units. Sulfur-assisted furan ring formation, TE domain mediated hydrolysis, decarboxylation, and keto-enol tautomerization would generate microperfuranone attached to the T domain. Finally, microperfuranone is released by the TE domain.
Interaction partners:
- Nucleoporin NSP1
Sequence:
MVGSVVEAHRQSVGCLRNLSQLLAWASNTSGGLIFYSREDDVLTSTRISYAELLADAGEKARLIGQITGLSSESIILLHFDTQREVIEWFWAATLAGYLPAISTPFVDDTARRKAHLLHLHAQLNQPVVLTSKRLVPEFLGLEELRLHDVESLLSSAAKDGLIQYLGVQKLAEDVAVLMLTSGSTGSAKAVPLRHGQLLTAIQGKSTHHGTLPGDVFYNWVGLDHVASLTEIHLHALILGSDQVHTAASELLRNSLQFVRLLDTHKVAYTFAPNFFLTKVLDSLRENPTFTADLSSLKALISGGESNVVVTCDKLTRELRRRGVQAEVIRPGFGMTETCAGSIYSRACPSYDIRQSLEFASLGSCIPGMHMRIMSITEPGKLAAPGESGELQVAGPVVFDHYYNDETATRNAFTPDGWFITGDLGWIDDAGNLNLAGRTKDTIIVNGVKWSSTELEAAIEEEAVSGLVRSFTVVVPTRPPGSATEEIAVVYSPAYAPEDYHARYETAQVISKTVSLLTGTKPARLIPLPQSLLEKSSLGKISHSKVRAALESGEYASIERADQLILAQYRQFKWRPAKSDSERAVQKALVEFLQVPAEGINMDDSIYDLGVSSLNLILLRSTLQRMLDPKIDIPLSIILNNPTPGAIARSIDSSRSSLAGYNAIVPLQQHRHGGTPLFCIHPGSGEVLVFVALAAHFPTRPVYALRTRGYGSNEQLFGSIEETVETYATQIRQVQPHGPYAIAGYSLGSTLAFEVAKVLEAQGEEVKFLASIDYPPHIAHYVRDLNWTDVLLHIAFFLELIDEKTMVEVTPYLHTLDRQTALTHILNIGDAERARALAIDTKHLGLISDIAENFRVNVKTYKPQGKVQHLDVFVADPPTYAARDRKDWRENKLGRWVDFCETKVEFHDCPGIHAKMLNREHIAGFAKVFKAAMRRRGV
Protein: Inositol phosphosphingolipids phospholipase C (IPS phospholipase C) (IPS-PLC) (EC 3.1.4.-) (Neutral sphingomyelinase) (N-SMase) (nSMase) (P40015)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Responsible for the hydrolysis of the phosphosphingolipids (IPS), inositol phosphorylceramide (IPC), mannosylinositol phosphorylceramide (MIPC), and mannosyldiinositol phosphorylceramide (M(IP)2C). Regulates sphingolipid metabolism in mitochondria, especially the formation of alpha-hydroxylated very long chain phytoceramides. The generated ceramides contribute to the normal function of mitochondria. Also active on sphingomyelin (SM), but this activity is probably not physiologically relevant.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:14699160}; Multi-pass membrane protein {ECO:0000255}. Mitochondrion outer membrane {ECO:0000269|PubMed:14699160, ECO:0000269|PubMed:17880915}; Multi-pass membrane protein {ECO:0000255}. Note=Localization is regulated in a growth-dependent manner. Predominantly in the ER during early growth and becomes associated with mitochondria in late logarithmic growth. {ECO:0000269|PubMed:14699160}.
Interaction partners:
- Serine palmitoyltransferase 1
- 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase 1
- Serine/threonine-protein phosphatase PP1-1
- Serine palmitoyltransferase 2
- Alkaline ceramidase YPC1
- Alkaline ceramidase YDC1
- Ceramide synthase LAC1
- Serine/threonine-protein kinase SCH9
- Ceramide synthase LAG1
- Inositolphosphotransferase 1
Sequence:
MYNRKDRDVHERKEDGQSEFEALNGTNAIMSDNSKAYSIKFLTFNTWGLKYVSKHRKERLRAIADKLAGHSMLTPISDELLPNGGDSNENEDYDVIALQEIWCVEDWKYLASACASKYPYQRLFHSGILTGPGLAILSKVPIESTFLYRFPINGRPSAVFRGDWYVGKSIAITVLNTGTRPIAIMNSHMHAPYAKQGDAAYLCHRSCQAWDFSRLIKLYRQAGYAVIVVGDLNSRPGSLPHKFLTQEAGLVDSWEQLHGKQDLAVIARLSPLQQLLKGCTTCDSLLNTWRAQRQPDEACRLDYALIDPDFLQTVDAGVRFTERIPHLDCSVSDHFAYSCTLNIVPQGTESRPSTSVKRAKTHDRELILQRYSNYETMIECIHTYLKTAQRQKFFRGLHFWASILLLIASLVVTTFTANKAGWSSIFWVLFAIAVSISGTIDGAISFLFGRSEIRALIEVEQEVLDAEHHLQTFLSEK
Protein: Endoglin (CD antigen CD105) (P17813)
Organism: Homo sapiens (Human)
Function: Vascular endothelium glycoprotein that plays an important role in the regulation of angiogenesis. Required for normal structure and integrity of adult vasculature. Regulates the migration of vascular endothelial cells. Required for normal extraembryonic angiogenesis and for embryonic heart development (By similarity). May regulate endothelial cell shape changes in response to blood flow, which drive vascular remodeling and establishment of normal vascular morphology during angiogenesis (By similarity). May play a critical role in the binding of endothelial cells to integrins and/or other RGD receptors. Acts as TGF-beta coreceptor and is involved in the TGF-beta/BMP signaling cascade that ultimately leads to the activation of SMAD transcription factors. Required for GDF2/BMP9 signaling through SMAD1 in endothelial cells and modulates TGFB1 signaling through SMAD3.
Subcellular location: Cell membrane {ECO:0000269|PubMed:10545596, ECO:0000269|PubMed:1326540, ECO:0000269|PubMed:1692830, ECO:0000269|PubMed:17540773, ECO:0000269|PubMed:8370410}; Single-pass type I membrane protein {ECO:0000305|PubMed:1692830, ECO:0000305|PubMed:8370410}.
Interaction partners:
- Activin receptor type-1-like
- Transforming growth factor beta-1 proprotein
- TGF-beta receptor type-2
- Growth/differentiation factor 2
- Transforming growth factor beta-3 proprotein
- Bone morphogenetic protein receptor type-2
- Bone morphogenetic protein 10
- TGF-beta receptor type-1
- Thy-1 membrane glycoprotein
- Leucine-rich alpha-2-glycoprotein
Sequence:
MDRGTLPLAVALLLASCSLSPTSLAETVHCDLQPVGPERGEVTYTTSQVSKGCVAQAPNAILEVHVLFLEFPTGPSQLELTLQASKQNGTWPREVLLVLSVNSSVFLHLQALGIPLHLAYNSSLVTFQEPPGVNTTELPSFPKTQILEWAAERGPITSAAELNDPQSILLRLGQAQGSLSFCMLEASQDMGRTLEWRPRTPALVRGCHLEGVAGHKEAHILRVLPGHSAGPRTVTVKVELSCAPGDLDAVLILQGPPYVSWLIDANHNMQIWTTGEYSFKIFPEKNIRGFKLPDTPQGLLGEARMLNASIVASFVELPLASIVSLHASSCGGRLQTSPAPIQTTPPKDTCSPELLMSLIQTKCADDAMTLVLKKELVAHLKCTITGLTFWDPSCEAEDRGDKFVLRSAYSSCGMQVSASMISNEAVVNILSSSSPQRKKVHCLNMDSLSFQLGLYLSPHFLQASNTIEPGQQSFVQVRVSPSVSEFLLQLDSCHLDLGPEGGTVELIQGRAAKGNCVSLLSPSPEGDPRFSFLLHFYTVPIPKTGTLSCTVALRPKTGSQDQEVHRTVFMRLNIISPDLSGCTSKGLVLPAVLGITFGAFLIGALLTAALWYIYSHTRSPSKREPVVAVAAPASSESSSTNHSIGSTQSTPCSTSSMA
Protein: Transforming acidic coiled-coil protein, isoform A (Q8IPN1)
Organism: Drosophila melanogaster (Fruit fly)
Subcellular location: Cytoplasm, cytoskeleton {ECO:0000256|ARBA:ARBA00004245}.
Interaction partners:
Sequence:
MEFDDAENGLGMGFGGRGVLREINKNDGGIKLSPLAVKPSPKPTSMDQQKAMAAALGHQTAVPGGLKPEDDLVPKFGGLPEFDETQIPELAPLSTDMDTQLKSNHSDSDVFVECLSLHSERYTGDRSELEAYSSALNDVLEQQLSMTSVSTLGAEFNDPLAVSQHNNVSYEAMDVDDLNETMEMLKDVLNAEDRHLMQTHILSVTQSKPENNFVHYHPNQEQNRVELDQLAKHSKPNSDAKESESLVESVLSEESGTQSFEPKLTLSALDSTKDLAKHQEEMQTNTKDIFQKEKHHPVSSAQVKDAQNPKEPEKALNLKEASSELSTKSAKSLEYPNQEKQFSVAVESMERPCTAISLEQNASPAMEATEDRTVEELDQMDVDESMKVDDATVLNSCRQEQINAHSPVSSKFFLKLCVQNDTDCQDNKMDQKTAGKESALKMTEIELPVESVPSASLSPPTPALQAKIIELSLSPPIPTHRPKTAEELEFLALRELPLPDGVSTAGKVECKQLSHGLVPIVAVLPTPLYLDLKGNTTTASLPEPTSPSFPIKEPAEKQSHFPRSPRAQLEQKDMPYLEEAVVERSSHRKQSDFGVIAKSPIVFELTQPSPEKQHLNETLPMSEISPTSSNMTFDSGSITEDKSQKGTENIEPSSTLAVSLGSVDDKQRRTFSVVQPTKEEEEAKSRRTFCMENENPRRTFCMQQNASPAVEATEDTGADEVMDVDISMRADEVAVMKSHQQTWKERQAPISNSPPIPTHQRLNRPPEAISPVSPLGNGTVVLEEQTLSAKEQATLSASDEKDDVFLEHFGAISPVSDDMFKTSSASNNQAKFRVNADEETGGKGASAMIRKRSGTAGEQEEIFDAEFHDGVNNQNLILNSSDFDYLYTKGSNSVPIDRSSLLLKFDPLLGAPVPVNHPNQQEQALQNILGSNQHQNRLLSPTLEEHETSDGNQSFGVISSAKDTAKKWDFKPPVDRTKHVKMSVDVIDNDCNKTFDNSNTNTEDKTHNYNDMDELEKKIKNEVTRSEDIEKKLKEGELREEALIKRITEKDKTNAKLNGVIEAYEKAIAELISEKEQQAQLHERQLQEVQADRDANYHHLTSLETTFSDLHVKYEKSKEMTSQLKSNEESLLAERKQMMDNLRLQEQRYDKMKNHAMQQLEIANKKLDTYSREHADETKKLKALLKKEEISRVSMTEQLQQKSRENADLLKICEELIYGKGQGGSS
Protein: Remorin 4.1 (AtREM4.1) (Remorin group 4 member 1) (Q93YN8)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Collaborates with REM4.2 to positively regulate the BCTV and BSCTV susceptibility.
Subcellular location: Cell membrane {ECO:0000269|PubMed:25289013}.
Interaction partners:
- Plant calmodulin-binding protein-like protein
- ADP-glucose phosphorylase
- Thylakoid lumenal P17.1 protein
- At5g43150
- dCTP pyrophosphatase 1
- At2g22080
- Stress-response A/B barrel domain-containing protein HS1
- B3 domain-containing protein REM1
- Galactose mutarotase
- Galactose mutarotase-like superfamily protein
Sequence:
MLTLYGQERSPENSTTSTTDASDRRDETPSSEIVVRDIHAMTTTTELTRPQQRGSGGGYLSPSRSIAFSDGTTSSGENFTTVSREFNALVIAGSSMDNNSNGTNQSGGHRDVIRDERNELTRIGENDDVGDHGQVPEEDSNPWAIVPDDYNNRDGSENNIVLASSGGQNRMVTTASVQRVKREEVEAKITAWQTAKVAKINNRFKRQDAVINGWLNEQVHRANSWMKKIERKLEDRRAKAMEKTQNKVAKAQRKAEERRATAEGKRGTEVARVLEVANLMRAVGRPPAKRSFFSLS
Protein: Organic solute transporter subunit beta (OST-beta) (Solute carrier family 51 subunit beta) (Q80WK2)
Organism: Mus musculus (Mouse)
Function: Essential component of the Ost-alpha/Ost-beta complex, a heterodimer that acts as the intestinal basolateral transporter responsible for bile acid export from enterocytes into portal blood. The Ost-alpha/Ost-beta complex efficiently transports the major species of bile acids (taurocholate). Taurine conjugates are transported more efficiently across the basolateral membrane than glycine-conjugated bile acids. Can also transport steroids such as estrone 3-sulfate and dehydroepiandrosterone 3-sulfate, therefore playing a role in the enterohepatic circulation of sterols (By similarity). Able to transport eicosanoids such as prostaglandin E2 (By similarity). Modulates SLC51A glycosylation, membrane trafficking and stability activities.
Subcellular location: Cell membrane {ECO:0000269|PubMed:15563450, ECO:0000269|PubMed:17650074, ECO:0000269|PubMed:22535958}; Single-pass membrane protein {ECO:0000269|PubMed:15563450, ECO:0000269|PubMed:17650074, ECO:0000269|PubMed:22535958}. Note=Mainly restricted to the lateral and basal membranes of ileal enterocytes.
Interaction partners:
- Organic solute transporter subunit alpha
- Ileal sodium/bile acid cotransporter
- Bile salt export pump
- Bile acid receptor
- Hepatic sodium/bile acid cotransporter
- Cytochrome P450 7A1
- Nuclear receptor subfamily 0 group B member 2
- Fibroblast growth factor 15
- 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase
- Gastrotropin
Sequence:
MDHSAEKAAANAEVPQELLEEMLWYFRAEDAAPWNYSILVLAVLVVMTSMFLLRRSILANRNRKKQPQDKETPEDLHLDDSIMKENNSQVFLRETLISEKPDLAPGEPELKEKDSSLVFLPDPQETES
Protein: HTH-type transcriptional regulator CueR (Copper efflux regulator) (Copper export regulator) (P0A9G4)
Organism: Escherichia coli (strain K12)
Function: Regulates the transcription of the copA and cueO genes. It detects cytoplasmic copper stress and activates transcription in response to increasing copper concentrations.
Subcellular location: Cytoplasm {ECO:0000305}.
Interaction partners:
- RNA polymerase sigma factor RpoD
- Multicopper oxidase CueO
- Copper-exporting P-type ATPase
- Transcriptional regulatory protein CusR
- Cation efflux system protein CusF
- Zinc/cadmium/lead-transporting P-type ATPase
- Cation efflux system protein CusA
- DNA-directed RNA polymerase subunit beta
- DNA-directed RNA polymerase subunit alpha
- DNA-directed RNA polymerase subunit omega
Sequence:
MNISDVAKITGLTSKAIRFYEEKGLVTPPMRSENGYRTYTQQHLNELTLLRQARQVGFNLEESGELVNLFNDPQRHSADVKRRTLEKVAEIERHIEELQSMRDQLLALANACPGDDSADCPIIENLSGCCHHRAG