wanglab/gogpt-training-data huggingface dataset:
Protein: Orexin/Hypocretin receptor type 1 (Hypocretin receptor type 1) (Orexin receptor type 1) (Ox-1-R) (Ox1-R) (Ox1R) (P58307)
Organism: Mus musculus (Mouse)
Function: Moderately selective excitatory receptor for orexin-A and, with a lower affinity, for orexin-B neuropeptide. Triggers an increase in cytoplasmic Ca(2+) levels in response to orexin-A binding.
Subcellular location: Cell membrane {ECO:0000250|UniProtKB:O43613}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O43613}.
Interaction partners:
- Hypocretin neuropeptide precursor
- Orexin receptor type 2
- Corticotropin-releasing factor receptor 1
Sequence:
MEPSATPGAQPGVPTSSGEPFHLPPDYEDEFLRYLWRDYLYPKQYEWVLIAAYVAVFLIALVGNTLVCLAVWRNHHMRTVTNYFIVNLSLADVLVTAICLPASLLVDITESWLFGQALCKVIPYLQAVSVSVAVLTLSFIALDRWYAICHPLLFKSTARRARGSILGIWAVSLAVMVPQAAVMECSSVLPELANRTRLFSVCDEHWADELYPKIYHSCFFIVTYLAPLGLMAMAYFQIFRKLWGRQIPGTTSALVRNWKRPSEQLEAQHQGLCTEPQPRARAFLAEVKQMRARRKTAKMLMVVLLVFALCYLPISVLNVLKRVFGMFRQASDREAVYACFTFSHWLVYANSAANPIIYNFLSGKFREQFKAAFSCCLPGLGPGSSARHKSLSLQSRCSVSKVSEHVVLTTVTTVLS
Protein: Segment polarity protein dishevelled homolog DVL-1 (Dishevelled-1) (DSH homolog 1) (O14640)
Organism: Homo sapiens (Human)
Function: Participates in Wnt signaling by binding to the cytoplasmic C-terminus of frizzled family members and transducing the Wnt signal to down-stream effectors. Plays a role both in canonical and non-canonical Wnt signaling. Plays a role in the signal transduction pathways mediated by multiple Wnt genes. Required for LEF1 activation upon WNT1 and WNT3A signaling. DVL1 and PAK1 form a ternary complex with MUSK which is important for MUSK-dependent regulation of AChR clustering during the formation of the neuromuscular junction (NMJ).
Subcellular location: Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Localizes at the cell membrane upon interaction with frizzled family members. {ECO:0000250}.
Interaction partners:
- Glycogen synthase kinase-3 beta
- Axin-1
- Disheveled-associated activator of morphogenesis 1
- Inversin
- Low-density lipoprotein receptor-related protein 5
- Vang-like protein 2
- Low-density lipoprotein receptor-related protein 6
- Vang-like protein 1
- Proto-oncogene FRAT1
- Protein naked cuticle homolog 2
Sequence:
MAETKIIYHMDEEETPYLVKLPVAPERVTLADFKNVLSNRPVHAYKFFFKSMDQDFGVVKEEIFDDNAKLPCFNGRVVSWLVLAEGAHSDAGSQGTDSHTDLPPPLERTGGIGDSRPPSFHPNVASSRDGMDNETGTESMVSHRRERARRRNREEAARTNGHPRGDRRRDVGLPPDSASTALSSELESSSFVDSDEDGSTSRLSSSTEQSTSSRLIRKHKRRRRKQRLRQADRASSFSSITDSTMSLNIVTVTLNMERHHFLGISIVGQSNDRGDGGIYIGSIMKGGAVAADGRIEPGDMLLQVNDVNFENMSNDDAVRVLREIVSQTGPISLTVAKCWDPTPRSYFTVPRADPVRPIDPAAWLSHTAALTGALPRYGTSPCSSAVTRTSSSSLTSSVPGAPQLEEAPLTVKSDMSAVVRVMQLPDSGLEIRDRMWLKITIANAVIGADVVDWLYTHVEGFKERREARKYASSLLKHGFLRHTVNKITFSEQCYYVFGDLCSNLATLNLNSGSSGTSDQDTLAPLPHPAAPWPLGQGYPYQYPGPPPCFPPAYQDPGFSYGSGSTGSQQSEGSKSSGSTRSSRRAPGREKERRAAGAGGSGSESDHTAPSGVGSSWRERPAGQLSRGSSPRSQASATAPGLPPPHPTTKAYTVVGGPPGGPPVRELAAVPPELTGSRQSFQKAMGNPCEFFVDIM
Protein: Triacylglycerol lipase ptl1 (EC 3.1.1.3) (Q9Y7P3)
Organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Function: Lipid particle-localized triacylglycerol (TAG) lipase. The lipid droplet/particle is a lipid storage compartment which serves as a depot of energy and building blocks for membrane lipid biosynthesis. Involved in the mobilization of the non-polar storage lipids triacylglycerols (TAGs) from lipid particles by hydrolysis of TAGs, releasing and supplying specific fatty acids to the appropriate metabolic pathways.
Subcellular location: Lipid droplet {ECO:0000250|UniProtKB:P40308}. Note=Partially retained in the endoplasmic reticulum in cells lacking triacylglycerols. {ECO:0000250|UniProtKB:P40308}.
Interaction partners:
- Putative lipase atg15
- Diacylglycerol O-acyltransferase 1
- Phospholipid:diacylglycerol acyltransferase
- Triacylglycerol lipase ptl3
- Putative monoglyceride lipase
- Putative phospholipase A2
- Nuclear elongation and deformation protein 1
- Probable diacylglycerol pyrophosphate phosphatase 1
- Long-chain-fatty-acid--CoA ligase 2
- Long-chain-fatty-acid--CoA ligase 1
Sequence:
MTALFNFWRIMYANISSIWLLVVSFFEWLFSATSISQQRGSGPRKGKVVMNKDCRSWEDWKVLATTIDKASGRWKWRFTPASDKYDYLLIDRCTVSLKRYRQRKSVYPMLMFLRSSLLRNFGNIGNSSLYTENYSGTKILIEEYVREVNNCLEFLYHTKRLSYDVKCDFFSAARISFGTTCLYFNGGTAFGLYHFGVAKTLWKRNLLPQILAGCASGALIASLLSVYRDEELNGLFDTFPSELWKICQQTSDYSLSKVVEYGNMLDISMIASFVRQRLGTITFQEAFERTGRIVNIVAPPSAVSGSPQVLNYFTAPNVLIWSAVCSSNSWAAIYRSSPLLAKLPDGSTEVCTPKNFIWPYAGLPNTGRSNPYARISEIFNVNHFVITQSRPSLFPTFYDELHHHRVSGYSLKMIRLVGLEMAYRFRQLDILGLLPPRLRRFFVDDYVPSAYITLTPTFSFSDIKHAFTKPSLSDIQYWILVGERATWQAIPLLQVRCKTEISLRHLSKNLTNSYVEPLSVNNLASPFVTNLEENQEKMLKIFKVK
Protein: Rab18 (Q9NJQ1)
Organism: Trypanosoma brucei
Interaction partners:
Sequence:
MAQGDNSPVKIVLLGESGVGKSSLLLSFSLGTFDGDVRSTIGIDFRTKDVSVVDSMGRQKKLKLHLWDTAGQERFRTLTSSYYRGAHAVVLVYDVNEPQTFHALRKWIDEADAFCRLDGVEEAVVYLLVGNKIDKCEVGGGATGMAVPKEDAQQLARDRHMLLAFTSAKTRVGVEQAFDEVARSAYEKMMSKSESRYSGVNLSKTSDPTSGAVCC
Protein: Chromatin structure-remodeling complex protein RSC58 (Remodel the structure of chromatin complex subunit 58) (Q07979)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Component of the chromatin structure-remodeling complex (RSC), which is involved in transcription regulation and nucleosome positioning. RSC is responsible for the transfer of a histone octamer from a nucleosome core particle to naked DNA. The reaction requires ATP and involves an activated RSC-nucleosome intermediate. Remodeling reaction also involves DNA translocation, DNA twist and conformational change. As a reconfigurer of centromeric and flanking nucleosomes, RSC complex is required both for proper kinetochore function in chromosome segregation and, via a PKC1-dependent signaling pathway, for organization of the cellular cytoskeleton.
Subcellular location: Nucleus {ECO:0000269|PubMed:12697820}. Note=Localizes to centromeric and flanking chromatin. Association with these loci is dependent on STH1.
Interaction partners:
- Actin-like protein ARP9
- Chromatin structure-remodeling complex subunit RSC1
- High temperature lethal protein 1
- Regulator of Ty1 transposition protein 102
- Nuclear protein STH1/NPS1
- Chromatin structure-remodeling complex subunit RSC7
- Chromatin structure-remodeling complex protein RSC3
- Chromatin structure-remodeling complex subunit RSC2
- Chromatin structure-remodeling complex subunit RSC4
- Chromatin structure-remodeling complex protein RSC6
Sequence:
MTESVGGNKLVDFLVNVQSILNAASVKCHVVDESFPAKFFEKNPDKIYESYCKFIKNRSNSEGLIRNEDKLVLTTINKRFENGEYEPIQGGFYKLYHDIKLVCTILIHFYPQGTRNYQLVDKFYKFSSELLLRECCRIGIALTQTNNIKSRSGKLLSGNEMDEYDDDDATELDKIISYDFIKISMNYTVPISQTYQIRTKDMDLFSSIISKSNLDKRPHELPNTNFKINNVLPQTDIENEAPRLGFVGANTSNIPDPTLPPTEMMTRFLHPNWYALPTTVWLKYGNYNSWAPSFNENGTVVDSTTRGLIWLERIGYMDLYEKNEKKVKQEELLNTNEEGINRKQNDENNKNVDGKSNGVQDDGGDNDNDATIASANSESTENKEQFIIKLQNLYNWTPSNYIGDDEIENFRNGTPDKLVSDSLLKLKRLRKERILNKVLKPTTEERELYFKVKRILKEVILAKKVSKVPINNVRAFPVLQTNYNGSIPVVRAQPGRKRKHKK
Protein: Glucose-6-phosphate isomerase (EC 5.3.1.9) (Q8ILA4)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
- Probable ATP-dependent 6-phosphofructokinase
- Bifunctional glucose-6-phosphate 1-dehydrogenase/6-phosphogluconolactonase
- Phosphotransferase
- transketolase
- Enolase
- glutamine--fructose-6-phosphate transaminase
- Glyceraldehyde-3-phosphate dehydrogenase
- Fructose-bisphosphate aldolase
- Triosephosphate isomerase
- Phosphoglucomutase, putative
Sequence:
MNMEITNLKSYKELVTLSAEEKTKDLKDYLNDKNRSESLIKKFKNFYMDLSRQRYSEKTLNKLVEYAEEVELKKKVEKTFMGEKVNMTENRSVLHTALRIPIEKINTHKIIIDNKNVLEDVHGVLKKIEKYSDDIRNGVIKTCKNTKFKNVICIGIGGSYLGTEFVYEAMKYYYYNMELNKNEKDQVNNFNNNYDQDNVFNVRFLANVDPNDVNRAIQNLDQYDTLVIIISKTFTTAETMLNARSIKKWLSLKIKDDENLSKHMVAVSTNLKLTDEFGISRDNVFEFWDWVGGRFSVTSSVGILPLSIAFGYKNMRNFLNGCHDMDEHFLHADLKENIPVLLALTSFYNSHFFDYKNVAILPYFQNLLKFSAHIQQLSMESNGKSVDRNNQPIHYNTCQVYFGEPGTNGQHSFYQLIHQGQVIPVELIGFKHSHFPIKFDKEVVSNHDELMTNFFAQADALAIGKTYEQVKEENEKNKMSPELLTHKVFNGNRPSTLLLFDELNFYTCGLLLSLYESRIVAEGFLLNINSFDQWGVELGKVLAKEVRNYFNDTRNQKKSDNTYNFNESTKILLNYYLSK
Protein: Tetratricopeptide repeat protein 17 (TPR repeat protein 17) (E7F211)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Function: Plays a role in primary ciliogenesis by modulating actin polymerization.
Subcellular location: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}.
Interaction partners:
- Ubiquitin domain-containing protein UBFD1
- Fucosyltransferase
Sequence:
MTRSFRVEWTDGRKMADDKSNSIGDNSTNKRLWSSSIRGSALIFICALLAEPARATTHWVVTEDGKIQQQVDSPLNLKHPHHLVLFMQQETRVNYLKKLEKQLVAQKIHIEENEDRDTGLEQRHYKEDADCVTAKVPLGDLDLYDGTFISLESKDINPEQFLDLMSALPPDLEKPDCAKLLDLPYSIHAFQHLRGVQEKVNLTSPLLSKDDPIFTSLCLKLGQSVDEVGHRIHQALLKNSSSWVLYNLASFYWRIKNEPRRAVDCVVRALHFSPRQHKDVALVNMANVLHRAHFSADAAILAHAALDLTTDLLTSHYTLGNIYAMLGEYNHSVLCYEQALQAQPGFEQALRRKHAVLCQQKLEQRLEAQHRSLQRTLNELKEYQKQHDHYLRQQEMLDKHKLIQEEQILRNIIHETQMAKEAQLGNHQMCHMGQQKFTLHCPFDLPVRYHRGELFENVHYIQFGEEVSVASSVALVSELSVNESHSPQQSYTVSLGREPAAHWDKETTTTDESRTVLWPRRSDCAQRFPTIPPAYLLPTYYLPPESRNLKALNILLESISPPPSAKMPDCSLKNVVGNRDPLESMSWALEKELRDPQAAEVLLKRSGGRSLEQTGALIAQALEKMSGPRWMMQNEAGLFWRAKGNGTQALVCLRQALHSAPPQHRDLPLVNTANLLLHYGLHSEAHELLQQALQINQSEPHTLLSLVNVHLSQGNLTGALAVFRQALSLSVHCGQCRASLPLMRCLQFYPFLYNLQHQACSSGGACEVEEDSELEDWDTGSSSSGRQEVWDSDAMPVSALEDSLLFEKVVVDSNGSGEASGQDRTREPKAEGGEEEEQDWRLREELIGAFEGALDMNGKTGDLRGIRVLKNDRVMGARGGGPCFGNCEDDEGAEWITFQVKRVKKPKSDASEGWVGEGDVRQTEPTASNSILEISGPTIPSPGPSERWKDYSSLGWPGPEECQRTRRVDLTTVASTWLAVSAKNIDITEHIDFATPLQEPAVEPVCNANLPASMHTLDHLSGVANRGGIHYTGESQLREVLQNLGKDKFPSQSFEQVGTRIAKVLEKNQTSWVLSSMAALYWRVKGQGKRAIDCLRQALNYAPHHMKDVPLISLANIFQNARLWEDALTVARMAVEIAPHFVVNHFTLANVYIAMEEFEKAMHWYESTLKLQPEFGPAKDRLRTIQCYLLSKRDRRAP
Protein: T-box brain protein 1 (T-brain-1) (TBR-1) (TES-56) (Q64336)
Organism: Mus musculus (Mouse)
Function: Transcriptional repressor involved in multiple aspects of cortical development, including neuronal migration, laminar and areal identity, and axonal projection. As transcriptional repressor of FEZF2, it blocks the formation of the corticospinal (CS) tract from layer 6 projection neurons, thereby restricting the origin of CS axons specifically to layer 5 neurons.
Subcellular location: Nucleus {ECO:0000250|UniProtKB:Q16650}.
Interaction partners:
- Peripheral plasma membrane protein CASK
- DNA-binding protein SATB2
- Paired box protein Pax-6
- Neurogenic differentiation factor 6
- Fez family zinc finger protein 2
- Homeobox protein cut-like 1
- Forkhead box protein G1
- B-cell lymphoma/leukemia 11B
- Forkhead box protein P2
- Homeobox protein EMX1
Sequence:
MQLEHCLSPSIMLSKKFLNVSSSYPHSGGSELVLHDHPIISTTDNLERSSPLKKITRGMTNQSDTDNFPDSKDSPGDVQRSKLSPVLDGVSELRHSFDGSAADRYLLSQSSQPQSAATAPSAMFPYPSQHGPAHPAFSIGSPSRYMAHHPVITNGAYNSLLSNSSPQGYPTAGYPYPQQYGHSYQGAPFYQFSSTQPGLVPGKAQVYLCNRPLWLKFHRHQTEMIITKQGRRMFPFLSFNISGLDPTAHYNIFVDVILADPNHWRFQGGKWVPCGKADTNVQGNRVYMHPDSPNTGAHWMRQEISFGKLKLTNNKGASNNNGQMVVLQSLHKYQPRLHVVEVNEDGTEDTSQPGRVQTFTFPETQFIAVTAYQNTDITQLKIDHNPFAKGFRDNYDTIYTGCDMDRLTPSPNDSPRSQIVPGARYAMAGSFLQDQFVSNYAKARFHPGAGAGPGPGTDRSVPHTNGLLSPQQAEDPGAPSPQRWFVTPANNRLDFAASAYDTATDFAGNAATLLSYAAAGVKALPLQAAGCTGRPLGYYADPSGWGARSPPQYCGAKSGSVLPCWPNSAAAAARMAGANPYLGEEAEGLAAERSPLAPAAEDAKPKDLSDSSWIETPSSIKSIDSSDSGIYEQAKRRRISPADTPVSESSSPLKSEVLAQRDCEKNCAKDIGGYYGFYSHS
Protein: Defensin beta 118 (Beta-defensin 118) (Epididymal secretory protein 13.6) (ESP13.6) (Q95LI0)
Organism: Macaca mulatta (Rhesus macaque)
Function: Host defense peptide that exhibits antimicrobial activity against both Gram-negative bacteria, such as E.coli and S.typhimurium, and Gram-positive bacteria, such as S.aureus and B.subtilis (By similarity). Inhibits cell adhesion of E.coli on intestinal epithelial enterocytes (By similarity). Causes rapid permeabilization of both the outer and inner membrane of E.coli, leading to morphological alterations on the bacterial surface (By similarity). Binds to bacterial lipopolysaccharides (LPS) with high affinity, and may thereby be involved in immunoregulation through LPS neutralization (By similarity). May contribute to epididymal innate immunity and protect the sperm against attack by microorganisms (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:11564719}.
Interaction partners:
- Beta-defensin
- Beta-defensin
- Beta-defensin 122
- Defensin beta 129
- Beta-defensin 1
- Synaptonemal complex protein 3
Sequence:
MKLLLLALPILVLLPQVIPAYGGEKKCWNRSGHCRKQCKDGEAVKETCKNHRACCVPSNEDHRRLPTTSPTPLSDSTPGIIDNILTIRFTTDYFEISSKKDMVEESEAGQGTQTSPPNVHHTS
Protein: Opioid receptor, delta 1a (A3QJX7)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
Interaction partners:
- Pro-opiomelanocortin protein
- Proenkephalin a
- Proenkephalin b.
- Phosphatase and actin regulator 4A.
- Phosphatase and actin regulator 4A
- Zinc finger protein 131
- Prodynorphin.
Sequence:
MEPSVIPGADIPDLYSINPFNVTFPDDVLSFVPDGRNYTEPNPVKSPAGIIIAISITALYSVICVVGLLGNILVMYGVVRYTKLKTATNIYIFNLALADALATSTLPFQSTKYLMNTWPFGELLCKVVIAIDYYNMFTSIFTLTMMSVDRYIAVCHPVRALEFRTPIKAKIINVCIWILSSAVGVPIMIMAVTRVTNQNTTVCMLKFPDPDWYWDTVTKICVFIFAFVVPVLVITICYGLMILRLKSVRLLSGSKEKDRNMRRITRMVLVVVAAFIICWTPIHIFIIVKTLVDINQKNPFVIASWHLCIALGYTNSSLNPVLYAFLDENFKRCFRDFCLPFRTRADQSNLNRARNATREPVSVCAPSDTGKKPV
Protein: N-alpha-acetyltransferase 15, NatA auxiliary subunit (A0A0B4J1W3)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPAVSLPPKENALFKRILRCYEHKQYRNGLKFCKQILSNPKFAEHGETLAMKGLTLNCLGKKEEAYELVRRGLRNDLKSHVCWHVYGLLQRSDKKYDEAIKCYRNALKWDKDNLQILRDLSLLQIQMRDLEGYRETRYQLLQLRPAQRASWIGYAIAYHLLEDYEMAAKILEEFRKTQQTSPDKVDYEYSELLLYQNQVLREAGLYREALEHLCTYEKQICDKLAVEETKGELLLQLCRLEDAADVYRGLQERNPENWAYYKGLEKALKPANMLERLKIYEEAWTKYPRGLVPRRLPLNFLSGEKFKECLDKFLRMNFSKGCPPVFNTLRSLYKDKEKVAIIEELVVGYETSLKSCRLFNPNDDGKEEPPTTLLWVQYYLAQHYDKIGQPSIALEYINTAIESTPTLIELFLVKAKIYKHAGNIKEAARWMDEAQALDTADRFINSKCAKYMLKANLIKEAEEMCSKFTREGTSAVENLNEMQCMWFQTECAQAYKAMNKFGEALKKCHEIERHFIEITDDQFDFHTYCMRKITLRSYVDLLKLEDVLRQHPFYFKAARIAIEIYLKLHDNPLTDENKEHEADTANMSDKELKKLRNKQRRAQKKAQIEEEKKNAEKEKQQRNQKKKKDDDDEEIGGPKEELIPEKLAKVETPLEEAIKFLTPLKNLVKNKIETHLFAFEIYFRKEKFLLMLQSVKRAFAIDSSHPWLHECMIRLFNTVCESKDLSDTVRTVLKQEMNRLFGATNPKNFNETFLKRNSDSLPHRLSAAKMVYYLDPSSQKRAIELATTLDESLTNRNLQTCMEVLEALYDGSLGDCKEAAEIYRANCHKLFPYALAFMPPGYEEDMKITVNGDSSAEAEELANEI
Protein: Coiled-coil domain-containing protein 170 (Q8IYT3)
Organism: Homo sapiens (Human)
Function: Plays a role in Golgi-associated microtubules organization and stabilization.
Subcellular location: Golgi apparatus {ECO:0000269|PubMed:28687497}.
Interaction partners:
- Damage-control phosphatase ARMT1
- Estrogen receptor
- Required for meiotic nuclear division protein 1 homolog
- Zinc finger HIT domain-containing protein 1
Sequence:
MSLDCTSHIALGAASPAPEETYDHLSEVPVTREQLNHYRNVAQNARSELAATLVKFECAQSELQDLRSKMLSKEVSCQELKAEMESYKENNARKSSLLTSLRDRVQELEEESAALSTSKIRTEITAHAAIKENQELKKKVVELNEKLQKCSKENEENKKQVSKNCRKHEEFLTQLRDCLDPDERNDKASDEDLILKLRDLRKENEFVKGQIVILEETINVHEMEAKASRETIMRLASEVNREQKKAASCTEEKEKLNQDLLSAVEAKEALEREVKIFQERLLAGQQVWDASKQEVSLLKKSSSELEKSLKASQDAVTTSQSQYFSFREKIAALLRGRLSMTGSTEDTILEKIREMDSREESRDRMVSQLEAQISELVEQLGKESGFHQKALQRAQKAENMLETLQGQLTHLEAELVSGGVLRDNLNFEKQKYLKFLDQLSQKMKLDQMAAELGFDMRLDVVLARTEQLVRLESNAVIENKTIAHNLQRKLKTQKERLESKELHMSLLRQKIAQLEEEKQARTALVVERDNAHLTIRNLQKKVERLQKELNTCRDLHTELKAKLADTNELKIKTLEQTKAIEDLNKSRDQLEKMKEKAEKKLMSVKSELDTTEHEAKENKERARNMIEVVTSEMKTLKKSLEEAEKREKQLADFREVVSQMLGLNVTSLALPDYEIIKCLERLVHSHQHHFVTCACLKDVTTGQERHPQGHLQLLH
Protein: Acetyl-CoA:benzylalcohol acetyltranferase-like protein (At5g47950) (HXXXD-type acyl-transferase family protein) (Putative acetyl-CoA:benzylalcohol acetyltranferase) (Q9FGV4)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Interaction partners:
Sequence:
MDTMKVETIGKEIIKPSATTPTDLSTLQLSIMDILMPPVYAVAFLFYTKDDLISQEQTSHTLKTSLSEILTKFHPLAGRVNGVTIKSTDEGAVFVEARVDNCDLSGFLRSPDTESLKQLLPVDDEPAPTWPLLLVKATYFRCGGMAIGLCISHRLADAASLSIFLQAWAATARGESDLVASPDFCSTKLYPAANEAIKIPGEVVNRTSVTKRFVFVASKIEELRNKVASDVVPRPTRVQSVTSLIWKCVVTASTDTIREKALFQPANLRTKIPSLLSENQIGNLLFNSLILDGKAGMDIVETVKELQKRAEDLSGLVQDEEGSSMTIGWRLFGEIINSKFNREDHDMHSVTSWCKIPLYDACFGWGSPVWVAGSVSPNLDYVTVLIDSKDGQGIEAWVTLPQENMLLLEQSTELLAFASPNPSVLI
Protein: Small glutamine-rich tetratricopeptide repeat-containing protein alpha (Alpha-SGT) (Vpu-binding protein) (UBP) (O43765)
Organism: Homo sapiens (Human)
Function: Co-chaperone that binds misfolded and hydrophobic patches-containing client proteins in the cytosol. Mediates their targeting to the endoplasmic reticulum but also regulates their sorting to the proteasome when targeting fails. Functions in tail-anchored/type II transmembrane proteins membrane insertion constituting with ASNA1 and the BAG6 complex a targeting module. Functions upstream of the BAG6 complex and ASNA1, binding more rapidly the transmembrane domain of newly synthesized proteins. It is also involved in the regulation of the endoplasmic reticulum-associated misfolded protein catabolic process via its interaction with BAG6: collaborates with the BAG6 complex to maintain hydrophobic substrates in non-ubiquitinated states. Competes with RNF126 for interaction with BAG6, preventing the ubiquitination of client proteins associated with the BAG6 complex. Binds directly to HSC70 and HSP70 and regulates their ATPase activity.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16580629}. Nucleus {ECO:0000269|PubMed:16580629}. Note=Co-localizes with HSP90AB1 in the cytoplasm. Increased nuclear accumulation seen during cell apoptosis. {ECO:0000269|PubMed:16580629}.
Interaction partners:
- Golgi to ER traffic protein 4 homolog
- Ubiquitin-like protein 4A
- Heat shock cognate 71 kDa protein
- Large proline-rich protein BAG6
- Heat shock 70 kDa protein 4
- Heat shock protein 105 kDa
- ATPase GET3
- Heat shock protein HSP 90-alpha
- BAG family molecular chaperone regulator 2
- Guided entry of tail-anchored proteins factor 1
Sequence:
MDNKKRLAYAIIQFLHDQLRHGGLSSDAQESLEVAIQCLETAFGVTVEDSDLALPQTLPEIFEAAATGKEMPQDLRSPARTPPSEEDSAEAERLKTEGNEQMKVENFEAAVHFYGKAIELNPANAVYFCNRAAAYSKLGNYAGAVQDCERAICIDPAYSKAYGRMGLALSSLNKHVEAVAYYKKALELDPDNETYKSNLKIAELKLREAPSPTGGVGSFDIAGLLNNPGFMSMASNLMNNPQIQQLMSGMISGGNNPLGTPGTSPSQNDLASLIQAGQQFAQQMQQQNPELIEQLRSQIRSRTPSASNDDQQE
Protein: Membrane progestin receptor alpha (mPR alpha) (Membrane progesterone P4 receptor alpha) (Membrane progesterone receptor alpha) (Progesterone and adipoQ receptor family member 7) (Progestin and adipoQ receptor family member 7) (Progestin and adipoQ receptor family member VII) (Q86WK9)
Organism: Homo sapiens (Human)
Function: Plasma membrane progesterone (P4) receptor coupled to G proteins. Seems to act through a G(i) mediated pathway. May be involved in oocyte maturation. Involved in neurosteroid inhibition of apoptosis. Also binds dehydroepiandrosterone (DHEA), pregnanolone, pregnenolone and allopregnanolone.
Subcellular location: Cell membrane {ECO:0000303|PubMed:23763432}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Membrane-associated progesterone receptor component 1
- Membrane-associated progesterone receptor component 2
- Membrane progestin receptor delta
- Adiponectin
Sequence:
MAMAQKLSHLLPSLRQVIQEPQLSLQPEPVFTVDRAEVPPLFWKPYIYAGYRPLHQTWRFYFRTLFQQHNEAVNVWTHLLAALVLLLRLALFVETVDFWGDPHALPLFIIVLASFTYLSFSALAHLLQAKSEFWHYSFFFLDYVGVAVYQFGSALAHFYYAIEPAWHAQVQAVFLPMAAFLAWLSCIGSCYNKYIQKPGLLGRTCQEVPSVLAYALDISPVVHRIFVSSDPTTDDPALLYHKCQVVFFLLAAAFFSTFMPERWFPGSCHVFGQGHQLFHIFLVLCTLAQLEAVALDYEARRPIYEPLHTHWPHNFSGLFLLTVGSSILTAFLLSQLVQRKLDQKTK
Protein: Prenyltransferase vrtC (EC 2.5.1.-) (Viridicatumtoxin synthesis protein C) (D7PHZ4)
Organism: Penicillium aethiopicum
Function: Prenyltransferase; part of the gene cluster that mediates the biosynthesis of viridicatumtoxin, a tetracycline-like fungal meroterpenoid with a unique, fused spirobicyclic ring system. The first step of the pathway is the production of the malonamoyl-CoA starter unit for the polyketide synthase vrtA. The aldolase vrtJ may be involved in the synthesis of the malonamate substrate for malonamoyl-CoA synthetase vrtB. The polyketide synthase vrtA then may utilize the malonamoyl-CoA starter unit, followed by sequential condensation of eight malonyl-CoA units to form the polyketide backbone. The cyclization of the last ring could be mediated by the lactamase-like protein vrtG. The proposed post-PKS tailoring steps are an hydroxylation at C5 catalyzed the cytochrome P450 monooxygenase vrtE, a hydroxylation at C12a catalyzed by VrtH and/or VrtI, and an O-methylation by the O-methyltransferase vrtF. VrtC is then proposed to catalyze the transfer of a geranyl group synthesized by vrtD to the aromatic C ring of the tetracyclic polyketide intermediate of viridicatumtoxin to yield previridicatumtoxin. Finally, the cytochrome P450 monooxygenase vrtK catalyzes the spirocyclization of the geranyl moiety of previridicatumtoxin to afford viridicatumtoxin.
Interaction partners:
Sequence:
MGDATATEVFPVMDSIAVAMGDVESQLRVFHNVSRFLPTDDANQVFWWRTTGRHFAIMMHEARYSEARQVELLLFYRFVIAPRLGPRPTSATPWFHSRVAPGIGDGSPIGYSWRWGTGPDTKPLIRHYIEAIGPLTGTTADPLNEFAAKEMLYQLGQLVPGVELPLAWKFAAHIRPSLTDEPTRAVAGSSILIGLQCAPESAGIEVMAGLMTRSPAQVPELLHSIFPRAMRDAYGPDASLDGLNMVRDFVCHDPQGQYLTILGTTAIDCCAAASSRFKVYVTTTNTSFAHLAAVMTLGGRKPEAPESLTQLQELWYALKGLDPEFPVTAEPLSSVCGAANGTASGNPNANVSGVTFYFDIHPKYPFPHIKLQVDISKHTISDLGAINAVTEFLARRGQAADAQAYLNVVRAMVPDEELRTRRGLQAFFAFAFKNGAVDITSYFLPQIYRRYAEVQAELEPRKDCQGRSELSSKLQRRSRFDSY
Protein: L-galactose dehydrogenase (At-GalDH) (L-GalDH) (EC 1.1.1.316) (O81884)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Catalyzes the oxidation of L-galactose to L-galactono-1,4-lactone in the presence of NAD(+). Uses NAD(+) as a hydrogen acceptor much more efficiently than NADP(+).
Interaction partners:
- L-galactono-1,4-lactone dehydrogenase, mitochondrial
- Inositol-phosphate phosphatase
- Bifunctional phosphatase IMPL2, chloroplastic
- GDP-L-galactose phosphorylase 1
- GDP-L-galactose phosphorylase 2
- GDP-mannose 3,5-epimerase
- Phosphomannomutase
- Mannose-1-phosphate guanylyltransferase 1
- L-gulonolactone oxidase 2
- Probable truncated L-gulonolactone oxidase 7, mitochondrial
Sequence:
MTKIELRALGNTGLKVSAVGFGASPLGSVFGPVAEDDAVATVREAFRLGINFFDTSPYYGGTLSEKMLGKGLKALQVPRSDYIVATKCGRYKEGFDFSAERVRKSIDESLERLQLDYVDILHCHDIEFGSLDQIVSETIPALQKLKQEGKTRFIGITGLPLDIFTYVLDRVPPGTVDVILSYCHYGVNDSTLLDLLPYLKSKGVGVISASPLAMGLLTEQGPPEWHPASPELKSASKAAVAHCKSKGKKITKLALQYSLANKEISSVLVGMSSVSQVEENVAAVTELESLGMDQETLSEVEAILEPVKNLTWPSGIHQN
Protein: ST8 alpha-N-acetyl-neuraminide alpha-2,8-sialyltransferase 4 (A1KQY6)
Organism: Rattus norvegicus (Rat)
Subcellular location: Golgi apparatus membrane {ECO:0000256|ARBA:ARBA00004323}; Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004323}. Secreted {ECO:0000256|ARBA:ARBA00004613}.
Interaction partners:
- Neural cell adhesion molecule 1
Sequence:
MHKVSHLKRNPSPREAAQSDPSPASANCAAGRWAALENRESSTAERPSDLILGSRLHAPFANFRFLPLDYFPKTEPLYQEKVPELGQPGLSRAPKMRSIRKRWTICTISLLLIFYKTKEIARTEEHQETQLIGDGELCLSRSLVNNSDKITRKAGSTIFQHSVQGWKINSSLVLEIRKNILRFLDAERDVSVVKSSFKPGDVIHYVLDRRRTLNISHDLHSLLPEVSPMKNRRFKTCAVVGNSGILLDSGCGKEIDSHNFVIRCNLAPVVEFAADVGTKSDFITMNPSVVQRAFGGFRNESDREKFVHRLSMLNDSVLWIPAFMVKGGEKHVEWVNALILKNKLKVRTAYPSLRLIHAVRGYWLTNKVPIKRPSTGLLMYTLATRFCDEIHLYGFWPFPKDLNGKAVKYHYYDDLKYRYFSNASPHRMPLEFKTLNVLHNRGALKLTTGKCMKQ