wanglab/gogpt-training-data huggingface dataset:
Protein: Obg-like ATPase 1 (Ribosome-binding ATPase YchF) (AtYchF1) (Q9SA73)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Function: Hydrolyzes ATP, and can also hydrolyze GTP with lower efficiency. Has lower affinity for GTP (Potential). Exhibits GTPase activity (By similarity). Confers sensitivity to salinity stress by suppressing the anti-oxidation enzymatic activities and increasing lipid peroxidation thus leading to the accumulation of reactive oxygen species (ROS). Acts as negative regulator of disease resistance against bacterial pathogen.
Subcellular location: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03167}. Cytoplasm, cytosol {ECO:0000269|PubMed:23550829}. Note=Localized mainly in the cytosol under NaCl treatment, but translocates to the plasma membrane upon wounding. {ECO:0000269|PubMed:23550829}.
Interaction partners:
- Transducin/WD40 repeat-like superfamily protein
- Alanine--tRNA ligase
- AT5g37360/MNJ8_150
- Stress response protein
- Germin-like protein subfamily 1 member 15
- Heavy metal-associated isoprenylated plant protein 43
- Heavy metal-associated isoprenylated plant protein 33
- Pseudouridine synthase and archaeosine transglycosylase
- Disease resistance-like protein DSC2
- Ras-related protein RABB1a
Sequence:
MPPKAKAKDAGPVERPILGRFSSHLKIGIVGLPNVGKSTLFNTLTKLSIPAENFPFCTIEPNEARVNIPDERFDWLCQTYKPKSEIPAFLEIHDIAGLVRGAHEGQGLGNNFLSHIRAVDGIFHVLRAFEDADIIHVDDIVDPVRDLETITEELRLKDIEFVGKKIDDVEKSMKRSNDKQLKIELELLQKVKAWLEDGKDVRFGDWKTADIEILNTFQLLSAKPVVYLINLNERDYQRKKNKFLPKIHAWVQEHGGDTMIPFSGVFERSLADMAPDEAAKYCEENKLQSALPRIIKTGFSAINLIYFFTAGPDEVKCWQIRRQSKAPQAAGAIHTDFERGFICAEVMKFEDLKELGNEPAVKAAGKYRQEGKTYVVQDGDIIFFKFNVSGGGKK
Protein: Serine/threonine-protein kinase SIK3 (EC 2.7.11.1) (Salt-inducible kinase 3) (SIK-3) (Serine/threonine-protein kinase QSK) (Q9Y2K2)
Organism: Homo sapiens (Human)
Function: Positive regulator of mTOR signaling that functions by triggering the degradation of DEPTOR, an mTOR inhibitor. Involved in the dynamic regulation of mTOR signaling in chondrocyte differentiation during skeletogenesis. Negatively regulates cAMP signaling pathway possibly by acting on CRTC2/TORC2 and CRTC3/TORC3 (Probable). Prevents HDAC4 translocation to the nucleus (By similarity).
Subcellular location: Cytoplasm {ECO:0000269|PubMed:16306228}. Note=Locates to punctate structures within the cytoplasm on binding to YWHAZ. {ECO:0000269|PubMed:16306228}.
Interaction partners:
- 14-3-3 protein zeta/delta
Sequence:
MAAAAASGAGGAAGAGTGGAGPAGRLLPPPAPGSPAAPAAVSPAAGQPRPPAPASRGPMPARIGYYEIDRTIGKGNFAVVKRATHLVTKAKVAIKIIDKTQLDEENLKKIFREVQIMKMLCHPHIIRLYQVMETERMIYLVTEYASGGEIFDHLVAHGRMAEKEARRKFKQIVTAVYFCHCRNIVHRDLKAENLLLDANLNIKIADFGFSNLFTPGQLLKTWCGSPPYAAPELFEGKEYDGPKVDIWSLGVVLYVLVCGALPFDGSTLQNLRARVLSGKFRIPFFMSTECEHLIRHMLVLDPNKRLSMEQICKHKWMKLGDADPNFDRLIAECQQLKEERQVDPLNEDVLLAMEDMGLDKEQTLQSLRSDAYDHYSAIYSLLCDRHKRHKTLRLGALPSMPRALAFQAPVNIQAEQAGTAMNISVPQVQLINPENQIVEPDGTLNLDSDEGEEPSPEALVRYLSMRRHTVGVADPRTEVMEDLQKLLPGFPGVNPQAPFLQVAPNVNFMHNLLPMQNLQPTGQLEYKEQSLLQPPTLQLLNGMGPLGRRASDGGANIQLHAQQLLKRPRGPSPLVTMTPAVPAVTPVDEESSDGEPDQEAVQSSTYKDSNTLHLPTERFSPVRRFSDGAASIQAFKAHLEKMGNNSSIKQLQQECEQLQKMYGGQIDERTLEKTQQQHMLYQQEQHHQILQQQIQDSICPPQPSPPLQAACENQPALLTHQLQRLRIQPSSPPPNHPNNHLFRQPSNSPPPMSSAMIQPHGAASSSQFQGLPSRSAIFQQQPENCSSPPNVALTCLGMQQPAQSQQVTIQVQEPVDMLSNMPGTAAGSSGRGISISPSAGQMQMQHRTNLMATLSYGHRPLSKQLSADSAEAHSLNVNRFSPANYDQAHLHPHLFSDQSRGSPSSYSPSTGVGFSPTQALKVPPLDQFPTFPPSAHQQPPHYTTSALQQALLSPTPPDYTRHQQVPHILQGLLSPRHSLTGHSDIRLPPTEFAQLIKRQQQQRQQQQQQQQQQEYQELFRHMNQGDAGSLAPSLGGQSMTERQALSYQNADSYHHHTSPQHLLQIRAQECVSQASSPTPPHGYAHQPALMHSESMEEDCSCEGAKDGFQDSKSSSTLTKGCHDSPLLLSTGGPGDPESLLGTVSHAQELGIHPYGHQPTAAFSKNKVPSREPVIGNCMDRSSPGQAVELPDHNGLGYPARPSVHEHHRPRALQRHHTIQNSDDAYVQLDNLPGMSLVAGKALSSARMSDAVLSQSSLMGSQQFQDGENEECGASLGGHEHPDLSDGSQHLNSSCYPSTCITDILLSYKHPEVSFSMEQAGV
Protein: Zinc finger CCCH domain-containing protein 10 (Q96K80)
Organism: Homo sapiens (Human)
Function: Specific regulator of miRNA biogenesis. Binds, via the C3H1-type zinc finger domains, to the binding motif 5'-GCAGCGC-3' on microRNA pri-MIR143 and negatively regulates the processing to mature microRNA.
Subcellular location: Nucleus {ECO:0000269|PubMed:28431233}.
Interaction partners:
Sequence:
MPDRDSYANGTGSSGGGPGGGGSEEASGAGVGSGGASSDAICRDFLRNVCKRGKRCRYRHPDMSEVSNLGVSKNEFIFCHDFQNKECSRPNCRFIHGSKEDEDGYKKTGELPPRLRQKVAAGLGLSPADLPNGKEEVPICRDFLKGDCQRGAKCKFRHLQRDFEFDARGGGGTGGGSTGSVLPGRRHDLYDIYDLPDRGFEDHEPGPKRRRGGCCPPDGPHFESYEYSLAPPRGVECRLLEEENAMLRKRVEELKKQVSNLLATNEVLLEQNAQFRNQAKVITLSSTAPATEQTLAPTVGTVATFNHGIAQTHTTLSSQALQPRPVSQQELVAPAGAPAAPPTNAAPPAAPPPPPPHLTPEITPLSAALAQTIAQGMAPPPVSMAPVAVSVAPVAPVAVSMAQPLAGITMSHTTTPMVTYPIASQSMRITAMPH
Protein: RAB11 family interacting protein 5 (A0A1B0GTL5)
Organism: Homo sapiens (Human)
Subcellular location: Endomembrane system {ECO:0000256|ARBA:ARBA00004308}. Recycling endosome {ECO:0000256|ARBA:ARBA00004172}.
Interaction partners:
Sequence:
MALVRGAEPAAGPSRWLPTHVQVTVLRARGLRGKSSGAGSTSDAYTVIQVGREKYSTSVVEKTHGCPEWREECSFELPPGALDGLLRAQEADAGPAPWAASSAAACELVLTTMHRSLIGVDKFLGQATVALDEVFGAGRAQHTQWYKLHSKPGKKEKERGEIEVTIQFTRNNLSASMFDLSMKDKPRSPFSKIRDKMKGKKKYDLESASAILPSSAIEDPDLGSLGKMGKAKGFFLRNKLRKSSLTQSNTSLGSDSTLSSASGSLAYQGPGAELLTRSPSRSSWLSTEGGRDSAQSPKLFTHKRTYSDEANQMRVAPPRALLDLQGHLDAASRSSLCVNGSHIYNEEPQGPVRHRSSISGSLPSSGSLQAVSSRFSEEGPRSTDDTWPRGSRSNSSSEAVLGQEELSAQAKVLAPGASHPGEEEGARLPEGKPVQVATPIVASSEAVAEKEGARKEERKPRMGLFHHHHQGLSRSELGRRSSLGEKGGPILGASPHHSSSGEEKAKSSWFGLREAKDPTQKPSLDVSPQVESDPAALPHHLPCSPWAPAPPTPAPTAAPMLSTNLFAAASPAAATAAAAATTAAPEATPPGLLGLTNPFLTSLQSNPFFEELIADIALNSPSPAPSLPSASRASPTPLASPGKALPEWDNTFNVFAASRLRPEARSEILAPAGVGLEAAGLQDPGPGAMTAKAAEPQGEPGGGGGGGGGGGGRGGSSVWLEPRVPLDLGPNHQSASAADPGLLGSVGAGLPSSSAQLQLRASGSEPDRELPAPEVEAGQSPADSGTSLFSSPEVISVWERLPGPESAAEGQDDESSRGENQLCPDVETADDAWPWDVVTISPAAETASLVFRGESDEPAPQVQPESPETVSPKGSEGLPPPEPEPKPEWVSDKGLQPSTPPPKPPRLFTPSRSQEEEEEKAAVGLSNRGPETEGEDASPSALVVGPPETKEEGEKRESEESDSCSSATLLGQPGLEELVEDASPPVSGPCLSAPASCPEGPAPIPCHSKSLALQSQHIWGTPEVGEGPEAPEAQGQDPVGEGLGSLSATSQQADVWVSKEDALNPFLFQGSRDPPSLSSASPPGSRESSIHSGPEELPTPPEPDFPPPPLPPWASHHRGGPSPPCSPLSEAWPLTTSSAPPGEPALLPGPHEPSPPGGSPALLREDLAAATPASPLVLLPLETRPAEEPQPSASPHPVKPLSAAPVEGSPDRKQSRSSLSIALSSGLEKLKTVTSGSIQPVTQAPQAGQMVDTKRLKDSAVLDQSAKYYHLTHDELISLLLQRERELSQRDEHVQELESYIDRLLVRIMETSPTLLQIPPGPPK
Protein: Rifin (Q9NFB2)
Organism: Plasmodium falciparum (isolate 3D7)
Interaction partners:
Sequence:
MKLHYTKLLLFFFTLNILLTSYHAHNKNKPSITPHHTRSTTSRLLSEYDTESSIYDSDDEIDSVKEIFERQASQRLREYDERLQEKRQKRKEQRDKNIQKIIHKDKMEKNLAEKIEKGCLRCGCGLGSVAGSIGLFGAVAINIWKPAALDAAITAALNANAVKIAAAANAAGEVIGKALVIAELQKMGISTLKGQTLKSFFRTISYKNVSSITKAVYGQHYEICVYDPSRNLLSSFGDVNRHIGICNSVWKQISAVSQRGQYISHEEVIKRTVETMMSEAEVSAKAAAKTAEAANKLAIEEAQEQVMEATIYNWYTTIGYTILAILIIVLIMIIIYLILRYRRKKKMKKKAQYTKLLNE
Protein: Aldo-keto reductase family 1 member C4 (EC 1.1.1.-) (EC 1.1.1.209) (EC 1.1.1.210) (EC 1.1.1.51) (EC 1.1.1.53) (EC 1.1.1.62) (3-alpha-hydroxysteroid dehydrogenase type I) (3-alpha-HSD1) (EC 1.1.1.357) (3alpha-hydroxysteroid 3-dehydrogenase) (Chlordecone reductase) (CDR) (EC 1.1.1.225) (Dihydrodiol dehydrogenase 4) (DD-4) (DD4) (HAKRA) (P17516)
Organism: Homo sapiens (Human)
Function: Cytosolic aldo-keto reductase that catalyzes the NADH and NADPH-dependent reduction of ketosteroids to hydroxysteroids. Liver specific enzyme that acts as NAD(P)(H)-dependent 3-, 17- and 20-ketosteroid reductase on the steroid nucleus and side chain. Displays the ability to catalyze both oxidation and reduction in vitro, but most probably acts as a reductase in vivo since the oxidase activity measured in vitro is inhibited by physiological concentration of NADPH. Acts preferentially as a 3-alpha-hydroxysteroid dehydrogenase (HSD) with a subsidiary 3-beta-HSD activity. Catalyzes efficiently the transformation of the potent androgen 5-alpha-dihydrotestosterone (5alpha-DHT or 17beta-hydroxy-5alpha-androstan-3-one) into the less active form, 5-alpha-androstan-3-alpha,17-beta-diol (3-alpha-diol). Catalyzes the reduction of estrone into 17beta-estradiol but with low efficiency. Metabolizes a broad spectrum of natural and synthetic therapeutic steroid and plays an important role in metabolism of androgens, estrogens, progestereone and conjugated steroids. Catalyzes the biotransformation of the pesticide chlordecone (kepone) to its corresponding alcohol leading to increased biliary excretion of the pesticide and concomitant reduction of its neurotoxicity since bile is the major excretory route.
Subcellular location: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q04828}.
Interaction partners:
- Polyprenal reductase
- 3-oxo-5-alpha-steroid 4-dehydrogenase 1
- 3-oxo-5-alpha-steroid 4-dehydrogenase 2
- 11-beta-hydroxysteroid dehydrogenase 1
- Dehydrogenase/reductase SDR family member 9
- 7-alpha-hydroxycholest-4-en-3-one 12-alpha-hydroxylase
- Sterol 26-hydroxylase, mitochondrial
- UDP-glucuronosyltransferase 1A6
- Trans-1,2-dihydrobenzene-1,2-diol dehydrogenase
- UDP-glucuronosyltransferase 2B15
Sequence:
MDPKYQRVELNDGHFMPVLGFGTYAPPEVPRNRAVEVTKLAIEAGFRHIDSAYLYNNEEQVGLAIRSKIADGSVKREDIFYTSKLWCTFFQPQMVQPALESSLKKLQLDYVDLYLLHFPMALKPGETPLPKDENGKVIFDTVDLSATWEVMEKCKDAGLAKSIGVSNFNCRQLEMILNKPGLKYKPVCNQVECHPYLNQSKLLDFCKSKDIVLVAHSALGTQRHKLWVDPNSPVLLEDPVLCALAKKHKQTPALIALRYQLQRGVVVLAKSYNEQRIRENIQVFEFQLTSEDMKVLDGLNRNYRYVVMDFLMDHPDYPFSDEY
Protein: Group IID secretory phospholipase A2 (GIID sPLA2) (sPLA2-IID) (EC 3.1.1.4) (PLA2IID) (Phosphatidylcholine 2-acylhydrolase 2D) (Secretory-type PLA, stroma-associated homolog) (Q9UNK4)
Organism: Homo sapiens (Human)
Function: Secretory calcium-dependent phospholipase A2 that primarily targets extracellular lipids, exerting anti-inflammatory and immunosuppressive functions. Hydrolyzes the ester bond of the fatty acyl group attached at sn-2 position of phospholipids (phospholipase A2 activity) with preference for phosphatidylethanolamines and phosphatidylglycerols over phosphatidylcholines. In draining lymph nodes, selectively hydrolyzes diacyl and alkenyl forms of phosphatidylethanolamines, releasing omega-3 polyunsaturated fatty acids (PUFAs) such as eicosapentaenoate and docosahexaenoate that are precursors of the anti-inflammatory lipid mediators, resolvins (By similarity). During the resolution phase of acute inflammation drives docosahexaenoate-derived resolvin D1 synthesis, which suppresses dendritic cell activation and T-helper 1 immune response (By similarity). May act in an autocrine and paracrine manner (By similarity). Via a mechanism independent of its catalytic activity, promotes differentiation of regulatory T cells (Tregs) and participates in the maintenance of immune tolerance (By similarity). May contribute to lipid remodeling of cellular membranes and generation of lipid mediators involved in pathogen clearance. Displays bactericidal activity against Gram-positive bacteria by directly hydrolyzing phospholipids of the bacterial membrane (By similarity).
Subcellular location: Secreted {ECO:0000269|PubMed:10455175}.
Interaction partners:
- Group 3 secretory phospholipase A2
- Group XIIA secretory phospholipase A2
- Secretory phospholipase A2 receptor
- Lysosomal phospholipase A and acyltransferase
- Phospholipase A and acyltransferase 3
- Platelet-activating factor acetylhydrolase
- Cytochrome P450 2E1
- Phospholipase B1, membrane-associated
- Lysophosphatidylcholine acyltransferase 2
- Prostaglandin G/H synthase 2
Sequence:
MELALLCGLVVMAGVIPIQGGILNLNKMVKQVTGKMPILSYWPYGCHCGLGGRGQPKDATDWCCQTHDCCYDHLKTQGCSIYKDYYRYNFSQGNIHCSDKGSWCEQQLCACDKEVAFCLKRNLDTYQKRLRFYWRPHCRGQTPGC
Protein: Transcription regulatory protein SNF5, putative (BSH) (F4J581)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
Sequence:
MKGLVSTGWKGPVKFRIYRPTAENLVPIRLDIQFEGQRYKDAFTWNPSDPDNEVVIFAKRTVKDLKLPYAFVTQIAQSIQSQLSDFRAYEGQDMYTGEKIIPIKLDLRVNHTLIKDQFLWDLNNFESDPEEFARTLCKDLGVEDPEVGPAVAFAIREQLYEIAIQSVASARESRLSKKGRRGSDHGSASKASGLSMDLMKLFSFKSSVVRKRKDLDVYEPVVDLLTSEEVDALEAREERHAR
Protein: phosphorylase kinase (EC 2.7.11.19) (A0JME5)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Phosphorylase b kinase regulatory subunit
- Phosphorylase b kinase regulatory subunit
- Phosphorylase b kinase regulatory subunit
- Calmodulin
- Calmodulin-like protein 4
- phosphorylase kinase
- Phosphorylase kinase, gamma 1b
- Calmodulin-like 4b.
- Phosphorylase b kinase regulatory subunit
- Doublecortin-like kinase 2b.
Sequence:
MTKEDEIPDWAGAQDFYQKYDPKEILGRGVSSVVRRCIHKRTTQEYAVKVIDITPSDKMNTEEIEEIRNATIKEIDILKKVCGQENIIQLKDCFETKAFFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRSLLEVVQFLHSQNIVHRDLKPENILLDDNMNIKLTDFGFAVQIAPGQKLNEVCGTPGYLAPEIIECSMDPHHQGYGAAVDLWSAGVIMFTLLAGSPPFWHRKQMLMLRMILAGNYQFTSPEWDDRSDTVKDLISKMLVVNPEKRFTATDALNHPFFQQYVVAEVRHFSPYRKFKVICMTVLATMRIYCNYRRAKPVTKEVIKSDPYAVKPIRKLIDACAFKIYGHWVKKGQTQNRAALFENSPKAILLSLAAESVDSSLRMM
Protein: DNA/RNA-binding protein Alba-like domain-containing protein (Q583I9)
Organism: Trypanosoma brucei brucei (strain 927/4 GUTat10.1)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- DNA/RNA-binding protein Alba-like domain-containing protein
- DNA/RNA-binding protein Alba-like domain-containing protein
Sequence:
MPSYPPRDEYRRVRKNEGAKEKGQGAENEIRVTARPGSRGYITYALALLRGEEGKPKYDSVKISAMGAAIRSAVGVAEVLKRRVAGLHQTTEISSEVIHDEYEGIGEKKDKMEVERKVSTILITLSLKPLDVNHIGYQAPLPESEVKEEEERDPVERRRGGRGGRGAGRGGSRGGRGRGGNDRRGGGNEE
Protein: Phospholipid scramblase 3 (PL scramblase 3) (Ca(2+)-dependent phospholipid scramblase 3) (Q9NRY6)
Organism: Homo sapiens (Human)
Function: Catalyzes calcium-induced ATP-independent rapid bidirectional and non-specific movement of the phospholipids (lipid scrambling or lipid flip-flop) between the inner and outer membrane of the mitochondria. Plays an important role in mitochondrial respiratory function, morphology, and apoptotic response. Mediates the translocation of cardiolipin from the mitochondrial inner membrane to outer membrane enhancing t-Bid induced cytochrome c release and apoptosis. Enhances TNFSF10-induced apoptosis by regulating the distribution of cardiolipin in the mitochondrial membrane resulting in increased release of apoptogenic factors and consequent amplification of the activity of caspases. Regulates cardiolipin de novo biosynthesis and its resynthesis.
Subcellular location: Mitochondrion membrane {ECO:0000269|PubMed:14573790, ECO:0000269|PubMed:17226776, ECO:0000269|PubMed:18491232}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6QBQ4}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q6QBQ4}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q6QBQ4}. Nucleus {ECO:0000250|UniProtKB:Q9JIZ9}. Note=Palmitoylation regulates its localization to the cell membrane or the nucleus; trafficking to the cell membrane is dependent upon palmitoylation whereas in the absence of palmitoylation, localizes to the nucleus. {ECO:0000250|UniProtKB:Q9JIZ9}.
Interaction partners:
Sequence:
MAGYLPPKGYAPSPPPPYPVTPGYPEPALHPGPGQAPVPAQVPAPAPGFALFPSPGPVALGSAAPFLPLPGVPSGLEFLVQIDQILIHQKAERVETFLGWETCNRYELRSGAGQPLGQAAEESNCCARLCCGARRPLRVRLADPGDREVLRLLRPLHCGCSCCPCGLQEMEVQAPPGTTIGHVLQTWHPFLPKFSIQDADRQTVLRVVGPCWTCGCGTDTNFEVKTRDESRSVGRISKQWGGLVREALTDADDFGLQFPLDLDVRVKAVLLGATFLIDYMFFEKRGGAGPSAVTS
Protein: Calnexin (IP90) (Major histocompatibility complex class I antigen-binding protein p88) (p90) (P27824)
Organism: Homo sapiens (Human)
Function: Calcium-binding protein that interacts with newly synthesized monoglucosylated glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins. Associated with partial T-cell antigen receptor complexes that escape the ER of immature thymocytes, it may function as a signaling complex regulating thymocyte maturation. Additionally it may play a role in receptor-mediated endocytosis at the synapse.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:22314232}; Single-pass type I membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:P24643}; Single-pass type I membrane protein {ECO:0000255}. Melanosome membrane {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}; Single-pass type I membrane protein {ECO:0000255}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:12643545, PubMed:17081065). The palmitoylated form preferentially localizes to the perinuclear rough ER (PubMed:22314232). Localizes to endoplasmic reticulum mitochondria-associated membrane (MAMs) that connect the endoplasmic reticulum and the mitochondria (By similarity). {ECO:0000250|UniProtKB:P24643, ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:22314232}.
Interaction partners:
- Protein disulfide-isomerase A3
- Calreticulin
- Endoplasmic reticulum chaperone BiP
- Tapasin
- Endoplasmin
- ER degradation-enhancing alpha-mannosidase-like protein 1
- Transitional endoplasmic reticulum ATPase
- Protein disulfide-isomerase
- Protein OS-9
- Neutral alpha-glucosidase AB
Sequence:
MEGKWLLCMLLVLGTAIVEAHDGHDDDVIDIEDDLDDVIEEVEDSKPDTTAPPSSPKVTYKAPVPTGEVYFADSFDRGTLSGWILSKAKKDDTDDEIAKYDGKWEVEEMKESKLPGDKGLVLMSRAKHHAISAKLNKPFLFDTKPLIVQYEVNFQNGIECGGAYVKLLSKTPELNLDQFHDKTPYTIMFGPDKCGEDYKLHFIFRHKNPKTGIYEEKHAKRPDADLKTYFTDKKTHLYTLILNPDNSFEILVDQSVVNSGNLLNDMTPPVNPSREIEDPEDRKPEDWDERPKIPDPEAVKPDDWDEDAPAKIPDEEATKPEGWLDDEPEYVPDPDAEKPEDWDEDMDGEWEAPQIANPRCESAPGCGVWQRPVIDNPNYKGKWKPPMIDNPSYQGIWKPRKIPNPDFFEDLEPFRMTPFSAIGLELWSMTSDIFFDNFIICADRRIVDDWANDGWGLKKAADGAAEPGVVGQMIEAAEERPWLWVVYILTVALPVFLVILFCCSGKKQTSGMEYKKTDAPQPDVKEEEEEKEEEKDKGDEEEEGEEKLEEKQKSDAEEDGGTVSQEEEDRKPKAEEDEILNRSPRNRKPRRE
Protein: Arginine vasopressin receptor 1Ab (Arginine vasotocin receptor 1a1) (F1Q5N3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Subcellular location: Cell membrane {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU046427}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651, ECO:0000256|RuleBase:RU046427}.
Interaction partners:
- Arginine vasopressin
- Guanine nucleotide-binding protein subunit alpha
- Oxytocin
- Guanine nucleotide-binding protein subunit alpha
- G-protein alpha 13a, alpha 13a)
- Guanine nucleotide-binding protein
- G-protein alpha 12 alpha 12) alpha 12a)
- Arginine vasopressin receptor 1Aa
Sequence:
MGNTSNQITANNTTDPFGRNEDVAKMEITVLSVTFLVAVVGNLCVLLAMHNTKKKSSRMHLFIKHLSLADLVVAFFQVLPQLCWEITYRFYGPDFLCRIVKHLQVLGMFASTYMMVMMTLDRYIAICHPLKTLQQPTRRAYIMICSTWLCSLLLSTPQYFIFSLSEIQNGSDVYDCWGHFIEPWGIRAYITWITVGIFLIPVVILMICYGFICHSIWKNFKCKTKRGAAHNPKSGMIGKASVSSVTIISRAKLRTVKMTFVIVLAYIVCWAPFFTVQMWSVWDENFSWDDSENAAVTLSALLASLNSCCNPWIYMLFSGHLLHDFLGCFPCWNKPQNTLHKEDSDSSIRRNTLLSKLTSVRAKDGFDSWKDPCNSRKSSQSIGLDYSRKSSQCLHFDCSRKSSQSVPMES
Protein: L-amino-acid oxidase (BatroxLAAO) (LAO) (EC 1.4.3.2) (P0CC17)
Organism: Bothrops atrox (Barba amarilla) (Fer-de-lance)
Function: Catalyzes an oxidative deamination of predominantly hydrophobic and aromatic L-amino acids, thus producing hydrogen peroxide that may contribute to the diverse toxic effects of this enzyme. Shows high catalytic activity against L-Met, L-Leu, L-Phe, L-Trp, L-Tyr, L-Ile. Shows no or weak activity on L-Cys, L-Val, L-Gln, L-Thr, L-Ser, L-Lys, L-Arg, L-Asn, L-Glu, L-Gly, L-Pro, L-Asp and L-His. Induces platelet aggregation in platelet-rich plasma, probably due to hydrogen peroxide production, since catalase inhibits aggregation effect. Induces moderate mouse paw edema. Induces apoptosis and shows cytotoxicity against several cancer cell lines, which is inhibited by catalase. Shows hemolytic activity and antibacterial activities against both Gram-positive and Gram-negative bacteria. Has parasiticidal activities against both trypanosomes and leishmania, as a result of enzyme-catalyzed hydrogen peroxide production. Unlike other snake venom L-amino acid oxidases, does not induce hemorrhage (with 50 ug of enzyme).
Subcellular location: Secreted {ECO:0000269|PubMed:18804547}.
Interaction partners:
Sequence:
MNVFFTFSLLFLAALGSCADDRNPLEECFRETDYEEFLEIAKNGLSTTSNPKRVVIVGAGMSGLSAAYVLANAGHQVTVLEASERAGGRVKTYRNEKEGWYANLGPMRLPEKHRIVREYIRKFDLQLNEFSQENENAWYFIKNIRKRVGEVNKDPGVLEYPVKPSEVGKSAGQLYEESLQKAVEELRRTNCSYMLNKYDTYSTKEYLLKEGNLSPGAVDMIGDLLNEDSGYYVSFIESLKHDDIFAYEKRFDEIVGGMDKLPTSMYQAIQEKVHLNARVIKIQQDVKEVTVTYQTSEKETLSVTADYVIVCTTSRAARRIKFEPPLPPKKAHALRSVHYRSGTKIFLTCTKKFWEDDGIHGGKSTTDLPSRFIYYPNHNFPNGVGVIIAYGIGDDANYFQALDFEDCGDIVINDLSLIHQLPKEEIQAICRPSMIQRWSLDKYAMGGITTFTPYQFQHFSEALTAPVDRIYFAGEYTAQAHGWIDSTIKSGLRAARDVNRASEIKK
Protein: Chd3 protein (Q8K0T3)
Organism: Mus musculus (Mouse)
Interaction partners:
Sequence:
MFNIADGGFTELHTLWQNEERAAISSGKLNEIWHRRHDYWLLAGIVLHGYARWQDIQNDAQFAIINEPFKTEANKGNFLEMKNKFLARRFKLLEQALVIEEQLRRAAYLNLSQEPAHPAMALHARFAEAECLAESHQHLSKESLAGNKPANAVLHKVLNQLEELLSDMKADVTRLPATLSRIPPIAARLQMSERSILSRLASKGTEPHPTPAFPPGPYATPPGYGAAFSAAPVGALAAAGANYSQMPAGSFITATTNGPPVLVKKEKEMVGALVSDGLGLDRKEPRAGEVICIDD
Protein: Protein ASG7 (A-specific gene 7 protein) (P46993)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Required for receptor inhibition of inappropriately expressed a-factor receptor (STE3) in MAT a cells. Inhibits signaling by relocalizing the G protein beta-gamma (STE4-STE18) subunit to intracellular membranes. May also be a mechanism for the down-regulation of the mating pheromone response after the zygotic fusion event, promoting the transition of the new diploid cell to vegetative growth.
Subcellular location: Endomembrane system {ECO:0000269|PubMed:11073983}; Multi-pass membrane protein {ECO:0000269|PubMed:11073983}.
Interaction partners:
- A-agglutinin-binding subunit
- Alpha-factor-transporting ATPase
- Mating hormone A-factor 2
- Pheromone alpha factor receptor
- Mating hormone A-factor 1
- Barrierpepsin
- Silenced mating-type protein A1
- Pheromone a factor receptor
Sequence:
MTTLASSIEHKTKHLAAPFENDENPWMKKYCCQCKSCKMSVPVQPWLPRFFVFGILCPVFWLVNLLAWWFLQYWQPHELEFHDLQEDEYPGFYEYEAITKRTVIPIKEEVLQEIRVMQNFSDSNSEEYYESKDGMPSSFLNVNTEQVEDENDTLKKYRYAFLKKVAHDVLESHDLLRKTFRDWNLRSLLGLLIDSILIIFVVLLCKKSR
Protein: DUF19 domain-containing protein (Q20770)
Organism: Caenorhabditis elegans
Interaction partners:
- Putative serine protease F56F10.1
- Galectin
- EGF-like domain-containing protein
- Uncharacterized protein ZK1320.3
- Serine protease K12H4.7
- Putative serine protease K12H4.7
- C-type lectin domain-containing protein
- ShKT domain-containing protein
- Putative phospholipase B-like 2
- EGF-like domain-containing protein
Sequence:
MNQIVSALLIFAVGYATGNLCTDDTGYWISSLAEGVSDFAYGGTRLNTKYYCFEGCLNTGTALQNCKVDMSGNNGTRIERSREIKEVIALHQLARQRDEDPNAKSCVDPVLRQDVKNALQKTTRSNCKNIVNTLVLNLNRPGWAITCIQFNEFAIDDYTPDMNFCSYDSVSDTDIFTIRLAKLDMS
Protein: non-specific serine/threonine protein kinase (EC 2.7.11.1) (H0YJJ9)
Organism: Homo sapiens (Human)
Interaction partners:
Sequence:
MPRVKAAQAGRQSSAKRHLAEQFAVGEIITDMAKKEWKVGLPIGQGGFGCIYLADMNSSESVGSDAPCVVKVEPSDNGPLFTELKFYQRAAKPEQIQKWIRTRKLKYLGVPKYWGSGLHDKNGKSYRFMIMDRFGSDLQKIYEANAKRFSRKTVLQLSLRILDILEYIHEHEYVHGDIKASNLLLNYKNPDQVYLVDYGLAYRYCPEGVHKEYKEDPKRCHDGTIEFTSIDAHNGVAPSRRGDLEILGYCMIQWLTGHLPWEDNLKDPKYVRDSKIRYRENIASLMDKCFPEKNKPGEIAKYMETVKLLDYTEKPLYENLRDILLQGLKAIGSKDDGKLDLSVVENGGLKAKTITKVNFVIKLFFGLLVFIIAINTKRKYSSSSMKNNNRLHGN
Protein: Calcineurin B-like protein (Q8L7F6)
Organism: Pisum sativum (Garden pea) (Lathyrus oleraceus)
Subcellular location: Membrane {ECO:0000256|RuleBase:RU369080}.
Interaction partners:
Sequence:
MLQCLEGFKSLLASVLRCCDIDINQPRGLEDPELLARETVFSVSEIEALYELFKKISSAVIDDGLINKEEFQLALFKTNKKESLFADRVFDLFDTKHNGILGFEEFARALSVFHPNAPIDDKIEFSFQLYDLKQQGFIERQEVKQMVVATLAESGMNLSDDVIESIIDKTFEEADTKHDGKIDKEEWRNLVLRHPSLLKNMTLQYLKDITTTFPSFVFHSQVDDT