wanglab/gogpt-training-data huggingface dataset:
Protein: Serine/threonine-protein kinase PAK mbt (EC 2.7.11.1) (Protein mushroom bodies tiny) (p21-activated kinase-related protein) (Q9VXE5)
Organism: Drosophila melanogaster (Fruit fly)
Function: Involved in neurogenesis of the adult central nervous system, and together with Cdc42, regulates photoreceptor cell morphogenesis. Phosphorylates exogenous substrates when activated by Cdc42.
Subcellular location: Cell junction, adherens junction {ECO:0000269|PubMed:12490550}. Cell membrane {ECO:0000269|PubMed:12490550}; Peripheral membrane protein {ECO:0000269|PubMed:12490550}. Note=Apical membrane sites of adherens junctions of developing photoreceptor cells.
Interaction partners:
- Cdc42 homolog
- Integrin beta-PS
- AT17867p
- Ras-like GTP-binding protein Rho1
- Ras-related protein Rac1
- Ras-related protein Rac2
- Ras-like GTP-binding protein RhoL
- Tyrosine-protein kinase hopscotch
- RhoU, isoform B
- FI13065p
Sequence:
MFSKKKKKPLISMPSNFEHRVHTGFDKRENKYVGLPLQWASIVGNNQILKSSNRPLPLVDPSEITPTEILDLKTIVRPHHNNNKADTTSLNSSSTMMMGSMAPMNPMAPGAHPMMSHGPGMMMPPETGGIVLPKTSHVARSNSLRSSSPPRVRRVANVPPSVPEEEGPPAAGTPGVGGASSGGFKPPGAHPSLLYNSQHAHANGATGPLAVRTDQTNLQQYRSNLAPPSGGSMPQQQQTSPVGSVASGTRSNHSHTNNGNSGGSYPPMYPTSHQQQQQQQQQAKQGGDQNQNPLHPHAHPHPHHHQHLAKSASRASSSSGGASSAAQQASGASGGAAGQPKQDQRLTHEQFRAALQMVVSAGDPRENLDHFNKIGEGSTGTVCIATDKSTGRQVAVKKMDLRKQQRRELLFNEVVIMRDYHHPNIVETYSSFLVNDELWVVMEYLEGGALTDIVTHSRMDEEQIATVCKQCLKALAYLHSQGVIHRDIKSDSILLAADGRVKLSDFGFCAQVSQELPKRKSLVGTPYWMSPEVISRLPYGPEVDIWSLGIMVIEMVDGEPPFFNEPPLQAMRRIRDMQPPNLKNAHKVSPRLQSFLDRMLVRDPAQRATAAELLAHPFLRQAGPPSLLVPLMRNARHHP
Protein: Gamma-aminobutyric acid receptor subunit delta (GABA(A) receptor subunit delta) (GABAAR subunit delta) (P18506)
Organism: Rattus norvegicus (Rat)
Function: GABA, the major inhibitory neurotransmitter in the vertebrate brain, mediates neuronal inhibition by binding to the GABA/benzodiazepine receptor and opening an integral chloride channel.
Subcellular location: Cell membrane {ECO:0000269|PubMed:9464994}; Multi-pass membrane protein {ECO:0000250|UniProtKB:O14764}. Note=Delta subunits are found only on the extrasynaptic somatic and dendritic membranes. {ECO:0000269|PubMed:9464994}.
Interaction partners:
- Gamma-aminobutyric acid receptor subunit alpha-4
- Trafficking kinesin-binding protein 2
- Huntingtin-associated protein 1
- Vesicle-fusing ATPase
- Inactive phospholipase C-like protein 1
- Gamma-aminobutyric acid receptor subunit beta-3
- Gamma-aminobutyric acid type B receptor subunit 2
- Gamma-aminobutyric acid receptor subunit beta-2
- Gamma-aminobutyric acid receptor subunit beta-1
- Gamma-aminobutyric acid receptor subunit alpha-6
Sequence:
MDVLGWLLLPLLLLCTQPHHGARAMNDIGDYVGSNLEISWLPNLDGLMEGYARNFRPGIGGPPVNVALALEVASIDHISEANMEYTMTVFLHQSWRDSRLSYNHTNETLGLDSRFVDKLWLPDTFIVNAKSAWFHDVTVENKLIRLQPDGVILYSIRITSTVACDMDLAKYPMDEQECMLDLESYGYSSEDIVYYWSENQEQIHGLDRLQLAQFTITSYRFTTELMNFKSAGQFPRLSLHFQLRRNRGVYIIQSYMPSVLLVAMSWVSFWISQAAVPARVSLGITTVLTMTTLMVSARSSLPRASAIKALDVYFWICYVFVFAALVEYAFAHFNADYRKKRKAKVKVTKPRAEMDVRNAIVLFSLSAAGVSQELAISRRQGRVPGNLMGSYRSVEVEAKKEGGSRPGGPGGIRSRLKPIDADTIDIYARAVFPAAFAAVNIIYWAAYTM
Protein: Succinate dehydrogenase [ubiquinone] flavoprotein subunit, mitochondrial (EC 1.3.5.1) (Flavoprotein subunit of complex II) (FP) (Q6ZDY8)
Organism: Oryza sativa subsp. japonica (Rice)
Function: Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q).
Subcellular location: Mitochondrion inner membrane {ECO:0000250|UniProtKB:O82663}; Peripheral membrane protein {ECO:0000250|UniProtKB:O82663}; Matrix side {ECO:0000250|UniProtKB:O82663}.
Interaction partners:
- Succinate dehydrogenase iron-sulfur subunit 2, mitochondrial
- Succinate dehydrogenase iron-sulfur subunit 1, mitochondrial
- fumarate hydratase
- Succinate--CoA ligase subunit alpha, mitochondrial
- Succinate dehydrogenase subunit 3-1
- Succinate dehydrogenase subunit 3-2
- Succinate--CoA ligase subunit beta, mitochondrial
- NADH dehydrogenase flavoprotein 1, mitochondrial
- NADH-ubiquinone oxidoreductase 75 kDa subunit, mitochondrial, putative, expressed
- 2-oxoglutarate dehydrogenase, mitochondrial
Sequence:
MWRGCVSRGLRSLSKGKGSSSSAPVSAAARLFSTASSSYTVVDHSYDAVVVGAGGAGLRAAIGLSEHGFNTACITKLFPTRSHTVAAQGGINAALGNMTEDDWRWHMYDTVKGSDWLGDQDSIQYMCREAPKAVIELENYGLPFSRTEDGKIYQRAFGGQSLDFGKGGQAYRCACAADRTGHAMLHTLYGQAMKHNTQFFVEYFALDLIMDSEGTCQGVIALNMEDGTLHRFRATNTILATGGYGRAYFSATSAHTCTGDGNAMVARAGLPLQDLEFVQFHPTGIYGAGCLITEGSRGEGGILRNSEGERFMERYAPTAKDLASRDVVSRSMTMEIREGRGVGPLKDHIYLHLNHLPPEVLKERLPGISETAAIFAGVDVTKEPIPVLPTVHYNMGGIPTNYHGEVVTMKGDNPDSVVPGLMAAGEAACASVHGANRLGANSLLDIVVFGRACANRVAETAKPGEKQKPLQKSAGEKTIAWLDKLRNANGSLPTSKIRLNMQRVMQNNAAVFRTQETLEEGCKLITKAWESYHDVKISDRSLIWNSDLIETIELENLLINACITMHSAEARKESRGAHAREDFTKRDDEQWMKHSLGYWENEKVRLAYRPVHMNTLDSEVESFPPKARVY
Protein: Cannabinoid receptor 2 (CB-2) (CB2) (mCB2) (P47936)
Organism: Mus musculus (Mouse)
Function: Heterotrimeric G protein-coupled receptor for endocannabinoid 2-arachidonoylglycerol mediating inhibition of adenylate cyclase. May function in inflammatory response, nociceptive transmission and bone homeostasis.
Subcellular location: Cell membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell projection, dendrite {ECO:0000250}. Perikaryon {ECO:0000250}. Note=Localizes to apical dendrite of pyramidal neurons. {ECO:0000250}.
Interaction partners:
- G-protein coupled receptor 55
- Cannabinoid receptor 1
- N-arachidonyl glycine receptor
- Fatty-acid amide hydrolase 1
- Monoglyceride lipase
- Transient receptor potential cation channel subfamily V member 1
- Corticosteroid-binding globulin
- N-acyl-phosphatidylethanolamine-hydrolyzing phospholipase D
- 5-hydroxytryptamine receptor 1A
Sequence:
MEGCRETEVTNGSNGGLEFNPMKEYMILSSGQQIAVAVLCTLMGLLSALENMAVLYIILSSRRLRRKPSYLFISSLAGADFLASVIFACNFVIFHVFHGVDSNAIFLLKIGSVTMTFTASVGSLLLTAVDRYLCLCYPPTYKALVTRGRALVALCVMWVLSALISYLPLMGWTCCPSPCSELFPLIPNDYLLGWLLFIAILFSGIIYTYGYVLWKAHRHVATLAEHQDRQVPGIARMRLDVRLAKTLGLVLAVLLICWFPALALMGHSLVTTLSDQVKEAFAFCSMLCLVNSMVNPIIYALRSGEIRSAAQHCLIGWKKYLQGLGPEGKEEGPRSSVTETEADVKTT
Protein: Trehalase (EC 3.2.1.28) (Alpha-trehalose glucohydrolase) (A2Q9W0)
Organism: Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513)
Interaction partners:
Sequence:
MSSSSAQHRRNTSLDPFSDPDVYYGDEDNIARMRDRKRAFSSTLKSFNRDDIQEFLGGGFPARRASHDETPAVPRKFLIDVDTTLHSLLEREDTDRNMQITIEDVGPKVFSVGTAASSGYNRFDLRGTYMLSNLLQELTIAQDYGRKHIVLDEARLSENPVARLSRLIKNSFWNALTRRIDGHNIAEAGRDPKDWTDDPRPRVYVPPGAPEQLEYYKGIAEAHPELRLDVQLLDSNITPEYTRKLNDKPGLLALAMEKKVDEATGKTEYSGVPFVVPGGRFNELYNWDSYMMSLGLLVSNRVDLAKGMVINFCFCIKHYGKILNANRSYYLMRSQPPFLTDMALRVYERIKNEPDAMEFLRNATLAAIKEYYSVWTAEPRFDPVSGLSRYRPEGEGVPPETEPTHFLHILTPYAEKHGMTFEEFVEAYNERKILEPELDEYFLHDRAVRESGHDTSYRLERVCANLATVDLNSLLYKYEVDIARIIRTYFKDKLEIPQEFRTASTQDIQFESSSVWDRRARRRKIRMDTYLWDEEKGMYFDYDTAKQERTTYESATTYWAMWAGLATPHQASQLVQSLKRFEAYGGLVSGTEESRGAVGLDRPNRQWDYPYGWAPQQMLAWTGLMRYGYQEEAERLAYKWLYMITKAFVDFNGVVVEKYDVTRPIDPHRVDAEYGNQGVDFKGAPREGFGWVNASYVYGLEILNAHQRRALGAITPYETYNKAVAVQDF
Protein: Major facilitator superfamily (MFS) profile domain-containing protein (H2FLL6)
Organism: Caenorhabditis elegans
Subcellular location: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
Interaction partners:
Sequence:
MSSRKVMVFVVTFVSYGLYHASRKALSGVKSSIKADWLSNSSGHAPLFTNEADAKHFLGSLDAIFMAAYAAALFFWGWLGDRLNPKLVVAAGMVGSAVTLTLFGAIPKWFNFYHAPYYIMTYVAFGLVQACGWPSEIAIMANWFGKGNRGFVMGVWAACQPVGNIFGSIFTAMVLPLGYQYTFVFNSVLIALGAIVVVMAIDSSPNEEHEDGVEANSSEPHHNFHGEPISLFKAVLLPGVLAYCICNACLKLVNYAFFFWLPLYLTDAYHWEESQADQLSIWYDFGGIIGSVLGGYITDKMGKRSPLIVAMLVCSIGSLYFYAHVGPHMFWNAVVMTTVGVTVSGPYNLIVGSISIDLGSQPALAGNTQAMSTVSGLLDGTGSAGSAVGQLLIPIIQDDLGWKAVFYVFMLLNGFAILAILKRCIIDLKSLRKLRSGEESPLLNDEAGDHED
Protein: Sensor histidine kinase ZraS (EC 2.7.13.3) (P14377)
Organism: Escherichia coli (strain K12)
Function: Member of the two-component regulatory system ZraS/ZraR. May function as a membrane-associated protein kinase that phosphorylates ZraR in response to high concentrations of zinc or lead in the medium.
Subcellular location: Cell inner membrane {ECO:0000269|PubMed:11243806, ECO:0000269|PubMed:15919996}; Multi-pass membrane protein {ECO:0000255}.
Interaction partners:
- Transcriptional regulatory protein ZraR
- Signaling pathway modulator ZraP
- Galactofuranose-binding protein YtfQ
- Chemotaxis protein methyltransferase
- Transcriptional regulatory protein CreB
- Sensor protein BasS
- Aerobic respiration control sensor protein ArcB
- Transcriptional regulatory protein BaeR
- Sensor histidine kinase YpdA
- Transcriptional regulatory protein CusR
Sequence:
MRFMQRSKDSLAKWLSAILPVVIVGLVGLFAVTVIRDYGRASEADRQALLEKGNVLIRALESGSRVGMGMRMHHVQQQALLEEMAGQPGVLWFAVTDAQGIIILHSDPDKVGRALYSPDEMQKLKPEENSRWRLLGKTETTPALEVYRLFQPMSAPWRHGMHNMPRCNGKAVPQVDAQQAIFIAVDASDLVATQSGEKRNTLIILFALATVLLASVLSFFWYRRYLRSRQLLQDEMKRKEKLVALGHLAAGVAHEIRNPLSSIKGLAKYFAERAPAGGEAHQLAQVMAKEADRLNRVVSELLELVKPTHLALQAVDLNTLINHSLQLVSQDANSREIQLRFTANDTLPEIQADPDRLTQVLLNLYLNAIQAIGQHGVISVTASESGAGVKISVTDSGKGIAADQLDAIFTPYFTTKAEGTGLGLAVVHNIVEQHGGTIQVASQEGKGSTFTLWLPVNITRKDPQG
Protein: ELMO family protein LMO1 (Q07799)
Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Function: Forms a transiant heterodimeric complex with DCK1, that acts as a guanine nucleotide exchange factor (GEF) for the small GTPase RHO5. DCK1, LMO1 and RHO5 relocate to mitochondria upon oxidative stress and trigger cell death. The DCK1/LMO1/RHO5 signaling module mediates mitochondrial turnover under nitrogen starvation conditions via mitophagy. The DCK1/LMO1/RHO5 signaling module also plays a role in cell wall integrity signaling.
Subcellular location: Cytoplasm {ECO:0000269|PubMed:14562095}. Mitochondrion {ECO:0000269|PubMed:25598154}. Note=Quickly relocates to mitochondria under oxidative stress. {ECO:0000269|PubMed:25598154}.
Interaction partners:
- DOCK-like protein 1
- GTP-binding protein RHO5
Sequence:
MKHNRQMPDESLENIKVLLNPKLGKPVKSLTSAQSKACYHTLISNKNLNKTSDEYEKLLANYILLCDEKYLCKTVIPDSRFWAILCDNCQKLRSETLVANLIRIFNVALKCQDSNKNEVIVSICHISRENSQLIGILLQLLSQRPIHIPLFTDTILCITLFLKCSLTLCETSLSHAVEFVPRILILLFQYNFPASMSELLYIEDLQPLILEEFVPLKQRLINFLSSVSIDDYSCSLKADLLTAIKDNSVFQKGLEMEMGDLPSINLLNAYDTFTFLNSPNGSFKRLYTEQLLFGENDFPLYEAIFKLSDQFRRLFNLSGKKENQYSDSERDLKLQIATAVLNRQTCFYKTLELFLRFWIESLAKSQSDLVSLLNLAIITLKYVCLSSSDLEAAIQTKSLLKTQVVALDSMRYKFARTLQLDSIKKEQYRTWSSSIASFDTMLSGQVRDYVRHQRLLQLQKGTWVYAENPLNPEAGTPKVYFLIVSDNHANLLAREFETQTNDLPYLFDNKILTSPGSEALANGRTKVVVLKHITSFKSIELTTPSRRTSSNVYIKLDEANVYTGVELKDRNDRTVLKFYLDTEEGRYIWLDGLKLISPFQHEDISEDTKEQIDTLFDLRKNVQMINLNVRQDIIVPPPEPSDEDEDEEFYNLETLKKVTQNFYFD
Protein: Fus RNA binding protein (Q5PQK2)
Organism: Rattus norvegicus (Rat)
Subcellular location: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
Interaction partners:
- RCG31562, isoform CRA_c.
- Ribonuclease 3
- Transportin-1
- Superoxide dismutase
- Ubiquilin 2
- Serine/arginine-rich splicing factor 2
- Heterogeneous nuclear ribonucleoprotein A1
- Heterogeneous nuclear ribonucleoproteins A2/B1
- Y-box-binding protein 1
- Heterogeneous nuclear ribonucleoprotein D0
Sequence:
MASNDYTQQATQSYGAYPTQPGQGYSQQSNQPYGQQSYSGYGQSADTSGYGQSSYGSSYGQTQNTGYGTQSAPQGYGSTGGYGSSQSSQSSYGQQSSYPGYGQQPAPSSTSGSYGGSSQSSSYGQPQSGGYGQQSGYGGQQQSYGQQQSSYNPPQGYGQQNQYNSSSGGGGGGGGGNYGQDQSSMSGGGGGGGYGNQDQSGGGGGGYGGGQQDRGGRGRGGGGGYNRSSGGYEPRGRGGGRGGRGGMGGSDRGGFNKFGGPRDQGSRHDSEQDNSDNNTIFVQGLGENVTIESVADYFKQIGIIKTNKKTGQPMINLYTDRETGKLKGEATVSFDDPPSAKAAIDWFDGKEFSGNPIKVSFATRRADFNRGGGNGRGGRGRGGPMGRGGYGGGGSGGGGRGGFPSGGGGGGGQQRAGDWKCPNPTCENMNFSWRSECNQCKAPKPDGPGGGPGGSHMGGNYGDDRRGRGGYDRGGYRGRGGDRGGFRGGRGGGDRGGFGPGKMDSRGEHRQDRRERPY
Protein: X11L, isoform F (X2JE74)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
- Peripheral plasma membrane protein CASK
- Protein ROP
- Amyloid-beta-like protein
- Fasciclin-2
- Syntaxin-1A
- FI17352p1
Sequence:
MNSNSCSDSSNESMVNPPHIQMNFGQQAQQQQSHQHQQQQQQQERYVWEMRTRSPNVTPASTVLNSPDLNGELSYVPLQGLSPSGGGVQGSGSYGSNAGRDSGSYYYQRPQLHQIRLGRSPGSQFETRDVLPQGLASPGSPTDVGKADGQCLRDGEIVVFDDIDTNWMNKASSGQRPGSNEDVLKVTKMIGQLPIAEYEGSPRRFGSQPNTNTITMGGPRKRPPGFPQRVSPTTSVANNATAAAKASVGNLIDLVDHEEERSGTLREKTPTFDYLYEFSETRKVLEEFFKANPEDEKRYTDYTTESGDDVASSQPQEYPATPMEQAYIGQRLARIPKDELYMVHRSPTKKPPSDQNPSTAYQEHNDIELYIDSNSRSSGDLADTELEANLRRHSRNFTLSPETTDYDSNCGDLDSLSNDINCPTDFGKLYTSMPVLEDGLSSGHASDTENNVSVVCDKQQSSQSQPVHEHNGNGERLENDYNVMSASLATLTTDASQSALISDFASLPMPPAPPPSSPPQIEIADASESMTMVPDADNPLDSHYGAVYAAALGGTHTEKSAGSGLGVTPVTAGGSLPSQAASEIQEAMKEIRSALQRAKTQPEKLKFCDEVLPTDPDSPVWVPRKGTTISTAQGAAADEEPDTDLETDRLLGQQRHDEQDFFADQSLADNNANEGTDIASNGHLNGTSDNNNPNPMNNSKPQTYSTATIRQGIGTSLTPNSPDICQIVGTTDISISSPEKLQFTKSPTGSIKSLKDSANSDKKAKSRNKEGLLEPKVLIEGVLFRARYLGSTQLVCEGQPTKSTRMMQAEEAVSRIKALAPEGESQPSTEVDLFISTEKIMVLNTDLKEIMMDHALRTISYIADIGDLVVLMARRRFVPNSVVDPSITSPLGDVPTPGIGEEESPPKEPLSKHNRTPKMICHVFESDEAQFIAQSIGQAFQVAYMEFLKANGIENESLAKEMDYQEVLNSQEIFGDELEIFAKKELQKEVVVPKAKGEILGVVIVESGWGSMLPTVVIANLMSSGAAARCGQLNIGDQLIAINGMSLVGLPLSTCQSYIRNAKNQTAVKFTVVPCPPVVEVKILRPKALFQLGFSVQNGVICSLLRGGIAERGGVRVGHRIIEINNQSVVAVPHDTIVKLLSSSVGEILMKTMPTSMFRLLTGQETPIYI
Protein: Transcription factor MafG (V-maf musculoaponeurotic fibrosarcoma oncogene homolog G) (O54790)
Organism: Mus musculus (Mouse)
Function: Since they lack a putative transactivation domain, the small Mafs behave as transcriptional repressors when they dimerize among themselves. However, they seem to serve as transcriptional activators by dimerizing with other (usually larger) basic-zipper proteins, such as NFE2, NFE2L1 and NFE2L2, and recruiting them to specific DNA-binding sites. Small Maf proteins heterodimerize with Fos and may act as competitive repressors of the NFE2L2 transcription factor. Transcription factor, component of erythroid-specific transcription factor NFE2L2. Activates globin gene expression when associated with NFE2L2 (By similarity). May be involved in signal transduction of extracellular H(+) (By similarity).
Subcellular location: Nucleus {ECO:0000250|UniProtKB:O15525, ECO:0000255|PROSITE-ProRule:PRU00978}.
Interaction partners:
- Nuclear factor erythroid 2-related factor 2
- Transcription factor NF-E2 45 kDa subunit
- Endoplasmic reticulum membrane sensor NFE2L1
- Transcription factor MafK
- Transcription regulator protein BACH2
- DNA
- Nuclear factor erythroid 2-related factor 3
- Transcription factor MafF
- Chromodomain-helicase-DNA-binding protein 8
- Protein c-Fos
Sequence:
MTTPNKGNKALKVKREPGENGTSLTDEELVTMSVRELNQHLRGLSKEEIIQLKQRRRTLKNRGYAASCRVKRVTQKEELEKQKAELQQEVEKLASENASMKLELDALRSKYEALQNFARTVARSPVAPARGPLAAGLGPLVPGKVAATSVITIVKSKTDARS
Protein: Serpin, putative (Q9U5W7)
Organism: Drosophila melanogaster (Fruit fly)
Interaction partners:
Sequence:
MASKVSILLLLTVHLLAAQTFAQELIAWQRQQQQQQQQQLQLQQQLLLQQQQHQRNPRPELGLRSLPGNPWTQNNQEAISDVVAVDLTKREPVTPPPNRPPPVFSYMDRFSSELFKEIIKSQSQQNVVFSPFSVHALLALIYGASDGKTFRELQKAGEFSKNAMAVAQDFESVIKYKKHLEGADLTLATKVYYNRELGGVNHSYDEYAKFYFSAGTEAVDMQNAKDTAAKINAWVMDTTRNKIRDLVTPTDVDPQTQALLVNAVYFQGRWEHEFATMDTSPYDFQHTNGRISKVAMMFNDDVYGLAELPELGATALELAYKDSATSMLILLPNETTGLGKMLQQLSRPEFDLNRVAHRLRRQSVAVRLPKFQFEFEQDMTEPLKNLGVHQMFTPNSQVTKLMDQPVRVSKILQKAYINVGEAGTEASAASYAKFVPLSLPPKPTEFVANRPFVFAVRTPSSVLFIGHVEYPTPMSV
Protein: Purple acid phosphatase 5 (EC 3.1.3.2) (Q9C927)
Organism: Arabidopsis thaliana (Mouse-ear cress)
Subcellular location: Secreted {ECO:0000250}.
Interaction partners:
- Uncharacterized mitochondrial protein AtMg00170/AtMg00620
- Putative ubiquitin-like protein
- Curculin-like
- Uncharacterized protein
- Uncharacterized protein
- B3 domain-containing protein REM10
- Ubiquitin family protein
- RING-type E3 ubiquitin transferase
- La-related protein 6C
- UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
Sequence:
MSLETFPPPAGYNAPEQVHITQGDHNGRGMIISWVTSLNEDGSNVVTYWIASSDGSDNKSVIATTSSYRYFDYTSGYLHHAIIKELEYKTKYFYELGTGRSTRQFNLTPPKVGPDVPYTFGVIGDLGQTYASNQTLYNYMSNPKGQAVLFAGDLSYADDHPNHDQSKWDSYGRFVEPSAAYQPWIWAAGNHEIDYAQSIGETQPFKPYKNRYHVPYRASQNKYTPQNSWLQDEFKKVNRSETPWLIVLVHAPWYNSNNYHYMEGESMRVTFEPWFVENKVDIVFAGHVHAYERSERVSNIQYNITDGMSTPVKDQNAPVYITIGDGGNIEGIANIFTDPQPSYSAFREASFGHALLEIKNRTHAHYTWHRNKEDEAVIADSIWLKNRYYLPEEETI
Protein: Mannose-6-phosphate isomerase (EC 5.3.1.8) (Phosphohexomutase) (Phosphomannose isomerase) (PMI) (P34949)
Organism: Homo sapiens (Human)
Function: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q924M7}.
Interaction partners:
- Phosphomannomutase 2
- Glucose-6-phosphate isomerase
- Phosphomannomutase 1
- Hexokinase-1
- Glutamine--fructose-6-phosphate aminotransferase 1
- Glucosamine-6-phosphate deaminase 1
- Hexokinase-3
- Glutamine--fructose-6-phosphate aminotransferase 2
- Hexokinase HKDC1
- ATP-dependent 6-phosphofructokinase, muscle type
Sequence:
MAAPRVFPLSCAVQQYAWGKMGSNSEVARLLASSDPLAQIAEDKPYAELWMGTHPRGDAKILDNRISQKTLSQWIAENQDSLGSKVKDTFNGNLPFLFKVLSVETPLSIQAHPNKELAEKLHLQAPQHYPDANHKPEMAIALTPFQGLCGFRPVEEIVTFLKKVPEFQFLIGDEAATHLKQTMSHDSQAVASSLQSCFSHLMKSEKKVVVEQLNLLVKRISQQAAAGNNMEDIFGELLLQLHQQYPGDIGCFAIYFLNLLTLKPGEAMFLEANVPHAYLKGDCVECMACSDNTVRAGLTPKFIDVPTLCEMLSYTPSSSKDRLFLPTRSQEDPYLSIYDPPVPDFTIMKTEVPGSVTEYKVLALDSASILLMVQGTVIASTPTTQTPIPLQRGGVLFIGANESVSLKLTEPKDLLIFRACCLL
Protein: DnaJ homolog subfamily B member 14 (Q8TBM8)
Organism: Homo sapiens (Human)
Function: Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway. Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities. Can also act independently of HSPA8/Hsc70: together with DNAJB12, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers. While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70. When overexpressed, forms membranous structures together with DNAJB12 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear.
Subcellular location: Endoplasmic reticulum membrane {ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}; Single-pass membrane protein {ECO:0000255}. Nucleus membrane {ECO:0000269|PubMed:24732912}; Single-pass membrane protein {ECO:0000255}. Note=Localizes to the endoplasmic reticulum membrane (PubMed:23018488, PubMed:24732912, PubMed:27916661). When overexpressed, forms membranous structures in the nucleus (PubMed:24732912). {ECO:0000269|PubMed:23018488, ECO:0000269|PubMed:24732912, ECO:0000269|PubMed:27916661}.; SUBCELLULAR LOCATION: Note=(Microbial infection) Upon SV40 infection, colocalizes with BCAP31, DNAJB12 and DNAJC18 in punctate structures within the endoplasmic reticulum membrane. {ECO:0000269|PubMed:25631089}.
Interaction partners:
- Heat shock cognate 71 kDa protein
- Heat shock-related 70 kDa protein 2
- Small glutamine-rich tetratricopeptide repeat-containing protein alpha
- Heat shock protein 105 kDa
- Heat shock 70 kDa protein 4
- Stress-70 protein, mitochondrial
- Heat shock 70 kDa protein 1-like
- Heat shock 70 kDa protein 1A
Sequence:
MEGNRDEAEKCVEIAREALNAGNREKAQRFLQKAEKLYPLPSARALLEIIMKNGSTAGNSPHCRKPSGSGDQSKPNCTKDSTSGSGEGGKGYTKDQVDGVLSINKCKNYYEVLGVTKDAGDEDLKKAYRKLALKFHPDKNHAPGATDAFKKIGNAYAVLSNPEKRKQYDLTGNEEQACNHQNNGRFNFHRGCEADITPEDLFNIFFGGGFPSGSVHSFSNGRAGYSQQHQHRHSGHEREEERGDGGFSVFIQLMPIIVLILVSLLSQLMVSNPPYSLYPRSGTGQTIKMQTENLGVVYYVNKDFKNEYKGMLLQKVEKSVEEDYVTNIRNNCWKERQQKTDMQYAAKVYRDDRLRRKADALSMDNCKELERLTSLYKGG
Protein: Antithrombin (Serine (Or cysteine) proteinase inhibitor, clade C (Antithrombin), member 1) (Serpin peptidase inhibitor, clade C (antithrombin), member 1) (Q8AYE3)
Organism: Danio rerio (Zebrafish) (Brachydanio rerio)
Interaction partners:
- Prothrombin
- Fibrinogen alpha chain
- Plasminogen
- Fibrinogen beta chain
- Protein AMBP
- Tissue factor pathway inhibitor
- coagulation factor Xa
- Fgg protein
- Thrombomodulin.
- Tissue factor
Sequence:
MKLLACMWALWAFALCSIHATKDICNAKPKDLPLEPMCIYRNPDEIQPNKEPENIPVGTNPRVWELSKANSRFALSLFKQLAEGKSNDENIFLSPISISTAFAMTKLGACNTTLEQLMKVFQFDTIKEKTSDQVHFFFAKLNCRLYRKKHETTELISANRLFGDKSTTFNETFQHISETVYGAKLMPLDFKEKPEASRITINEWIANKTENRIKDTLPEGSIDTNTILVLVNAIYFKGQWKNKFDKQNVMKLDFHVSPTHKCPVPMMYQEKKFQYAKIPEDKVKILELPYNGGDITMVLILPIEGATLSEVVANMNLKKLVGWLHAMKETTVAVQIPRFRVEDSFSLKEQLTKMGLEDLFSPANASLPGMVADAEGPNLFISDAYHKAFLEVNEEGSEASAATAVVATGRSLNIFREQFVADRPFLLFIRESSINALIFTGRVANPCRSS
Protein: Baculoviral IAP repeat-containing protein 1 (Neuronal apoptosis inhibitory protein) (Q13075)
Organism: Homo sapiens (Human)
Function: Anti-apoptotic protein which acts by inhibiting the activities of CASP3, CASP7 and CASP9. Can inhibit the autocleavage of pro-CASP9 and cleavage of pro-CASP3 by CASP9. Capable of inhibiting CASP9 autoproteolysis at 'Asp-315' and decreasing the rate of auto proteolysis at 'Asp-330'. Acts as a mediator of neuronal survival in pathological conditions. Prevents motor-neuron apoptosis induced by a variety of signals. Possible role in the prevention of spinal muscular atrophy that seems to be caused by inappropriate persistence of motor-neuron apoptosis: mutated or deleted forms of NAIP have been found in individuals with severe spinal muscular atrophy.
Interaction partners:
- NLR family CARD domain-containing protein 4
- Interferon-inducible protein AIM2
- NACHT, LRR and PYD domains-containing protein 1
- NACHT, LRR and PYD domains-containing protein 3
- Pyrin
- Caspase-1
- NACHT, LRR and PYD domains-containing protein 6
- Apoptosis-associated speck-like protein containing a CARD
- NACHT, LRR and PYD domains-containing protein 4
- MHC class II transactivator
Sequence:
MATQQKASDERISQFDHNLLPELSALLGLDAVQLAKELEEEEQKERAKMQKGYNSQMRSEAKRLKTFVTYEPYSSWIPQEMAAAGFYFTGVKSGIQCFCCSLILFGAGLTRLPIEDHKRFHPDCGFLLNKDVGNIAKYDIRVKNLKSRLRGGKMRYQEEEARLASFRNWPFYVQGISPCVLSEAGFVFTGKQDTVQCFSCGGCLGNWEEGDDPWKEHAKWFPKCEFLRSKKSSEEITQYIQSYKGFVDITGEHFVNSWVQRELPMASAYCNDSIFAYEELRLDSFKDWPRESAVGVAALAKAGLFYTGIKDIVQCFSCGGCLEKWQEGDDPLDDHTRCFPNCPFLQNMKSSAEVTPDLQSRGELCELLETTSESNLEDSIAVGPIVPEMAQGEAQWFQEAKNLNEQLRAAYTSASFRHMSLLDISSDLATDHLLGCDLSIASKHISKPVQEPLVLPEVFGNLNSVMCVEGEAGSGKTVLLKKIAFLWASGCCPLLNRFQLVFYLSLSSTRPDEGLASIICDQLLEKEGSVTEMCVRNIIQQLKNQVLFLLDDYKEICSIPQVIGKLIQKNHLSRTCLLIAVRTNRARDIRRYLETILEIKAFPFYNTVCILRKLFSHNMTRLRKFMVYFGKNQSLQKIQKTPLFVAAICAHWFQYPFDPSFDDVAVFKSYMERLSLRNKATAEILKATVSSCGELALKGFFSCCFEFNDDDLAEAGVDEDEDLTMCLMSKFTAQRLRPFYRFLSPAFQEFLAGMRLIELLDSDRQEHQDLGLYHLKQINSPMMTVSAYNNFLNYVSSLPSTKAGPKIVSHLLHLVDNKESLENISENDDYLKHQPEISLQMQLLRGLWQICPQAYFSMVSEHLLVLALKTAYQSNTVAACSPFVLQFLQGRTLTLGALNLQYFFDHPESLSLLRSIHFPIRGNKTSPRAHFSVLETCFDKSQVPTIDQDYASAFEPMNEWERNLAEKEDNVKSYMDMQRRASPDLSTGYWKLSPKQYKIPCLEVDVNDIDVVGQDMLEILMTVFSASQRIELHLNHSRGFIESIRPALELSKASVTKCSISKLELSAAEQELLLTLPSLESLEVSGTIQSQDQIFPNLDKFLCLKELSVDLEGNINVFSVIPEEFPNFHHMEKLLIQISAEYDPSKLVKLIQNSPNLHVFHLKCNFFSDFGSLMTMLVSCKKLTEIKFSDSFFQAVPFVASLPNFISLKILNLEGQQFPDEETSEKFAYILGSLSNLEELILPTGDGIYRVAKLIIQQCQQLHCLRVLSFFKTLNDDSVVEIAKVAISGGFQKLENLKLSINHKITEEGYRNFFQALDNMPNLQELDISRHFTECIKAQATTVKSLSQCVLRLPRLIRLNMLSWLLDADDIALLNVMKERHPQSKYLTILQKWILPFSPIIQK
Protein: Short-chain dehydrogenase/reductase 3 (EC 1.1.1.300) (Retinal short-chain dehydrogenase/reductase 1) (retSDR1) (O88876)
Organism: Mus musculus (Mouse)
Function: Catalyzes the reduction of all-trans-retinal to all-trans-retinol in the presence of NADPH.
Subcellular location: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}.
Interaction partners:
- Cytochrome P450 26A1
- Retinal dehydrogenase 2
- Retinaldehyde dehydrogenase 3
- Dehydrogenase/reductase SDR family member 9
- Lecithin retinol acyltransferase
- Aldehyde dehydrogenase 1A1
- Beta,beta-carotene 15,15'-dioxygenase
- All-trans-retinol 13,14-reductase
- Dehydrogenase/reductase SDR family member 4
- Diacylglycerol O-acyltransferase 1
Sequence:
MVWKWLGALVVFPLQMIYLVTKAAVGMVLPPKLRDLSRESVLITGGGRGIGRHLAREFAERGARKIVLWGRTEKCLKETTEEIRQMGTECHYFICDVGNREEVYQMAKAVREKVGDITILVNNAAVVHGKSLMDSDDDALLKSQHVNTLGQFWTTKAFLPRMLELQNGHIVCLNSVLALSAIPGAIDYCTSKASAFAFMESLTLGLLDCPGVSATTVLPFHTSTEMFQGMRVRFPNLFPPLKPETVARRTVDAVQQNQALLLLPWTMNILIILKSILPQAALEEIHRFSGTYTCMNTFKGRT